python-csb 1.2.3+dfsg-3 / usr / lib / python2.7 / dist-packages / csb / test / data / 3p1u.pdb

HEADER    SUGAR BINDING PROTEIN                   30-SEP-10   3P1U              
TITLE     CRYSTAL STRUCTURE OF A SUSD HOMOLOG (BDI_0600) FROM PARABACTEROIDES   
TITLE    2 DISTASONIS ATCC 8503 AT 2.05 A RESOLUTION                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUSD HOMOLOG;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SEQUENCE DATABASE RESIDUES 26-553;                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PARABACTEROIDES DISTASONIS ATCC 8503;           
SOURCE   3 ORGANISM_TAXID: 435591;                                              
SOURCE   4 STRAIN: DSM 20701 / NCTC 11152;                                      
SOURCE   5 ATCC: 8503;                                                          
SOURCE   6 GENE: BDI_0600;                                                      
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: HK100;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,      
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, PSI-BIOLOGY, SUGAR BINDING PROTEIN     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   2   20-JUL-11 3P1U    1       KEYWDS                                   
REVDAT   1   03-NOV-10 3P1U    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF A SUSD HOMOLOG (YP_001301998.1) FROM    
JRNL        TITL 2 PARABACTEROIDES DISTASONIS ATCC 8503 AT 2.05 A RESOLUTION    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 69269                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.244                          
REMARK   3   R VALUE            (WORKING SET)  : 0.243                          
REMARK   3   FREE R VALUE                      : 0.265                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.060                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3503                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.05                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.10                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 5083                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2027                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4834                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2017                   
REMARK   3   BIN FREE R VALUE                        : 0.2216                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.90                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 249                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8073                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 592                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.65                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.63020                                              
REMARK   3    B22 (A**2) : 1.63020                                              
REMARK   3    B33 (A**2) : -3.26040                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.854                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.840                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8338   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11343  ; 10.000 ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2866   ; 10.000 ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 233    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1216   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8338   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1085   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 10979  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.37                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.85                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 13.57                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -42.4473   13.0140   75.1758           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0868 T22:   -0.0585                                    
REMARK   3     T33:   -0.0542 T12:    0.0021                                    
REMARK   3     T13:    0.0087 T23:    0.0234                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2527 L22:    0.3714                                    
REMARK   3     L33:    0.2603 L12:    0.0579                                    
REMARK   3     L13:   -0.0213 L23:   -0.0252                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0018 S12:    0.0112 S13:   -0.0026                     
REMARK   3     S21:    0.0008 S22:   -0.0027 S23:    0.0222                     
REMARK   3     S31:   -0.0026 S32:   -0.0458 S33:    0.0045                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -43.6159   -8.6921  127.6560           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0933 T22:   -0.0809                                    
REMARK   3     T33:   -0.0385 T12:   -0.0040                                    
REMARK   3     T13:    0.0047 T23:    0.0247                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3152 L22:    0.4956                                    
REMARK   3     L33:    0.2410 L12:   -0.0961                                    
REMARK   3     L13:    0.0868 L23:   -0.0773                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0223 S12:    0.0020 S13:   -0.0093                     
REMARK   3     S21:    0.0504 S22:    0.0119 S23:    0.0521                     
REMARK   3     S31:   -0.0243 S32:   -0.0104 S33:   -0.0342                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1. A MET-INHIBITION PROTOCOL WAS USED     
REMARK   3  FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE   
REMARK   3  OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75   
REMARK   3  FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET               
REMARK   3  INCORPORATION. 2. SULFATE FROM THE CRYSTALLIZATION BUFFER IS        
REMARK   3  MODELED INTO THE STRUCTURE. 3. ATOM RECORD CONTAINS SUM OF TLS      
REMARK   3  AND RESIDUAL B ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U     
REMARK   3  FACTORS. 4. LYS 64 ON THE A AND B SUBUNITS AND PRO 462 ON THE A     
REMARK   3  AND B SUBUNITS ARE RAMACHANDRAN OUTLIERS, BUT THEIR MODELING IS     
REMARK   3  SUPPORTED BY ELECTRON DENSITY. 5. THE R AND R-FREE VALUES ARE       
REMARK   3  ELEVATED COMPARED WITH OTHER STRUCTURES IN THE PDB REFINED AT THE   
REMARK   3  SAME RESOLUTION, AND THIS CAN LIKELY BE ATTRIBUTED TO               
REMARK   3  UNIDENTIFIED CRYSTAL DISORDERS THAT RESULT IN REDUCED DATA          
REMARK   3  QUALITY. 6. THE REFINEMENT WAS RESTRAINED AGAINST THE MAD PHASES.   
REMARK   4                                                                      
REMARK   4 3P1U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061851.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.47                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91837,0.97916,0.97860            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69272                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.701                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.25200                            
REMARK 200  R SYM                      (I) : 0.25200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.96500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.96500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.13M AMMONIUM SULFATE, 0.1M PHOSPHATE   
REMARK 280  -CITRATE PH 4.47, NANODROP, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,Z                                                 
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     ASN A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     ASP A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     PRO A    32                                                      
REMARK 465     THR A    33                                                      
REMARK 465     ASP A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     VAL A    36                                                      
REMARK 465     ASN A    37                                                      
REMARK 465     TYR A    38                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     ASN B    26                                                      
REMARK 465     GLU B    27                                                      
REMARK 465     ASN B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     ASP B    30                                                      
REMARK 465     LYS B    31                                                      
REMARK 465     PRO B    32                                                      
REMARK 465     THR B    33                                                      
REMARK 465     ASP B    34                                                      
REMARK 465     ASP B    35                                                      
REMARK 465     VAL B    36                                                      
REMARK 465     ASN B    37                                                      
REMARK 465     TYR B    38                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A  39    CG   OD1                                            
REMARK 470     MSE A  40    CG  SE    CE                                        
REMARK 470     GLU A 116    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 117    CE   NZ                                             
REMARK 470     ASP A 118    CG   OD1  OD2                                       
REMARK 470     LYS A 119    CG   CD   CE   NZ                                   
REMARK 470     LYS A 162    CE   NZ                                             
REMARK 470     ASP A 176    CG   OD1  OD2                                       
REMARK 470     LYS A 200    CG   CD   CE   NZ                                   
REMARK 470     GLN A 298    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 301    CG1  CG2                                            
REMARK 470     TYR A 367    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A 442    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 526    CE   NZ                                             
REMARK 470     LYS A 553    CD   CE                                             
REMARK 470     ASN B  39    CG   OD1                                            
REMARK 470     MSE B  40    CG  SE    CE                                        
REMARK 470     LYS B 117    CG   CD   CE   NZ                                   
REMARK 470     LYS B 119    CG   CD   CE   NZ                                   
REMARK 470     SER B 185    OG                                                  
REMARK 470     GLN B 298    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 429    CE   NZ                                             
REMARK 470     GLN B 442    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 524    CD   CE   NZ                                        
REMARK 470     LYS B 553    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  54       77.11     61.44                                   
REMARK 500    ASN A  58      -75.06   -112.80                                   
REMARK 500    LYS A  64      -81.20    -91.90                                   
REMARK 500    GLN A  67      -85.95   -138.88                                   
REMARK 500    ASN A 290      -44.96     69.84                                   
REMARK 500    LEU A 464       30.13    -98.69                                   
REMARK 500    ASP A 487      104.23    -38.85                                   
REMARK 500    ASN A 518       41.84   -142.28                                   
REMARK 500    ILE B  54       76.00     61.77                                   
REMARK 500    ASN B  58      -74.65   -113.10                                   
REMARK 500    LYS B  64      -81.31    -91.83                                   
REMARK 500    GLN B  67      -85.66   -138.88                                   
REMARK 500    ASP B 118       88.14   -161.23                                   
REMARK 500    ASN B 290      -45.13     70.18                                   
REMARK 500    LEU B 464       32.32    -98.34                                   
REMARK 500    ASP B 487      104.28    -38.75                                   
REMARK 500    ASN B 518       41.72   -142.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 744        DISTANCE =  5.15 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 554                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 394774   RELATED DB: TARGETDB                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT (RESIDUES 26-553) WAS EXPRESSED WITH A PURIFICATION    
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE       
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.          
DBREF  3P1U A   26   553  UNP    A6L9L2   A6L9L2_PARD8    26    553             
DBREF  3P1U B   26   553  UNP    A6L9L2   A6L9L2_PARD8    26    553             
SEQADV 3P1U GLY A    0  UNP  A6L9L2              LEADER SEQUENCE                
SEQADV 3P1U GLY B    0  UNP  A6L9L2              LEADER SEQUENCE                
SEQRES   1 A  529  GLY ASN GLU ASN PRO ASP LYS PRO THR ASP ASP VAL ASN          
SEQRES   2 A  529  TYR ASN MSE ASN GLU PRO ARG LEU ALA SER THR LEU ARG          
SEQRES   3 A  529  GLY GLY LEU ILE ILE GLU GLY ASN VAL GLU GLN ARG LEU          
SEQRES   4 A  529  LYS PRO LEU GLN ILE ASP PHE TYR SER GLN MSE THR VAL          
SEQRES   5 A  529  ASP GLY GLY GLY TRP GLY THR LYS ASN TYR ILE GLN ASP          
SEQRES   6 A  529  ASP GLU TRP ASN ASN LEU VAL TRP GLU GLU TYR LEU LYS          
SEQRES   7 A  529  GLN ILE ALA SER ILE ASN ILE VAL ILE ARG SER LEU THR          
SEQRES   8 A  529  GLU LYS ASP LYS ASP ALA TYR ALA ASN THR ILE ALA PHE          
SEQRES   9 A  529  ALA ARG ILE TRP ARG VAL TYR VAL HIS THR LEU ALA ALA          
SEQRES  10 A  529  ASP LYS PHE GLY PRO MSE PRO PHE PRO ALA TYR GLU ILE          
SEQRES  11 A  529  VAL GLU ALA ASN PRO PRO TYR LYS SER LEU LYS ASP ILE          
SEQRES  12 A  529  TYR ASP GLU TYR PHE ARG GLU LEU ASP ALA ALA ILE ASN          
SEQRES  13 A  529  GLY PHE ASN ASP SER ALA GLN PRO ILE PHE SER ASP ALA          
SEQRES  14 A  529  GLY ILE ASP LEU ILE TYR LYS ASN ASP VAL SER LYS TRP          
SEQRES  15 A  529  LYS ARG PHE ALA ASN SER LEU ARG LEU ARG LEU ALA VAL          
SEQRES  16 A  529  ARG LEU THR GLU VAL ASP GLN GLU LYS CYS ILE ALA GLU          
SEQRES  17 A  529  ALA ASN ALA ALA ILE SER SER PRO ALA GLY LEU ILE SER          
SEQRES  18 A  529  ASP LYS ALA ASP ASN ALA TYR MSE PRO PRO LYS ALA ASP          
SEQRES  19 A  529  GLY SER TRP GLY GLN ASP TYR ASN TYR THR MSE PHE GLN          
SEQRES  20 A  529  ILE THR TRP SER GLY PRO ILE CYS MSE SER LYS SER VAL          
SEQRES  21 A  529  GLU LYS LEU VAL THR ASN ILE GLY GLY VAL ALA TRP PRO          
SEQRES  22 A  529  GLN GLY VAL VAL ASN GLN THR SER GLY VAL ALA VAL SER          
SEQRES  23 A  529  SER VAL HIS PRO GLU LYS VAL ASP PRO ARG ALA PRO LYS          
SEQRES  24 A  529  ILE PHE GLN PRO GLY ILE GLU ASN GLY ASP TRP LYS GLY          
SEQRES  25 A  529  LEU VAL TYR GLY PRO LYS ALA GLU GLU ALA ASN THR GLY          
SEQRES  26 A  529  ILE TYR GLN SER LYS GLN CYS ALA GLU LEU GLY PHE ILE          
SEQRES  27 A  529  ILE LYS ASP GLY TYR PRO TYR LYS SER ARG PRO TYR ASP          
SEQRES  28 A  529  LEU PHE LEU SER GLU GLU VAL HIS PHE LEU LYS ALA GLU          
SEQRES  29 A  529  LEU TYR ALA ARG GLY PHE ILE ALA GLY ASP ALA LYS SER          
SEQRES  30 A  529  GLU TYR GLU ALA GLY VAL ARG ALA SER PHE ALA THR TRP          
SEQRES  31 A  529  GLY VAL THR SER GLU VAL ASP ASP TYR LEU THR SER THR          
SEQRES  32 A  529  GLU LYS ASN GLU ALA GLY THR SER ALA ARG TYR ASP ASP          
SEQRES  33 A  529  GLN GLN GLY ALA GLY ASN THR ALA LEU GLU LYS ILE ILE          
SEQRES  34 A  529  THR GLN LYS TYR ILE ALA GLY ILE PRO ASP LEU ALA GLN          
SEQRES  35 A  529  GLU GLY TRP ASN ASP LYS ARG ARG LEU ASN LEU PRO ARG          
SEQRES  36 A  529  LEU ASP VAL ALA VAL TYR ARG ASP GLN ALA VAL TYR ASN          
SEQRES  37 A  529  ASN ASN ASP LYS ASP ILE LEU LYS SER ALA ASN PHE ILE          
SEQRES  38 A  529  LYS ARG MSE ARG TYR PRO THR LYS GLU SER LEU ILE ASN          
SEQRES  39 A  529  ALA THR GLU TYR GLU LYS GLY LYS SER MSE LEU GLY GLY          
SEQRES  40 A  529  LYS GLY ASP ILE VAL SER THR PRO LEU TRP TRP ASP LYS          
SEQRES  41 A  529  ASN SER ASN TYR CYS THR SER SER LYS                          
SEQRES   1 B  529  GLY ASN GLU ASN PRO ASP LYS PRO THR ASP ASP VAL ASN          
SEQRES   2 B  529  TYR ASN MSE ASN GLU PRO ARG LEU ALA SER THR LEU ARG          
SEQRES   3 B  529  GLY GLY LEU ILE ILE GLU GLY ASN VAL GLU GLN ARG LEU          
SEQRES   4 B  529  LYS PRO LEU GLN ILE ASP PHE TYR SER GLN MSE THR VAL          
SEQRES   5 B  529  ASP GLY GLY GLY TRP GLY THR LYS ASN TYR ILE GLN ASP          
SEQRES   6 B  529  ASP GLU TRP ASN ASN LEU VAL TRP GLU GLU TYR LEU LYS          
SEQRES   7 B  529  GLN ILE ALA SER ILE ASN ILE VAL ILE ARG SER LEU THR          
SEQRES   8 B  529  GLU LYS ASP LYS ASP ALA TYR ALA ASN THR ILE ALA PHE          
SEQRES   9 B  529  ALA ARG ILE TRP ARG VAL TYR VAL HIS THR LEU ALA ALA          
SEQRES  10 B  529  ASP LYS PHE GLY PRO MSE PRO PHE PRO ALA TYR GLU ILE          
SEQRES  11 B  529  VAL GLU ALA ASN PRO PRO TYR LYS SER LEU LYS ASP ILE          
SEQRES  12 B  529  TYR ASP GLU TYR PHE ARG GLU LEU ASP ALA ALA ILE ASN          
SEQRES  13 B  529  GLY PHE ASN ASP SER ALA GLN PRO ILE PHE SER ASP ALA          
SEQRES  14 B  529  GLY ILE ASP LEU ILE TYR LYS ASN ASP VAL SER LYS TRP          
SEQRES  15 B  529  LYS ARG PHE ALA ASN SER LEU ARG LEU ARG LEU ALA VAL          
SEQRES  16 B  529  ARG LEU THR GLU VAL ASP GLN GLU LYS CYS ILE ALA GLU          
SEQRES  17 B  529  ALA ASN ALA ALA ILE SER SER PRO ALA GLY LEU ILE SER          
SEQRES  18 B  529  ASP LYS ALA ASP ASN ALA TYR MSE PRO PRO LYS ALA ASP          
SEQRES  19 B  529  GLY SER TRP GLY GLN ASP TYR ASN TYR THR MSE PHE GLN          
SEQRES  20 B  529  ILE THR TRP SER GLY PRO ILE CYS MSE SER LYS SER VAL          
SEQRES  21 B  529  GLU LYS LEU VAL THR ASN ILE GLY GLY VAL ALA TRP PRO          
SEQRES  22 B  529  GLN GLY VAL VAL ASN GLN THR SER GLY VAL ALA VAL SER          
SEQRES  23 B  529  SER VAL HIS PRO GLU LYS VAL ASP PRO ARG ALA PRO LYS          
SEQRES  24 B  529  ILE PHE GLN PRO GLY ILE GLU ASN GLY ASP TRP LYS GLY          
SEQRES  25 B  529  LEU VAL TYR GLY PRO LYS ALA GLU GLU ALA ASN THR GLY          
SEQRES  26 B  529  ILE TYR GLN SER LYS GLN CYS ALA GLU LEU GLY PHE ILE          
SEQRES  27 B  529  ILE LYS ASP GLY TYR PRO TYR LYS SER ARG PRO TYR ASP          
SEQRES  28 B  529  LEU PHE LEU SER GLU GLU VAL HIS PHE LEU LYS ALA GLU          
SEQRES  29 B  529  LEU TYR ALA ARG GLY PHE ILE ALA GLY ASP ALA LYS SER          
SEQRES  30 B  529  GLU TYR GLU ALA GLY VAL ARG ALA SER PHE ALA THR TRP          
SEQRES  31 B  529  GLY VAL THR SER GLU VAL ASP ASP TYR LEU THR SER THR          
SEQRES  32 B  529  GLU LYS ASN GLU ALA GLY THR SER ALA ARG TYR ASP ASP          
SEQRES  33 B  529  GLN GLN GLY ALA GLY ASN THR ALA LEU GLU LYS ILE ILE          
SEQRES  34 B  529  THR GLN LYS TYR ILE ALA GLY ILE PRO ASP LEU ALA GLN          
SEQRES  35 B  529  GLU GLY TRP ASN ASP LYS ARG ARG LEU ASN LEU PRO ARG          
SEQRES  36 B  529  LEU ASP VAL ALA VAL TYR ARG ASP GLN ALA VAL TYR ASN          
SEQRES  37 B  529  ASN ASN ASP LYS ASP ILE LEU LYS SER ALA ASN PHE ILE          
SEQRES  38 B  529  LYS ARG MSE ARG TYR PRO THR LYS GLU SER LEU ILE ASN          
SEQRES  39 B  529  ALA THR GLU TYR GLU LYS GLY LYS SER MSE LEU GLY GLY          
SEQRES  40 B  529  LYS GLY ASP ILE VAL SER THR PRO LEU TRP TRP ASP LYS          
SEQRES  41 B  529  ASN SER ASN TYR CYS THR SER SER LYS                          
MODRES 3P1U MSE A   40  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE A   74  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE A  147  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE A  253  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE A  269  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE A  280  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE A  508  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE A  528  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE B   40  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE B   74  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE B  147  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE B  253  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE B  269  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE B  280  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE B  508  MET  SELENOMETHIONINE                                   
MODRES 3P1U MSE B  528  MET  SELENOMETHIONINE                                   
HET    MSE  A  40       5                                                       
HET    MSE  A  74       8                                                       
HET    MSE  A 147       8                                                       
HET    MSE  A 253       8                                                       
HET    MSE  A 269       8                                                       
HET    MSE  A 280       8                                                       
HET    MSE  A 508       8                                                       
HET    MSE  A 528       8                                                       
HET    MSE  B  40       5                                                       
HET    MSE  B  74       8                                                       
HET    MSE  B 147       8                                                       
HET    MSE  B 253       8                                                       
HET    MSE  B 269       8                                                       
HET    MSE  B 280       8                                                       
HET    MSE  B 508       8                                                       
HET    MSE  B 528       8                                                       
HET    SO4  B 554       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *592(H2 O)                                                    
HELIX    1   1 ASN A   41  ILE A   54  1                                  14    
HELIX    2   2 ASN A   58  LYS A   64  1                                   7    
HELIX    3   3 GLN A   67  GLN A   73  1                                   7    
HELIX    4   4 TRP A   81  TYR A   86  5                                   6    
HELIX    5   5 ASP A   89  LYS A  119  1                                  31    
HELIX    6   6 TYR A  122  GLY A  145  1                                  24    
HELIX    7   7 SER A  163  PHE A  182  1                                  20    
HELIX    8   8 ASP A  192  ASP A  196  5                                   5    
HELIX    9   9 ASP A  202  ARG A  220  1                                  19    
HELIX   10  10 ASP A  225  SER A  239  1                                  15    
HELIX   11  11 ASP A  246  ASN A  250  5                                   5    
HELIX   12  12 ASN A  266  ILE A  272  1                                   7    
HELIX   13  13 SER A  281  THR A  289  1                                   9    
HELIX   14  14 ARG A  320  ILE A  324  1                                   5    
HELIX   15  15 LYS A  342  ALA A  346  5                                   5    
HELIX   16  16 THR A  348  CYS A  356  5                                   9    
HELIX   17  17 LEU A  378  ARG A  392  1                                  15    
HELIX   18  18 ASP A  398  TRP A  414  1                                  17    
HELIX   19  19 VAL A  416  THR A  425  1                                  10    
HELIX   20  20 THR A  447  ALA A  459  1                                  13    
HELIX   21  21 LEU A  464  ASN A  476  1                                  13    
HELIX   22  22 LYS A  500  PHE A  504  5                                   5    
HELIX   23  23 LYS A  513  ASN A  518  1                                   6    
HELIX   24  24 ASN A  518  GLY A  530  1                                  13    
HELIX   25  25 MSE B   40  ILE B   54  1                                  15    
HELIX   26  26 ASN B   58  LYS B   64  1                                   7    
HELIX   27  27 GLN B   67  GLN B   73  1                                   7    
HELIX   28  28 TRP B   81  TYR B   86  5                                   6    
HELIX   29  29 ASP B   89  LYS B  119  1                                  31    
HELIX   30  30 TYR B  122  GLY B  145  1                                  24    
HELIX   31  31 SER B  163  PHE B  182  1                                  20    
HELIX   32  32 ASP B  192  ASP B  196  5                                   5    
HELIX   33  33 ASP B  202  ARG B  220  1                                  19    
HELIX   34  34 ASP B  225  SER B  239  1                                  15    
HELIX   35  35 ASP B  246  ASN B  250  5                                   5    
HELIX   36  36 ASN B  266  ILE B  272  1                                   7    
HELIX   37  37 SER B  281  THR B  289  1                                   9    
HELIX   38  38 ARG B  320  ILE B  324  1                                   5    
HELIX   39  39 LYS B  342  ALA B  346  5                                   5    
HELIX   40  40 THR B  348  CYS B  356  5                                   9    
HELIX   41  41 LEU B  378  ARG B  392  1                                  15    
HELIX   42  42 ASP B  398  TRP B  414  1                                  17    
HELIX   43  43 VAL B  416  THR B  425  1                                  10    
HELIX   44  44 THR B  447  ALA B  459  1                                  13    
HELIX   45  45 LEU B  464  ASN B  476  1                                  13    
HELIX   46  46 LYS B  500  PHE B  504  5                                   5    
HELIX   47  47 LYS B  513  ASN B  518  1                                   6    
HELIX   48  48 ASN B  518  GLY B  530  1                                  13    
SHEET    1   A 2 VAL A  76  ASP A  77  0                                        
SHEET    2   A 2 ILE A 278  CYS A 279 -1  O  CYS A 279   N  VAL A  76           
SHEET    1   B 2 MSE A 147  PRO A 148  0                                        
SHEET    2   B 2 TYR A 161  LYS A 162 -1  O  LYS A 162   N  MSE A 147           
SHEET    1   C 2 ALA A 251  MSE A 253  0                                        
SHEET    2   C 2 TYR A 374  PHE A 377 -1  O  TYR A 374   N  MSE A 253           
SHEET    1   D 2 PHE A 325  GLN A 326  0                                        
SHEET    2   D 2 GLU A 358  LEU A 359 -1  O  GLU A 358   N  GLN A 326           
SHEET    1   E 2 ILE A 363  LYS A 364  0                                        
SHEET    2   E 2 TYR A 367  PRO A 368 -1  O  TYR A 367   N  LYS A 364           
SHEET    1   F 2 VAL B  76  ASP B  77  0                                        
SHEET    2   F 2 ILE B 278  CYS B 279 -1  O  CYS B 279   N  VAL B  76           
SHEET    1   G 2 MSE B 147  PRO B 148  0                                        
SHEET    2   G 2 TYR B 161  LYS B 162 -1  O  LYS B 162   N  MSE B 147           
SHEET    1   H 2 ALA B 251  MSE B 253  0                                        
SHEET    2   H 2 TYR B 374  PHE B 377 -1  O  TYR B 374   N  MSE B 253           
SHEET    1   I 2 PHE B 325  GLN B 326  0                                        
SHEET    2   I 2 GLU B 358  LEU B 359 -1  O  GLU B 358   N  GLN B 326           
SHEET    1   J 2 ILE B 363  LYS B 364  0                                        
SHEET    2   J 2 TYR B 367  PRO B 368 -1  O  TYR B 367   N  LYS B 364           
LINK         C   ASN A  39                 N   MSE A  40     1555   1555  1.36  
LINK         C   MSE A  40                 N   ASN A  41     1555   1555  1.34  
LINK         C   GLN A  73                 N   MSE A  74     1555   1555  1.36  
LINK         C   MSE A  74                 N   THR A  75     1555   1555  1.36  
LINK         C   PRO A 146                 N   MSE A 147     1555   1555  1.33  
LINK         C   MSE A 147                 N   PRO A 148     1555   1555  1.36  
LINK         C   TYR A 252                 N   MSE A 253     1555   1555  1.34  
LINK         C   MSE A 253                 N   PRO A 254     1555   1555  1.35  
LINK         C   THR A 268                 N   MSE A 269     1555   1555  1.35  
LINK         C   MSE A 269                 N   PHE A 270     1555   1555  1.35  
LINK         C   CYS A 279                 N   MSE A 280     1555   1555  1.34  
LINK         C   MSE A 280                 N   SER A 281     1555   1555  1.34  
LINK         C   ARG A 507                 N   MSE A 508     1555   1555  1.34  
LINK         C   MSE A 508                 N   ARG A 509     1555   1555  1.35  
LINK         C   SER A 527                 N   MSE A 528     1555   1555  1.36  
LINK         C   MSE A 528                 N   LEU A 529     1555   1555  1.36  
LINK         C   ASN B  39                 N   MSE B  40     1555   1555  1.35  
LINK         C   MSE B  40                 N   ASN B  41     1555   1555  1.35  
LINK         C   GLN B  73                 N   MSE B  74     1555   1555  1.36  
LINK         C   MSE B  74                 N   THR B  75     1555   1555  1.35  
LINK         C   PRO B 146                 N   MSE B 147     1555   1555  1.33  
LINK         C   MSE B 147                 N   PRO B 148     1555   1555  1.36  
LINK         C   TYR B 252                 N   MSE B 253     1555   1555  1.34  
LINK         C   MSE B 253                 N   PRO B 254     1555   1555  1.35  
LINK         C   THR B 268                 N   MSE B 269     1555   1555  1.35  
LINK         C   MSE B 269                 N   PHE B 270     1555   1555  1.35  
LINK         C   CYS B 279                 N   MSE B 280     1555   1555  1.34  
LINK         C   MSE B 280                 N   SER B 281     1555   1555  1.34  
LINK         C   ARG B 507                 N   MSE B 508     1555   1555  1.34  
LINK         C   MSE B 508                 N   ARG B 509     1555   1555  1.34  
LINK         C   SER B 527                 N   MSE B 528     1555   1555  1.36  
LINK         C   MSE B 528                 N   LEU B 529     1555   1555  1.36  
CISPEP   1 ILE A  461    PRO A  462          0         0.29                     
CISPEP   2 LEU A  477    PRO A  478          0        -2.10                     
CISPEP   3 ILE B  461    PRO B  462          0         0.69                     
CISPEP   4 LEU B  477    PRO B  478          0        -2.44                     
SITE     1 AC1  4 ARG A 130  ARG B 130  ALA B 177  HOH B1049                    
CRYST1  130.242  130.242  114.822  90.00  90.00 120.00 P 6          12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007678  0.004433  0.000000        0.00000                         
SCALE2      0.000000  0.008866  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008709        0.00000                         
ATOM      1  N   ASN A  39     -46.136  22.677 108.323  1.00 45.77           N  
ANISOU    1  N   ASN A  39     6221   5889   5281    -83    409     -1       N  
ATOM      2  CA  ASN A  39     -47.450  23.307 108.255  1.00 45.50           C  
ANISOU    2  CA  ASN A  39     6172   5853   5262    -62    463    -23       C  
ATOM      3  C   ASN A  39     -47.726  23.880 106.861  1.00 48.51           C  
ANISOU    3  C   ASN A  39     6507   6222   5705    -36    461    -25       C  
ATOM      4  O   ASN A  39     -48.722  23.517 106.238  1.00 47.77           O  
ANISOU    4  O   ASN A  39     6373   6135   5642    -22    487    -17       O  
ATOM      5  CB  ASN A  39     -47.582  24.397 109.322  1.00 46.77           C  
ANISOU    5  CB  ASN A  39     6380   6006   5384    -63    488    -58       C  
HETATM    6  N   MSE A  40     -46.834  24.784 106.368  1.00 44.83           N  
ANISOU    6  N   MSE A  40     6045   5736   5254    -32    428    -36       N  
HETATM    7  CA  MSE A  40     -46.989  25.408 105.051  1.00 44.02           C  
ANISOU    7  CA  MSE A  40     5903   5619   5205    -10    423    -37       C  
HETATM    8  C   MSE A  40     -46.416  24.503 103.946  1.00 45.68           C  
ANISOU    8  C   MSE A  40     6075   5834   5446    -13    386     -5       C  
HETATM    9  O   MSE A  40     -45.429  24.857 103.297  1.00 44.59           O  
ANISOU    9  O   MSE A  40     5934   5684   5326    -15    348     -2       O  
HETATM   10  CB  MSE A  40     -46.321  26.793 105.029  1.00 46.50           C  
ANISOU   10  CB  MSE A  40     6239   5907   5521     -5    408    -62       C  
ATOM     11  N   ASN A  41     -47.028  23.322 103.757  1.00 41.17           N  
ANISOU   11  N   ASN A  41     5479   5281   4882    -15    397     17       N  
ATOM     12  CA  ASN A  41     -46.588  22.354 102.750  1.00 39.82           C  
ANISOU   12  CA  ASN A  41     5274   5115   4739    -19    367     45       C  
ATOM     13  C   ASN A  41     -47.234  22.648 101.392  1.00 41.11           C  
ANISOU   13  C   ASN A  41     5392   5274   4954      4    374     47       C  
ATOM     14  O   ASN A  41     -46.705  22.240 100.354  1.00 40.05           O  
ANISOU   14  O   ASN A  41     5233   5138   4847      5    346     65       O  
ATOM     15  CB  ASN A  41     -46.927  20.919 103.201  1.00 40.74           C  
ANISOU   15  CB  ASN A  41     5389   5251   4838    -34    375     68       C  
ATOM     16  CG  ASN A  41     -46.339  20.540 104.544  1.00 66.86           C  
ANISOU   16  CG  ASN A  41     8744   8565   8094    -57    367     70       C  
ATOM     17  OD1 ASN A  41     -47.043  20.100 105.453  1.00 62.56           O  
ANISOU   17  OD1 ASN A  41     8216   8034   7521    -65    398     70       O  
ATOM     18  ND2 ASN A  41     -45.031  20.700 104.693  1.00 60.84           N  
ANISOU   18  ND2 ASN A  41     8003   7795   7319    -68    325     73       N  
ATOM     19  N   GLU A  42     -48.396  23.346 101.401  1.00 36.14           N  
ANISOU   19  N   GLU A  42     4752   4644   4337     24    414     30       N  
ATOM     20  CA  GLU A  42     -49.145  23.660 100.177  1.00 34.93           C  
ANISOU   20  CA  GLU A  42     4554   4487   4231     47    422     32       C  
ATOM     21  C   GLU A  42     -48.327  24.536  99.177  1.00 35.53           C  
ANISOU   21  C   GLU A  42     4624   4543   4333     57    390     30       C  
ATOM     22  O   GLU A  42     -48.269  24.208  97.988  1.00 34.36           O  
ANISOU   22  O   GLU A  42     4442   4395   4217     63    372     46       O  
ATOM     23  CB  GLU A  42     -50.490  24.321 100.515  1.00 36.72           C  
ANISOU   23  CB  GLU A  42     4772   4715   4464     66    470     12       C  
ATOM     24  CG  GLU A  42     -51.384  24.529  99.309  1.00 45.88           C  
ANISOU   24  CG  GLU A  42     5884   5875   5673     90    479     17       C  
ATOM     25  CD  GLU A  42     -52.783  24.979  99.660  1.00 62.38           C  
ANISOU   25  CD  GLU A  42     7958   7969   7773    110    527      2       C  
ATOM     26  OE1 GLU A  42     -52.990  26.203  99.824  1.00 61.22           O  
ANISOU   26  OE1 GLU A  42     7822   7805   7632    129    543    -20       O  
ATOM     27  OE2 GLU A  42     -53.654  24.102  99.853  1.00 49.67           O  
ANISOU   27  OE2 GLU A  42     6328   6381   6165    105    551     11       O  
ATOM     28  N   PRO A  43     -47.672  25.651  99.638  1.00 30.31           N  
ANISOU   28  N   PRO A  43     3996   3863   3658     57    383     10       N  
ATOM     29  CA  PRO A  43     -46.889  26.473  98.694  1.00 29.39           C  
ANISOU   29  CA  PRO A  43     3874   3727   3568     64    354      9       C  
ATOM     30  C   PRO A  43     -45.713  25.703  98.091  1.00 30.41           C  
ANISOU   30  C   PRO A  43     3995   3860   3701     47    312     32       C  
ATOM     31  O   PRO A  43     -45.332  25.962  96.943  1.00 29.72           O  
ANISOU   31  O   PRO A  43     3885   3762   3643     55    292     41       O  
ATOM     32  CB  PRO A  43     -46.410  27.653  99.558  1.00 31.80           C  
ANISOU   32  CB  PRO A  43     4220   4011   3849     61    356    -18       C  
ATOM     33  CG  PRO A  43     -47.286  27.630 100.772  1.00 36.91           C  
ANISOU   33  CG  PRO A  43     4889   4668   4466     61    396    -35       C  
ATOM     34  CD  PRO A  43     -47.628  26.209 101.003  1.00 32.26           C  
ANISOU   34  CD  PRO A  43     4287   4104   3865     49    401    -14       C  
ATOM     35  N   ARG A  44     -45.138  24.734  98.865  1.00 24.83           N  
ANISOU   35  N   ARG A  44     3306   3165   2963     25    299     42       N  
ATOM     36  CA AARG A  44     -44.017  23.926  98.391  0.50 23.66           C  
ANISOU   36  CA AARG A  44     3150   3020   2819     10    260     64       C  
ATOM     37  CA BARG A  44     -44.014  23.925  98.393  0.50 23.80           C  
ANISOU   37  CA BARG A  44     3168   3038   2836     10    260     64       C  
ATOM     38  C   ARG A  44     -44.470  22.939  97.309  1.00 26.48           C  
ANISOU   38  C   ARG A  44     3466   3388   3205     16    259     86       C  
ATOM     39  O   ARG A  44     -43.838  22.846  96.257  1.00 25.14           O  
ANISOU   39  O   ARG A  44     3277   3214   3060     18    235     98       O  
ATOM     40  CB AARG A  44     -43.345  23.181  99.564  0.50 22.55           C  
ANISOU   40  CB AARG A  44     3040   2889   2638    -14    246     70       C  
ATOM     41  CB BARG A  44     -43.355  23.171  99.564  0.50 23.34           C  
ANISOU   41  CB BARG A  44     3140   2989   2739    -14    247     70       C  
ATOM     42  CG AARG A  44     -42.217  22.254  99.123  0.50 29.10           C  
ANISOU   42  CG AARG A  44     3860   3723   3475    -27    208     94       C  
ATOM     43  CG BARG A  44     -41.937  22.682  99.248  0.50 32.36           C  
ANISOU   43  CG BARG A  44     4282   4129   3884    -28    202     87       C  
ATOM     44  CD AARG A  44     -41.551  21.564 100.291  0.50 31.47           C  
ANISOU   44  CD AARG A  44     4190   4030   3736    -48    191    102       C  
ATOM     45  CD BARG A  44     -41.375  21.769 100.333  0.50 38.65           C  
ANISOU   45  CD BARG A  44     5104   4937   4643    -49    187     99       C  
ATOM     46  NE AARG A  44     -40.555  22.416 100.936  0.50 34.92           N  
ANISOU   46  NE AARG A  44     4658   4456   4153    -60    168     88       N  
ATOM     47  NE BARG A  44     -41.301  22.433 101.637  0.50 46.84           N  
ANISOU   47  NE BARG A  44     6184   5972   5640    -59    195     79       N  
ATOM     48  CZ AARG A  44     -39.279  22.469 100.567  0.50 47.25           C  
ANISOU   48  CZ AARG A  44     6216   6011   5726    -68    129     97       C  
ATOM     49  CZ BARG A  44     -42.124  22.170 102.647  0.50 60.50           C  
ANISOU   49  CZ BARG A  44     7936   7714   7339    -63    223     74       C  
ATOM     50  NH1AARG A  44     -38.847  21.745  99.540  0.50 35.79           N  
ANISOU   50  NH1AARG A  44     4732   4562   4306    -65    112    118       N  
ATOM     51  NH1BARG A  44     -43.056  21.234 102.525  0.50 47.60           N  
ANISOU   51  NH1BARG A  44     6283   6094   5710    -60    246     88       N  
ATOM     52  NH2AARG A  44     -38.429  23.255 101.210  0.50 32.44           N  
ANISOU   52  NH2AARG A  44     4369   4127   3832    -81    108     83       N  
ATOM     53  NH2BARG A  44     -41.996  22.814 103.799  0.50 47.91           N  
ANISOU   53  NH2BARG A  44     6382   6116   5704    -73    230     54       N  
ATOM     54  N   LEU A  45     -45.581  22.213  97.563  1.00 22.43           N  
ANISOU   54  N   LEU A  45     2942   2892   2690     19    287     90       N  
ATOM     55  CA  LEU A  45     -46.127  21.237  96.615  1.00 21.65           C  
ANISOU   55  CA  LEU A  45     2805   2803   2616     22    288    109       C  
ATOM     56  C   LEU A  45     -46.689  21.931  95.347  1.00 24.06           C  
ANISOU   56  C   LEU A  45     3079   3103   2960     44    292    106       C  
ATOM     57  O   LEU A  45     -46.676  21.341  94.265  1.00 23.19           O  
ANISOU   57  O   LEU A  45     2941   2996   2873     46    279    121       O  
ATOM     58  CB  LEU A  45     -47.230  20.397  97.301  1.00 22.15           C  
ANISOU   58  CB  LEU A  45     2865   2885   2667     18    320    112       C  
ATOM     59  CG  LEU A  45     -47.781  19.203  96.498  1.00 26.90           C  
ANISOU   59  CG  LEU A  45     3432   3498   3290     15    320    132       C  
ATOM     60  CD1 LEU A  45     -46.699  18.134  96.278  1.00 26.43           C  
ANISOU   60  CD1 LEU A  45     3376   3438   3227     -1    287    152       C  
ATOM     61  CD2 LEU A  45     -48.968  18.596  97.193  1.00 30.11           C  
ANISOU   61  CD2 LEU A  45     3833   3919   3686     11    356    133       C  
ATOM     62  N   ALA A  46     -47.185  23.179  95.492  1.00 20.21           N  
ANISOU   62  N   ALA A  46     2598   2604   2477     60    311     86       N  
ATOM     63  CA  ALA A  46     -47.736  23.941  94.362  1.00 19.49           C  
ANISOU   63  CA  ALA A  46     2479   2505   2420     82    314     84       C  
ATOM     64  C   ALA A  46     -46.632  24.356  93.370  1.00 21.67           C  
ANISOU   64  C   ALA A  46     2753   2767   2713     82    280     92       C  
ATOM     65  O   ALA A  46     -46.880  24.409  92.162  1.00 21.42           O  
ANISOU   65  O   ALA A  46     2694   2735   2709     93    272    101       O  
ATOM     66  CB  ALA A  46     -48.472  25.172  94.869  1.00 20.60           C  
ANISOU   66  CB  ALA A  46     2630   2635   2562    101    342     62       C  
ATOM     67  N   SER A  47     -45.411  24.641  93.883  1.00 16.59           N  
ANISOU   67  N   SER A  47     2140   2114   2052     68    259     88       N  
ATOM     68  CA  SER A  47     -44.276  25.032  93.033  1.00 16.13           C  
ANISOU   68  CA  SER A  47     2080   2042   2008     65    229     94       C  
ATOM     69  C   SER A  47     -43.740  23.840  92.201  1.00 19.70           C  
ANISOU   69  C   SER A  47     2511   2506   2470     55    207    117       C  
ATOM     70  O   SER A  47     -43.137  24.052  91.148  1.00 19.59           O  
ANISOU   70  O   SER A  47     2484   2484   2475     57    189    125       O  
ATOM     71  CB  SER A  47     -43.151  25.633  93.879  1.00 18.75           C  
ANISOU   71  CB  SER A  47     2446   2360   2317     50    213     83       C  
ATOM     72  OG  SER A  47     -42.597  24.677  94.771  1.00 21.26           O  
ANISOU   72  OG  SER A  47     2780   2691   2608     30    203     89       O  
ATOM     73  N   THR A  48     -43.974  22.585  92.672  1.00 15.13           N  
ANISOU   73  N   THR A  48     1929   1943   1877     44    211    127       N  
ATOM     74  CA  THR A  48     -43.488  21.387  91.959  1.00 14.21           C  
ANISOU   74  CA  THR A  48     1794   1835   1770     35    192    146       C  
ATOM     75  C   THR A  48     -44.335  21.067  90.712  1.00 16.97           C  
ANISOU   75  C   THR A  48     2110   2192   2147     47    199    155       C  
ATOM     76  O   THR A  48     -43.899  20.287  89.861  1.00 15.70           O  
ANISOU   76  O   THR A  48     1934   2035   1998     42    183    168       O  
ATOM     77  CB  THR A  48     -43.393  20.187  92.905  1.00 20.92           C  
ANISOU   77  CB  THR A  48     2656   2697   2597     19    193    155       C  
ATOM     78  OG1 THR A  48     -44.703  19.825  93.338  1.00 20.36           O  
ANISOU   78  OG1 THR A  48     2577   2637   2520     22    222    152       O  
ATOM     79  CG2 THR A  48     -42.500  20.457  94.098  1.00 20.16           C  
ANISOU   79  CG2 THR A  48     2593   2595   2472      5    181    149       C  
ATOM     80  N   LEU A  49     -45.548  21.673  90.601  1.00 14.14           N  
ANISOU   80  N   LEU A  49     1740   1835   1798     63    222    146       N  
ATOM     81  CA  LEU A  49     -46.413  21.480  89.429  1.00 14.27           C  
ANISOU   81  CA  LEU A  49     1723   1858   1839     75    226    153       C  
ATOM     82  C   LEU A  49     -45.710  21.936  88.149  1.00 18.73           C  
ANISOU   82  C   LEU A  49     2280   2413   2423     81    203    160       C  
ATOM     83  O   LEU A  49     -45.355  21.099  87.314  1.00 19.06           O  
ANISOU   83  O   LEU A  49     2308   2461   2473     74    189    172       O  
ATOM     84  CB  LEU A  49     -47.756  22.221  89.605  1.00 14.55           C  
ANISOU   84  CB  LEU A  49     1747   1896   1884     94    253    142       C  
ATOM     85  CG  LEU A  49     -48.793  21.518  90.483  1.00 19.29           C  
ANISOU   85  CG  LEU A  49     2342   2512   2474     89    279    139       C  
ATOM     86  CD1 LEU A  49     -49.970  22.413  90.746  1.00 19.23           C  
ANISOU   86  CD1 LEU A  49     2325   2504   2477    109    307    126       C  
ATOM     87  CD2 LEU A  49     -49.256  20.211  89.847  1.00 22.48           C  
ANISOU   87  CD2 LEU A  49     2720   2932   2890     81    275    154       C  
ATOM     88  N   ARG A  50     -45.425  23.249  88.031  1.00 14.59           N  
ANISOU   88  N   ARG A  50     1767   1873   1904     91    201    151       N  
ATOM     89  CA  ARG A  50     -44.669  23.766  86.888  1.00 14.70           C  
ANISOU   89  CA  ARG A  50     1776   1876   1933     94    182    158       C  
ATOM     90  C   ARG A  50     -43.175  23.437  87.021  1.00 19.77           C  
ANISOU   90  C   ARG A  50     2434   2513   2566     76    160    163       C  
ATOM     91  O   ARG A  50     -42.498  23.205  86.015  1.00 18.83           O  
ANISOU   91  O   ARG A  50     2305   2392   2457     73    144    174       O  
ATOM     92  CB  ARG A  50     -44.869  25.278  86.737  1.00 15.59           C  
ANISOU   92  CB  ARG A  50     1896   1970   2056    111    187    149       C  
ATOM     93  CG  ARG A  50     -46.265  25.666  86.282  1.00 21.69           C  
ANISOU   93  CG  ARG A  50     2648   2747   2846    132    203    148       C  
ATOM     94  CD  ARG A  50     -46.288  27.075  85.731  1.00 22.54           C  
ANISOU   94  CD  ARG A  50     2760   2834   2969    150    202    145       C  
ATOM     95  NE  ARG A  50     -47.639  27.495  85.368  1.00 20.33           N  
ANISOU   95  NE  ARG A  50     2460   2558   2708    173    216    145       N  
ATOM     96  CZ  ARG A  50     -48.419  28.225  86.155  1.00 30.60           C  
ANISOU   96  CZ  ARG A  50     3765   3851   4011    188    239    130       C  
ATOM     97  NH1 ARG A  50     -47.981  28.635  87.339  1.00 18.15           N  
ANISOU   97  NH1 ARG A  50     2217   2263   2417    181    250    113       N  
ATOM     98  NH2 ARG A  50     -49.638  28.563  85.760  1.00 17.38           N  
ANISOU   98  NH2 ARG A  50     2067   2180   2357    211    251    132       N  
ATOM     99  N   GLY A  51     -42.682  23.408  88.262  1.00 17.36           N  
ANISOU   99  N   GLY A  51     2151   2205   2239     65    161    155       N  
ATOM    100  CA  GLY A  51     -41.276  23.145  88.552  1.00 17.87           C  
ANISOU  100  CA  GLY A  51     2230   2265   2296     48    139    160       C  
ATOM    101  C   GLY A  51     -40.803  21.779  88.094  1.00 22.88           C  
ANISOU  101  C   GLY A  51     2850   2911   2934     38    127    175       C  
ATOM    102  O   GLY A  51     -39.776  21.668  87.413  1.00 23.04           O  
ANISOU  102  O   GLY A  51     2864   2926   2962     33    109    183       O  
ATOM    103  N   GLY A  52     -41.544  20.736  88.488  1.00 19.40           N  
ANISOU  103  N   GLY A  52     2403   2484   2485     36    138    179       N  
ATOM    104  CA  GLY A  52     -41.220  19.354  88.136  1.00 19.40           C  
ANISOU  104  CA  GLY A  52     2391   2492   2487     26    128    193       C  
ATOM    105  C   GLY A  52     -41.219  19.093  86.642  1.00 23.37           C  
ANISOU  105  C   GLY A  52     2871   2997   3012     32    122    201       C  
ATOM    106  O   GLY A  52     -40.394  18.319  86.144  1.00 22.07           O  
ANISOU  106  O   GLY A  52     2701   2832   2853     25    109    211       O  
ATOM    107  N   LEU A  53     -42.141  19.751  85.907  1.00 20.79           N  
ANISOU  107  N   LEU A  53     2532   2671   2697     46    133    198       N  
ATOM    108  CA  LEU A  53     -42.230  19.617  84.451  1.00 21.15           C  
ANISOU  108  CA  LEU A  53     2558   2718   2759     52    127    205       C  
ATOM    109  C   LEU A  53     -41.104  20.416  83.749  1.00 22.34           C  
ANISOU  109  C   LEU A  53     2714   2856   2918     52    113    207       C  
ATOM    110  O   LEU A  53     -40.749  20.108  82.610  1.00 21.99           O  
ANISOU  110  O   LEU A  53     2659   2814   2884     52    105    215       O  
ATOM    111  CB  LEU A  53     -43.618  20.094  83.954  1.00 21.94           C  
ANISOU  111  CB  LEU A  53     2643   2824   2869     66    140    202       C  
ATOM    112  CG  LEU A  53     -43.884  19.934  82.445  1.00 27.41           C  
ANISOU  112  CG  LEU A  53     3317   3522   3576     72    132    210       C  
ATOM    113  CD1 LEU A  53     -43.933  18.461  82.046  1.00 27.80           C  
ANISOU  113  CD1 LEU A  53     3355   3583   3626     60    128    216       C  
ATOM    114  CD2 LEU A  53     -45.161  20.620  82.050  1.00 30.22           C  
ANISOU  114  CD2 LEU A  53     3659   3882   3942     88    141    207       C  
ATOM    115  N   ILE A  54     -40.536  21.435  84.450  1.00 16.87           N  
ANISOU  115  N   ILE A  54     2039   2151   2219     51    110    200       N  
ATOM    116  CA  ILE A  54     -39.461  22.300  83.909  1.00 15.92           C  
ANISOU  116  CA  ILE A  54     1925   2017   2107     50     98    201       C  
ATOM    117  C   ILE A  54     -39.931  23.081  82.652  1.00 16.92           C  
ANISOU  117  C   ILE A  54     2042   2140   2249     63    101    205       C  
ATOM    118  O   ILE A  54     -39.633  22.688  81.522  1.00 15.94           O  
ANISOU  118  O   ILE A  54     1906   2019   2132     62     95    214       O  
ATOM    119  CB  ILE A  54     -38.114  21.508  83.667  1.00 18.93           C  
ANISOU  119  CB  ILE A  54     2303   2399   2491     36     83    210       C  
ATOM    120  CG1 ILE A  54     -37.728  20.661  84.912  1.00 19.68           C  
ANISOU  120  CG1 ILE A  54     2407   2498   2572     25     78    210       C  
ATOM    121  CG2 ILE A  54     -36.971  22.469  83.265  1.00 19.60           C  
ANISOU  121  CG2 ILE A  54     2393   2470   2585     32     72    211       C  
ATOM    122  CD1 ILE A  54     -36.442  19.772  84.715  1.00 26.86           C  
ANISOU  122  CD1 ILE A  54     3310   3408   3487     14     62    220       C  
ATOM    123  N   ILE A  55     -40.708  24.134  82.862  1.00 12.87           N  
ANISOU  123  N   ILE A  55     1534   1619   1738     75    111    197       N  
ATOM    124  CA  ILE A  55     -41.177  25.005  81.772  1.00 12.78           C  
ANISOU  124  CA  ILE A  55     1515   1600   1739     89    112    202       C  
ATOM    125  C   ILE A  55     -40.803  26.477  82.061  1.00 15.93           C  
ANISOU  125  C   ILE A  55     1933   1977   2143     94    112    195       C  
ATOM    126  O   ILE A  55     -41.598  27.391  81.805  1.00 14.83           O  
ANISOU  126  O   ILE A  55     1794   1829   2012    110    119    193       O  
ATOM    127  CB  ILE A  55     -42.712  24.817  81.506  1.00 15.82           C  
ANISOU  127  CB  ILE A  55     1885   1998   2130    105    123    202       C  
ATOM    128  CG1 ILE A  55     -43.537  24.962  82.826  1.00 16.38           C  
ANISOU  128  CG1 ILE A  55     1961   2070   2193    110    139    189       C  
ATOM    129  CG2 ILE A  55     -42.982  23.467  80.818  1.00 15.61           C  
ANISOU  129  CG2 ILE A  55     1839   1990   2103     99    119    211       C  
ATOM    130  CD1 ILE A  55     -45.061  25.082  82.617  1.00 21.22           C  
ANISOU  130  CD1 ILE A  55     2555   2691   2816    128    152    188       C  
ATOM    131  N   GLU A  56     -39.578  26.696  82.580  1.00 12.71           N  
ANISOU  131  N   GLU A  56     1540   1559   1730     79    103    192       N  
ATOM    132  CA  GLU A  56     -39.094  28.035  82.945  1.00 12.16           C  
ANISOU  132  CA  GLU A  56     1490   1467   1664     78    102    184       C  
ATOM    133  C   GLU A  56     -38.241  28.692  81.816  1.00 15.73           C  
ANISOU  133  C   GLU A  56     1942   1906   2129     74     92    195       C  
ATOM    134  O   GLU A  56     -37.597  29.718  82.045  1.00 16.36           O  
ANISOU  134  O   GLU A  56     2037   1966   2214     69     89    190       O  
ATOM    135  CB  GLU A  56     -38.316  27.995  84.293  1.00 13.14           C  
ANISOU  135  CB  GLU A  56     1632   1587   1773     62     96    172       C  
ATOM    136  CG  GLU A  56     -37.481  26.731  84.504  1.00 17.33           C  
ANISOU  136  CG  GLU A  56     2156   2133   2296     45     84    179       C  
ATOM    137  CD  GLU A  56     -36.350  26.528  83.512  1.00 19.49           C  
ANISOU  137  CD  GLU A  56     2418   2405   2582     36     71    192       C  
ATOM    138  OE1 GLU A  56     -36.632  26.091  82.374  1.00  7.45           O  
ANISOU  138  OE1 GLU A  56      877    888   1066     43     74    203       O  
ATOM    139  OE2 GLU A  56     -35.177  26.687  83.914  1.00 13.37           O  
ANISOU  139  OE2 GLU A  56     1649   1623   1807     20     58    191       O  
ATOM    140  N   GLY A  57     -38.267  28.086  80.617  1.00 11.87           N  
ANISOU  140  N   GLY A  57     1436   1429   1646     76     89    210       N  
ATOM    141  CA  GLY A  57     -37.634  28.645  79.415  1.00 10.82           C  
ANISOU  141  CA  GLY A  57     1302   1287   1524     74     84    222       C  
ATOM    142  C   GLY A  57     -36.112  28.646  79.417  1.00 13.06           C  
ANISOU  142  C   GLY A  57     1588   1563   1810     54     75    225       C  
ATOM    143  O   GLY A  57     -35.492  29.129  78.464  1.00 10.80           O  
ANISOU  143  O   GLY A  57     1302   1269   1533     50     72    236       O  
ATOM    144  N   ASN A  58     -35.496  28.122  80.489  1.00 11.07           N  
ANISOU  144  N   ASN A  58     1340   1315   1551     41     69    217       N  
ATOM    145  CA  ASN A  58     -34.036  28.110  80.627  1.00 10.94           C  
ANISOU  145  CA  ASN A  58     1324   1294   1539     22     58    219       C  
ATOM    146  C   ASN A  58     -33.511  26.679  80.567  1.00 16.22           C  
ANISOU  146  C   ASN A  58     1977   1982   2206     15     53    225       C  
ATOM    147  O   ASN A  58     -32.993  26.258  79.528  1.00 16.25           O  
ANISOU  147  O   ASN A  58     1967   1991   2217     12     53    236       O  
ATOM    148  CB  ASN A  58     -33.612  28.806  81.943  1.00 12.50           C  
ANISOU  148  CB  ASN A  58     1540   1478   1731     12     51    205       C  
ATOM    149  CG  ASN A  58     -32.111  28.908  82.149  1.00 29.52           C  
ANISOU  149  CG  ASN A  58     3694   3628   3894    -10     37    206       C  
ATOM    150  OD1 ASN A  58     -31.300  28.420  81.342  1.00 19.54           O  
ANISOU  150  OD1 ASN A  58     2414   2370   2640    -16     33    219       O  
ATOM    151  ND2 ASN A  58     -31.710  29.541  83.244  1.00 19.09           N  
ANISOU  151  ND2 ASN A  58     2390   2295   2568    -21     28    194       N  
ATOM    152  N   VAL A  59     -33.697  25.901  81.663  1.00 12.61           N  
ANISOU  152  N   VAL A  59     1521   1534   1736     12     49    218       N  
ATOM    153  CA  VAL A  59     -33.351  24.476  81.671  1.00 11.73           C  
ANISOU  153  CA  VAL A  59     1396   1438   1623      8     45    224       C  
ATOM    154  C   VAL A  59     -34.287  23.730  80.708  1.00 12.41           C  
ANISOU  154  C   VAL A  59     1469   1536   1709     20     55    230       C  
ATOM    155  O   VAL A  59     -33.869  22.764  80.065  1.00 11.50           O  
ANISOU  155  O   VAL A  59     1341   1430   1598     17     54    237       O  
ATOM    156  CB  VAL A  59     -33.402  23.876  83.117  1.00 16.11           C  
ANISOU  156  CB  VAL A  59     1959   1999   2163      2     38    217       C  
ATOM    157  CG1 VAL A  59     -33.109  22.371  83.103  1.00 15.86           C  
ANISOU  157  CG1 VAL A  59     1914   1981   2131     -1     34    225       C  
ATOM    158  CG2 VAL A  59     -32.429  24.609  84.046  1.00 16.30           C  
ANISOU  158  CG2 VAL A  59     1997   2012   2186    -12     24    210       C  
ATOM    159  N   GLU A  60     -35.518  24.277  80.507  1.00  7.89           N  
ANISOU  159  N   GLU A  60      901    964   1134     33     65    226       N  
ATOM    160  CA  GLU A  60     -36.482  23.740  79.545  1.00  7.33           C  
ANISOU  160  CA  GLU A  60      818    904   1063     44     72    232       C  
ATOM    161  C   GLU A  60     -35.891  23.711  78.132  1.00 13.29           C  
ANISOU  161  C   GLU A  60     1565   1659   1826     42     71    243       C  
ATOM    162  O   GLU A  60     -36.010  22.699  77.437  1.00 13.60           O  
ANISOU  162  O   GLU A  60     1593   1710   1864     42     73    247       O  
ATOM    163  CB  GLU A  60     -37.773  24.572  79.555  1.00  8.25           C  
ANISOU  163  CB  GLU A  60      938   1017   1178     59     81    228       C  
ATOM    164  CG  GLU A  60     -38.812  24.078  78.556  1.00 11.96           C  
ANISOU  164  CG  GLU A  60     1394   1500   1650     70     85    234       C  
ATOM    165  CD  GLU A  60     -39.916  25.064  78.245  1.00 23.11           C  
ANISOU  165  CD  GLU A  60     2806   2907   3066     87     90    234       C  
ATOM    166  OE1 GLU A  60     -39.892  26.183  78.807  1.00 16.41           O  
ANISOU  166  OE1 GLU A  60     1972   2043   2221     91     93    228       O  
ATOM    167  OE2 GLU A  60     -40.772  24.741  77.392  1.00 14.29           O  
ANISOU  167  OE2 GLU A  60     1677   1801   1951     95     90    240       O  
ATOM    168  N   GLN A  61     -35.272  24.841  77.691  1.00 10.43           N  
ANISOU  168  N   GLN A  61     1210   1282   1471     40     70    246       N  
ATOM    169  CA  GLN A  61     -34.674  24.929  76.352  1.00  9.91           C  
ANISOU  169  CA  GLN A  61     1139   1216   1411     37     71    257       C  
ATOM    170  C   GLN A  61     -33.583  23.877  76.176  1.00 14.54           C  
ANISOU  170  C   GLN A  61     1715   1810   2001     26     70    260       C  
ATOM    171  O   GLN A  61     -33.487  23.256  75.116  1.00 15.14           O  
ANISOU  171  O   GLN A  61     1783   1894   2076     26     74    266       O  
ATOM    172  CB  GLN A  61     -34.097  26.341  76.103  1.00 10.98           C  
ANISOU  172  CB  GLN A  61     1286   1333   1555     34     71    261       C  
ATOM    173  CG  GLN A  61     -33.700  26.588  74.638  1.00 11.67           C  
ANISOU  173  CG  GLN A  61     1371   1419   1645     32     75    274       C  
ATOM    174  CD  GLN A  61     -32.901  27.868  74.455  1.00 28.39           C  
ANISOU  174  CD  GLN A  61     3499   3517   3773     24     76    280       C  
ATOM    175  OE1 GLN A  61     -32.251  28.372  75.385  1.00 28.04           O  
ANISOU  175  OE1 GLN A  61     3459   3460   3734     14     71    273       O  
ATOM    176  NE2 GLN A  61     -32.827  28.341  73.227  1.00 12.20           N  
ANISOU  176  NE2 GLN A  61     1451   1462   1722     25     81    293       N  
ATOM    177  N   ARG A  62     -32.820  23.622  77.238  1.00 11.43           N  
ANISOU  177  N   ARG A  62     1320   1413   1609     16     63    255       N  
ATOM    178  CA  ARG A  62     -31.654  22.739  77.193  1.00 11.26           C  
ANISOU  178  CA  ARG A  62     1286   1395   1595      6     59    259       C  
ATOM    179  C   ARG A  62     -31.998  21.241  77.320  1.00 17.25           C  
ANISOU  179  C   ARG A  62     2037   2168   2349     10     60    258       C  
ATOM    180  O   ARG A  62     -31.111  20.399  77.164  1.00 18.03           O  
ANISOU  180  O   ARG A  62     2125   2269   2456      5     59    261       O  
ATOM    181  CB  ARG A  62     -30.633  23.163  78.244  1.00  8.43           C  
ANISOU  181  CB  ARG A  62      930   1028   1243     -5     48    256       C  
ATOM    182  CG  ARG A  62     -30.012  24.500  77.926  1.00  9.98           C  
ANISOU  182  CG  ARG A  62     1133   1210   1449    -13     47    258       C  
ATOM    183  CD  ARG A  62     -29.639  25.279  79.163  1.00 21.14           C  
ANISOU  183  CD  ARG A  62     2558   2613   2862    -22     35    250       C  
ATOM    184  NE  ARG A  62     -28.874  26.478  78.821  1.00 26.28           N  
ANISOU  184  NE  ARG A  62     3213   3248   3525    -33     34    253       N  
ATOM    185  CZ  ARG A  62     -29.424  27.611  78.391  1.00 32.34           C  
ANISOU  185  CZ  ARG A  62     3994   4002   4292    -28     41    253       C  
ATOM    186  NH1 ARG A  62     -30.746  27.716  78.277  1.00 18.49           N  
ANISOU  186  NH1 ARG A  62     2248   2249   2527    -11     49    250       N  
ATOM    187  NH2 ARG A  62     -28.660  28.641  78.063  1.00 15.02           N  
ANISOU  187  NH2 ARG A  62     1805   1793   2111    -39     41    256       N  
ATOM    188  N   LEU A  63     -33.285  20.904  77.546  1.00 14.35           N  
ANISOU  188  N   LEU A  63     1673   1807   1971     18     63    254       N  
ATOM    189  CA  LEU A  63     -33.705  19.494  77.593  1.00 14.54           C  
ANISOU  189  CA  LEU A  63     1690   1842   1991     20     65    253       C  
ATOM    190  C   LEU A  63     -34.782  19.178  76.546  1.00 17.57           C  
ANISOU  190  C   LEU A  63     2071   2236   2371     27     73    253       C  
ATOM    191  O   LEU A  63     -34.850  18.051  76.061  1.00 16.80           O  
ANISOU  191  O   LEU A  63     1966   2145   2273     26     75    254       O  
ATOM    192  CB  LEU A  63     -34.183  19.087  79.024  1.00 14.64           C  
ANISOU  192  CB  LEU A  63     1709   1858   1997     19     60    248       C  
ATOM    193  CG  LEU A  63     -35.527  19.689  79.509  1.00 19.74           C  
ANISOU  193  CG  LEU A  63     2362   2505   2632     26     66    242       C  
ATOM    194  CD1 LEU A  63     -36.714  18.799  79.091  1.00 19.73           C  
ANISOU  194  CD1 LEU A  63     2353   2516   2627     32     73    241       C  
ATOM    195  CD2 LEU A  63     -35.531  19.845  80.999  1.00 22.77           C  
ANISOU  195  CD2 LEU A  63     2758   2887   3008     22     62    236       C  
ATOM    196  N   LYS A  64     -35.636  20.172  76.210  1.00 14.22           N  
ANISOU  196  N   LYS A  64     1651   1810   1942     35     75    253       N  
ATOM    197  CA  LYS A  64     -36.751  19.944  75.296  1.00 13.53           C  
ANISOU  197  CA  LYS A  64     1559   1732   1850     42     78    254       C  
ATOM    198  C   LYS A  64     -36.364  20.248  73.811  1.00 16.53           C  
ANISOU  198  C   LYS A  64     1939   2112   2229     42     80    262       C  
ATOM    199  O   LYS A  64     -35.980  19.326  73.094  1.00 16.14           O  
ANISOU  199  O   LYS A  64     1886   2069   2179     38     83    262       O  
ATOM    200  CB  LYS A  64     -38.019  20.725  75.752  1.00 14.83           C  
ANISOU  200  CB  LYS A  64     1726   1897   2011     53     79    251       C  
ATOM    201  CG  LYS A  64     -39.304  20.365  74.978  1.00 20.04           C  
ANISOU  201  CG  LYS A  64     2378   2570   2668     60     80    253       C  
ATOM    202  CD  LYS A  64     -39.747  18.915  75.222  1.00 18.87           C  
ANISOU  202  CD  LYS A  64     2221   2433   2517     54     81    249       C  
ATOM    203  CE  LYS A  64     -41.128  18.639  74.668  1.00 12.87           C  
ANISOU  203  CE  LYS A  64     1450   1686   1754     60     80    248       C  
ATOM    204  NZ  LYS A  64     -41.228  18.991  73.225  1.00 10.05           N  
ANISOU  204  NZ  LYS A  64     1093   1332   1395     63     75    255       N  
ATOM    205  N   PRO A  65     -36.368  21.543  73.350  1.00 12.33           N  
ANISOU  205  N   PRO A  65     1414   1571   1698     47     80    267       N  
ATOM    206  CA  PRO A  65     -36.042  21.804  71.934  1.00 11.88           C  
ANISOU  206  CA  PRO A  65     1361   1516   1639     46     83    276       C  
ATOM    207  C   PRO A  65     -34.620  21.392  71.540  1.00 13.42           C  
ANISOU  207  C   PRO A  65     1553   1707   1838     35     89    278       C  
ATOM    208  O   PRO A  65     -34.412  20.883  70.436  1.00 11.99           O  
ANISOU  208  O   PRO A  65     1371   1533   1651     32     94    280       O  
ATOM    209  CB  PRO A  65     -36.260  23.321  71.788  1.00 13.74           C  
ANISOU  209  CB  PRO A  65     1605   1738   1875     52     81    283       C  
ATOM    210  CG  PRO A  65     -36.232  23.851  73.173  1.00 17.99           C  
ANISOU  210  CG  PRO A  65     2147   2267   2421     53     79    275       C  
ATOM    211  CD  PRO A  65     -36.771  22.782  74.048  1.00 13.49           C  
ANISOU  211  CD  PRO A  65     1570   1708   1849     53     78    266       C  
ATOM    212  N   LEU A  66     -33.647  21.602  72.434  1.00  8.70           N  
ANISOU  212  N   LEU A  66      954   1101   1251     28     88    276       N  
ATOM    213  CA  LEU A  66     -32.246  21.365  72.095  1.00  7.62           C  
ANISOU  213  CA  LEU A  66      811    960   1123     18     93    279       C  
ATOM    214  C   LEU A  66     -31.746  19.963  72.482  1.00 10.46           C  
ANISOU  214  C   LEU A  66     1160   1326   1487     15     94    273       C  
ATOM    215  O   LEU A  66     -30.571  19.668  72.292  1.00 10.20           O  
ANISOU  215  O   LEU A  66     1120   1291   1466      9     99    275       O  
ATOM    216  CB  LEU A  66     -31.343  22.462  72.687  1.00  7.49           C  
ANISOU  216  CB  LEU A  66      798    930   1118     11     90    281       C  
ATOM    217  CG  LEU A  66     -31.750  23.920  72.337  1.00 12.07           C  
ANISOU  217  CG  LEU A  66     1391   1499   1696     14     90    287       C  
ATOM    218  CD1 LEU A  66     -30.779  24.914  72.937  1.00 11.75           C  
ANISOU  218  CD1 LEU A  66     1353   1443   1667      4     87    288       C  
ATOM    219  CD2 LEU A  66     -31.857  24.118  70.830  1.00 14.34           C  
ANISOU  219  CD2 LEU A  66     1682   1790   1976     16     99    297       C  
ATOM    220  N   GLN A  67     -32.656  19.069  72.939  1.00  7.54           N  
ANISOU  220  N   GLN A  67      789    964   1111     20     90    267       N  
ATOM    221  CA  GLN A  67     -32.286  17.670  73.201  1.00  7.49           C  
ANISOU  221  CA  GLN A  67      774    961   1109     18     91    264       C  
ATOM    222  C   GLN A  67     -33.358  16.657  72.737  1.00 11.48           C  
ANISOU  222  C   GLN A  67     1281   1477   1606     21     94    259       C  
ATOM    223  O   GLN A  67     -33.265  16.155  71.624  1.00  9.68           O  
ANISOU  223  O   GLN A  67     1052   1252   1374     21    102    258       O  
ATOM    224  CB  GLN A  67     -31.881  17.446  74.676  1.00  8.87           C  
ANISOU  224  CB  GLN A  67      947   1132   1292     15     82    262       C  
ATOM    225  CG  GLN A  67     -30.529  18.084  75.036  1.00 14.53           C  
ANISOU  225  CG  GLN A  67     1659   1840   2022      8     78    266       C  
ATOM    226  CD  GLN A  67     -29.839  17.369  76.168  1.00 22.05           C  
ANISOU  226  CD  GLN A  67     2605   2790   2983      5     68    267       C  
ATOM    227  OE1 GLN A  67     -29.327  16.247  76.008  1.00 14.98           O  
ANISOU  227  OE1 GLN A  67     1700   1896   2096      6     70    268       O  
ATOM    228  NE2 GLN A  67     -29.663  18.063  77.284  1.00  4.19           N  
ANISOU  228  NE2 GLN A  67      451    527    612     11     16    112       N  
ATOM    229  N   ILE A  68     -34.384  16.361  73.599  1.00 10.14           N  
ANISOU  229  N   ILE A  68     1111   1310   1431     24     88    255       N  
ATOM    230  CA  ILE A  68     -35.392  15.311  73.290  1.00  9.93           C  
ANISOU  230  CA  ILE A  68     1084   1293   1398     24     89    251       C  
ATOM    231  C   ILE A  68     -36.230  15.598  72.027  1.00 12.99           C  
ANISOU  231  C   ILE A  68     1472   1687   1774     27     91    250       C  
ATOM    232  O   ILE A  68     -36.750  14.658  71.414  1.00 12.48           O  
ANISOU  232  O   ILE A  68     1408   1630   1705     24     92    246       O  
ATOM    233  CB  ILE A  68     -36.270  14.927  74.528  1.00 13.58           C  
ANISOU  233  CB  ILE A  68     1545   1757   1858     24     85    248       C  
ATOM    234  CG1 ILE A  68     -37.229  16.062  74.926  1.00 13.22           C  
ANISOU  234  CG1 ILE A  68     1502   1714   1807     30     82    248       C  
ATOM    235  CG2 ILE A  68     -35.389  14.479  75.714  1.00 15.29           C  
ANISOU  235  CG2 ILE A  68     1762   1966   2082     21     81    250       C  
ATOM    236  CD1 ILE A  68     -38.246  15.660  76.083  1.00 14.67           C  
ANISOU  236  CD1 ILE A  68     1685   1903   1988     31     82    245       C  
ATOM    237  N   ASP A  69     -36.324  16.895  71.607  1.00  9.32           N  
ANISOU  237  N   ASP A  69     1013   1222   1306     31     89    256       N  
ATOM    238  CA  ASP A  69     -36.945  17.248  70.325  1.00  9.55           C  
ANISOU  238  CA  ASP A  69     1046   1258   1324     34     88    259       C  
ATOM    239  C   ASP A  69     -36.072  16.775  69.178  1.00 16.19           C  
ANISOU  239  C   ASP A  69     1891   2100   2161     28     97    259       C  
ATOM    240  O   ASP A  69     -36.585  16.237  68.200  1.00 16.95           O  
ANISOU  240  O   ASP A  69     1990   2205   2246     26     97    256       O  
ATOM    241  CB  ASP A  69     -37.178  18.760  70.221  1.00 10.38           C  
ANISOU  241  CB  ASP A  69     1157   1359   1429     41     85    267       C  
ATOM    242  CG  ASP A  69     -38.396  19.248  70.974  1.00 14.85           C  
ANISOU  242  CG  ASP A  69     1720   1927   1996     49     78    266       C  
ATOM    243  OD1 ASP A  69     -38.919  18.485  71.813  1.00 15.73           O  
ANISOU  243  OD1 ASP A  69     1824   2043   2110     48     78    260       O  
ATOM    244  OD2 ASP A  69     -38.817  20.405  70.739  1.00 14.63           O  
ANISOU  244  OD2 ASP A  69     1695   1895   1967     58     75    273       O  
ATOM    245  N   PHE A  70     -34.729  16.957  69.304  1.00 13.11           N  
ANISOU  245  N   PHE A  70     1500   1701   1782     25    104    261       N  
ATOM    246  CA  PHE A  70     -33.772  16.479  68.295  1.00 13.03           C  
ANISOU  246  CA  PHE A  70     1492   1691   1770     20    117    260       C  
ATOM    247  C   PHE A  70     -33.758  14.954  68.251  1.00 17.26           C  
ANISOU  247  C   PHE A  70     2023   2228   2307     17    121    250       C  
ATOM    248  O   PHE A  70     -33.631  14.369  67.172  1.00 18.14           O  
ANISOU  248  O   PHE A  70     2139   2343   2409     14    130    245       O  
ATOM    249  CB  PHE A  70     -32.343  17.002  68.592  1.00 14.40           C  
ANISOU  249  CB  PHE A  70     1660   1853   1957     16    124    265       C  
ATOM    250  CG  PHE A  70     -32.132  18.488  68.407  1.00 15.57           C  
ANISOU  250  CG  PHE A  70     1814   1996   2105     16    123    276       C  
ATOM    251  CD1 PHE A  70     -32.834  19.191  67.432  1.00 17.95           C  
ANISOU  251  CD1 PHE A  70     2127   2302   2391     18    122    282       C  
ATOM    252  CD2 PHE A  70     -31.102  19.148  69.075  1.00 17.06           C  
ANISOU  252  CD2 PHE A  70     1998   2175   2310     12    123    280       C  
ATOM    253  CE1 PHE A  70     -32.598  20.552  67.222  1.00 19.02           C  
ANISOU  253  CE1 PHE A  70     2270   2430   2527     18    122    293       C  
ATOM    254  CE2 PHE A  70     -30.852  20.505  68.846  1.00 19.61           C  
ANISOU  254  CE2 PHE A  70     2327   2490   2633      9    124    289       C  
ATOM    255  CZ  PHE A  70     -31.605  21.200  67.928  1.00 17.96           C  
ANISOU  255  CZ  PHE A  70     2132   2284   2410     13    124    296       C  
ATOM    256  N   TYR A  71     -33.830  14.306  69.432  1.00 11.47           N  
ANISOU  256  N   TYR A  71     1282   1490   1584     18    116    247       N  
ATOM    257  CA  TYR A  71     -33.731  12.845  69.529  1.00 10.16           C  
ANISOU  257  CA  TYR A  71     1114   1323   1424     16    120    239       C  
ATOM    258  C   TYR A  71     -34.957  12.153  68.904  1.00 13.25           C  
ANISOU  258  C   TYR A  71     1510   1723   1802     13    117    231       C  
ATOM    259  O   TYR A  71     -34.801  11.209  68.128  1.00 11.86           O  
ANISOU  259  O   TYR A  71     1338   1547   1622     10    125    223       O  
ATOM    260  CB  TYR A  71     -33.530  12.405  70.999  1.00 10.22           C  
ANISOU  260  CB  TYR A  71     1114   1323   1444     17    113    240       C  
ATOM    261  CG  TYR A  71     -32.363  13.101  71.696  1.00 10.14           C  
ANISOU  261  CG  TYR A  71     1099   1307   1448     17    111    247       C  
ATOM    262  CD1 TYR A  71     -31.299  13.630  70.964  1.00 11.77           C  
ANISOU  262  CD1 TYR A  71     1303   1511   1660     17    120    250       C  
ATOM    263  CD2 TYR A  71     -32.283  13.148  73.084  1.00 10.84           C  
ANISOU  263  CD2 TYR A  71     1184   1391   1543     17    101    251       C  
ATOM    264  CE1 TYR A  71     -30.240  14.282  71.594  1.00 12.31           C  
ANISOU  264  CE1 TYR A  71     1363   1571   1742     15    117    257       C  
ATOM    265  CE2 TYR A  71     -31.210  13.770  73.729  1.00 11.67           C  
ANISOU  265  CE2 TYR A  71     1284   1490   1659     16     96    256       C  
ATOM    266  CZ  TYR A  71     -30.188  14.334  72.978  1.00 17.96           C  
ANISOU  266  CZ  TYR A  71     2077   2284   2464     15    104    259       C  
ATOM    267  OH  TYR A  71     -29.136  14.959  73.604  1.00 15.68           O  
ANISOU  267  OH  TYR A  71     1779   1989   2188     12     98    265       O  
ATOM    268  N   SER A  72     -36.169  12.675  69.186  1.00 10.01           N  
ANISOU  268  N   SER A  72     1100   1320   1383     14    106    234       N  
ATOM    269  CA  SER A  72     -37.402  12.160  68.583  1.00 10.07           C  
ANISOU  269  CA  SER A  72     1109   1338   1379     11    100    228       C  
ATOM    270  C   SER A  72     -37.599  12.740  67.168  1.00 13.56           C  
ANISOU  270  C   SER A  72     1559   1789   1804     10    100    230       C  
ATOM    271  O   SER A  72     -38.397  12.209  66.387  1.00 13.23           O  
ANISOU  271  O   SER A  72     1521   1755   1750      5     95    224       O  
ATOM    272  CB  SER A  72     -38.606  12.502  69.459  1.00 13.96           C  
ANISOU  272  CB  SER A  72     1595   1837   1873     13     90    231       C  
ATOM    273  OG  SER A  72     -38.739  13.907  69.619  1.00 21.36           O  
ANISOU  273  OG  SER A  72     2532   2775   2809     21     86    239       O  
ATOM    274  N   GLN A  73     -36.883  13.860  66.855  1.00  9.60           N  
ANISOU  274  N   GLN A  73     1061   1283   1301     15    104    238       N  
ATOM    275  CA  GLN A  73     -36.997  14.588  65.572  1.00  9.12           C  
ANISOU  275  CA  GLN A  73     1012   1231   1224     14    103    244       C  
ATOM    276  C   GLN A  73     -38.395  15.214  65.378  1.00 12.08           C  
ANISOU  276  C   GLN A  73     1386   1615   1589     19     86    249       C  
ATOM    277  O   GLN A  73     -38.789  15.512  64.244  1.00 11.81           O  
ANISOU  277  O   GLN A  73     1360   1590   1537     17     81    253       O  
ATOM    278  CB  GLN A  73     -36.600  13.697  64.371  1.00 10.43           C  
ANISOU  278  CB  GLN A  73     1188   1399   1376      7    113    235       C  
ATOM    279  CG  GLN A  73     -35.113  13.332  64.355  1.00 13.03           C  
ANISOU  279  CG  GLN A  73     1516   1717   1716      6    132    232       C  
ATOM    280  CD  GLN A  73     -34.725  12.587  63.099  1.00 26.28           C  
ANISOU  280  CD  GLN A  73     3207   3399   3380      0    146    222       C  
ATOM    281  OE1 GLN A  73     -35.123  12.945  61.985  1.00 20.48           O  
ANISOU  281  OE1 GLN A  73     2485   2673   2622     -4    144    224       O  
ATOM    282  NE2 GLN A  73     -33.846  11.611  63.242  1.00 14.85           N  
ANISOU  282  NE2 GLN A  73     1756   1942   1945     -1    161    212       N  
HETATM  283  N   MSE A  74     -39.112  15.486  66.506  1.00  7.43           N  
ANISOU  283  N   MSE A  74      786   1026   1012     24     79    251       N  
HETATM  284  CA  MSE A  74     -40.424  16.150  66.466  1.00  6.24           C  
ANISOU  284  CA  MSE A  74      630    884    857     31     64    257       C  
HETATM  285  C   MSE A  74     -40.294  17.620  66.048  1.00 12.98           C  
ANISOU  285  C   MSE A  74     1490   1734   1707     40     61    270       C  
HETATM  286  O   MSE A  74     -41.145  18.127  65.319  1.00 13.74           O  
ANISOU  286  O   MSE A  74     1589   1839   1794     45     49    278       O  
HETATM  287  CB  MSE A  74     -41.151  16.021  67.817  1.00  6.30           C  
ANISOU  287  CB  MSE A  74      624    891    878     35     62    254       C  
HETATM  288  CG  MSE A  74     -41.672  14.631  68.077  1.00 10.72           C  
ANISOU  288  CG  MSE A  74     1177   1457   1440     26     62    243       C  
HETATM  289 SE   MSE A  74     -43.027  14.589  69.447  0.75 16.15          SE  
ANISOU  289 SE   MSE A  74     1847   2149   2140     30     58    242      SE  
HETATM  290  CE  MSE A  74     -43.600  12.751  69.239  1.00 13.37           C  
ANISOU  290  CE  MSE A  74     1489   1804   1786     13     57    230       C  
ATOM    291  N   THR A  75     -39.231  18.310  66.528  1.00 11.27           N  
ANISOU  291  N   THR A  75     1278   1504   1499     42     71    275       N  
ATOM    292  CA  THR A  75     -38.877  19.663  66.067  1.00 11.68           C  
ANISOU  292  CA  THR A  75     1341   1549   1550     47     71    288       C  
ATOM    293  C   THR A  75     -37.373  19.761  65.911  1.00 15.99           C  
ANISOU  293  C   THR A  75     1893   2085   2098     39     85    289       C  
ATOM    294  O   THR A  75     -36.637  19.041  66.593  1.00 16.26           O  
ANISOU  294  O   THR A  75     1920   2114   2142     34     93    281       O  
ATOM    295  CB  THR A  75     -39.406  20.760  67.039  1.00 21.53           C  
ANISOU  295  CB  THR A  75     2583   2787   2809     58     65    293       C  
ATOM    296  OG1 THR A  75     -38.567  20.828  68.191  1.00 24.87           O  
ANISOU  296  OG1 THR A  75     3005   3199   3247     56     73    288       O  
ATOM    297  CG2 THR A  75     -40.856  20.552  67.438  1.00 18.02           C  
ANISOU  297  CG2 THR A  75     2127   2353   2367     66     55    290       C  
ATOM    298  N   VAL A  76     -36.900  20.632  65.006  1.00 11.99           N  
ANISOU  298  N   VAL A  76     1399   1574   1584     38     89    301       N  
ATOM    299  CA  VAL A  76     -35.462  20.803  64.787  1.00 11.15           C  
ANISOU  299  CA  VAL A  76     1297   1459   1482     30    105    303       C  
ATOM    300  C   VAL A  76     -35.081  22.282  64.761  1.00 15.69           C  
ANISOU  300  C   VAL A  76     1879   2020   2061     32    105    317       C  
ATOM    301  O   VAL A  76     -35.233  22.948  63.730  1.00 14.79           O  
ANISOU  301  O   VAL A  76     1778   1907   1934     33    105    330       O  
ATOM    302  CB  VAL A  76     -34.961  20.054  63.504  1.00 14.28           C  
ANISOU  302  CB  VAL A  76     1701   1864   1861     22    116    301       C  
ATOM    303  CG1 VAL A  76     -33.449  20.189  63.350  1.00 14.14           C  
ANISOU  303  CG1 VAL A  76     1684   1838   1852     14    136    303       C  
ATOM    304  CG2 VAL A  76     -35.369  18.586  63.530  1.00 13.86           C  
ANISOU  304  CG2 VAL A  76     1642   1821   1804     19    115    285       C  
ATOM    305  N   ASP A  77     -34.580  22.800  65.895  1.00 13.06           N  
ANISOU  305  N   ASP A  77     1541   1675   1748     32    106    316       N  
ATOM    306  CA  ASP A  77     -34.040  24.149  65.956  1.00 12.16           C  
ANISOU  306  CA  ASP A  77     1435   1544   1641     31    108    327       C  
ATOM    307  C   ASP A  77     -32.909  24.269  64.934  1.00 16.88           C  
ANISOU  307  C   ASP A  77     2039   2141   2234     20    124    335       C  
ATOM    308  O   ASP A  77     -32.067  23.374  64.838  1.00 16.48           O  
ANISOU  308  O   ASP A  77     1980   2095   2186     12    135    328       O  
ATOM    309  CB  ASP A  77     -33.519  24.454  67.379  1.00 13.11           C  
ANISOU  309  CB  ASP A  77     1547   1652   1781     29    106    320       C  
ATOM    310  CG  ASP A  77     -33.058  25.885  67.573  1.00 16.42           C  
ANISOU  310  CG  ASP A  77     1976   2052   2210     27    107    329       C  
ATOM    311  OD1 ASP A  77     -32.031  26.264  66.970  1.00 15.09           O  
ANISOU  311  OD1 ASP A  77     1811   1878   2045     16    117    337       O  
ATOM    312  OD2 ASP A  77     -33.649  26.586  68.414  1.00 23.86           O  
ANISOU  312  OD2 ASP A  77     2922   2985   3160     34     98    327       O  
ATOM    313  N   GLY A  78     -32.955  25.324  64.121  1.00 14.20           N  
ANISOU  313  N   GLY A  78     1714   1795   1887     19    125    351       N  
ATOM    314  CA  GLY A  78     -32.013  25.514  63.020  1.00 14.35           C  
ANISOU  314  CA  GLY A  78     1742   1814   1897      8    141    361       C  
ATOM    315  C   GLY A  78     -30.576  25.773  63.440  1.00 18.43           C  
ANISOU  315  C   GLY A  78     2251   2319   2434     -5    156    360       C  
ATOM    316  O   GLY A  78     -29.671  25.742  62.604  1.00 19.51           O  
ANISOU  316  O   GLY A  78     2390   2457   2566    -15    174    366       O  
ATOM    317  N   GLY A  79     -30.367  26.026  64.737  1.00 13.83           N  
ANISOU  317  N   GLY A  79     1657   1726   1872     -4    148    353       N  
ATOM    318  CA  GLY A  79     -29.045  26.349  65.279  1.00 13.41           C  
ANISOU  318  CA  GLY A  79     1594   1661   1840    -17    156    353       C  
ATOM    319  C   GLY A  79     -28.036  25.216  65.182  1.00 16.97           C  
ANISOU  319  C   GLY A  79     2027   2121   2297    -25    170    345       C  
ATOM    320  O   GLY A  79     -28.411  24.044  65.059  1.00 15.83           O  
ANISOU  320  O   GLY A  79     1878   1991   2145    -18    170    335       O  
ATOM    321  N   GLY A  80     -26.750  25.570  65.269  1.00 14.09           N  
ANISOU  321  N   GLY A  80     1653   1749   1951    -38    181    348       N  
ATOM    322  CA  GLY A  80     -25.658  24.605  65.196  1.00 13.94           C  
ANISOU  322  CA  GLY A  80     1615   1738   1944    -44    196    342       C  
ATOM    323  C   GLY A  80     -25.335  23.974  66.530  1.00 18.27           C  
ANISOU  323  C   GLY A  80     2145   2286   2513    -42    183    330       C  
ATOM    324  O   GLY A  80     -24.196  24.054  67.001  1.00 17.83           O  
ANISOU  324  O   GLY A  80     2072   2225   2479    -52    186    331       O  
ATOM    325  N   TRP A  81     -26.335  23.320  67.152  1.00 15.24           N  
ANISOU  325  N   TRP A  81     1763   1907   2120    -30    168    321       N  
ATOM    326  CA  TRP A  81     -26.151  22.661  68.446  1.00 15.37           C  
ANISOU  326  CA  TRP A  81     1766   1924   2151    -28    154    311       C  
ATOM    327  C   TRP A  81     -25.602  21.250  68.262  1.00 19.97           C  
ANISOU  327  C   TRP A  81     2333   2516   2740    -26    164    304       C  
ATOM    328  O   TRP A  81     -26.101  20.493  67.427  1.00 19.69           O  
ANISOU  328  O   TRP A  81     2303   2489   2690    -20    173    301       O  
ATOM    329  CB  TRP A  81     -27.474  22.628  69.232  1.00 14.17           C  
ANISOU  329  CB  TRP A  81     1623   1772   1987    -18    137    305       C  
ATOM    330  CG  TRP A  81     -28.089  23.980  69.432  1.00 15.28           C  
ANISOU  330  CG  TRP A  81     1780   1903   2124    -17    128    311       C  
ATOM    331  CD1 TRP A  81     -29.108  24.532  68.714  1.00 18.19           C  
ANISOU  331  CD1 TRP A  81     2164   2272   2476    -10    128    316       C  
ATOM    332  CD2 TRP A  81     -27.659  24.987  70.359  1.00 15.42           C  
ANISOU  332  CD2 TRP A  81     1799   1906   2154    -25    119    311       C  
ATOM    333  NE1 TRP A  81     -29.379  25.801  69.174  1.00 17.88           N  
ANISOU  333  NE1 TRP A  81     2135   2218   2440    -10    121    320       N  
ATOM    334  CE2 TRP A  81     -28.498  26.108  70.180  1.00 19.34           C  
ANISOU  334  CE2 TRP A  81     2314   2393   2642    -20    115    316       C  
ATOM    335  CE3 TRP A  81     -26.636  25.053  71.325  1.00 16.87           C  
ANISOU  335  CE3 TRP A  81     1970   2083   2355    -35    112    308       C  
ATOM    336  CZ2 TRP A  81     -28.365  27.272  70.945  1.00 18.66           C  
ANISOU  336  CZ2 TRP A  81     2236   2290   2565    -25    107    316       C  
ATOM    337  CZ3 TRP A  81     -26.515  26.201  72.091  1.00 18.33           C  
ANISOU  337  CZ3 TRP A  81     2164   2253   2548    -42    102    307       C  
ATOM    338  CH2 TRP A  81     -27.370  27.294  71.898  1.00 19.04           C  
ANISOU  338  CH2 TRP A  81     2274   2332   2629    -37    101    310       C  
ATOM    339  N   GLY A  82     -24.576  20.910  69.045  1.00 16.55           N  
ANISOU  339  N   GLY A  82     1880   2079   2329    -30    160    303       N  
ATOM    340  CA  GLY A  82     -23.904  19.615  68.959  1.00 16.02           C  
ANISOU  340  CA  GLY A  82     1795   2017   2274    -26    169    297       C  
ATOM    341  C   GLY A  82     -24.769  18.441  69.371  1.00 18.52           C  
ANISOU  341  C   GLY A  82     2115   2339   2581    -15    161    288       C  
ATOM    342  O   GLY A  82     -24.518  17.309  68.950  1.00 17.99           O  
ANISOU  342  O   GLY A  82     2042   2276   2519     -9    172    283       O  
ATOM    343  N   THR A  83     -25.810  18.699  70.208  1.00 14.22           N  
ANISOU  343  N   THR A  83     1582   1794   2026    -12    142    286       N  
ATOM    344  CA  THR A  83     -26.749  17.648  70.648  1.00 13.27           C  
ANISOU  344  CA  THR A  83     1467   1679   1897     -3    134    279       C  
ATOM    345  C   THR A  83     -27.534  17.087  69.472  1.00 16.01           C  
ANISOU  345  C   THR A  83     1824   2033   2225      2    147    274       C  
ATOM    346  O   THR A  83     -28.012  15.959  69.535  1.00 15.22           O  
ANISOU  346  O   THR A  83     1725   1937   2122      7    146    267       O  
ATOM    347  CB  THR A  83     -27.671  18.177  71.742  1.00 21.41           C  
ANISOU  347  CB  THR A  83     2507   2708   2919     -1    116    278       C  
ATOM    348  OG1 THR A  83     -28.218  19.431  71.322  1.00 20.32           O  
ANISOU  348  OG1 THR A  83     2382   2567   2770     -3    116    282       O  
ATOM    349  CG2 THR A  83     -26.954  18.340  73.081  1.00 20.62           C  
ANISOU  349  CG2 THR A  83     2399   2602   2834     -6    101    279       C  
ATOM    350  N   LYS A  84     -27.647  17.876  68.377  1.00 12.53           N  
ANISOU  350  N   LYS A  84     1394   1594   1772     -1    157    279       N  
ATOM    351  CA  LYS A  84     -28.261  17.426  67.127  1.00 12.06           C  
ANISOU  351  CA  LYS A  84     1346   1543   1693      1    168    276       C  
ATOM    352  C   LYS A  84     -27.435  16.255  66.548  1.00 15.99           C  
ANISOU  352  C   LYS A  84     1835   2042   2199      1    186    268       C  
ATOM    353  O   LYS A  84     -27.999  15.311  65.990  1.00 15.49           O  
ANISOU  353  O   LYS A  84     1778   1983   2122      5    191    259       O  
ATOM    354  CB  LYS A  84     -28.313  18.592  66.122  1.00 13.99           C  
ANISOU  354  CB  LYS A  84     1604   1789   1925     -3    175    285       C  
ATOM    355  CG  LYS A  84     -29.308  18.391  64.986  1.00 22.60           C  
ANISOU  355  CG  LYS A  84     2711   2889   2988     -1    178    284       C  
ATOM    356  CD  LYS A  84     -29.341  19.605  64.033  1.00 24.87           C  
ANISOU  356  CD  LYS A  84     3013   3176   3261     -5    183    297       C  
ATOM    357  CE  LYS A  84     -29.847  20.862  64.710  1.00 27.73           C  
ANISOU  357  CE  LYS A  84     3379   3530   3628     -3    167    306       C  
ATOM    358  NZ  LYS A  84     -29.855  22.023  63.783  1.00 34.12           N  
ANISOU  358  NZ  LYS A  84     4204   4337   4425     -6    172    321       N  
ATOM    359  N   ASN A  85     -26.105  16.285  66.776  1.00 12.98           N  
ANISOU  359  N   ASN A  85     1437   1655   1840     -1    195    271       N  
ATOM    360  CA  ASN A  85     -25.188  15.231  66.340  1.00 12.84           C  
ANISOU  360  CA  ASN A  85     1407   1636   1835      1    214    265       C  
ATOM    361  C   ASN A  85     -24.935  14.234  67.492  1.00 17.20           C  
ANISOU  361  C   ASN A  85     1944   2183   2408      8    202    261       C  
ATOM    362  O   ASN A  85     -23.951  13.488  67.464  1.00 16.48           O  
ANISOU  362  O   ASN A  85     1837   2088   2338     11    214    258       O  
ATOM    363  CB  ASN A  85     -23.870  15.844  65.867  1.00 13.73           C  
ANISOU  363  CB  ASN A  85     1507   1747   1964     -5    232    272       C  
ATOM    364  CG  ASN A  85     -24.053  16.971  64.889  1.00 27.24           C  
ANISOU  364  CG  ASN A  85     3233   3461   3655    -13    242    280       C  
ATOM    365  OD1 ASN A  85     -23.811  18.137  65.203  1.00 22.96           O  
ANISOU  365  OD1 ASN A  85     2690   2914   3118    -21    236    290       O  
ATOM    366  ND2 ASN A  85     -24.613  16.663  63.726  1.00 14.92           N  
ANISOU  366  ND2 ASN A  85     1691   1908   2070    -12    255    275       N  
ATOM    367  N   TYR A  86     -25.820  14.255  68.525  1.00 14.22           N  
ANISOU  367  N   TYR A  86     1572   1805   2025      9    179    261       N  
ATOM    368  CA  TYR A  86     -25.742  13.369  69.711  1.00 13.90           C  
ANISOU  368  CA  TYR A  86     1522   1760   1999     14    165    260       C  
ATOM    369  C   TYR A  86     -24.499  13.647  70.601  1.00 16.98           C  
ANISOU  369  C   TYR A  86     1892   2144   2416     12    157    268       C  
ATOM    370  O   TYR A  86     -24.207  12.862  71.511  1.00 16.38           O  
ANISOU  370  O   TYR A  86     1806   2063   2354     17    146    269       O  
ATOM    371  CB  TYR A  86     -25.827  11.866  69.312  1.00 14.97           C  
ANISOU  371  CB  TYR A  86     1658   1893   2138     21    176    250       C  
ATOM    372  CG  TYR A  86     -27.037  11.517  68.459  1.00 16.71           C  
ANISOU  372  CG  TYR A  86     1897   2119   2332     21    181    241       C  
ATOM    373  CD1 TYR A  86     -28.237  12.215  68.594  1.00 18.57           C  
ANISOU  373  CD1 TYR A  86     2147   2362   2548     17    168    243       C  
ATOM    374  CD2 TYR A  86     -27.025  10.406  67.621  1.00 17.46           C  
ANISOU  374  CD2 TYR A  86     1997   2212   2426     24    197    230       C  
ATOM    375  CE1 TYR A  86     -29.356  11.886  67.830  1.00 19.61           C  
ANISOU  375  CE1 TYR A  86     2293   2500   2658     16    169    236       C  
ATOM    376  CE2 TYR A  86     -28.145  10.053  66.868  1.00 18.32           C  
ANISOU  376  CE2 TYR A  86     2123   2326   2510     21    198    221       C  
ATOM    377  CZ  TYR A  86     -29.309  10.795  66.975  1.00 26.83           C  
ANISOU  377  CZ  TYR A  86     3213   3414   3569     17    183    225       C  
ATOM    378  OH  TYR A  86     -30.415  10.447  66.237  1.00 27.45           O  
ANISOU  378  OH  TYR A  86     3306   3499   3626     14    182    217       O  
ATOM    379  N   ILE A  87     -23.809  14.786  70.372  1.00 12.85           N  
ANISOU  379  N   ILE A  87     1362   1620   1898      5    161    274       N  
ATOM    380  CA  ILE A  87     -22.698  15.204  71.242  1.00 12.89           C  
ANISOU  380  CA  ILE A  87     1349   1621   1928      0    150    282       C  
ATOM    381  C   ILE A  87     -23.278  15.861  72.494  1.00 16.65           C  
ANISOU  381  C   ILE A  87     1834   2096   2396     -5    124    284       C  
ATOM    382  O   ILE A  87     -24.060  16.808  72.383  1.00 17.49           O  
ANISOU  382  O   ILE A  87     1957   2203   2484     -9    121    284       O  
ATOM    383  CB  ILE A  87     -21.705  16.158  70.487  1.00 16.15           C  
ANISOU  383  CB  ILE A  87     1751   2034   2352    -10    165    287       C  
ATOM    384  CG1 ILE A  87     -21.220  15.520  69.148  1.00 16.83           C  
ANISOU  384  CG1 ILE A  87     1831   2123   2441     -5    196    283       C  
ATOM    385  CG2 ILE A  87     -20.510  16.540  71.396  1.00 16.98           C  
ANISOU  385  CG2 ILE A  87     1832   2134   2485    -17    151    295       C  
ATOM    386  CD1 ILE A  87     -20.393  16.484  68.231  1.00 20.64           C  
ANISOU  386  CD1 ILE A  87     2308   2606   2930    -16    217    290       C  
ATOM    387  N   GLN A  88     -22.990  15.294  73.675  1.00 11.79           N  
ANISOU  387  N   GLN A  88     1211   1479   1792     -3    105    286       N  
ATOM    388  CA  GLN A  88     -23.603  15.761  74.918  1.00 11.54           C  
ANISOU  388  CA  GLN A  88     1190   1445   1748     -6     82    287       C  
ATOM    389  C   GLN A  88     -23.009  17.062  75.413  1.00 16.79           C  
ANISOU  389  C   GLN A  88     1852   2107   2419    -18     70    291       C  
ATOM    390  O   GLN A  88     -21.789  17.246  75.371  1.00 16.65           O  
ANISOU  390  O   GLN A  88     1815   2088   2425    -24     70    296       O  
ATOM    391  CB  GLN A  88     -23.516  14.685  76.016  1.00 12.66           C  
ANISOU  391  CB  GLN A  88     1328   1587   1897     -1     65    289       C  
ATOM    392  CG  GLN A  88     -24.316  13.418  75.705  1.00 18.19           C  
ANISOU  392  CG  GLN A  88     2036   2288   2589      9     74    284       C  
ATOM    393  CD  GLN A  88     -25.806  13.679  75.648  1.00 31.92           C  
ANISOU  393  CD  GLN A  88     3797   4031   4301      9     76    278       C  
ATOM    394  OE1 GLN A  88     -26.492  13.717  76.671  1.00 25.06           O  
ANISOU  394  OE1 GLN A  88     2939   3163   3420      8     62    279       O  
ATOM    395  NE2 GLN A  88     -26.350  13.772  74.438  1.00 25.87           N  
ANISOU  395  NE2 GLN A  88     3037   3269   3525     11     93    273       N  
ATOM    396  N   ASP A  89     -23.866  17.956  75.931  1.00 13.16           N  
ANISOU  396  N   ASP A  89     1413   1647   1942    -22     61    288       N  
ATOM    397  CA  ASP A  89     -23.421  19.139  76.643  1.00 12.80           C  
ANISOU  397  CA  ASP A  89     1369   1595   1899    -34     46    289       C  
ATOM    398  C   ASP A  89     -23.546  18.864  78.138  1.00 16.15           C  
ANISOU  398  C   ASP A  89     1798   2019   2318    -36     22    288       C  
ATOM    399  O   ASP A  89     -24.661  18.851  78.673  1.00 15.25           O  
ANISOU  399  O   ASP A  89     1704   1907   2184    -32     19    283       O  
ATOM    400  CB  ASP A  89     -24.258  20.379  76.236  1.00 14.07           C  
ANISOU  400  CB  ASP A  89     1550   1751   2044    -37     53    286       C  
ATOM    401  CG  ASP A  89     -23.786  21.688  76.885  1.00 20.40           C  
ANISOU  401  CG  ASP A  89     2357   2544   2851    -51     40    286       C  
ATOM    402  OD1 ASP A  89     -23.569  21.696  78.122  1.00 17.81           O  
ANISOU  402  OD1 ASP A  89     2031   2215   2523    -56     20    283       O  
ATOM    403  OD2 ASP A  89     -23.743  22.717  76.180  1.00 25.71           O  
ANISOU  403  OD2 ASP A  89     3035   3210   3525    -56     50    288       O  
ATOM    404  N   ASP A  90     -22.419  18.516  78.790  1.00 12.57           N  
ANISOU  404  N   ASP A  90     1327   1565   1883    -41      7    293       N  
ATOM    405  CA  ASP A  90     -22.413  18.120  80.203  1.00 12.25           C  
ANISOU  405  CA  ASP A  90     1292   1526   1836    -43    -18    294       C  
ATOM    406  C   ASP A  90     -22.997  19.205  81.119  1.00 16.06           C  
ANISOU  406  C   ASP A  90     1798   2006   2299    -52    -31    287       C  
ATOM    407  O   ASP A  90     -23.636  18.882  82.125  1.00 15.30           O  
ANISOU  407  O   ASP A  90     1717   1911   2184    -51    -43    284       O  
ATOM    408  CB  ASP A  90     -21.000  17.748  80.654  1.00 13.81           C  
ANISOU  408  CB  ASP A  90     1464   1724   2059    -48    -35    303       C  
ATOM    409  CG  ASP A  90     -20.968  17.112  82.021  1.00 19.12           C  
ANISOU  409  CG  ASP A  90     2142   2399   2725    -48    -61    307       C  
ATOM    410  OD1 ASP A  90     -21.571  16.031  82.184  1.00 20.11           O  
ANISOU  410  OD1 ASP A  90     2273   2526   2841    -37    -59    309       O  
ATOM    411  OD2 ASP A  90     -20.377  17.712  82.938  1.00 20.88           O  
ANISOU  411  OD2 ASP A  90     2364   2621   2948    -61    -85    308       O  
ATOM    412  N   GLU A  91     -22.769  20.492  80.780  1.00 12.80           N  
ANISOU  412  N   GLU A  91     1389   1586   1890    -63    -28    284       N  
ATOM    413  CA  GLU A  91     -23.293  21.614  81.567  1.00 12.48           C  
ANISOU  413  CA  GLU A  91     1371   1538   1831    -71    -37    275       C  
ATOM    414  C   GLU A  91     -24.832  21.624  81.540  1.00 16.02           C  
ANISOU  414  C   GLU A  91     1843   1988   2256    -59    -25    268       C  
ATOM    415  O   GLU A  91     -25.460  21.871  82.571  1.00 15.28           O  
ANISOU  415  O   GLU A  91     1768   1893   2143    -60    -34    261       O  
ATOM    416  CB  GLU A  91     -22.713  22.955  81.051  1.00 13.94           C  
ANISOU  416  CB  GLU A  91     1555   1713   2029    -84    -34    274       C  
ATOM    417  CG  GLU A  91     -23.020  24.151  81.942  1.00 19.00           C  
ANISOU  417  CG  GLU A  91     2220   2344   2657    -95    -46    264       C  
ATOM    418  CD  GLU A  91     -24.292  24.894  81.588  1.00 20.84           C  
ANISOU  418  CD  GLU A  91     2476   2569   2873    -86    -30    257       C  
ATOM    419  OE1 GLU A  91     -24.702  24.840  80.407  1.00  9.97           O  
ANISOU  419  OE1 GLU A  91     1095   1194   1499    -76    -10    261       O  
ATOM    420  OE2 GLU A  91     -24.816  25.616  82.464  1.00 15.53           O  
ANISOU  420  OE2 GLU A  91     1827   1890   2186    -89    -37    246       O  
ATOM    421  N   TRP A  92     -25.440  21.249  80.375  1.00 12.55           N  
ANISOU  421  N   TRP A  92     1399   1552   1816    -47     -3    270       N  
ATOM    422  CA  TRP A  92     -26.904  21.133  80.251  1.00 11.40           C  
ANISOU  422  CA  TRP A  92     1270   1410   1651    -35      8    265       C  
ATOM    423  C   TRP A  92     -27.420  19.954  81.075  1.00 16.04           C  
ANISOU  423  C   TRP A  92     1861   2006   2228    -30      2    264       C  
ATOM    424  O   TRP A  92     -28.338  20.119  81.881  1.00 15.68           O  
ANISOU  424  O   TRP A  92     1832   1962   2164    -28      0    258       O  
ATOM    425  CB  TRP A  92     -27.309  20.943  78.784  1.00  9.61           C  
ANISOU  425  CB  TRP A  92     1038   1186   1427    -27     28    268       C  
ATOM    426  CG  TRP A  92     -27.144  22.155  77.919  1.00 10.38           C  
ANISOU  426  CG  TRP A  92     1139   1276   1530    -31     37    270       C  
ATOM    427  CD1 TRP A  92     -26.655  23.376  78.288  1.00 13.42           C  
ANISOU  427  CD1 TRP A  92     1530   1649   1920    -41     30    268       C  
ATOM    428  CD2 TRP A  92     -27.469  22.255  76.528  1.00 10.17           C  
ANISOU  428  CD2 TRP A  92     1110   1250   1502    -25     54    274       C  
ATOM    429  NE1 TRP A  92     -26.670  24.238  77.213  1.00 12.87           N  
ANISOU  429  NE1 TRP A  92     1463   1572   1853    -42     42    273       N  
ATOM    430  CE2 TRP A  92     -27.158  23.572  76.116  1.00 14.15           C  
ANISOU  430  CE2 TRP A  92     1622   1744   2012    -32     57    277       C  
ATOM    431  CE3 TRP A  92     -27.992  21.354  75.580  1.00 11.15           C  
ANISOU  431  CE3 TRP A  92     1231   1384   1621    -15     66    276       C  
ATOM    432  CZ2 TRP A  92     -27.368  24.015  74.805  1.00 13.03           C  
ANISOU  432  CZ2 TRP A  92     1482   1600   1868    -29     72    283       C  
ATOM    433  CZ3 TRP A  92     -28.188  21.792  74.280  1.00 12.41           C  
ANISOU  433  CZ3 TRP A  92     1394   1544   1777    -13     80    280       C  
ATOM    434  CH2 TRP A  92     -27.867  23.102  73.900  1.00 13.07           C  
ANISOU  434  CH2 TRP A  92     1484   1617   1865    -20     83    285       C  
ATOM    435  N   ASN A  93     -26.841  18.737  80.846  1.00 12.39           N  
ANISOU  435  N   ASN A  93     1383   1549   1777    -27      1    271       N  
ATOM    436  CA  ASN A  93     -27.270  17.505  81.521  1.00 11.85           C  
ANISOU  436  CA  ASN A  93     1316   1486   1700    -22     -4    273       C  
ATOM    437  C   ASN A  93     -27.226  17.635  83.035  1.00 18.12           C  
ANISOU  437  C   ASN A  93     2123   2280   2482    -29    -23    272       C  
ATOM    438  O   ASN A  93     -28.097  17.098  83.718  1.00 19.01           O  
ANISOU  438  O   ASN A  93     2248   2397   2577    -25    -23    271       O  
ATOM    439  CB  ASN A  93     -26.424  16.310  81.061  1.00 10.74           C  
ANISOU  439  CB  ASN A  93     1156   1347   1579    -17     -3    282       C  
ATOM    440  CG  ASN A  93     -26.615  15.948  79.605  1.00 22.18           C  
ANISOU  440  CG  ASN A  93     2596   2796   3035    -10     18    281       C  
ATOM    441  OD1 ASN A  93     -27.297  16.646  78.845  1.00 14.18           O  
ANISOU  441  OD1 ASN A  93     1590   1784   2014     -9     31    276       O  
ATOM    442  ND2 ASN A  93     -26.015  14.839  79.187  1.00 12.72           N  
ANISOU  442  ND2 ASN A  93     1383   1598   1852     -5     22    285       N  
ATOM    443  N   ASN A  94     -26.209  18.349  83.573  1.00 14.81           N  
ANISOU  443  N   ASN A  94     1701   1856   2069    -40    -40    273       N  
ATOM    444  CA  ASN A  94     -26.105  18.576  85.016  1.00 14.76           C  
ANISOU  444  CA  ASN A  94     1710   1850   2047    -49    -61    271       C  
ATOM    445  C   ASN A  94     -27.271  19.437  85.528  1.00 18.20           C  
ANISOU  445  C   ASN A  94     2172   2284   2459    -49    -53    259       C  
ATOM    446  O   ASN A  94     -27.856  19.119  86.562  1.00 18.66           O  
ANISOU  446  O   ASN A  94     2246   2346   2496    -50    -58    256       O  
ATOM    447  CB  ASN A  94     -24.765  19.220  85.374  1.00 15.65           C  
ANISOU  447  CB  ASN A  94     1813   1959   2175    -62    -82    273       C  
ATOM    448  CG  ASN A  94     -24.584  19.436  86.860  1.00 34.59           C  
ANISOU  448  CG  ASN A  94     4229   4358   4555    -74   -107    271       C  
ATOM    449  OD1 ASN A  94     -24.740  18.519  87.668  1.00 20.45           O  
ANISOU  449  OD1 ASN A  94     2445   2574   2752    -71   -117    277       O  
ATOM    450  ND2 ASN A  94     -24.278  20.661  87.250  1.00 30.76           N  
ANISOU  450  ND2 ASN A  94     3754   3866   4066    -87   -116    262       N  
ATOM    451  N   LEU A  95     -27.623  20.523  84.786  1.00 13.49           N  
ANISOU  451  N   LEU A  95     1579   1681   1866    -48    -40    251       N  
ATOM    452  CA  LEU A  95     -28.753  21.389  85.160  1.00 12.85           C  
ANISOU  452  CA  LEU A  95     1520   1596   1765    -44    -30    239       C  
ATOM    453  C   LEU A  95     -30.056  20.596  85.167  1.00 14.67           C  
ANISOU  453  C   LEU A  95     1755   1835   1982    -32    -15    239       C  
ATOM    454  O   LEU A  95     -30.848  20.716  86.102  1.00 12.89           O  
ANISOU  454  O   LEU A  95     1548   1613   1738    -32    -13    231       O  
ATOM    455  CB  LEU A  95     -28.872  22.590  84.189  1.00 12.89           C  
ANISOU  455  CB  LEU A  95     1525   1591   1781    -43    -18    235       C  
ATOM    456  CG  LEU A  95     -27.737  23.624  84.240  1.00 17.95           C  
ANISOU  456  CG  LEU A  95     2165   2221   2434    -57    -31    234       C  
ATOM    457  CD1 LEU A  95     -27.870  24.618  83.120  1.00 18.41           C  
ANISOU  457  CD1 LEU A  95     2222   2268   2503    -54    -16    234       C  
ATOM    458  CD2 LEU A  95     -27.706  24.349  85.590  1.00 20.39           C  
ANISOU  458  CD2 LEU A  95     2496   2523   2727    -68    -45    222       C  
ATOM    459  N   VAL A  96     -30.269  19.768  84.127  1.00 11.64           N  
ANISOU  459  N   VAL A  96     1355   1458   1610    -24     -4    246       N  
ATOM    460  CA  VAL A  96     -31.467  18.926  83.999  1.00 11.42           C  
ANISOU  460  CA  VAL A  96     1329   1438   1573    -14     10    246       C  
ATOM    461  C   VAL A  96     -31.535  17.908  85.154  1.00 17.27           C  
ANISOU  461  C   VAL A  96     2076   2185   2301    -18      1    249       C  
ATOM    462  O   VAL A  96     -32.558  17.811  85.835  1.00 16.82           O  
ANISOU  462  O   VAL A  96     2032   2132   2227    -16      9    245       O  
ATOM    463  CB  VAL A  96     -31.496  18.220  82.609  1.00 14.57           C  
ANISOU  463  CB  VAL A  96     1710   1840   1985     -7     20    252       C  
ATOM    464  CG1 VAL A  96     -32.639  17.218  82.524  1.00 14.02           C  
ANISOU  464  CG1 VAL A  96     1640   1778   1907     -1     31    252       C  
ATOM    465  CG2 VAL A  96     -31.583  19.243  81.479  1.00 14.39           C  
ANISOU  465  CG2 VAL A  96     1684   1813   1970     -4     29    250       C  
ATOM    466  N   TRP A  97     -30.421  17.183  85.390  1.00 15.30           N  
ANISOU  466  N   TRP A  97     1818   1935   2061    -23    -14    259       N  
ATOM    467  CA  TRP A  97     -30.299  16.196  86.466  1.00 15.41           C  
ANISOU  467  CA  TRP A  97     1838   1952   2064    -27    -26    266       C  
ATOM    468  C   TRP A  97     -30.624  16.820  87.828  1.00 19.34           C  
ANISOU  468  C   TRP A  97     2360   2451   2536    -35    -33    260       C  
ATOM    469  O   TRP A  97     -31.488  16.312  88.550  1.00 17.94           O  
ANISOU  469  O   TRP A  97     2196   2279   2341    -34    -27    259       O  
ATOM    470  CB  TRP A  97     -28.881  15.606  86.466  1.00 14.62           C  
ANISOU  470  CB  TRP A  97     1724   1850   1983    -30    -45    278       C  
ATOM    471  CG  TRP A  97     -28.581  14.676  87.607  1.00 16.21           C  
ANISOU  471  CG  TRP A  97     1932   2053   2175    -34    -62    288       C  
ATOM    472  CD1 TRP A  97     -28.106  15.024  88.839  1.00 19.33           C  
ANISOU  472  CD1 TRP A  97     2341   2449   2554    -44    -83    290       C  
ATOM    473  CD2 TRP A  97     -28.487  13.248  87.531  1.00 16.19           C  
ANISOU  473  CD2 TRP A  97     1921   2050   2180    -29    -63    301       C  
ATOM    474  NE1 TRP A  97     -27.779  13.896  89.556  1.00 18.99           N  
ANISOU  474  NE1 TRP A  97     2300   2408   2509    -45    -98    304       N  
ATOM    475  CE2 TRP A  97     -28.005  12.792  88.778  1.00 20.25           C  
ANISOU  475  CE2 TRP A  97     2446   2565   2684    -35    -85    311       C  
ATOM    476  CE3 TRP A  97     -28.776  12.303  86.531  1.00 17.36           C  
ANISOU  476  CE3 TRP A  97     2055   2195   2343    -19    -47    304       C  
ATOM    477  CZ2 TRP A  97     -27.842  11.432  89.065  1.00 19.81           C  
ANISOU  477  CZ2 TRP A  97     2387   2507   2633    -31    -91    327       C  
ATOM    478  CZ3 TRP A  97     -28.621  10.957  86.819  1.00 18.90           C  
ANISOU  478  CZ3 TRP A  97     2249   2388   2545    -16    -52    316       C  
ATOM    479  CH2 TRP A  97     -28.151  10.533  88.069  1.00 19.68           C  
ANISOU  479  CH2 TRP A  97     2358   2487   2634    -21    -74    329       C  
ATOM    480  N   GLU A  98     -29.963  17.953  88.158  1.00 16.36           N  
ANISOU  480  N   GLU A  98     1989   2068   2159    -43    -45    253       N  
ATOM    481  CA  GLU A  98     -30.155  18.633  89.445  1.00 16.24           C  
ANISOU  481  CA  GLU A  98     2000   2053   2119    -52    -54    244       C  
ATOM    482  C   GLU A  98     -31.575  19.160  89.625  1.00 18.58           C  
ANISOU  482  C   GLU A  98     2312   2350   2397    -45    -30    231       C  
ATOM    483  O   GLU A  98     -32.103  19.108  90.729  1.00 17.32           O  
ANISOU  483  O   GLU A  98     2173   2194   2213    -49    -29    226       O  
ATOM    484  CB  GLU A  98     -29.129  19.769  89.624  1.00 17.94           C  
ANISOU  484  CB  GLU A  98     2218   2260   2340    -63    -71    238       C  
ATOM    485  CG  GLU A  98     -27.708  19.273  89.863  1.00 29.07           C  
ANISOU  485  CG  GLU A  98     3613   3670   3763    -72    -99    250       C  
ATOM    486  CD  GLU A  98     -27.501  18.565  91.189  1.00 53.43           C  
ANISOU  486  CD  GLU A  98     6712   6762   6827    -79   -119    257       C  
ATOM    487  OE1 GLU A  98     -27.754  19.190  92.243  1.00 43.87           O  
ANISOU  487  OE1 GLU A  98     5529   5552   5590    -89   -126    246       O  
ATOM    488  OE2 GLU A  98     -27.012  17.412  91.174  1.00 53.75           O  
ANISOU  488  OE2 GLU A  98     6738   6806   6877    -76   -129    273       O  
ATOM    489  N   GLU A  99     -32.205  19.660  88.535  1.00 15.53           N  
ANISOU  489  N   GLU A  99     1916   1961   2024    -35    -12    226       N  
ATOM    490  CA  GLU A  99     -33.560  20.235  88.621  1.00 15.57           C  
ANISOU  490  CA  GLU A  99     1932   1967   2018    -26     10    214       C  
ATOM    491  C   GLU A  99     -34.631  19.172  88.924  1.00 19.45           C  
ANISOU  491  C   GLU A  99     2424   2469   2498    -21     24    218       C  
ATOM    492  O   GLU A  99     -35.478  19.397  89.788  1.00 20.88           O  
ANISOU  492  O   GLU A  99     2621   2654   2659    -21     36    209       O  
ATOM    493  CB  GLU A  99     -33.912  21.029  87.347  1.00 16.73           C  
ANISOU  493  CB  GLU A  99     2066   2106   2182    -16     22    211       C  
ATOM    494  CG  GLU A  99     -35.185  21.866  87.481  1.00 25.42           C  
ANISOU  494  CG  GLU A  99     3179   3206   3276     -5     42    198       C  
ATOM    495  CD  GLU A  99     -35.146  22.951  88.553  1.00 42.55           C  
ANISOU  495  CD  GLU A  99     5372   5365   5429    -10     40    183       C  
ATOM    496  OE1 GLU A  99     -34.077  23.583  88.726  1.00 25.58           O  
ANISOU  496  OE1 GLU A  99     3230   3206   3283    -21     24    181       O  
ATOM    497  OE2 GLU A  99     -36.212  23.229  89.149  1.00 34.66           O  
ANISOU  497  OE2 GLU A  99     4385   4367   4416     -4     57    173       O  
ATOM    498  N   TYR A 100     -34.578  17.997  88.235  1.00 13.38           N  
ANISOU  498  N   TYR A 100     1637   1706   1742    -18     24    230       N  
ATOM    499  CA  TYR A 100     -35.531  16.902  88.503  1.00 11.92           C  
ANISOU  499  CA  TYR A 100     1451   1530   1547    -17     37    235       C  
ATOM    500  C   TYR A 100     -35.411  16.397  89.937  1.00 14.01           C  
ANISOU  500  C   TYR A 100     1736   1798   1789    -26     29    239       C  
ATOM    501  O   TYR A 100     -36.417  16.244  90.617  1.00 13.19           O  
ANISOU  501  O   TYR A 100     1643   1701   1668    -27     45    235       O  
ATOM    502  CB  TYR A 100     -35.339  15.732  87.512  1.00 12.34           C  
ANISOU  502  CB  TYR A 100     1485   1585   1620    -14     36    246       C  
ATOM    503  CG  TYR A 100     -35.872  16.005  86.120  1.00 12.64           C  
ANISOU  503  CG  TYR A 100     1506   1624   1674     -4     48    243       C  
ATOM    504  CD1 TYR A 100     -37.219  16.297  85.913  1.00 14.37           C  
ANISOU  504  CD1 TYR A 100     1724   1848   1888      2     66    236       C  
ATOM    505  CD2 TYR A 100     -35.074  15.803  84.997  1.00 12.68           C  
ANISOU  505  CD2 TYR A 100     1496   1625   1698     -2     42    248       C  
ATOM    506  CE1 TYR A 100     -37.729  16.488  84.629  1.00 14.76           C  
ANISOU  506  CE1 TYR A 100     1757   1899   1950     11     74    235       C  
ATOM    507  CE2 TYR A 100     -35.582  15.962  83.708  1.00 13.08           C  
ANISOU  507  CE2 TYR A 100     1534   1677   1758      5     53    246       C  
ATOM    508  CZ  TYR A 100     -36.903  16.329  83.530  1.00 18.72           C  
ANISOU  508  CZ  TYR A 100     2248   2397   2467     11     66    240       C  
ATOM    509  OH  TYR A 100     -37.394  16.515  82.263  1.00 17.52           O  
ANISOU  509  OH  TYR A 100     2085   2248   2325     18     73    239       O  
ATOM    510  N   LEU A 101     -34.179  16.136  90.397  1.00 11.44           N  
ANISOU  510  N   LEU A 101     1413   1469   1463    -35      6    247       N  
ATOM    511  CA  LEU A 101     -33.955  15.641  91.764  1.00 11.71           C  
ANISOU  511  CA  LEU A 101     1468   1507   1474    -45     -6    253       C  
ATOM    512  C   LEU A 101     -34.327  16.692  92.820  1.00 15.32           C  
ANISOU  512  C   LEU A 101     1951   1965   1904    -50     -2    238       C  
ATOM    513  O   LEU A 101     -34.878  16.343  93.869  1.00 14.72           O  
ANISOU  513  O   LEU A 101     1896   1895   1802    -56      4    239       O  
ATOM    514  CB  LEU A 101     -32.497  15.170  91.947  1.00 11.92           C  
ANISOU  514  CB  LEU A 101     1489   1530   1509    -51    -36    267       C  
ATOM    515  CG  LEU A 101     -32.122  13.881  91.197  1.00 16.58           C  
ANISOU  515  CG  LEU A 101     2059   2119   2123    -46    -39    282       C  
ATOM    516  CD1 LEU A 101     -30.662  13.577  91.344  1.00 17.15           C  
ANISOU  516  CD1 LEU A 101     2122   2186   2208    -49    -68    294       C  
ATOM    517  CD2 LEU A 101     -32.962  12.694  91.683  1.00 19.43           C  
ANISOU  517  CD2 LEU A 101     2428   2484   2471    -46    -28    292       C  
ATOM    518  N   LYS A 102     -34.095  17.992  92.505  1.00 11.59           N  
ANISOU  518  N   LYS A 102     1481   1486   1438    -49     -3    224       N  
ATOM    519  CA  LYS A 102     -34.509  19.105  93.368  1.00 11.52           C  
ANISOU  519  CA  LYS A 102     1497   1474   1407    -52      4    206       C  
ATOM    520  C   LYS A 102     -36.039  19.107  93.534  1.00 15.44           C  
ANISOU  520  C   LYS A 102     1999   1976   1892    -43     36    198       C  
ATOM    521  O   LYS A 102     -36.543  19.243  94.656  1.00 14.60           O  
ANISOU  521  O   LYS A 102     1917   1874   1757    -48     45    190       O  
ATOM    522  CB  LYS A 102     -34.025  20.450  92.773  1.00 14.34           C  
ANISOU  522  CB  LYS A 102     1851   1819   1780    -51      0    194       C  
ATOM    523  CG  LYS A 102     -34.615  21.687  93.449  1.00 32.02           C  
ANISOU  523  CG  LYS A 102     4115   4050   4000    -50     13    173       C  
ATOM    524  CD  LYS A 102     -34.131  22.976  92.774  1.00 40.79           C  
ANISOU  524  CD  LYS A 102     5223   5146   5130    -49      8    163       C  
ATOM    525  CE  LYS A 102     -34.816  24.206  93.321  1.00 51.34           C  
ANISOU  525  CE  LYS A 102     6582   6472   6453    -46     24    141       C  
ATOM    526  NZ  LYS A 102     -36.264  24.233  92.976  1.00 62.30           N  
ANISOU  526  NZ  LYS A 102     7965   7864   7844    -27     56    136       N  
ATOM    527  N   GLN A 103     -36.771  18.880  92.422  1.00 12.57           N  
ANISOU  527  N   GLN A 103     1612   1614   1550    -31     53    201       N  
ATOM    528  CA  GLN A 103     -38.233  18.854  92.432  1.00 12.35           C  
ANISOU  528  CA  GLN A 103     1582   1593   1517    -21     82    194       C  
ATOM    529  C   GLN A 103     -38.774  17.611  93.149  1.00 16.31           C  
ANISOU  529  C   GLN A 103     2088   2106   2002    -28     91    204       C  
ATOM    530  O   GLN A 103     -39.705  17.724  93.945  1.00 16.30           O  
ANISOU  530  O   GLN A 103     2101   2111   1982    -28    112    196       O  
ATOM    531  CB  GLN A 103     -38.789  18.947  90.999  1.00 13.16           C  
ANISOU  531  CB  GLN A 103     1658   1696   1649     -8     93    195       C  
ATOM    532  CG  GLN A 103     -38.422  20.264  90.276  1.00 16.63           C  
ANISOU  532  CG  GLN A 103     2093   2122   2102     -1     88    186       C  
ATOM    533  CD  GLN A 103     -39.072  21.490  90.906  1.00 26.64           C  
ANISOU  533  CD  GLN A 103     3379   3383   3359      5    104    168       C  
ATOM    534  OE1 GLN A 103     -40.090  21.400  91.605  1.00 18.04           O  
ANISOU  534  OE1 GLN A 103     2298   2302   2257      9    124    161       O  
ATOM    535  NE2 GLN A 103     -38.564  22.673  90.562  1.00 14.34           N  
ANISOU  535  NE2 GLN A 103     1826   1811   1811      8     97    160       N  
ATOM    536  N   ILE A 104     -38.159  16.423  92.897  1.00 12.35           N  
ANISOU  536  N   ILE A 104     1577   1607   1509    -34     75    222       N  
ATOM    537  CA  ILE A 104     -38.539  15.177  93.595  1.00 12.10           C  
ANISOU  537  CA  ILE A 104     1553   1583   1463    -41     80    235       C  
ATOM    538  C   ILE A 104     -38.363  15.336  95.119  1.00 17.12           C  
ANISOU  538  C   ILE A 104     2221   2222   2063    -53     76    233       C  
ATOM    539  O   ILE A 104     -39.273  15.006  95.883  1.00 16.16           O  
ANISOU  539  O   ILE A 104     2112   2108   1921    -57     97    232       O  
ATOM    540  CB  ILE A 104     -37.728  13.948  93.042  1.00 14.77           C  
ANISOU  540  CB  ILE A 104     1876   1917   1818    -44     61    254       C  
ATOM    541  CG1 ILE A 104     -38.052  13.681  91.533  1.00 14.42           C  
ANISOU  541  CG1 ILE A 104     1802   1872   1805    -34     69    254       C  
ATOM    542  CG2 ILE A 104     -37.966  12.681  93.911  1.00 15.52           C  
ANISOU  542  CG2 ILE A 104     1983   2017   1897    -54     63    269       C  
ATOM    543  CD1 ILE A 104     -39.532  13.302  91.240  1.00 22.74           C  
ANISOU  543  CD1 ILE A 104     2846   2933   2860    -31     96    251       C  
ATOM    544  N   ALA A 105     -37.195  15.874  95.552  1.00 15.53           N  
ANISOU  544  N   ALA A 105     2033   2015   1854    -59     50    231       N  
ATOM    545  CA  ALA A 105     -36.907  16.103  96.973  1.00 16.58           C  
ANISOU  545  CA  ALA A 105     2200   2150   1951    -72     42    228       C  
ATOM    546  C   ALA A 105     -37.945  17.034  97.593  1.00 22.21           C  
ANISOU  546  C   ALA A 105     2931   2865   2642    -69     70    207       C  
ATOM    547  O   ALA A 105     -38.392  16.794  98.712  1.00 21.71           O  
ANISOU  547  O   ALA A 105     2893   2809   2546    -78     80    206       O  
ATOM    548  CB  ALA A 105     -35.511  16.694  97.136  1.00 17.37           C  
ANISOU  548  CB  ALA A 105     2305   2243   2051    -79      8    227       C  
ATOM    549  N   SER A 106     -38.369  18.074  96.835  1.00 19.69           N  
ANISOU  549  N   SER A 106     2600   2540   2342    -57     84    190       N  
ATOM    550  CA  SER A 106     -39.381  19.029  97.285  1.00 20.14           C  
ANISOU  550  CA  SER A 106     2671   2597   2385    -51    113    169       C  
ATOM    551  C   SER A 106     -40.739  18.335  97.512  1.00 24.81           C  
ANISOU  551  C   SER A 106     3257   3200   2969    -47    146    172       C  
ATOM    552  O   SER A 106     -41.396  18.582  98.534  1.00 25.06           O  
ANISOU  552  O   SER A 106     3311   3237   2973    -50    168    161       O  
ATOM    553  CB  SER A 106     -39.526  20.161  96.275  1.00 23.54           C  
ANISOU  553  CB  SER A 106     3085   3016   2843    -36    119    156       C  
ATOM    554  OG  SER A 106     -40.471  21.122  96.707  1.00 33.27           O  
ANISOU  554  OG  SER A 106     4330   4246   4065    -28    147    135       O  
ATOM    555  N   ILE A 107     -41.133  17.421  96.588  1.00 20.73           N  
ANISOU  555  N   ILE A 107     2710   2688   2477    -42    150    186       N  
ATOM    556  CA  ILE A 107     -42.366  16.637  96.752  1.00 20.45           C  
ANISOU  556  CA  ILE A 107     2666   2663   2439    -41    179    191       C  
ATOM    557  C   ILE A 107     -42.233  15.701  97.972  1.00 24.24           C  
ANISOU  557  C   ILE A 107     3172   3151   2887    -58    178    204       C  
ATOM    558  O   ILE A 107     -43.178  15.567  98.747  1.00 23.91           O  
ANISOU  558  O   ILE A 107     3141   3118   2824    -62    206    200       O  
ATOM    559  CB  ILE A 107     -42.730  15.845  95.443  1.00 23.08           C  
ANISOU  559  CB  ILE A 107     2963   2999   2807    -35    179    204       C  
ATOM    560  CG1 ILE A 107     -42.743  16.777  94.210  1.00 22.89           C  
ANISOU  560  CG1 ILE A 107     2917   2968   2812    -19    176    194       C  
ATOM    561  CG2 ILE A 107     -44.077  15.116  95.602  1.00 24.01           C  
ANISOU  561  CG2 ILE A 107     3070   3128   2924    -36    210    207       C  
ATOM    562  CD1 ILE A 107     -42.921  16.057  92.856  1.00 24.89           C  
ANISOU  562  CD1 ILE A 107     3138   3222   3095    -14    172    205       C  
ATOM    563  N   ASN A 108     -41.010  15.131  98.187  1.00 20.89           N  
ANISOU  563  N   ASN A 108     2758   2723   2456    -68    145    219       N  
ATOM    564  CA  ASN A 108     -40.732  14.242  99.335  1.00 21.57           C  
ANISOU  564  CA  ASN A 108     2870   2814   2510    -84    137    234       C  
ATOM    565  C   ASN A 108     -40.874  14.974 100.681  1.00 27.74           C  
ANISOU  565  C   ASN A 108     3690   3600   3250    -92    147    220       C  
ATOM    566  O   ASN A 108     -41.284  14.361 101.667  1.00 28.10           O  
ANISOU  566  O   ASN A 108     3757   3654   3265   -103    159    228       O  
ATOM    567  CB  ASN A 108     -39.330  13.608  99.215  1.00 20.58           C  
ANISOU  567  CB  ASN A 108     2744   2682   2392    -90     96    253       C  
ATOM    568  CG  ASN A 108     -39.228  12.520  98.166  1.00 32.70           C  
ANISOU  568  CG  ASN A 108     4250   4213   3961    -85     90    271       C  
ATOM    569  OD1 ASN A 108     -40.205  12.148  97.522  1.00 22.37           O  
ANISOU  569  OD1 ASN A 108     2922   2909   2670    -80    114    270       O  
ATOM    570  ND2 ASN A 108     -38.042  11.963  98.007  1.00 23.30           N  
ANISOU  570  ND2 ASN A 108     3056   3016   2780    -88     58    286       N  
ATOM    571  N   ILE A 109     -40.504  16.288 100.730  1.00 25.05           N  
ANISOU  571  N   ILE A 109     3359   3252   2906    -88    141    199       N  
ATOM    572  CA  ILE A 109     -40.638  17.090 101.964  1.00 25.50           C  
ANISOU  572  CA  ILE A 109     3454   3312   2923    -95    151    181       C  
ATOM    573  C   ILE A 109     -42.115  17.196 102.356  1.00 28.96           C  
ANISOU  573  C   ILE A 109     3896   3759   3350    -90    198    169       C  
ATOM    574  O   ILE A 109     -42.460  17.003 103.523  1.00 28.74           O  
ANISOU  574  O   ILE A 109     3899   3738   3282   -101    214    168       O  
ATOM    575  CB  ILE A 109     -39.984  18.513 101.804  1.00 28.83           C  
ANISOU  575  CB  ILE A 109     3884   3722   3350    -91    136    159       C  
ATOM    576  CG1 ILE A 109     -38.550  18.435 101.199  1.00 29.12           C  
ANISOU  576  CG1 ILE A 109     3907   3749   3407    -95     91    171       C  
ATOM    577  CG2 ILE A 109     -40.000  19.290 103.138  1.00 30.20           C  
ANISOU  577  CG2 ILE A 109     4102   3896   3478   -102    142    139       C  
ATOM    578  CD1 ILE A 109     -37.510  17.684 102.055  1.00 38.69           C  
ANISOU  578  CD1 ILE A 109     5140   4966   4594   -112     56    189       C  
ATOM    579  N   VAL A 110     -42.998  17.457 101.357  1.00 24.86           N  
ANISOU  579  N   VAL A 110     3343   3238   2865    -73    222    162       N  
ATOM    580  CA  VAL A 110     -44.444  17.568 101.576  1.00 24.04           C  
ANISOU  580  CA  VAL A 110     3233   3142   2758    -66    267    152       C  
ATOM    581  C   VAL A 110     -45.042  16.210 102.016  1.00 26.76           C  
ANISOU  581  C   VAL A 110     3577   3500   3091    -78    283    172       C  
ATOM    582  O   VAL A 110     -45.753  16.151 103.016  1.00 25.54           O  
ANISOU  582  O   VAL A 110     3444   3355   2907    -84    313    167       O  
ATOM    583  CB  VAL A 110     -45.171  18.142 100.313  1.00 27.49           C  
ANISOU  583  CB  VAL A 110     3631   3576   3240    -45    282    143       C  
ATOM    584  CG1 VAL A 110     -46.679  18.250 100.547  1.00 27.58           C  
ANISOU  584  CG1 VAL A 110     3631   3596   3251    -36    328    132       C  
ATOM    585  CG2 VAL A 110     -44.591  19.492  99.916  1.00 27.11           C  
ANISOU  585  CG2 VAL A 110     3586   3512   3202    -34    268    124       C  
ATOM    586  N   ILE A 111     -44.713  15.115 101.283  1.00 23.45           N  
ANISOU  586  N   ILE A 111     3135   3081   2695    -81    263    196       N  
ATOM    587  CA  ILE A 111     -45.238  13.773 101.603  1.00 23.19           C  
ANISOU  587  CA  ILE A 111     3100   3056   2654    -93    276    217       C  
ATOM    588  C   ILE A 111     -44.837  13.331 103.021  1.00 29.02           C  
ANISOU  588  C   ILE A 111     3881   3799   3345   -112    271    227       C  
ATOM    589  O   ILE A 111     -45.682  12.847 103.771  1.00 28.99           O  
ANISOU  589  O   ILE A 111     3890   3806   3319   -121    302    231       O  
ATOM    590  CB  ILE A 111     -44.822  12.718 100.527  1.00 25.14           C  
ANISOU  590  CB  ILE A 111     3318   3298   2936    -94    252    238       C  
ATOM    591  CG1 ILE A 111     -45.244  13.168  99.117  1.00 24.78           C  
ANISOU  591  CG1 ILE A 111     3233   3250   2933    -77    256    228       C  
ATOM    592  CG2 ILE A 111     -45.404  11.330 100.865  1.00 25.30           C  
ANISOU  592  CG2 ILE A 111     3337   3324   2950   -107    267    259       C  
ATOM    593  CD1 ILE A 111     -44.736  12.248  97.966  1.00 31.67           C  
ANISOU  593  CD1 ILE A 111     4080   4116   3838    -76    232    245       C  
ATOM    594  N   ARG A 112     -43.552  13.518 103.392  1.00 26.05           N  
ANISOU  594  N   ARG A 112     3529   3417   2952   -118    233    231       N  
ATOM    595  CA  ARG A 112     -43.045  13.090 104.704  1.00 26.46           C  
ANISOU  595  CA  ARG A 112     3623   3474   2958   -136    221    242       C  
ATOM    596  C   ARG A 112     -43.689  13.880 105.863  1.00 30.90           C  
ANISOU  596  C   ARG A 112     4220   4044   3477   -141    253    222       C  
ATOM    597  O   ARG A 112     -44.046  13.289 106.885  1.00 31.21           O  
ANISOU  597  O   ARG A 112     4287   4093   3480   -155    268    232       O  
ATOM    598  CB  ARG A 112     -41.509  13.201 104.756  1.00 26.76           C  
ANISOU  598  CB  ARG A 112     3672   3502   2991   -140    170    250       C  
ATOM    599  CG  ARG A 112     -40.897  12.702 106.068  1.00 37.67           C  
ANISOU  599  CG  ARG A 112     5097   4890   4327   -158    150    266       C  
ATOM    600  CD  ARG A 112     -39.382  12.560 105.980  1.00 49.73           C  
ANISOU  600  CD  ARG A 112     6625   6409   5859   -162     97    280       C  
ATOM    601  NE  ARG A 112     -38.717  13.837 105.706  1.00 57.71           N  
ANISOU  601  NE  ARG A 112     7635   7414   6879   -156     79    256       N  
ATOM    602  CZ  ARG A 112     -38.253  14.190 104.509  1.00 70.65           C  
ANISOU  602  CZ  ARG A 112     9239   9043   8562   -144     65    252       C  
ATOM    603  NH1 ARG A 112     -38.358  13.359 103.478  1.00 56.49           N  
ANISOU  603  NH1 ARG A 112     7411   7247   6807   -135     66    267       N  
ATOM    604  NH2 ARG A 112     -37.650  15.357 104.344  1.00 56.70           N  
ANISOU  604  NH2 ARG A 112     7474   7270   6800   -141     50    231       N  
ATOM    605  N   SER A 113     -43.837  15.209 105.699  1.00 27.12           N  
ANISOU  605  N   SER A 113     3741   3561   3004   -129    263    192       N  
ATOM    606  CA  SER A 113     -44.399  16.063 106.745  1.00 27.57           C  
ANISOU  606  CA  SER A 113     3831   3622   3021   -132    294    168       C  
ATOM    607  C   SER A 113     -45.903  15.834 106.925  1.00 32.00           C  
ANISOU  607  C   SER A 113     4381   4194   3582   -128    348    163       C  
ATOM    608  O   SER A 113     -46.374  15.760 108.058  1.00 31.48           O  
ANISOU  608  O   SER A 113     4349   4139   3474   -139    375    159       O  
ATOM    609  CB  SER A 113     -44.118  17.533 106.450  1.00 31.39           C  
ANISOU  609  CB  SER A 113     4316   4094   3515   -119    289    138       C  
ATOM    610  OG  SER A 113     -44.705  17.933 105.224  1.00 41.58           O  
ANISOU  610  OG  SER A 113     5564   5379   4854    -99    303    130       O  
ATOM    611  N   LEU A 114     -46.662  15.711 105.803  1.00 28.57           N  
ANISOU  611  N   LEU A 114     3900   3759   3195   -113    365    164       N  
ATOM    612  CA  LEU A 114     -48.117  15.495 105.872  1.00 29.09           C  
ANISOU  612  CA  LEU A 114     3949   3837   3269   -109    416    160       C  
ATOM    613  C   LEU A 114     -48.476  14.117 106.432  1.00 35.55           C  
ANISOU  613  C   LEU A 114     4774   4666   4068   -128    427    187       C  
ATOM    614  O   LEU A 114     -49.434  14.004 107.195  1.00 35.59           O  
ANISOU  614  O   LEU A 114     4790   4682   4051   -134    470    182       O  
ATOM    615  CB  LEU A 114     -48.778  15.704 104.501  1.00 28.55           C  
ANISOU  615  CB  LEU A 114     3828   3766   3256    -89    424    156       C  
ATOM    616  CG  LEU A 114     -48.893  17.150 104.031  1.00 32.44           C  
ANISOU  616  CG  LEU A 114     4312   4248   3767    -67    430    128       C  
ATOM    617  CD1 LEU A 114     -49.554  17.220 102.698  1.00 32.12           C  
ANISOU  617  CD1 LEU A 114     4220   4206   3778    -49    435    128       C  
ATOM    618  CD2 LEU A 114     -49.663  17.995 105.034  1.00 35.63           C  
ANISOU  618  CD2 LEU A 114     4740   4656   4143    -63    472    102       C  
ATOM    619  N   THR A 115     -47.713  13.056 106.042  1.00 33.68           N  
ANISOU  619  N   THR A 115     4531   4425   3842   -137    391    214       N  
ATOM    620  CA  THR A 115     -47.947  11.690 106.559  1.00 34.64           C  
ANISOU  620  CA  THR A 115     4662   4553   3948   -156    398    243       C  
ATOM    621  C   THR A 115     -47.729  11.633 108.070  1.00 41.11           C  
ANISOU  621  C   THR A 115     5534   5379   4706   -174    404    246       C  
ATOM    622  O   THR A 115     -48.467  10.940 108.773  1.00 41.55           O  
ANISOU  622  O   THR A 115     5602   5444   4739   -187    436    258       O  
ATOM    623  CB  THR A 115     -47.060  10.665 105.828  1.00 42.75           C  
ANISOU  623  CB  THR A 115     5675   5570   5000   -160    355    269       C  
ATOM    624  OG1 THR A 115     -45.709  11.123 105.841  1.00 44.34           O  
ANISOU  624  OG1 THR A 115     5892   5762   5193   -157    311    268       O  
ATOM    625  CG2 THR A 115     -47.516  10.413 104.394  1.00 40.40           C  
ANISOU  625  CG2 THR A 115     5325   5268   4757   -147    357    270       C  
ATOM    626  N   GLU A 116     -46.727  12.382 108.576  1.00 38.67           N  
ANISOU  626  N   GLU A 116     5258   5065   4369   -174    375    235       N  
ATOM    627  CA  GLU A 116     -46.436  12.438 110.006  1.00 39.45           C  
ANISOU  627  CA  GLU A 116     5411   5171   4407   -192    376    236       C  
ATOM    628  C   GLU A 116     -47.475  13.298 110.753  1.00 45.04           C  
ANISOU  628  C   GLU A 116     6137   5889   5087   -190    429    208       C  
ATOM    629  O   GLU A 116     -47.943  12.904 111.825  1.00 45.07           O  
ANISOU  629  O   GLU A 116     6174   5904   5047   -205    457    214       O  
ATOM    630  CB  GLU A 116     -45.013  12.979 110.247  1.00 40.92           C  
ANISOU  630  CB  GLU A 116     5623   5349   4575   -194    325    233       C  
ATOM    631  N   LYS A 117     -47.844  14.472 110.175  1.00 42.41           N  
ANISOU  631  N   LYS A 117     5784   5551   4781   -170    445    177       N  
ATOM    632  CA  LYS A 117     -48.819  15.385 110.793  1.00 43.19           C  
ANISOU  632  CA  LYS A 117     5896   5655   4859   -163    496    146       C  
ATOM    633  C   LYS A 117     -50.227  14.765 110.789  1.00 48.55           C  
ANISOU  633  C   LYS A 117     6549   6346   5550   -163    550    153       C  
ATOM    634  O   LYS A 117     -50.780  14.485 111.855  1.00 49.00           O  
ANISOU  634  O   LYS A 117     6637   6416   5566   -177    585    154       O  
ATOM    635  CB  LYS A 117     -48.816  16.759 110.066  1.00 45.54           C  
ANISOU  635  CB  LYS A 117     6175   5941   5188   -140    496    114       C  
ATOM    636  CG  LYS A 117     -49.566  17.874 110.817  1.00 58.79           C  
ANISOU  636  CG  LYS A 117     7876   7621   6842   -132    543     79       C  
ATOM    637  CD  LYS A 117     -51.036  17.963 110.402  1.00 68.62           C  
ANISOU  637  CD  LYS A 117     9080   8872   8121   -115    597     70       C  
ATOM    638  N   ASP A 118     -50.802  14.548 109.589  1.00 45.19           N  
ANISOU  638  N   ASP A 118     6069   5919   5182   -149    555    157       N  
ATOM    639  CA  ASP A 118     -52.127  13.938 109.455  1.00 45.39           C  
ANISOU  639  CA  ASP A 118     6063   5957   5227   -150    602    164       C  
ATOM    640  C   ASP A 118     -52.261  13.210 108.106  1.00 49.03           C  
ANISOU  640  C   ASP A 118     6471   6414   5745   -144    582    183       C  
ATOM    641  O   ASP A 118     -52.560  13.842 107.086  1.00 48.44           O  
ANISOU  641  O   ASP A 118     6357   6334   5713   -123    581    169       O  
ATOM    642  CB  ASP A 118     -53.235  14.997 109.619  1.00 47.46           C  
ANISOU  642  CB  ASP A 118     6314   6224   5496   -132    654    133       C  
ATOM    643  N   LYS A 119     -51.963  11.897 108.089  1.00 45.43           N  
ANISOU  643  N   LYS A 119     6017   5959   5287   -162    564    214       N  
ATOM    644  CA  LYS A 119     -52.038  11.096 106.866  1.00 44.61           C  
ANISOU  644  CA  LYS A 119     5868   5849   5233   -160    545    232       C  
ATOM    645  C   LYS A 119     -53.485  10.887 106.432  1.00 48.13           C  
ANISOU  645  C   LYS A 119     6270   6306   5711   -157    589    229       C  
ATOM    646  O   LYS A 119     -53.771  10.871 105.232  1.00 47.83           O  
ANISOU  646  O   LYS A 119     6188   6265   5721   -145    579    227       O  
ATOM    647  CB  LYS A 119     -51.337   9.746 107.061  1.00 47.14           C  
ANISOU  647  CB  LYS A 119     6206   6165   5542   -180    516    266       C  
ATOM    648  N   ASP A 120     -54.410  10.739 107.417  1.00 44.17           N  
ANISOU  648  N   ASP A 120     5783   5818   5183   -168    638    227       N  
ATOM    649  CA AASP A 120     -55.831  10.529 107.127  0.50 43.77           C  
ANISOU  649  CA AASP A 120     5690   5779   5162   -167    683    225       C  
ATOM    650  CA BASP A 120     -55.831  10.529 107.134  0.50 43.68           C  
ANISOU  650  CA BASP A 120     5679   5768   5151   -167    683    225       C  
ATOM    651  C   ASP A 120     -56.523  11.825 106.675  1.00 46.56           C  
ANISOU  651  C   ASP A 120     6013   6135   5542   -139    706    193       C  
ATOM    652  O   ASP A 120     -57.357  11.790 105.773  1.00 46.28           O  
ANISOU  652  O   ASP A 120     5927   6104   5553   -130    717    191       O  
ATOM    653  CB AASP A 120     -56.555   9.925 108.346  0.50 46.16           C  
ANISOU  653  CB AASP A 120     6017   6096   5428   -189    729    234       C  
ATOM    654  CB BASP A 120     -56.553   9.928 108.367  0.50 45.96           C  
ANISOU  654  CB BASP A 120     5992   6070   5401   -189    730    234       C  
ATOM    655  CG AASP A 120     -56.083   8.527 108.707  0.50 56.06           C  
ANISOU  655  CG AASP A 120     7293   7346   6663   -217    711    269       C  
ATOM    656  CG BASP A 120     -56.387  10.741 109.653  0.50 55.04           C  
ANISOU  656  CG BASP A 120     7192   7225   6495   -190    752    217       C  
ATOM    657  OD1AASP A 120     -54.859   8.345 108.901  0.50 56.86           O  
ANISOU  657  OD1AASP A 120     7429   7436   6740   -221    668    281       O  
ATOM    658  OD1BASP A 120     -55.501  11.630 109.688  0.50 55.22           O  
ANISOU  658  OD1BASP A 120     7239   7238   6504   -177    724    200       O  
ATOM    659  OD2AASP A 120     -56.942   7.638 108.876  0.50 61.23           O  
ANISOU  659  OD2AASP A 120     7932   8009   7325   -234    742    285       O  
ATOM    660  OD2BASP A 120     -57.096  10.444 110.637  0.50 61.00           O  
ANISOU  660  OD2BASP A 120     7966   7992   7218   -205    798    220       O  
ATOM    661  N   ALA A 121     -56.176  12.974 107.305  1.00 41.83           N  
ANISOU  661  N   ALA A 121     5447   5533   4915   -127    712    169       N  
ATOM    662  CA  ALA A 121     -56.799  14.270 106.962  1.00 41.12           C  
ANISOU  662  CA  ALA A 121     5333   5442   4849   -100    735    139       C  
ATOM    663  C   ALA A 121     -56.285  14.830 105.624  1.00 42.70           C  
ANISOU  663  C   ALA A 121     5503   5628   5091    -78    693    134       C  
ATOM    664  O   ALA A 121     -57.042  15.466 104.896  1.00 42.01           O  
ANISOU  664  O   ALA A 121     5376   5543   5045    -57    708    120       O  
ATOM    665  CB  ALA A 121     -56.565  15.277 108.076  1.00 42.28           C  
ANISOU  665  CB  ALA A 121     5527   5587   4949    -95    755    114       C  
ATOM    666  N   TYR A 122     -54.991  14.634 105.328  1.00 37.72           N  
ANISOU  666  N   TYR A 122     4893   4985   4453    -84    642    145       N  
ATOM    667  CA  TYR A 122     -54.395  15.128 104.081  1.00 36.45           C  
ANISOU  667  CA  TYR A 122     4708   4812   4330    -67    602    141       C  
ATOM    668  C   TYR A 122     -54.191  13.979 103.067  1.00 36.95           C  
ANISOU  668  C   TYR A 122     4741   4874   4423    -76    572    167       C  
ATOM    669  O   TYR A 122     -53.256  14.022 102.264  1.00 36.17           O  
ANISOU  669  O   TYR A 122     4638   4764   4340    -71    529    172       O  
ATOM    670  CB  TYR A 122     -53.055  15.849 104.365  1.00 37.91           C  
ANISOU  670  CB  TYR A 122     4934   4983   4489    -65    566    132       C  
ATOM    671  CG  TYR A 122     -53.206  17.095 105.213  1.00 40.81           C  
ANISOU  671  CG  TYR A 122     5330   5347   4830    -54    592    103       C  
ATOM    672  CD1 TYR A 122     -53.471  18.331 104.630  1.00 43.11           C  
ANISOU  672  CD1 TYR A 122     5603   5628   5149    -28    598     80       C  
ATOM    673  CD2 TYR A 122     -53.026  17.050 106.592  1.00 42.08           C  
ANISOU  673  CD2 TYR A 122     5540   5513   4937    -70    609     98       C  
ATOM    674  CE1 TYR A 122     -53.602  19.484 105.404  1.00 44.67           C  
ANISOU  674  CE1 TYR A 122     5829   5819   5323    -18    622     51       C  
ATOM    675  CE2 TYR A 122     -53.161  18.195 107.378  1.00 43.42           C  
ANISOU  675  CE2 TYR A 122     5739   5678   5080    -61    634     69       C  
ATOM    676  CZ  TYR A 122     -53.446  19.412 106.779  1.00 52.30           C  
ANISOU  676  CZ  TYR A 122     6844   6791   6235    -35    641     44       C  
ATOM    677  OH  TYR A 122     -53.570  20.546 107.547  1.00 55.12           O  
ANISOU  677  OH  TYR A 122     7233   7142   6569    -26    666     13       O  
ATOM    678  N   ALA A 123     -55.096  12.971 103.085  1.00 30.66           N  
ANISOU  678  N   ALA A 123     3922   4089   3637    -89    596    182       N  
ATOM    679  CA  ALA A 123     -54.981  11.790 102.221  1.00 28.97           C  
ANISOU  679  CA  ALA A 123     3683   3874   3450   -101    571    205       C  
ATOM    680  C   ALA A 123     -55.027  12.146 100.724  1.00 29.63           C  
ANISOU  680  C   ALA A 123     3724   3952   3581    -82    547    200       C  
ATOM    681  O   ALA A 123     -54.279  11.566  99.936  1.00 29.11           O  
ANISOU  681  O   ALA A 123     3653   3877   3530    -87    510    214       O  
ATOM    682  CB  ALA A 123     -56.071  10.786 102.558  1.00 29.96           C  
ANISOU  682  CB  ALA A 123     3791   4012   3579   -119    607    219       C  
ATOM    683  N   ASN A 124     -55.907  13.104 100.333  1.00 23.52           N  
ANISOU  683  N   ASN A 124     2921   3184   2832    -61    570    182       N  
ATOM    684  CA  ASN A 124     -56.044  13.516  98.920  1.00 21.49           C  
ANISOU  684  CA  ASN A 124     2624   2923   2619    -43    548    178       C  
ATOM    685  C   ASN A 124     -54.812  14.297  98.430  1.00 23.05           C  
ANISOU  685  C   ASN A 124     2840   3104   2814    -30    509    171       C  
ATOM    686  O   ASN A 124     -54.451  14.201  97.255  1.00 21.84           O  
ANISOU  686  O   ASN A 124     2666   2945   2688    -24    478    177       O  
ATOM    687  CB  ASN A 124     -57.313  14.336  98.717  1.00 19.33           C  
ANISOU  687  CB  ASN A 124     2315   2658   2371    -23    582    162       C  
ATOM    688  CG  ASN A 124     -58.582  13.568  99.007  1.00 25.94           C  
ANISOU  688  CG  ASN A 124     3124   3513   3220    -36    619    169       C  
ATOM    689  OD1 ASN A 124     -58.771  12.433  98.557  1.00 18.33           O  
ANISOU  689  OD1 ASN A 124     2142   2554   2270    -54    609    186       O  
ATOM    690  ND2 ASN A 124     -59.511  14.203  99.702  1.00 14.94           N  
ANISOU  690  ND2 ASN A 124     1724   2129   1824    -26    663    154       N  
ATOM    691  N   THR A 125     -54.151  15.051  99.340  1.00 18.78           N  
ANISOU  691  N   THR A 125     2340   2557   2241    -27    511    159       N  
ATOM    692  CA  THR A 125     -52.928  15.797  99.006  1.00 17.70           C  
ANISOU  692  CA  THR A 125     2223   2404   2099    -18    475    153       C  
ATOM    693  C   THR A 125     -51.732  14.836  98.884  1.00 20.07           C  
ANISOU  693  C   THR A 125     2540   2697   2388    -36    436    173       C  
ATOM    694  O   THR A 125     -50.918  14.974  97.969  1.00 19.30           O  
ANISOU  694  O   THR A 125     2435   2590   2308    -30    402    176       O  
ATOM    695  CB  THR A 125     -52.669  16.901 100.055  1.00 24.61           C  
ANISOU  695  CB  THR A 125     3135   3273   2942    -12    489    132       C  
ATOM    696  OG1 THR A 125     -53.878  17.630 100.277  1.00 24.07           O  
ANISOU  696  OG1 THR A 125     3051   3211   2885      4    531    114       O  
ATOM    697  CG2 THR A 125     -51.556  17.854  99.636  1.00 20.52           C  
ANISOU  697  CG2 THR A 125     2633   2738   2427     -2    456    122       C  
ATOM    698  N   ILE A 126     -51.646  13.847  99.797  1.00 15.89           N  
ANISOU  698  N   ILE A 126     2034   2174   1831    -57    443    187       N  
ATOM    699  CA  ILE A 126     -50.589  12.840  99.765  1.00 15.34           C  
ANISOU  699  CA  ILE A 126     1980   2098   1752    -73    409    208       C  
ATOM    700  C   ILE A 126     -50.733  11.946  98.526  1.00 18.59           C  
ANISOU  700  C   ILE A 126     2355   2508   2201    -74    393    222       C  
ATOM    701  O   ILE A 126     -49.749  11.708  97.826  1.00 17.80           O  
ANISOU  701  O   ILE A 126     2253   2397   2112    -73    358    230       O  
ATOM    702  CB  ILE A 126     -50.572  12.012 101.091  1.00 19.09           C  
ANISOU  702  CB  ILE A 126     2488   2578   2187    -95    422    221       C  
ATOM    703  CG1 ILE A 126     -50.193  12.916 102.296  1.00 19.74           C  
ANISOU  703  CG1 ILE A 126     2613   2661   2227    -95    430    206       C  
ATOM    704  CG2 ILE A 126     -49.614  10.802 100.979  1.00 20.05           C  
ANISOU  704  CG2 ILE A 126     2620   2692   2306   -110    388    247       C  
ATOM    705  CD1 ILE A 126     -50.579  12.351 103.649  1.00 25.44           C  
ANISOU  705  CD1 ILE A 126     3366   3392   2907   -114    458    214       C  
ATOM    706  N   ALA A 127     -51.982  11.502  98.217  1.00 15.24           N  
ANISOU  706  N   ALA A 127     1900   2094   1797    -77    420    224       N  
ATOM    707  CA  ALA A 127     -52.249  10.667  97.034  1.00 14.41           C  
ANISOU  707  CA  ALA A 127     1760   1988   1726    -80    407    235       C  
ATOM    708  C   ALA A 127     -51.792  11.373  95.752  1.00 17.92           C  
ANISOU  708  C   ALA A 127     2185   2426   2199    -61    380    226       C  
ATOM    709  O   ALA A 127     -51.022  10.801  94.979  1.00 17.18           O  
ANISOU  709  O   ALA A 127     2087   2323   2117    -65    350    236       O  
ATOM    710  CB  ALA A 127     -53.728  10.335  96.951  1.00 14.99           C  
ANISOU  710  CB  ALA A 127     1801   2076   1818    -84    442    234       C  
ATOM    711  N   PHE A 128     -52.180  12.664  95.583  1.00 14.44           N  
ANISOU  711  N   PHE A 128     1735   1987   1766    -41    391    208       N  
ATOM    712  CA  PHE A 128     -51.752  13.467  94.432  1.00 13.99           C  
ANISOU  712  CA  PHE A 128     1662   1922   1732    -23    367    201       C  
ATOM    713  C   PHE A 128     -50.226  13.623  94.395  1.00 18.56           C  
ANISOU  713  C   PHE A 128     2268   2487   2297    -25    333    204       C  
ATOM    714  O   PHE A 128     -49.628  13.549  93.322  1.00 17.77           O  
ANISOU  714  O   PHE A 128     2155   2379   2216    -20    307    208       O  
ATOM    715  CB  PHE A 128     -52.440  14.854  94.444  1.00 15.61           C  
ANISOU  715  CB  PHE A 128     1858   2129   1946     -2    386    182       C  
ATOM    716  CG  PHE A 128     -51.638  15.942  93.763  1.00 16.74           C  
ANISOU  716  CG  PHE A 128     2005   2259   2097     15    362    173       C  
ATOM    717  CD1 PHE A 128     -51.616  16.049  92.379  1.00 19.35           C  
ANISOU  717  CD1 PHE A 128     2308   2587   2456     25    342    177       C  
ATOM    718  CD2 PHE A 128     -50.847  16.812  94.503  1.00 18.51           C  
ANISOU  718  CD2 PHE A 128     2263   2472   2298     19    359    162       C  
ATOM    719  CE1 PHE A 128     -50.814  16.998  91.751  1.00 20.07           C  
ANISOU  719  CE1 PHE A 128     2406   2665   2554     38    320    171       C  
ATOM    720  CE2 PHE A 128     -50.053  17.766  93.871  1.00 21.00           C  
ANISOU  720  CE2 PHE A 128     2583   2775   2623     31    336    156       C  
ATOM    721  CZ  PHE A 128     -50.051  17.862  92.501  1.00 19.12           C  
ANISOU  721  CZ  PHE A 128     2317   2533   2413     41    318    161       C  
ATOM    722  N   ALA A 129     -49.599  13.865  95.572  1.00 15.77           N  
ANISOU  722  N   ALA A 129     1951   2130   1911    -31    335    201       N  
ATOM    723  CA  ALA A 129     -48.153  14.074  95.656  1.00 15.48           C  
ANISOU  723  CA  ALA A 129     1938   2080   1861    -33    302    204       C  
ATOM    724  C   ALA A 129     -47.381  12.832  95.237  1.00 20.07           C  
ANISOU  724  C   ALA A 129     2518   2658   2449    -46    277    224       C  
ATOM    725  O   ALA A 129     -46.336  12.949  94.599  1.00 20.00           O  
ANISOU  725  O   ALA A 129     2510   2640   2451    -42    248    227       O  
ATOM    726  CB  ALA A 129     -47.764  14.484  97.061  1.00 16.37           C  
ANISOU  726  CB  ALA A 129     2091   2193   1936    -40    309    198       C  
ATOM    727  N   ARG A 130     -47.917  11.631  95.557  1.00 16.75           N  
ANISOU  727  N   ARG A 130     2095   2243   2025    -60    289    238       N  
ATOM    728  CA  ARG A 130     -47.293  10.357  95.158  1.00 15.82           C  
ANISOU  728  CA  ARG A 130     1976   2119   1916    -71    267    257       C  
ATOM    729  C   ARG A 130     -47.389  10.143  93.633  1.00 18.43           C  
ANISOU  729  C   ARG A 130     2273   2446   2282    -64    255    257       C  
ATOM    730  O   ARG A 130     -46.474   9.572  93.038  1.00 18.20           O  
ANISOU  730  O   ARG A 130     2244   2408   2264    -66    231    266       O  
ATOM    731  CB  ARG A 130     -47.925   9.176  95.924  1.00 14.68           C  
ANISOU  731  CB  ARG A 130     1839   1980   1759    -90    286    272       C  
ATOM    732  CG  ARG A 130     -47.727   9.276  97.445  1.00 19.62           C  
ANISOU  732  CG  ARG A 130     2502   2609   2345    -99    295    275       C  
ATOM    733  CD  ARG A 130     -48.474   8.196  98.204  1.00 13.17           C  
ANISOU  733  CD  ARG A 130     1693   1797   1514   -118    319    290       C  
ATOM    734  NE  ARG A 130     -47.849   6.884  98.043  1.00 14.60           N  
ANISOU  734  NE  ARG A 130     1879   1968   1701   -129    298    312       N  
ATOM    735  CZ  ARG A 130     -48.215   5.804  98.723  1.00 24.59           C  
ANISOU  735  CZ  ARG A 130     3157   3233   2954   -147    310    330       C  
ATOM    736  NH1 ARG A 130     -49.191   5.876  99.619  1.00 10.66           N  
ANISOU  736  NH1 ARG A 130     1402   1481   1169   -157    345    329       N  
ATOM    737  NH2 ARG A 130     -47.599   4.648  98.522  1.00 13.04           N  
ANISOU  737  NH2 ARG A 130     1698   1756   1499   -156    290    351       N  
ATOM    738  N   ILE A 131     -48.503  10.643  92.995  1.00 14.17           N  
ANISOU  738  N   ILE A 131     1706   1915   1761    -55    273    246       N  
ATOM    739  CA AILE A 131     -48.679  10.549  91.543  0.50 13.27           C  
ANISOU  739  CA AILE A 131     1563   1801   1678    -48    261    244       C  
ATOM    740  CA BILE A 131     -48.690  10.563  91.534  0.50 13.37           C  
ANISOU  740  CA BILE A 131     1575   1814   1691    -48    261    244       C  
ATOM    741  C   ILE A 131     -47.709  11.488  90.821  1.00 17.19           C  
ANISOU  741  C   ILE A 131     2061   2288   2181    -33    238    237       C  
ATOM    742  O   ILE A 131     -47.044  11.072  89.864  1.00 16.53           O  
ANISOU  742  O   ILE A 131     1971   2198   2112    -33    217    243       O  
ATOM    743  CB AILE A 131     -50.164  10.829  91.139  0.50 16.30           C  
ANISOU  743  CB AILE A 131     1916   2198   2079    -42    284    236       C  
ATOM    744  CB BILE A 131     -50.176  10.897  91.136  0.50 16.51           C  
ANISOU  744  CB BILE A 131     1943   2225   2106    -41    285    235       C  
ATOM    745  CG1AILE A 131     -51.121   9.796  91.787  0.50 16.63           C  
ANISOU  745  CG1AILE A 131     1953   2249   2118    -60    308    244       C  
ATOM    746  CG1BILE A 131     -51.193   9.954  91.850  0.50 17.02           C  
ANISOU  746  CG1BILE A 131     2002   2299   2166    -58    310    243       C  
ATOM    747  CG2AILE A 131     -50.324  10.855  89.601  0.50 16.50           C  
ANISOU  747  CG2AILE A 131     1913   2224   2133    -35    268    234       C  
ATOM    748  CG2BILE A 131     -50.364  10.886  89.601  0.50 16.74           C  
ANISOU  748  CG2BILE A 131     1943   2255   2164    -34    269    234       C  
ATOM    749  CD1AILE A 131     -52.598  10.202  91.768  0.50 20.33           C  
ANISOU  749  CD1AILE A 131     2393   2732   2599    -55    336    236       C  
ATOM    750  CD1BILE A 131     -51.024   8.476  91.539  0.50 22.30           C  
ANISOU  750  CD1BILE A 131     2669   2963   2842    -77    300    258       C  
ATOM    751  N   TRP A 132     -47.635  12.767  91.269  1.00 13.67           N  
ANISOU  751  N   TRP A 132     1626   1842   1726    -22    244    225       N  
ATOM    752  CA  TRP A 132     -46.769  13.757  90.643  1.00 13.45           C  
ANISOU  752  CA  TRP A 132     1601   1805   1704     -9    224    218       C  
ATOM    753  C   TRP A 132     -45.290  13.434  90.859  1.00 17.38           C  
ANISOU  753  C   TRP A 132     2120   2292   2192    -17    199    226       C  
ATOM    754  O   TRP A 132     -44.467  13.709  89.986  1.00 16.78           O  
ANISOU  754  O   TRP A 132     2038   2208   2128    -11    179    227       O  
ATOM    755  CB  TRP A 132     -47.104  15.169  91.144  1.00 12.35           C  
ANISOU  755  CB  TRP A 132     1470   1665   1558      4    238    203       C  
ATOM    756  CG  TRP A 132     -46.626  16.250  90.228  1.00 13.04           C  
ANISOU  756  CG  TRP A 132     1552   1744   1660     18    223    196       C  
ATOM    757  CD1 TRP A 132     -45.608  17.127  90.457  1.00 15.71           C  
ANISOU  757  CD1 TRP A 132     1910   2070   1990     21    210    190       C  
ATOM    758  CD2 TRP A 132     -47.038  16.460  88.868  1.00 12.79           C  
ANISOU  758  CD2 TRP A 132     1493   1713   1654     29    218    197       C  
ATOM    759  NE1 TRP A 132     -45.412  17.925  89.351  1.00 14.86           N  
ANISOU  759  NE1 TRP A 132     1790   1955   1902     34    199    187       N  
ATOM    760  CE2 TRP A 132     -46.260  17.519  88.353  1.00 16.30           C  
ANISOU  760  CE2 TRP A 132     1944   2145   2103     39    203    192       C  
ATOM    761  CE3 TRP A 132     -47.996  15.853  88.031  1.00 14.09           C  
ANISOU  761  CE3 TRP A 132     1629   1887   1836     30    223    201       C  
ATOM    762  CZ2 TRP A 132     -46.411  17.992  87.043  1.00 15.79           C  
ANISOU  762  CZ2 TRP A 132     1861   2080   2060     51    195    193       C  
ATOM    763  CZ3 TRP A 132     -48.143  16.321  86.735  1.00 15.71           C  
ANISOU  763  CZ3 TRP A 132     1815   2092   2061     42    212    202       C  
ATOM    764  CH2 TRP A 132     -47.366  17.384  86.256  1.00 16.30           C  
ANISOU  764  CH2 TRP A 132     1899   2155   2140     53    199    198       C  
ATOM    765  N   ARG A 133     -44.961  12.789  91.996  1.00 14.53           N  
ANISOU  765  N   ARG A 133     1781   1931   1809    -30    200    234       N  
ATOM    766  CA  ARG A 133     -43.598  12.324  92.284  1.00 13.98           C  
ANISOU  766  CA  ARG A 133     1728   1852   1731    -37    174    245       C  
ATOM    767  C   ARG A 133     -43.193  11.234  91.277  1.00 17.22           C  
ANISOU  767  C   ARG A 133     2121   2257   2162    -40    160    257       C  
ATOM    768  O   ARG A 133     -42.068  11.246  90.772  1.00 18.30           O  
ANISOU  768  O   ARG A 133     2258   2386   2309    -37    138    261       O  
ATOM    769  CB  ARG A 133     -43.514  11.790  93.733  1.00 14.34           C  
ANISOU  769  CB  ARG A 133     1801   1900   1746    -50    179    253       C  
ATOM    770  CG  ARG A 133     -42.157  11.215  94.118  1.00 18.43           C  
ANISOU  770  CG  ARG A 133     2336   2410   2256    -58    150    267       C  
ATOM    771  CD  ARG A 133     -42.189  10.675  95.540  1.00 18.51           C  
ANISOU  771  CD  ARG A 133     2374   2423   2234    -71    154    277       C  
ATOM    772  NE  ARG A 133     -40.962   9.965  95.886  1.00 12.86           N  
ANISOU  772  NE  ARG A 133     1672   1700   1514    -78    125    294       N  
ATOM    773  CZ  ARG A 133     -40.819   8.648  95.783  1.00 27.79           C  
ANISOU  773  CZ  ARG A 133     3560   3586   3413    -84    119    313       C  
ATOM    774  NH1 ARG A 133     -41.826   7.895  95.356  1.00 21.94           N  
ANISOU  774  NH1 ARG A 133     2804   2847   2685    -87    140    316       N  
ATOM    775  NH2 ARG A 133     -39.673   8.073  96.117  1.00 15.33           N  
ANISOU  775  NH2 ARG A 133     1992   1999   1832    -88     91    329       N  
ATOM    776  N   VAL A 134     -44.136  10.340  90.934  1.00 12.50           N  
ANISOU  776  N   VAL A 134     1509   1665   1575    -45    174    262       N  
ATOM    777  CA  VAL A 134     -43.900   9.302  89.930  1.00 12.02           C  
ANISOU  777  CA  VAL A 134     1434   1599   1535    -48    163    270       C  
ATOM    778  C   VAL A 134     -43.698   9.928  88.539  1.00 15.55           C  
ANISOU  778  C   VAL A 134     1861   2044   2003    -36    154    261       C  
ATOM    779  O   VAL A 134     -42.674   9.678  87.898  1.00 15.06           O  
ANISOU  779  O   VAL A 134     1798   1973   1951    -34    136    265       O  
ATOM    780  CB  VAL A 134     -45.041   8.238  89.925  1.00 15.68           C  
ANISOU  780  CB  VAL A 134     1887   2068   2004    -59    181    276       C  
ATOM    781  CG1 VAL A 134     -45.006   7.395  88.646  1.00 15.18           C  
ANISOU  781  CG1 VAL A 134     1805   1999   1964    -61    172    278       C  
ATOM    782  CG2 VAL A 134     -44.965   7.351  91.163  1.00 15.56           C  
ANISOU  782  CG2 VAL A 134     1892   2049   1969    -73    186    290       C  
ATOM    783  N   TYR A 135     -44.642  10.810  88.113  1.00 11.22           N  
ANISOU  783  N   TYR A 135     1299   1505   1460    -27    167    250       N  
ATOM    784  CA  TYR A 135     -44.602  11.439  86.785  1.00 11.08           C  
ANISOU  784  CA  TYR A 135     1264   1487   1460    -16    159    244       C  
ATOM    785  C   TYR A 135     -43.309  12.223  86.541  1.00 14.54           C  
ANISOU  785  C   TYR A 135     1712   1915   1898     -9    141    242       C  
ATOM    786  O   TYR A 135     -42.684  12.058  85.494  1.00 12.63           O  
ANISOU  786  O   TYR A 135     1462   1669   1669     -7    129    244       O  
ATOM    787  CB  TYR A 135     -45.839  12.342  86.562  1.00 12.22           C  
ANISOU  787  CB  TYR A 135     1393   1641   1610     -6    174    234       C  
ATOM    788  CG  TYR A 135     -45.821  13.062  85.231  1.00 14.23           C  
ANISOU  788  CG  TYR A 135     1633   1896   1880      6    165    229       C  
ATOM    789  CD1 TYR A 135     -46.042  12.375  84.040  1.00 16.85           C  
ANISOU  789  CD1 TYR A 135     1948   2230   2225      3    157    232       C  
ATOM    790  CD2 TYR A 135     -45.591  14.431  85.160  1.00 15.16           C  
ANISOU  790  CD2 TYR A 135     1754   2008   1997     19    163    222       C  
ATOM    791  CE1 TYR A 135     -45.993  13.026  82.807  1.00 18.30           C  
ANISOU  791  CE1 TYR A 135     2120   2413   2420     13    147    229       C  
ATOM    792  CE2 TYR A 135     -45.563  15.100  83.934  1.00 16.22           C  
ANISOU  792  CE2 TYR A 135     1878   2142   2145     30    154    221       C  
ATOM    793  CZ  TYR A 135     -45.765  14.393  82.759  1.00 21.99           C  
ANISOU  793  CZ  TYR A 135     2592   2877   2886     27    146    225       C  
ATOM    794  OH  TYR A 135     -45.731  15.044  81.548  1.00 18.62           O  
ANISOU  794  OH  TYR A 135     2157   2450   2469     36    136    225       O  
ATOM    795  N   VAL A 136     -42.920  13.100  87.495  1.00 12.99           N  
ANISOU  795  N   VAL A 136     1533   1716   1687     -7    141    238       N  
ATOM    796  CA  VAL A 136     -41.704  13.916  87.354  1.00 13.06           C  
ANISOU  796  CA  VAL A 136     1551   1716   1697     -2    124    236       C  
ATOM    797  C   VAL A 136     -40.441  13.028  87.229  1.00 16.84           C  
ANISOU  797  C   VAL A 136     2032   2186   2179     -9    106    247       C  
ATOM    798  O   VAL A 136     -39.579  13.301  86.385  1.00 16.32           O  
ANISOU  798  O   VAL A 136     1960   2114   2126     -6     94    247       O  
ATOM    799  CB  VAL A 136     -41.568  14.969  88.499  1.00 17.64           C  
ANISOU  799  CB  VAL A 136     2151   2293   2258     -1    127    227       C  
ATOM    800  CG1 VAL A 136     -40.232  15.710  88.410  1.00 17.75           C  
ANISOU  800  CG1 VAL A 136     2175   2297   2274     -1    108    226       C  
ATOM    801  CG2 VAL A 136     -42.728  15.952  88.473  1.00 17.61           C  
ANISOU  801  CG2 VAL A 136     2142   2293   2254      9    147    215       C  
ATOM    802  N   HIS A 137     -40.367  11.928  88.026  1.00 12.83           N  
ANISOU  802  N   HIS A 137     1533   1678   1662    -19    105    257       N  
ATOM    803  CA  HIS A 137     -39.209  11.031  87.985  1.00 11.95           C  
ANISOU  803  CA  HIS A 137     1424   1559   1557    -24     87    268       C  
ATOM    804  C   HIS A 137     -39.108  10.256  86.650  1.00 14.28           C  
ANISOU  804  C   HIS A 137     1701   1850   1874    -21     86    271       C  
ATOM    805  O   HIS A 137     -38.003   9.963  86.207  1.00 14.19           O  
ANISOU  805  O   HIS A 137     1686   1830   1874    -20     72    276       O  
ATOM    806  CB  HIS A 137     -39.209  10.065  89.177  1.00 13.03           C  
ANISOU  806  CB  HIS A 137     1577   1695   1678    -34     86    280       C  
ATOM    807  CG  HIS A 137     -37.913   9.324  89.338  1.00 16.17           C  
ANISOU  807  CG  HIS A 137     1978   2082   2081    -37     65    293       C  
ATOM    808  ND1 HIS A 137     -37.716   8.085  88.760  1.00 17.59           N  
ANISOU  808  ND1 HIS A 137     2150   2255   2278    -38     63    303       N  
ATOM    809  CD2 HIS A 137     -36.760   9.721  89.925  1.00 17.74           C  
ANISOU  809  CD2 HIS A 137     2188   2278   2276    -37     45    298       C  
ATOM    810  CE1 HIS A 137     -36.472   7.745  89.055  1.00 17.02           C  
ANISOU  810  CE1 HIS A 137     2082   2175   2211    -37     43    314       C  
ATOM    811  NE2 HIS A 137     -35.859   8.697  89.758  1.00 17.41           N  
ANISOU  811  NE2 HIS A 137     2141   2226   2247    -37     31    311       N  
ATOM    812  N   THR A 138     -40.270   9.951  85.994  1.00 10.51           N  
ANISOU  812  N   THR A 138     1212   1379   1403    -21    100    266       N  
ATOM    813  CA  THR A 138     -40.255   9.267  84.683  1.00 10.58           C  
ANISOU  813  CA  THR A 138     1205   1385   1429    -20     99    266       C  
ATOM    814  C   THR A 138     -39.511  10.111  83.658  1.00 15.49           C  
ANISOU  814  C   THR A 138     1820   2005   2061    -11     91    261       C  
ATOM    815  O   THR A 138     -38.709   9.583  82.898  1.00 15.14           O  
ANISOU  815  O   THR A 138     1772   1954   2029    -10     84    263       O  
ATOM    816  CB  THR A 138     -41.703   8.926  84.197  1.00 16.38           C  
ANISOU  816  CB  THR A 138     1927   2128   2167    -24    113    261       C  
ATOM    817  OG1 THR A 138     -42.396  10.132  83.857  1.00 17.05           O  
ANISOU  817  OG1 THR A 138     2005   2223   2251    -15    119    252       O  
ATOM    818  CG2 THR A 138     -42.496   8.128  85.220  1.00 13.66           C  
ANISOU  818  CG2 THR A 138     1589   1787   1813    -35    124    267       C  
ATOM    819  N   LEU A 139     -39.719  11.451  83.698  1.00 13.22           N  
ANISOU  819  N   LEU A 139     1534   1721   1768     -5     93    254       N  
ATOM    820  CA  LEU A 139     -39.059  12.391  82.770  1.00 12.86           C  
ANISOU  820  CA  LEU A 139     1484   1673   1731      3     87    250       C  
ATOM    821  C   LEU A 139     -37.544  12.384  82.956  1.00 15.92           C  
ANISOU  821  C   LEU A 139     1876   2051   2123      1     73    255       C  
ATOM    822  O   LEU A 139     -36.814  12.622  82.005  1.00 16.18           O  
ANISOU  822  O   LEU A 139     1902   2080   2167      5     69    255       O  
ATOM    823  CB  LEU A 139     -39.610  13.819  82.964  1.00 12.96           C  
ANISOU  823  CB  LEU A 139     1499   1689   1737     10     92    243       C  
ATOM    824  CG  LEU A 139     -41.144  13.959  82.921  1.00 17.61           C  
ANISOU  824  CG  LEU A 139     2079   2287   2323     14    105    238       C  
ATOM    825  CD1 LEU A 139     -41.573  15.352  83.339  1.00 18.03           C  
ANISOU  825  CD1 LEU A 139     2138   2341   2372     23    111    230       C  
ATOM    826  CD2 LEU A 139     -41.693  13.619  81.541  1.00 18.65           C  
ANISOU  826  CD2 LEU A 139     2195   2424   2466     16    106    237       C  
ATOM    827  N   ALA A 140     -37.071  12.087  84.185  1.00 11.49           N  
ANISOU  827  N   ALA A 140     1326   1487   1553     -4     66    261       N  
ATOM    828  CA  ALA A 140     -35.637  11.999  84.468  1.00 10.49           C  
ANISOU  828  CA  ALA A 140     1201   1351   1432     -6     50    268       C  
ATOM    829  C   ALA A 140     -35.090  10.604  84.124  1.00 14.07           C  
ANISOU  829  C   ALA A 140     1649   1800   1899     -7     46    277       C  
ATOM    830  O   ALA A 140     -34.069  10.493  83.441  1.00 14.37           O  
ANISOU  830  O   ALA A 140     1677   1831   1952     -4     40    279       O  
ATOM    831  CB  ALA A 140     -35.374  12.315  85.932  1.00 11.17           C  
ANISOU  831  CB  ALA A 140     1305   1438   1502    -12     41    270       C  
ATOM    832  N   ALA A 141     -35.789   9.532  84.585  1.00 10.08           N  
ANISOU  832  N   ALA A 141     1147   1294   1388    -11     52    281       N  
ATOM    833  CA  ALA A 141     -35.345   8.141  84.391  1.00  9.33           C  
ANISOU  833  CA  ALA A 141     1049   1190   1305    -12     49    290       C  
ATOM    834  C   ALA A 141     -35.364   7.705  82.911  1.00 12.48           C  
ANISOU  834  C   ALA A 141     1436   1587   1721     -8     57    284       C  
ATOM    835  O   ALA A 141     -34.549   6.888  82.513  1.00 12.30           O  
ANISOU  835  O   ALA A 141     1407   1553   1714     -6     53    288       O  
ATOM    836  CB  ALA A 141     -36.194   7.201  85.223  1.00 10.07           C  
ANISOU  836  CB  ALA A 141     1153   1284   1389    -20     55    297       C  
ATOM    837  N   ASP A 142     -36.304   8.244  82.105  1.00  9.23           N  
ANISOU  837  N   ASP A 142     1018   1183   1305     -8     68    274       N  
ATOM    838  CA  ASP A 142     -36.391   7.885  80.673  1.00  8.40           C  
ANISOU  838  CA  ASP A 142      903   1076   1211     -5     74    267       C  
ATOM    839  C   ASP A 142     -35.259   8.532  79.868  1.00 13.34           C  
ANISOU  839  C   ASP A 142     1523   1700   1847      1     71    265       C  
ATOM    840  O   ASP A 142     -34.959   8.086  78.754  1.00 13.35           O  
ANISOU  840  O   ASP A 142     1518   1698   1858      4     76    261       O  
ATOM    841  CB  ASP A 142     -37.770   8.275  80.086  1.00  9.44           C  
ANISOU  841  CB  ASP A 142     1031   1221   1336     -7     83    258       C  
ATOM    842  CG  ASP A 142     -38.933   7.443  80.618  1.00 16.36           C  
ANISOU  842  CG  ASP A 142     1909   2100   2207    -15     90    259       C  
ATOM    843  OD1 ASP A 142     -38.672   6.401  81.271  1.00 15.27           O  
ANISOU  843  OD1 ASP A 142     1777   1952   2071    -21     89    267       O  
ATOM    844  OD2 ASP A 142     -40.102   7.804  80.334  1.00 22.37           O  
ANISOU  844  OD2 ASP A 142     2664   2871   2963    -17     96    254       O  
ATOM    845  N   LYS A 143     -34.602   9.565  80.451  1.00 10.06           N  
ANISOU  845  N   LYS A 143     1110   1285   1429      3     63    268       N  
ATOM    846  CA  LYS A 143     -33.477  10.264  79.815  1.00  9.46           C  
ANISOU  846  CA  LYS A 143     1026   1206   1363      7     59    267       C  
ATOM    847  C   LYS A 143     -32.142   9.627  80.191  1.00 13.68           C  
ANISOU  847  C   LYS A 143     1555   1730   1912      9     50    276       C  
ATOM    848  O   LYS A 143     -31.353   9.291  79.308  1.00 14.61           O  
ANISOU  848  O   LYS A 143     1663   1844   2045     13     55    275       O  
ATOM    849  CB  LYS A 143     -33.469  11.760  80.213  1.00 11.32           C  
ANISOU  849  CB  LYS A 143     1266   1445   1590      7     55    265       C  
ATOM    850  CG  LYS A 143     -34.623  12.557  79.646  1.00 10.15           C  
ANISOU  850  CG  LYS A 143     1120   1305   1432     10     64    258       C  
ATOM    851  CD  LYS A 143     -34.579  14.015  80.126  1.00 13.29           C  
ANISOU  851  CD  LYS A 143     1524   1703   1824     11     60    256       C  
ATOM    852  CE  LYS A 143     -35.655  14.868  79.484  1.00 14.41           C  
ANISOU  852  CE  LYS A 143     1666   1850   1959     16     68    250       C  
ATOM    853  NZ  LYS A 143     -37.020  14.391  79.825  1.00 18.60           N  
ANISOU  853  NZ  LYS A 143     2197   2389   2482     17     75    247       N  
ATOM    854  N   PHE A 144     -31.854   9.525  81.510  1.00  9.75           N  
ANISOU  854  N   PHE A 144     1064   1231   1409      6     37    284       N  
ATOM    855  CA  PHE A 144     -30.536   9.085  81.994  1.00 10.01           C  
ANISOU  855  CA  PHE A 144     1090   1256   1457      7     24    294       C  
ATOM    856  C   PHE A 144     -30.460   7.581  82.273  1.00 14.34           C  
ANISOU  856  C   PHE A 144     1640   1795   2014     10     22    302       C  
ATOM    857  O   PHE A 144     -29.366   7.015  82.280  1.00 13.97           O  
ANISOU  857  O   PHE A 144     1583   1740   1986     15     15    310       O  
ATOM    858  CB  PHE A 144     -30.122   9.881  83.249  1.00 11.91           C  
ANISOU  858  CB  PHE A 144     1338   1499   1687      2      6    299       C  
ATOM    859  CG  PHE A 144     -30.069  11.376  83.053  1.00 12.68           C  
ANISOU  859  CG  PHE A 144     1437   1602   1780     -1      6    291       C  
ATOM    860  CD1 PHE A 144     -28.967  11.976  82.456  1.00 15.00           C  
ANISOU  860  CD1 PHE A 144     1717   1892   2089      0      3    291       C  
ATOM    861  CD2 PHE A 144     -31.071  12.196  83.560  1.00 14.79           C  
ANISOU  861  CD2 PHE A 144     1718   1875   2026     -4     10    284       C  
ATOM    862  CE1 PHE A 144     -28.899  13.367  82.311  1.00 15.20           C  
ANISOU  862  CE1 PHE A 144     1745   1920   2111     -4      3    284       C  
ATOM    863  CE2 PHE A 144     -30.997  13.587  83.422  1.00 17.59           C  
ANISOU  863  CE2 PHE A 144     2076   2231   2378     -6     10    276       C  
ATOM    864  CZ  PHE A 144     -29.909  14.161  82.800  1.00 14.92           C  
ANISOU  864  CZ  PHE A 144     1726   1889   2056     -6      6    277       C  
ATOM    865  N   GLY A 145     -31.603   6.969  82.585  1.00 10.72           N  
ANISOU  865  N   GLY A 145     1192   1338   1543      5     29    302       N  
ATOM    866  CA  GLY A 145     -31.662   5.551  82.926  1.00 10.74           C  
ANISOU  866  CA  GLY A 145     1199   1330   1552      6     28    310       C  
ATOM    867  C   GLY A 145     -31.541   5.303  84.419  1.00 14.66           C  
ANISOU  867  C   GLY A 145     1707   1824   2037      1     13    324       C  
ATOM    868  O   GLY A 145     -32.060   6.081  85.225  1.00 15.56           O  
ANISOU  868  O   GLY A 145     1833   1949   2131     -5     10    323       O  
ATOM    869  N   PRO A 146     -30.830   4.221  84.837  1.00  9.42           N  
ANISOU  869  N   PRO A 146     1044   1148   1387      5      3    338       N  
ATOM    870  CA  PRO A 146     -30.680   3.963  86.285  1.00  9.10           C  
ANISOU  870  CA  PRO A 146     1017   1106   1333      1    -14    355       C  
ATOM    871  C   PRO A 146     -30.110   5.171  87.024  1.00 12.99           C  
ANISOU  871  C   PRO A 146     1513   1610   1814     -3    -31    355       C  
ATOM    872  O   PRO A 146     -29.114   5.741  86.598  1.00 13.77           O  
ANISOU  872  O   PRO A 146     1596   1709   1928      2    -39    353       O  
ATOM    873  CB  PRO A 146     -29.733   2.751  86.339  1.00 10.73           C  
ANISOU  873  CB  PRO A 146     1218   1296   1564      9    -25    370       C  
ATOM    874  CG  PRO A 146     -29.136   2.656  84.965  1.00 14.43           C  
ANISOU  874  CG  PRO A 146     1667   1758   2059     19    -14    359       C  
ATOM    875  CD  PRO A 146     -30.147   3.199  84.029  1.00  9.83           C  
ANISOU  875  CD  PRO A 146     1084   1184   1465     15      7    340       C  
HETATM  876  N   MSE A 147     -30.803   5.620  88.064  1.00  8.13           N  
ANISOU  876  N   MSE A 147      915   1003   1169    -12    -33    356       N  
HETATM  877  CA  MSE A 147     -30.432   6.829  88.779  1.00  6.69           C  
ANISOU  877  CA  MSE A 147      740    831    972    -17    -47    353       C  
HETATM  878  C   MSE A 147     -31.052   6.823  90.173  1.00 14.19           C  
ANISOU  878  C   MSE A 147     1716   1787   1890    -27    -52    360       C  
HETATM  879  O   MSE A 147     -31.861   5.949  90.478  1.00 14.83           O  
ANISOU  879  O   MSE A 147     1807   1865   1963    -30    -41    366       O  
HETATM  880  CB  MSE A 147     -30.897   8.080  87.989  1.00  7.22           C  
ANISOU  880  CB  MSE A 147      801    906   1036    -17    -33    334       C  
HETATM  881  CG  MSE A 147     -32.425   8.158  87.809  1.00 12.06           C  
ANISOU  881  CG  MSE A 147     1423   1526   1635    -20     -9    324       C  
HETATM  882 SE   MSE A 147     -32.993   9.726  86.816  0.75 16.78          SE  
ANISOU  882 SE   MSE A 147     2012   2132   2232    -17      6    303      SE  
HETATM  883  CE  MSE A 147     -32.361  11.136  88.071  1.00 14.01           C  
ANISOU  883  CE  MSE A 147     1677   1785   1861    -24    -12    300       C  
ATOM    884  N   PRO A 148     -30.744   7.831  91.031  1.00 12.38           N  
ANISOU  884  N   PRO A 148     1498   1565   1642    -34    -66    357       N  
ATOM    885  CA  PRO A 148     -31.395   7.877  92.345  1.00 12.96           C  
ANISOU  885  CA  PRO A 148     1598   1645   1680    -44    -67    361       C  
ATOM    886  C   PRO A 148     -32.888   8.161  92.232  1.00 17.86           C  
ANISOU  886  C   PRO A 148     2228   2273   2286    -47    -37    347       C  
ATOM    887  O   PRO A 148     -33.321   8.871  91.320  1.00 16.58           O  
ANISOU  887  O   PRO A 148     2053   2114   2133    -42    -22    331       O  
ATOM    888  CB  PRO A 148     -30.656   9.026  93.073  1.00 14.51           C  
ANISOU  888  CB  PRO A 148     1804   1847   1862    -50    -88    356       C  
ATOM    889  CG  PRO A 148     -29.449   9.316  92.237  1.00 18.51           C  
ANISOU  889  CG  PRO A 148     2285   2349   2400    -44   -103    355       C  
ATOM    890  CD  PRO A 148     -29.814   8.959  90.849  1.00 13.87           C  
ANISOU  890  CD  PRO A 148     1676   1755   1837    -34    -80    349       C  
ATOM    891  N   PHE A 149     -33.677   7.567  93.121  1.00 15.57           N  
ANISOU  891  N   PHE A 149     1957   1986   1973    -54    -29    355       N  
ATOM    892  CA  PHE A 149     -35.095   7.875  93.252  1.00 15.61           C  
ANISOU  892  CA  PHE A 149     1970   2000   1961    -58     -1    343       C  
ATOM    893  C   PHE A 149     -35.370   8.170  94.732  1.00 20.97           C  
ANISOU  893  C   PHE A 149     2679   2687   2603    -69     -2    346       C  
ATOM    894  O   PHE A 149     -35.674   7.252  95.499  1.00 20.79           O  
ANISOU  894  O   PHE A 149     2671   2662   2564    -77     -1    361       O  
ATOM    895  CB  PHE A 149     -35.962   6.690  92.750  1.00 17.17           C  
ANISOU  895  CB  PHE A 149     2160   2193   2170    -59     18    350       C  
ATOM    896  CG  PHE A 149     -37.427   7.020  92.493  1.00 18.63           C  
ANISOU  896  CG  PHE A 149     2342   2388   2350    -61     48    336       C  
ATOM    897  CD1 PHE A 149     -37.938   8.282  92.786  1.00 21.28           C  
ANISOU  897  CD1 PHE A 149     2682   2733   2668    -60     58    320       C  
ATOM    898  CD2 PHE A 149     -38.284   6.073  91.945  1.00 20.56           C  
ANISOU  898  CD2 PHE A 149     2576   2629   2606    -64     64    339       C  
ATOM    899  CE1 PHE A 149     -39.281   8.584  92.542  1.00 22.21           C  
ANISOU  899  CE1 PHE A 149     2794   2860   2785    -60     85    308       C  
ATOM    900  CE2 PHE A 149     -39.628   6.375  91.709  1.00 23.19           C  
ANISOU  900  CE2 PHE A 149     2902   2972   2936    -66     90    327       C  
ATOM    901  CZ  PHE A 149     -40.115   7.631  92.001  1.00 21.15           C  
ANISOU  901  CZ  PHE A 149     2648   2725   2663    -63    100    312       C  
ATOM    902  N   PRO A 150     -35.017   9.401  95.201  1.00 18.61           N  
ANISOU  902  N   PRO A 150     2390   2392   2288    -71    -11    334       N  
ATOM    903  CA  PRO A 150     -35.064   9.671  96.649  1.00 18.98           C  
ANISOU  903  CA  PRO A 150     2469   2446   2297    -82    -17    336       C  
ATOM    904  C   PRO A 150     -36.375   9.259  97.304  1.00 24.72           C  
ANISOU  904  C   PRO A 150     3213   3181   3000    -89     12    337       C  
ATOM    905  O   PRO A 150     -37.455   9.610  96.816  1.00 25.05           O  
ANISOU  905  O   PRO A 150     3244   3226   3046    -85     40    323       O  
ATOM    906  CB  PRO A 150     -34.822  11.175  96.735  1.00 20.64           C  
ANISOU  906  CB  PRO A 150     2684   2659   2499    -82    -20    315       C  
ATOM    907  CG  PRO A 150     -34.028  11.496  95.526  1.00 24.84           C  
ANISOU  907  CG  PRO A 150     3188   3184   3066    -73    -32    311       C  
ATOM    908  CD  PRO A 150     -34.527  10.573  94.445  1.00 20.36           C  
ANISOU  908  CD  PRO A 150     2597   2613   2525    -64    -16    318       C  
ATOM    909  N   ALA A 151     -36.285   8.467  98.387  1.00 21.78           N  
ANISOU  909  N   ALA A 151     2864   2808   2602    -99      4    355       N  
ATOM    910  CA  ALA A 151     -37.457   8.001  99.118  1.00 21.65           C  
ANISOU  910  CA  ALA A 151     2866   2800   2562   -108     31    359       C  
ATOM    911  C   ALA A 151     -38.020   9.112  99.996  1.00 24.85           C  
ANISOU  911  C   ALA A 151     3295   3216   2932   -114     47    340       C  
ATOM    912  O   ALA A 151     -37.264   9.953 100.488  1.00 24.59           O  
ANISOU  912  O   ALA A 151     3276   3184   2883   -116     27    332       O  
ATOM    913  CB  ALA A 151     -37.093   6.797  99.969  1.00 22.68           C  
ANISOU  913  CB  ALA A 151     3016   2926   2676   -118     17    387       C  
ATOM    914  N   TYR A 152     -39.343   9.124 100.198  1.00 21.04           N  
ANISOU  914  N   TYR A 152     2815   2741   2438   -116     84    332       N  
ATOM    915  CA  TYR A 152     -39.971  10.140 101.043  1.00 21.41           C  
ANISOU  915  CA  TYR A 152     2885   2798   2452   -120    105    313       C  
ATOM    916  C   TYR A 152     -40.049   9.700 102.511  1.00 27.82           C  
ANISOU  916  C   TYR A 152     3736   3617   3219   -136    107    326       C  
ATOM    917  O   TYR A 152     -40.106  10.550 103.399  1.00 27.38           O  
ANISOU  917  O   TYR A 152     3708   3568   3129   -141    112    311       O  
ATOM    918  CB  TYR A 152     -41.369  10.534 100.505  1.00 21.49           C  
ANISOU  918  CB  TYR A 152     2876   2815   2476   -113    146    296       C  
ATOM    919  CG  TYR A 152     -42.275   9.353 100.219  1.00 21.69           C  
ANISOU  919  CG  TYR A 152     2886   2842   2514   -117    168    310       C  
ATOM    920  CD1 TYR A 152     -42.998   8.741 101.239  1.00 23.15           C  
ANISOU  920  CD1 TYR A 152     3093   3034   2670   -131    190    320       C  
ATOM    921  CD2 TYR A 152     -42.486   8.910  98.917  1.00 21.80           C  
ANISOU  921  CD2 TYR A 152     2865   2850   2568   -109    168    312       C  
ATOM    922  CE1 TYR A 152     -43.849   7.671 100.980  1.00 23.00           C  
ANISOU  922  CE1 TYR A 152     3059   3015   2664   -137    210    333       C  
ATOM    923  CE2 TYR A 152     -43.336   7.841  98.645  1.00 22.36           C  
ANISOU  923  CE2 TYR A 152     2923   2922   2652   -115    187    323       C  
ATOM    924  CZ  TYR A 152     -44.022   7.228  99.679  1.00 29.96           C  
ANISOU  924  CZ  TYR A 152     3905   3891   3588   -130    208    334       C  
ATOM    925  OH  TYR A 152     -44.868   6.178  99.415  1.00 32.60           O  
ANISOU  925  OH  TYR A 152     4226   4225   3936   -138    227    346       O  
ATOM    926  N   GLU A 153     -40.032   8.362 102.770  1.00 25.93           N  
ANISOU  926  N   GLU A 153     3501   3374   2977   -144    103    353       N  
ATOM    927  CA  GLU A 153     -40.140   7.830 104.140  1.00 27.29           C  
ANISOU  927  CA  GLU A 153     3712   3553   3104   -160    105    369       C  
ATOM    928  C   GLU A 153     -39.019   8.356 105.040  1.00 33.30           C  
ANISOU  928  C   GLU A 153     4504   4315   3834   -166     69    370       C  
ATOM    929  O   GLU A 153     -39.288   8.819 106.154  1.00 33.45           O  
ANISOU  929  O   GLU A 153     4558   4343   3807   -177     79    363       O  
ATOM    930  CB  GLU A 153     -40.146   6.285 104.137  1.00 28.80           C  
ANISOU  930  CB  GLU A 153     3902   3736   3305   -167    100    401       C  
ATOM    931  CG  GLU A 153     -41.358   5.671 103.444  1.00 36.85           C  
ANISOU  931  CG  GLU A 153     4896   4755   4349   -167    137    400       C  
ATOM    932  CD  GLU A 153     -41.156   5.333 101.977  1.00 47.82           C  
ANISOU  932  CD  GLU A 153     6245   6133   5790   -154    128    398       C  
ATOM    933  OE1 GLU A 153     -40.301   5.977 101.326  1.00 47.81           O  
ANISOU  933  OE1 GLU A 153     6230   6128   5809   -142    104    388       O  
ATOM    934  OE2 GLU A 153     -41.850   4.415 101.481  1.00 28.46           O  
ANISOU  934  OE2 GLU A 153     3778   3677   3359   -157    146    407       O  
ATOM    935  N   ILE A 154     -37.764   8.305 104.554  1.00 30.35           N  
ANISOU  935  N   ILE A 154     4117   3933   3483   -160     28    378       N  
ATOM    936  CA  ILE A 154     -36.608   8.773 105.330  1.00 30.47           C  
ANISOU  936  CA  ILE A 154     4155   3949   3473   -167    -11    381       C  
ATOM    937  C   ILE A 154     -35.799   9.823 104.557  1.00 35.65           C  
ANISOU  937  C   ILE A 154     4789   4600   4156   -157    -32    361       C  
ATOM    938  O   ILE A 154     -35.891   9.895 103.331  1.00 35.19           O  
ANISOU  938  O   ILE A 154     4695   4535   4140   -144    -24    354       O  
ATOM    939  CB  ILE A 154     -35.713   7.577 105.797  1.00 33.46           C  
ANISOU  939  CB  ILE A 154     4544   4321   3847   -172    -48    417       C  
ATOM    940  CG1 ILE A 154     -35.253   6.712 104.589  1.00 33.60           C  
ANISOU  940  CG1 ILE A 154     4522   4325   3918   -159    -60    431       C  
ATOM    941  CG2 ILE A 154     -36.436   6.727 106.863  1.00 34.50           C  
ANISOU  941  CG2 ILE A 154     4710   4460   3940   -186    -30    436       C  
ATOM    942  CD1 ILE A 154     -34.198   5.612 104.944  1.00 41.77           C  
ANISOU  942  CD1 ILE A 154     5562   5351   4958   -159   -100    466       C  
ATOM    943  N   VAL A 155     -35.000  10.635 105.279  1.00 33.25           N  
ANISOU  943  N   VAL A 155     4508   4300   3827   -165    -60    353       N  
ATOM    944  CA  VAL A 155     -34.134  11.640 104.656  1.00 33.28           C  
ANISOU  944  CA  VAL A 155     4493   4298   3853   -159    -82    336       C  
ATOM    945  C   VAL A 155     -32.772  11.012 104.316  1.00 35.97           C  
ANISOU  945  C   VAL A 155     4814   4632   4221   -157   -127    359       C  
ATOM    946  O   VAL A 155     -31.911  10.891 105.193  1.00 35.99           O  
ANISOU  946  O   VAL A 155     4837   4637   4200   -167   -163    372       O  
ATOM    947  CB  VAL A 155     -33.969  12.902 105.563  1.00 37.99           C  
ANISOU  947  CB  VAL A 155     5123   4900   4413   -171    -89    312       C  
ATOM    948  CG1 VAL A 155     -33.238  14.018 104.817  1.00 37.78           C  
ANISOU  948  CG1 VAL A 155     5076   4866   4414   -165   -105    293       C  
ATOM    949  CG2 VAL A 155     -35.317  13.388 106.075  1.00 38.05           C  
ANISOU  949  CG2 VAL A 155     5153   4914   4389   -173    -42    292       C  
ATOM    950  N   GLU A 156     -32.604  10.555 103.065  1.00 31.58           N  
ANISOU  950  N   GLU A 156     4218   4066   3713   -142   -124    365       N  
ATOM    951  CA  GLU A 156     -31.365   9.901 102.632  1.00 31.41           C  
ANISOU  951  CA  GLU A 156     4174   4037   3723   -137   -161    386       C  
ATOM    952  C   GLU A 156     -30.232  10.913 102.484  1.00 35.68           C  
ANISOU  952  C   GLU A 156     4705   4577   4274   -139   -192    374       C  
ATOM    953  O   GLU A 156     -30.395  11.922 101.795  1.00 34.85           O  
ANISOU  953  O   GLU A 156     4586   4470   4185   -135   -178    351       O  
ATOM    954  CB  GLU A 156     -31.584   9.146 101.310  1.00 32.46           C  
ANISOU  954  CB  GLU A 156     4271   4161   3903   -122   -144    392       C  
ATOM    955  CG  GLU A 156     -32.573   7.995 101.421  1.00 43.45           C  
ANISOU  955  CG  GLU A 156     5669   5551   5288   -122   -119    407       C  
ATOM    956  CD  GLU A 156     -33.047   7.445 100.089  1.00 61.75           C  
ANISOU  956  CD  GLU A 156     7955   7861   7647   -109    -95    405       C  
ATOM    957  OE1 GLU A 156     -33.452   8.254  99.224  1.00 51.64           O  
ANISOU  957  OE1 GLU A 156     6658   6582   6383   -103    -75    382       O  
ATOM    958  OE2 GLU A 156     -33.105   6.202  99.947  1.00 58.69           O  
ANISOU  958  OE2 GLU A 156     7561   7464   7273   -106    -95    425       O  
ATOM    959  N   ALA A 157     -29.081  10.657 103.152  1.00 33.28           N  
ANISOU  959  N   ALA A 157     4407   4274   3963   -146   -236    392       N  
ATOM    960  CA  ALA A 157     -27.906  11.534 103.054  1.00 33.28           C  
ANISOU  960  CA  ALA A 157     4395   4274   3976   -151   -270    384       C  
ATOM    961  C   ALA A 157     -27.365  11.531 101.633  1.00 37.24           C  
ANISOU  961  C   ALA A 157     4851   4766   4534   -136   -268    382       C  
ATOM    962  O   ALA A 157     -27.070  12.591 101.082  1.00 37.83           O  
ANISOU  962  O   ALA A 157     4912   4838   4623   -137   -267    362       O  
ATOM    963  CB  ALA A 157     -26.827  11.077 104.027  1.00 34.33           C  
ANISOU  963  CB  ALA A 157     4540   4411   4094   -160   -319    407       C  
ATOM    964  N   ASN A 158     -27.297  10.342 101.012  1.00 32.59           N  
ANISOU  964  N   ASN A 158     4239   4170   3973   -123   -264    403       N  
ATOM    965  CA  ASN A 158     -26.886  10.202  99.623  1.00 31.62           C  
ANISOU  965  CA  ASN A 158     4074   4038   3901   -108   -256    401       C  
ATOM    966  C   ASN A 158     -27.755   9.146  98.940  1.00 34.04           C  
ANISOU  966  C   ASN A 158     4373   4339   4224    -96   -225    409       C  
ATOM    967  O   ASN A 158     -27.508   7.946  99.096  1.00 34.11           O  
ANISOU  967  O   ASN A 158     4378   4341   4240    -91   -235    433       O  
ATOM    968  CB  ASN A 158     -25.396   9.822  99.532  1.00 33.04           C  
ANISOU  968  CB  ASN A 158     4229   4214   4110   -105   -297    420       C  
ATOM    969  CG  ASN A 158     -24.839   9.875  98.124  1.00 50.19           C  
ANISOU  969  CG  ASN A 158     6359   6378   6333    -91   -288    415       C  
ATOM    970  OD1 ASN A 158     -25.287  10.664  97.275  1.00 40.07           O  
ANISOU  970  OD1 ASN A 158     5068   5096   5061    -89   -262    394       O  
ATOM    971  ND2 ASN A 158     -23.789   9.104  97.874  1.00 40.41           N  
ANISOU  971  ND2 ASN A 158     5094   5133   5126    -82   -312    435       N  
ATOM    972  N   PRO A 159     -28.886   9.565  98.300  1.00 28.84           N  
ANISOU  972  N   PRO A 159     3713   3681   3564    -93   -186    389       N  
ATOM    973  CA  PRO A 159     -29.797   8.569  97.701  1.00 27.72           C  
ANISOU  973  CA  PRO A 159     3564   3534   3435    -84   -157    395       C  
ATOM    974  C   PRO A 159     -29.085   7.656  96.708  1.00 28.95           C  
ANISOU  974  C   PRO A 159     3688   3679   3634    -71   -164    408       C  
ATOM    975  O   PRO A 159     -28.343   8.128  95.848  1.00 28.84           O  
ANISOU  975  O   PRO A 159     3648   3661   3648    -65   -171    401       O  
ATOM    976  CB  PRO A 159     -30.867   9.430  97.017  1.00 29.44           C  
ANISOU  976  CB  PRO A 159     3778   3756   3653    -82   -122    370       C  
ATOM    977  CG  PRO A 159     -30.788  10.748  97.697  1.00 34.17           C  
ANISOU  977  CG  PRO A 159     4396   4363   4226    -92   -129    353       C  
ATOM    978  CD  PRO A 159     -29.364  10.943  98.076  1.00 30.03           C  
ANISOU  978  CD  PRO A 159     3868   3837   3707    -96   -169    362       C  
ATOM    979  N   PRO A 160     -29.216   6.324  96.871  1.00 23.54           N  
ANISOU  979  N   PRO A 160     3006   2985   2953    -68   -164    429       N  
ATOM    980  CA  PRO A 160     -28.480   5.415  95.988  1.00 22.34           C  
ANISOU  980  CA  PRO A 160     2826   2819   2842    -54   -171    442       C  
ATOM    981  C   PRO A 160     -29.083   5.333  94.598  1.00 23.21           C  
ANISOU  981  C   PRO A 160     2915   2924   2978    -45   -140    426       C  
ATOM    982  O   PRO A 160     -30.285   5.552  94.429  1.00 22.14           O  
ANISOU  982  O   PRO A 160     2789   2795   2829    -50   -112    413       O  
ATOM    983  CB  PRO A 160     -28.562   4.076  96.717  1.00 24.70           C  
ANISOU  983  CB  PRO A 160     3142   3110   3134    -54   -180    468       C  
ATOM    984  CG  PRO A 160     -29.831   4.141  97.479  1.00 29.45           C  
ANISOU  984  CG  PRO A 160     3774   3720   3697    -67   -159    465       C  
ATOM    985  CD  PRO A 160     -30.011   5.585  97.879  1.00 25.15           C  
ANISOU  985  CD  PRO A 160     3240   3191   3125    -76   -157    443       C  
ATOM    986  N   TYR A 161     -28.253   4.998  93.595  1.00 18.11           N  
ANISOU  986  N   TYR A 161     2241   2269   2371    -33   -144    428       N  
ATOM    987  CA  TYR A 161     -28.729   4.761  92.236  1.00 16.39           C  
ANISOU  987  CA  TYR A 161     2005   2046   2178    -24   -117    415       C  
ATOM    988  C   TYR A 161     -29.559   3.488  92.207  1.00 20.05           C  
ANISOU  988  C   TYR A 161     2477   2500   2641    -24   -100    424       C  
ATOM    989  O   TYR A 161     -29.162   2.480  92.801  1.00 20.14           O  
ANISOU  989  O   TYR A 161     2496   2500   2656    -22   -115    445       O  
ATOM    990  CB  TYR A 161     -27.539   4.637  91.260  1.00 16.17           C  
ANISOU  990  CB  TYR A 161     1946   2010   2189    -12   -125    415       C  
ATOM    991  CG  TYR A 161     -26.993   5.963  90.765  1.00 15.32           C  
ANISOU  991  CG  TYR A 161     1823   1910   2087    -13   -128    400       C  
ATOM    992  CD1 TYR A 161     -26.499   6.911  91.658  1.00 17.14           C  
ANISOU  992  CD1 TYR A 161     2062   2150   2300    -22   -150    400       C  
ATOM    993  CD2 TYR A 161     -26.794   6.190  89.406  1.00 15.58           C  
ANISOU  993  CD2 TYR A 161     1834   1941   2146     -5   -111    387       C  
ATOM    994  CE1 TYR A 161     -25.907   8.092  91.209  1.00 16.90           C  
ANISOU  994  CE1 TYR A 161     2018   2125   2279    -25   -154    387       C  
ATOM    995  CE2 TYR A 161     -26.182   7.355  88.947  1.00 16.26           C  
ANISOU  995  CE2 TYR A 161     1906   2033   2240     -7   -114    376       C  
ATOM    996  CZ  TYR A 161     -25.750   8.309  89.852  1.00 20.56           C  
ANISOU  996  CZ  TYR A 161     2459   2585   2769    -17   -136    376       C  
ATOM    997  OH  TYR A 161     -25.156   9.463  89.403  1.00 17.16           O  
ANISOU  997  OH  TYR A 161     2015   2158   2347    -20   -138    365       O  
ATOM    998  N   LYS A 162     -30.732   3.541  91.582  1.00 15.79           N  
ANISOU  998  N   LYS A 162     1938   1963   2097    -27    -72    409       N  
ATOM    999  CA  LYS A 162     -31.600   2.374  91.498  1.00 15.76           C  
ANISOU  999  CA  LYS A 162     1943   1950   2095    -30    -55    416       C  
ATOM   1000  C   LYS A 162     -31.744   1.914  90.070  1.00 17.44           C  
ANISOU 1000  C   LYS A 162     2135   2153   2336    -22    -37    405       C  
ATOM   1001  O   LYS A 162     -31.717   2.733  89.154  1.00 16.23           O  
ANISOU 1001  O   LYS A 162     1967   2007   2191    -18    -29    387       O  
ATOM   1002  CB  LYS A 162     -32.983   2.670  92.114  1.00 18.87           C  
ANISOU 1002  CB  LYS A 162     2356   2356   2457    -43    -36    410       C  
ATOM   1003  CG  LYS A 162     -32.943   2.906  93.625  1.00 32.08           C  
ANISOU 1003  CG  LYS A 162     4055   4036   4097    -53    -49    423       C  
ATOM   1004  CD  LYS A 162     -34.337   3.134  94.192  1.00 39.81           C  
ANISOU 1004  CD  LYS A 162     5052   5027   5047    -65    -25    416       C  
ATOM   1005  N   SER A 163     -31.872   0.592  89.866  1.00 13.72           N  
ANISOU 1005  N   SER A 163     1666   1665   1880    -20    -32    415       N  
ATOM   1006  CA  SER A 163     -32.069   0.021  88.535  1.00 12.68           C  
ANISOU 1006  CA  SER A 163     1519   1523   1774    -14    -15    403       C  
ATOM   1007  C   SER A 163     -33.409   0.450  87.975  1.00 14.87           C  
ANISOU 1007  C   SER A 163     1797   1813   2039    -23      8    385       C  
ATOM   1008  O   SER A 163     -34.326   0.751  88.742  1.00 12.79           O  
ANISOU 1008  O   SER A 163     1547   1561   1752    -34     15    386       O  
ATOM   1009  CB  SER A 163     -31.997  -1.502  88.593  1.00 15.01           C  
ANISOU 1009  CB  SER A 163     1821   1796   2086    -12    -15    418       C  
ATOM   1010  OG  SER A 163     -33.003  -2.027  89.443  1.00 16.61           O  
ANISOU 1010  OG  SER A 163     2045   1999   2269    -26     -8    428       O  
ATOM   1011  N   LEU A 164     -33.545   0.459  86.636  1.00 11.47           N  
ANISOU 1011  N   LEU A 164     1352   1381   1627    -18     22    368       N  
ATOM   1012  CA  LEU A 164     -34.806   0.824  85.997  1.00 10.77           C  
ANISOU 1012  CA  LEU A 164     1260   1303   1528    -26     41    352       C  
ATOM   1013  C   LEU A 164     -35.899  -0.175  86.322  1.00 14.36           C  
ANISOU 1013  C   LEU A 164     1725   1752   1978    -39     53    357       C  
ATOM   1014  O   LEU A 164     -37.069   0.195  86.369  1.00 14.23           O  
ANISOU 1014  O   LEU A 164     1711   1749   1948    -49     66    349       O  
ATOM   1015  CB  LEU A 164     -34.633   0.963  84.474  1.00 10.57           C  
ANISOU 1015  CB  LEU A 164     1219   1277   1522    -19     49    335       C  
ATOM   1016  CG  LEU A 164     -33.910   2.237  84.005  1.00 14.29           C  
ANISOU 1016  CG  LEU A 164     1678   1759   1993    -11     44    326       C  
ATOM   1017  CD1 LEU A 164     -33.746   2.242  82.505  1.00 14.23           C  
ANISOU 1017  CD1 LEU A 164     1658   1749   2000     -5     54    312       C  
ATOM   1018  CD2 LEU A 164     -34.656   3.496  84.462  1.00 15.00           C  
ANISOU 1018  CD2 LEU A 164     1772   1868   2060    -17     46    320       C  
ATOM   1019  N   LYS A 165     -35.516  -1.436  86.630  1.00 10.39           N  
ANISOU 1019  N   LYS A 165     1231   1229   1488    -39     48    372       N  
ATOM   1020  CA  LYS A 165     -36.472  -2.447  87.072  1.00  9.35           C  
ANISOU 1020  CA  LYS A 165     1112   1089   1352    -53     59    380       C  
ATOM   1021  C   LYS A 165     -37.093  -2.030  88.415  1.00 13.42           C  
ANISOU 1021  C   LYS A 165     1643   1618   1839    -64     59    391       C  
ATOM   1022  O   LYS A 165     -38.308  -1.980  88.533  1.00 13.07           O  
ANISOU 1022  O   LYS A 165     1600   1583   1782    -77     76    386       O  
ATOM   1023  CB  LYS A 165     -35.795  -3.817  87.197  1.00 11.20           C  
ANISOU 1023  CB  LYS A 165     1355   1296   1607    -48     52    396       C  
ATOM   1024  CG  LYS A 165     -36.743  -4.920  87.669  1.00 11.13           C  
ANISOU 1024  CG  LYS A 165     1361   1274   1594    -64     62    406       C  
ATOM   1025  CD  LYS A 165     -35.991  -6.156  88.108  1.00 13.20           C  
ANISOU 1025  CD  LYS A 165     1636   1508   1873    -59     52    428       C  
ATOM   1026  CE  LYS A 165     -36.931  -7.269  88.539  1.00 23.10           C  
ANISOU 1026  CE  LYS A 165     2906   2747   3125    -77     64    439       C  
ATOM   1027  NZ  LYS A 165     -37.753  -6.877  89.723  1.00 28.30           N  
ANISOU 1027  NZ  LYS A 165     3577   3422   3752    -92     68    451       N  
ATOM   1028  N   ASP A 166     -36.241  -1.682  89.414  1.00 10.84           N  
ANISOU 1028  N   ASP A 166     1326   1293   1499    -58     41    406       N  
ATOM   1029  CA  ASP A 166     -36.712  -1.234  90.733  1.00 11.70           C  
ANISOU 1029  CA  ASP A 166     1453   1415   1577    -69     41    415       C  
ATOM   1030  C   ASP A 166     -37.447   0.097  90.639  1.00 16.88           C  
ANISOU 1030  C   ASP A 166     2103   2095   2216    -71     53    396       C  
ATOM   1031  O   ASP A 166     -38.455   0.290  91.320  1.00 17.44           O  
ANISOU 1031  O   ASP A 166     2184   2177   2266    -83     68    396       O  
ATOM   1032  CB  ASP A 166     -35.544  -1.132  91.724  1.00 13.54           C  
ANISOU 1032  CB  ASP A 166     1698   1645   1801    -62     15    433       C  
ATOM   1033  CG  ASP A 166     -34.988  -2.478  92.162  1.00 22.51           C  
ANISOU 1033  CG  ASP A 166     2846   2759   2949    -61      3    458       C  
ATOM   1034  OD1 ASP A 166     -35.583  -3.522  91.783  1.00 22.26           O  
ANISOU 1034  OD1 ASP A 166     2816   2712   2930    -67     17    461       O  
ATOM   1035  OD2 ASP A 166     -34.001  -2.490  92.925  1.00 27.24           O  
ANISOU 1035  OD2 ASP A 166     3453   3354   3543    -55    -21    475       O  
ATOM   1036  N   ILE A 167     -36.961   1.013  89.770  1.00 13.40           N  
ANISOU 1036  N   ILE A 167     1645   1660   1786    -60     49    380       N  
ATOM   1037  CA  ILE A 167     -37.617   2.309  89.544  1.00 12.70           C  
ANISOU 1037  CA  ILE A 167     1550   1590   1685    -60     59    362       C  
ATOM   1038  C   ILE A 167     -39.031   2.120  88.937  1.00 15.42           C  
ANISOU 1038  C   ILE A 167     1885   1941   2032    -68     82    351       C  
ATOM   1039  O   ILE A 167     -39.995   2.703  89.437  1.00 15.57           O  
ANISOU 1039  O   ILE A 167     1907   1974   2034    -74     96    345       O  
ATOM   1040  CB  ILE A 167     -36.714   3.254  88.673  1.00 15.47           C  
ANISOU 1040  CB  ILE A 167     1886   1944   2050    -47     49    350       C  
ATOM   1041  CG1 ILE A 167     -35.468   3.726  89.475  1.00 15.61           C  
ANISOU 1041  CG1 ILE A 167     1911   1960   2060    -43     25    359       C  
ATOM   1042  CG2 ILE A 167     -37.511   4.448  88.149  1.00 15.95           C  
ANISOU 1042  CG2 ILE A 167     1937   2020   2103    -46     62    331       C  
ATOM   1043  CD1 ILE A 167     -34.462   4.630  88.653  1.00 20.19           C  
ANISOU 1043  CD1 ILE A 167     2475   2541   2656    -32     15    349       C  
ATOM   1044  N   TYR A 168     -39.155   1.257  87.900  1.00 10.53           N  
ANISOU 1044  N   TYR A 168     1255   1312   1435    -68     87    347       N  
ATOM   1045  CA  TYR A 168     -40.456   0.998  87.262  1.00  9.86           C  
ANISOU 1045  CA  TYR A 168     1160   1232   1355    -77    105    337       C  
ATOM   1046  C   TYR A 168     -41.391   0.182  88.151  1.00 14.62           C  
ANISOU 1046  C   TYR A 168     1773   1833   1947    -94    118    348       C  
ATOM   1047  O   TYR A 168     -42.593   0.448  88.173  1.00 13.87           O  
ANISOU 1047  O   TYR A 168     1671   1752   1847   -102    134    341       O  
ATOM   1048  CB  TYR A 168     -40.283   0.342  85.884  1.00  9.94           C  
ANISOU 1048  CB  TYR A 168     1157   1231   1388    -75    104    328       C  
ATOM   1049  CG  TYR A 168     -40.260   1.344  84.750  1.00 10.79           C  
ANISOU 1049  CG  TYR A 168     1249   1350   1501    -65    104    310       C  
ATOM   1050  CD1 TYR A 168     -39.145   2.148  84.523  1.00 12.27           C  
ANISOU 1050  CD1 TYR A 168     1434   1538   1690    -52     92    308       C  
ATOM   1051  CD2 TYR A 168     -41.363   1.510  83.918  1.00 11.50           C  
ANISOU 1051  CD2 TYR A 168     1327   1451   1594    -71    114    297       C  
ATOM   1052  CE1 TYR A 168     -39.132   3.102  83.502  1.00 10.91           C  
ANISOU 1052  CE1 TYR A 168     1249   1375   1520    -44     92    294       C  
ATOM   1053  CE2 TYR A 168     -41.356   2.448  82.883  1.00 12.21           C  
ANISOU 1053  CE2 TYR A 168     1404   1551   1686    -62    112    284       C  
ATOM   1054  CZ  TYR A 168     -40.239   3.246  82.683  1.00 16.26           C  
ANISOU 1054  CZ  TYR A 168     1917   2063   2199    -49    102    283       C  
ATOM   1055  OH  TYR A 168     -40.236   4.186  81.684  1.00 14.89           O  
ANISOU 1055  OH  TYR A 168     1732   1898   2026    -41    101    271       O  
ATOM   1056  N   ASP A 169     -40.835  -0.776  88.944  1.00 12.29           N  
ANISOU 1056  N   ASP A 169     1496   1522   1651    -98    110    367       N  
ATOM   1057  CA  ASP A 169     -41.645  -1.547  89.901  1.00 13.10           C  
ANISOU 1057  CA  ASP A 169     1612   1622   1741   -114    123    382       C  
ATOM   1058  C   ASP A 169     -42.213  -0.630  90.973  1.00 19.48           C  
ANISOU 1058  C   ASP A 169     2430   2451   2522   -119    133    382       C  
ATOM   1059  O   ASP A 169     -43.315  -0.869  91.469  1.00 20.54           O  
ANISOU 1059  O   ASP A 169     2566   2592   2645   -133    153    384       O  
ATOM   1060  CB  ASP A 169     -40.819  -2.680  90.540  1.00 14.86           C  
ANISOU 1060  CB  ASP A 169     1855   1823   1968   -115    110    405       C  
ATOM   1061  CG  ASP A 169     -40.495  -3.825  89.586  1.00 25.53           C  
ANISOU 1061  CG  ASP A 169     3201   3151   3350   -114    107    405       C  
ATOM   1062  OD1 ASP A 169     -40.964  -3.780  88.412  1.00 27.20           O  
ANISOU 1062  OD1 ASP A 169     3394   3364   3575   -114    115    386       O  
ATOM   1063  OD2 ASP A 169     -39.777  -4.768  90.008  1.00 23.88           O  
ANISOU 1063  OD2 ASP A 169     3005   2920   3147   -112     96    423       O  
ATOM   1064  N   GLU A 170     -41.475   0.450  91.311  1.00 15.90           N  
ANISOU 1064  N   GLU A 170     1981   2006   2055   -107    120    378       N  
ATOM   1065  CA  GLU A 170     -41.941   1.440  92.273  1.00 15.60           C  
ANISOU 1065  CA  GLU A 170     1953   1986   1990   -109    130    374       C  
ATOM   1066  C   GLU A 170     -43.043   2.303  91.663  1.00 18.61           C  
ANISOU 1066  C   GLU A 170     2313   2383   2373   -108    149    354       C  
ATOM   1067  O   GLU A 170     -44.000   2.653  92.357  1.00 18.25           O  
ANISOU 1067  O   GLU A 170     2272   2350   2311   -115    169    351       O  
ATOM   1068  CB  GLU A 170     -40.778   2.313  92.757  1.00 16.76           C  
ANISOU 1068  CB  GLU A 170     2110   2135   2123    -99    109    375       C  
ATOM   1069  CG  GLU A 170     -41.169   3.282  93.860  1.00 23.29           C  
ANISOU 1069  CG  GLU A 170     2953   2977   2918   -102    118    371       C  
ATOM   1070  CD  GLU A 170     -40.026   4.106  94.415  1.00 23.03           C  
ANISOU 1070  CD  GLU A 170     2934   2945   2871    -95     94    371       C  
ATOM   1071  OE1 GLU A 170     -38.854   3.726  94.194  1.00 20.51           O  
ANISOU 1071  OE1 GLU A 170     2613   2615   2565    -89     70    381       O  
ATOM   1072  OE2 GLU A 170     -40.304   5.084  95.142  1.00 13.36           O  
ANISOU 1072  OE2 GLU A 170     1722   1733   1622    -97    101    361       O  
ATOM   1073  N   TYR A 171     -42.928   2.630  90.340  1.00 13.75           N  
ANISOU 1073  N   TYR A 171     1676   1767   1780    -98    144    340       N  
ATOM   1074  CA  TYR A 171     -43.940   3.442  89.650  1.00 12.41           C  
ANISOU 1074  CA  TYR A 171     1487   1613   1616    -95    158    322       C  
ATOM   1075  C   TYR A 171     -45.341   2.853  89.837  1.00 16.33           C  
ANISOU 1075  C   TYR A 171     1975   2116   2114   -110    181    323       C  
ATOM   1076  O   TYR A 171     -46.204   3.504  90.421  1.00 15.71           O  
ANISOU 1076  O   TYR A 171     1895   2053   2023   -112    199    318       O  
ATOM   1077  CB  TYR A 171     -43.613   3.579  88.144  1.00 12.03           C  
ANISOU 1077  CB  TYR A 171     1419   1561   1591    -86    148    311       C  
ATOM   1078  CG  TYR A 171     -42.390   4.428  87.838  1.00 12.42           C  
ANISOU 1078  CG  TYR A 171     1470   1607   1641    -71    130    307       C  
ATOM   1079  CD1 TYR A 171     -41.956   5.407  88.730  1.00 14.27           C  
ANISOU 1079  CD1 TYR A 171     1718   1847   1857    -66    126    307       C  
ATOM   1080  CD2 TYR A 171     -41.768   4.362  86.597  1.00 13.26           C  
ANISOU 1080  CD2 TYR A 171     1565   1707   1766    -63    119    301       C  
ATOM   1081  CE1 TYR A 171     -40.874   6.232  88.429  1.00 14.79           C  
ANISOU 1081  CE1 TYR A 171     1783   1910   1926    -55    110    303       C  
ATOM   1082  CE2 TYR A 171     -40.682   5.178  86.286  1.00 14.76           C  
ANISOU 1082  CE2 TYR A 171     1755   1895   1958    -51    106    298       C  
ATOM   1083  CZ  TYR A 171     -40.252   6.128  87.197  1.00 22.73           C  
ANISOU 1083  CZ  TYR A 171     2776   2909   2952    -47    100    299       C  
ATOM   1084  OH  TYR A 171     -39.181   6.931  86.896  1.00 22.74           O  
ANISOU 1084  OH  TYR A 171     2776   2908   2957    -38     86    296       O  
ATOM   1085  N   PHE A 172     -45.544   1.579  89.393  1.00 12.22           N  
ANISOU 1085  N   PHE A 172     1450   1583   1608   -121    182    330       N  
ATOM   1086  CA  PHE A 172     -46.850   0.901  89.470  1.00 12.33           C  
ANISOU 1086  CA  PHE A 172     1455   1602   1627   -139    202    332       C  
ATOM   1087  C   PHE A 172     -47.335   0.780  90.920  1.00 17.25           C  
ANISOU 1087  C   PHE A 172     2096   2232   2228   -150    220    344       C  
ATOM   1088  O   PHE A 172     -48.508   1.020  91.200  1.00 17.18           O  
ANISOU 1088  O   PHE A 172     2075   2237   2216   -158    242    340       O  
ATOM   1089  CB  PHE A 172     -46.774  -0.498  88.817  1.00 14.18           C  
ANISOU 1089  CB  PHE A 172     1689   1819   1882   -150    197    338       C  
ATOM   1090  CG  PHE A 172     -46.216  -0.507  87.411  1.00 15.08           C  
ANISOU 1090  CG  PHE A 172     1790   1925   2015   -140    180    326       C  
ATOM   1091  CD1 PHE A 172     -46.962  -0.020  86.348  1.00 18.26           C  
ANISOU 1091  CD1 PHE A 172     2168   2340   2429   -139    183    309       C  
ATOM   1092  CD2 PHE A 172     -44.997  -1.114  87.134  1.00 16.62           C  
ANISOU 1092  CD2 PHE A 172     1997   2100   2218   -133    164    332       C  
ATOM   1093  CE1 PHE A 172     -46.459  -0.055  85.044  1.00 18.79           C  
ANISOU 1093  CE1 PHE A 172     2228   2402   2511   -131    169    298       C  
ATOM   1094  CE2 PHE A 172     -44.494  -1.148  85.829  1.00 19.16           C  
ANISOU 1094  CE2 PHE A 172     2308   2415   2557   -125    153    320       C  
ATOM   1095  CZ  PHE A 172     -45.229  -0.620  84.794  1.00 17.13           C  
ANISOU 1095  CZ  PHE A 172     2031   2172   2306   -124    156    303       C  
ATOM   1096  N   ARG A 173     -46.425   0.405  91.836  1.00 14.68           N  
ANISOU 1096  N   ARG A 173     1797   1894   1886   -151    210    360       N  
ATOM   1097  CA  ARG A 173     -46.724   0.256  93.264  1.00 14.82           C  
ANISOU 1097  CA  ARG A 173     1837   1917   1877   -162    224    374       C  
ATOM   1098  C   ARG A 173     -47.212   1.587  93.876  1.00 17.44           C  
ANISOU 1098  C   ARG A 173     2169   2269   2187   -156    240    362       C  
ATOM   1099  O   ARG A 173     -48.212   1.604  94.599  1.00 16.65           O  
ANISOU 1099  O   ARG A 173     2072   2181   2075   -167    266    363       O  
ATOM   1100  CB  ARG A 173     -45.475  -0.276  94.008  1.00 15.05           C  
ANISOU 1100  CB  ARG A 173     1896   1930   1893   -161    203    394       C  
ATOM   1101  CG  ARG A 173     -45.539  -0.172  95.525  1.00 24.96           C  
ANISOU 1101  CG  ARG A 173     3180   3191   3112   -170    212    407       C  
ATOM   1102  CD  ARG A 173     -44.443  -1.008  96.202  1.00 36.49           C  
ANISOU 1102  CD  ARG A 173     4668   4634   4563   -172    190    432       C  
ATOM   1103  NE  ARG A 173     -43.127  -0.831  95.566  1.00 43.56           N  
ANISOU 1103  NE  ARG A 173     5558   5518   5474   -154    158    430       N  
ATOM   1104  CZ  ARG A 173     -42.585  -1.713  94.724  1.00 55.22           C  
ANISOU 1104  CZ  ARG A 173     7026   6976   6981   -150    145    435       C  
ATOM   1105  NH1 ARG A 173     -43.229  -2.835  94.422  1.00 44.79           N  
ANISOU 1105  NH1 ARG A 173     5701   5642   5674   -163    158    443       N  
ATOM   1106  NH2 ARG A 173     -41.395  -1.483  94.189  1.00 39.01           N  
ANISOU 1106  NH2 ARG A 173     4967   4915   4941   -134    120    433       N  
ATOM   1107  N   GLU A 174     -46.538   2.699  93.540  1.00 13.27           N  
ANISOU 1107  N   GLU A 174     1639   1746   1659   -138    225    349       N  
ATOM   1108  CA  GLU A 174     -46.920   4.026  94.035  1.00 13.05           C  
ANISOU 1108  CA  GLU A 174     1612   1733   1613   -129    238    334       C  
ATOM   1109  C   GLU A 174     -48.222   4.500  93.408  1.00 15.99           C  
ANISOU 1109  C   GLU A 174     1954   2120   2001   -127    260    319       C  
ATOM   1110  O   GLU A 174     -49.060   5.073  94.100  1.00 16.42           O  
ANISOU 1110  O   GLU A 174     2010   2188   2043   -128    285    313       O  
ATOM   1111  CB  GLU A 174     -45.797   5.048  93.778  1.00 14.23           C  
ANISOU 1111  CB  GLU A 174     1767   1880   1760   -112    214    325       C  
ATOM   1112  CG  GLU A 174     -44.597   4.874  94.692  1.00 23.97           C  
ANISOU 1112  CG  GLU A 174     3030   3105   2973   -114    194    339       C  
ATOM   1113  CD  GLU A 174     -44.863   5.249  96.135  1.00 36.54           C  
ANISOU 1113  CD  GLU A 174     4649   4706   4528   -122    208    341       C  
ATOM   1114  OE1 GLU A 174     -45.183   6.433  96.391  1.00 30.46           O  
ANISOU 1114  OE1 GLU A 174     3880   3946   3746   -114    219    324       O  
ATOM   1115  OE2 GLU A 174     -44.771   4.357  97.008  1.00 18.91           O  
ANISOU 1115  OE2 GLU A 174     2438   2469   2278   -135    208    360       O  
ATOM   1116  N   LEU A 175     -48.401   4.260  92.088  1.00 11.02           N  
ANISOU 1116  N   LEU A 175     1299   1488   1401   -124    251    313       N  
ATOM   1117  CA  LEU A 175     -49.612   4.677  91.382  1.00 10.44           C  
ANISOU 1117  CA  LEU A 175     1194   1427   1345   -121    267    300       C  
ATOM   1118  C   LEU A 175     -50.848   3.917  91.886  1.00 16.39           C  
ANISOU 1118  C   LEU A 175     1939   2188   2099   -140    294    306       C  
ATOM   1119  O   LEU A 175     -51.901   4.524  92.084  1.00 15.78           O  
ANISOU 1119  O   LEU A 175     1844   2126   2023   -138    317    298       O  
ATOM   1120  CB  LEU A 175     -49.448   4.500  89.849  1.00  9.50           C  
ANISOU 1120  CB  LEU A 175     1053   1304   1253   -116    248    294       C  
ATOM   1121  CG  LEU A 175     -48.446   5.455  89.165  1.00 13.07           C  
ANISOU 1121  CG  LEU A 175     1507   1752   1707    -96    227    285       C  
ATOM   1122  CD1 LEU A 175     -48.256   5.089  87.689  1.00 12.99           C  
ANISOU 1122  CD1 LEU A 175     1480   1736   1720    -94    210    280       C  
ATOM   1123  CD2 LEU A 175     -48.888   6.902  89.296  1.00 12.42           C  
ANISOU 1123  CD2 LEU A 175     1417   1682   1620    -81    236    272       C  
ATOM   1124  N   ASP A 176     -50.705   2.597  92.141  1.00 14.67           N  
ANISOU 1124  N   ASP A 176     1733   1959   1882   -158    293    322       N  
ATOM   1125  CA  ASP A 176     -51.811   1.776  92.649  1.00 15.46           C  
ANISOU 1125  CA  ASP A 176     1827   2064   1984   -180    319    331       C  
ATOM   1126  C   ASP A 176     -52.246   2.225  94.061  1.00 20.74           C  
ANISOU 1126  C   ASP A 176     2512   2744   2624   -183    346    334       C  
ATOM   1127  O   ASP A 176     -53.442   2.390  94.315  1.00 20.64           O  
ANISOU 1127  O   ASP A 176     2481   2746   2615   -190    375    330       O  
ATOM   1128  CB  ASP A 176     -51.423   0.290  92.656  1.00 17.56           C  
ANISOU 1128  CB  ASP A 176     2107   2310   2255   -198    310    348       C  
ATOM   1129  N   ALA A 177     -51.268   2.451  94.964  1.00 18.14           N  
ANISOU 1129  N   ALA A 177     2217   2408   2266   -179    337    342       N  
ATOM   1130  CA  ALA A 177     -51.550   2.875  96.342  1.00 18.34           C  
ANISOU 1130  CA  ALA A 177     2265   2444   2259   -183    361    344       C  
ATOM   1131  C   ALA A 177     -52.121   4.297  96.389  1.00 21.57           C  
ANISOU 1131  C   ALA A 177     2661   2870   2665   -167    378    323       C  
ATOM   1132  O   ALA A 177     -52.944   4.600  97.253  1.00 21.44           O  
ANISOU 1132  O   ALA A 177     2648   2867   2633   -172    410    320       O  
ATOM   1133  CB  ALA A 177     -50.284   2.790  97.183  1.00 19.06           C  
ANISOU 1133  CB  ALA A 177     2396   2524   2320   -182    340    357       C  
ATOM   1134  N   ALA A 178     -51.674   5.173  95.466  1.00 17.79           N  
ANISOU 1134  N   ALA A 178     2168   2391   2202   -146    357    308       N  
ATOM   1135  CA  ALA A 178     -52.140   6.558  95.418  1.00 17.27           C  
ANISOU 1135  CA  ALA A 178     2090   2336   2136   -128    370    288       C  
ATOM   1136  C   ALA A 178     -53.596   6.651  94.912  1.00 20.70           C  
ANISOU 1136  C   ALA A 178     2485   2785   2596   -128    396    280       C  
ATOM   1137  O   ALA A 178     -54.359   7.481  95.401  1.00 20.23           O  
ANISOU 1137  O   ALA A 178     2418   2737   2531   -120    423    268       O  
ATOM   1138  CB  ALA A 178     -51.226   7.384  94.545  1.00 17.62           C  
ANISOU 1138  CB  ALA A 178     2131   2373   2191   -109    341    278       C  
ATOM   1139  N   ILE A 179     -53.990   5.758  93.962  1.00 17.15           N  
ANISOU 1139  N   ILE A 179     2010   2334   2174   -138    387    286       N  
ATOM   1140  CA  ILE A 179     -55.387   5.684  93.488  1.00 17.31           C  
ANISOU 1140  CA  ILE A 179     1990   2368   2219   -143    408    280       C  
ATOM   1141  C   ILE A 179     -56.305   5.219  94.628  1.00 22.68           C  
ANISOU 1141  C   ILE A 179     2672   3057   2886   -160    446    287       C  
ATOM   1142  O   ILE A 179     -57.408   5.742  94.786  1.00 22.82           O  
ANISOU 1142  O   ILE A 179     2665   3092   2915   -156    475    278       O  
ATOM   1143  CB  ILE A 179     -55.510   4.761  92.230  1.00 20.24           C  
ANISOU 1143  CB  ILE A 179     2336   2733   2619   -153    387    285       C  
ATOM   1144  CG1 ILE A 179     -54.728   5.350  91.028  1.00 20.04           C  
ANISOU 1144  CG1 ILE A 179     2307   2702   2607   -134    354    276       C  
ATOM   1145  CG2 ILE A 179     -57.003   4.516  91.860  1.00 21.30           C  
ANISOU 1145  CG2 ILE A 179     2430   2883   2780   -163    408    282       C  
ATOM   1146  CD1 ILE A 179     -54.593   4.366  89.799  1.00 22.98           C  
ANISOU 1146  CD1 ILE A 179     2665   3065   3001   -144    330    279       C  
ATOM   1147  N   ASN A 180     -55.813   4.290  95.464  1.00 20.10           N  
ANISOU 1147  N   ASN A 180     2377   2721   2537   -179    448    304       N  
ATOM   1148  CA  ASN A 180     -56.574   3.781  96.608  1.00 20.29           C  
ANISOU 1148  CA  ASN A 180     2411   2754   2545   -199    485    314       C  
ATOM   1149  C   ASN A 180     -56.448   4.723  97.828  1.00 24.09           C  
ANISOU 1149  C   ASN A 180     2920   3242   2990   -189    507    307       C  
ATOM   1150  O   ASN A 180     -57.225   4.612  98.781  1.00 23.76           O  
ANISOU 1150  O   ASN A 180     2883   3212   2933   -201    544    310       O  
ATOM   1151  CB  ASN A 180     -56.107   2.363  96.973  1.00 20.91           C  
ANISOU 1151  CB  ASN A 180     2514   2816   2613   -223    477    337       C  
ATOM   1152  CG  ASN A 180     -56.261   1.363  95.841  1.00 41.46           C  
ANISOU 1152  CG  ASN A 180     5094   5410   5251   -235    458    343       C  
ATOM   1153  OD1 ASN A 180     -57.069   1.543  94.913  1.00 30.06           O  
ANISOU 1153  OD1 ASN A 180     3610   3976   3837   -233    460    332       O  
ATOM   1154  ND2 ASN A 180     -55.501   0.282  95.900  1.00 36.62           N  
ANISOU 1154  ND2 ASN A 180     4504   4776   4632   -248    440    360       N  
ATOM   1155  N   GLY A 181     -55.481   5.644  97.769  1.00 19.83           N  
ANISOU 1155  N   GLY A 181     2399   2697   2438   -169    484    297       N  
ATOM   1156  CA  GLY A 181     -55.215   6.587  98.850  1.00 19.48           C  
ANISOU 1156  CA  GLY A 181     2385   2657   2358   -160    499    287       C  
ATOM   1157  C   GLY A 181     -56.268   7.672  98.997  1.00 22.67           C  
ANISOU 1157  C   GLY A 181     2768   3077   2770   -145    533    267       C  
ATOM   1158  O   GLY A 181     -56.579   8.090 100.118  1.00 23.16           O  
ANISOU 1158  O   GLY A 181     2851   3146   2803   -146    564    261       O  
ATOM   1159  N   PHE A 182     -56.820   8.160  97.855  1.00 18.11           N  
ANISOU 1159  N   PHE A 182     2148   2503   2230   -129    527    256       N  
ATOM   1160  CA  PHE A 182     -57.838   9.224  97.869  1.00 17.26           C  
ANISOU 1160  CA  PHE A 182     2013   2408   2135   -111    557    237       C  
ATOM   1161  C   PHE A 182     -59.032   8.860  98.761  1.00 22.21           C  
ANISOU 1161  C   PHE A 182     2630   3050   2757   -125    606    239       C  
ATOM   1162  O   PHE A 182     -59.479   7.705  98.762  1.00 21.33           O  
ANISOU 1162  O   PHE A 182     2508   2942   2653   -149    614    255       O  
ATOM   1163  CB  PHE A 182     -58.322   9.544  96.441  1.00 18.14           C  
ANISOU 1163  CB  PHE A 182     2078   2522   2291    -96    541    230       C  
ATOM   1164  CG  PHE A 182     -57.300  10.228  95.566  1.00 18.30           C  
ANISOU 1164  CG  PHE A 182     2105   2530   2318    -77    501    224       C  
ATOM   1165  CD1 PHE A 182     -57.012  11.582  95.731  1.00 20.40           C  
ANISOU 1165  CD1 PHE A 182     2383   2793   2577    -54    502    207       C  
ATOM   1166  CD2 PHE A 182     -56.725   9.562  94.489  1.00 19.45           C  
ANISOU 1166  CD2 PHE A 182     2242   2667   2480    -83    464    234       C  
ATOM   1167  CE1 PHE A 182     -56.105  12.229  94.890  1.00 20.65           C  
ANISOU 1167  CE1 PHE A 182     2419   2812   2616    -38    467    203       C  
ATOM   1168  CE2 PHE A 182     -55.811  10.208  93.652  1.00 21.31           C  
ANISOU 1168  CE2 PHE A 182     2483   2892   2722    -66    431    228       C  
ATOM   1169  CZ  PHE A 182     -55.503  11.537  93.860  1.00 19.34           C  
ANISOU 1169  CZ  PHE A 182     2245   2639   2464    -45    432    214       C  
ATOM   1170  N   ASN A 183     -59.550   9.845  99.517  1.00 19.51           N  
ANISOU 1170  N   ASN A 183     2293   2717   2403   -111    641    223       N  
ATOM   1171  CA  ASN A 183     -60.715   9.646 100.384  1.00 20.14           C  
ANISOU 1171  CA  ASN A 183     2363   2814   2478   -122    693    222       C  
ATOM   1172  C   ASN A 183     -61.566  10.925 100.433  1.00 25.41           C  
ANISOU 1172  C   ASN A 183     3004   3489   3160    -95    724    199       C  
ATOM   1173  O   ASN A 183     -61.035  12.009 100.694  1.00 24.00           O  
ANISOU 1173  O   ASN A 183     2849   3303   2965    -75    720    182       O  
ATOM   1174  CB  ASN A 183     -60.271   9.233 101.804  1.00 20.09           C  
ANISOU 1174  CB  ASN A 183     2408   2806   2420   -141    712    230       C  
ATOM   1175  CG  ASN A 183     -61.417   8.819 102.719  1.00 44.13           C  
ANISOU 1175  CG  ASN A 183     5445   5866   5455   -158    767    234       C  
ATOM   1176  OD1 ASN A 183     -62.592   8.778 102.321  1.00 43.64           O  
ANISOU 1176  OD1 ASN A 183     5334   5817   5428   -156    793    231       O  
ATOM   1177  ND2 ASN A 183     -61.092   8.477 103.953  1.00 33.21           N  
ANISOU 1177  ND2 ASN A 183     4109   4484   4025   -176    785    242       N  
ATOM   1178  N   ASP A 184     -62.893  10.798 100.173  1.00 24.10           N  
ANISOU 1178  N   ASP A 184     2790   3340   3028    -95    754    197       N  
ATOM   1179  CA  ASP A 184     -63.814  11.948 100.154  1.00 25.18           C  
ANISOU 1179  CA  ASP A 184     2895   3486   3188    -68    785    177       C  
ATOM   1180  C   ASP A 184     -63.942  12.621 101.534  1.00 31.61           C  
ANISOU 1180  C   ASP A 184     3744   4303   3964    -62    831    162       C  
ATOM   1181  O   ASP A 184     -64.316  13.794 101.614  1.00 31.24           O  
ANISOU 1181  O   ASP A 184     3687   4256   3926    -34    851    140       O  
ATOM   1182  CB  ASP A 184     -65.198  11.526  99.630  1.00 27.99           C  
ANISOU 1182  CB  ASP A 184     3189   3859   3588    -72    807    181       C  
ATOM   1183  CG  ASP A 184     -65.187  11.052  98.182  1.00 40.44           C  
ANISOU 1183  CG  ASP A 184     4728   5434   5203    -74    762    192       C  
ATOM   1184  OD1 ASP A 184     -64.336  10.197  97.843  1.00 41.95           O  
ANISOU 1184  OD1 ASP A 184     4941   5615   5384    -93    727    206       O  
ATOM   1185  OD2 ASP A 184     -66.088  11.458  97.421  1.00 45.42           O  
ANISOU 1185  OD2 ASP A 184     5307   6075   5877    -58    764    186       O  
ATOM   1186  N   SER A 185     -63.622  11.883 102.615  1.00 29.67           N  
ANISOU 1186  N   SER A 185     3540   4059   3675    -88    847    172       N  
ATOM   1187  CA  SER A 185     -63.693  12.421 103.975  1.00 30.06           C  
ANISOU 1187  CA  SER A 185     3628   4111   3681    -87    890    159       C  
ATOM   1188  C   SER A 185     -62.491  13.331 104.278  1.00 33.72           C  
ANISOU 1188  C   SER A 185     4143   4558   4111    -73    864    144       C  
ATOM   1189  O   SER A 185     -62.596  14.237 105.109  1.00 33.57           O  
ANISOU 1189  O   SER A 185     4148   4539   4067    -60    895    123       O  
ATOM   1190  CB  SER A 185     -63.763  11.289 104.991  1.00 34.46           C  
ANISOU 1190  CB  SER A 185     4215   4676   4203   -122    915    178       C  
ATOM   1191  OG  SER A 185     -64.874  10.446 104.732  1.00 45.28           O  
ANISOU 1191  OG  SER A 185     5538   6061   5605   -138    940    191       O  
ATOM   1192  N   ALA A 186     -61.348  13.089 103.599  1.00 29.57           N  
ANISOU 1192  N   ALA A 186     3632   4019   3586    -75    808    155       N  
ATOM   1193  CA  ALA A 186     -60.131  13.880 103.797  1.00 28.95           C  
ANISOU 1193  CA  ALA A 186     3597   3923   3478    -64    777    143       C  
ATOM   1194  C   ALA A 186     -60.264  15.276 103.173  1.00 32.10           C  
ANISOU 1194  C   ALA A 186     3977   4315   3906    -30    774    119       C  
ATOM   1195  O   ALA A 186     -61.181  15.516 102.384  1.00 30.62           O  
ANISOU 1195  O   ALA A 186     3739   4134   3763    -14    785    116       O  
ATOM   1196  CB  ALA A 186     -58.935  13.154 103.198  1.00 29.33           C  
ANISOU 1196  CB  ALA A 186     3660   3959   3524    -77    721    163       C  
ATOM   1197  N   GLN A 187     -59.332  16.195 103.516  1.00 29.33           N  
ANISOU 1197  N   GLN A 187     3667   3950   3528    -19    758    104       N  
ATOM   1198  CA  GLN A 187     -59.314  17.555 102.959  1.00 29.49           C  
ANISOU 1198  CA  GLN A 187     3676   3958   3572     12    752     82       C  
ATOM   1199  C   GLN A 187     -59.052  17.512 101.437  1.00 32.41           C  
ANISOU 1199  C   GLN A 187     4008   4320   3986     23    707     92       C  
ATOM   1200  O   GLN A 187     -58.398  16.585 100.950  1.00 31.99           O  
ANISOU 1200  O   GLN A 187     3955   4266   3932      6    672    113       O  
ATOM   1201  CB  GLN A 187     -58.227  18.413 103.660  1.00 31.07           C  
ANISOU 1201  CB  GLN A 187     3932   4142   3732     15    737     65       C  
ATOM   1202  CG  GLN A 187     -58.402  18.525 105.187  1.00 48.10           C  
ANISOU 1202  CG  GLN A 187     6133   6304   5837      4    779     52       C  
ATOM   1203  CD  GLN A 187     -59.626  19.333 105.578  1.00 70.55           C  
ANISOU 1203  CD  GLN A 187     8959   9153   8693     25    835     29       C  
ATOM   1204  OE1 GLN A 187     -60.065  20.241 104.856  1.00 67.32           O  
ANISOU 1204  OE1 GLN A 187     8519   8737   8323     53    839     14       O  
ATOM   1205  NE2 GLN A 187     -60.135  19.088 106.775  1.00 63.06           N  
ANISOU 1205  NE2 GLN A 187     8035   8217   7708     12    882     23       N  
ATOM   1206  N   PRO A 188     -59.528  18.527 100.661  1.00 27.92           N  
ANISOU 1206  N   PRO A 188     3408   3746   3454     53    708     79       N  
ATOM   1207  CA  PRO A 188     -59.241  18.528  99.211  1.00 26.68           C  
ANISOU 1207  CA  PRO A 188     3220   3583   3335     62    665     89       C  
ATOM   1208  C   PRO A 188     -57.736  18.611  98.929  1.00 28.64           C  
ANISOU 1208  C   PRO A 188     3502   3814   3564     56    618     94       C  
ATOM   1209  O   PRO A 188     -56.965  18.989  99.817  1.00 28.41           O  
ANISOU 1209  O   PRO A 188     3519   3776   3498     51    617     84       O  
ATOM   1210  CB  PRO A 188     -59.986  19.777  98.699  1.00 28.64           C  
ANISOU 1210  CB  PRO A 188     3438   3825   3618     97    680     72       C  
ATOM   1211  CG  PRO A 188     -60.965  20.122  99.784  1.00 33.99           C  
ANISOU 1211  CG  PRO A 188     4116   4512   4286    103    737     56       C  
ATOM   1212  CD  PRO A 188     -60.325  19.705 101.059  1.00 29.93           C  
ANISOU 1212  CD  PRO A 188     3656   3998   3718     79    748     54       C  
ATOM   1213  N   ILE A 189     -57.309  18.229  97.696  1.00 23.96           N  
ANISOU 1213  N   ILE A 189     2888   3218   2998     55    578    109       N  
ATOM   1214  CA  ILE A 189     -55.879  18.253  97.315  1.00 22.62           C  
ANISOU 1214  CA  ILE A 189     2746   3034   2816     50    533    114       C  
ATOM   1215  C   ILE A 189     -55.231  19.586  97.709  1.00 25.48           C  
ANISOU 1215  C   ILE A 189     3140   3378   3162     65    530     95       C  
ATOM   1216  O   ILE A 189     -54.242  19.595  98.440  1.00 24.04           O  
ANISOU 1216  O   ILE A 189     3000   3188   2946     52    518     92       O  
ATOM   1217  CB  ILE A 189     -55.690  17.936  95.799  1.00 25.06           C  
ANISOU 1217  CB  ILE A 189     3022   3341   3160     54    497    128       C  
ATOM   1218  CG1 ILE A 189     -56.316  16.560  95.436  1.00 25.53           C  
ANISOU 1218  CG1 ILE A 189     3053   3416   3233     35    499    146       C  
ATOM   1219  CG2 ILE A 189     -54.203  17.995  95.410  1.00 24.13           C  
ANISOU 1219  CG2 ILE A 189     2931   3208   3031     48    454    133       C  
ATOM   1220  CD1 ILE A 189     -56.274  16.215  93.943  1.00 28.52           C  
ANISOU 1220  CD1 ILE A 189     3399   3794   3644     39    466    157       C  
ATOM   1221  N   PHE A 190     -55.841  20.712  97.289  1.00 22.43           N  
ANISOU 1221  N   PHE A 190     2735   2986   2803     92    543     80       N  
ATOM   1222  CA  PHE A 190     -55.393  22.045  97.699  1.00 22.33           C  
ANISOU 1222  CA  PHE A 190     2752   2954   2778    107    546     58       C  
ATOM   1223  C   PHE A 190     -56.537  22.808  98.380  1.00 25.98           C  
ANISOU 1223  C   PHE A 190     3207   3419   3245    126    595     38       C  
ATOM   1224  O   PHE A 190     -57.708  22.471  98.176  1.00 25.03           O  
ANISOU 1224  O   PHE A 190     3048   3313   3148    133    620     42       O  
ATOM   1225  CB  PHE A 190     -54.857  22.841  96.490  1.00 23.98           C  
ANISOU 1225  CB  PHE A 190     2948   3146   3015    125    512     59       C  
ATOM   1226  CG  PHE A 190     -53.669  22.204  95.805  1.00 25.17           C  
ANISOU 1226  CG  PHE A 190     3107   3294   3163    108    467     77       C  
ATOM   1227  CD1 PHE A 190     -52.393  22.313  96.344  1.00 27.98           C  
ANISOU 1227  CD1 PHE A 190     3504   3638   3488     94    446     75       C  
ATOM   1228  CD2 PHE A 190     -53.820  21.530  94.600  1.00 27.23           C  
ANISOU 1228  CD2 PHE A 190     3332   3562   3451    107    446     95       C  
ATOM   1229  CE1 PHE A 190     -51.295  21.727  95.706  1.00 28.71           C  
ANISOU 1229  CE1 PHE A 190     3599   3728   3581     80    406     91       C  
ATOM   1230  CE2 PHE A 190     -52.718  20.955  93.957  1.00 29.64           C  
ANISOU 1230  CE2 PHE A 190     3645   3864   3754     93    407    110       C  
ATOM   1231  CZ  PHE A 190     -51.466  21.054  94.517  1.00 27.66           C  
ANISOU 1231  CZ  PHE A 190     3432   3602   3476     81    389    108       C  
ATOM   1232  N   SER A 191     -56.199  23.835  99.201  1.00 22.96           N  
ANISOU 1232  N   SER A 191     2864   3021   2840    134    609     15       N  
ATOM   1233  CA  SER A 191     -57.210  24.660  99.888  1.00 23.29           C  
ANISOU 1233  CA  SER A 191     2904   3061   2885    154    657     -8       C  
ATOM   1234  C   SER A 191     -58.034  25.464  98.875  1.00 27.85           C  
ANISOU 1234  C   SER A 191     3437   3632   3513    187    662    -11       C  
ATOM   1235  O   SER A 191     -59.223  25.709  99.097  1.00 27.55           O  
ANISOU 1235  O   SER A 191     3373   3601   3494    205    702    -20       O  
ATOM   1236  CB  SER A 191     -56.545  25.600 100.889  1.00 26.26           C  
ANISOU 1236  CB  SER A 191     3333   3419   3224    154    666    -33       C  
ATOM   1237  OG  SER A 191     -55.658  26.494 100.242  1.00 33.74           O  
ANISOU 1237  OG  SER A 191     4294   4343   4184    164    631    -38       O  
ATOM   1238  N   ASP A 192     -57.403  25.858  97.756  1.00 24.64           N  
ANISOU 1238  N   ASP A 192     3022   3211   3129    196    621     -2       N  
ATOM   1239  CA  ASP A 192     -58.078  26.553  96.665  1.00 24.76           C  
ANISOU 1239  CA  ASP A 192     2996   3220   3192    226    617      0       C  
ATOM   1240  C   ASP A 192     -57.998  25.710  95.391  1.00 29.09           C  
ANISOU 1240  C   ASP A 192     3509   3780   3764    218    580     27       C  
ATOM   1241  O   ASP A 192     -56.920  25.212  95.047  1.00 28.67           O  
ANISOU 1241  O   ASP A 192     3474   3725   3696    198    544     39       O  
ATOM   1242  CB  ASP A 192     -57.443  27.944  96.434  1.00 26.77           C  
ANISOU 1242  CB  ASP A 192     3275   3443   3452    245    603    -14       C  
ATOM   1243  CG  ASP A 192     -58.051  28.722  95.273  1.00 40.45           C  
ANISOU 1243  CG  ASP A 192     4970   5166   5233    277    595     -9       C  
ATOM   1244  OD1 ASP A 192     -59.283  28.621  95.070  1.00 41.23           O  
ANISOU 1244  OD1 ASP A 192     5027   5279   5361    294    619     -6       O  
ATOM   1245  OD2 ASP A 192     -57.314  29.502  94.632  1.00 49.26           O  
ANISOU 1245  OD2 ASP A 192     6100   6260   6358    285    566     -8       O  
ATOM   1246  N   ALA A 193     -59.141  25.531  94.696  1.00 25.87           N  
ANISOU 1246  N   ALA A 193     3050   3386   3393    233    589     36       N  
ATOM   1247  CA  ALA A 193     -59.199  24.726  93.468  1.00 25.23           C  
ANISOU 1247  CA  ALA A 193     2934   3318   3335    225    556     60       C  
ATOM   1248  C   ALA A 193     -58.281  25.290  92.369  1.00 28.62           C  
ANISOU 1248  C   ALA A 193     3371   3728   3774    232    512     68       C  
ATOM   1249  O   ALA A 193     -57.664  24.524  91.629  1.00 27.86           O  
ANISOU 1249  O   ALA A 193     3272   3638   3675    215    479     84       O  
ATOM   1250  CB  ALA A 193     -60.630  24.642  92.964  1.00 26.13           C  
ANISOU 1250  CB  ALA A 193     2992   3447   3488    242    573     65       C  
ATOM   1251  N   GLY A 194     -58.154  26.621  92.323  1.00 24.86           N  
ANISOU 1251  N   GLY A 194     2908   3230   3308    257    515     55       N  
ATOM   1252  CA  GLY A 194     -57.325  27.309  91.333  1.00 23.98           C  
ANISOU 1252  CA  GLY A 194     2806   3099   3206    265    478     62       C  
ATOM   1253  C   GLY A 194     -55.845  26.961  91.408  1.00 26.63           C  
ANISOU 1253  C   GLY A 194     3180   3426   3511    239    449     65       C  
ATOM   1254  O   GLY A 194     -55.112  27.159  90.434  1.00 26.37           O  
ANISOU 1254  O   GLY A 194     3149   3384   3486    239    416     77       O  
ATOM   1255  N   ILE A 195     -55.386  26.445  92.578  1.00 21.62           N  
ANISOU 1255  N   ILE A 195     2577   2797   2842    218    462     57       N  
ATOM   1256  CA  ILE A 195     -53.978  26.050  92.765  1.00 20.02           C  
ANISOU 1256  CA  ILE A 195     2409   2588   2610    193    435     61       C  
ATOM   1257  C   ILE A 195     -53.624  24.833  91.887  1.00 22.94           C  
ANISOU 1257  C   ILE A 195     2760   2973   2984    175    405     84       C  
ATOM   1258  O   ILE A 195     -52.560  24.814  91.265  1.00 22.21           O  
ANISOU 1258  O   ILE A 195     2678   2872   2889    166    373     93       O  
ATOM   1259  CB  ILE A 195     -53.657  25.798  94.269  1.00 22.60           C  
ANISOU 1259  CB  ILE A 195     2774   2918   2897    175    455     47       C  
ATOM   1260  CG1 ILE A 195     -53.979  27.054  95.124  1.00 23.22           C  
ANISOU 1260  CG1 ILE A 195     2875   2979   2969    193    485     21       C  
ATOM   1261  CG2 ILE A 195     -52.197  25.359  94.450  1.00 21.83           C  
ANISOU 1261  CG2 ILE A 195     2709   2815   2772    150    423     54       C  
ATOM   1262  CD1 ILE A 195     -53.831  26.844  96.646  1.00 28.44           C  
ANISOU 1262  CD1 ILE A 195     3575   3644   3588    176    510      5       C  
ATOM   1263  N   ASP A 196     -54.529  23.826  91.824  1.00 18.91           N  
ANISOU 1263  N   ASP A 196     2219   2484   2481    168    418     94       N  
ATOM   1264  CA  ASP A 196     -54.326  22.660  90.963  1.00 18.36           C  
ANISOU 1264  CA  ASP A 196     2130   2429   2418    152    393    113       C  
ATOM   1265  C   ASP A 196     -54.488  23.068  89.495  1.00 21.66           C  
ANISOU 1265  C   ASP A 196     2520   2842   2867    168    369    123       C  
ATOM   1266  O   ASP A 196     -55.610  23.135  88.985  1.00 21.71           O  
ANISOU 1266  O   ASP A 196     2491   2859   2899    182    378    126       O  
ATOM   1267  CB  ASP A 196     -55.307  21.528  91.338  1.00 20.61           C  
ANISOU 1267  CB  ASP A 196     2392   2736   2704    140    414    119       C  
ATOM   1268  CG  ASP A 196     -55.174  20.268  90.492  1.00 32.42           C  
ANISOU 1268  CG  ASP A 196     3869   4244   4207    122    391    138       C  
ATOM   1269  OD1 ASP A 196     -54.165  20.145  89.761  1.00 34.06           O  
ANISOU 1269  OD1 ASP A 196     4087   4443   4413    116    359    146       O  
ATOM   1270  OD2 ASP A 196     -56.064  19.401  90.581  1.00 37.21           O  
ANISOU 1270  OD2 ASP A 196     4449   4866   4821    112    405    144       O  
ATOM   1271  N   LEU A 197     -53.370  23.381  88.835  1.00 17.12           N  
ANISOU 1271  N   LEU A 197     1962   2254   2289    165    339    128       N  
ATOM   1272  CA  LEU A 197     -53.365  23.890  87.460  1.00 16.78           C  
ANISOU 1272  CA  LEU A 197     1901   2205   2270    180    316    138       C  
ATOM   1273  C   LEU A 197     -53.845  22.836  86.437  1.00 20.54           C  
ANISOU 1273  C   LEU A 197     2344   2700   2760    172    301    154       C  
ATOM   1274  O   LEU A 197     -54.220  23.194  85.319  1.00 20.64           O  
ANISOU 1274  O   LEU A 197     2334   2713   2794    185    286    162       O  
ATOM   1275  CB  LEU A 197     -51.950  24.388  87.086  1.00 16.51           C  
ANISOU 1275  CB  LEU A 197     1895   2152   2226    175    290    140       C  
ATOM   1276  CG  LEU A 197     -51.366  25.482  87.995  1.00 21.10           C  
ANISOU 1276  CG  LEU A 197     2511   2712   2794    180    300    123       C  
ATOM   1277  CD1 LEU A 197     -49.864  25.571  87.843  1.00 20.93           C  
ANISOU 1277  CD1 LEU A 197     2516   2677   2758    165    275    127       C  
ATOM   1278  CD2 LEU A 197     -52.022  26.832  87.725  1.00 22.98           C  
ANISOU 1278  CD2 LEU A 197     2742   2935   3054    209    311    116       C  
ATOM   1279  N   ILE A 198     -53.824  21.544  86.816  1.00 16.02           N  
ANISOU 1279  N   ILE A 198     1770   2142   2176    149    304    158       N  
ATOM   1280  CA  ILE A 198     -54.177  20.469  85.887  1.00 14.80           C  
ANISOU 1280  CA  ILE A 198     1589   2003   2032    137    288    172       C  
ATOM   1281  C   ILE A 198     -55.661  20.106  85.945  1.00 16.84           C  
ANISOU 1281  C   ILE A 198     1810   2279   2308    141    307    172       C  
ATOM   1282  O   ILE A 198     -56.329  20.098  84.906  1.00 15.79           O  
ANISOU 1282  O   ILE A 198     1646   2155   2198    149    294    179       O  
ATOM   1283  CB  ILE A 198     -53.259  19.220  86.083  1.00 17.54           C  
ANISOU 1283  CB  ILE A 198     1953   2351   2358    110    277    178       C  
ATOM   1284  CG1 ILE A 198     -51.767  19.618  86.029  1.00 17.30           C  
ANISOU 1284  CG1 ILE A 198     1955   2304   2313    107    257    178       C  
ATOM   1285  CG2 ILE A 198     -53.588  18.116  85.037  1.00 17.87           C  
ANISOU 1285  CG2 ILE A 198     1971   2406   2412     98    260    190       C  
ATOM   1286  CD1 ILE A 198     -50.850  18.529  86.286  1.00 21.84           C  
ANISOU 1286  CD1 ILE A 198     2547   2879   2871     85    247    184       C  
ATOM   1287  N   TYR A 199     -56.174  19.748  87.147  1.00 12.07           N  
ANISOU 1287  N   TYR A 199     1209   1683   1695    134    338    165       N  
ATOM   1288  CA  TYR A 199     -57.547  19.253  87.261  1.00 11.33           C  
ANISOU 1288  CA  TYR A 199     1078   1608   1620    134    358    166       C  
ATOM   1289  C   TYR A 199     -58.414  20.032  88.259  1.00 16.36           C  
ANISOU 1289  C   TYR A 199     1709   2246   2261    151    396    153       C  
ATOM   1290  O   TYR A 199     -59.583  19.686  88.449  1.00 17.13           O  
ANISOU 1290  O   TYR A 199     1773   2359   2374    151    418    154       O  
ATOM   1291  CB  TYR A 199     -57.556  17.751  87.575  1.00 11.03           C  
ANISOU 1291  CB  TYR A 199     1039   1581   1569    104    361    174       C  
ATOM   1292  CG  TYR A 199     -56.996  16.898  86.454  1.00 11.43           C  
ANISOU 1292  CG  TYR A 199     1087   1634   1624     89    327    186       C  
ATOM   1293  CD1 TYR A 199     -57.492  17.004  85.157  1.00 12.68           C  
ANISOU 1293  CD1 TYR A 199     1215   1798   1805     97    306    192       C  
ATOM   1294  CD2 TYR A 199     -56.070  15.891  86.714  1.00 12.01           C  
ANISOU 1294  CD2 TYR A 199     1186   1703   1676     66    317    192       C  
ATOM   1295  CE1 TYR A 199     -57.025  16.184  84.134  1.00 12.55           C  
ANISOU 1295  CE1 TYR A 199     1197   1783   1789     82    277    201       C  
ATOM   1296  CE2 TYR A 199     -55.603  15.058  85.701  1.00 12.55           C  
ANISOU 1296  CE2 TYR A 199     1251   1771   1748     52    290    201       C  
ATOM   1297  CZ  TYR A 199     -56.095  15.198  84.412  1.00 19.81           C  
ANISOU 1297  CZ  TYR A 199     2143   2697   2689     60    271    204       C  
ATOM   1298  OH  TYR A 199     -55.658  14.369  83.412  1.00 20.15           O  
ANISOU 1298  OH  TYR A 199     2184   2739   2732     46    245    211       O  
ATOM   1299  N   LYS A 200     -57.873  21.131  88.834  1.00 13.18           N  
ANISOU 1299  N   LYS A 200     1336   1825   1846    166    405    141       N  
ATOM   1300  CA  LYS A 200     -58.622  21.997  89.775  1.00 13.59           C  
ANISOU 1300  CA  LYS A 200     1387   1874   1901    185    442    125       C  
ATOM   1301  C   LYS A 200     -59.291  21.187  90.920  1.00 18.37           C  
ANISOU 1301  C   LYS A 200     1990   2497   2494    168    479    121       C  
ATOM   1302  O   LYS A 200     -60.491  21.339  91.169  1.00 18.21           O  
ANISOU 1302  O   LYS A 200     1938   2487   2493    180    508    117       O  
ATOM   1303  CB  LYS A 200     -59.659  22.863  89.024  1.00 16.19           C  
ANISOU 1303  CB  LYS A 200     1677   2205   2268    215    445    125       C  
ATOM   1304  N   ASN A 201     -58.494  20.309  91.600  1.00 15.14           N  
ANISOU 1304  N   ASN A 201     1613   2088   2052    141    476    125       N  
ATOM   1305  CA  ASN A 201     -58.950  19.487  92.750  1.00 15.00           C  
ANISOU 1305  CA  ASN A 201     1601   2084   2016    122    509    123       C  
ATOM   1306  C   ASN A 201     -59.860  18.301  92.367  1.00 19.38           C  
ANISOU 1306  C   ASN A 201     2116   2659   2589    106    514    137       C  
ATOM   1307  O   ASN A 201     -60.301  17.567  93.251  1.00 19.09           O  
ANISOU 1307  O   ASN A 201     2081   2633   2538     89    542    138       O  
ATOM   1308  CB  ASN A 201     -59.600  20.357  93.849  1.00 15.18           C  
ANISOU 1308  CB  ASN A 201     1631   2105   2031    138    553    104       C  
ATOM   1309  CG  ASN A 201     -58.598  21.019  94.766  1.00 34.64           C  
ANISOU 1309  CG  ASN A 201     4148   4552   4460    138    556     90       C  
ATOM   1310  OD1 ASN A 201     -57.413  20.658  94.804  1.00 27.83           O  
ANISOU 1310  OD1 ASN A 201     3318   3682   3574    121    528     97       O  
ATOM   1311  ND2 ASN A 201     -59.072  21.930  95.597  1.00 26.22           N  
ANISOU 1311  ND2 ASN A 201     3093   3481   3389    154    591     71       N  
ATOM   1312  N   ASP A 202     -60.068  18.061  91.055  1.00 15.83           N  
ANISOU 1312  N   ASP A 202     1634   2214   2167    109    484    148       N  
ATOM   1313  CA  ASP A 202     -60.883  16.924  90.614  1.00 15.21           C  
ANISOU 1313  CA  ASP A 202     1520   2154   2107     91    484    160       C  
ATOM   1314  C   ASP A 202     -60.133  15.608  90.839  1.00 18.75           C  
ANISOU 1314  C   ASP A 202     1991   2601   2531     59    472    171       C  
ATOM   1315  O   ASP A 202     -59.204  15.283  90.091  1.00 18.39           O  
ANISOU 1315  O   ASP A 202     1960   2547   2481     52    436    178       O  
ATOM   1316  CB  ASP A 202     -61.297  17.078  89.134  1.00 16.69           C  
ANISOU 1316  CB  ASP A 202     1668   2345   2327    102    454    167       C  
ATOM   1317  CG  ASP A 202     -62.423  16.142  88.707  1.00 25.27           C  
ANISOU 1317  CG  ASP A 202     2709   3452   3439     88    457    176       C  
ATOM   1318  OD1 ASP A 202     -62.480  15.006  89.225  1.00 25.75           O  
ANISOU 1318  OD1 ASP A 202     2775   3520   3489     60    468    182       O  
ATOM   1319  OD2 ASP A 202     -63.197  16.521  87.807  1.00 31.75           O  
ANISOU 1319  OD2 ASP A 202     3490   4281   4291    103    445    178       O  
ATOM   1320  N   VAL A 203     -60.504  14.877  91.911  1.00 15.12           N  
ANISOU 1320  N   VAL A 203     1540   2150   2056     39    502    173       N  
ATOM   1321  CA  VAL A 203     -59.858  13.616  92.297  1.00 14.12           C  
ANISOU 1321  CA  VAL A 203     1439   2021   1907      9    495    185       C  
ATOM   1322  C   VAL A 203     -60.028  12.532  91.215  1.00 19.13           C  
ANISOU 1322  C   VAL A 203     2046   2660   2561     -8    469    198       C  
ATOM   1323  O   VAL A 203     -59.064  11.831  90.891  1.00 19.16           O  
ANISOU 1323  O   VAL A 203     2073   2654   2553    -22    442    206       O  
ATOM   1324  CB  VAL A 203     -60.370  13.134  93.692  1.00 17.24           C  
ANISOU 1324  CB  VAL A 203     1846   2425   2281     -7    537    185       C  
ATOM   1325  CG1 VAL A 203     -60.120  11.645  93.893  1.00 16.83           C  
ANISOU 1325  CG1 VAL A 203     1805   2374   2217    -39    531    202       C  
ATOM   1326  CG2 VAL A 203     -59.741  13.951  94.814  1.00 17.00           C  
ANISOU 1326  CG2 VAL A 203     1859   2385   2216      2    553    173       C  
ATOM   1327  N   SER A 204     -61.255  12.407  90.646  1.00 16.23           N  
ANISOU 1327  N   SER A 204     1631   2308   2226     -7    477    199       N  
ATOM   1328  CA  SER A 204     -61.555  11.388  89.628  1.00 15.81           C  
ANISOU 1328  CA  SER A 204     1553   2261   2194    -25    453    209       C  
ATOM   1329  C   SER A 204     -60.674  11.551  88.380  1.00 19.09           C  
ANISOU 1329  C   SER A 204     1976   2666   2613    -17    409    211       C  
ATOM   1330  O   SER A 204     -60.257  10.556  87.788  1.00 18.32           O  
ANISOU 1330  O   SER A 204     1883   2564   2515    -36    386    219       O  
ATOM   1331  CB  SER A 204     -63.029  11.435  89.243  1.00 19.63           C  
ANISOU 1331  CB  SER A 204     1981   2764   2712    -22    467    208       C  
ATOM   1332  OG  SER A 204     -63.360  12.668  88.628  1.00 26.68           O  
ANISOU 1332  OG  SER A 204     2853   3659   3625      9    459    201       O  
ATOM   1333  N   LYS A 205     -60.379  12.807  87.992  1.00 16.11           N  
ANISOU 1333  N   LYS A 205     1600   2283   2239     11    398    203       N  
ATOM   1334  CA  LYS A 205     -59.509  13.082  86.843  1.00 15.70           C  
ANISOU 1334  CA  LYS A 205     1558   2220   2188     19    360    205       C  
ATOM   1335  C   LYS A 205     -58.051  12.768  87.166  1.00 20.12           C  
ANISOU 1335  C   LYS A 205     2163   2762   2718     10    346    207       C  
ATOM   1336  O   LYS A 205     -57.299  12.353  86.277  1.00 19.79           O  
ANISOU 1336  O   LYS A 205     2129   2713   2676      4    317    212       O  
ATOM   1337  CB  LYS A 205     -59.666  14.535  86.372  1.00 18.00           C  
ANISOU 1337  CB  LYS A 205     1838   2509   2492     51    354    198       C  
ATOM   1338  CG  LYS A 205     -60.989  14.800  85.662  1.00 28.87           C  
ANISOU 1338  CG  LYS A 205     3166   3902   3902     62    354    199       C  
ATOM   1339  CD  LYS A 205     -61.087  16.233  85.173  1.00 36.11           C  
ANISOU 1339  CD  LYS A 205     4075   4813   4833     95    346    195       C  
ATOM   1340  CE  LYS A 205     -62.384  16.493  84.456  1.00 45.03           C  
ANISOU 1340  CE  LYS A 205     5153   5958   5996    108    343    198       C  
ATOM   1341  NZ  LYS A 205     -62.474  17.895  83.980  1.00 54.55           N  
ANISOU 1341  NZ  LYS A 205     6354   7157   7216    142    334    196       N  
ATOM   1342  N   TRP A 206     -57.655  12.908  88.455  1.00 17.64           N  
ANISOU 1342  N   TRP A 206     1879   2443   2381      8    369    204       N  
ATOM   1343  CA  TRP A 206     -56.310  12.526  88.898  1.00 17.49           C  
ANISOU 1343  CA  TRP A 206     1901   2409   2334     -3    356    208       C  
ATOM   1344  C   TRP A 206     -56.144  11.014  88.913  1.00 18.25           C  
ANISOU 1344  C   TRP A 206     2002   2505   2426    -30    350    220       C  
ATOM   1345  O   TRP A 206     -55.055  10.513  88.630  1.00 18.10           O  
ANISOU 1345  O   TRP A 206     2005   2474   2398    -37    327    226       O  
ATOM   1346  CB  TRP A 206     -55.989  13.123  90.277  1.00 17.17           C  
ANISOU 1346  CB  TRP A 206     1892   2364   2268      2    379    201       C  
ATOM   1347  CG  TRP A 206     -55.449  14.516  90.209  1.00 18.72           C  
ANISOU 1347  CG  TRP A 206     2102   2550   2460     25    372    190       C  
ATOM   1348  CD1 TRP A 206     -56.093  15.663  90.567  1.00 22.01           C  
ANISOU 1348  CD1 TRP A 206     2512   2969   2883     46    393    178       C  
ATOM   1349  CD2 TRP A 206     -54.218  14.921  89.601  1.00 18.43           C  
ANISOU 1349  CD2 TRP A 206     2084   2498   2418     31    341    191       C  
ATOM   1350  NE1 TRP A 206     -55.305  16.754  90.288  1.00 21.79           N  
ANISOU 1350  NE1 TRP A 206     2502   2927   2852     63    377    170       N  
ATOM   1351  CE2 TRP A 206     -54.155  16.329  89.678  1.00 22.81           C  
ANISOU 1351  CE2 TRP A 206     2645   3046   2975     54    345    179       C  
ATOM   1352  CE3 TRP A 206     -53.153  14.228  88.996  1.00 19.32           C  
ANISOU 1352  CE3 TRP A 206     2209   2603   2527     20    312    200       C  
ATOM   1353  CZ2 TRP A 206     -53.074  17.058  89.173  1.00 21.99           C  
ANISOU 1353  CZ2 TRP A 206     2559   2927   2868     63    321    177       C  
ATOM   1354  CZ3 TRP A 206     -52.074  14.949  88.516  1.00 20.68           C  
ANISOU 1354  CZ3 TRP A 206     2398   2762   2697     30    289    198       C  
ATOM   1355  CH2 TRP A 206     -52.036  16.344  88.612  1.00 21.43           C  
ANISOU 1355  CH2 TRP A 206     2499   2851   2793     50    293    187       C  
ATOM   1356  N   LYS A 207     -57.235  10.276  89.207  1.00 12.58           N  
ANISOU 1356  N   LYS A 207     1262   1800   1719    -45    371    224       N  
ATOM   1357  CA  LYS A 207     -57.217   8.809  89.165  1.00 11.52           C  
ANISOU 1357  CA  LYS A 207     1129   1664   1585    -73    367    235       C  
ATOM   1358  C   LYS A 207     -57.084   8.321  87.725  1.00 15.27           C  
ANISOU 1358  C   LYS A 207     1587   2136   2079    -77    336    237       C  
ATOM   1359  O   LYS A 207     -56.328   7.386  87.462  1.00 15.49           O  
ANISOU 1359  O   LYS A 207     1632   2152   2102    -91    319    244       O  
ATOM   1360  CB  LYS A 207     -58.484   8.222  89.813  1.00 11.87           C  
ANISOU 1360  CB  LYS A 207     1151   1722   1637    -89    400    239       C  
ATOM   1361  CG  LYS A 207     -58.513   8.346  91.323  1.00 16.70           C  
ANISOU 1361  CG  LYS A 207     1788   2335   2223    -93    433    240       C  
ATOM   1362  CD  LYS A 207     -59.785   7.740  91.900  1.00 23.30           C  
ANISOU 1362  CD  LYS A 207     2599   3185   3068   -110    467    244       C  
ATOM   1363  CE  LYS A 207     -59.830   7.835  93.399  1.00 37.19           C  
ANISOU 1363  CE  LYS A 207     4385   4946   4798   -115    502    245       C  
ATOM   1364  NZ  LYS A 207     -61.098   7.290  93.944  1.00 46.60           N  
ANISOU 1364  NZ  LYS A 207     5552   6153   6000   -133    539    249       N  
ATOM   1365  N   ARG A 208     -57.798   8.982  86.778  1.00 11.28           N  
ANISOU 1365  N   ARG A 208     1048   1641   1596    -63    328    231       N  
ATOM   1366  CA  ARG A 208     -57.704   8.651  85.344  1.00 10.49           C  
ANISOU 1366  CA  ARG A 208      934   1541   1512    -65    297    232       C  
ATOM   1367  C   ARG A 208     -56.281   8.886  84.822  1.00 14.78           C  
ANISOU 1367  C   ARG A 208     1506   2067   2041    -56    271    231       C  
ATOM   1368  O   ARG A 208     -55.744   8.042  84.111  1.00 14.65           O  
ANISOU 1368  O   ARG A 208     1497   2043   2025    -69    252    234       O  
ATOM   1369  CB  ARG A 208     -58.718   9.472  84.523  1.00  8.01           C  
ANISOU 1369  CB  ARG A 208      581   1242   1222    -49    292    226       C  
ATOM   1370  CG  ARG A 208     -60.174   9.109  84.811  1.00 14.83           C  
ANISOU 1370  CG  ARG A 208     1407   2124   2106    -60    313    227       C  
ATOM   1371  CD  ARG A 208     -61.134   9.933  83.966  1.00 19.86           C  
ANISOU 1371  CD  ARG A 208     2003   2775   2768    -42    304    224       C  
ATOM   1372  NE  ARG A 208     -62.532   9.598  84.242  1.00 24.19           N  
ANISOU 1372  NE  ARG A 208     2511   3342   3339    -52    324    225       N  
ATOM   1373  CZ  ARG A 208     -63.199   8.632  83.614  1.00 35.60           C  
ANISOU 1373  CZ  ARG A 208     3929   4795   4801    -75    313    228       C  
ATOM   1374  NH1 ARG A 208     -62.602   7.903  82.679  1.00 18.04           N  
ANISOU 1374  NH1 ARG A 208     1719   2564   2573    -90    282    230       N  
ATOM   1375  NH2 ARG A 208     -64.466   8.387  83.920  1.00 23.40           N  
ANISOU 1375  NH2 ARG A 208     2345   3268   3279    -85    333    229       N  
ATOM   1376  N   PHE A 209     -55.664  10.043  85.194  1.00 10.88           N  
ANISOU 1376  N   PHE A 209     1030   1568   1535    -35    273    227       N  
ATOM   1377  CA  PHE A 209     -54.295  10.377  84.790  1.00 10.70           C  
ANISOU 1377  CA  PHE A 209     1035   1530   1501    -27    251    227       C  
ATOM   1378  C   PHE A 209     -53.298   9.374  85.364  1.00 17.01           C  
ANISOU 1378  C   PHE A 209     1863   2317   2284    -44    248    234       C  
ATOM   1379  O   PHE A 209     -52.407   8.908  84.649  1.00 17.60           O  
ANISOU 1379  O   PHE A 209     1949   2381   2358    -48    227    236       O  
ATOM   1380  CB  PHE A 209     -53.933  11.818  85.234  1.00 12.02           C  
ANISOU 1380  CB  PHE A 209     1215   1694   1660     -4    256    220       C  
ATOM   1381  CG  PHE A 209     -52.482  12.189  85.015  1.00 13.56           C  
ANISOU 1381  CG  PHE A 209     1437   1873   1842      2    237    221       C  
ATOM   1382  CD1 PHE A 209     -52.021  12.555  83.752  1.00 16.48           C  
ANISOU 1382  CD1 PHE A 209     1803   2239   2221     10    214    221       C  
ATOM   1383  CD2 PHE A 209     -51.584  12.214  86.078  1.00 15.48           C  
ANISOU 1383  CD2 PHE A 209     1711   2106   2064     -2    242    221       C  
ATOM   1384  CE1 PHE A 209     -50.682  12.897  83.551  1.00 16.99           C  
ANISOU 1384  CE1 PHE A 209     1890   2290   2275     14    198    221       C  
ATOM   1385  CE2 PHE A 209     -50.243  12.550  85.874  1.00 18.05           C  
ANISOU 1385  CE2 PHE A 209     2059   2418   2381      3    223    222       C  
ATOM   1386  CZ  PHE A 209     -49.799  12.888  84.612  1.00 16.22           C  
ANISOU 1386  CZ  PHE A 209     1820   2183   2160     11    203    222       C  
ATOM   1387  N   ALA A 210     -53.456   9.028  86.660  1.00 13.99           N  
ANISOU 1387  N   ALA A 210     1494   1935   1888    -53    270    237       N  
ATOM   1388  CA  ALA A 210     -52.603   8.042  87.322  1.00 14.14           C  
ANISOU 1388  CA  ALA A 210     1540   1941   1891    -69    267    247       C  
ATOM   1389  C   ALA A 210     -52.712   6.687  86.631  1.00 18.18           C  
ANISOU 1389  C   ALA A 210     2044   2449   2416    -88    257    253       C  
ATOM   1390  O   ALA A 210     -51.700   6.005  86.436  1.00 17.57           O  
ANISOU 1390  O   ALA A 210     1986   2357   2334    -94    241    259       O  
ATOM   1391  CB  ALA A 210     -52.999   7.911  88.777  1.00 15.15           C  
ANISOU 1391  CB  ALA A 210     1681   2073   2001    -77    294    250       C  
ATOM   1392  N   ASN A 211     -53.938   6.306  86.229  1.00 14.97           N  
ANISOU 1392  N   ASN A 211     1608   2054   2026    -98    266    252       N  
ATOM   1393  CA  ASN A 211     -54.185   5.031  85.565  1.00 14.78           C  
ANISOU 1393  CA  ASN A 211     1575   2026   2015   -118    258    256       C  
ATOM   1394  C   ASN A 211     -53.652   5.046  84.129  1.00 16.57           C  
ANISOU 1394  C   ASN A 211     1798   2248   2251   -112    230    250       C  
ATOM   1395  O   ASN A 211     -53.181   4.016  83.632  1.00 15.24           O  
ANISOU 1395  O   ASN A 211     1638   2066   2085   -125    218    252       O  
ATOM   1396  CB  ASN A 211     -55.659   4.713  85.577  1.00 17.57           C  
ANISOU 1396  CB  ASN A 211     1896   2394   2384   -131    274    255       C  
ATOM   1397  CG  ASN A 211     -55.955   3.250  85.545  1.00 45.10           C  
ANISOU 1397  CG  ASN A 211     5383   5874   5879   -159    276    262       C  
ATOM   1398  OD1 ASN A 211     -55.273   2.440  86.181  1.00 34.35           O  
ANISOU 1398  OD1 ASN A 211     4049   4497   4506   -170    279    271       O  
ATOM   1399  ND2 ASN A 211     -57.073   2.895  84.942  1.00 42.59           N  
ANISOU 1399  ND2 ASN A 211     5032   5567   5581   -172    277    258       N  
ATOM   1400  N   SER A 212     -53.737   6.225  83.449  1.00 11.84           N  
ANISOU 1400  N   SER A 212     1186   1657   1657    -92    221    242       N  
ATOM   1401  CA  SER A 212     -53.201   6.396  82.098  1.00 10.81           C  
ANISOU 1401  CA  SER A 212     1053   1522   1530    -85    196    237       C  
ATOM   1402  C   SER A 212     -51.677   6.317  82.122  1.00 13.52           C  
ANISOU 1402  C   SER A 212     1428   1849   1861    -79    185    240       C  
ATOM   1403  O   SER A 212     -51.073   5.745  81.213  1.00 12.15           O  
ANISOU 1403  O   SER A 212     1260   1666   1691    -84    169    238       O  
ATOM   1404  CB  SER A 212     -53.649   7.731  81.512  1.00 14.53           C  
ANISOU 1404  CB  SER A 212     1507   2006   2008    -64    190    232       C  
ATOM   1405  OG  SER A 212     -55.063   7.806  81.427  1.00 22.43           O  
ANISOU 1405  OG  SER A 212     2475   3023   3023    -67    199    230       O  
ATOM   1406  N   LEU A 213     -51.054   6.842  83.201  1.00 10.44           N  
ANISOU 1406  N   LEU A 213     1057   1453   1457    -71    194    243       N  
ATOM   1407  CA  LEU A 213     -49.608   6.751  83.395  1.00 10.44           C  
ANISOU 1407  CA  LEU A 213     1083   1437   1446    -67    183    247       C  
ATOM   1408  C   LEU A 213     -49.197   5.292  83.652  1.00 13.66           C  
ANISOU 1408  C   LEU A 213     1504   1832   1854    -85    182    255       C  
ATOM   1409  O   LEU A 213     -48.162   4.846  83.150  1.00 12.60           O  
ANISOU 1409  O   LEU A 213     1382   1685   1722    -84    168    256       O  
ATOM   1410  CB  LEU A 213     -49.169   7.644  84.573  1.00 10.83           C  
ANISOU 1410  CB  LEU A 213     1149   1485   1479    -57    192    248       C  
ATOM   1411  CG  LEU A 213     -47.687   8.022  84.605  1.00 16.34           C  
ANISOU 1411  CG  LEU A 213     1869   2172   2170    -48    177    250       C  
ATOM   1412  CD1 LEU A 213     -47.322   8.935  83.414  1.00 16.65           C  
ANISOU 1412  CD1 LEU A 213     1899   2210   2216    -33    163    243       C  
ATOM   1413  CD2 LEU A 213     -47.336   8.709  85.906  1.00 19.06           C  
ANISOU 1413  CD2 LEU A 213     2232   2515   2496    -43    184    251       C  
ATOM   1414  N   ARG A 214     -50.046   4.526  84.391  1.00 10.05           N  
ANISOU 1414  N   ARG A 214     1044   1378   1398   -101    198    260       N  
ATOM   1415  CA  ARG A 214     -49.802   3.102  84.618  1.00  9.74           C  
ANISOU 1415  CA  ARG A 214     1016   1324   1361   -119    198    269       C  
ATOM   1416  C   ARG A 214     -49.789   2.362  83.274  1.00 13.93           C  
ANISOU 1416  C   ARG A 214     1538   1848   1907   -126    184    263       C  
ATOM   1417  O   ARG A 214     -48.846   1.627  82.992  1.00 13.40           O  
ANISOU 1417  O   ARG A 214     1486   1764   1842   -127    174    266       O  
ATOM   1418  CB  ARG A 214     -50.872   2.503  85.558  1.00  9.96           C  
ANISOU 1418  CB  ARG A 214     1040   1358   1388   -137    220    276       C  
ATOM   1419  CG  ARG A 214     -50.408   1.233  86.286  1.00 18.85           C  
ANISOU 1419  CG  ARG A 214     2187   2466   2509   -152    223    290       C  
ATOM   1420  CD  ARG A 214     -51.536   0.210  86.442  1.00 27.31           C  
ANISOU 1420  CD  ARG A 214     3247   3538   3590   -177    238    295       C  
ATOM   1421  NE  ARG A 214     -52.699   0.765  87.146  1.00 37.96           N  
ANISOU 1421  NE  ARG A 214     4580   4907   4935   -180    261    294       N  
ATOM   1422  CZ  ARG A 214     -53.192   0.263  88.276  1.00 50.43           C  
ANISOU 1422  CZ  ARG A 214     6168   6487   6506   -196    283    306       C  
ATOM   1423  NH1 ARG A 214     -52.637  -0.808  88.832  1.00 37.16           N  
ANISOU 1423  NH1 ARG A 214     4512   4787   4819   -209    282    320       N  
ATOM   1424  NH2 ARG A 214     -54.260   0.810  88.842  1.00 33.08           N  
ANISOU 1424  NH2 ARG A 214     3953   4308   4306   -198    307    303       N  
ATOM   1425  N   LEU A 215     -50.774   2.678  82.382  1.00 11.35           N  
ANISOU 1425  N   LEU A 215     1186   1536   1591   -127    182    253       N  
ATOM   1426  CA  LEU A 215     -50.849   2.080  81.034  1.00 11.44           C  
ANISOU 1426  CA  LEU A 215     1189   1544   1614   -135    168    245       C  
ATOM   1427  C   LEU A 215     -49.645   2.499  80.166  1.00 15.15           C  
ANISOU 1427  C   LEU A 215     1672   2006   2080   -119    151    240       C  
ATOM   1428  O   LEU A 215     -49.097   1.673  79.435  1.00 14.78           O  
ANISOU 1428  O   LEU A 215     1633   1945   2037   -125    143    236       O  
ATOM   1429  CB  LEU A 215     -52.174   2.475  80.343  1.00 11.79           C  
ANISOU 1429  CB  LEU A 215     1203   1608   1668   -139    166    238       C  
ATOM   1430  CG  LEU A 215     -52.429   1.837  78.957  1.00 16.50           C  
ANISOU 1430  CG  LEU A 215     1791   2204   2274   -150    150    228       C  
ATOM   1431  CD1 LEU A 215     -52.482   0.315  79.051  1.00 16.73           C  
ANISOU 1431  CD1 LEU A 215     1829   2216   2310   -174    153    229       C  
ATOM   1432  CD2 LEU A 215     -53.706   2.366  78.345  1.00 18.00           C  
ANISOU 1432  CD2 LEU A 215     1950   2416   2473   -152    145    222       C  
ATOM   1433  N   ARG A 216     -49.218   3.776  80.276  1.00 11.34           N  
ANISOU 1433  N   ARG A 216     1191   1531   1589    -99    149    240       N  
ATOM   1434  CA  ARG A 216     -48.057   4.291  79.538  1.00 10.30           C  
ANISOU 1434  CA  ARG A 216     1069   1392   1454    -85    136    236       C  
ATOM   1435  C   ARG A 216     -46.761   3.553  79.955  1.00 13.97           C  
ANISOU 1435  C   ARG A 216     1555   1835   1916    -86    134    243       C  
ATOM   1436  O   ARG A 216     -46.008   3.096  79.095  1.00 14.02           O  
ANISOU 1436  O   ARG A 216     1568   1831   1926    -85    126    238       O  
ATOM   1437  CB  ARG A 216     -47.909   5.818  79.766  1.00  9.32           C  
ANISOU 1437  CB  ARG A 216      942   1276   1322    -66    136    236       C  
ATOM   1438  CG  ARG A 216     -46.629   6.412  79.174  1.00 13.95           C  
ANISOU 1438  CG  ARG A 216     1541   1855   1905    -52    125    235       C  
ATOM   1439  CD  ARG A 216     -46.425   7.852  79.614  1.00 22.19           C  
ANISOU 1439  CD  ARG A 216     2586   2904   2942    -36    126    236       C  
ATOM   1440  NE  ARG A 216     -47.213   8.787  78.811  1.00 26.25           N  
ANISOU 1440  NE  ARG A 216     3084   3431   3459    -27    123    231       N  
ATOM   1441  CZ  ARG A 216     -47.293  10.090  79.061  1.00 34.93           C  
ANISOU 1441  CZ  ARG A 216     4182   4534   4555    -13    124    231       C  
ATOM   1442  NH1 ARG A 216     -46.696  10.605  80.131  1.00 20.30           N  
ANISOU 1442  NH1 ARG A 216     2344   2676   2696     -7    130    233       N  
ATOM   1443  NH2 ARG A 216     -48.010  10.880  78.272  1.00 17.22           N  
ANISOU 1443  NH2 ARG A 216     1925   2302   2317     -4    119    228       N  
ATOM   1444  N   LEU A 217     -46.521   3.433  81.268  1.00 10.83           N  
ANISOU 1444  N   LEU A 217     1170   1434   1513    -87    142    253       N  
ATOM   1445  CA  LEU A 217     -45.309   2.795  81.795  1.00 11.44           C  
ANISOU 1445  CA  LEU A 217     1266   1492   1588    -86    138    261       C  
ATOM   1446  C   LEU A 217     -45.346   1.265  81.629  1.00 17.22           C  
ANISOU 1446  C   LEU A 217     2004   2208   2330   -101    139    264       C  
ATOM   1447  O   LEU A 217     -44.297   0.620  81.646  1.00 17.41           O  
ANISOU 1447  O   LEU A 217     2041   2214   2359    -98    133    269       O  
ATOM   1448  CB  LEU A 217     -45.101   3.174  83.276  1.00 11.54           C  
ANISOU 1448  CB  LEU A 217     1291   1506   1587    -83    144    272       C  
ATOM   1449  CG  LEU A 217     -44.989   4.676  83.565  1.00 15.96           C  
ANISOU 1449  CG  LEU A 217     1850   2078   2137    -69    143    268       C  
ATOM   1450  CD1 LEU A 217     -45.079   4.947  85.032  1.00 16.13           C  
ANISOU 1450  CD1 LEU A 217     1884   2102   2143    -71    152    276       C  
ATOM   1451  CD2 LEU A 217     -43.703   5.257  82.985  1.00 19.75           C  
ANISOU 1451  CD2 LEU A 217     2335   2551   2619    -56    129    266       C  
ATOM   1452  N   ALA A 218     -46.554   0.689  81.458  1.00 14.65           N  
ANISOU 1452  N   ALA A 218     1667   1888   2010   -117    147    261       N  
ATOM   1453  CA  ALA A 218     -46.704  -0.746  81.221  1.00 14.47           C  
ANISOU 1453  CA  ALA A 218     1650   1849   1999   -134    148    262       C  
ATOM   1454  C   ALA A 218     -46.290  -1.099  79.790  1.00 18.38           C  
ANISOU 1454  C   ALA A 218     2144   2336   2503   -132    138    249       C  
ATOM   1455  O   ALA A 218     -45.526  -2.043  79.585  1.00 17.91           O  
ANISOU 1455  O   ALA A 218     2099   2256   2452   -134    136    249       O  
ATOM   1456  CB  ALA A 218     -48.143  -1.170  81.467  1.00 15.24           C  
ANISOU 1456  CB  ALA A 218     1734   1955   2100   -154    159    262       C  
ATOM   1457  N   VAL A 219     -46.755  -0.300  78.797  1.00 14.28           N  
ANISOU 1457  N   VAL A 219     1611   1834   1982   -128    132    237       N  
ATOM   1458  CA  VAL A 219     -46.405  -0.517  77.382  1.00 13.47           C  
ANISOU 1458  CA  VAL A 219     1509   1727   1883   -127    123    223       C  
ATOM   1459  C   VAL A 219     -44.899  -0.278  77.144  1.00 15.86           C  
ANISOU 1459  C   VAL A 219     1825   2017   2184   -109    119    224       C  
ATOM   1460  O   VAL A 219     -44.322  -0.862  76.229  1.00 15.79           O  
ANISOU 1460  O   VAL A 219     1823   1996   2179   -109    116    215       O  
ATOM   1461  CB  VAL A 219     -47.296   0.343  76.428  1.00 16.89           C  
ANISOU 1461  CB  VAL A 219     1924   2182   2311   -126    116    213       C  
ATOM   1462  CG1 VAL A 219     -46.874   0.166  74.969  1.00 16.57           C  
ANISOU 1462  CG1 VAL A 219     1888   2139   2269   -125    106    199       C  
ATOM   1463  CG2 VAL A 219     -48.770  -0.001  76.606  1.00 16.72           C  
ANISOU 1463  CG2 VAL A 219     1885   2173   2296   -144    119    212       C  
ATOM   1464  N   ARG A 220     -44.248   0.496  78.044  1.00 10.79           N  
ANISOU 1464  N   ARG A 220     1187   1378   1536    -96    120    234       N  
ATOM   1465  CA  ARG A 220     -42.799   0.722  77.998  1.00  9.72           C  
ANISOU 1465  CA  ARG A 220     1061   1231   1402    -80    116    237       C  
ATOM   1466  C   ARG A 220     -42.024  -0.616  78.155  1.00 13.90           C  
ANISOU 1466  C   ARG A 220     1603   1734   1943    -83    117    241       C  
ATOM   1467  O   ARG A 220     -40.877  -0.720  77.710  1.00 12.58           O  
ANISOU 1467  O   ARG A 220     1441   1556   1782    -72    115    240       O  
ATOM   1468  CB  ARG A 220     -42.379   1.707  79.111  1.00  8.56           C  
ANISOU 1468  CB  ARG A 220      915   1091   1246    -70    115    248       C  
ATOM   1469  CG  ARG A 220     -40.918   2.161  79.019  1.00 13.94           C  
ANISOU 1469  CG  ARG A 220     1602   1764   1930    -54    108    251       C  
ATOM   1470  CD  ARG A 220     -40.764   3.442  78.210  1.00 13.78           C  
ANISOU 1470  CD  ARG A 220     1574   1757   1904    -44    105    244       C  
ATOM   1471  NE  ARG A 220     -41.238   4.614  78.952  1.00 13.09           N  
ANISOU 1471  NE  ARG A 220     1483   1684   1806    -40    105    247       N  
ATOM   1472  CZ  ARG A 220     -42.381   5.242  78.695  1.00 27.12           C  
ANISOU 1472  CZ  ARG A 220     3251   3477   3578    -42    108    242       C  
ATOM   1473  NH1 ARG A 220     -43.146   4.854  77.682  1.00 18.21           N  
ANISOU 1473  NH1 ARG A 220     2114   2353   2452    -49    108    234       N  
ATOM   1474  NH2 ARG A 220     -42.740   6.297  79.412  1.00 14.83           N  
ANISOU 1474  NH2 ARG A 220     1691   1929   2013    -36    110    244       N  
ATOM   1475  N   LEU A 221     -42.665  -1.633  78.784  1.00 10.31           N  
ANISOU 1475  N   LEU A 221     1153   1271   1493    -98    122    247       N  
ATOM   1476  CA  LEU A 221     -42.003  -2.904  79.111  1.00 10.66           C  
ANISOU 1476  CA  LEU A 221     1212   1289   1550   -100    123    255       C  
ATOM   1477  C   LEU A 221     -42.368  -4.050  78.126  1.00 15.74           C  
ANISOU 1477  C   LEU A 221     1858   1917   2205   -113    127    241       C  
ATOM   1478  O   LEU A 221     -42.148  -5.221  78.448  1.00 15.96           O  
ANISOU 1478  O   LEU A 221     1899   1921   2245   -119    130    247       O  
ATOM   1479  CB  LEU A 221     -42.345  -3.326  80.566  1.00 10.69           C  
ANISOU 1479  CB  LEU A 221     1223   1287   1551   -109    127    273       C  
ATOM   1480  CG  LEU A 221     -42.180  -2.240  81.646  1.00 14.75           C  
ANISOU 1480  CG  LEU A 221     1737   1818   2050   -100    124    284       C  
ATOM   1481  CD1 LEU A 221     -42.580  -2.770  83.016  1.00 15.10           C  
ANISOU 1481  CD1 LEU A 221     1792   1858   2088   -111    130    302       C  
ATOM   1482  CD2 LEU A 221     -40.763  -1.712  81.679  1.00 15.08           C  
ANISOU 1482  CD2 LEU A 221     1781   1854   2092    -81    114    288       C  
ATOM   1483  N   THR A 222     -42.873  -3.710  76.912  1.00 12.23           N  
ANISOU 1483  N   THR A 222     1405   1484   1756   -117    125    224       N  
ATOM   1484  CA  THR A 222     -43.259  -4.743  75.921  1.00 12.53           C  
ANISOU 1484  CA  THR A 222     1449   1510   1803   -131    127    208       C  
ATOM   1485  C   THR A 222     -42.073  -5.640  75.511  1.00 16.71           C  
ANISOU 1485  C   THR A 222     1993   2010   2344   -123    130    204       C  
ATOM   1486  O   THR A 222     -42.280  -6.792  75.139  1.00 16.91           O  
ANISOU 1486  O   THR A 222     2029   2016   2381   -135    134    195       O  
ATOM   1487  CB  THR A 222     -43.912  -4.106  74.686  1.00 16.70           C  
ANISOU 1487  CB  THR A 222     1967   2059   2320   -136    122    191       C  
ATOM   1488  OG1 THR A 222     -43.018  -3.153  74.124  1.00 14.91           O  
ANISOU 1488  OG1 THR A 222     1739   1840   2085   -117    119    188       O  
ATOM   1489  CG2 THR A 222     -45.240  -3.462  74.997  1.00 15.55           C  
ANISOU 1489  CG2 THR A 222     1804   1938   2167   -146    118    194       C  
ATOM   1490  N   GLU A 223     -40.842  -5.093  75.535  1.00 12.77           N  
ANISOU 1490  N   GLU A 223     1496   1511   1848   -101    129    208       N  
ATOM   1491  CA  GLU A 223     -39.660  -5.825  75.062  1.00 11.78           C  
ANISOU 1491  CA  GLU A 223     1379   1359   1736    -89    134    203       C  
ATOM   1492  C   GLU A 223     -38.893  -6.505  76.207  1.00 14.46           C  
ANISOU 1492  C   GLU A 223     1727   1677   2092    -81    134    223       C  
ATOM   1493  O   GLU A 223     -38.405  -7.623  76.037  1.00 14.89           O  
ANISOU 1493  O   GLU A 223     1792   1703   2163    -79    139    220       O  
ATOM   1494  CB  GLU A 223     -38.723  -4.890  74.261  1.00 12.71           C  
ANISOU 1494  CB  GLU A 223     1492   1488   1849    -72    135    196       C  
ATOM   1495  CG  GLU A 223     -39.442  -4.056  73.204  1.00 20.70           C  
ANISOU 1495  CG  GLU A 223     2498   2525   2844    -78    133    181       C  
ATOM   1496  CD  GLU A 223     -40.270  -4.863  72.225  1.00 35.02           C  
ANISOU 1496  CD  GLU A 223     4319   4334   4655    -96    135    162       C  
ATOM   1497  OE1 GLU A 223     -39.677  -5.642  71.449  1.00 19.91           O  
ANISOU 1497  OE1 GLU A 223     2417   2400   2748    -94    143    148       O  
ATOM   1498  OE2 GLU A 223     -41.515  -4.735  72.254  1.00 32.30           O  
ANISOU 1498  OE2 GLU A 223     3968   4004   4301   -113    129    160       O  
ATOM   1499  N   VAL A 224     -38.753  -5.816  77.357  1.00 10.16           N  
ANISOU 1499  N   VAL A 224     1178   1144   1540    -75    127    242       N  
ATOM   1500  CA  VAL A 224     -37.955  -6.328  78.478  1.00  9.71           C  
ANISOU 1500  CA  VAL A 224     1127   1068   1494    -66    123    263       C  
ATOM   1501  C   VAL A 224     -38.738  -7.337  79.363  1.00 13.75           C  
ANISOU 1501  C   VAL A 224     1650   1565   2008    -83    125    275       C  
ATOM   1502  O   VAL A 224     -38.140  -8.268  79.906  1.00 13.70           O  
ANISOU 1502  O   VAL A 224     1655   1533   2017    -78    123    289       O  
ATOM   1503  CB  VAL A 224     -37.323  -5.173  79.318  1.00 12.91           C  
ANISOU 1503  CB  VAL A 224     1525   1491   1889    -53    113    277       C  
ATOM   1504  CG1 VAL A 224     -38.395  -4.400  80.098  1.00 12.49           C  
ANISOU 1504  CG1 VAL A 224     1469   1461   1815    -65    112    283       C  
ATOM   1505  CG2 VAL A 224     -36.244  -5.706  80.256  1.00 12.78           C  
ANISOU 1505  CG2 VAL A 224     1514   1455   1886    -41    105    297       C  
ATOM   1506  N   ASP A 225     -40.062  -7.136  79.520  1.00  9.64           N  
ANISOU 1506  N   ASP A 225     1126   1061   1474   -102    128    273       N  
ATOM   1507  CA  ASP A 225     -40.867  -8.006  80.371  1.00  9.01           C  
ANISOU 1507  CA  ASP A 225     1056    970   1396   -121    132    285       C  
ATOM   1508  C   ASP A 225     -42.328  -7.991  79.938  1.00 11.55           C  
ANISOU 1508  C   ASP A 225     1370   1307   1711   -143    139    273       C  
ATOM   1509  O   ASP A 225     -43.110  -7.170  80.426  1.00 10.73           O  
ANISOU 1509  O   ASP A 225     1256   1229   1593   -149    140    277       O  
ATOM   1510  CB  ASP A 225     -40.729  -7.587  81.860  1.00 10.85           C  
ANISOU 1510  CB  ASP A 225     1293   1211   1618   -117    128    310       C  
ATOM   1511  CG  ASP A 225     -41.259  -8.614  82.856  1.00 14.30           C  
ANISOU 1511  CG  ASP A 225     1746   1632   2057   -134    133    328       C  
ATOM   1512  OD1 ASP A 225     -42.039  -9.495  82.442  1.00 13.83           O  
ANISOU 1512  OD1 ASP A 225     1688   1559   2006   -152    141    321       O  
ATOM   1513  OD2 ASP A 225     -40.911  -8.513  84.051  1.00 17.36           O  
ANISOU 1513  OD2 ASP A 225     2141   2018   2435   -130    128    350       O  
ATOM   1514  N   GLN A 226     -42.708  -8.926  79.030  1.00  8.58           N  
ANISOU 1514  N   GLN A 226      998    914   1347   -157    143    257       N  
ATOM   1515  CA  GLN A 226     -44.087  -9.038  78.530  1.00  8.36           C  
ANISOU 1515  CA  GLN A 226      962    899   1316   -181    146    244       C  
ATOM   1516  C   GLN A 226     -45.068  -9.402  79.644  1.00 13.54           C  
ANISOU 1516  C   GLN A 226     1617   1556   1970   -201    153    261       C  
ATOM   1517  O   GLN A 226     -46.216  -8.968  79.609  1.00 13.02           O  
ANISOU 1517  O   GLN A 226     1536   1514   1897   -215    155    256       O  
ATOM   1518  CB  GLN A 226     -44.179 -10.075  77.393  1.00  9.86           C  
ANISOU 1518  CB  GLN A 226     1160   1067   1519   -192    148    224       C  
ATOM   1519  CG  GLN A 226     -43.540  -9.626  76.086  1.00 21.10           C  
ANISOU 1519  CG  GLN A 226     2582   2496   2940   -178    144    203       C  
ATOM   1520  CD  GLN A 226     -42.065  -9.917  76.041  1.00 38.77           C  
ANISOU 1520  CD  GLN A 226     4832   4712   5189   -155    146    206       C  
ATOM   1521  OE1 GLN A 226     -41.518 -10.614  76.897  1.00 31.38           O  
ANISOU 1521  OE1 GLN A 226     3907   3752   4266   -149    148    223       O  
ATOM   1522  NE2 GLN A 226     -41.400  -9.441  74.999  1.00 37.02           N  
ANISOU 1522  NE2 GLN A 226     4608   4496   4963   -141    146    190       N  
ATOM   1523  N   GLU A 227     -44.639 -10.258  80.602  1.00 10.11           N  
ANISOU 1523  N   GLU A 227     1201   1098   1545   -202    156    281       N  
ATOM   1524  CA  GLU A 227     -45.512 -10.680  81.699  1.00  9.45           C  
ANISOU 1524  CA  GLU A 227     1120   1013   1457   -222    165    299       C  
ATOM   1525  C   GLU A 227     -45.934  -9.481  82.576  1.00 13.46           C  
ANISOU 1525  C   GLU A 227     1616   1554   1945   -218    167    309       C  
ATOM   1526  O   GLU A 227     -47.116  -9.328  82.876  1.00 12.94           O  
ANISOU 1526  O   GLU A 227     1538   1505   1874   -236    176    309       O  
ATOM   1527  CB  GLU A 227     -44.837 -11.763  82.551  1.00 10.67           C  
ANISOU 1527  CB  GLU A 227     1298   1134   1622   -221    166    320       C  
ATOM   1528  CG  GLU A 227     -45.752 -12.328  83.630  1.00 23.09           C  
ANISOU 1528  CG  GLU A 227     2878   2704   3192   -245    177    340       C  
ATOM   1529  CD  GLU A 227     -45.206 -13.525  84.385  1.00 45.64           C  
ANISOU 1529  CD  GLU A 227     5760   5523   6060   -247    178    363       C  
ATOM   1530  OE1 GLU A 227     -44.006 -13.843  84.217  1.00 44.01           O  
ANISOU 1530  OE1 GLU A 227     5564   5294   5864   -225    168    366       O  
ATOM   1531  OE2 GLU A 227     -45.983 -14.150  85.140  1.00 36.70           O  
ANISOU 1531  OE2 GLU A 227     4636   4383   4927   -270    188    378       O  
ATOM   1532  N   LYS A 228     -44.968  -8.618  82.952  1.00  9.91           N  
ANISOU 1532  N   LYS A 228     1168   1113   1484   -194    160    315       N  
ATOM   1533  CA  LYS A 228     -45.262  -7.431  83.758  1.00  9.28           C  
ANISOU 1533  CA  LYS A 228     1079   1062   1384   -188    162    322       C  
ATOM   1534  C   LYS A 228     -45.996  -6.365  82.916  1.00 12.16           C  
ANISOU 1534  C   LYS A 228     1421   1456   1743   -187    162    303       C  
ATOM   1535  O   LYS A 228     -46.948  -5.751  83.398  1.00  9.70           O  
ANISOU 1535  O   LYS A 228     1098   1166   1422   -195    171    304       O  
ATOM   1536  CB  LYS A 228     -43.973  -6.858  84.371  1.00 10.84           C  
ANISOU 1536  CB  LYS A 228     1287   1258   1573   -165    151    334       C  
ATOM   1537  CG  LYS A 228     -44.220  -5.767  85.425  1.00 15.55           C  
ANISOU 1537  CG  LYS A 228     1882   1879   2147   -161    154    343       C  
ATOM   1538  CD  LYS A 228     -43.005  -5.573  86.338  1.00 20.52           C  
ANISOU 1538  CD  LYS A 228     2528   2502   2768   -146    143    360       C  
ATOM   1539  CE  LYS A 228     -42.781  -6.767  87.252  1.00 37.48           C  
ANISOU 1539  CE  LYS A 228     4697   4627   4917   -155    143    384       C  
ATOM   1540  NZ  LYS A 228     -41.630  -6.558  88.164  1.00 50.76           N  
ANISOU 1540  NZ  LYS A 228     6394   6304   6589   -140    128    402       N  
ATOM   1541  N   CYS A 229     -45.579  -6.190  81.639  1.00  9.77           N  
ANISOU 1541  N   CYS A 229     1112   1152   1448   -178    154    285       N  
ATOM   1542  CA  CYS A 229     -46.245  -5.255  80.703  1.00  9.69           C  
ANISOU 1542  CA  CYS A 229     1082   1167   1433   -177    151    267       C  
ATOM   1543  C   CYS A 229     -47.759  -5.546  80.609  1.00 14.89           C  
ANISOU 1543  C   CYS A 229     1726   1838   2096   -201    158    262       C  
ATOM   1544  O   CYS A 229     -48.580  -4.652  80.840  1.00 13.94           O  
ANISOU 1544  O   CYS A 229     1588   1742   1967   -201    162    261       O  
ATOM   1545  CB  CYS A 229     -45.579  -5.303  79.324  1.00  9.50           C  
ANISOU 1545  CB  CYS A 229     1058   1136   1415   -167    142    250       C  
ATOM   1546  SG  CYS A 229     -46.654  -4.784  77.956  1.00 13.16           S  
ANISOU 1546  SG  CYS A 229     1502   1622   1876   -177    137    228       S  
ATOM   1547  N   ILE A 230     -48.115  -6.807  80.318  1.00 13.09           N  
ANISOU 1547  N   ILE A 230     1504   1590   1881   -221    161    259       N  
ATOM   1548  CA  ILE A 230     -49.506  -7.232  80.160  1.00 13.04           C  
ANISOU 1548  CA  ILE A 230     1482   1592   1882   -247    167    254       C  
ATOM   1549  C   ILE A 230     -50.276  -7.200  81.501  1.00 18.12           C  
ANISOU 1549  C   ILE A 230     2121   2244   2521   -259    182    272       C  
ATOM   1550  O   ILE A 230     -51.416  -6.741  81.537  1.00 18.42           O  
ANISOU 1550  O   ILE A 230     2136   2305   2558   -269    188    269       O  
ATOM   1551  CB  ILE A 230     -49.568  -8.627  79.474  1.00 16.05           C  
ANISOU 1551  CB  ILE A 230     1875   1945   2279   -267    165    245       C  
ATOM   1552  CG1 ILE A 230     -48.962  -8.560  78.046  1.00 15.83           C  
ANISOU 1552  CG1 ILE A 230     1850   1912   2251   -257    152    224       C  
ATOM   1553  CG2 ILE A 230     -51.011  -9.171  79.447  1.00 16.58           C  
ANISOU 1553  CG2 ILE A 230     1926   2019   2356   -298    171    242       C  
ATOM   1554  CD1 ILE A 230     -48.643  -9.930  77.418  1.00 22.56           C  
ANISOU 1554  CD1 ILE A 230     2722   2732   3119   -269    151    214       C  
ATOM   1555  N   ALA A 231     -49.630  -7.641  82.604  1.00 15.17           N  
ANISOU 1555  N   ALA A 231     1769   1853   2143   -256    189    291       N  
ATOM   1556  CA  ALA A 231     -50.266  -7.645  83.931  1.00 15.68           C  
ANISOU 1556  CA  ALA A 231     1834   1925   2198   -267    205    309       C  
ATOM   1557  C   ALA A 231     -50.586  -6.217  84.406  1.00 19.33           C  
ANISOU 1557  C   ALA A 231     2282   2419   2644   -253    210    309       C  
ATOM   1558  O   ALA A 231     -51.676  -5.973  84.924  1.00 18.91           O  
ANISOU 1558  O   ALA A 231     2213   2383   2588   -265    226    312       O  
ATOM   1559  CB  ALA A 231     -49.371  -8.345  84.941  1.00 16.60           C  
ANISOU 1559  CB  ALA A 231     1979   2016   2310   -264    207    331       C  
ATOM   1560  N   GLU A 232     -49.647  -5.269  84.200  1.00 15.44           N  
ANISOU 1560  N   GLU A 232     1792   1932   2142   -227    199    305       N  
ATOM   1561  CA  GLU A 232     -49.857  -3.875  84.604  1.00 15.18           C  
ANISOU 1561  CA  GLU A 232     1748   1926   2094   -212    203    303       C  
ATOM   1562  C   GLU A 232     -50.849  -3.155  83.677  1.00 19.22           C  
ANISOU 1562  C   GLU A 232     2230   2461   2613   -212    202    286       C  
ATOM   1563  O   GLU A 232     -51.649  -2.347  84.148  1.00 19.71           O  
ANISOU 1563  O   GLU A 232     2276   2543   2669   -210    213    286       O  
ATOM   1564  CB  GLU A 232     -48.525  -3.114  84.679  1.00 16.20           C  
ANISOU 1564  CB  GLU A 232     1891   2052   2213   -186    190    304       C  
ATOM   1565  CG  GLU A 232     -47.599  -3.604  85.792  1.00 25.19           C  
ANISOU 1565  CG  GLU A 232     3056   3173   3342   -184    189    323       C  
ATOM   1566  CD  GLU A 232     -48.116  -3.404  87.209  1.00 45.00           C  
ANISOU 1566  CD  GLU A 232     5574   5692   5833   -191    205    337       C  
ATOM   1567  OE1 GLU A 232     -49.016  -2.555  87.403  1.00 42.22           O  
ANISOU 1567  OE1 GLU A 232     5206   5363   5474   -192    217    330       O  
ATOM   1568  OE2 GLU A 232     -47.556  -4.032  88.136  1.00 41.15           O  
ANISOU 1568  OE2 GLU A 232     5109   5189   5337   -194    204    355       O  
ATOM   1569  N   ALA A 233     -50.832  -3.488  82.369  1.00 15.30           N  
ANISOU 1569  N   ALA A 233     1726   1959   2128   -215    188    272       N  
ATOM   1570  CA  ALA A 233     -51.774  -2.904  81.406  1.00 14.70           C  
ANISOU 1570  CA  ALA A 233     1623   1904   2059   -217    183    257       C  
ATOM   1571  C   ALA A 233     -53.194  -3.408  81.655  1.00 20.12           C  
ANISOU 1571  C   ALA A 233     2289   2601   2756   -242    195    259       C  
ATOM   1572  O   ALA A 233     -54.143  -2.633  81.555  1.00 20.94           O  
ANISOU 1572  O   ALA A 233     2365   2728   2862   -240    199    254       O  
ATOM   1573  CB  ALA A 233     -51.346  -3.227  79.989  1.00 15.12           C  
ANISOU 1573  CB  ALA A 233     1677   1948   2118   -216    165    243       C  
ATOM   1574  N   ASN A 234     -53.342  -4.718  82.010  1.00 16.69           N  
ANISOU 1574  N   ASN A 234     1865   2146   2329   -265    203    266       N  
ATOM   1575  CA  ASN A 234     -54.656  -5.293  82.353  1.00 16.80           C  
ANISOU 1575  CA  ASN A 234     1861   2168   2356   -292    217    269       C  
ATOM   1576  C   ASN A 234     -55.226  -4.636  83.607  1.00 19.83           C  
ANISOU 1576  C   ASN A 234     2235   2568   2730   -289    239    281       C  
ATOM   1577  O   ASN A 234     -56.419  -4.361  83.668  1.00 18.08           O  
ANISOU 1577  O   ASN A 234     1985   2368   2517   -300    250    278       O  
ATOM   1578  CB  ASN A 234     -54.559  -6.818  82.546  1.00 18.84           C  
ANISOU 1578  CB  ASN A 234     2138   2397   2624   -317    221    276       C  
ATOM   1579  CG  ASN A 234     -54.632  -7.605  81.255  1.00 32.16           C  
ANISOU 1579  CG  ASN A 234     3823   4070   4325   -331    204    260       C  
ATOM   1580  OD1 ASN A 234     -55.397  -7.280  80.341  1.00 20.48           O  
ANISOU 1580  OD1 ASN A 234     2319   2609   2853   -337    194    245       O  
ATOM   1581  ND2 ASN A 234     -53.954  -8.740  81.220  1.00 22.94           N  
ANISOU 1581  ND2 ASN A 234     2683   2871   3164   -340    202    263       N  
ATOM   1582  N   ALA A 235     -54.363  -4.361  84.604  1.00 17.38           N  
ANISOU 1582  N   ALA A 235     1951   2252   2402   -275    246    293       N  
ATOM   1583  CA  ALA A 235     -54.785  -3.685  85.831  1.00 17.75           C  
ANISOU 1583  CA  ALA A 235     1995   2315   2436   -271    268    303       C  
ATOM   1584  C   ALA A 235     -55.219  -2.244  85.535  1.00 22.45           C  
ANISOU 1584  C   ALA A 235     2566   2936   3029   -250    267    291       C  
ATOM   1585  O   ALA A 235     -56.175  -1.753  86.136  1.00 23.19           O  
ANISOU 1585  O   ALA A 235     2640   3048   3121   -253    288    293       O  
ATOM   1586  CB  ALA A 235     -53.653  -3.694  86.849  1.00 18.35           C  
ANISOU 1586  CB  ALA A 235     2106   2376   2491   -259    269    317       C  
ATOM   1587  N   ALA A 236     -54.546  -1.585  84.566  1.00 18.23           N  
ANISOU 1587  N   ALA A 236     2031   2403   2494   -230    245    280       N  
ATOM   1588  CA  ALA A 236     -54.875  -0.216  84.176  1.00 17.96           C  
ANISOU 1588  CA  ALA A 236     1976   2390   2458   -209    242    270       C  
ATOM   1589  C   ALA A 236     -56.196  -0.156  83.395  1.00 22.63           C  
ANISOU 1589  C   ALA A 236     2530   3000   3070   -219    241    261       C  
ATOM   1590  O   ALA A 236     -57.011   0.726  83.641  1.00 22.43           O  
ANISOU 1590  O   ALA A 236     2480   2994   3047   -211    252    259       O  
ATOM   1591  CB  ALA A 236     -53.743   0.380  83.342  1.00 18.09           C  
ANISOU 1591  CB  ALA A 236     2005   2400   2469   -188    219    263       C  
ATOM   1592  N   ILE A 237     -56.406  -1.101  82.460  1.00 19.80           N  
ANISOU 1592  N   ILE A 237     2165   2633   2724   -238    227    256       N  
ATOM   1593  CA  ILE A 237     -57.629  -1.139  81.642  1.00 19.74           C  
ANISOU 1593  CA  ILE A 237     2122   2643   2736   -251    221    247       C  
ATOM   1594  C   ILE A 237     -58.853  -1.620  82.468  1.00 24.11           C  
ANISOU 1594  C   ILE A 237     2653   3206   3301   -274    245    255       C  
ATOM   1595  O   ILE A 237     -59.971  -1.161  82.231  1.00 23.54           O  
ANISOU 1595  O   ILE A 237     2545   3156   3244   -276    248    250       O  
ATOM   1596  CB  ILE A 237     -57.409  -2.004  80.347  1.00 23.04           C  
ANISOU 1596  CB  ILE A 237     2544   3049   3162   -265    196    237       C  
ATOM   1597  CG1 ILE A 237     -56.209  -1.458  79.505  1.00 22.56           C  
ANISOU 1597  CG1 ILE A 237     2503   2980   3088   -242    176    230       C  
ATOM   1598  CG2 ILE A 237     -58.705  -2.079  79.495  1.00 24.45           C  
ANISOU 1598  CG2 ILE A 237     2685   3247   3359   -281    186    228       C  
ATOM   1599  CD1 ILE A 237     -55.760  -2.374  78.373  1.00 25.69           C  
ANISOU 1599  CD1 ILE A 237     2913   3360   3488   -255    157    220       C  
ATOM   1600  N   SER A 238     -58.624  -2.505  83.461  1.00 21.42           N  
ANISOU 1600  N   SER A 238     2334   2849   2955   -290    263    267       N  
ATOM   1601  CA  SER A 238     -59.714  -3.066  84.275  1.00 22.23           C  
ANISOU 1601  CA  SER A 238     2420   2959   3068   -315    289    275       C  
ATOM   1602  C   SER A 238     -60.053  -2.181  85.490  1.00 27.35           C  
ANISOU 1602  C   SER A 238     3063   3623   3704   -301    318    282       C  
ATOM   1603  O   SER A 238     -61.086  -2.395  86.135  1.00 27.82           O  
ANISOU 1603  O   SER A 238     3102   3694   3773   -318    343    288       O  
ATOM   1604  CB  SER A 238     -59.365  -4.479  84.738  1.00 25.77           C  
ANISOU 1604  CB  SER A 238     2895   3380   3516   -341    296    286       C  
ATOM   1605  OG  SER A 238     -59.084  -5.327  83.636  1.00 34.69           O  
ANISOU 1605  OG  SER A 238     4030   4493   4656   -353    272    277       O  
ATOM   1606  N   SER A 239     -59.174  -1.200  85.815  1.00 23.34           N  
ANISOU 1606  N   SER A 239     2576   3115   3177   -272    315    281       N  
ATOM   1607  CA  SER A 239     -59.370  -0.324  86.983  1.00 22.72           C  
ANISOU 1607  CA  SER A 239     2500   3049   3084   -258    342    286       C  
ATOM   1608  C   SER A 239     -60.722   0.421  86.937  1.00 27.57           C  
ANISOU 1608  C   SER A 239     3070   3691   3716   -254    358    279       C  
ATOM   1609  O   SER A 239     -61.064   1.033  85.919  1.00 26.78           O  
ANISOU 1609  O   SER A 239     2942   3602   3630   -242    340    268       O  
ATOM   1610  CB  SER A 239     -58.227   0.675  87.103  1.00 24.07           C  
ANISOU 1610  CB  SER A 239     2696   3215   3233   -228    331    282       C  
ATOM   1611  OG  SER A 239     -58.411   1.525  88.222  1.00 28.69           O  
ANISOU 1611  OG  SER A 239     3286   3812   3804   -216    356    284       O  
ATOM   1612  N   PRO A 240     -61.471   0.445  88.073  1.00 24.73           N  
ANISOU 1612  N   PRO A 240     2702   3341   3352   -263    394    285       N  
ATOM   1613  CA  PRO A 240     -62.750   1.183  88.090  1.00 24.68           C  
ANISOU 1613  CA  PRO A 240     2651   3360   3365   -257    413    279       C  
ATOM   1614  C   PRO A 240     -62.550   2.705  88.054  1.00 28.33           C  
ANISOU 1614  C   PRO A 240     3110   3832   3820   -220    411    269       C  
ATOM   1615  O   PRO A 240     -63.502   3.448  87.794  1.00 27.85           O  
ANISOU 1615  O   PRO A 240     3011   3792   3780   -208    419    262       O  
ATOM   1616  CB  PRO A 240     -63.398   0.731  89.398  1.00 26.73           C  
ANISOU 1616  CB  PRO A 240     2912   3625   3618   -276    455    289       C  
ATOM   1617  CG  PRO A 240     -62.265   0.354  90.272  1.00 31.26           C  
ANISOU 1617  CG  PRO A 240     3538   4178   4159   -278    458    300       C  
ATOM   1618  CD  PRO A 240     -61.199  -0.208  89.372  1.00 26.50           C  
ANISOU 1618  CD  PRO A 240     2959   3555   3556   -278    419    300       C  
ATOM   1619  N   ALA A 241     -61.302   3.171  88.307  1.00 24.49           N  
ANISOU 1619  N   ALA A 241     2663   3332   3308   -202    400    268       N  
ATOM   1620  CA  ALA A 241     -60.965   4.599  88.278  1.00 24.27           C  
ANISOU 1620  CA  ALA A 241     2639   3310   3274   -168    397    259       C  
ATOM   1621  C   ALA A 241     -61.056   5.166  86.852  1.00 26.99           C  
ANISOU 1621  C   ALA A 241     2958   3659   3637   -153    366    250       C  
ATOM   1622  O   ALA A 241     -61.297   6.365  86.673  1.00 26.22           O  
ANISOU 1622  O   ALA A 241     2847   3571   3546   -127    366    243       O  
ATOM   1623  CB  ALA A 241     -59.567   4.814  88.835  1.00 25.02           C  
ANISOU 1623  CB  ALA A 241     2781   3386   3337   -158    389    261       C  
ATOM   1624  N   GLY A 242     -60.853   4.299  85.856  1.00 22.03           N  
ANISOU 1624  N   GLY A 242     2328   3024   3019   -169    339    252       N  
ATOM   1625  CA  GLY A 242     -60.929   4.683  84.453  1.00 20.90           C  
ANISOU 1625  CA  GLY A 242     2164   2886   2891   -158    307    245       C  
ATOM   1626  C   GLY A 242     -59.655   5.310  83.933  1.00 22.13           C  
ANISOU 1626  C   GLY A 242     2349   3028   3030   -137    284    241       C  
ATOM   1627  O   GLY A 242     -58.701   5.501  84.685  1.00 19.97           O  
ANISOU 1627  O   GLY A 242     2110   2743   2736   -130    291    244       O  
ATOM   1628  N   LEU A 243     -59.632   5.631  82.630  1.00 18.99           N  
ANISOU 1628  N   LEU A 243     1938   2634   2642   -129    255    236       N  
ATOM   1629  CA  LEU A 243     -58.473   6.260  81.980  1.00 18.72           C  
ANISOU 1629  CA  LEU A 243     1929   2589   2595   -110    233    233       C  
ATOM   1630  C   LEU A 243     -58.882   7.618  81.384  1.00 22.53           C  
ANISOU 1630  C   LEU A 243     2391   3084   3087    -83    224    229       C  
ATOM   1631  O   LEU A 243     -60.056   7.992  81.454  1.00 22.70           O  
ANISOU 1631  O   LEU A 243     2377   3122   3126    -79    233    228       O  
ATOM   1632  CB  LEU A 243     -57.937   5.337  80.853  1.00 18.65           C  
ANISOU 1632  CB  LEU A 243     1930   2571   2586   -125    206    231       C  
ATOM   1633  CG  LEU A 243     -57.516   3.925  81.278  1.00 23.35           C  
ANISOU 1633  CG  LEU A 243     2546   3150   3176   -151    212    235       C  
ATOM   1634  CD1 LEU A 243     -57.634   2.954  80.125  1.00 23.60           C  
ANISOU 1634  CD1 LEU A 243     2573   3178   3217   -170    190    231       C  
ATOM   1635  CD2 LEU A 243     -56.117   3.919  81.832  1.00 25.52           C  
ANISOU 1635  CD2 LEU A 243     2859   3405   3430   -142    213    239       C  
ATOM   1636  N   ILE A 244     -57.935   8.317  80.720  1.00 18.58           N  
ANISOU 1636  N   ILE A 244     1909   2575   2576    -66    204    227       N  
ATOM   1637  CA  ILE A 244     -58.267   9.542  79.983  1.00 18.39           C  
ANISOU 1637  CA  ILE A 244     1868   2560   2561    -41    191    225       C  
ATOM   1638  C   ILE A 244     -58.989   9.156  78.677  1.00 23.29           C  
ANISOU 1638  C   ILE A 244     2461   3192   3195    -51    166    225       C  
ATOM   1639  O   ILE A 244     -58.338   8.851  77.668  1.00 22.59           O  
ANISOU 1639  O   ILE A 244     2387   3098   3099    -56    142    223       O  
ATOM   1640  CB  ILE A 244     -56.999  10.427  79.742  1.00 21.08           C  
ANISOU 1640  CB  ILE A 244     2239   2885   2885    -22    180    224       C  
ATOM   1641  CG1 ILE A 244     -56.362  10.860  81.103  1.00 21.26           C  
ANISOU 1641  CG1 ILE A 244     2287   2898   2893    -14    203    224       C  
ATOM   1642  CG2 ILE A 244     -57.337  11.656  78.867  1.00 21.84           C  
ANISOU 1642  CG2 ILE A 244     2319   2988   2990      2    164    224       C  
ATOM   1643  CD1 ILE A 244     -55.024  11.657  80.976  1.00 27.68           C  
ANISOU 1643  CD1 ILE A 244     3131   3695   3690      1    192    223       C  
ATOM   1644  N   SER A 245     -60.324   8.995  78.762  1.00 21.42           N  
ANISOU 1644  N   SER A 245     2185   2973   2979    -57    173    225       N  
ATOM   1645  CA  SER A 245     -61.139   8.435  77.680  1.00 21.86           C  
ANISOU 1645  CA  SER A 245     2214   3043   3051    -73    150    225       C  
ATOM   1646  C   SER A 245     -61.726   9.506  76.759  1.00 25.92           C  
ANISOU 1646  C   SER A 245     2701   3569   3576    -50    128    227       C  
ATOM   1647  O   SER A 245     -62.222   9.177  75.680  1.00 25.74           O  
ANISOU 1647  O   SER A 245     2661   3559   3562    -60    102    227       O  
ATOM   1648  CB  SER A 245     -62.252   7.567  78.254  1.00 25.87           C  
ANISOU 1648  CB  SER A 245     2692   3562   3577    -96    167    225       C  
ATOM   1649  OG  SER A 245     -63.011   8.287  79.213  1.00 35.58           O  
ANISOU 1649  OG  SER A 245     3898   4801   4819    -81    195    227       O  
ATOM   1650  N   ASP A 246     -61.711  10.779  77.193  1.00 22.92           N  
ANISOU 1650  N   ASP A 246     2320   3189   3199    -20    140    229       N  
ATOM   1651  CA  ASP A 246     -62.214  11.880  76.359  1.00 22.69           C  
ANISOU 1651  CA  ASP A 246     2269   3170   3182      4    120    233       C  
ATOM   1652  C   ASP A 246     -61.421  13.175  76.593  1.00 24.87           C  
ANISOU 1652  C   ASP A 246     2570   3431   3447     34    125    234       C  
ATOM   1653  O   ASP A 246     -60.649  13.262  77.551  1.00 24.28           O  
ANISOU 1653  O   ASP A 246     2524   3342   3359     36    148    231       O  
ATOM   1654  CB  ASP A 246     -63.740  12.103  76.581  1.00 25.05           C  
ANISOU 1654  CB  ASP A 246     2516   3489   3512      9    128    236       C  
ATOM   1655  CG  ASP A 246     -64.092  12.838  77.865  1.00 35.62           C  
ANISOU 1655  CG  ASP A 246     3847   4826   4860     29    166    234       C  
ATOM   1656  OD1 ASP A 246     -63.421  12.599  78.887  1.00 36.23           O  
ANISOU 1656  OD1 ASP A 246     3954   4892   4922     23    192    230       O  
ATOM   1657  OD2 ASP A 246     -65.091  13.588  77.863  1.00 41.18           O  
ANISOU 1657  OD2 ASP A 246     4515   5543   5590     49    169    237       O  
ATOM   1658  N   LYS A 247     -61.620  14.190  75.711  1.00 20.50           N  
ANISOU 1658  N   LYS A 247     2006   2881   2901     57    104    240       N  
ATOM   1659  CA  LYS A 247     -60.884  15.470  75.767  1.00 19.08           C  
ANISOU 1659  CA  LYS A 247     1850   2686   2714     85    105    242       C  
ATOM   1660  C   LYS A 247     -61.048  16.206  77.108  1.00 20.47           C  
ANISOU 1660  C   LYS A 247     2026   2855   2897    103    140    237       C  
ATOM   1661  O   LYS A 247     -60.178  16.990  77.485  1.00 19.45           O  
ANISOU 1661  O   LYS A 247     1927   2708   2755    118    148    235       O  
ATOM   1662  CB  LYS A 247     -61.285  16.383  74.588  1.00 21.53           C  
ANISOU 1662  CB  LYS A 247     2144   3002   3033    106     76    252       C  
ATOM   1663  CG  LYS A 247     -62.787  16.622  74.475  1.00 32.78           C  
ANISOU 1663  CG  LYS A 247     3519   4447   4489    116     73    256       C  
ATOM   1664  CD  LYS A 247     -63.137  17.397  73.213  1.00 40.63           C  
ANISOU 1664  CD  LYS A 247     4500   5447   5491    134     38    268       C  
ATOM   1665  CE  LYS A 247     -64.626  17.587  73.066  1.00 48.47           C  
ANISOU 1665  CE  LYS A 247     5439   6461   6517    144     31    274       C  
ATOM   1666  NZ  LYS A 247     -64.967  18.292  71.804  1.00 57.39           N  
ANISOU 1666  NZ  LYS A 247     6556   7597   7652    161     -7    288       N  
ATOM   1667  N   ALA A 248     -62.157  15.951  77.824  1.00 16.60           N  
ANISOU 1667  N   ALA A 248     1504   2379   2426    101    162    235       N  
ATOM   1668  CA  ALA A 248     -62.414  16.590  79.118  1.00 15.81           C  
ANISOU 1668  CA  ALA A 248     1403   2273   2331    117    199    229       C  
ATOM   1669  C   ALA A 248     -61.443  16.072  80.212  1.00 18.27           C  
ANISOU 1669  C   ALA A 248     1754   2572   2617    101    222    221       C  
ATOM   1670  O   ALA A 248     -61.229  16.753  81.220  1.00 18.30           O  
ANISOU 1670  O   ALA A 248     1774   2565   2615    115    247    215       O  
ATOM   1671  CB  ALA A 248     -63.853  16.349  79.540  1.00 16.69           C  
ANISOU 1671  CB  ALA A 248     1467   2404   2470    116    217    228       C  
ATOM   1672  N   ASP A 249     -60.847  14.883  79.994  1.00 12.97           N  
ANISOU 1672  N   ASP A 249     1100   1899   1931     73    211    223       N  
ATOM   1673  CA  ASP A 249     -59.935  14.271  80.967  1.00 12.75           C  
ANISOU 1673  CA  ASP A 249     1107   1859   1878     57    228    219       C  
ATOM   1674  C   ASP A 249     -58.457  14.622  80.677  1.00 17.18           C  
ANISOU 1674  C   ASP A 249     1709   2401   2418     61    212    219       C  
ATOM   1675  O   ASP A 249     -57.587  14.340  81.503  1.00 17.28           O  
ANISOU 1675  O   ASP A 249     1753   2402   2411     53    223    216       O  
ATOM   1676  CB  ASP A 249     -60.121  12.743  80.990  1.00 14.04           C  
ANISOU 1676  CB  ASP A 249     1265   2029   2041     24    228    221       C  
ATOM   1677  CG  ASP A 249     -61.537  12.295  81.311  1.00 18.75           C  
ANISOU 1677  CG  ASP A 249     1821   2644   2660     14    245    222       C  
ATOM   1678  OD1 ASP A 249     -62.244  13.031  82.043  1.00 18.02           O  
ANISOU 1678  OD1 ASP A 249     1711   2558   2578     31    270    219       O  
ATOM   1679  OD2 ASP A 249     -61.912  11.175  80.898  1.00 18.44           O  
ANISOU 1679  OD2 ASP A 249     1767   2612   2626    -11    235    224       O  
ATOM   1680  N   ASN A 250     -58.177  15.215  79.491  1.00 14.06           N  
ANISOU 1680  N   ASN A 250     1313   2003   2025     73    185    223       N  
ATOM   1681  CA  ASN A 250     -56.801  15.531  79.058  1.00 13.33           C  
ANISOU 1681  CA  ASN A 250     1256   1894   1914     76    169    224       C  
ATOM   1682  C   ASN A 250     -56.017  16.303  80.112  1.00 18.24           C  
ANISOU 1682  C   ASN A 250     1907   2500   2524     88    187    219       C  
ATOM   1683  O   ASN A 250     -56.547  17.232  80.715  1.00 19.31           O  
ANISOU 1683  O   ASN A 250     2035   2635   2667    106    204    215       O  
ATOM   1684  CB  ASN A 250     -56.812  16.298  77.738  1.00 12.17           C  
ANISOU 1684  CB  ASN A 250     1102   1747   1773     92    142    230       C  
ATOM   1685  CG  ASN A 250     -57.220  15.466  76.547  1.00 28.87           C  
ANISOU 1685  CG  ASN A 250     3200   3876   3892     76    118    234       C  
ATOM   1686  OD1 ASN A 250     -57.436  14.253  76.644  1.00 22.14           O  
ANISOU 1686  OD1 ASN A 250     2343   3031   3040     53    120    232       O  
ATOM   1687  ND2 ASN A 250     -57.275  16.090  75.385  1.00 19.60           N  
ANISOU 1687  ND2 ASN A 250     2022   2705   2721     88     94    241       N  
ATOM   1688  N   ALA A 251     -54.733  15.936  80.314  1.00 14.10           N  
ANISOU 1688  N   ALA A 251     1415   1963   1980     76    183    218       N  
ATOM   1689  CA  ALA A 251     -53.876  16.614  81.281  1.00 13.48           C  
ANISOU 1689  CA  ALA A 251     1365   1869   1887     84    195    213       C  
ATOM   1690  C   ALA A 251     -53.067  17.722  80.609  1.00 16.96           C  
ANISOU 1690  C   ALA A 251     1822   2297   2327    100    179    215       C  
ATOM   1691  O   ALA A 251     -52.337  17.464  79.645  1.00 15.58           O  
ANISOU 1691  O   ALA A 251     1654   2118   2147     94    159    220       O  
ATOM   1692  CB  ALA A 251     -52.944  15.614  81.946  1.00 13.91           C  
ANISOU 1692  CB  ALA A 251     1444   1918   1924     63    198    213       C  
ATOM   1693  N   TYR A 252     -53.239  18.966  81.078  1.00 14.17           N  
ANISOU 1693  N   TYR A 252     1472   1935   1977    120    190    210       N  
ATOM   1694  CA  TYR A 252     -52.510  20.113  80.546  1.00 13.43           C  
ANISOU 1694  CA  TYR A 252     1394   1826   1883    134    178    211       C  
ATOM   1695  C   TYR A 252     -51.760  20.829  81.658  1.00 15.40           C  
ANISOU 1695  C   TYR A 252     1672   2059   2121    138    191    203       C  
ATOM   1696  O   TYR A 252     -52.202  20.814  82.809  1.00 15.28           O  
ANISOU 1696  O   TYR A 252     1658   2045   2101    138    214    194       O  
ATOM   1697  CB  TYR A 252     -53.476  21.108  79.865  1.00 15.08           C  
ANISOU 1697  CB  TYR A 252     1580   2037   2112    158    174    215       C  
ATOM   1698  CG  TYR A 252     -54.358  20.498  78.801  1.00 16.77           C  
ANISOU 1698  CG  TYR A 252     1764   2269   2339    155    158    224       C  
ATOM   1699  CD1 TYR A 252     -53.874  20.267  77.516  1.00 18.79           C  
ANISOU 1699  CD1 TYR A 252     2023   2526   2591    149    133    233       C  
ATOM   1700  CD2 TYR A 252     -55.722  20.319  79.019  1.00 17.67           C  
ANISOU 1700  CD2 TYR A 252     1845   2398   2470    161    169    223       C  
ATOM   1701  CE1 TYR A 252     -54.703  19.786  76.504  1.00 19.01           C  
ANISOU 1701  CE1 TYR A 252     2025   2570   2627    146    116    240       C  
ATOM   1702  CE2 TYR A 252     -56.563  19.853  78.010  1.00 18.23           C  
ANISOU 1702  CE2 TYR A 252     1886   2486   2554    158    151    231       C  
ATOM   1703  CZ  TYR A 252     -56.047  19.580  76.756  1.00 23.21           C  
ANISOU 1703  CZ  TYR A 252     2523   3118   3177    150    123    239       C  
ATOM   1704  OH  TYR A 252     -56.867  19.108  75.764  1.00 23.04           O  
ANISOU 1704  OH  TYR A 252     2475   3114   3165    146    104    246       O  
HETATM 1705  N   MSE A 253     -50.681  21.538  81.306  1.00 10.13           N  
ANISOU 1705  N   MSE A 253     1026   1376   1448    141    179    204       N  
HETATM 1706  CA  MSE A 253     -50.004  22.424  82.247  1.00  8.95           C  
ANISOU 1706  CA  MSE A 253      903   1208   1288    146    188    195       C  
HETATM 1707  C   MSE A 253     -49.991  23.853  81.692  1.00 15.26           C  
ANISOU 1707  C   MSE A 253     1706   1992   2100    166    183    196       C  
HETATM 1708  O   MSE A 253     -49.255  24.147  80.746  1.00 15.11           O  
ANISOU 1708  O   MSE A 253     1695   1966   2083    165    165    204       O  
HETATM 1709  CB  MSE A 253     -48.574  21.938  82.539  1.00  9.53           C  
ANISOU 1709  CB  MSE A 253     1002   1275   1345    127    178    195       C  
HETATM 1710  CG  MSE A 253     -47.852  22.779  83.605  1.00 14.47           C  
ANISOU 1710  CG  MSE A 253     1655   1884   1959    127    186    185       C  
HETATM 1711 SE   MSE A 253     -48.693  22.669  85.382  0.75 20.04          SE  
ANISOU 1711 SE   MSE A 253     2368   2595   2652    127    217    170      SE  
HETATM 1712  CE  MSE A 253     -48.225  20.911  85.816  1.00 16.90           C  
ANISOU 1712  CE  MSE A 253     1973   2212   2237    100    212    177       C  
ATOM   1713  N   PRO A 254     -50.895  24.727  82.177  1.00 13.42           N  
ANISOU 1713  N   PRO A 254     1467   1755   1879    186    200    188       N  
ATOM   1714  CA  PRO A 254     -50.937  26.087  81.639  1.00 13.59           C  
ANISOU 1714  CA  PRO A 254     1492   1758   1914    207    195    190       C  
ATOM   1715  C   PRO A 254     -49.748  26.929  82.105  1.00 17.61           C  
ANISOU 1715  C   PRO A 254     2036   2244   2413    204    194    183       C  
ATOM   1716  O   PRO A 254     -49.346  26.858  83.267  1.00 16.55           O  
ANISOU 1716  O   PRO A 254     1920   2104   2263    194    207    170       O  
ATOM   1717  CB  PRO A 254     -52.266  26.635  82.166  1.00 15.30           C  
ANISOU 1717  CB  PRO A 254     1690   1976   2147    229    217    182       C  
ATOM   1718  CG  PRO A 254     -52.504  25.902  83.420  1.00 19.72           C  
ANISOU 1718  CG  PRO A 254     2253   2547   2693    217    239    170       C  
ATOM   1719  CD  PRO A 254     -51.884  24.535  83.261  1.00 15.05           C  
ANISOU 1719  CD  PRO A 254     1663   1970   2086    190    227    177       C  
ATOM   1720  N   PRO A 255     -49.136  27.716  81.199  1.00 15.36           N  
ANISOU 1720  N   PRO A 255     1759   1943   2134    209    178    192       N  
ATOM   1721  CA  PRO A 255     -48.055  28.603  81.637  1.00 15.02           C  
ANISOU 1721  CA  PRO A 255     1747   1876   2084    205    177    185       C  
ATOM   1722  C   PRO A 255     -48.612  29.837  82.353  1.00 19.06           C  
ANISOU 1722  C   PRO A 255     2268   2367   2605    226    195    172       C  
ATOM   1723  O   PRO A 255     -49.809  30.118  82.249  1.00 18.76           O  
ANISOU 1723  O   PRO A 255     2210   2333   2583    247    205    172       O  
ATOM   1724  CB  PRO A 255     -47.359  28.972  80.332  1.00 16.21           C  
ANISOU 1724  CB  PRO A 255     1901   2018   2240    204    156    201       C  
ATOM   1725  CG  PRO A 255     -48.437  28.936  79.306  1.00 20.77           C  
ANISOU 1725  CG  PRO A 255     2452   2607   2833    220    150    214       C  
ATOM   1726  CD  PRO A 255     -49.488  27.940  79.780  1.00 16.69           C  
ANISOU 1726  CD  PRO A 255     1911   2114   2317    220    161    209       C  
ATOM   1727  N   LYS A 256     -47.751  30.569  83.089  1.00 15.82           N  
ANISOU 1727  N   LYS A 256     1889   1936   2187    219    198    159       N  
ATOM   1728  CA  LYS A 256     -48.172  31.794  83.778  1.00 15.50           C  
ANISOU 1728  CA  LYS A 256     1863   1873   2155    238    216    144       C  
ATOM   1729  C   LYS A 256     -48.732  32.809  82.799  1.00 19.69           C  
ANISOU 1729  C   LYS A 256     2384   2388   2711    263    211    155       C  
ATOM   1730  O   LYS A 256     -49.808  33.366  83.039  1.00 18.81           O  
ANISOU 1730  O   LYS A 256     2262   2271   2615    287    228    149       O  
ATOM   1731  CB  LYS A 256     -47.007  32.410  84.564  1.00 17.48           C  
ANISOU 1731  CB  LYS A 256     2150   2102   2391    222    214    130       C  
ATOM   1732  CG  LYS A 256     -46.740  31.736  85.898  1.00 20.00           C  
ANISOU 1732  CG  LYS A 256     2483   2431   2684    205    225    114       C  
ATOM   1733  CD  LYS A 256     -45.676  32.490  86.685  1.00 19.44           C  
ANISOU 1733  CD  LYS A 256     2448   2337   2601    191    222     99       C  
ATOM   1734  CE  LYS A 256     -45.474  31.917  88.052  1.00 25.79           C  
ANISOU 1734  CE  LYS A 256     3269   3151   3378    174    231     83       C  
ATOM   1735  NZ  LYS A 256     -44.415  32.641  88.795  1.00 34.22           N  
ANISOU 1735  NZ  LYS A 256     4372   4198   4431    159    224     69       N  
ATOM   1736  N   ALA A 257     -47.999  33.054  81.664  1.00 16.69           N  
ANISOU 1736  N   ALA A 257     2007   2000   2335    258    189    173       N  
ATOM   1737  CA  ALA A 257     -48.382  34.061  80.655  1.00 16.86           C  
ANISOU 1737  CA  ALA A 257     2024   2003   2377    280    181    187       C  
ATOM   1738  C   ALA A 257     -48.759  35.404  81.322  1.00 21.16           C  
ANISOU 1738  C   ALA A 257     2585   2517   2937    301    199    172       C  
ATOM   1739  O   ALA A 257     -49.760  36.024  80.950  1.00 20.32           O  
ANISOU 1739  O   ALA A 257     2464   2404   2852    329    203    178       O  
ATOM   1740  CB  ALA A 257     -49.540  33.542  79.801  1.00 17.70           C  
ANISOU 1740  CB  ALA A 257     2096   2133   2497    295    176    202       C  
ATOM   1741  N   ASP A 258     -47.950  35.840  82.324  1.00 18.39           N  
ANISOU 1741  N   ASP A 258     2265   2148   2573    288    207    153       N  
ATOM   1742  CA  ASP A 258     -48.223  37.055  83.094  1.00 18.94           C  
ANISOU 1742  CA  ASP A 258     2356   2187   2654    304    226    135       C  
ATOM   1743  C   ASP A 258     -47.168  38.153  82.833  1.00 23.70           C  
ANISOU 1743  C   ASP A 258     2989   2754   3260    297    215    136       C  
ATOM   1744  O   ASP A 258     -47.131  39.159  83.548  1.00 23.74           O  
ANISOU 1744  O   ASP A 258     3019   2730   3271    304    228    118       O  
ATOM   1745  CB  ASP A 258     -48.305  36.730  84.608  1.00 20.92           C  
ANISOU 1745  CB  ASP A 258     2620   2443   2885    296    247    107       C  
ATOM   1746  CG  ASP A 258     -47.004  36.185  85.201  1.00 30.67           C  
ANISOU 1746  CG  ASP A 258     3878   3683   4092    261    237    100       C  
ATOM   1747  OD1 ASP A 258     -46.144  35.712  84.419  1.00 29.98           O  
ANISOU 1747  OD1 ASP A 258     3786   3604   4001    243    214    117       O  
ATOM   1748  OD2 ASP A 258     -46.880  36.172  86.444  1.00 37.99           O  
ANISOU 1748  OD2 ASP A 258     4825   4609   5002    252    251     78       O  
ATOM   1749  N   GLY A 259     -46.323  37.940  81.824  1.00 20.26           N  
ANISOU 1749  N   GLY A 259     2553   2323   2823    281    192    156       N  
ATOM   1750  CA  GLY A 259     -45.276  38.893  81.466  1.00 20.20           C  
ANISOU 1750  CA  GLY A 259     2572   2284   2820    270    181    161       C  
ATOM   1751  C   GLY A 259     -43.914  38.530  82.027  1.00 24.31           C  
ANISOU 1751  C   GLY A 259     3111   2806   3320    235    173    152       C  
ATOM   1752  O   GLY A 259     -42.901  39.116  81.631  1.00 24.08           O  
ANISOU 1752  O   GLY A 259     3098   2756   3293    220    161    158       O  
ATOM   1753  N   SER A 260     -43.876  37.564  82.972  1.00 21.13           N  
ANISOU 1753  N   SER A 260     2705   2427   2897    222    178    137       N  
ATOM   1754  CA  SER A 260     -42.614  37.093  83.555  1.00 20.74           C  
ANISOU 1754  CA  SER A 260     2670   2383   2829    190    168    130       C  
ATOM   1755  C   SER A 260     -41.769  36.388  82.503  1.00 22.47           C  
ANISOU 1755  C   SER A 260     2875   2618   3046    173    148    152       C  
ATOM   1756  O   SER A 260     -42.313  35.695  81.637  1.00 21.94           O  
ANISOU 1756  O   SER A 260     2783   2571   2982    182    145    169       O  
ATOM   1757  CB  SER A 260     -42.883  36.153  84.726  1.00 24.97           C  
ANISOU 1757  CB  SER A 260     3204   2941   3343    182    178    113       C  
ATOM   1758  OG  SER A 260     -43.609  36.808  85.754  1.00 36.37           O  
ANISOU 1758  OG  SER A 260     4664   4371   4785    197    199     90       O  
ATOM   1759  N   TRP A 261     -40.441  36.589  82.549  1.00 17.92           N  
ANISOU 1759  N   TRP A 261     2313   2030   2465    148    136    152       N  
ATOM   1760  CA  TRP A 261     -39.524  35.990  81.580  1.00 17.12           C  
ANISOU 1760  CA  TRP A 261     2200   1942   2364    131    120    172       C  
ATOM   1761  C   TRP A 261     -39.577  34.461  81.639  1.00 20.98           C  
ANISOU 1761  C   TRP A 261     2668   2466   2839    123    116    176       C  
ATOM   1762  O   TRP A 261     -39.476  33.877  82.721  1.00 20.94           O  
ANISOU 1762  O   TRP A 261     2666   2471   2818    114    119    162       O  
ATOM   1763  CB  TRP A 261     -38.079  36.487  81.820  1.00 15.50           C  
ANISOU 1763  CB  TRP A 261     2013   1719   2159    104    109    168       C  
ATOM   1764  CG  TRP A 261     -37.116  36.103  80.730  1.00 15.99           C  
ANISOU 1764  CG  TRP A 261     2062   1789   2225     88     96    189       C  
ATOM   1765  CD1 TRP A 261     -36.711  36.878  79.684  1.00 18.89           C  
ANISOU 1765  CD1 TRP A 261     2434   2138   2606     87     93    205       C  
ATOM   1766  CD2 TRP A 261     -36.474  34.831  80.560  1.00 15.55           C  
ANISOU 1766  CD2 TRP A 261     1988   1760   2159     73     88    196       C  
ATOM   1767  NE1 TRP A 261     -35.843  36.173  78.880  1.00 17.95           N  
ANISOU 1767  NE1 TRP A 261     2300   2035   2485     71     85    221       N  
ATOM   1768  CE2 TRP A 261     -35.680  34.913  79.396  1.00 18.94           C  
ANISOU 1768  CE2 TRP A 261     2411   2187   2597     63     82    215       C  
ATOM   1769  CE3 TRP A 261     -36.477  33.628  81.294  1.00 16.64           C  
ANISOU 1769  CE3 TRP A 261     2117   1923   2282     67     86    189       C  
ATOM   1770  CZ2 TRP A 261     -34.903  33.839  78.942  1.00 17.98           C  
ANISOU 1770  CZ2 TRP A 261     2273   2088   2472     49     75    225       C  
ATOM   1771  CZ3 TRP A 261     -35.748  32.552  80.815  1.00 17.59           C  
ANISOU 1771  CZ3 TRP A 261     2220   2064   2400     54     78    200       C  
ATOM   1772  CH2 TRP A 261     -34.959  32.666  79.664  1.00 18.13           C  
ANISOU 1772  CH2 TRP A 261     2282   2130   2478     45     73    217       C  
ATOM   1773  N   GLY A 262     -39.717  33.830  80.474  1.00 17.08           N  
ANISOU 1773  N   GLY A 262     2153   1989   2348    127    111    195       N  
ATOM   1774  CA  GLY A 262     -39.700  32.376  80.355  1.00 16.74           C  
ANISOU 1774  CA  GLY A 262     2091   1976   2294    119    107    200       C  
ATOM   1775  C   GLY A 262     -40.849  31.673  81.054  1.00 20.85           C  
ANISOU 1775  C   GLY A 262     2601   2515   2807    131    118    191       C  
ATOM   1776  O   GLY A 262     -40.739  30.492  81.388  1.00 21.53           O  
ANISOU 1776  O   GLY A 262     2677   2622   2882    120    116    190       O  
ATOM   1777  N   GLN A 263     -41.982  32.379  81.250  1.00 15.94           N  
ANISOU 1777  N   GLN A 263     1980   1884   2194    153    130    185       N  
ATOM   1778  CA  GLN A 263     -43.160  31.779  81.891  1.00 15.13           C  
ANISOU 1778  CA  GLN A 263     1864   1798   2086    165    144    176       C  
ATOM   1779  C   GLN A 263     -44.353  31.683  80.928  1.00 18.89           C  
ANISOU 1779  C   GLN A 263     2316   2285   2576    186    146    189       C  
ATOM   1780  O   GLN A 263     -45.494  31.560  81.368  1.00 19.54           O  
ANISOU 1780  O   GLN A 263     2386   2376   2662    201    159    182       O  
ATOM   1781  CB  GLN A 263     -43.538  32.537  83.178  1.00 16.04           C  
ANISOU 1781  CB  GLN A 263     1999   1899   2199    172    160    154       C  
ATOM   1782  CG  GLN A 263     -42.510  32.365  84.314  1.00 21.65           C  
ANISOU 1782  CG  GLN A 263     2731   2605   2889    149    157    140       C  
ATOM   1783  CD  GLN A 263     -42.392  30.922  84.775  1.00 26.58           C  
ANISOU 1783  CD  GLN A 263     3345   3257   3496    134    155    141       C  
ATOM   1784  OE1 GLN A 263     -43.390  30.208  84.942  1.00 13.65           O  
ANISOU 1784  OE1 GLN A 263     1691   1637   1856    143    166    141       O  
ATOM   1785  NE2 GLN A 263     -41.180  30.500  85.078  1.00 19.34           N  
ANISOU 1785  NE2 GLN A 263     2438   2342   2569    111    140    142       N  
ATOM   1786  N   ASP A 264     -44.074  31.669  79.617  1.00 15.40           N  
ANISOU 1786  N   ASP A 264     1866   1845   2140    186    131    208       N  
ATOM   1787  CA  ASP A 264     -45.105  31.493  78.585  1.00 15.43           C  
ANISOU 1787  CA  ASP A 264     1847   1861   2153    203    127    222       C  
ATOM   1788  C   ASP A 264     -44.996  30.091  78.002  1.00 18.30           C  
ANISOU 1788  C   ASP A 264     2194   2253   2507    189    118    231       C  
ATOM   1789  O   ASP A 264     -44.205  29.284  78.493  1.00 17.35           O  
ANISOU 1789  O   ASP A 264     2078   2140   2373    169    118    225       O  
ATOM   1790  CB  ASP A 264     -44.915  32.538  77.455  1.00 17.39           C  
ANISOU 1790  CB  ASP A 264     2102   2091   2413    213    117    239       C  
ATOM   1791  CG  ASP A 264     -44.923  33.978  77.929  1.00 23.54           C  
ANISOU 1791  CG  ASP A 264     2902   2838   3205    226    125    231       C  
ATOM   1792  OD1 ASP A 264     -45.686  34.288  78.859  1.00 22.84           O  
ANISOU 1792  OD1 ASP A 264     2812   2743   3121    240    140    216       O  
ATOM   1793  OD2 ASP A 264     -44.243  34.812  77.296  1.00 28.05           O  
ANISOU 1793  OD2 ASP A 264     3488   3387   3781    223    118    242       O  
ATOM   1794  N   TYR A 265     -45.752  29.804  76.915  1.00 14.73           N  
ANISOU 1794  N   TYR A 265     1722   1814   2060    198    110    245       N  
ATOM   1795  CA  TYR A 265     -45.500  28.617  76.118  1.00 13.39           C  
ANISOU 1795  CA  TYR A 265     1541   1666   1880    184     99    253       C  
ATOM   1796  C   TYR A 265     -44.225  28.888  75.354  1.00 17.39           C  
ANISOU 1796  C   TYR A 265     2064   2162   2381    171     90    263       C  
ATOM   1797  O   TYR A 265     -44.241  29.632  74.371  1.00 17.14           O  
ANISOU 1797  O   TYR A 265     2036   2121   2354    179     82    277       O  
ATOM   1798  CB  TYR A 265     -46.672  28.327  75.165  1.00 13.95           C  
ANISOU 1798  CB  TYR A 265     1589   1754   1957    196     91    265       C  
ATOM   1799  CG  TYR A 265     -46.525  27.014  74.426  1.00 15.05           C  
ANISOU 1799  CG  TYR A 265     1718   1916   2085    180     81    270       C  
ATOM   1800  CD1 TYR A 265     -46.692  25.797  75.084  1.00 16.51           C  
ANISOU 1800  CD1 TYR A 265     1892   2117   2263    168     87    260       C  
ATOM   1801  CD2 TYR A 265     -46.219  26.985  73.071  1.00 14.99           C  
ANISOU 1801  CD2 TYR A 265     1712   1912   2071    177     66    284       C  
ATOM   1802  CE1 TYR A 265     -46.517  24.586  74.419  1.00 16.03           C  
ANISOU 1802  CE1 TYR A 265     1824   2073   2193    153     79    263       C  
ATOM   1803  CE2 TYR A 265     -46.078  25.781  72.386  1.00 15.37           C  
ANISOU 1803  CE2 TYR A 265     1753   1980   2109    162     59    287       C  
ATOM   1804  CZ  TYR A 265     -46.222  24.581  73.066  1.00 21.84           C  
ANISOU 1804  CZ  TYR A 265     2563   2813   2924    150     65    275       C  
ATOM   1805  OH  TYR A 265     -46.066  23.390  72.397  1.00 21.60           O  
ANISOU 1805  OH  TYR A 265     2526   2797   2883    135     58    276       O  
ATOM   1806  N   ASN A 266     -43.088  28.500  75.956  1.00 13.72           N  
ANISOU 1806  N   ASN A 266     1610   1694   1909    152     92    255       N  
ATOM   1807  CA  ASN A 266     -41.778  29.050  75.653  1.00 13.22           C  
ANISOU 1807  CA  ASN A 266     1564   1615   1844    140     88    260       C  
ATOM   1808  C   ASN A 266     -41.261  28.894  74.226  1.00 15.64           C  
ANISOU 1808  C   ASN A 266     1870   1926   2148    133     79    277       C  
ATOM   1809  O   ASN A 266     -40.364  29.644  73.833  1.00 14.98           O  
ANISOU 1809  O   ASN A 266     1799   1826   2066    127     78    284       O  
ATOM   1810  CB  ASN A 266     -40.752  28.635  76.691  1.00 13.17           C  
ANISOU 1810  CB  ASN A 266     1567   1607   1832    121     90    248       C  
ATOM   1811  CG  ASN A 266     -40.989  29.296  78.030  1.00 28.19           C  
ANISOU 1811  CG  ASN A 266     3480   3495   3735    126     99    233       C  
ATOM   1812  OD1 ASN A 266     -41.189  30.511  78.120  1.00 16.67           O  
ANISOU 1812  OD1 ASN A 266     2032   2015   2285    137    102    231       O  
ATOM   1813  ND2 ASN A 266     -41.081  28.500  79.082  1.00 22.80           N  
ANISOU 1813  ND2 ASN A 266     2796   2824   3044    119    103    221       N  
ATOM   1814  N   TYR A 267     -41.898  28.024  73.401  1.00 11.08           N  
ANISOU 1814  N   TYR A 267     1277   1369   1564    136     74    283       N  
ATOM   1815  CA  TYR A 267     -41.551  27.954  71.969  1.00 10.46           C  
ANISOU 1815  CA  TYR A 267     1200   1296   1480    131     66    299       C  
ATOM   1816  C   TYR A 267     -41.737  29.333  71.309  1.00 14.78           C  
ANISOU 1816  C   TYR A 267     1758   1824   2033    144     62    313       C  
ATOM   1817  O   TYR A 267     -41.026  29.663  70.359  1.00 15.00           O  
ANISOU 1817  O   TYR A 267     1797   1847   2056    137     59    325       O  
ATOM   1818  CB  TYR A 267     -42.402  26.899  71.236  1.00 11.31           C  
ANISOU 1818  CB  TYR A 267     1292   1428   1579    133     59    302       C  
ATOM   1819  CG  TYR A 267     -41.977  25.469  71.494  1.00 13.03           C  
ANISOU 1819  CG  TYR A 267     1502   1661   1788    117     62    292       C  
ATOM   1820  CD1 TYR A 267     -40.739  25.001  71.058  1.00 14.69           C  
ANISOU 1820  CD1 TYR A 267     1719   1870   1992    101     64    294       C  
ATOM   1821  CD2 TYR A 267     -42.874  24.540  72.008  1.00 14.21           C  
ANISOU 1821  CD2 TYR A 267     1635   1825   1937    118     63    283       C  
ATOM   1822  CE1 TYR A 267     -40.369  23.668  71.226  1.00 14.73           C  
ANISOU 1822  CE1 TYR A 267     1717   1887   1992     89     67    286       C  
ATOM   1823  CE2 TYR A 267     -42.519  23.201  72.170  1.00 15.15           C  
ANISOU 1823  CE2 TYR A 267     1750   1956   2050    104     65    276       C  
ATOM   1824  CZ  TYR A 267     -41.264  22.771  71.782  1.00 19.99           C  
ANISOU 1824  CZ  TYR A 267     2371   2566   2657     90     67    277       C  
ATOM   1825  OH  TYR A 267     -40.911  21.456  71.949  1.00 18.28           O  
ANISOU 1825  OH  TYR A 267     2150   2359   2438     78     69    271       O  
ATOM   1826  N   THR A 268     -42.688  30.155  71.843  1.00 11.18           N  
ANISOU 1826  N   THR A 268     1301   1358   1589    163     63    310       N  
ATOM   1827  CA  THR A 268     -42.941  31.511  71.329  1.00 10.74           C  
ANISOU 1827  CA  THR A 268     1256   1281   1543    179     60    324       C  
ATOM   1828  C   THR A 268     -41.719  32.415  71.525  1.00 13.38           C  
ANISOU 1828  C   THR A 268     1612   1589   1881    167     65    325       C  
ATOM   1829  O   THR A 268     -41.408  33.218  70.653  1.00 13.60           O  
ANISOU 1829  O   THR A 268     1653   1604   1911    169     61    341       O  
ATOM   1830  CB  THR A 268     -44.210  32.120  71.979  1.00 17.02           C  
ANISOU 1830  CB  THR A 268     2044   2071   2354    203     63    318       C  
ATOM   1831  OG1 THR A 268     -44.032  32.175  73.394  1.00 13.72           O  
ANISOU 1831  OG1 THR A 268     1629   1643   1939    200     76    298       O  
ATOM   1832  CG2 THR A 268     -45.479  31.337  71.638  1.00 15.07           C  
ANISOU 1832  CG2 THR A 268     1772   1849   2107    214     56    321       C  
HETATM 1833  N   MSE A 269     -41.005  32.258  72.655  1.00  8.56           N  
ANISOU 1833  N   MSE A 269     1007    973   1272    155     73    308       N  
HETATM 1834  CA  MSE A 269     -39.804  33.061  72.916  1.00  8.12           C  
ANISOU 1834  CA  MSE A 269      970    893   1220    141     76    307       C  
HETATM 1835  C   MSE A 269     -38.627  32.615  72.032  1.00 14.16           C  
ANISOU 1835  C   MSE A 269     1737   1666   1978    120     74    317       C  
HETATM 1836  O   MSE A 269     -37.961  33.459  71.422  1.00 14.30           O  
ANISOU 1836  O   MSE A 269     1768   1666   2000    114     75    330       O  
HETATM 1837  CB  MSE A 269     -39.416  33.005  74.405  1.00  9.42           C  
ANISOU 1837  CB  MSE A 269     1140   1052   1388    132     83    285       C  
HETATM 1838  CG  MSE A 269     -38.230  33.913  74.754  1.00 14.91           C  
ANISOU 1838  CG  MSE A 269     1855   1722   2090    117     84    282       C  
HETATM 1839 SE   MSE A 269     -37.801  33.928  76.655  0.75 20.56          SE  
ANISOU 1839 SE   MSE A 269     2580   2429   2804    106     87    254      SE  
HETATM 1840  CE  MSE A 269     -37.354  32.036  76.893  1.00 17.56           C  
ANISOU 1840  CE  MSE A 269     2179   2085   2408     90     84    251       C  
ATOM   1841  N   PHE A 270     -38.390  31.289  71.940  1.00 11.67           N  
ANISOU 1841  N   PHE A 270     1408   1375   1652    110     74    313       N  
ATOM   1842  CA  PHE A 270     -37.263  30.749  71.170  1.00 11.91           C  
ANISOU 1842  CA  PHE A 270     1437   1412   1675     91     75    321       C  
ATOM   1843  C   PHE A 270     -37.388  31.069  69.663  1.00 16.52           C  
ANISOU 1843  C   PHE A 270     2027   1998   2252     95     73    341       C  
ATOM   1844  O   PHE A 270     -36.414  31.523  69.046  1.00 16.05           O  
ANISOU 1844  O   PHE A 270     1977   1929   2192     82     77    352       O  
ATOM   1845  CB  PHE A 270     -37.125  29.222  71.383  1.00 13.47           C  
ANISOU 1845  CB  PHE A 270     1620   1635   1864     83     76    311       C  
ATOM   1846  CG  PHE A 270     -37.233  28.758  72.821  1.00 14.78           C  
ANISOU 1846  CG  PHE A 270     1780   1803   2033     82     77    294       C  
ATOM   1847  CD1 PHE A 270     -36.459  29.345  73.819  1.00 18.01           C  
ANISOU 1847  CD1 PHE A 270     2199   2195   2450     73     78    285       C  
ATOM   1848  CD2 PHE A 270     -37.994  27.640  73.152  1.00 16.14           C  
ANISOU 1848  CD2 PHE A 270     1939   1994   2198     86     76    286       C  
ATOM   1849  CE1 PHE A 270     -36.540  28.899  75.143  1.00 18.86           C  
ANISOU 1849  CE1 PHE A 270     2305   2307   2556     71     78    270       C  
ATOM   1850  CE2 PHE A 270     -38.054  27.180  74.472  1.00 18.70           C  
ANISOU 1850  CE2 PHE A 270     2262   2322   2524     84     78    272       C  
ATOM   1851  CZ  PHE A 270     -37.333  27.815  75.459  1.00 17.07           C  
ANISOU 1851  CZ  PHE A 270     2065   2098   2321     76     78    264       C  
ATOM   1852  N   GLN A 271     -38.582  30.817  69.065  1.00 12.91           N  
ANISOU 1852  N   GLN A 271     1562   1554   1787    110     66    347       N  
ATOM   1853  CA  GLN A 271     -38.770  31.019  67.625  1.00 12.66           C  
ANISOU 1853  CA  GLN A 271     1538   1528   1745    113     61    367       C  
ATOM   1854  C   GLN A 271     -39.134  32.460  67.258  1.00 16.06           C  
ANISOU 1854  C   GLN A 271     1983   1935   2183    126     56    383       C  
ATOM   1855  O   GLN A 271     -38.535  33.023  66.346  1.00 15.80           O  
ANISOU 1855  O   GLN A 271     1964   1893   2145    119     58    400       O  
ATOM   1856  CB  GLN A 271     -39.804  30.029  67.050  1.00 13.91           C  
ANISOU 1856  CB  GLN A 271     1682   1712   1890    120     51    367       C  
ATOM   1857  CG  GLN A 271     -39.996  30.176  65.531  1.00 19.37           C  
ANISOU 1857  CG  GLN A 271     2382   2411   2566    121     44    387       C  
ATOM   1858  CD  GLN A 271     -40.929  29.142  64.969  1.00 28.81           C  
ANISOU 1858  CD  GLN A 271     3565   3633   3747    125     33    386       C  
ATOM   1859  OE1 GLN A 271     -40.574  27.977  64.811  1.00 22.23           O  
ANISOU 1859  OE1 GLN A 271     2726   2817   2904    112     37    375       O  
ATOM   1860  NE2 GLN A 271     -42.091  29.581  64.516  1.00 19.76           N  
ANISOU 1860  NE2 GLN A 271     2415   2491   2601    142     18    397       N  
ATOM   1861  N   ILE A 272     -40.177  33.020  67.889  1.00 12.48           N  
ANISOU 1861  N   ILE A 272     1526   1473   1743    146     52    380       N  
ATOM   1862  CA  ILE A 272     -40.670  34.348  67.511  1.00 12.23           C  
ANISOU 1862  CA  ILE A 272     1508   1419   1721    163     47    396       C  
ATOM   1863  C   ILE A 272     -39.811  35.479  68.108  1.00 16.19           C  
ANISOU 1863  C   ILE A 272     2028   1887   2237    156     56    394       C  
ATOM   1864  O   ILE A 272     -39.224  36.257  67.360  1.00 15.35           O  
ANISOU 1864  O   ILE A 272     1938   1763   2130    150     56    411       O  
ATOM   1865  CB  ILE A 272     -42.188  34.515  67.843  1.00 15.08           C  
ANISOU 1865  CB  ILE A 272     1854   1783   2092    190     39    394       C  
ATOM   1866  CG1 ILE A 272     -43.023  33.340  67.250  1.00 15.10           C  
ANISOU 1866  CG1 ILE A 272     1837   1819   2081    193     28    395       C  
ATOM   1867  CG2 ILE A 272     -42.711  35.881  67.355  1.00 15.93           C  
ANISOU 1867  CG2 ILE A 272     1975   1866   2212    210     32    413       C  
ATOM   1868  CD1 ILE A 272     -44.519  33.309  67.706  1.00 19.99           C  
ANISOU 1868  CD1 ILE A 272     2436   2447   2713    217     22    390       C  
ATOM   1869  N   THR A 273     -39.761  35.580  69.458  1.00 13.57           N  
ANISOU 1869  N   THR A 273     1694   1546   1917    157     62    372       N  
ATOM   1870  CA  THR A 273     -39.036  36.666  70.138  1.00 13.38           C  
ANISOU 1870  CA  THR A 273     1688   1489   1907    150     69    367       C  
ATOM   1871  C   THR A 273     -37.544  36.676  69.765  1.00 18.16           C  
ANISOU 1871  C   THR A 273     2302   2089   2508    122     74    372       C  
ATOM   1872  O   THR A 273     -36.987  37.741  69.495  1.00 18.60           O  
ANISOU 1872  O   THR A 273     2375   2118   2572    116     76    383       O  
ATOM   1873  CB  THR A 273     -39.245  36.586  71.668  1.00 21.18           C  
ANISOU 1873  CB  THR A 273     2673   2473   2903    153     75    340       C  
ATOM   1874  OG1 THR A 273     -40.623  36.309  71.947  1.00 17.67           O  
ANISOU 1874  OG1 THR A 273     2214   2040   2460    177     74    335       O  
ATOM   1875  CG2 THR A 273     -38.806  37.867  72.389  1.00 20.60           C  
ANISOU 1875  CG2 THR A 273     2620   2362   2844    150     81    333       C  
ATOM   1876  N   TRP A 274     -36.902  35.487  69.733  1.00 14.57           N  
ANISOU 1876  N   TRP A 274     1835   1660   2042    105     76    366       N  
ATOM   1877  CA  TRP A 274     -35.465  35.393  69.438  1.00 14.16           C  
ANISOU 1877  CA  TRP A 274     1786   1606   1989     79     82    369       C  
ATOM   1878  C   TRP A 274     -35.174  35.129  67.940  1.00 17.54           C  
ANISOU 1878  C   TRP A 274     2215   2045   2403     73     84    391       C  
ATOM   1879  O   TRP A 274     -34.007  35.009  67.556  1.00 18.01           O  
ANISOU 1879  O   TRP A 274     2276   2106   2462     52     92    395       O  
ATOM   1880  CB  TRP A 274     -34.792  34.325  70.323  1.00 12.65           C  
ANISOU 1880  CB  TRP A 274     1580   1430   1796     65     84    350       C  
ATOM   1881  CG  TRP A 274     -34.841  34.626  71.800  1.00 13.69           C  
ANISOU 1881  CG  TRP A 274     1715   1550   1938     65     83    330       C  
ATOM   1882  CD1 TRP A 274     -35.109  35.831  72.385  1.00 16.80           C  
ANISOU 1882  CD1 TRP A 274     2124   1915   2343     72     83    325       C  
ATOM   1883  CD2 TRP A 274     -34.471  33.737  72.864  1.00 13.38           C  
ANISOU 1883  CD2 TRP A 274     1664   1524   1896     56     82    311       C  
ATOM   1884  NE1 TRP A 274     -35.009  35.725  73.755  1.00 16.31           N  
ANISOU 1884  NE1 TRP A 274     2062   1850   2283     68     82    304       N  
ATOM   1885  CE2 TRP A 274     -34.614  34.451  74.077  1.00 17.46           C  
ANISOU 1885  CE2 TRP A 274     2192   2021   2420     58     80    296       C  
ATOM   1886  CE3 TRP A 274     -34.056  32.394  72.914  1.00 14.24           C  
ANISOU 1886  CE3 TRP A 274     1757   1658   1997     47     81    307       C  
ATOM   1887  CZ2 TRP A 274     -34.348  33.869  75.326  1.00 16.70           C  
ANISOU 1887  CZ2 TRP A 274     2091   1932   2320     50     78    277       C  
ATOM   1888  CZ3 TRP A 274     -33.800  31.817  74.154  1.00 15.61           C  
ANISOU 1888  CZ3 TRP A 274     1924   1836   2169     40     78    290       C  
ATOM   1889  CH2 TRP A 274     -33.943  32.551  75.338  1.00 16.32           C  
ANISOU 1889  CH2 TRP A 274     2027   1910   2264     41     76    276       C  
ATOM   1890  N   SER A 275     -36.241  35.061  67.091  1.00 12.70           N  
ANISOU 1890  N   SER A 275     1603   1443   1780     91     77    404       N  
ATOM   1891  CA  SER A 275     -36.099  34.853  65.629  1.00 11.95           C  
ANISOU 1891  CA  SER A 275     1513   1360   1667     86     77    424       C  
ATOM   1892  C   SER A 275     -35.231  33.615  65.283  1.00 16.37           C  
ANISOU 1892  C   SER A 275     2062   1944   2214     67     86    418       C  
ATOM   1893  O   SER A 275     -34.404  33.666  64.363  1.00 16.56           O  
ANISOU 1893  O   SER A 275     2093   1968   2229     53     95    430       O  
ATOM   1894  CB  SER A 275     -35.550  36.108  64.953  1.00 13.87           C  
ANISOU 1894  CB  SER A 275     1778   1577   1914     80     81    446       C  
ATOM   1895  OG  SER A 275     -36.451  37.193  65.086  1.00 21.61           O  
ANISOU 1895  OG  SER A 275     2769   2535   2906    101     73    455       O  
ATOM   1896  N   GLY A 276     -35.456  32.522  66.005  1.00 12.83           N  
ANISOU 1896  N   GLY A 276     1596   1514   1766     69     84    398       N  
ATOM   1897  CA  GLY A 276     -34.761  31.265  65.771  1.00 12.24           C  
ANISOU 1897  CA  GLY A 276     1509   1460   1681     55     92    390       C  
ATOM   1898  C   GLY A 276     -35.699  30.172  65.315  1.00 15.60           C  
ANISOU 1898  C   GLY A 276     1926   1912   2091     64     84    386       C  
ATOM   1899  O   GLY A 276     -36.429  29.597  66.123  1.00 15.43           O  
ANISOU 1899  O   GLY A 276     1891   1898   2072     73     78    372       O  
ATOM   1900  N   PRO A 277     -35.737  29.883  63.994  1.00 11.97           N  
ANISOU 1900  N   PRO A 277     1472   1464   1610     61     85    399       N  
ATOM   1901  CA  PRO A 277     -36.700  28.885  63.493  1.00 11.60           C  
ANISOU 1901  CA  PRO A 277     1419   1442   1548     68     76    395       C  
ATOM   1902  C   PRO A 277     -36.557  27.513  64.142  1.00 14.94           C  
ANISOU 1902  C   PRO A 277     1824   1879   1972     62     80    374       C  
ATOM   1903  O   PRO A 277     -35.454  26.968  64.216  1.00 14.44           O  
ANISOU 1903  O   PRO A 277     1758   1817   1911     48     93    367       O  
ATOM   1904  CB  PRO A 277     -36.406  28.832  61.986  1.00 13.53           C  
ANISOU 1904  CB  PRO A 277     1678   1694   1768     60     80    410       C  
ATOM   1905  CG  PRO A 277     -35.766  30.121  61.678  1.00 18.22           C  
ANISOU 1905  CG  PRO A 277     2289   2267   2368     56     86    428       C  
ATOM   1906  CD  PRO A 277     -34.978  30.505  62.892  1.00 13.94           C  
ANISOU 1906  CD  PRO A 277     1739   1707   1851     50     95    417       C  
ATOM   1907  N   ILE A 278     -37.674  26.965  64.637  1.00 11.45           N  
ANISOU 1907  N   ILE A 278     1371   1449   1532     73     68    364       N  
ATOM   1908  CA  ILE A 278     -37.729  25.594  65.135  1.00 11.14           C  
ANISOU 1908  CA  ILE A 278     1317   1424   1492     68     70    347       C  
ATOM   1909  C   ILE A 278     -38.495  24.756  64.117  1.00 16.07           C  
ANISOU 1909  C   ILE A 278     1940   2069   2097     68     62    348       C  
ATOM   1910  O   ILE A 278     -39.709  24.930  63.954  1.00 15.24           O  
ANISOU 1910  O   ILE A 278     1831   1971   1989     80     48    352       O  
ATOM   1911  CB  ILE A 278     -38.350  25.534  66.559  1.00 13.67           C  
ANISOU 1911  CB  ILE A 278     1625   1741   1828     76     66    335       C  
ATOM   1912  CG1 ILE A 278     -37.491  26.359  67.569  1.00 13.50           C  
ANISOU 1912  CG1 ILE A 278     1608   1700   1823     73     73    332       C  
ATOM   1913  CG2 ILE A 278     -38.506  24.084  67.020  1.00 14.26           C  
ANISOU 1913  CG2 ILE A 278     1686   1830   1901     71     67    319       C  
ATOM   1914  CD1 ILE A 278     -38.109  26.492  68.981  1.00 20.15           C  
ANISOU 1914  CD1 ILE A 278     2442   2536   2677     82     70    320       C  
ATOM   1915  N   CYS A 279     -37.761  23.989  63.311  1.00 12.32           N  
ANISOU 1915  N   CYS A 279     1471   1602   1608     55     72    345       N  
ATOM   1916  CA  CYS A 279     -38.264  23.452  62.066  1.00 12.11           C  
ANISOU 1916  CA  CYS A 279     1452   1592   1558     53     65    348       C  
ATOM   1917  C   CYS A 279     -38.907  22.110  62.167  1.00 12.54           C  
ANISOU 1917  C   CYS A 279     1495   1663   1608     50     60    332       C  
ATOM   1918  O   CYS A 279     -38.586  21.321  63.058  1.00 11.80           O  
ANISOU 1918  O   CYS A 279     1390   1567   1527     46     67    318       O  
ATOM   1919  CB  CYS A 279     -37.175  23.466  60.997  1.00 13.15           C  
ANISOU 1919  CB  CYS A 279     1599   1723   1673     41     81    354       C  
ATOM   1920  SG  CYS A 279     -36.551  25.110  60.602  1.00 17.66           S  
ANISOU 1920  SG  CYS A 279     2187   2276   2246     41     86    377       S  
HETATM 1921  N   MSE A 280     -39.737  21.784  61.167  1.00  7.16           N  
ANISOU 1921  N   MSE A 280      818    996    905     49     47    335       N  
HETATM 1922  CA  MSE A 280     -40.197  20.437  60.938  1.00  5.73           C  
ANISOU 1922  CA  MSE A 280      631    830    715     42     43    320       C  
HETATM 1923  C   MSE A 280     -39.023  19.636  60.367  1.00 11.19           C  
ANISOU 1923  C   MSE A 280     1333   1521   1396     28     63    311       C  
HETATM 1924  O   MSE A 280     -38.258  20.169  59.566  1.00 11.24           O  
ANISOU 1924  O   MSE A 280     1357   1525   1391     24     73    320       O  
HETATM 1925  CB  MSE A 280     -41.376  20.441  59.937  1.00  6.52           C  
ANISOU 1925  CB  MSE A 280      735    947    795     43     21    327       C  
HETATM 1926  CG  MSE A 280     -41.890  19.041  59.590  1.00 11.20           C  
ANISOU 1926  CG  MSE A 280     1324   1554   1376     33     15    310       C  
HETATM 1927 SE   MSE A 280     -43.330  19.072  58.268  0.75 16.53          SE  
ANISOU 1927 SE   MSE A 280     2004   2252   2025     32    -17    319      SE  
HETATM 1928  CE  MSE A 280     -42.367  19.821  56.775  1.00 13.23           C  
ANISOU 1928  CE  MSE A 280     1621   1833   1574     26    -10    335       C  
ATOM   1929  N   SER A 281     -38.817  18.409  60.851  1.00  8.53           N  
ANISOU 1929  N   SER A 281      988   1186   1067     22     70    293       N  
ATOM   1930  CA  SER A 281     -37.722  17.569  60.361  1.00  8.11           C  
ANISOU 1930  CA  SER A 281      943   1131   1007     11     91    282       C  
ATOM   1931  C   SER A 281     -38.087  16.934  59.033  1.00 12.26           C  
ANISOU 1931  C   SER A 281     1484   1671   1504      3     87    277       C  
ATOM   1932  O   SER A 281     -39.274  16.791  58.724  1.00 12.41           O  
ANISOU 1932  O   SER A 281     1502   1701   1511      3     66    277       O  
ATOM   1933  CB  SER A 281     -37.388  16.483  61.376  1.00 10.35           C  
ANISOU 1933  CB  SER A 281     1212   1409   1310      9     99    266       C  
ATOM   1934  OG  SER A 281     -38.479  15.594  61.550  1.00 14.22           O  
ANISOU 1934  OG  SER A 281     1695   1908   1798      7     85    256       O  
ATOM   1935  N   LYS A 282     -37.064  16.525  58.240  1.00  8.92           N  
ANISOU 1935  N   LYS A 282     1075   1247   1068     -6    109    271       N  
ATOM   1936  CA ALYS A 282     -37.294  15.839  56.969  0.50  8.74           C  
ANISOU 1936  CA ALYS A 282     1071   1236   1014    -15    109    262       C  
ATOM   1937  CA BLYS A 282     -37.293  15.836  56.969  0.50  8.69           C  
ANISOU 1937  CA BLYS A 282     1065   1230   1008    -15    109    262       C  
ATOM   1938  C   LYS A 282     -38.014  14.509  57.219  1.00 13.07           C  
ANISOU 1938  C   LYS A 282     1612   1789   1565    -21    100    242       C  
ATOM   1939  O   LYS A 282     -38.900  14.129  56.448  1.00 13.48           O  
ANISOU 1939  O   LYS A 282     1673   1854   1594    -27     84    237       O  
ATOM   1940  CB ALYS A 282     -35.956  15.600  56.233  0.50 10.99           C  
ANISOU 1940  CB ALYS A 282     1370   1516   1289    -22    139    257       C  
ATOM   1941  CB BLYS A 282     -35.951  15.597  56.231  0.50 10.85           C  
ANISOU 1941  CB BLYS A 282     1352   1498   1271    -22    139    257       C  
ATOM   1942  CG ALYS A 282     -36.120  15.129  54.780  0.50 22.89           C  
ANISOU 1942  CG ALYS A 282     2903   3036   2758    -33    142    250       C  
ATOM   1943  CG BLYS A 282     -36.097  14.877  54.875  0.50 21.37           C  
ANISOU 1943  CG BLYS A 282     2709   2843   2568    -34    144    245       C  
ATOM   1944  CD ALYS A 282     -36.644  16.250  53.872  0.50 33.67           C  
ANISOU 1944  CD ALYS A 282     4286   4411   4095    -33    127    271       C  
ATOM   1945  CD BLYS A 282     -36.842  15.731  53.842  0.50 32.27           C  
ANISOU 1945  CD BLYS A 282     4109   4237   3916    -36    125    262       C  
ATOM   1946  CE ALYS A 282     -36.786  15.800  52.442  0.50 42.61           C  
ANISOU 1946  CE ALYS A 282     5446   5557   5185    -45    128    264       C  
ATOM   1947  CE BLYS A 282     -37.006  15.009  52.528  0.50 42.12           C  
ANISOU 1947  CE BLYS A 282     5383   5497   5125    -49    127    249       C  
ATOM   1948  NZ ALYS A 282     -37.287  16.893  51.572  0.50 51.22           N  
ANISOU 1948  NZ ALYS A 282     6555   6657   6247    -45    111    287       N  
ATOM   1949  NZ BLYS A 282     -37.748  15.831  51.540  0.50 51.12           N  
ANISOU 1949  NZ BLYS A 282     6542   6651   6231    -51    105    267       N  
ATOM   1950  N   SER A 283     -37.674  13.828  58.341  1.00  9.97           N  
ANISOU 1950  N   SER A 283     1203   1386   1200    -18    108    232       N  
ATOM   1951  CA  SER A 283     -38.316  12.574  58.731  1.00 10.03           C  
ANISOU 1951  CA  SER A 283     1203   1394   1214    -23    101    215       C  
ATOM   1952  C   SER A 283     -39.827  12.757  58.894  1.00 13.24           C  
ANISOU 1952  C   SER A 283     1601   1813   1618    -23     73    219       C  
ATOM   1953  O   SER A 283     -40.599  11.966  58.359  1.00 13.15           O  
ANISOU 1953  O   SER A 283     1593   1810   1592    -33     61    208       O  
ATOM   1954  CB  SER A 283     -37.713  12.049  60.029  1.00 13.01           C  
ANISOU 1954  CB  SER A 283     1563   1757   1623    -19    113    209       C  
ATOM   1955  OG  SER A 283     -36.327  11.803  59.886  1.00 20.77           O  
ANISOU 1955  OG  SER A 283     2550   2729   2612    -18    138    205       O  
ATOM   1956  N   VAL A 284     -40.250  13.828  59.613  1.00  9.79           N  
ANISOU 1956  N   VAL A 284     1150   1375   1194    -12     62    235       N  
ATOM   1957  CA  VAL A 284     -41.676  14.113  59.831  1.00  9.96           C  
ANISOU 1957  CA  VAL A 284     1158   1408   1217     -8     36    241       C  
ATOM   1958  C   VAL A 284     -42.385  14.467  58.511  1.00 14.62           C  
ANISOU 1958  C   VAL A 284     1762   2014   1779    -12     18    248       C  
ATOM   1959  O   VAL A 284     -43.496  13.995  58.270  1.00 13.81           O  
ANISOU 1959  O   VAL A 284     1653   1924   1670    -18     -3    243       O  
ATOM   1960  CB  VAL A 284     -41.894  15.198  60.928  1.00 13.95           C  
ANISOU 1960  CB  VAL A 284     1648   1907   1745      6     33    255       C  
ATOM   1961  CG1 VAL A 284     -43.350  15.661  60.965  1.00 14.07           C  
ANISOU 1961  CG1 VAL A 284     1651   1934   1761     12      8    263       C  
ATOM   1962  CG2 VAL A 284     -41.458  14.681  62.295  1.00 13.70           C  
ANISOU 1962  CG2 VAL A 284     1603   1863   1738      8     46    247       C  
ATOM   1963  N   GLU A 285     -41.702  15.227  57.619  1.00 11.90           N  
ANISOU 1963  N   GLU A 285     1437   1669   1415    -11     24    259       N  
ATOM   1964  CA  GLU A 285     -42.257  15.538  56.299  1.00 11.77           C  
ANISOU 1964  CA  GLU A 285     1438   1668   1367    -16      7    267       C  
ATOM   1965  C   GLU A 285     -42.565  14.243  55.536  1.00 17.07           C  
ANISOU 1965  C   GLU A 285     2120   2349   2017    -33      2    247       C  
ATOM   1966  O   GLU A 285     -43.643  14.113  54.961  1.00 16.56           O  
ANISOU 1966  O   GLU A 285     2055   2300   1937    -38    -24    247       O  
ATOM   1967  CB  GLU A 285     -41.293  16.420  55.488  1.00 12.84           C  
ANISOU 1967  CB  GLU A 285     1596   1799   1484    -15     21    281       C  
ATOM   1968  CG  GLU A 285     -41.904  16.929  54.185  1.00 16.66           C  
ANISOU 1968  CG  GLU A 285     2099   2297   1933    -18      0    294       C  
ATOM   1969  CD  GLU A 285     -40.933  17.598  53.230  1.00 23.77           C  
ANISOU 1969  CD  GLU A 285     3027   3196   2809    -21     17    306       C  
ATOM   1970  OE1 GLU A 285     -39.743  17.741  53.589  1.00 12.71           O  
ANISOU 1970  OE1 GLU A 285     1627   1781   1421    -20     46    305       O  
ATOM   1971  OE2 GLU A 285     -41.357  17.942  52.104  1.00 17.43           O  
ANISOU 1971  OE2 GLU A 285     2244   2405   1973    -25      1    318       O  
ATOM   1972  N   LYS A 286     -41.643  13.250  55.606  1.00 14.16           N  
ANISOU 1972  N   LYS A 286     1758   1971   1651    -41     27    228       N  
ATOM   1973  CA  LYS A 286     -41.840  11.945  54.967  1.00 14.09           C  
ANISOU 1973  CA  LYS A 286     1762   1967   1626    -57     27    205       C  
ATOM   1974  C   LYS A 286     -43.042  11.201  55.581  1.00 18.27           C  
ANISOU 1974  C   LYS A 286     2270   2501   2169    -62      6    196       C  
ATOM   1975  O   LYS A 286     -43.739  10.475  54.875  1.00 18.19           O  
ANISOU 1975  O   LYS A 286     2269   2503   2141    -76     -9    183       O  
ATOM   1976  CB  LYS A 286     -40.564  11.084  55.086  1.00 16.02           C  
ANISOU 1976  CB  LYS A 286     2014   2196   1877    -60     61    188       C  
ATOM   1977  CG  LYS A 286     -39.390  11.615  54.271  1.00 22.68           C  
ANISOU 1977  CG  LYS A 286     2878   3036   2702    -59     85    193       C  
ATOM   1978  CD  LYS A 286     -38.167  10.717  54.404  1.00 26.42           C  
ANISOU 1978  CD  LYS A 286     3357   3496   3188    -61    118    175       C  
ATOM   1979  CE  LYS A 286     -37.003  11.225  53.587  1.00 27.88           C  
ANISOU 1979  CE  LYS A 286     3559   3678   3355    -60    145    180       C  
ATOM   1980  NZ  LYS A 286     -35.812  10.352  53.727  1.00 24.54           N  
ANISOU 1980  NZ  LYS A 286     3136   3241   2947    -60    178    163       N  
ATOM   1981  N   LEU A 287     -43.291  11.406  56.900  1.00 14.09           N  
ANISOU 1981  N   LEU A 287     1715   1965   1673    -52      6    202       N  
ATOM   1982  CA  LEU A 287     -44.386  10.740  57.613  1.00 13.56           C  
ANISOU 1982  CA  LEU A 287     1627   1902   1624    -57    -10    195       C  
ATOM   1983  C   LEU A 287     -45.756  11.389  57.324  1.00 17.56           C  
ANISOU 1983  C   LEU A 287     2121   2427   2125    -55    -42    207       C  
ATOM   1984  O   LEU A 287     -46.780  10.704  57.390  1.00 17.19           O  
ANISOU 1984  O   LEU A 287     2060   2389   2082    -65    -59    199       O  
ATOM   1985  CB  LEU A 287     -44.120  10.739  59.135  1.00 13.37           C  
ANISOU 1985  CB  LEU A 287     1582   1863   1634    -47      3    197       C  
ATOM   1986  CG  LEU A 287     -42.896   9.939  59.615  1.00 18.06           C  
ANISOU 1986  CG  LEU A 287     2183   2440   2240    -48     31    185       C  
ATOM   1987  CD1 LEU A 287     -42.613  10.210  61.073  1.00 18.01           C  
ANISOU 1987  CD1 LEU A 287     2158   2421   2263    -37     40    192       C  
ATOM   1988  CD2 LEU A 287     -43.086   8.452  59.387  1.00 20.45           C  
ANISOU 1988  CD2 LEU A 287     2491   2738   2540    -65     33    164       C  
ATOM   1989  N   VAL A 288     -45.783  12.729  57.098  1.00 13.45           N  
ANISOU 1989  N   VAL A 288     1600   1910   1599    -40    -50    229       N  
ATOM   1990  CA  VAL A 288     -47.061  13.468  56.930  1.00 12.82           C  
ANISOU 1990  CA  VAL A 288     1506   1847   1521    -34    -80    244       C  
ATOM   1991  C   VAL A 288     -47.454  13.674  55.444  1.00 18.46           C  
ANISOU 1991  C   VAL A 288     2238   2577   2198    -41   -104    250       C  
ATOM   1992  O   VAL A 288     -48.606  14.013  55.155  1.00 18.54           O  
ANISOU 1992  O   VAL A 288     2235   2603   2207    -39   -134    260       O  
ATOM   1993  CB  VAL A 288     -47.074  14.809  57.723  1.00 15.34           C  
ANISOU 1993  CB  VAL A 288     1810   2158   1860    -11    -78    265       C  
ATOM   1994  CG1 VAL A 288     -46.905  14.562  59.219  1.00 14.67           C  
ANISOU 1994  CG1 VAL A 288     1706   2060   1808     -6    -60    258       C  
ATOM   1995  CG2 VAL A 288     -46.004  15.769  57.204  1.00 14.75           C  
ANISOU 1995  CG2 VAL A 288     1759   2074   1772     -4    -65    278       C  
ATOM   1996  N   THR A 289     -46.497  13.473  54.514  1.00 16.09           N  
ANISOU 1996  N   THR A 289     1970   2274   1869    -50    -89    244       N  
ATOM   1997  CA  THR A 289     -46.744  13.661  53.076  1.00 16.65           C  
ANISOU 1997  CA  THR A 289     2065   2360   1900    -59   -109    249       C  
ATOM   1998  C   THR A 289     -47.655  12.575  52.508  1.00 21.10           C  
ANISOU 1998  C   THR A 289     2629   2940   2449    -79   -132    232       C  
ATOM   1999  O   THR A 289     -47.502  11.400  52.847  1.00 20.60           O  
ANISOU 1999  O   THR A 289     2564   2870   2394    -92   -119    208       O  
ATOM   2000  CB  THR A 289     -45.399  13.740  52.306  1.00 28.33           C  
ANISOU 2000  CB  THR A 289     3579   3833   3354    -63    -81    247       C  
ATOM   2001  OG1 THR A 289     -44.687  14.895  52.737  1.00 29.42           O  
ANISOU 2001  OG1 THR A 289     3716   3959   3505    -46    -66    267       O  
ATOM   2002  CG2 THR A 289     -45.591  13.790  50.786  1.00 28.01           C  
ANISOU 2002  CG2 THR A 289     3568   3808   3265    -75    -98    250       C  
ATOM   2003  N   ASN A 290     -48.619  12.979  51.631  1.00 17.95           N  
ANISOU 2003  N   ASN A 290     2232   2561   2028    -82   -168    244       N  
ATOM   2004  CA  ASN A 290     -49.486  12.066  50.862  1.00 18.40           C  
ANISOU 2004  CA  ASN A 290     2294   2635   2064   -104   -196    228       C  
ATOM   2005  C   ASN A 290     -50.519  11.313  51.719  1.00 22.42           C  
ANISOU 2005  C   ASN A 290     2767   3147   2605   -110   -209    217       C  
ATOM   2006  O   ASN A 290     -51.670  11.179  51.303  1.00 22.34           O  
ANISOU 2006  O   ASN A 290     2744   3156   2590   -120   -245    219       O  
ATOM   2007  CB  ASN A 290     -48.650  11.083  50.018  1.00 21.04           C  
ANISOU 2007  CB  ASN A 290     2664   2965   2364   -124   -176    203       C  
ATOM   2008  CG  ASN A 290     -49.433  10.422  48.914  1.00 41.51           C  
ANISOU 2008  CG  ASN A 290     5273   5577   4922   -147   -208    191       C  
ATOM   2009  OD1 ASN A 290     -50.085  11.084  48.098  1.00 38.24           O  
ANISOU 2009  OD1 ASN A 290     4864   5181   4483   -147   -241    208       O  
ATOM   2010  ND2 ASN A 290     -49.304   9.112  48.800  1.00 31.07           N  
ANISOU 2010  ND2 ASN A 290     3961   4249   3595   -168   -198    160       N  
ATOM   2011  N   ILE A 291     -50.093  10.769  52.879  1.00 18.87           N  
ANISOU 2011  N   ILE A 291     2303   2680   2187   -108   -181    205       N  
ATOM   2012  CA  ILE A 291     -50.971   9.966  53.749  1.00 19.04           C  
ANISOU 2012  CA  ILE A 291     2293   2703   2240   -116   -188    194       C  
ATOM   2013  C   ILE A 291     -52.319  10.673  54.031  1.00 23.48           C  
ANISOU 2013  C   ILE A 291     2820   3282   2820   -106   -220    212       C  
ATOM   2014  O   ILE A 291     -52.339  11.851  54.387  1.00 22.91           O  
ANISOU 2014  O   ILE A 291     2737   3209   2761    -83   -220    235       O  
ATOM   2015  CB  ILE A 291     -50.231   9.541  55.069  1.00 21.80           C  
ANISOU 2015  CB  ILE A 291     2632   3029   2621   -110   -152    185       C  
ATOM   2016  CG1 ILE A 291     -51.094   8.551  55.908  1.00 22.08           C  
ANISOU 2016  CG1 ILE A 291     2641   3064   2684   -122   -157    172       C  
ATOM   2017  CG2 ILE A 291     -49.800  10.783  55.904  1.00 22.08           C  
ANISOU 2017  CG2 ILE A 291     2656   3056   2677    -83   -138    207       C  
ATOM   2018  CD1 ILE A 291     -50.375   7.954  57.145  1.00 25.99           C  
ANISOU 2018  CD1 ILE A 291     3131   3537   3207   -119   -124    163       C  
ATOM   2019  N   GLY A 292     -53.421   9.955  53.804  1.00 20.33           N  
ANISOU 2019  N   GLY A 292     2404   2898   2424   -125   -247    203       N  
ATOM   2020  CA  GLY A 292     -54.760  10.481  54.043  1.00 20.30           C  
ANISOU 2020  CA  GLY A 292     2362   2911   2440   -117   -278    219       C  
ATOM   2021  C   GLY A 292     -55.477  10.931  52.785  1.00 24.37           C  
ANISOU 2021  C   GLY A 292     2882   3450   2927   -122   -320    230       C  
ATOM   2022  O   GLY A 292     -56.700  11.078  52.785  1.00 23.73           O  
ANISOU 2022  O   GLY A 292     2769   3387   2861   -122   -351    239       O  
ATOM   2023  N   GLY A 293     -54.706  11.205  51.731  1.00 21.73           N  
ANISOU 2023  N   GLY A 293     2588   3115   2552   -124   -320    233       N  
ATOM   2024  CA  GLY A 293     -55.249  11.578  50.423  1.00 22.01           C  
ANISOU 2024  CA  GLY A 293     2638   3173   2552   -130   -359    244       C  
ATOM   2025  C   GLY A 293     -55.841  12.978  50.349  1.00 25.90           C  
ANISOU 2025  C   GLY A 293     3112   3675   3053   -104   -384    278       C  
ATOM   2026  O   GLY A 293     -56.325  13.389  49.289  1.00 25.40           O  
ANISOU 2026  O   GLY A 293     3060   3631   2962   -107   -420    292       O  
ATOM   2027  N   VAL A 294     -55.825  13.725  51.478  1.00 22.44           N  
ANISOU 2027  N   VAL A 294     2647   3224   2654    -78   -365    291       N  
ATOM   2028  CA  VAL A 294     -56.393  15.082  51.511  1.00 22.15           C  
ANISOU 2028  CA  VAL A 294     2592   3193   2632    -51   -385    323       C  
ATOM   2029  C   VAL A 294     -55.443  16.078  50.844  1.00 24.44           C  
ANISOU 2029  C   VAL A 294     2920   3474   2894    -37   -376    341       C  
ATOM   2030  O   VAL A 294     -54.286  16.192  51.251  1.00 23.56           O  
ANISOU 2030  O   VAL A 294     2828   3342   2782    -33   -338    336       O  
ATOM   2031  CB  VAL A 294     -56.774  15.523  52.958  1.00 25.98           C  
ANISOU 2031  CB  VAL A 294     3036   3668   3169    -29   -367    328       C  
ATOM   2032  CG1 VAL A 294     -57.418  16.911  52.955  1.00 25.98           C  
ANISOU 2032  CG1 VAL A 294     3016   3671   3185      1   -388    359       C  
ATOM   2033  CG2 VAL A 294     -57.700  14.500  53.614  1.00 25.85           C  
ANISOU 2033  CG2 VAL A 294     2982   3660   3179    -44   -372    310       C  
ATOM   2034  N   ALA A 295     -55.932  16.791  49.801  1.00 20.28           N  
ANISOU 2034  N   ALA A 295     2401   2962   2341    -32   -413    364       N  
ATOM   2035  CA  ALA A 295     -55.117  17.757  49.047  1.00 19.46           C  
ANISOU 2035  CA  ALA A 295     2336   2851   2207    -22   -408    386       C  
ATOM   2036  C   ALA A 295     -54.598  18.898  49.940  1.00 22.06           C  
ANISOU 2036  C   ALA A 295     2658   3157   2567      8   -381    403       C  
ATOM   2037  O   ALA A 295     -55.208  19.208  50.970  1.00 20.53           O  
ANISOU 2037  O   ALA A 295     2425   2958   2417     25   -379    407       O  
ATOM   2038  CB  ALA A 295     -55.921  18.326  47.889  1.00 20.69           C  
ANISOU 2038  CB  ALA A 295     2498   3028   2335    -20   -457    410       C  
ATOM   2039  N   TRP A 296     -53.466  19.528  49.537  1.00 18.70           N  
ANISOU 2039  N   TRP A 296     2269   2717   2119     12   -359    414       N  
ATOM   2040  CA  TRP A 296     -52.872  20.652  50.275  1.00 18.43           C  
ANISOU 2040  CA  TRP A 296     2233   2659   2110     37   -334    430       C  
ATOM   2041  C   TRP A 296     -53.906  21.788  50.476  1.00 23.28           C  
ANISOU 2041  C   TRP A 296     2820   3274   2751     65   -363    459       C  
ATOM   2042  O   TRP A 296     -54.578  22.187  49.524  1.00 23.26           O  
ANISOU 2042  O   TRP A 296     2822   3286   2728     67   -401    480       O  
ATOM   2043  CB  TRP A 296     -51.622  21.179  49.539  1.00 17.08           C  
ANISOU 2043  CB  TRP A 296     2108   2477   1906     33   -313    441       C  
ATOM   2044  CG  TRP A 296     -50.970  22.350  50.212  1.00 17.83           C  
ANISOU 2044  CG  TRP A 296     2204   2546   2025     55   -289    458       C  
ATOM   2045  CD1 TRP A 296     -51.170  23.671  49.938  1.00 21.01           C  
ANISOU 2045  CD1 TRP A 296     2612   2941   2430     76   -304    490       C  
ATOM   2046  CD2 TRP A 296     -50.017  22.301  51.283  1.00 17.16           C  
ANISOU 2046  CD2 TRP A 296     2115   2439   1965     58   -248    444       C  
ATOM   2047  NE1 TRP A 296     -50.412  24.450  50.782  1.00 20.18           N  
ANISOU 2047  NE1 TRP A 296     2507   2809   2351     90   -273    495       N  
ATOM   2048  CE2 TRP A 296     -49.679  23.634  51.604  1.00 21.07           C  
ANISOU 2048  CE2 TRP A 296     2614   2914   2477     79   -239    467       C  
ATOM   2049  CE3 TRP A 296     -49.384  21.258  51.977  1.00 18.04           C  
ANISOU 2049  CE3 TRP A 296     2222   2546   2087     44   -218    414       C  
ATOM   2050  CZ2 TRP A 296     -48.753  23.950  52.604  1.00 19.91           C  
ANISOU 2050  CZ2 TRP A 296     2467   2744   2356     85   -203    460       C  
ATOM   2051  CZ3 TRP A 296     -48.480  21.574  52.977  1.00 19.17           C  
ANISOU 2051  CZ3 TRP A 296     2362   2666   2255     52   -184    409       C  
ATOM   2052  CH2 TRP A 296     -48.179  22.905  53.286  1.00 19.77           C  
ANISOU 2052  CH2 TRP A 296     2442   2724   2347     71   -178    431       C  
ATOM   2053  N   PRO A 297     -54.098  22.272  51.737  1.00 20.54           N  
ANISOU 2053  N   PRO A 297     2442   2911   2450     86   -346    460       N  
ATOM   2054  CA  PRO A 297     -55.144  23.290  51.976  1.00 20.77           C  
ANISOU 2054  CA  PRO A 297     2443   2941   2509    114   -371    484       C  
ATOM   2055  C   PRO A 297     -54.773  24.671  51.428  1.00 26.09           C  
ANISOU 2055  C   PRO A 297     3142   3600   3172    133   -376    516       C  
ATOM   2056  O   PRO A 297     -53.590  24.997  51.315  1.00 26.03           O  
ANISOU 2056  O   PRO A 297     3168   3575   3149    129   -349    518       O  
ATOM   2057  CB  PRO A 297     -55.281  23.302  53.498  1.00 22.08           C  
ANISOU 2057  CB  PRO A 297     2576   3093   2722    127   -344    470       C  
ATOM   2058  CG  PRO A 297     -53.959  22.854  54.000  1.00 25.99           C  
ANISOU 2058  CG  PRO A 297     3094   3571   3209    114   -302    450       C  
ATOM   2059  CD  PRO A 297     -53.426  21.872  52.993  1.00 21.60           C  
ANISOU 2059  CD  PRO A 297     2568   3028   2611     84   -305    437       C  
ATOM   2060  N   GLN A 298     -55.785  25.492  51.112  1.00 23.06           N  
ANISOU 2060  N   GLN A 298     2740   3222   2801    155   -412    543       N  
ATOM   2061  CA  GLN A 298     -55.558  26.831  50.563  1.00 23.10           C  
ANISOU 2061  CA  GLN A 298     2769   3212   2798    175   -421    577       C  
ATOM   2062  C   GLN A 298     -55.261  27.852  51.668  1.00 26.66           C  
ANISOU 2062  C   GLN A 298     3209   3631   3290    202   -392    583       C  
ATOM   2063  O   GLN A 298     -55.671  27.662  52.817  1.00 25.97           O  
ANISOU 2063  O   GLN A 298     3087   3538   3241    211   -378    566       O  
ATOM   2064  CB  GLN A 298     -56.769  27.284  49.727  1.00 24.90           C  
ANISOU 2064  CB  GLN A 298     2982   3457   3022    189   -473    605       C  
ATOM   2065  N   GLY A 299     -54.547  28.924  51.306  1.00 23.20           N  
ANISOU 2065  N   GLY A 299     2803   3170   2842    212   -384    606       N  
ATOM   2066  CA  GLY A 299     -54.263  30.036  52.210  1.00 22.66           C  
ANISOU 2066  CA  GLY A 299     2731   3070   2810    237   -361    615       C  
ATOM   2067  C   GLY A 299     -53.286  29.712  53.327  1.00 26.40           C  
ANISOU 2067  C   GLY A 299     3206   3525   3298    227   -315    587       C  
ATOM   2068  O   GLY A 299     -53.371  30.292  54.415  1.00 26.27           O  
ANISOU 2068  O   GLY A 299     3173   3489   3320    247   -297    582       O  
ATOM   2069  N   VAL A 300     -52.330  28.806  53.065  1.00 22.03           N  
ANISOU 2069  N   VAL A 300     2675   2979   2715    198   -296    568       N  
ATOM   2070  CA  VAL A 300     -51.288  28.486  54.045  1.00 21.00           C  
ANISOU 2070  CA  VAL A 300     2549   2833   2597    188   -254    543       C  
ATOM   2071  C   VAL A 300     -50.171  29.532  53.971  1.00 24.29           C  
ANISOU 2071  C   VAL A 300     2998   3221   3010    192   -232    558       C  
ATOM   2072  O   VAL A 300     -49.554  29.700  52.917  1.00 23.33           O  
ANISOU 2072  O   VAL A 300     2908   3101   2854    180   -234    573       O  
ATOM   2073  CB  VAL A 300     -50.743  27.038  53.863  1.00 24.48           C  
ANISOU 2073  CB  VAL A 300     2997   3292   3013    158   -241    516       C  
ATOM   2074  CG1 VAL A 300     -49.613  26.749  54.852  1.00 23.75           C  
ANISOU 2074  CG1 VAL A 300     2908   3182   2934    149   -200    494       C  
ATOM   2075  CG2 VAL A 300     -51.863  26.013  54.008  1.00 24.27           C  
ANISOU 2075  CG2 VAL A 300     2938   3291   2994    153   -262    500       C  
ATOM   2076  N   VAL A 301     -49.983  30.304  55.055  1.00 20.57           N  
ANISOU 2076  N   VAL A 301     2517   2724   2574    208   -213    557       N  
ATOM   2077  CA  VAL A 301     -48.989  31.377  55.079  1.00 19.95           C  
ANISOU 2077  CA  VAL A 301     2466   2616   2498    212   -193    571       C  
ATOM   2078  C   VAL A 301     -48.204  31.367  56.375  1.00 22.10           C  
ANISOU 2078  C   VAL A 301     2733   2868   2795    209   -159    548       C  
ATOM   2079  O   VAL A 301     -48.708  30.903  57.395  1.00 21.39           O  
ANISOU 2079  O   VAL A 301     2615   2783   2730    215   -154    528       O  
ATOM   2080  CB  VAL A 301     -49.652  32.760  54.843  1.00 24.63           C  
ANISOU 2080  CB  VAL A 301     3061   3190   3106    240   -213    603       C  
ATOM   2081  N   ASN A 302     -46.973  31.921  56.357  1.00 17.72           N  
ANISOU 2081  N   ASN A 302     2205   2293   2236    199   -136    553       N  
ATOM   2082  CA  ASN A 302     -46.223  32.143  57.586  1.00 16.61           C  
ANISOU 2082  CA  ASN A 302     2060   2130   2120    198   -107    535       C  
ATOM   2083  C   ASN A 302     -46.802  33.370  58.279  1.00 20.81           C  
ANISOU 2083  C   ASN A 302     2585   2636   2686    225   -111    546       C  
ATOM   2084  O   ASN A 302     -46.853  34.438  57.681  1.00 21.00           O  
ANISOU 2084  O   ASN A 302     2628   2643   2710    236   -120    572       O  
ATOM   2085  CB  ASN A 302     -44.731  32.341  57.288  1.00 12.53           C  
ANISOU 2085  CB  ASN A 302     1572   1600   1590    177    -83    538       C  
ATOM   2086  CG  ASN A 302     -43.888  32.516  58.531  1.00 23.97           C  
ANISOU 2086  CG  ASN A 302     3016   3027   3062    173    -56    519       C  
ATOM   2087  OD1 ASN A 302     -43.887  33.575  59.172  1.00 18.02           O  
ANISOU 2087  OD1 ASN A 302     2266   2247   2333    186    -52    525       O  
ATOM   2088  ND2 ASN A 302     -43.143  31.491  58.886  1.00 10.87           N  
ANISOU 2088  ND2 ASN A 302     1353   1380   1398    154    -39    497       N  
ATOM   2089  N   GLN A 303     -47.356  33.191  59.485  1.00 17.67           N  
ANISOU 2089  N   GLN A 303     2161   2236   2315    237   -104    526       N  
ATOM   2090  CA  GLN A 303     -48.080  34.272  60.175  1.00 17.51           C  
ANISOU 2090  CA  GLN A 303     2131   2193   2328    265   -107    532       C  
ATOM   2091  C   GLN A 303     -47.142  35.278  60.895  1.00 19.71           C  
ANISOU 2091  C   GLN A 303     2429   2435   2623    266    -84    530       C  
ATOM   2092  O   GLN A 303     -47.623  36.259  61.470  1.00 19.23           O  
ANISOU 2092  O   GLN A 303     2365   2351   2589    289    -83    535       O  
ATOM   2093  CB  GLN A 303     -49.121  33.695  61.151  1.00 19.07           C  
ANISOU 2093  CB  GLN A 303     2294   2405   2549    278   -108    512       C  
ATOM   2094  CG  GLN A 303     -50.200  32.853  60.461  1.00 33.86           C  
ANISOU 2094  CG  GLN A 303     4143   4311   4410    279   -134    516       C  
ATOM   2095  CD  GLN A 303     -51.222  32.338  61.445  1.00 56.99           C  
ANISOU 2095  CD  GLN A 303     7036   7253   7364    291   -132    497       C  
ATOM   2096  OE1 GLN A 303     -52.021  33.097  62.006  1.00 54.12           O  
ANISOU 2096  OE1 GLN A 303     6657   6877   7031    317   -134    501       O  
ATOM   2097  NE2 GLN A 303     -51.270  31.025  61.615  1.00 48.82           N  
ANISOU 2097  NE2 GLN A 303     5988   6243   6319    271   -129    477       N  
ATOM   2098  N   THR A 304     -45.811  35.054  60.827  1.00 15.16           N  
ANISOU 2098  N   THR A 304     1874   1855   2033    240    -66    524       N  
ATOM   2099  CA  THR A 304     -44.841  35.982  61.431  1.00 14.95           C  
ANISOU 2099  CA  THR A 304     1865   1794   2020    236    -46    523       C  
ATOM   2100  C   THR A 304     -44.344  37.001  60.389  1.00 18.34           C  
ANISOU 2100  C   THR A 304     2325   2204   2440    234    -50    553       C  
ATOM   2101  O   THR A 304     -44.316  38.202  60.665  1.00 17.27           O  
ANISOU 2101  O   THR A 304     2201   2036   2324    247    -47    564       O  
ATOM   2102  CB  THR A 304     -43.676  35.202  62.084  1.00 19.40           C  
ANISOU 2102  CB  THR A 304     2429   2362   2578    210    -24    498       C  
ATOM   2103  OG1 THR A 304     -44.209  34.257  63.005  1.00 16.56           O  
ANISOU 2103  OG1 THR A 304     2044   2020   2226    212    -21    473       O  
ATOM   2104  CG2 THR A 304     -42.680  36.123  62.801  1.00 16.63           C  
ANISOU 2104  CG2 THR A 304     2095   1978   2244    203     -5    494       C  
ATOM   2105  N   SER A 305     -43.985  36.521  59.186  1.00 15.39           N  
ANISOU 2105  N   SER A 305     1964   1849   2034    218    -56    567       N  
ATOM   2106  CA  SER A 305     -43.482  37.384  58.115  1.00 15.48           C  
ANISOU 2106  CA  SER A 305     2005   1845   2031    213    -59    598       C  
ATOM   2107  C   SER A 305     -44.589  37.775  57.131  1.00 20.27           C  
ANISOU 2107  C   SER A 305     2616   2459   2628    233    -89    626       C  
ATOM   2108  O   SER A 305     -44.430  38.734  56.370  1.00 20.19           O  
ANISOU 2108  O   SER A 305     2630   2430   2611    237    -95    656       O  
ATOM   2109  CB  SER A 305     -42.340  36.699  57.371  1.00 17.78           C  
ANISOU 2109  CB  SER A 305     2312   2152   2291    183    -44    597       C  
ATOM   2110  OG  SER A 305     -42.747  35.445  56.844  1.00 22.54           O  
ANISOU 2110  OG  SER A 305     2903   2791   2869    176    -54    587       O  
ATOM   2111  N   GLY A 306     -45.679  37.003  57.124  1.00 16.83           N  
ANISOU 2111  N   GLY A 306     2155   2051   2190    245   -108    618       N  
ATOM   2112  CA  GLY A 306     -46.786  37.216  56.195  1.00 16.67           C  
ANISOU 2112  CA  GLY A 306     2131   2042   2159    263   -141    644       C  
ATOM   2113  C   GLY A 306     -46.544  36.586  54.837  1.00 20.08           C  
ANISOU 2113  C   GLY A 306     2582   2501   2548    243   -153    657       C  
ATOM   2114  O   GLY A 306     -47.367  36.723  53.931  1.00 20.01           O  
ANISOU 2114  O   GLY A 306     2575   2505   2523    254   -182    680       O  
ATOM   2115  N   VAL A 307     -45.404  35.879  54.686  1.00 16.84           N  
ANISOU 2115  N   VAL A 307     2184   2100   2115    214   -129    642       N  
ATOM   2116  CA  VAL A 307     -45.038  35.237  53.420  1.00 16.60           C  
ANISOU 2116  CA  VAL A 307     2173   2093   2040    192   -134    651       C  
ATOM   2117  C   VAL A 307     -45.897  33.988  53.171  1.00 19.86           C  
ANISOU 2117  C   VAL A 307     2565   2542   2437    190   -154    635       C  
ATOM   2118  O   VAL A 307     -45.927  33.078  54.007  1.00 19.55           O  
ANISOU 2118  O   VAL A 307     2502   2514   2411    184   -144    605       O  
ATOM   2119  CB  VAL A 307     -43.509  34.914  53.356  1.00 19.80           C  
ANISOU 2119  CB  VAL A 307     2598   2494   2431    164    -99    639       C  
ATOM   2120  CG1 VAL A 307     -43.154  34.192  52.057  1.00 19.47           C  
ANISOU 2120  CG1 VAL A 307     2577   2478   2342    142   -101    645       C  
ATOM   2121  CG2 VAL A 307     -42.676  36.185  53.514  1.00 19.77           C  
ANISOU 2121  CG2 VAL A 307     2615   2454   2442    163    -81    657       C  
ATOM   2122  N   ALA A 308     -46.615  33.960  52.034  1.00 15.66           N  
ANISOU 2122  N   ALA A 308     2042   2029   1878    193   -185    656       N  
ATOM   2123  CA  ALA A 308     -47.461  32.825  51.663  1.00 15.26           C  
ANISOU 2123  CA  ALA A 308     1974   2014   1810    188   -208    644       C  
ATOM   2124  C   ALA A 308     -46.609  31.614  51.256  1.00 19.08           C  
ANISOU 2124  C   ALA A 308     2471   2517   2261    157   -188    621       C  
ATOM   2125  O   ALA A 308     -45.442  31.777  50.874  1.00 17.97           O  
ANISOU 2125  O   ALA A 308     2357   2367   2103    141   -163    624       O  
ATOM   2126  CB  ALA A 308     -48.389  33.218  50.522  1.00 16.12           C  
ANISOU 2126  CB  ALA A 308     2093   2136   1897    198   -248    675       C  
ATOM   2127  N   VAL A 309     -47.186  30.394  51.349  1.00 15.73           N  
ANISOU 2127  N   VAL A 309     2025   2119   1831    149   -199    597       N  
ATOM   2128  CA  VAL A 309     -46.472  29.172  50.971  1.00 15.18           C  
ANISOU 2128  CA  VAL A 309     1967   2067   1733    122   -182    573       C  
ATOM   2129  C   VAL A 309     -46.032  29.223  49.496  1.00 18.40           C  
ANISOU 2129  C   VAL A 309     2413   2486   2091    106   -186    591       C  
ATOM   2130  O   VAL A 309     -46.804  29.648  48.630  1.00 17.50           O  
ANISOU 2130  O   VAL A 309     2310   2382   1957    113   -219    616       O  
ATOM   2131  CB  VAL A 309     -47.294  27.872  51.300  1.00 18.48           C  
ANISOU 2131  CB  VAL A 309     2356   2510   2156    116   -195    546       C  
ATOM   2132  CG1 VAL A 309     -48.536  27.757  50.410  1.00 18.35           C  
ANISOU 2132  CG1 VAL A 309     2336   2518   2120    121   -239    560       C  
ATOM   2133  CG2 VAL A 309     -46.419  26.624  51.181  1.00 18.02           C  
ANISOU 2133  CG2 VAL A 309     2308   2462   2078     90   -170    518       C  
ATOM   2134  N   SER A 310     -44.770  28.872  49.231  1.00 14.56           N  
ANISOU 2134  N   SER A 310     1950   1997   1587     85   -152    581       N  
ATOM   2135  CA  SER A 310     -44.246  28.823  47.872  1.00 14.23           C  
ANISOU 2135  CA  SER A 310     1946   1965   1495     68   -149    593       C  
ATOM   2136  C   SER A 310     -44.785  27.573  47.155  1.00 18.08           C  
ANISOU 2136  C   SER A 310     2436   2484   1949     53   -167    575       C  
ATOM   2137  O   SER A 310     -45.636  26.871  47.707  1.00 18.33           O  
ANISOU 2137  O   SER A 310     2438   2527   1998     57   -185    557       O  
ATOM   2138  CB  SER A 310     -42.721  28.792  47.899  1.00 16.90           C  
ANISOU 2138  CB  SER A 310     2302   2290   1829     51   -104    585       C  
ATOM   2139  OG  SER A 310     -42.251  27.594  48.492  1.00 21.68           O  
ANISOU 2139  OG  SER A 310     2891   2902   2445     39    -82    549       O  
ATOM   2140  N   SER A 311     -44.271  27.278  45.939  1.00 14.58           N  
ANISOU 2140  N   SER A 311     2029   2054   1456     33   -161    579       N  
ATOM   2141  CA ASER A 311     -44.680  26.077  45.207  0.50 14.53           C  
ANISOU 2141  CA ASER A 311     2030   2075   1414     16   -175    559       C  
ATOM   2142  CA BSER A 311     -44.669  26.076  45.202  0.50 14.42           C  
ANISOU 2142  CA BSER A 311     2017   2062   1400     16   -174    559       C  
ATOM   2143  C   SER A 311     -44.065  24.825  45.849  1.00 18.40           C  
ANISOU 2143  C   SER A 311     2506   2567   1918      3   -144    518       C  
ATOM   2144  O   SER A 311     -44.492  23.705  45.553  1.00 18.22           O  
ANISOU 2144  O   SER A 311     2481   2563   1877    -10   -155    495       O  
ATOM   2145  CB ASER A 311     -44.276  26.177  43.738  0.50 18.41           C  
ANISOU 2145  CB ASER A 311     2568   2579   1847     -1   -174    574       C  
ATOM   2146  CB BSER A 311     -44.238  26.177  43.745  0.50 17.94           C  
ANISOU 2146  CB BSER A 311     2509   2519   1788     -1   -173    574       C  
ATOM   2147  OG ASER A 311     -42.870  26.265  43.589  0.50 27.66           O  
ANISOU 2147  OG ASER A 311     3762   3738   3009    -13   -127    570       O  
ATOM   2148  OG BSER A 311     -44.853  27.286  43.114  0.50 26.43           O  
ANISOU 2148  OG BSER A 311     3600   3594   2849     11   -205    613       O  
ATOM   2149  N   VAL A 312     -43.085  25.022  46.770  1.00 15.15           N  
ANISOU 2149  N   VAL A 312     2083   2133   1539      6   -107    510       N  
ATOM   2150  CA  VAL A 312     -42.441  23.928  47.492  1.00 14.69           C  
ANISOU 2150  CA  VAL A 312     2009   2073   1499     -3    -78    475       C  
ATOM   2151  C   VAL A 312     -43.370  23.398  48.611  1.00 18.74           C  
ANISOU 2151  C   VAL A 312     2482   2587   2050      8    -96    458       C  
ATOM   2152  O   VAL A 312     -43.339  23.903  49.742  1.00 17.43           O  
ANISOU 2152  O   VAL A 312     2293   2405   1925     22    -90    461       O  
ATOM   2153  CB  VAL A 312     -41.041  24.344  48.046  1.00 17.97           C  
ANISOU 2153  CB  VAL A 312     2426   2465   1936     -4    -35    475       C  
ATOM   2154  CG1 VAL A 312     -40.352  23.164  48.744  1.00 17.68           C  
ANISOU 2154  CG1 VAL A 312     2374   2428   1918    -13     -7    440       C  
ATOM   2155  CG2 VAL A 312     -40.156  24.906  46.933  1.00 17.87           C  
ANISOU 2155  CG2 VAL A 312     2451   2451   1887    -16    -15    493       C  
ATOM   2156  N   HIS A 313     -44.258  22.454  48.256  1.00 16.73           N  
ANISOU 2156  N   HIS A 313     2223   2354   1780      0   -120    444       N  
ATOM   2157  CA  HIS A 313     -45.164  21.784  49.203  1.00 16.69           C  
ANISOU 2157  CA  HIS A 313     2182   2354   1807      6   -136    426       C  
ATOM   2158  C   HIS A 313     -45.767  20.527  48.540  1.00 20.96           C  
ANISOU 2158  C   HIS A 313     2727   2917   2320    -13   -154    405       C  
ATOM   2159  O   HIS A 313     -45.877  20.472  47.309  1.00 21.12           O  
ANISOU 2159  O   HIS A 313     2776   2952   2296    -24   -168    411       O  
ATOM   2160  CB  HIS A 313     -46.289  22.745  49.677  1.00 17.65           C  
ANISOU 2160  CB  HIS A 313     2279   2474   1954     28   -168    449       C  
ATOM   2161  CG  HIS A 313     -47.251  23.135  48.598  1.00 21.76           C  
ANISOU 2161  CG  HIS A 313     2810   3012   2445     30   -208    470       C  
ATOM   2162  ND1 HIS A 313     -48.332  22.331  48.268  1.00 23.88           N  
ANISOU 2162  ND1 HIS A 313     3066   3303   2704     22   -240    460       N  
ATOM   2163  CD2 HIS A 313     -47.312  24.268  47.863  1.00 24.32           C  
ANISOU 2163  CD2 HIS A 313     3155   3333   2752     39   -223    503       C  
ATOM   2164  CE1 HIS A 313     -48.987  22.980  47.319  1.00 23.98           C  
ANISOU 2164  CE1 HIS A 313     3092   3328   2692     27   -275    486       C  
ATOM   2165  NE2 HIS A 313     -48.410  24.148  47.037  1.00 24.55           N  
ANISOU 2165  NE2 HIS A 313     3186   3385   2758     37   -265    513       N  
ATOM   2166  N   PRO A 314     -46.140  19.486  49.330  1.00 16.98           N  
ANISOU 2166  N   PRO A 314     2197   2415   1839    -17   -153    379       N  
ATOM   2167  CA  PRO A 314     -46.719  18.280  48.710  1.00 16.49           C  
ANISOU 2167  CA  PRO A 314     2140   2373   1754    -36   -170    357       C  
ATOM   2168  C   PRO A 314     -48.122  18.527  48.160  1.00 19.50           C  
ANISOU 2168  C   PRO A 314     2512   2774   2123    -34   -219    372       C  
ATOM   2169  O   PRO A 314     -48.831  19.409  48.650  1.00 19.01           O  
ANISOU 2169  O   PRO A 314     2426   2709   2086    -15   -238    393       O  
ATOM   2170  CB  PRO A 314     -46.736  17.270  49.854  1.00 17.92           C  
ANISOU 2170  CB  PRO A 314     2294   2546   1970    -39   -155    330       C  
ATOM   2171  CG  PRO A 314     -46.820  18.097  51.087  1.00 22.13           C  
ANISOU 2171  CG  PRO A 314     2798   3064   2546    -18   -149    343       C  
ATOM   2172  CD  PRO A 314     -46.055  19.359  50.805  1.00 17.73           C  
ANISOU 2172  CD  PRO A 314     2260   2496   1982     -6   -137    368       C  
ATOM   2173  N   GLU A 315     -48.528  17.744  47.130  1.00 15.54           N  
ANISOU 2173  N   GLU A 315     2030   2293   1584    -55   -239    360       N  
ATOM   2174  CA  GLU A 315     -49.882  17.816  46.564  1.00 15.21           C  
ANISOU 2174  CA  GLU A 315     1977   2272   1529    -56   -289    371       C  
ATOM   2175  C   GLU A 315     -50.917  17.373  47.614  1.00 17.45           C  
ANISOU 2175  C   GLU A 315     2214   2559   1857    -51   -305    361       C  
ATOM   2176  O   GLU A 315     -51.936  18.039  47.799  1.00 16.58           O  
ANISOU 2176  O   GLU A 315     2077   2457   1766    -36   -336    381       O  
ATOM   2177  CB  GLU A 315     -49.986  16.933  45.299  1.00 17.07           C  
ANISOU 2177  CB  GLU A 315     2246   2528   1713    -83   -304    355       C  
ATOM   2178  CG  GLU A 315     -51.365  16.947  44.653  1.00 30.97           C  
ANISOU 2178  CG  GLU A 315     3996   4313   3458    -88   -360    366       C  
ATOM   2179  CD  GLU A 315     -51.501  16.062  43.427  1.00 51.94           C  
ANISOU 2179  CD  GLU A 315     6686   6989   6062   -117   -378    348       C  
ATOM   2180  OE1 GLU A 315     -50.731  16.264  42.460  1.00 46.81           O  
ANISOU 2180  OE1 GLU A 315     6080   6340   5365   -125   -366    352       O  
ATOM   2181  OE2 GLU A 315     -52.445  15.239  43.393  1.00 44.33           O  
ANISOU 2181  OE2 GLU A 315     5704   6040   5101   -132   -407    331       O  
ATOM   2182  N   LYS A 316     -50.629  16.262  48.319  1.00 13.24           N  
ANISOU 2182  N   LYS A 316     1669   2018   1342    -63   -281    331       N  
ATOM   2183  CA  LYS A 316     -51.487  15.758  49.392  1.00 12.47           C  
ANISOU 2183  CA  LYS A 316     1530   1922   1287    -60   -289    320       C  
ATOM   2184  C   LYS A 316     -50.719  15.726  50.697  1.00 15.32           C  
ANISOU 2184  C   LYS A 316     1876   2259   1685    -49   -249    311       C  
ATOM   2185  O   LYS A 316     -49.521  15.425  50.701  1.00 13.87           O  
ANISOU 2185  O   LYS A 316     1716   2063   1493    -54   -214    300       O  
ATOM   2186  CB  LYS A 316     -52.020  14.349  49.051  1.00 15.35           C  
ANISOU 2186  CB  LYS A 316     1893   2299   1639    -87   -303    292       C  
ATOM   2187  CG  LYS A 316     -52.924  14.315  47.825  1.00 25.14           C  
ANISOU 2187  CG  LYS A 316     3143   3565   2843   -101   -349    298       C  
ATOM   2188  CD  LYS A 316     -53.341  12.885  47.479  1.00 32.78           C  
ANISOU 2188  CD  LYS A 316     4115   4543   3798   -131   -360    267       C  
ATOM   2189  CE  LYS A 316     -54.222  12.822  46.251  1.00 45.12           C  
ANISOU 2189  CE  LYS A 316     5689   6132   5323   -147   -408    272       C  
ATOM   2190  NZ  LYS A 316     -53.487  13.216  45.018  1.00 55.19           N  
ANISOU 2190  NZ  LYS A 316     7014   7411   6544   -152   -406    280       N  
ATOM   2191  N   VAL A 317     -51.385  16.070  51.811  1.00 13.09           N  
ANISOU 2191  N   VAL A 317     1556   1974   1445    -33   -252    318       N  
ATOM   2192  CA  VAL A 317     -50.719  16.127  53.119  1.00 13.14           C  
ANISOU 2192  CA  VAL A 317     1548   1958   1485    -22   -217    312       C  
ATOM   2193  C   VAL A 317     -51.704  15.834  54.263  1.00 17.71           C  
ANISOU 2193  C   VAL A 317     2086   2539   2104    -17   -223    306       C  
ATOM   2194  O   VAL A 317     -52.905  16.094  54.128  1.00 18.51           O  
ANISOU 2194  O   VAL A 317     2163   2656   2213    -12   -254    317       O  
ATOM   2195  CB  VAL A 317     -49.992  17.501  53.324  1.00 17.57           C  
ANISOU 2195  CB  VAL A 317     2119   2503   2052      0   -202    335       C  
ATOM   2196  CG1 VAL A 317     -51.002  18.630  53.567  1.00 17.59           C  
ANISOU 2196  CG1 VAL A 317     2098   2510   2075     22   -227    359       C  
ATOM   2197  CG2 VAL A 317     -48.974  17.423  54.466  1.00 17.04           C  
ANISOU 2197  CG2 VAL A 317     2049   2414   2010      5   -163    324       C  
ATOM   2198  N   ASP A 318     -51.188  15.304  55.398  1.00 13.42           N  
ANISOU 2198  N   ASP A 318     1533   1980   1585    -17   -193    291       N  
ATOM   2199  CA  ASP A 318     -51.980  15.121  56.615  1.00 12.46           C  
ANISOU 2199  CA  ASP A 318     1374   1858   1501    -11   -192    288       C  
ATOM   2200  C   ASP A 318     -52.543  16.489  57.049  1.00 17.08           C  
ANISOU 2200  C   ASP A 318     1940   2443   2108     16   -201    311       C  
ATOM   2201  O   ASP A 318     -51.796  17.466  57.105  1.00 16.51           O  
ANISOU 2201  O   ASP A 318     1883   2356   2034     31   -188    324       O  
ATOM   2202  CB  ASP A 318     -51.101  14.519  57.736  1.00 13.23           C  
ANISOU 2202  CB  ASP A 318     1473   1937   1617    -14   -156    272       C  
ATOM   2203  CG  ASP A 318     -51.865  14.116  58.990  1.00 16.80           C  
ANISOU 2203  CG  ASP A 318     1891   2389   2103    -12   -151    265       C  
ATOM   2204  OD1 ASP A 318     -52.552  14.985  59.570  1.00 17.37           O  
ANISOU 2204  OD1 ASP A 318     1940   2463   2196      6   -157    279       O  
ATOM   2205  OD2 ASP A 318     -51.647  12.994  59.476  1.00 18.68           O  
ANISOU 2205  OD2 ASP A 318     2128   2621   2347    -27   -136    247       O  
ATOM   2206  N   PRO A 319     -53.889  16.607  57.250  1.00 14.50           N  
ANISOU 2206  N   PRO A 319     1578   2130   1800     22   -224    317       N  
ATOM   2207  CA  PRO A 319     -54.477  17.943  57.525  1.00 14.22           C  
ANISOU 2207  CA  PRO A 319     1524   2093   1784     50   -235    340       C  
ATOM   2208  C   PRO A 319     -53.889  18.638  58.759  1.00 17.44           C  
ANISOU 2208  C   PRO A 319     1930   2479   2218     69   -203    342       C  
ATOM   2209  O   PRO A 319     -53.921  19.870  58.843  1.00 17.75           O  
ANISOU 2209  O   PRO A 319     1968   2509   2266     92   -205    360       O  
ATOM   2210  CB  PRO A 319     -55.968  17.646  57.692  1.00 16.22           C  
ANISOU 2210  CB  PRO A 319     1737   2366   2060     50   -260    340       C  
ATOM   2211  CG  PRO A 319     -56.185  16.369  56.944  1.00 20.78           C  
ANISOU 2211  CG  PRO A 319     2321   2960   2615     19   -275    324       C  
ATOM   2212  CD  PRO A 319     -54.934  15.570  57.127  1.00 15.86           C  
ANISOU 2212  CD  PRO A 319     1728   2320   1977      3   -245    305       C  
ATOM   2213  N   ARG A 320     -53.327  17.858  59.699  1.00 12.59           N  
ANISOU 2213  N   ARG A 320     1316   1855   1614     58   -175    323       N  
ATOM   2214  CA  ARG A 320     -52.732  18.406  60.924  1.00 12.19           C  
ANISOU 2214  CA  ARG A 320     1264   1784   1584     73   -146    322       C  
ATOM   2215  C   ARG A 320     -51.391  19.109  60.637  1.00 16.02           C  
ANISOU 2215  C   ARG A 320     1782   2251   2053     78   -131    329       C  
ATOM   2216  O   ARG A 320     -51.080  20.115  61.272  1.00 15.49           O  
ANISOU 2216  O   ARG A 320     1717   2169   2001     95   -119    338       O  
ATOM   2217  CB  ARG A 320     -52.535  17.291  61.974  1.00 12.49           C  
ANISOU 2217  CB  ARG A 320     1293   1818   1635     59   -124    301       C  
ATOM   2218  CG  ARG A 320     -53.835  16.632  62.418  1.00 20.84           C  
ANISOU 2218  CG  ARG A 320     2316   2890   2710     53   -134    295       C  
ATOM   2219  CD  ARG A 320     -53.584  15.367  63.225  1.00 27.38           C  
ANISOU 2219  CD  ARG A 320     3142   3715   3546     34   -114    276       C  
ATOM   2220  NE  ARG A 320     -53.038  14.288  62.394  1.00 23.35           N  
ANISOU 2220  NE  ARG A 320     2654   3207   3012     10   -118    264       N  
ATOM   2221  CZ  ARG A 320     -52.868  13.039  62.820  1.00 25.65           C  
ANISOU 2221  CZ  ARG A 320     2946   3495   3306     -9   -105    247       C  
ATOM   2222  NH1 ARG A 320     -53.198  12.704  64.060  1.00  3.95           N  
ANISOU 2222  NH1 ARG A 320      386    610    506    -23    -17    167       N  
ATOM   2223  NH2 ARG A 320     -52.374  12.116  62.007  1.00 13.54           N  
ANISOU 2223  NH2 ARG A 320     1433   1960   1751    -28   -108    235       N  
ATOM   2224  N   ALA A 321     -50.598  18.570  59.666  1.00 12.78           N  
ANISOU 2224  N   ALA A 321     1400   1844   1614     61   -131    324       N  
ATOM   2225  CA  ALA A 321     -49.244  19.073  59.357  1.00 12.90           C  
ANISOU 2225  CA  ALA A 321     1445   1843   1614     61   -113    329       C  
ATOM   2226  C   ALA A 321     -49.182  20.619  59.094  1.00 16.19           C  
ANISOU 2226  C   ALA A 321     1870   2251   2033     82   -119    353       C  
ATOM   2227  O   ALA A 321     -48.390  21.310  59.742  1.00 15.38           O  
ANISOU 2227  O   ALA A 321     1774   2128   1941     91   -100    357       O  
ATOM   2228  CB  ALA A 321     -48.646  18.306  58.183  1.00 14.01           C  
ANISOU 2228  CB  ALA A 321     1611   1991   1722     41   -115    322       C  
ATOM   2229  N   PRO A 322     -50.035  21.193  58.172  1.00 12.67           N  
ANISOU 2229  N   PRO A 322     1422   1816   1576     90   -149    371       N  
ATOM   2230  CA  PRO A 322     -49.964  22.651  57.928  1.00 12.48           C  
ANISOU 2230  CA  PRO A 322     1407   1780   1555    110   -154    396       C  
ATOM   2231  C   PRO A 322     -50.491  23.479  59.104  1.00 16.13           C  
ANISOU 2231  C   PRO A 322     1846   2229   2053    133   -148    400       C  
ATOM   2232  O   PRO A 322     -50.310  24.700  59.127  1.00 15.24           O  
ANISOU 2232  O   PRO A 322     1742   2100   1948    150   -147    417       O  
ATOM   2233  CB  PRO A 322     -50.824  22.847  56.660  1.00 14.42           C  
ANISOU 2233  CB  PRO A 322     1655   2044   1780    111   -190    413       C  
ATOM   2234  CG  PRO A 322     -51.048  21.460  56.111  1.00 18.96           C  
ANISOU 2234  CG  PRO A 322     2231   2640   2334     87   -199    394       C  
ATOM   2235  CD  PRO A 322     -51.016  20.549  57.283  1.00 14.40           C  
ANISOU 2235  CD  PRO A 322     1633   2059   1779     79   -178    371       C  
ATOM   2236  N   LYS A 323     -51.148  22.821  60.083  1.00 12.39           N  
ANISOU 2236  N   LYS A 323     1344   1762   1602    133   -143    384       N  
ATOM   2237  CA  LYS A 323     -51.626  23.504  61.287  1.00 11.72           C  
ANISOU 2237  CA  LYS A 323     1237   1664   1550    153   -133    384       C  
ATOM   2238  C   LYS A 323     -50.587  23.431  62.413  1.00 14.85           C  
ANISOU 2238  C   LYS A 323     1644   2042   1956    149   -100    370       C  
ATOM   2239  O   LYS A 323     -50.514  24.339  63.245  1.00 14.07           O  
ANISOU 2239  O   LYS A 323     1543   1926   1876    166    -88    373       O  
ATOM   2240  CB  LYS A 323     -52.979  22.940  61.742  1.00 14.32           C  
ANISOU 2240  CB  LYS A 323     1530   2012   1899    156   -144    377       C  
ATOM   2241  CG  LYS A 323     -54.123  23.322  60.817  1.00 26.59           C  
ANISOU 2241  CG  LYS A 323     3068   3582   3453    167   -178    395       C  
ATOM   2242  CD  LYS A 323     -55.470  23.040  61.441  1.00 39.48           C  
ANISOU 2242  CD  LYS A 323     4658   5229   5113    174   -186    390       C  
ATOM   2243  CE  LYS A 323     -56.603  23.554  60.584  1.00 52.82           C  
ANISOU 2243  CE  LYS A 323     6329   6934   6808    189   -222    410       C  
ATOM   2244  NZ  LYS A 323     -57.924  23.333  61.229  1.00 62.01           N  
ANISOU 2244  NZ  LYS A 323     7446   8111   8004    198   -227    406       N  
ATOM   2245  N   ILE A 324     -49.727  22.397  62.388  1.00 11.63           N  
ANISOU 2245  N   ILE A 324     1249   1637   1533    127    -88    355       N  
ATOM   2246  CA  ILE A 324     -48.607  22.309  63.329  1.00 11.34           C  
ANISOU 2246  CA  ILE A 324     1223   1583   1502    122    -60    344       C  
ATOM   2247  C   ILE A 324     -47.448  23.180  62.833  1.00 14.52           C  
ANISOU 2247  C   ILE A 324     1653   1969   1893    123    -53    355       C  
ATOM   2248  O   ILE A 324     -46.906  23.986  63.598  1.00 13.88           O  
ANISOU 2248  O   ILE A 324     1579   1870   1827    132    -39    356       O  
ATOM   2249  CB  ILE A 324     -48.156  20.824  63.548  1.00 14.42           C  
ANISOU 2249  CB  ILE A 324     1613   1980   1884    100    -50    324       C  
ATOM   2250  CG1 ILE A 324     -49.347  19.931  63.995  1.00 15.11           C  
ANISOU 2250  CG1 ILE A 324     1674   2084   1984     96    -57    314       C  
ATOM   2251  CG2 ILE A 324     -46.989  20.749  64.557  1.00 14.86           C  
ANISOU 2251  CG2 ILE A 324     1679   2020   1949     96    -25    314       C  
ATOM   2252  CD1 ILE A 324     -49.017  18.392  64.065  1.00 19.67           C  
ANISOU 2252  CD1 ILE A 324     2252   2667   2552     73    -50    296       C  
ATOM   2253  N   PHE A 325     -47.089  23.041  61.537  1.00 10.79           N  
ANISOU 2253  N   PHE A 325     1199   1504   1395    113    -62    363       N  
ATOM   2254  CA  PHE A 325     -45.948  23.756  60.966  1.00 10.38           C  
ANISOU 2254  CA  PHE A 325     1175   1439   1332    111    -52    374       C  
ATOM   2255  C   PHE A 325     -46.370  24.729  59.873  1.00 15.27           C  
ANISOU 2255  C   PHE A 325     1805   2058   1937    121    -72    398       C  
ATOM   2256  O   PHE A 325     -47.087  24.346  58.943  1.00 14.78           O  
ANISOU 2256  O   PHE A 325     1742   2015   1858    117    -93    403       O  
ATOM   2257  CB  PHE A 325     -44.902  22.765  60.420  1.00 11.57           C  
ANISOU 2257  CB  PHE A 325     1341   1594   1461     89    -39    363       C  
ATOM   2258  CG  PHE A 325     -44.430  21.742  61.424  1.00 12.13           C  
ANISOU 2258  CG  PHE A 325     1402   1662   1544     80    -22    341       C  
ATOM   2259  CD1 PHE A 325     -43.447  22.059  62.356  1.00 14.07           C  
ANISOU 2259  CD1 PHE A 325     1650   1891   1805     80     -2    337       C  
ATOM   2260  CD2 PHE A 325     -44.919  20.441  61.397  1.00 13.57           C  
ANISOU 2260  CD2 PHE A 325     1574   1860   1722     69    -26    326       C  
ATOM   2261  CE1 PHE A 325     -42.991  21.104  63.266  1.00 14.67           C  
ANISOU 2261  CE1 PHE A 325     1718   1965   1891     72     12    319       C  
ATOM   2262  CE2 PHE A 325     -44.457  19.484  62.305  1.00 16.09           C  
ANISOU 2262  CE2 PHE A 325     1886   2176   2053     60    -10    308       C  
ATOM   2263  CZ  PHE A 325     -43.500  19.822  63.236  1.00 14.24           C  
ANISOU 2263  CZ  PHE A 325     1654   1924   1832     62      8    306       C  
ATOM   2264  N   GLN A 326     -45.890  25.981  59.958  1.00 12.71           N  
ANISOU 2264  N   GLN A 326     1494   1714   1621    132    -66    413       N  
ATOM   2265  CA  GLN A 326     -46.143  26.994  58.938  1.00 12.88           C  
ANISOU 2265  CA  GLN A 326     1532   1733   1631    141    -82    439       C  
ATOM   2266  C   GLN A 326     -44.965  27.046  57.938  1.00 17.67           C  
ANISOU 2266  C   GLN A 326     2168   2335   2209    125    -71    447       C  
ATOM   2267  O   GLN A 326     -43.888  26.528  58.235  1.00 16.94           O  
ANISOU 2267  O   GLN A 326     2083   2239   2115    110    -48    433       O  
ATOM   2268  CB  GLN A 326     -46.375  28.382  59.590  1.00 13.94           C  
ANISOU 2268  CB  GLN A 326     1664   1843   1791    164    -82    452       C  
ATOM   2269  CG  GLN A 326     -45.176  28.909  60.386  1.00 22.75           C  
ANISOU 2269  CG  GLN A 326     2791   2933   2919    159    -55    447       C  
ATOM   2270  CD  GLN A 326     -45.470  30.248  61.028  1.00 35.01           C  
ANISOU 2270  CD  GLN A 326     4344   4461   4498    181    -55    457       C  
ATOM   2271  OE1 GLN A 326     -46.574  30.790  60.919  1.00 30.75           O  
ANISOU 2271  OE1 GLN A 326     3793   3922   3969    201    -73    469       O  
ATOM   2272  NE2 GLN A 326     -44.487  30.804  61.718  1.00 22.41           N  
ANISOU 2272  NE2 GLN A 326     2759   2842   2914    176    -35    452       N  
ATOM   2273  N   PRO A 327     -45.148  27.664  56.738  1.00 15.38           N  
ANISOU 2273  N   PRO A 327     1898   2049   1897    127    -87    471       N  
ATOM   2274  CA  PRO A 327     -44.039  27.690  55.754  1.00 15.27           C  
ANISOU 2274  CA  PRO A 327     1915   2034   1854    110    -74    479       C  
ATOM   2275  C   PRO A 327     -42.827  28.492  56.243  1.00 18.80           C  
ANISOU 2275  C   PRO A 327     2373   2454   2315    108    -47    483       C  
ATOM   2276  O   PRO A 327     -42.941  29.282  57.189  1.00 18.01           O  
ANISOU 2276  O   PRO A 327     2263   2334   2244    122    -45    484       O  
ATOM   2277  CB  PRO A 327     -44.678  28.338  54.513  1.00 17.49           C  
ANISOU 2277  CB  PRO A 327     2213   2322   2112    117   -100    506       C  
ATOM   2278  CG  PRO A 327     -46.158  28.242  54.738  1.00 21.82           C  
ANISOU 2278  CG  PRO A 327     2735   2883   2673    133   -130    508       C  
ATOM   2279  CD  PRO A 327     -46.366  28.303  56.201  1.00 17.11           C  
ANISOU 2279  CD  PRO A 327     2111   2274   2115    145   -119    492       C  
ATOM   2280  N   GLY A 328     -41.682  28.303  55.570  1.00 14.61           N  
ANISOU 2280  N   GLY A 328     1864   1924   1764     89    -28    484       N  
ATOM   2281  CA  GLY A 328     -40.449  29.023  55.880  1.00 14.23           C  
ANISOU 2281  CA  GLY A 328     1827   1852   1727     83     -3    488       C  
ATOM   2282  C   GLY A 328     -40.652  30.518  56.002  1.00 17.89           C  
ANISOU 2282  C   GLY A 328     2299   2292   2205     98    -10    512       C  
ATOM   2283  O   GLY A 328     -41.365  31.120  55.196  1.00 18.55           O  
ANISOU 2283  O   GLY A 328     2395   2377   2276    108    -30    535       O  
ATOM   2284  N   ILE A 329     -40.057  31.125  57.033  1.00 13.19           N  
ANISOU 2284  N   ILE A 329     1699   1673   1640    100      5    507       N  
ATOM   2285  CA  ILE A 329     -40.256  32.543  57.325  1.00 13.20           C  
ANISOU 2285  CA  ILE A 329     1708   1648   1661    114      0    526       C  
ATOM   2286  C   ILE A 329     -39.680  33.471  56.214  1.00 18.10           C  
ANISOU 2286  C   ILE A 329     2359   2255   2263    107      4    555       C  
ATOM   2287  O   ILE A 329     -40.171  34.585  56.030  1.00 17.40           O  
ANISOU 2287  O   ILE A 329     2281   2148   2181    122     -8    578       O  
ATOM   2288  CB  ILE A 329     -39.705  32.899  58.747  1.00 15.69           C  
ANISOU 2288  CB  ILE A 329     2012   1941   2010    115     16    509       C  
ATOM   2289  CG1 ILE A 329     -40.230  34.279  59.230  1.00 16.14           C  
ANISOU 2289  CG1 ILE A 329     2073   1969   2090    135      7    523       C  
ATOM   2290  CG2 ILE A 329     -38.159  32.813  58.794  1.00 15.53           C  
ANISOU 2290  CG2 ILE A 329     2000   1913   1989     92     42    504       C  
ATOM   2291  CD1 ILE A 329     -39.970  34.577  60.727  1.00 21.84           C  
ANISOU 2291  CD1 ILE A 329     2783   2671   2843    138     18    503       C  
ATOM   2292  N   GLU A 330     -38.678  32.982  55.451  1.00 15.75           N  
ANISOU 2292  N   GLU A 330     2075   1967   1941     85     23    555       N  
ATOM   2293  CA  GLU A 330     -37.999  33.809  54.450  1.00 16.11           C  
ANISOU 2293  CA  GLU A 330     2150   2001   1969     74     32    582       C  
ATOM   2294  C   GLU A 330     -38.617  33.687  53.039  1.00 20.93           C  
ANISOU 2294  C   GLU A 330     2780   2631   2540     75     15    603       C  
ATOM   2295  O   GLU A 330     -38.919  34.706  52.423  1.00 21.35           O  
ANISOU 2295  O   GLU A 330     2855   2672   2586     83      3    632       O  
ATOM   2296  CB  GLU A 330     -36.490  33.501  54.418  1.00 17.32           C  
ANISOU 2296  CB  GLU A 330     2307   2152   2120     50     66    573       C  
ATOM   2297  CG  GLU A 330     -35.688  34.469  53.560  1.00 27.12           C  
ANISOU 2297  CG  GLU A 330     3577   3378   3350     37     81    600       C  
ATOM   2298  CD  GLU A 330     -34.204  34.165  53.493  1.00 50.98           C  
ANISOU 2298  CD  GLU A 330     6599   6398   6371     12    115    592       C  
ATOM   2299  OE1 GLU A 330     -33.848  32.985  53.270  1.00 39.28           O  
ANISOU 2299  OE1 GLU A 330     5109   4940   4876      2    127    572       O  
ATOM   2300  OE2 GLU A 330     -33.401  35.123  53.564  1.00 51.66           O  
ANISOU 2300  OE2 GLU A 330     6697   6462   6472      2    131    606       O  
ATOM   2301  N   ASN A 331     -38.737  32.441  52.500  1.00 17.27           N  
ANISOU 2301  N   ASN A 331     2314   2197   2049     65     14    587       N  
ATOM   2302  CA  ASN A 331     -39.203  32.248  51.107  1.00 17.41           C  
ANISOU 2302  CA  ASN A 331     2355   2236   2024     61     -2    604       C  
ATOM   2303  C   ASN A 331     -40.547  31.459  50.994  1.00 20.53           C  
ANISOU 2303  C   ASN A 331     2735   2656   2410     73    -35    595       C  
ATOM   2304  O   ASN A 331     -41.059  31.272  49.892  1.00 20.34           O  
ANISOU 2304  O   ASN A 331     2728   2650   2350     70    -54    608       O  
ATOM   2305  CB  ASN A 331     -38.104  31.590  50.244  1.00 17.56           C  
ANISOU 2305  CB  ASN A 331     2393   2268   2011     36     26    598       C  
ATOM   2306  CG  ASN A 331     -37.749  30.173  50.656  1.00 30.21           C  
ANISOU 2306  CG  ASN A 331     3976   3887   3615     26     41    562       C  
ATOM   2307  OD1 ASN A 331     -38.234  29.645  51.661  1.00 25.32           O  
ANISOU 2307  OD1 ASN A 331     3329   3270   3022     36     32    542       O  
ATOM   2308  ND2 ASN A 331     -36.894  29.531  49.878  1.00 20.02           N  
ANISOU 2308  ND2 ASN A 331     2701   2608   2297      7     66    555       N  
ATOM   2309  N   GLY A 332     -41.080  31.014  52.127  1.00 16.54           N  
ANISOU 2309  N   GLY A 332     2199   2152   1936     84    -41    573       N  
ATOM   2310  CA  GLY A 332     -42.366  30.320  52.165  1.00 15.98           C  
ANISOU 2310  CA  GLY A 332     2107   2102   1862     94    -70    564       C  
ATOM   2311  C   GLY A 332     -42.303  28.852  51.774  1.00 18.88           C  
ANISOU 2311  C   GLY A 332     2473   2497   2206     77    -67    539       C  
ATOM   2312  O   GLY A 332     -43.343  28.224  51.557  1.00 17.69           O  
ANISOU 2312  O   GLY A 332     2310   2366   2046     81    -93    533       O  
ATOM   2313  N   ASP A 333     -41.078  28.279  51.690  1.00 15.77           N  
ANISOU 2313  N   ASP A 333     2088   2101   1802     58    -35    524       N  
ATOM   2314  CA  ASP A 333     -40.925  26.848  51.394  1.00 15.24           C  
ANISOU 2314  CA  ASP A 333     2019   2056   1716     42    -27    498       C  
ATOM   2315  C   ASP A 333     -41.449  26.010  52.543  1.00 17.18           C  
ANISOU 2315  C   ASP A 333     2232   2306   1991     48    -32    472       C  
ATOM   2316  O   ASP A 333     -41.122  26.277  53.701  1.00 16.35           O  
ANISOU 2316  O   ASP A 333     2109   2184   1920     55    -19    465       O  
ATOM   2317  CB  ASP A 333     -39.451  26.492  51.112  1.00 17.22           C  
ANISOU 2317  CB  ASP A 333     2285   2303   1956     24     11    488       C  
ATOM   2318  CG  ASP A 333     -38.924  26.989  49.776  1.00 27.61           C  
ANISOU 2318  CG  ASP A 333     3636   3621   3233     12     20    510       C  
ATOM   2319  OD1 ASP A 333     -39.714  27.581  49.007  1.00 28.98           O  
ANISOU 2319  OD1 ASP A 333     3826   3801   3384     18     -7    533       O  
ATOM   2320  OD2 ASP A 333     -37.731  26.763  49.490  1.00 31.84           O  
ANISOU 2320  OD2 ASP A 333     4184   4154   3761     -3     53    503       O  
ATOM   2321  N   TRP A 334     -42.300  25.026  52.240  1.00 13.07           N  
ANISOU 2321  N   TRP A 334     1704   1807   1456     44    -51    459       N  
ATOM   2322  CA  TRP A 334     -42.802  24.123  53.255  1.00 12.36           C  
ANISOU 2322  CA  TRP A 334     1584   1721   1391     47    -54    435       C  
ATOM   2323  C   TRP A 334     -42.159  22.773  53.090  1.00 16.41           C  
ANISOU 2323  C   TRP A 334     2101   2243   1891     29    -34    408       C  
ATOM   2324  O   TRP A 334     -42.640  21.947  52.310  1.00 16.73           O  
ANISOU 2324  O   TRP A 334     2149   2302   1905     18    -47    399       O  
ATOM   2325  CB  TRP A 334     -44.335  24.015  53.191  1.00 11.20           C  
ANISOU 2325  CB  TRP A 334     1420   1590   1245     57    -90    438       C  
ATOM   2326  CG  TRP A 334     -44.950  23.470  54.446  1.00 11.64           C  
ANISOU 2326  CG  TRP A 334     1442   1645   1335     64    -93    420       C  
ATOM   2327  CD1 TRP A 334     -45.354  24.181  55.538  1.00 14.22           C  
ANISOU 2327  CD1 TRP A 334     1747   1958   1696     82    -94    425       C  
ATOM   2328  CD2 TRP A 334     -45.210  22.090  54.745  1.00 11.65           C  
ANISOU 2328  CD2 TRP A 334     1429   1659   1337     52    -91    394       C  
ATOM   2329  NE1 TRP A 334     -45.869  23.331  56.494  1.00 13.43           N  
ANISOU 2329  NE1 TRP A 334     1620   1864   1617     82    -93    404       N  
ATOM   2330  CE2 TRP A 334     -45.810  22.043  56.024  1.00 15.06           C  
ANISOU 2330  CE2 TRP A 334     1831   2086   1805     63    -93    386       C  
ATOM   2331  CE3 TRP A 334     -45.046  20.888  54.030  1.00 13.21           C  
ANISOU 2331  CE3 TRP A 334     1638   1871   1508     32    -89    376       C  
ATOM   2332  CZ2 TRP A 334     -46.203  20.840  56.622  1.00 14.41           C  
ANISOU 2332  CZ2 TRP A 334     1730   2013   1733     55    -91    363       C  
ATOM   2333  CZ3 TRP A 334     -45.446  19.701  54.620  1.00 14.81           C  
ANISOU 2333  CZ3 TRP A 334     1822   2081   1724     25    -89    353       C  
ATOM   2334  CH2 TRP A 334     -46.015  19.683  55.901  1.00 15.28           C  
ANISOU 2334  CH2 TRP A 334     1851   2135   1819     35    -91    348       C  
ATOM   2335  N   LYS A 335     -40.979  22.604  53.687  1.00 12.09           N  
ANISOU 2335  N   LYS A 335     1552   1682   1360     24     -3    397       N  
ATOM   2336  CA  LYS A 335     -40.240  21.355  53.628  1.00 11.02           C  
ANISOU 2336  CA  LYS A 335     1419   1551   1218      9     19    373       C  
ATOM   2337  C   LYS A 335     -39.524  21.108  54.944  1.00 15.71           C  
ANISOU 2337  C   LYS A 335     1991   2129   1847     12     39    359       C  
ATOM   2338  O   LYS A 335     -39.280  22.052  55.708  1.00 15.43           O  
ANISOU 2338  O   LYS A 335     1949   2079   1836     21     43    370       O  
ATOM   2339  CB  LYS A 335     -39.234  21.359  52.445  1.00 12.66           C  
ANISOU 2339  CB  LYS A 335     1656   1761   1393     -5     41    376       C  
ATOM   2340  CG  LYS A 335     -38.141  22.438  52.553  1.00 22.53           C  
ANISOU 2340  CG  LYS A 335     2913   2993   2653     -3     63    394       C  
ATOM   2341  CD  LYS A 335     -37.099  22.291  51.446  1.00 28.91           C  
ANISOU 2341  CD  LYS A 335     3748   3805   3432    -18     90    394       C  
ATOM   2342  CE  LYS A 335     -35.997  23.317  51.556  1.00 34.76           C  
ANISOU 2342  CE  LYS A 335     4494   4528   4185    -19    114    411       C  
ATOM   2343  NZ  LYS A 335     -36.486  24.688  51.261  1.00 43.05           N  
ANISOU 2343  NZ  LYS A 335     5556   5571   5229    -12     96    442       N  
ATOM   2344  N   GLY A 336     -39.234  19.848  55.225  1.00 12.87           N  
ANISOU 2344  N   GLY A 336     1625   1774   1493      3     51    336       N  
ATOM   2345  CA  GLY A 336     -38.556  19.454  56.448  1.00 12.97           C  
ANISOU 2345  CA  GLY A 336     1619   1773   1537      5     68    323       C  
ATOM   2346  C   GLY A 336     -37.069  19.716  56.411  1.00 17.25           C  
ANISOU 2346  C   GLY A 336     2167   2302   2084      0     98    324       C  
ATOM   2347  O   GLY A 336     -36.429  19.546  55.370  1.00 17.92           O  
ANISOU 2347  O   GLY A 336     2271   2392   2145     -9    114    324       O  
ATOM   2348  N   LEU A 337     -36.504  20.146  57.546  1.00 12.85           N  
ANISOU 2348  N   LEU A 337     1594   1731   1557      6    106    326       N  
ATOM   2349  CA  LEU A 337     -35.070  20.387  57.662  1.00 12.49           C  
ANISOU 2349  CA  LEU A 337     1549   1673   1523      0    132    327       C  
ATOM   2350  C   LEU A 337     -34.325  19.062  57.824  1.00 15.55           C  
ANISOU 2350  C   LEU A 337     1929   2062   1917     -6    151    306       C  
ATOM   2351  O   LEU A 337     -34.622  18.301  58.747  1.00 15.20           O  
ANISOU 2351  O   LEU A 337     1868   2016   1890     -3    145    293       O  
ATOM   2352  CB  LEU A 337     -34.781  21.326  58.873  1.00 12.26           C  
ANISOU 2352  CB  LEU A 337     1506   1627   1524      7    130    335       C  
ATOM   2353  CG  LEU A 337     -33.292  21.604  59.188  1.00 16.74           C  
ANISOU 2353  CG  LEU A 337     2069   2183   2110      1    154    336       C  
ATOM   2354  CD1 LEU A 337     -32.606  22.282  58.028  1.00 17.55           C  
ANISOU 2354  CD1 LEU A 337     2190   2284   2194     -8    170    351       C  
ATOM   2355  CD2 LEU A 337     -33.153  22.452  60.437  1.00 18.00           C  
ANISOU 2355  CD2 LEU A 337     2216   2326   2297      6    147    341       C  
ATOM   2356  N   VAL A 338     -33.386  18.758  56.896  1.00 12.27           N  
ANISOU 2356  N   VAL A 338     1526   1649   1488    -15    175    303       N  
ATOM   2357  CA  VAL A 338     -32.571  17.533  56.988  1.00 12.07           C  
ANISOU 2357  CA  VAL A 338     1493   1621   1472    -19    197    283       C  
ATOM   2358  C   VAL A 338     -31.819  17.529  58.313  1.00 16.18           C  
ANISOU 2358  C   VAL A 338     1990   2128   2030    -15    202    281       C  
ATOM   2359  O   VAL A 338     -31.253  18.552  58.699  1.00 16.13           O  
ANISOU 2359  O   VAL A 338     1978   2112   2037    -14    205    295       O  
ATOM   2360  CB  VAL A 338     -31.614  17.372  55.771  1.00 15.77           C  
ANISOU 2360  CB  VAL A 338     1978   2093   1920    -28    226    282       C  
ATOM   2361  CG1 VAL A 338     -30.744  16.125  55.919  1.00 15.12           C  
ANISOU 2361  CG1 VAL A 338     1886   2006   1852    -30    249    261       C  
ATOM   2362  CG2 VAL A 338     -32.399  17.330  54.461  1.00 15.99           C  
ANISOU 2362  CG2 VAL A 338     2034   2136   1906    -34    218    283       C  
ATOM   2363  N   TYR A 339     -31.931  16.430  59.071  1.00 12.63           N  
ANISOU 2363  N   TYR A 339     1526   1677   1596    -12    199    265       N  
ATOM   2364  CA  TYR A 339     -31.485  16.388  60.458  1.00 12.64           C  
ANISOU 2364  CA  TYR A 339     1506   1666   1629     -7    196    265       C  
ATOM   2365  C   TYR A 339     -30.015  15.988  60.637  1.00 18.33           C  
ANISOU 2365  C   TYR A 339     2214   2379   2371     -8    220    260       C  
ATOM   2366  O   TYR A 339     -29.559  14.994  60.066  1.00 18.13           O  
ANISOU 2366  O   TYR A 339     2192   2355   2343    -10    237    247       O  
ATOM   2367  CB  TYR A 339     -32.407  15.465  61.291  1.00 13.30           C  
ANISOU 2367  CB  TYR A 339     1581   1752   1721     -2    179    253       C  
ATOM   2368  CG  TYR A 339     -31.973  15.308  62.732  1.00 14.26           C  
ANISOU 2368  CG  TYR A 339     1684   1863   1872      2    175    252       C  
ATOM   2369  CD1 TYR A 339     -32.300  16.264  63.687  1.00 15.68           C  
ANISOU 2369  CD1 TYR A 339     1857   2039   2062      6    161    262       C  
ATOM   2370  CD2 TYR A 339     -31.288  14.174  63.154  1.00 15.13           C  
ANISOU 2370  CD2 TYR A 339     1783   1967   1999      3    186    241       C  
ATOM   2371  CE1 TYR A 339     -31.910  16.122  65.016  1.00 16.28           C  
ANISOU 2371  CE1 TYR A 339     1918   2106   2161      9    156    261       C  
ATOM   2372  CE2 TYR A 339     -30.883  14.024  64.478  1.00 15.86           C  
ANISOU 2372  CE2 TYR A 339     1860   2051   2116      6    180    242       C  
ATOM   2373  CZ  TYR A 339     -31.185  15.007  65.405  1.00 21.81           C  
ANISOU 2373  CZ  TYR A 339     2608   2802   2876      8    165    252       C  
ATOM   2374  OH  TYR A 339     -30.791  14.864  66.712  1.00 20.35           O  
ANISOU 2374  OH  TYR A 339     2411   2610   2712     11    158    252       O  
ATOM   2375  N   GLY A 340     -29.322  16.727  61.504  1.00 16.34           N  
ANISOU 2375  N   GLY A 340     1948   2118   2143     -8    219    269       N  
ATOM   2376  CA  GLY A 340     -28.034  16.332  62.061  1.00 16.92           C  
ANISOU 2376  CA  GLY A 340     2003   2183   2244     -8    233    266       C  
ATOM   2377  C   GLY A 340     -26.817  16.469  61.164  1.00 22.29           C  
ANISOU 2377  C   GLY A 340     2681   2862   2926    -14    262    268       C  
ATOM   2378  O   GLY A 340     -25.884  15.674  61.284  1.00 22.52           O  
ANISOU 2378  O   GLY A 340     2695   2887   2973    -12    279    260       O  
ATOM   2379  N   PRO A 341     -26.683  17.571  60.380  1.00 19.29           N  
ANISOU 2379  N   PRO A 341     2314   2484   2532    -21    270    281       N  
ATOM   2380  CA  PRO A 341     -25.402  17.810  59.701  1.00 19.74           C  
ANISOU 2380  CA  PRO A 341     2366   2540   2595    -28    300    286       C  
ATOM   2381  C   PRO A 341     -24.369  18.359  60.697  1.00 24.32           C  
ANISOU 2381  C   PRO A 341     2921   3109   3211    -31    299    293       C  
ATOM   2382  O   PRO A 341     -24.726  18.670  61.840  1.00 24.56           O  
ANISOU 2382  O   PRO A 341     2943   3134   3255    -27    275    295       O  
ATOM   2383  CB  PRO A 341     -25.760  18.844  58.645  1.00 21.67           C  
ANISOU 2383  CB  PRO A 341     2635   2789   2811    -35    304    300       C  
ATOM   2384  CG  PRO A 341     -26.848  19.643  59.267  1.00 25.47           C  
ANISOU 2384  CG  PRO A 341     3123   3267   3287    -31    273    309       C  
ATOM   2385  CD  PRO A 341     -27.624  18.697  60.176  1.00 20.65           C  
ANISOU 2385  CD  PRO A 341     2503   2658   2685    -22    252    295       C  
ATOM   2386  N   LYS A 342     -23.104  18.502  60.271  1.00 20.13           N  
ANISOU 2386  N   LYS A 342     2378   2577   2694    -37    326    296       N  
ATOM   2387  CA  LYS A 342     -22.077  19.101  61.131  1.00 19.70           C  
ANISOU 2387  CA  LYS A 342     2298   2513   2673    -43    324    305       C  
ATOM   2388  C   LYS A 342     -22.455  20.554  61.485  1.00 23.94           C  
ANISOU 2388  C   LYS A 342     2845   3043   3207    -50    306    320       C  
ATOM   2389  O   LYS A 342     -23.066  21.246  60.667  1.00 24.07           O  
ANISOU 2389  O   LYS A 342     2885   3062   3197    -54    308    329       O  
ATOM   2390  CB  LYS A 342     -20.695  19.040  60.459  1.00 22.15           C  
ANISOU 2390  CB  LYS A 342     2592   2824   2999    -50    359    306       C  
ATOM   2391  CG  LYS A 342     -20.154  17.616  60.315  1.00 28.81           C  
ANISOU 2391  CG  LYS A 342     3421   3670   3855    -40    377    290       C  
ATOM   2392  CD  LYS A 342     -18.781  17.593  59.672  1.00 33.09           C  
ANISOU 2392  CD  LYS A 342     3944   4213   4416    -46    414    292       C  
ATOM   2393  CE  LYS A 342     -18.269  16.185  59.496  1.00 37.43           C  
ANISOU 2393  CE  LYS A 342     4479   4763   4979    -34    434    275       C  
ATOM   2394  NZ  LYS A 342     -16.905  16.165  58.904  1.00 42.31           N  
ANISOU 2394  NZ  LYS A 342     5075   5383   5619    -38    472    276       N  
ATOM   2395  N   ALA A 343     -22.167  20.980  62.739  1.00 20.83           N  
ANISOU 2395  N   ALA A 343     2434   2640   2839    -52    287    323       N  
ATOM   2396  CA  ALA A 343     -22.587  22.298  63.266  1.00 20.59           C  
ANISOU 2396  CA  ALA A 343     2414   2600   2808    -58    267    334       C  
ATOM   2397  C   ALA A 343     -22.273  23.468  62.310  1.00 24.72           C  
ANISOU 2397  C   ALA A 343     2951   3119   3322    -70    283    350       C  
ATOM   2398  O   ALA A 343     -23.072  24.396  62.203  1.00 24.25           O  
ANISOU 2398  O   ALA A 343     2912   3054   3247    -70    271    359       O  
ATOM   2399  CB  ALA A 343     -21.953  22.546  64.624  1.00 21.31           C  
ANISOU 2399  CB  ALA A 343     2484   2683   2930    -62    250    333       C  
ATOM   2400  N   GLU A 344     -21.109  23.422  61.619  1.00 21.25           N  
ANISOU 2400  N   GLU A 344     2500   2682   2893    -80    312    353       N  
ATOM   2401  CA  GLU A 344     -20.705  24.503  60.699  1.00 20.97           C  
ANISOU 2401  CA  GLU A 344     2477   2642   2849    -95    331    370       C  
ATOM   2402  C   GLU A 344     -21.582  24.550  59.423  1.00 24.52           C  
ANISOU 2402  C   GLU A 344     2960   3100   3259    -91    340    376       C  
ATOM   2403  O   GLU A 344     -21.576  25.556  58.710  1.00 24.92           O  
ANISOU 2403  O   GLU A 344     3028   3145   3295   -101    349    392       O  
ATOM   2404  CB  GLU A 344     -19.205  24.389  60.328  1.00 22.45           C  
ANISOU 2404  CB  GLU A 344     2640   2830   3060   -107    362    372       C  
ATOM   2405  CG  GLU A 344     -18.844  23.126  59.547  1.00 31.15           C  
ANISOU 2405  CG  GLU A 344     3735   3946   4156   -100    390    360       C  
ATOM   2406  CD  GLU A 344     -18.493  21.910  60.391  1.00 48.56           C  
ANISOU 2406  CD  GLU A 344     5912   6154   6385    -88    383    344       C  
ATOM   2407  OE1 GLU A 344     -18.703  21.956  61.626  1.00 45.00           O  
ANISOU 2407  OE1 GLU A 344     5450   5696   5951    -84    353    341       O  
ATOM   2408  OE2 GLU A 344     -17.993  20.917  59.816  1.00 37.79           O  
ANISOU 2408  OE2 GLU A 344     4538   4796   5023    -83    408    334       O  
ATOM   2409  N   GLU A 345     -22.323  23.465  59.140  1.00 19.75           N  
ANISOU 2409  N   GLU A 345     2363   2507   2634    -78    337    362       N  
ATOM   2410  CA  GLU A 345     -23.189  23.403  57.959  1.00 18.96           C  
ANISOU 2410  CA  GLU A 345     2294   2417   2494    -76    341    366       C  
ATOM   2411  C   GLU A 345     -24.611  23.908  58.267  1.00 22.42           C  
ANISOU 2411  C   GLU A 345     2750   2853   2916    -67    308    371       C  
ATOM   2412  O   GLU A 345     -25.431  24.030  57.354  1.00 22.27           O  
ANISOU 2412  O   GLU A 345     2757   2842   2865    -64    305    377       O  
ATOM   2413  CB  GLU A 345     -23.231  21.978  57.386  1.00 20.01           C  
ANISOU 2413  CB  GLU A 345     2426   2563   2613    -69    356    347       C  
ATOM   2414  CG  GLU A 345     -21.887  21.498  56.857  1.00 30.11           C  
ANISOU 2414  CG  GLU A 345     3691   3846   3906    -76    394    343       C  
ATOM   2415  CD  GLU A 345     -21.928  20.150  56.167  1.00 51.78           C  
ANISOU 2415  CD  GLU A 345     6440   6601   6634    -69    412    324       C  
ATOM   2416  OE1 GLU A 345     -22.818  19.950  55.308  1.00 44.49           O  
ANISOU 2416  OE1 GLU A 345     5545   5686   5672    -68    409    322       O  
ATOM   2417  OE2 GLU A 345     -21.010  19.334  56.407  1.00 50.70           O  
ANISOU 2417  OE2 GLU A 345     6279   6463   6523    -66    431    312       O  
ATOM   2418  N   ALA A 346     -24.895  24.225  59.551  1.00 18.44           N  
ANISOU 2418  N   ALA A 346     2233   2339   2434    -62    284    368       N  
ATOM   2419  CA  ALA A 346     -26.213  24.731  59.956  1.00 18.00           C  
ANISOU 2419  CA  ALA A 346     2192   2280   2368    -51    255    372       C  
ATOM   2420  C   ALA A 346     -26.515  26.081  59.299  1.00 22.09           C  
ANISOU 2420  C   ALA A 346     2732   2789   2872    -56    253    394       C  
ATOM   2421  O   ALA A 346     -25.627  26.936  59.205  1.00 22.20           O  
ANISOU 2421  O   ALA A 346     2745   2791   2898    -68    266    406       O  
ATOM   2422  CB  ALA A 346     -26.284  24.858  61.469  1.00 18.47           C  
ANISOU 2422  CB  ALA A 346     2234   2330   2454    -47    235    365       C  
ATOM   2423  N   ASN A 347     -27.769  26.260  58.813  1.00 18.43           N  
ANISOU 2423  N   ASN A 347     2289   2331   2383    -46    237    399       N  
ATOM   2424  CA  ASN A 347     -28.218  27.504  58.161  1.00 18.21           C  
ANISOU 2424  CA  ASN A 347     2284   2294   2340    -47    231    422       C  
ATOM   2425  C   ASN A 347     -27.433  27.816  56.868  1.00 22.84           C  
ANISOU 2425  C   ASN A 347     2887   2883   2909    -61    258    437       C  
ATOM   2426  O   ASN A 347     -27.302  28.984  56.486  1.00 21.88           O  
ANISOU 2426  O   ASN A 347     2780   2748   2784    -68    260    458       O  
ATOM   2427  CB  ASN A 347     -28.190  28.687  59.144  1.00 17.86           C  
ANISOU 2427  CB  ASN A 347     2237   2227   2321    -46    218    430       C  
ATOM   2428  CG  ASN A 347     -29.140  28.516  60.311  1.00 33.82           C  
ANISOU 2428  CG  ASN A 347     4248   4246   4354    -31    193    417       C  
ATOM   2429  OD1 ASN A 347     -30.210  27.910  60.191  1.00 27.08           O  
ANISOU 2429  OD1 ASN A 347     3398   3407   3486    -19    179    411       O  
ATOM   2430  ND2 ASN A 347     -28.784  29.072  61.451  1.00 24.27           N  
ANISOU 2430  ND2 ASN A 347     3028   3021   3171    -33    187    413       N  
ATOM   2431  N   THR A 348     -26.949  26.754  56.172  1.00 20.26           N  
ANISOU 2431  N   THR A 348     2559   2573   2568    -66    279    425       N  
ATOM   2432  CA  THR A 348     -26.284  26.882  54.866  1.00 20.29           C  
ANISOU 2432  CA  THR A 348     2579   2582   2548    -79    308    437       C  
ATOM   2433  C   THR A 348     -26.857  25.845  53.896  1.00 25.11           C  
ANISOU 2433  C   THR A 348     3204   3213   3122    -75    311    426       C  
ATOM   2434  O   THR A 348     -27.188  24.731  54.310  1.00 25.12           O  
ANISOU 2434  O   THR A 348     3193   3224   3127    -67    303    405       O  
ATOM   2435  CB  THR A 348     -24.757  26.710  55.011  1.00 26.16           C  
ANISOU 2435  CB  THR A 348     3301   3322   3317    -93    340    432       C  
ATOM   2436  OG1 THR A 348     -24.473  25.374  55.421  1.00 24.02           O  
ANISOU 2436  OG1 THR A 348     3008   3061   3057    -87    346    408       O  
ATOM   2437  CG2 THR A 348     -24.137  27.713  55.996  1.00 23.79           C  
ANISOU 2437  CG2 THR A 348     2984   3001   3053   -100    335    440       C  
ATOM   2438  N   GLY A 349     -26.959  26.213  52.619  1.00 21.81           N  
ANISOU 2438  N   GLY A 349     2815   2802   2669    -83    321    442       N  
ATOM   2439  CA  GLY A 349     -27.476  25.323  51.582  1.00 21.41           C  
ANISOU 2439  CA  GLY A 349     2785   2771   2578    -82    324    433       C  
ATOM   2440  C   GLY A 349     -28.887  24.841  51.854  1.00 24.46           C  
ANISOU 2440  C   GLY A 349     3174   3167   2955    -68    287    424       C  
ATOM   2441  O   GLY A 349     -29.798  25.652  52.038  1.00 24.72           O  
ANISOU 2441  O   GLY A 349     3214   3194   2986    -60    259    440       O  
ATOM   2442  N   ILE A 350     -29.074  23.506  51.918  1.00 19.73           N  
ANISOU 2442  N   ILE A 350     2566   2579   2351    -64    288    399       N  
ATOM   2443  CA  ILE A 350     -30.398  22.910  52.187  1.00 18.83           C  
ANISOU 2443  CA  ILE A 350     2451   2474   2229    -53    256    388       C  
ATOM   2444  C   ILE A 350     -30.759  23.013  53.677  1.00 22.06           C  
ANISOU 2444  C   ILE A 350     2833   2872   2677    -42    235    383       C  
ATOM   2445  O   ILE A 350     -31.906  22.750  54.053  1.00 21.67           O  
ANISOU 2445  O   ILE A 350     2779   2828   2626    -32    207    378       O  
ATOM   2446  CB  ILE A 350     -30.471  21.428  51.681  1.00 21.41           C  
ANISOU 2446  CB  ILE A 350     2782   2816   2537    -56    265    362       C  
ATOM   2447  CG1 ILE A 350     -29.540  20.498  52.518  1.00 21.32           C  
ANISOU 2447  CG1 ILE A 350     2742   2797   2559    -55    286    340       C  
ATOM   2448  CG2 ILE A 350     -30.162  21.339  50.169  1.00 22.08           C  
ANISOU 2448  CG2 ILE A 350     2898   2913   2578    -68    287    366       C  
ATOM   2449  CD1 ILE A 350     -29.771  18.981  52.291  1.00 26.30           C  
ANISOU 2449  CD1 ILE A 350     3375   3439   3181    -55    290    313       C  
ATOM   2450  N   TYR A 351     -29.772  23.373  54.530  1.00 17.15           N  
ANISOU 2450  N   TYR A 351     2191   2236   2089    -44    249    383       N  
ATOM   2451  CA  TYR A 351     -29.977  23.429  55.977  1.00 15.34           C  
ANISOU 2451  CA  TYR A 351     1938   1996   1895    -35    232    377       C  
ATOM   2452  C   TYR A 351     -30.407  24.831  56.462  1.00 15.99           C  
ANISOU 2452  C   TYR A 351     2023   2064   1988    -30    214    396       C  
ATOM   2453  O   TYR A 351     -30.423  25.084  57.668  1.00 13.44           O  
ANISOU 2453  O   TYR A 351     1684   1730   1694    -24    203    392       O  
ATOM   2454  CB  TYR A 351     -28.716  22.945  56.725  1.00 16.46           C  
ANISOU 2454  CB  TYR A 351     2056   2131   2068    -40    253    364       C  
ATOM   2455  CG  TYR A 351     -28.226  21.587  56.261  1.00 17.83           C  
ANISOU 2455  CG  TYR A 351     2225   2314   2234    -43    273    345       C  
ATOM   2456  CD1 TYR A 351     -28.931  20.425  56.568  1.00 19.35           C  
ANISOU 2456  CD1 TYR A 351     2413   2516   2425    -35    261    327       C  
ATOM   2457  CD2 TYR A 351     -27.046  21.461  55.535  1.00 18.65           C  
ANISOU 2457  CD2 TYR A 351     2330   2420   2336    -53    307    345       C  
ATOM   2458  CE1 TYR A 351     -28.492  19.175  56.134  1.00 19.47           C  
ANISOU 2458  CE1 TYR A 351     2427   2537   2435    -37    280    308       C  
ATOM   2459  CE2 TYR A 351     -26.587  20.214  55.108  1.00 19.66           C  
ANISOU 2459  CE2 TYR A 351     2455   2555   2460    -53    328    326       C  
ATOM   2460  CZ  TYR A 351     -27.316  19.072  55.408  1.00 25.48           C  
ANISOU 2460  CZ  TYR A 351     3189   3298   3194    -45    314    307       C  
ATOM   2461  OH  TYR A 351     -26.870  17.843  54.993  1.00 24.08           O  
ANISOU 2461  OH  TYR A 351     3010   3125   3013    -45    335    287       O  
ATOM   2462  N   GLN A 352     -30.820  25.715  55.527  1.00 13.34           N  
ANISOU 2462  N   GLN A 352     1712   1728   1628    -31    209    417       N  
ATOM   2463  CA  GLN A 352     -31.308  27.053  55.888  1.00 13.38           C  
ANISOU 2463  CA  GLN A 352     1723   1717   1644    -24    191    437       C  
ATOM   2464  C   GLN A 352     -32.671  26.964  56.602  1.00 18.76           C  
ANISOU 2464  C   GLN A 352     2396   2401   2331     -7    160    431       C  
ATOM   2465  O   GLN A 352     -33.691  26.661  55.966  1.00 17.89           O  
ANISOU 2465  O   GLN A 352     2295   2305   2197     -1    143    433       O  
ATOM   2466  CB  GLN A 352     -31.394  27.960  54.644  1.00 14.71           C  
ANISOU 2466  CB  GLN A 352     1920   1884   1784    -29    194    463       C  
ATOM   2467  CG  GLN A 352     -30.037  28.279  54.036  1.00 26.11           C  
ANISOU 2467  CG  GLN A 352     3372   3323   3226    -47    227    472       C  
ATOM   2468  CD  GLN A 352     -30.168  29.089  52.775  1.00 40.17           C  
ANISOU 2468  CD  GLN A 352     5185   5104   4975    -53    230    498       C  
ATOM   2469  OE1 GLN A 352     -30.431  30.294  52.806  1.00 37.12           O  
ANISOU 2469  OE1 GLN A 352     4810   4700   4594    -50    219    521       O  
ATOM   2470  NE2 GLN A 352     -29.937  28.455  51.638  1.00 25.48           N  
ANISOU 2470  NE2 GLN A 352     3340   3260   3080    -62    247    497       N  
ATOM   2471  N   SER A 353     -32.672  27.166  57.946  1.00 15.77           N  
ANISOU 2471  N   SER A 353     1999   2010   1984     -1    153    423       N  
ATOM   2472  CA  SER A 353     -33.875  27.030  58.780  1.00 14.93           C  
ANISOU 2472  CA  SER A 353     1880   1905   1886     15    129    415       C  
ATOM   2473  C   SER A 353     -34.965  28.062  58.430  1.00 18.69           C  
ANISOU 2473  C   SER A 353     2370   2376   2355     28    108    434       C  
ATOM   2474  O   SER A 353     -36.147  27.814  58.683  1.00 18.06           O  
ANISOU 2474  O   SER A 353     2283   2304   2274     41     87    430       O  
ATOM   2475  CB  SER A 353     -33.514  27.125  60.258  1.00 17.76           C  
ANISOU 2475  CB  SER A 353     2221   2251   2278     17    129    403       C  
ATOM   2476  OG  SER A 353     -32.886  28.362  60.561  1.00 26.49           O  
ANISOU 2476  OG  SER A 353     3331   3334   3398     13    135    415       O  
ATOM   2477  N   LYS A 354     -34.570  29.216  57.857  1.00 15.50           N  
ANISOU 2477  N   LYS A 354     1985   1958   1948     24    113    456       N  
ATOM   2478  CA  LYS A 354     -35.538  30.241  57.436  1.00 15.29           C  
ANISOU 2478  CA  LYS A 354     1972   1923   1914     38     93    478       C  
ATOM   2479  C   LYS A 354     -36.238  29.835  56.115  1.00 18.73           C  
ANISOU 2479  C   LYS A 354     2423   2380   2314     39     81    488       C  
ATOM   2480  O   LYS A 354     -37.227  30.461  55.720  1.00 17.91           O  
ANISOU 2480  O   LYS A 354     2327   2275   2202     52     59    505       O  
ATOM   2481  CB  LYS A 354     -34.860  31.621  57.296  1.00 17.43           C  
ANISOU 2481  CB  LYS A 354     2260   2168   2194     33    102    499       C  
ATOM   2482  CG  LYS A 354     -34.302  32.167  58.625  1.00 28.09           C  
ANISOU 2482  CG  LYS A 354     3598   3496   3580     33    108    490       C  
ATOM   2483  CD  LYS A 354     -33.949  33.662  58.555  1.00 33.31           C  
ANISOU 2483  CD  LYS A 354     4277   4127   4252     31    111    512       C  
ATOM   2484  CE  LYS A 354     -32.922  33.987  57.501  1.00 44.39           C  
ANISOU 2484  CE  LYS A 354     5698   5529   5640     11    131    530       C  
ATOM   2485  NZ  LYS A 354     -32.785  35.456  57.312  1.00 57.29           N  
ANISOU 2485  NZ  LYS A 354     7351   7132   7283      9    133    554       N  
ATOM   2486  N   GLN A 355     -35.744  28.750  55.461  1.00 14.81           N  
ANISOU 2486  N   GLN A 355     1928   1902   1795     25     95    476       N  
ATOM   2487  CA  GLN A 355     -36.336  28.240  54.218  1.00 14.24           C  
ANISOU 2487  CA  GLN A 355     1873   1852   1686     22     85    482       C  
ATOM   2488  C   GLN A 355     -36.967  26.854  54.428  1.00 17.59           C  
ANISOU 2488  C   GLN A 355     2282   2297   2106     24     75    457       C  
ATOM   2489  O   GLN A 355     -37.330  26.182  53.456  1.00 16.54           O  
ANISOU 2489  O   GLN A 355     2161   2183   1941     18     69    455       O  
ATOM   2490  CB  GLN A 355     -35.292  28.202  53.095  1.00 15.49           C  
ANISOU 2490  CB  GLN A 355     2054   2014   1817      4    110    490       C  
ATOM   2491  CG  GLN A 355     -34.795  29.590  52.686  1.00 27.23           C  
ANISOU 2491  CG  GLN A 355     3561   3482   3304      1    117    519       C  
ATOM   2492  CD  GLN A 355     -33.830  29.536  51.519  1.00 43.08           C  
ANISOU 2492  CD  GLN A 355     5591   5494   5281    -18    144    528       C  
ATOM   2493  OE1 GLN A 355     -33.452  28.464  51.035  1.00 36.52           O  
ANISOU 2493  OE1 GLN A 355     4762   4682   4432    -28    160    511       O  
ATOM   2494  NE2 GLN A 355     -33.408  30.697  51.049  1.00 38.36           N  
ANISOU 2494  NE2 GLN A 355     5014   4881   4680    -23    152    555       N  
ATOM   2495  N   CYS A 356     -37.113  26.434  55.703  1.00 13.42           N  
ANISOU 2495  N   CYS A 356     1728   1764   1607     30     73    439       N  
ATOM   2496  CA  CYS A 356     -37.787  25.183  56.048  1.00 12.44           C  
ANISOU 2496  CA  CYS A 356     1587   1656   1483     32     64    417       C  
ATOM   2497  C   CYS A 356     -39.044  25.472  56.860  1.00 15.61           C  
ANISOU 2497  C   CYS A 356     1971   2057   1903     49     39    417       C  
ATOM   2498  O   CYS A 356     -39.121  26.507  57.525  1.00 14.36           O  
ANISOU 2498  O   CYS A 356     1810   1882   1767     59     36    428       O  
ATOM   2499  CB  CYS A 356     -36.842  24.243  56.797  1.00 11.92           C  
ANISOU 2499  CB  CYS A 356     1507   1589   1434     23     86    394       C  
ATOM   2500  SG  CYS A 356     -35.468  23.615  55.794  1.00 15.52           S  
ANISOU 2500  SG  CYS A 356     1979   2050   1870      4    117    388       S  
ATOM   2501  N   ALA A 357     -40.032  24.559  56.815  1.00 12.81           N  
ANISOU 2501  N   ALA A 357     1606   1720   1542     51     22    405       N  
ATOM   2502  CA  ALA A 357     -41.270  24.716  57.590  1.00 12.54           C  
ANISOU 2502  CA  ALA A 357     1550   1687   1526     66      1    405       C  
ATOM   2503  C   ALA A 357     -40.956  24.843  59.087  1.00 16.23           C  
ANISOU 2503  C   ALA A 357     2001   2140   2027     72     12    393       C  
ATOM   2504  O   ALA A 357     -40.112  24.113  59.597  1.00 15.41           O  
ANISOU 2504  O   ALA A 357     1891   2033   1929     62     30    377       O  
ATOM   2505  CB  ALA A 357     -42.196  23.532  57.347  1.00 13.09           C  
ANISOU 2505  CB  ALA A 357     1610   1779   1585     62    -15    390       C  
ATOM   2506  N   GLU A 358     -41.568  25.836  59.764  1.00 13.45           N  
ANISOU 2506  N   GLU A 358     1640   1775   1695     88      3    402       N  
ATOM   2507  CA  GLU A 358     -41.326  26.077  61.199  1.00 13.55           C  
ANISOU 2507  CA  GLU A 358     1640   1773   1737     94     14    392       C  
ATOM   2508  C   GLU A 358     -42.637  26.000  61.994  1.00 18.30           C  
ANISOU 2508  C   GLU A 358     2219   2379   2353    109      0    386       C  
ATOM   2509  O   GLU A 358     -43.703  25.885  61.400  1.00 18.66           O  
ANISOU 2509  O   GLU A 358     2260   2439   2392    116    -19    392       O  
ATOM   2510  CB  GLU A 358     -40.640  27.444  61.414  1.00 14.79           C  
ANISOU 2510  CB  GLU A 358     1810   1905   1905     98     22    405       C  
ATOM   2511  CG  GLU A 358     -41.499  28.633  60.998  1.00 20.96           C  
ANISOU 2511  CG  GLU A 358     2598   2678   2689    116      5    427       C  
ATOM   2512  CD  GLU A 358     -40.906  29.991  61.319  1.00 33.29           C  
ANISOU 2512  CD  GLU A 358     4173   4212   4266    120     14    439       C  
ATOM   2513  OE1 GLU A 358     -39.674  30.071  61.527  1.00 22.71           O  
ANISOU 2513  OE1 GLU A 358     2840   2859   2927    106     32    435       O  
ATOM   2514  OE2 GLU A 358     -41.668  30.984  61.317  1.00 23.99           O  
ANISOU 2514  OE2 GLU A 358     2997   3021   3097    138      1    453       O  
ATOM   2515  N   LEU A 359     -42.559  26.099  63.343  1.00 14.79           N  
ANISOU 2515  N   LEU A 359     1764   1924   1932    114      9    374       N  
ATOM   2516  CA  LEU A 359     -43.756  26.012  64.206  1.00 14.41           C  
ANISOU 2516  CA  LEU A 359     1695   1881   1900    127      1    366       C  
ATOM   2517  C   LEU A 359     -44.795  27.079  63.832  1.00 19.52           C  
ANISOU 2517  C   LEU A 359     2340   2524   2554    148    -15    384       C  
ATOM   2518  O   LEU A 359     -44.454  28.257  63.697  1.00 20.12           O  
ANISOU 2518  O   LEU A 359     2430   2581   2635    156    -14    397       O  
ATOM   2519  CB  LEU A 359     -43.368  26.139  65.699  1.00 13.95           C  
ANISOU 2519  CB  LEU A 359     1631   1808   1861    129     16    353       C  
ATOM   2520  CG  LEU A 359     -42.342  25.112  66.222  1.00 17.63           C  
ANISOU 2520  CG  LEU A 359     2098   2277   2325    111     30    337       C  
ATOM   2521  CD1 LEU A 359     -41.999  25.384  67.663  1.00 17.31           C  
ANISOU 2521  CD1 LEU A 359     2053   2222   2300    113     41    326       C  
ATOM   2522  CD2 LEU A 359     -42.857  23.689  66.062  1.00 21.12           C  
ANISOU 2522  CD2 LEU A 359     2526   2740   2759    103     26    326       C  
ATOM   2523  N   GLY A 360     -46.043  26.645  63.627  1.00 16.39           N  
ANISOU 2523  N   GLY A 360     1924   2145   2157    156    -31    384       N  
ATOM   2524  CA  GLY A 360     -47.134  27.531  63.220  1.00 16.07           C  
ANISOU 2524  CA  GLY A 360     1876   2104   2124    177    -50    401       C  
ATOM   2525  C   GLY A 360     -48.277  27.600  64.215  1.00 19.94           C  
ANISOU 2525  C   GLY A 360     2341   2597   2640    193    -51    393       C  
ATOM   2526  O   GLY A 360     -48.993  28.605  64.271  1.00 20.07           O  
ANISOU 2526  O   GLY A 360     2350   2603   2672    216    -59    405       O  
ATOM   2527  N   PHE A 361     -48.465  26.525  65.015  1.00 15.85           N  
ANISOU 2527  N   PHE A 361     1806   2091   2126    184    -42    373       N  
ATOM   2528  CA  PHE A 361     -49.543  26.474  66.017  1.00 15.23           C  
ANISOU 2528  CA  PHE A 361     1701   2017   2070    197    -39    364       C  
ATOM   2529  C   PHE A 361     -49.252  27.425  67.200  1.00 19.19           C  
ANISOU 2529  C   PHE A 361     2207   2493   2590    210    -20    358       C  
ATOM   2530  O   PHE A 361     -50.159  27.737  67.979  1.00 19.51           O  
ANISOU 2530  O   PHE A 361     2229   2532   2650    227    -15    353       O  
ATOM   2531  CB  PHE A 361     -49.752  25.031  66.519  1.00 16.68           C  
ANISOU 2531  CB  PHE A 361     1868   2218   2250    180    -33    346       C  
ATOM   2532  CG  PHE A 361     -48.662  24.536  67.442  1.00 17.56           C  
ANISOU 2532  CG  PHE A 361     1993   2321   2360    165    -11    330       C  
ATOM   2533  CD1 PHE A 361     -47.472  24.031  66.933  1.00 20.04           C  
ANISOU 2533  CD1 PHE A 361     2326   2632   2655    147     -7    328       C  
ATOM   2534  CD2 PHE A 361     -48.828  24.568  68.822  1.00 19.25           C  
ANISOU 2534  CD2 PHE A 361     2198   2527   2588    170      6    317       C  
ATOM   2535  CE1 PHE A 361     -46.457  23.597  67.787  1.00 20.70           C  
ANISOU 2535  CE1 PHE A 361     2419   2708   2740    135     10    316       C  
ATOM   2536  CE2 PHE A 361     -47.815  24.129  69.673  1.00 21.73           C  
ANISOU 2536  CE2 PHE A 361     2524   2833   2899    157     22    305       C  
ATOM   2537  CZ  PHE A 361     -46.633  23.655  69.151  1.00 19.69           C  
ANISOU 2537  CZ  PHE A 361     2283   2573   2625    140     23    305       C  
ATOM   2538  N   ILE A 362     -47.983  27.882  67.331  1.00 14.30           N  
ANISOU 2538  N   ILE A 362     1614   1855   1964    202     -8    358       N  
ATOM   2539  CA  ILE A 362     -47.592  28.811  68.395  1.00 13.78           C  
ANISOU 2539  CA  ILE A 362     1558   1765   1914    211      8    351       C  
ATOM   2540  C   ILE A 362     -48.082  30.246  68.096  1.00 19.56           C  
ANISOU 2540  C   ILE A 362     2295   2478   2660    235      1    367       C  
ATOM   2541  O   ILE A 362     -47.760  31.177  68.835  1.00 17.84           O  
ANISOU 2541  O   ILE A 362     2089   2235   2455    244     13    363       O  
ATOM   2542  CB  ILE A 362     -46.057  28.753  68.673  1.00 16.03           C  
ANISOU 2542  CB  ILE A 362     1865   2036   2189    192     21    345       C  
ATOM   2543  CG1 ILE A 362     -45.239  29.193  67.430  1.00 15.84           C  
ANISOU 2543  CG1 ILE A 362     1861   2005   2151    184     13    363       C  
ATOM   2544  CG2 ILE A 362     -45.640  27.355  69.157  1.00 16.54           C  
ANISOU 2544  CG2 ILE A 362     1923   2117   2244    172     28    329       C  
ATOM   2545  CD1 ILE A 362     -43.697  29.414  67.713  1.00 17.46           C  
ANISOU 2545  CD1 ILE A 362     2087   2194   2353    167     27    359       C  
ATOM   2546  N   ILE A 363     -48.864  30.413  67.002  1.00 18.83           N  
ANISOU 2546  N   ILE A 363     2194   2395   2565    246    -19    386       N  
ATOM   2547  CA  ILE A 363     -49.474  31.697  66.645  1.00 19.33           C  
ANISOU 2547  CA  ILE A 363     2259   2442   2644    272    -29    404       C  
ATOM   2548  C   ILE A 363     -51.001  31.541  66.609  1.00 24.27           C  
ANISOU 2548  C   ILE A 363     2853   3085   3285    292    -42    407       C  
ATOM   2549  O   ILE A 363     -51.515  30.686  65.880  1.00 23.71           O  
ANISOU 2549  O   ILE A 363     2766   3040   3203    284    -59    411       O  
ATOM   2550  CB  ILE A 363     -48.915  32.226  65.283  1.00 22.73           C  
ANISOU 2550  CB  ILE A 363     2712   2866   3057    268    -44    428       C  
ATOM   2551  CG1 ILE A 363     -47.365  32.285  65.299  1.00 22.88           C  
ANISOU 2551  CG1 ILE A 363     2760   2871   3063    245    -29    424       C  
ATOM   2552  CG2 ILE A 363     -49.530  33.602  64.930  1.00 23.65           C  
ANISOU 2552  CG2 ILE A 363     2834   2962   3191    295    -55    449       C  
ATOM   2553  CD1 ILE A 363     -46.727  32.367  63.916  1.00 31.44           C  
ANISOU 2553  CD1 ILE A 363     3864   3957   4123    233    -40    445       C  
ATOM   2554  N   LYS A 364     -51.720  32.320  67.438  1.00 21.79           N  
ANISOU 2554  N   LYS A 364     2525   2755   2997    316    -33    403       N  
ATOM   2555  CA  LYS A 364     -53.183  32.241  67.507  1.00 22.09           C  
ANISOU 2555  CA  LYS A 364     2528   2808   3055    337    -42    405       C  
ATOM   2556  C   LYS A 364     -53.813  33.631  67.368  1.00 26.49           C  
ANISOU 2556  C   LYS A 364     3085   3343   3638    371    -48    421       C  
ATOM   2557  O   LYS A 364     -53.393  34.571  68.050  1.00 25.20           O  
ANISOU 2557  O   LYS A 364     2939   3150   3487    381    -30    416       O  
ATOM   2558  CB  LYS A 364     -53.629  31.571  68.822  1.00 24.50           C  
ANISOU 2558  CB  LYS A 364     2813   3123   3373    335    -19    380       C  
ATOM   2559  CG  LYS A 364     -55.131  31.303  68.898  1.00 35.62           C  
ANISOU 2559  CG  LYS A 364     4180   4552   4802    352    -27    381       C  
ATOM   2560  CD  LYS A 364     -55.515  30.650  70.213  1.00 41.54           C  
ANISOU 2560  CD  LYS A 364     4912   5311   5561    347     -1    357       C  
ATOM   2561  CE  LYS A 364     -56.985  30.327  70.274  1.00 49.93           C  
ANISOU 2561  CE  LYS A 364     5931   6395   6645    362     -6    358       C  
ATOM   2562  NZ  LYS A 364     -57.342  29.632  71.535  1.00 58.82           N  
ANISOU 2562  NZ  LYS A 364     7040   7530   7778    354     21    336       N  
ATOM   2563  N   ASP A 365     -54.818  33.765  66.464  1.00 24.60           N  
ANISOU 2563  N   ASP A 365     2825   3117   3406    387    -74    442       N  
ATOM   2564  CA  ASP A 365     -55.521  35.041  66.215  1.00 25.14           C  
ANISOU 2564  CA  ASP A 365     2888   3165   3500    422    -84    461       C  
ATOM   2565  C   ASP A 365     -54.549  36.174  65.787  1.00 29.90           C  
ANISOU 2565  C   ASP A 365     3530   3732   4096    425    -84    477       C  
ATOM   2566  O   ASP A 365     -54.763  37.338  66.133  1.00 30.75           O  
ANISOU 2566  O   ASP A 365     3644   3810   4228    451    -76    482       O  
ATOM   2567  CB  ASP A 365     -56.361  35.464  67.452  1.00 26.96           C  
ANISOU 2567  CB  ASP A 365     3093   3384   3765    448    -61    445       C  
ATOM   2568  CG  ASP A 365     -57.420  34.446  67.855  1.00 32.65           C  
ANISOU 2568  CG  ASP A 365     3771   4137   4495    447    -60    432       C  
ATOM   2569  OD1 ASP A 365     -57.828  33.639  66.992  1.00 32.55           O  
ANISOU 2569  OD1 ASP A 365     3741   4154   4471    435    -86    442       O  
ATOM   2570  OD2 ASP A 365     -57.879  34.496  69.016  1.00 37.20           O  
ANISOU 2570  OD2 ASP A 365     4331   4710   5093    458    -34    413       O  
ATOM   2571  N   GLY A 366     -53.500  35.808  65.037  1.00 25.76           N  
ANISOU 2571  N   GLY A 366     3034   3214   3541    398    -90    484       N  
ATOM   2572  CA  GLY A 366     -52.526  36.764  64.511  1.00 25.29           C  
ANISOU 2572  CA  GLY A 366     3012   3125   3472    395    -90    500       C  
ATOM   2573  C   GLY A 366     -51.476  37.214  65.518  1.00 29.16           C  
ANISOU 2573  C   GLY A 366     3527   3587   3967    385    -61    481       C  
ATOM   2574  O   GLY A 366     -50.688  38.121  65.229  1.00 29.23           O  
ANISOU 2574  O   GLY A 366     3566   3567   3974    383    -58    494       O  
ATOM   2575  N   TYR A 367     -51.440  36.570  66.705  1.00 24.80           N  
ANISOU 2575  N   TYR A 367     2962   3042   3420    377    -40    452       N  
ATOM   2576  CA  TYR A 367     -50.478  36.932  67.758  1.00 24.04           C  
ANISOU 2576  CA  TYR A 367     2887   2921   3326    366    -14    432       C  
ATOM   2577  C   TYR A 367     -49.828  35.678  68.380  1.00 25.74           C  
ANISOU 2577  C   TYR A 367     3099   3157   3522    337     -1    409       C  
ATOM   2578  O   TYR A 367     -50.416  34.595  68.342  1.00 25.05           O  
ANISOU 2578  O   TYR A 367     2987   3101   3429    331     -6    402       O  
ATOM   2579  CB  TYR A 367     -51.164  37.780  68.847  1.00 25.74           C  
ANISOU 2579  CB  TYR A 367     3096   3113   3572    394      3    419       C  
ATOM   2580  N   PRO A 368     -48.600  35.802  68.973  1.00 20.86           N  
ANISOU 2580  N   PRO A 368     2505   2523   2897    317     15    396       N  
ATOM   2581  CA  PRO A 368     -47.969  34.619  69.597  1.00 19.72           C  
ANISOU 2581  CA  PRO A 368     2357   2397   2737    291     26    375       C  
ATOM   2582  C   PRO A 368     -48.870  33.966  70.649  1.00 21.96           C  
ANISOU 2582  C   PRO A 368     2617   2698   3030    299     36    355       C  
ATOM   2583  O   PRO A 368     -49.420  34.655  71.508  1.00 21.23           O  
ANISOU 2583  O   PRO A 368     2521   2590   2957    318     49    345       O  
ATOM   2584  CB  PRO A 368     -46.687  35.186  70.220  1.00 21.42           C  
ANISOU 2584  CB  PRO A 368     2600   2587   2951    276     40    366       C  
ATOM   2585  CG  PRO A 368     -46.416  36.437  69.464  1.00 26.47           C  
ANISOU 2585  CG  PRO A 368     3261   3199   3598    286     33    387       C  
ATOM   2586  CD  PRO A 368     -47.750  37.003  69.100  1.00 22.42           C  
ANISOU 2586  CD  PRO A 368     2733   2684   3102    317     23    400       C  
ATOM   2587  N   TYR A 369     -49.060  32.641  70.546  1.00 18.04           N  
ANISOU 2587  N   TYR A 369     2102   2232   2520    284     33    349       N  
ATOM   2588  CA  TYR A 369     -49.904  31.880  71.471  1.00 17.77           C  
ANISOU 2588  CA  TYR A 369     2043   2215   2492    287     43    332       C  
ATOM   2589  C   TYR A 369     -49.131  31.619  72.788  1.00 21.79           C  
ANISOU 2589  C   TYR A 369     2566   2717   2997    272     64    310       C  
ATOM   2590  O   TYR A 369     -48.802  30.467  73.103  1.00 21.34           O  
ANISOU 2590  O   TYR A 369     2504   2678   2926    252     67    300       O  
ATOM   2591  CB  TYR A 369     -50.344  30.543  70.810  1.00 18.48           C  
ANISOU 2591  CB  TYR A 369     2111   2338   2570    274     30    335       C  
ATOM   2592  CG  TYR A 369     -51.529  29.864  71.474  1.00 19.63           C  
ANISOU 2592  CG  TYR A 369     2227   2505   2728    280     36    324       C  
ATOM   2593  CD1 TYR A 369     -52.148  30.425  72.590  1.00 21.30           C  
ANISOU 2593  CD1 TYR A 369     2430   2705   2958    298     55    312       C  
ATOM   2594  CD2 TYR A 369     -52.071  28.693  70.949  1.00 20.37           C  
ANISOU 2594  CD2 TYR A 369     2298   2626   2813    269     24    326       C  
ATOM   2595  CE1 TYR A 369     -53.245  29.812  73.194  1.00 21.72           C  
ANISOU 2595  CE1 TYR A 369     2454   2778   3023    304     64    303       C  
ATOM   2596  CE2 TYR A 369     -53.168  28.071  71.545  1.00 21.29           C  
ANISOU 2596  CE2 TYR A 369     2386   2762   2943    273     31    317       C  
ATOM   2597  CZ  TYR A 369     -53.747  28.629  72.673  1.00 27.59           C  
ANISOU 2597  CZ  TYR A 369     3173   3549   3759    290     52    306       C  
ATOM   2598  OH  TYR A 369     -54.827  28.020  73.262  1.00 28.06           O  
ANISOU 2598  OH  TYR A 369     3203   3628   3832    293     62    297       O  
ATOM   2599  N   LYS A 370     -48.828  32.703  73.540  1.00 18.19           N  
ANISOU 2599  N   LYS A 370     2128   2232   2551    282     77    302       N  
ATOM   2600  CA  LYS A 370     -48.018  32.629  74.766  1.00 17.89           C  
ANISOU 2600  CA  LYS A 370     2107   2184   2506    267     94    281       C  
ATOM   2601  C   LYS A 370     -48.725  31.870  75.902  1.00 20.25           C  
ANISOU 2601  C   LYS A 370     2390   2500   2805    267    110    263       C  
ATOM   2602  O   LYS A 370     -48.057  31.301  76.762  1.00 19.94           O  
ANISOU 2602  O   LYS A 370     2360   2463   2752    249    118    249       O  
ATOM   2603  CB  LYS A 370     -47.617  34.041  75.237  1.00 21.13           C  
ANISOU 2603  CB  LYS A 370     2542   2559   2928    277    102    277       C  
ATOM   2604  CG  LYS A 370     -46.677  34.765  74.277  1.00 33.53           C  
ANISOU 2604  CG  LYS A 370     4133   4110   4496    271     90    294       C  
ATOM   2605  CD  LYS A 370     -46.245  36.112  74.833  1.00 41.21           C  
ANISOU 2605  CD  LYS A 370     5132   5046   5481    277     99    288       C  
ATOM   2606  CE  LYS A 370     -45.250  36.799  73.935  1.00 48.80           C  
ANISOU 2606  CE  LYS A 370     6114   5988   6440    267     89    305       C  
ATOM   2607  NZ  LYS A 370     -44.769  38.075  74.525  1.00 56.15           N  
ANISOU 2607  NZ  LYS A 370     7071   6880   7383    269     98    297       N  
ATOM   2608  N   SER A 371     -50.069  31.897  75.924  1.00 15.53           N  
ANISOU 2608  N   SER A 371     1767   1912   2222    289    113    264       N  
ATOM   2609  CA  SER A 371     -50.843  31.284  77.013  1.00 14.51           C  
ANISOU 2609  CA  SER A 371     1621   1797   2095    290    132    247       C  
ATOM   2610  C   SER A 371     -51.183  29.798  76.749  1.00 16.46           C  
ANISOU 2610  C   SER A 371     1846   2077   2333    274    125    249       C  
ATOM   2611  O   SER A 371     -51.892  29.179  77.555  1.00 15.21           O  
ANISOU 2611  O   SER A 371     1670   1932   2175    273    140    238       O  
ATOM   2612  CB  SER A 371     -52.123  32.077  77.268  1.00 17.51           C  
ANISOU 2612  CB  SER A 371     1983   2171   2500    322    143    245       C  
ATOM   2613  OG  SER A 371     -52.959  32.079  76.121  1.00 24.41           O  
ANISOU 2613  OG  SER A 371     2831   3057   3387    336    124    265       O  
ATOM   2614  N   ARG A 372     -50.676  29.222  75.629  1.00 12.33           N  
ANISOU 2614  N   ARG A 372     1323   1565   1799    259    105    263       N  
ATOM   2615  CA  ARG A 372     -50.984  27.823  75.277  1.00 11.51           C  
ANISOU 2615  CA  ARG A 372     1199   1488   1685    243     97    265       C  
ATOM   2616  C   ARG A 372     -50.518  26.844  76.371  1.00 13.42           C  
ANISOU 2616  C   ARG A 372     1447   1737   1914    223    112    250       C  
ATOM   2617  O   ARG A 372     -49.334  26.806  76.710  1.00 11.52           O  
ANISOU 2617  O   ARG A 372     1230   1486   1661    208    114    245       O  
ATOM   2618  CB  ARG A 372     -50.365  27.442  73.919  1.00 11.79           C  
ANISOU 2618  CB  ARG A 372     1240   1530   1709    231     75    280       C  
ATOM   2619  CG  ARG A 372     -50.821  26.060  73.415  1.00 14.59           C  
ANISOU 2619  CG  ARG A 372     1574   1912   2056    216     65    281       C  
ATOM   2620  CD  ARG A 372     -49.980  25.571  72.254  1.00 15.97           C  
ANISOU 2620  CD  ARG A 372     1762   2091   2214    199     49    291       C  
ATOM   2621  NE  ARG A 372     -50.460  24.285  71.729  1.00 10.53           N  
ANISOU 2621  NE  ARG A 372     1055   1426   1518    185     39    290       N  
ATOM   2622  CZ  ARG A 372     -50.066  23.097  72.191  1.00 26.43           C  
ANISOU 2622  CZ  ARG A 372     3070   3448   3523    165     47    280       C  
ATOM   2623  NH1 ARG A 372     -49.214  23.021  73.205  1.00 14.82           N  
ANISOU 2623  NH1 ARG A 372     1616   1967   2049    157     62    270       N  
ATOM   2624  NH2 ARG A 372     -50.535  21.980  71.652  1.00 16.03           N  
ANISOU 2624  NH2 ARG A 372     1739   2150   2201    152     37    279       N  
ATOM   2625  N   PRO A 373     -51.432  25.988  76.888  1.00 10.78           N  
ANISOU 2625  N   PRO A 373     1090   1422   1583    220    122    243       N  
ATOM   2626  CA  PRO A 373     -51.014  25.003  77.894  1.00 10.52           C  
ANISOU 2626  CA  PRO A 373     1065   1396   1537    200    135    231       C  
ATOM   2627  C   PRO A 373     -50.153  23.900  77.291  1.00 14.97           C  
ANISOU 2627  C   PRO A 373     1635   1968   2085    176    121    236       C  
ATOM   2628  O   PRO A 373     -50.325  23.545  76.122  1.00 14.89           O  
ANISOU 2628  O   PRO A 373     1614   1968   2075    174    104    247       O  
ATOM   2629  CB  PRO A 373     -52.350  24.446  78.428  1.00 11.85           C  
ANISOU 2629  CB  PRO A 373     1205   1582   1715    204    148    226       C  
ATOM   2630  CG  PRO A 373     -53.417  25.372  77.878  1.00 16.45           C  
ANISOU 2630  CG  PRO A 373     1765   2164   2320    230    145    233       C  
ATOM   2631  CD  PRO A 373     -52.877  25.906  76.617  1.00 12.03           C  
ANISOU 2631  CD  PRO A 373     1215   1596   1759    234    121    247       C  
ATOM   2632  N   TYR A 374     -49.199  23.389  78.065  1.00 11.21           N  
ANISOU 2632  N   TYR A 374     1178   1488   1595    160    127    229       N  
ATOM   2633  CA  TYR A 374     -48.377  22.273  77.631  1.00 10.74           C  
ANISOU 2633  CA  TYR A 374     1122   1434   1523    139    117    232       C  
ATOM   2634  C   TYR A 374     -49.189  20.972  77.682  1.00 15.23           C  
ANISOU 2634  C   TYR A 374     1672   2023   2093    128    120    231       C  
ATOM   2635  O   TYR A 374     -49.932  20.751  78.636  1.00 14.27           O  
ANISOU 2635  O   TYR A 374     1541   1907   1974    129    135    224       O  
ATOM   2636  CB  TYR A 374     -47.121  22.153  78.513  1.00 11.14           C  
ANISOU 2636  CB  TYR A 374     1197   1473   1562    126    122    226       C  
ATOM   2637  CG  TYR A 374     -46.099  23.247  78.271  1.00 11.81           C  
ANISOU 2637  CG  TYR A 374     1302   1539   1647    130    116    228       C  
ATOM   2638  CD1 TYR A 374     -46.153  24.447  78.975  1.00 13.77           C  
ANISOU 2638  CD1 TYR A 374     1562   1772   1899    143    125    222       C  
ATOM   2639  CD2 TYR A 374     -45.027  23.048  77.403  1.00 11.87           C  
ANISOU 2639  CD2 TYR A 374     1317   1543   1649    120    104    236       C  
ATOM   2640  CE1 TYR A 374     -45.203  25.448  78.774  1.00 15.30           C  
ANISOU 2640  CE1 TYR A 374     1774   1946   2093    144    119    223       C  
ATOM   2641  CE2 TYR A 374     -44.049  24.025  77.224  1.00 12.51           C  
ANISOU 2641  CE2 TYR A 374     1415   1606   1731    121    100    238       C  
ATOM   2642  CZ  TYR A 374     -44.142  25.227  77.908  1.00 20.52           C  
ANISOU 2642  CZ  TYR A 374     2441   2605   2751    132    107    232       C  
ATOM   2643  OH  TYR A 374     -43.186  26.196  77.729  1.00 19.90           O  
ANISOU 2643  OH  TYR A 374     2380   2507   2674    131    102    235       O  
ATOM   2644  N   ASP A 375     -49.082  20.135  76.640  1.00 12.47           N  
ANISOU 2644  N   ASP A 375     1315   1682   1740    118    105    237       N  
ATOM   2645  CA  ASP A 375     -49.784  18.849  76.619  1.00 12.42           C  
ANISOU 2645  CA  ASP A 375     1291   1692   1734    104    106    236       C  
ATOM   2646  C   ASP A 375     -49.033  17.821  77.451  1.00 16.87           C  
ANISOU 2646  C   ASP A 375     1868   2253   2288     86    114    231       C  
ATOM   2647  O   ASP A 375     -47.841  17.580  77.213  1.00 16.67           O  
ANISOU 2647  O   ASP A 375     1860   2219   2253     78    108    232       O  
ATOM   2648  CB  ASP A 375     -49.965  18.350  75.175  1.00 13.95           C  
ANISOU 2648  CB  ASP A 375     1476   1897   1928     99     87    242       C  
ATOM   2649  CG  ASP A 375     -50.803  19.274  74.315  1.00 17.56           C  
ANISOU 2649  CG  ASP A 375     1918   2358   2394    116     75    250       C  
ATOM   2650  OD1 ASP A 375     -51.842  19.766  74.810  1.00 16.05           O  
ANISOU 2650  OD1 ASP A 375     1710   2173   2217    129     83    249       O  
ATOM   2651  OD2 ASP A 375     -50.466  19.441  73.126  1.00 24.03           O  
ANISOU 2651  OD2 ASP A 375     2744   3178   3207    116     59    257       O  
ATOM   2652  N   LEU A 376     -49.703  17.259  78.478  1.00 13.50           N  
ANISOU 2652  N   LEU A 376     1433   1833   1862     81    129    226       N  
ATOM   2653  CA  LEU A 376     -49.092  16.260  79.369  1.00 12.90           C  
ANISOU 2653  CA  LEU A 376     1371   1754   1776     64    137    224       C  
ATOM   2654  C   LEU A 376     -49.545  14.859  79.000  1.00 16.05           C  
ANISOU 2654  C   LEU A 376     1757   2164   2177     48    134    225       C  
ATOM   2655  O   LEU A 376     -48.714  13.990  78.749  1.00 15.86           O  
ANISOU 2655  O   LEU A 376     1745   2135   2148     35    127    227       O  
ATOM   2656  CB  LEU A 376     -49.437  16.569  80.850  1.00 13.39           C  
ANISOU 2656  CB  LEU A 376     1439   1815   1834     67    157    218       C  
ATOM   2657  CG  LEU A 376     -48.472  17.525  81.595  1.00 18.43           C  
ANISOU 2657  CG  LEU A 376     2101   2438   2462     74    160    214       C  
ATOM   2658  CD1 LEU A 376     -48.279  18.817  80.837  1.00 18.87           C  
ANISOU 2658  CD1 LEU A 376     2159   2486   2526     90    151    215       C  
ATOM   2659  CD2 LEU A 376     -48.967  17.810  82.993  1.00 21.32           C  
ANISOU 2659  CD2 LEU A 376     2474   2805   2823     76    181    206       C  
ATOM   2660  N   PHE A 377     -50.867  14.636  78.947  1.00 13.66           N  
ANISOU 2660  N   PHE A 377     1430   1874   1885     47    139    225       N  
ATOM   2661  CA  PHE A 377     -51.424  13.346  78.557  1.00 13.59           C  
ANISOU 2661  CA  PHE A 377     1408   1875   1880     30    135    225       C  
ATOM   2662  C   PHE A 377     -52.778  13.549  77.876  1.00 17.87           C  
ANISOU 2662  C   PHE A 377     1920   2434   2438     34    130    226       C  
ATOM   2663  O   PHE A 377     -53.721  14.037  78.509  1.00 16.91           O  
ANISOU 2663  O   PHE A 377     1780   2319   2325     43    144    225       O  
ATOM   2664  CB  PHE A 377     -51.571  12.419  79.783  1.00 15.58           C  
ANISOU 2664  CB  PHE A 377     1664   2127   2129     15    153    224       C  
ATOM   2665  CG  PHE A 377     -51.326  10.952  79.490  1.00 17.24           C  
ANISOU 2665  CG  PHE A 377     1878   2335   2338     -7    148    226       C  
ATOM   2666  CD1 PHE A 377     -51.930  10.331  78.398  1.00 20.86           C  
ANISOU 2666  CD1 PHE A 377     2320   2802   2805    -16    135    225       C  
ATOM   2667  CD2 PHE A 377     -50.581  10.170  80.361  1.00 18.67           C  
ANISOU 2667  CD2 PHE A 377     2079   2506   2510    -18    155    228       C  
ATOM   2668  CE1 PHE A 377     -51.699   8.980  78.127  1.00 21.62           C  
ANISOU 2668  CE1 PHE A 377     2421   2894   2900    -36    131    225       C  
ATOM   2669  CE2 PHE A 377     -50.372   8.811  80.102  1.00 21.99           C  
ANISOU 2669  CE2 PHE A 377     2503   2920   2930    -36    151    230       C  
ATOM   2670  CZ  PHE A 377     -50.935   8.225  78.988  1.00 20.27           C  
ANISOU 2670  CZ  PHE A 377     2270   2709   2722    -45    140    227       C  
ATOM   2671  N   LEU A 378     -52.867  13.209  76.572  1.00 14.39           N  
ANISOU 2671  N   LEU A 378     1472   1998   1998     29    110    228       N  
ATOM   2672  CA  LEU A 378     -54.101  13.384  75.801  1.00 14.52           C  
ANISOU 2672  CA  LEU A 378     1458   2031   2028     33     99    230       C  
ATOM   2673  C   LEU A 378     -54.786  12.045  75.566  1.00 17.18           C  
ANISOU 2673  C   LEU A 378     1780   2379   2371      9     96    227       C  
ATOM   2674  O   LEU A 378     -54.113  11.015  75.479  1.00 15.57           O  
ANISOU 2674  O   LEU A 378     1592   2167   2157     -8     94    225       O  
ATOM   2675  CB  LEU A 378     -53.802  14.072  74.451  1.00 14.99           C  
ANISOU 2675  CB  LEU A 378     1521   2090   2083     43     76    234       C  
ATOM   2676  CG  LEU A 378     -52.995  15.394  74.522  1.00 20.08           C  
ANISOU 2676  CG  LEU A 378     2185   2722   2723     64     77    238       C  
ATOM   2677  CD1 LEU A 378     -52.724  15.936  73.138  1.00 20.01           C  
ANISOU 2677  CD1 LEU A 378     2181   2713   2707     71     55    244       C  
ATOM   2678  CD2 LEU A 378     -53.719  16.441  75.368  1.00 23.53           C  
ANISOU 2678  CD2 LEU A 378     2609   3159   3172     84     91    238       C  
ATOM   2679  N   SER A 379     -56.133  12.061  75.406  1.00 14.23           N  
ANISOU 2679  N   SER A 379     1372   2021   2013      9     93    228       N  
ATOM   2680  CA  SER A 379     -56.930  10.837  75.208  1.00 14.25           C  
ANISOU 2680  CA  SER A 379     1356   2035   2024    -15     90    226       C  
ATOM   2681  C   SER A 379     -56.454  10.019  73.996  1.00 19.11           C  
ANISOU 2681  C   SER A 379     1984   2648   2629    -32     67    223       C  
ATOM   2682  O   SER A 379     -56.625   8.802  73.976  1.00 18.42           O  
ANISOU 2682  O   SER A 379     1895   2560   2542    -56     67    218       O  
ATOM   2683  CB  SER A 379     -58.413  11.176  75.069  1.00 16.44           C  
ANISOU 2683  CB  SER A 379     1592   2332   2322    -10     87    228       C  
ATOM   2684  OG  SER A 379     -58.666  11.918  73.888  1.00 19.46           O  
ANISOU 2684  OG  SER A 379     1965   2723   2707      4     61    233       O  
ATOM   2685  N   GLU A 380     -55.843  10.698  72.984  1.00 16.57           N  
ANISOU 2685  N   GLU A 380     1676   2324   2296    -19     48    225       N  
ATOM   2686  CA  GLU A 380     -55.298  10.028  71.785  1.00 16.69           C  
ANISOU 2686  CA  GLU A 380     1707   2336   2297    -33     29    221       C  
ATOM   2687  C   GLU A 380     -54.323   8.932  72.175  1.00 19.49           C  
ANISOU 2687  C   GLU A 380     2088   2675   2644    -50     40    215       C  
ATOM   2688  O   GLU A 380     -54.433   7.806  71.688  1.00 19.26           O  
ANISOU 2688  O   GLU A 380     2061   2645   2613    -71     33    208       O  
ATOM   2689  CB  GLU A 380     -54.583  11.045  70.861  1.00 18.06           C  
ANISOU 2689  CB  GLU A 380     1898   2507   2458    -16     15    226       C  
ATOM   2690  CG  GLU A 380     -55.479  12.139  70.331  1.00 25.13           C  
ANISOU 2690  CG  GLU A 380     2771   3417   3362      2     -1    234       C  
ATOM   2691  CD  GLU A 380     -55.583  13.368  71.210  1.00 27.82           C  
ANISOU 2691  CD  GLU A 380     3106   3753   3713     27     14    240       C  
ATOM   2692  OE1 GLU A 380     -56.202  13.271  72.290  1.00 17.51           O  
ANISOU 2692  OE1 GLU A 380     1782   2449   2421     28     32    239       O  
ATOM   2693  OE2 GLU A 380     -55.158  14.454  70.758  1.00 19.48           O  
ANISOU 2693  OE2 GLU A 380     2060   2691   2651     46      7    247       O  
ATOM   2694  N   GLU A 381     -53.346   9.267  73.050  1.00 15.01           N  
ANISOU 2694  N   GLU A 381     1540   2092   2070    -39     57    217       N  
ATOM   2695  CA  GLU A 381     -52.298   8.333  73.468  1.00 14.16           C  
ANISOU 2695  CA  GLU A 381     1457   1968   1956    -51     67    213       C  
ATOM   2696  C   GLU A 381     -52.883   7.080  74.114  1.00 18.07           C  
ANISOU 2696  C   GLU A 381     1944   2462   2460    -72     77    211       C  
ATOM   2697  O   GLU A 381     -52.475   5.970  73.773  1.00 17.60           O  
ANISOU 2697  O   GLU A 381     1897   2392   2397    -89     74    205       O  
ATOM   2698  CB  GLU A 381     -51.307   9.021  74.420  1.00 14.78           C  
ANISOU 2698  CB  GLU A 381     1553   2034   2030    -36     81    218       C  
ATOM   2699  CG  GLU A 381     -50.136   8.134  74.809  1.00 21.27           C  
ANISOU 2699  CG  GLU A 381     2399   2838   2845    -45     88    216       C  
ATOM   2700  CD  GLU A 381     -49.097   8.799  75.687  1.00 30.15           C  
ANISOU 2700  CD  GLU A 381     3539   3951   3964    -32     97    221       C  
ATOM   2701  OE1 GLU A 381     -48.853  10.015  75.506  1.00 17.19           O  
ANISOU 2701  OE1 GLU A 381     1899   2311   2319    -15     94    223       O  
ATOM   2702  OE2 GLU A 381     -48.448   8.079  76.479  1.00 20.08           O  
ANISOU 2702  OE2 GLU A 381     2278   2665   2688    -39    105    222       O  
ATOM   2703  N   VAL A 382     -53.868   7.256  75.035  1.00 14.05           N  
ANISOU 2703  N   VAL A 382     1414   1963   1962    -72     89    214       N  
ATOM   2704  CA  VAL A 382     -54.529   6.125  75.709  1.00 13.58           C  
ANISOU 2704  CA  VAL A 382     1345   1903   1911    -94    101    213       C  
ATOM   2705  C   VAL A 382     -55.088   5.125  74.682  1.00 16.52           C  
ANISOU 2705  C   VAL A 382     1709   2280   2290   -116     85    207       C  
ATOM   2706  O   VAL A 382     -54.881   3.914  74.824  1.00 15.69           O  
ANISOU 2706  O   VAL A 382     1614   2162   2185   -137     89    204       O  
ATOM   2707  CB  VAL A 382     -55.627   6.615  76.700  1.00 17.60           C  
ANISOU 2707  CB  VAL A 382     1829   2425   2433    -90    119    218       C  
ATOM   2708  CG1 VAL A 382     -56.506   5.458  77.167  1.00 17.53           C  
ANISOU 2708  CG1 VAL A 382     1806   2420   2436   -116    129    218       C  
ATOM   2709  CG2 VAL A 382     -55.002   7.340  77.892  1.00 16.99           C  
ANISOU 2709  CG2 VAL A 382     1769   2341   2347    -74    138    222       C  
ATOM   2710  N   HIS A 383     -55.716   5.641  73.598  1.00 11.91           N  
ANISOU 2710  N   HIS A 383     1106   1711   1707   -112     65    204       N  
ATOM   2711  CA  HIS A 383     -56.242   4.794  72.533  1.00 10.79           C  
ANISOU 2711  CA  HIS A 383      958   1575   1568   -134     46    197       C  
ATOM   2712  C   HIS A 383     -55.120   4.057  71.785  1.00 13.90           C  
ANISOU 2712  C   HIS A 383     1384   1952   1947   -142     38    188       C  
ATOM   2713  O   HIS A 383     -55.238   2.860  71.536  1.00 13.08           O  
ANISOU 2713  O   HIS A 383     1285   1840   1845   -165     36    181       O  
ATOM   2714  CB  HIS A 383     -57.100   5.610  71.556  1.00 11.18           C  
ANISOU 2714  CB  HIS A 383      982   1646   1620   -125     23    198       C  
ATOM   2715  CG  HIS A 383     -58.374   6.127  72.156  1.00 14.03           C  
ANISOU 2715  CG  HIS A 383     1305   2025   2001   -120     29    204       C  
ATOM   2716  ND1 HIS A 383     -59.374   5.264  72.579  1.00 15.59           N  
ANISOU 2716  ND1 HIS A 383     1479   2230   2216   -143     35    202       N  
ATOM   2717  CD2 HIS A 383     -58.813   7.400  72.284  1.00 15.26           C  
ANISOU 2717  CD2 HIS A 383     1443   2192   2164    -95     28    212       C  
ATOM   2718  CE1 HIS A 383     -60.349   6.038  73.023  1.00 15.04           C  
ANISOU 2718  CE1 HIS A 383     1375   2176   2163   -130     41    209       C  
ATOM   2719  NE2 HIS A 383     -60.055   7.333  72.871  1.00 15.21           N  
ANISOU 2719  NE2 HIS A 383     1399   2200   2179   -100     37    214       N  
ATOM   2720  N   PHE A 384     -54.005   4.763  71.475  1.00 10.32           N  
ANISOU 2720  N   PHE A 384      952   1491   1479   -123     37    190       N  
ATOM   2721  CA  PHE A 384     -52.878   4.143  70.760  1.00  9.61           C  
ANISOU 2721  CA  PHE A 384      892   1385   1376   -128     34    182       C  
ATOM   2722  C   PHE A 384     -52.093   3.175  71.642  1.00 15.29           C  
ANISOU 2722  C   PHE A 384     1630   2082   2099   -135     52    182       C  
ATOM   2723  O   PHE A 384     -51.482   2.233  71.128  1.00 14.99           O  
ANISOU 2723  O   PHE A 384     1611   2029   2057   -146     50    173       O  
ATOM   2724  CB  PHE A 384     -51.956   5.204  70.155  1.00 10.44           C  
ANISOU 2724  CB  PHE A 384     1011   1489   1466   -106     28    185       C  
ATOM   2725  CG  PHE A 384     -52.605   6.018  69.060  1.00 11.24           C  
ANISOU 2725  CG  PHE A 384     1101   1609   1562   -100      7    186       C  
ATOM   2726  CD1 PHE A 384     -53.046   5.411  67.888  1.00 12.67           C  
ANISOU 2726  CD1 PHE A 384     1283   1798   1735   -117    -12    177       C  
ATOM   2727  CD2 PHE A 384     -52.693   7.402  69.159  1.00 12.48           C  
ANISOU 2727  CD2 PHE A 384     1250   1775   1718    -77      5    197       C  
ATOM   2728  CE1 PHE A 384     -53.646   6.164  66.877  1.00 13.19           C  
ANISOU 2728  CE1 PHE A 384     1338   1881   1792   -111    -34    180       C  
ATOM   2729  CE2 PHE A 384     -53.262   8.157  68.132  1.00 14.70           C  
ANISOU 2729  CE2 PHE A 384     1522   2072   1994    -70    -16    201       C  
ATOM   2730  CZ  PHE A 384     -53.740   7.532  66.999  1.00 12.54           C  
ANISOU 2730  CZ  PHE A 384     1246   1807   1711    -87    -37    193       C  
ATOM   2731  N   LEU A 385     -52.115   3.393  72.975  1.00 13.14           N  
ANISOU 2731  N   LEU A 385     1353   1807   1834   -129     69    191       N  
ATOM   2732  CA  LEU A 385     -51.493   2.466  73.923  1.00 12.97           C  
ANISOU 2732  CA  LEU A 385     1348   1765   1815   -137     84    194       C  
ATOM   2733  C   LEU A 385     -52.251   1.143  73.924  1.00 16.66           C  
ANISOU 2733  C   LEU A 385     1809   2228   2293   -164     85    189       C  
ATOM   2734  O   LEU A 385     -51.640   0.083  73.797  1.00 15.82           O  
ANISOU 2734  O   LEU A 385     1722   2101   2187   -175     87    184       O  
ATOM   2735  CB  LEU A 385     -51.477   3.071  75.345  1.00 12.82           C  
ANISOU 2735  CB  LEU A 385     1326   1748   1798   -126    100    205       C  
ATOM   2736  CG  LEU A 385     -50.484   4.221  75.576  1.00 17.03           C  
ANISOU 2736  CG  LEU A 385     1871   2278   2321   -102    102    210       C  
ATOM   2737  CD1 LEU A 385     -50.785   4.947  76.878  1.00 16.51           C  
ANISOU 2737  CD1 LEU A 385     1799   2218   2255    -92    116    218       C  
ATOM   2738  CD2 LEU A 385     -49.050   3.718  75.570  1.00 20.16           C  
ANISOU 2738  CD2 LEU A 385     2293   2654   2713    -99    103    210       C  
ATOM   2739  N   LYS A 386     -53.601   1.210  73.997  1.00 13.51           N  
ANISOU 2739  N   LYS A 386     1383   1846   1904   -175     83    189       N  
ATOM   2740  CA  LYS A 386     -54.455   0.017  73.944  1.00 13.33           C  
ANISOU 2740  CA  LYS A 386     1350   1821   1893   -204     83    184       C  
ATOM   2741  C   LYS A 386     -54.410  -0.625  72.553  1.00 16.00           C  
ANISOU 2741  C   LYS A 386     1697   2156   2227   -218     64    170       C  
ATOM   2742  O   LYS A 386     -54.381  -1.850  72.446  1.00 15.70           O  
ANISOU 2742  O   LYS A 386     1670   2101   2194   -239     65    163       O  
ATOM   2743  CB  LYS A 386     -55.908   0.369  74.323  1.00 15.27           C  
ANISOU 2743  CB  LYS A 386     1560   2089   2152   -211     85    189       C  
ATOM   2744  CG  LYS A 386     -56.084   0.736  75.798  1.00 30.02           C  
ANISOU 2744  CG  LYS A 386     3422   3959   4024   -203    110    201       C  
ATOM   2745  CD  LYS A 386     -57.548   1.070  76.138  1.00 42.26           C  
ANISOU 2745  CD  LYS A 386     4934   5532   5589   -209    115    204       C  
ATOM   2746  CE  LYS A 386     -57.976   2.412  75.590  1.00 54.01           C  
ANISOU 2746  CE  LYS A 386     6401   7042   7078   -187    103    204       C  
ATOM   2747  NZ  LYS A 386     -59.408   2.691  75.872  1.00 64.42           N  
ANISOU 2747  NZ  LYS A 386     7679   8382   8416   -192    108    207       N  
ATOM   2748  N   ALA A 387     -54.358   0.215  71.479  1.00 11.52           N  
ANISOU 2748  N   ALA A 387     1126   1602   1648   -205     46    165       N  
ATOM   2749  CA  ALA A 387     -54.298  -0.274  70.094  1.00 11.03           C  
ANISOU 2749  CA  ALA A 387     1075   1539   1577   -218     26    150       C  
ATOM   2750  C   ALA A 387     -53.062  -1.145  69.859  1.00 13.73           C  
ANISOU 2750  C   ALA A 387     1450   1854   1911   -220     34    142       C  
ATOM   2751  O   ALA A 387     -53.163  -2.191  69.207  1.00 13.73           O  
ANISOU 2751  O   ALA A 387     1462   1844   1912   -241     28    128       O  
ATOM   2752  CB  ALA A 387     -54.304   0.898  69.123  1.00 11.81           C  
ANISOU 2752  CB  ALA A 387     1169   1657   1662   -200      8    151       C  
ATOM   2753  N   GLU A 388     -51.889  -0.724  70.400  1.00  8.55           N  
ANISOU 2753  N   GLU A 388      811   1186   1251   -199     47    149       N  
ATOM   2754  CA  GLU A 388     -50.649  -1.490  70.253  1.00  7.97           C  
ANISOU 2754  CA  GLU A 388      767   1087   1175   -197     56    143       C  
ATOM   2755  C   GLU A 388     -50.754  -2.842  70.964  1.00 13.22           C  
ANISOU 2755  C   GLU A 388     1439   1729   1854   -216     67    143       C  
ATOM   2756  O   GLU A 388     -50.384  -3.867  70.392  1.00 13.43           O  
ANISOU 2756  O   GLU A 388     1483   1736   1881   -228     67    130       O  
ATOM   2757  CB  GLU A 388     -49.442  -0.696  70.786  1.00  8.91           C  
ANISOU 2757  CB  GLU A 388      897   1200   1289   -171     66    153       C  
ATOM   2758  CG  GLU A 388     -48.146  -1.498  70.753  1.00 14.99           C  
ANISOU 2758  CG  GLU A 388     1693   1943   2061   -167     76    149       C  
ATOM   2759  CD  GLU A 388     -46.927  -0.824  71.347  1.00 22.10           C  
ANISOU 2759  CD  GLU A 388     2601   2836   2958   -144     85    160       C  
ATOM   2760  OE1 GLU A 388     -46.965   0.410  71.553  1.00 13.85           O  
ANISOU 2760  OE1 GLU A 388     1546   1808   1908   -129     83    168       O  
ATOM   2761  OE2 GLU A 388     -45.908  -1.524  71.547  1.00  9.27           O  
ANISOU 2761  OE2 GLU A 388      993   1190   1340   -140     94    159       O  
ATOM   2762  N   LEU A 389     -51.250  -2.843  72.217  1.00 10.55           N  
ANISOU 2762  N   LEU A 389     1088   1394   1527   -219     78    156       N  
ATOM   2763  CA  LEU A 389     -51.423  -4.079  72.994  1.00 11.29           C  
ANISOU 2763  CA  LEU A 389     1188   1466   1634   -238     90    160       C  
ATOM   2764  C   LEU A 389     -52.372  -5.070  72.285  1.00 15.85           C  
ANISOU 2764  C   LEU A 389     1760   2041   2219   -268     81    146       C  
ATOM   2765  O   LEU A 389     -52.132  -6.276  72.316  1.00 15.44           O  
ANISOU 2765  O   LEU A 389     1726   1964   2176   -284     86    141       O  
ATOM   2766  CB  LEU A 389     -51.948  -3.759  74.404  1.00 11.36           C  
ANISOU 2766  CB  LEU A 389     1184   1484   1650   -237    103    177       C  
ATOM   2767  CG  LEU A 389     -50.998  -2.954  75.303  1.00 15.90           C  
ANISOU 2767  CG  LEU A 389     1767   2056   2217   -211    113    191       C  
ATOM   2768  CD1 LEU A 389     -51.747  -2.314  76.441  1.00 16.12           C  
ANISOU 2768  CD1 LEU A 389     1778   2101   2246   -209    124    203       C  
ATOM   2769  CD2 LEU A 389     -49.857  -3.830  75.828  1.00 18.20           C  
ANISOU 2769  CD2 LEU A 389     2086   2319   2512   -209    121    196       C  
ATOM   2770  N   TYR A 390     -53.445  -4.552  71.637  1.00 12.91           N  
ANISOU 2770  N   TYR A 390     1364   1695   1845   -277     66    140       N  
ATOM   2771  CA  TYR A 390     -54.434  -5.406  70.954  1.00 13.35           C  
ANISOU 2771  CA  TYR A 390     1411   1752   1908   -308     54    127       C  
ATOM   2772  C   TYR A 390     -53.910  -5.912  69.604  1.00 17.86           C  
ANISOU 2772  C   TYR A 390     2006   2313   2468   -314     40    106       C  
ATOM   2773  O   TYR A 390     -54.222  -7.036  69.205  1.00 16.52           O  
ANISOU 2773  O   TYR A 390     1845   2127   2305   -340     37     93       O  
ATOM   2774  CB  TYR A 390     -55.779  -4.656  70.757  1.00 14.42           C  
ANISOU 2774  CB  TYR A 390     1510   1922   2048   -314     40    130       C  
ATOM   2775  CG  TYR A 390     -56.447  -4.205  72.047  1.00 15.44           C  
ANISOU 2775  CG  TYR A 390     1613   2062   2190   -310     56    147       C  
ATOM   2776  CD1 TYR A 390     -56.293  -4.933  73.227  1.00 17.44           C  
ANISOU 2776  CD1 TYR A 390     1876   2298   2454   -318     78    157       C  
ATOM   2777  CD2 TYR A 390     -57.362  -3.153  72.050  1.00 15.91           C  
ANISOU 2777  CD2 TYR A 390     1639   2152   2252   -301     49    153       C  
ATOM   2778  CE1 TYR A 390     -56.953  -4.561  74.400  1.00 18.29           C  
ANISOU 2778  CE1 TYR A 390     1963   2417   2571   -317     95    172       C  
ATOM   2779  CE2 TYR A 390     -58.042  -2.785  73.211  1.00 16.72           C  
ANISOU 2779  CE2 TYR A 390     1719   2266   2367   -298     67    167       C  
ATOM   2780  CZ  TYR A 390     -57.823  -3.482  74.388  1.00 24.32           C  
ANISOU 2780  CZ  TYR A 390     2693   3211   3337   -307     91    176       C  
ATOM   2781  OH  TYR A 390     -58.480  -3.111  75.539  1.00 23.68           O  
ANISOU 2781  OH  TYR A 390     2592   3142   3265   -305    111    189       O  
ATOM   2782  N   ALA A 391     -53.141  -5.070  68.883  1.00 15.51           N  
ANISOU 2782  N   ALA A 391     1718   2022   2152   -291     34    103       N  
ATOM   2783  CA  ALA A 391     -52.600  -5.448  67.573  1.00 15.07           C  
ANISOU 2783  CA  ALA A 391     1686   1958   2081   -295     24     83       C  
ATOM   2784  C   ALA A 391     -51.482  -6.479  67.704  1.00 18.44           C  
ANISOU 2784  C   ALA A 391     2144   2350   2513   -294     41     76       C  
ATOM   2785  O   ALA A 391     -51.312  -7.314  66.819  1.00 18.84           O  
ANISOU 2785  O   ALA A 391     2215   2385   2559   -308     37     56       O  
ATOM   2786  CB  ALA A 391     -52.093  -4.221  66.844  1.00 15.38           C  
ANISOU 2786  CB  ALA A 391     1727   2016   2100   -271     16     85       C  
ATOM   2787  N   ARG A 392     -50.736  -6.439  68.820  1.00 14.41           N  
ANISOU 2787  N   ARG A 392     1638   1825   2012   -277     59     92       N  
ATOM   2788  CA  ARG A 392     -49.609  -7.352  69.040  1.00 14.18           C  
ANISOU 2788  CA  ARG A 392     1636   1762   1991   -272     74     89       C  
ATOM   2789  C   ARG A 392     -50.041  -8.661  69.729  1.00 17.89           C  
ANISOU 2789  C   ARG A 392     2111   2207   2480   -295     82     90       C  
ATOM   2790  O   ARG A 392     -49.205  -9.536  69.975  1.00 17.91           O  
ANISOU 2790  O   ARG A 392     2136   2178   2493   -291     94     89       O  
ATOM   2791  CB  ARG A 392     -48.497  -6.655  69.838  1.00 12.45           C  
ANISOU 2791  CB  ARG A 392     1420   1539   1771   -242     86    106       C  
ATOM   2792  CG  ARG A 392     -47.866  -5.481  69.090  1.00 19.95           C  
ANISOU 2792  CG  ARG A 392     2370   2507   2703   -219     81    103       C  
ATOM   2793  CD  ARG A 392     -46.759  -4.838  69.887  1.00 20.87           C  
ANISOU 2793  CD  ARG A 392     2489   2619   2822   -193     92    119       C  
ATOM   2794  NE  ARG A 392     -45.601  -5.721  70.023  1.00 19.55           N  
ANISOU 2794  NE  ARG A 392     2342   2421   2665   -186    105    117       N  
ATOM   2795  CZ  ARG A 392     -44.519  -5.410  70.722  1.00 27.25           C  
ANISOU 2795  CZ  ARG A 392     3321   3387   3645   -165    113    130       C  
ATOM   2796  NH1 ARG A 392     -44.446  -4.252  71.361  1.00 16.18           N  
ANISOU 2796  NH1 ARG A 392     1906   2004   2238   -150    111    145       N  
ATOM   2797  NH2 ARG A 392     -43.508  -6.263  70.805  1.00 15.47           N  
ANISOU 2797  NH2 ARG A 392     1844   1867   2165   -158    123    128       N  
ATOM   2798  N   GLY A 393     -51.341  -8.792  69.998  1.00 13.84           N  
ANISOU 2798  N   GLY A 393     1577   1707   1974   -318     76     93       N  
ATOM   2799  CA  GLY A 393     -51.901  -9.990  70.615  1.00 13.49           C  
ANISOU 2799  CA  GLY A 393     1535   1642   1949   -344     83     95       C  
ATOM   2800  C   GLY A 393     -51.537 -10.147  72.078  1.00 16.26           C  
ANISOU 2800  C   GLY A 393     1888   1979   2312   -335    101    119       C  
ATOM   2801  O   GLY A 393     -51.696 -11.230  72.646  1.00 16.88           O  
ANISOU 2801  O   GLY A 393     1977   2033   2406   -353    110    123       O  
ATOM   2802  N   PHE A 394     -51.037  -9.069  72.700  1.00 11.18           N  
ANISOU 2802  N   PHE A 394     1238   1352   1660   -308    105    134       N  
ATOM   2803  CA  PHE A 394     -50.669  -9.076  74.118  1.00 10.44           C  
ANISOU 2803  CA  PHE A 394     1146   1249   1572   -298    120    157       C  
ATOM   2804  C   PHE A 394     -51.914  -9.157  74.990  1.00 14.22           C  
ANISOU 2804  C   PHE A 394     1605   1740   2059   -319    126    169       C  
ATOM   2805  O   PHE A 394     -51.936  -9.903  75.963  1.00 13.45           O  
ANISOU 2805  O   PHE A 394     1515   1623   1970   -329    139    183       O  
ATOM   2806  CB  PHE A 394     -49.840  -7.820  74.466  1.00 11.69           C  
ANISOU 2806  CB  PHE A 394     1303   1423   1718   -266    121    168       C  
ATOM   2807  CG  PHE A 394     -48.360  -7.924  74.138  1.00 13.12           C  
ANISOU 2807  CG  PHE A 394     1506   1583   1896   -244    122    165       C  
ATOM   2808  CD1 PHE A 394     -47.931  -8.539  72.965  1.00 16.44           C  
ANISOU 2808  CD1 PHE A 394     1940   1988   2317   -247    118    144       C  
ATOM   2809  CD2 PHE A 394     -47.410  -7.296  74.935  1.00 15.31           C  
ANISOU 2809  CD2 PHE A 394     1787   1860   2170   -220    127    180       C  
ATOM   2810  CE1 PHE A 394     -46.571  -8.620  72.655  1.00 17.45           C  
ANISOU 2810  CE1 PHE A 394     2087   2099   2445   -226    123    141       C  
ATOM   2811  CE2 PHE A 394     -46.050  -7.362  74.615  1.00 18.45           C  
ANISOU 2811  CE2 PHE A 394     2201   2241   2568   -200    128    178       C  
ATOM   2812  CZ  PHE A 394     -45.640  -8.019  73.475  1.00 16.52           C  
ANISOU 2812  CZ  PHE A 394     1969   1980   2326   -202    127    158       C  
ATOM   2813  N   ILE A 395     -52.966  -8.393  74.625  1.00 12.33           N  
ANISOU 2813  N   ILE A 395     1336   1532   1815   -325    117    165       N  
ATOM   2814  CA  ILE A 395     -54.272  -8.438  75.302  1.00 12.93           C  
ANISOU 2814  CA  ILE A 395     1387   1624   1901   -346    124    174       C  
ATOM   2815  C   ILE A 395     -55.380  -8.537  74.248  1.00 17.42           C  
ANISOU 2815  C   ILE A 395     1934   2209   2475   -369    107    157       C  
ATOM   2816  O   ILE A 395     -55.276  -7.910  73.186  1.00 15.80           O  
ANISOU 2816  O   ILE A 395     1725   2019   2259   -359     90    144       O  
ATOM   2817  CB  ILE A 395     -54.475  -7.187  76.232  1.00 15.96           C  
ANISOU 2817  CB  ILE A 395     1752   2034   2278   -326    133    190       C  
ATOM   2818  CG1 ILE A 395     -53.325  -7.062  77.266  1.00 16.06           C  
ANISOU 2818  CG1 ILE A 395     1788   2030   2283   -304    146    206       C  
ATOM   2819  CG2 ILE A 395     -55.863  -7.237  76.934  1.00 17.60           C  
ANISOU 2819  CG2 ILE A 395     1932   2258   2497   -347    144    198       C  
ATOM   2820  CD1 ILE A 395     -53.335  -5.743  78.072  1.00 20.80           C  
ANISOU 2820  CD1 ILE A 395     2377   2654   2872   -282    153    217       C  
ATOM   2821  N   ALA A 396     -56.429  -9.340  74.524  1.00 15.78           N  
ANISOU 2821  N   ALA A 396     1713   1999   2283   -401    111    158       N  
ATOM   2822  CA  ALA A 396     -57.560  -9.475  73.600  1.00 16.35           C  
ANISOU 2822  CA  ALA A 396     1761   2089   2363   -426     93    143       C  
ATOM   2823  C   ALA A 396     -58.369  -8.172  73.537  1.00 20.89           C  
ANISOU 2823  C   ALA A 396     2298   2704   2935   -413     86    148       C  
ATOM   2824  O   ALA A 396     -58.705  -7.597  74.576  1.00 20.66           O  
ANISOU 2824  O   ALA A 396     2252   2688   2910   -404    102    164       O  
ATOM   2825  CB  ALA A 396     -58.455 -10.626  74.032  1.00 17.32           C  
ANISOU 2825  CB  ALA A 396     1876   2198   2506   -464    102    145       C  
ATOM   2826  N   GLY A 397     -58.625  -7.696  72.324  1.00 17.60           N  
ANISOU 2826  N   GLY A 397     1872   2305   2511   -411     61    133       N  
ATOM   2827  CA  GLY A 397     -59.373  -6.462  72.114  1.00 17.55           C  
ANISOU 2827  CA  GLY A 397     1830   2334   2502   -397     50    137       C  
ATOM   2828  C   GLY A 397     -59.404  -6.012  70.671  1.00 21.10           C  
ANISOU 2828  C   GLY A 397     2280   2800   2939   -394     20    122       C  
ATOM   2829  O   GLY A 397     -58.687  -6.561  69.827  1.00 20.45           O  
ANISOU 2829  O   GLY A 397     2227   2699   2844   -398     10    107       O  
ATOM   2830  N   ASP A 398     -60.227  -4.990  70.376  1.00 17.67           N  
ANISOU 2830  N   ASP A 398     1811   2397   2505   -385      5    127       N  
ATOM   2831  CA  ASP A 398     -60.382  -4.473  69.019  1.00 17.92           C  
ANISOU 2831  CA  ASP A 398     1839   2446   2523   -381    -26    116       C  
ATOM   2832  C   ASP A 398     -59.328  -3.387  68.724  1.00 21.26           C  
ANISOU 2832  C   ASP A 398     2281   2871   2924   -344    -26    120       C  
ATOM   2833  O   ASP A 398     -59.493  -2.231  69.126  1.00 19.85           O  
ANISOU 2833  O   ASP A 398     2084   2711   2747   -319    -23    133       O  
ATOM   2834  CB  ASP A 398     -61.812  -3.926  68.813  1.00 20.32           C  
ANISOU 2834  CB  ASP A 398     2095   2784   2843   -389    -44    120       C  
ATOM   2835  CG  ASP A 398     -62.168  -3.624  67.362  1.00 32.93           C  
ANISOU 2835  CG  ASP A 398     3687   4399   4426   -393    -81    109       C  
ATOM   2836  OD1 ASP A 398     -61.238  -3.544  66.524  1.00 33.50           O  
ANISOU 2836  OD1 ASP A 398     3794   4463   4474   -384    -91    100       O  
ATOM   2837  OD2 ASP A 398     -63.364  -3.411  67.079  1.00 40.60           O  
ANISOU 2837  OD2 ASP A 398     4619   5396   5411   -406   -101    111       O  
ATOM   2838  N   ALA A 399     -58.238  -3.771  68.032  1.00 18.23           N  
ANISOU 2838  N   ALA A 399     1937   2469   2523   -341    -29    108       N  
ATOM   2839  CA  ALA A 399     -57.139  -2.855  67.717  1.00 17.70           C  
ANISOU 2839  CA  ALA A 399     1889   2400   2435   -309    -27    111       C  
ATOM   2840  C   ALA A 399     -57.578  -1.748  66.746  1.00 19.85           C  
ANISOU 2840  C   ALA A 399     2146   2700   2694   -297    -53    112       C  
ATOM   2841  O   ALA A 399     -57.230  -0.585  66.946  1.00 19.33           O  
ANISOU 2841  O   ALA A 399     2077   2644   2623   -268    -50    124       O  
ATOM   2842  CB  ALA A 399     -55.966  -3.629  67.134  1.00 18.51           C  
ANISOU 2842  CB  ALA A 399     2033   2476   2523   -312    -23     97       C  
ATOM   2843  N   LYS A 400     -58.360  -2.113  65.702  1.00 15.35           N  
ANISOU 2843  N   LYS A 400     1568   2143   2120   -319    -80    101       N  
ATOM   2844  CA  LYS A 400     -58.840  -1.155  64.697  1.00 15.37           C  
ANISOU 2844  CA  LYS A 400     1558   2173   2110   -310   -109    103       C  
ATOM   2845  C   LYS A 400     -59.658  -0.031  65.342  1.00 18.87           C  
ANISOU 2845  C   LYS A 400     1962   2640   2570   -291   -110    122       C  
ATOM   2846  O   LYS A 400     -59.397   1.147  65.083  1.00 17.85           O  
ANISOU 2846  O   LYS A 400     1831   2521   2430   -263   -116    132       O  
ATOM   2847  CB  LYS A 400     -59.676  -1.875  63.612  1.00 18.15           C  
ANISOU 2847  CB  LYS A 400     1904   2535   2456   -342   -140     87       C  
ATOM   2848  CG  LYS A 400     -60.176  -0.941  62.505  1.00 25.50           C  
ANISOU 2848  CG  LYS A 400     2824   3494   3370   -334   -174     91       C  
ATOM   2849  CD  LYS A 400     -61.046  -1.674  61.492  1.00 28.56           C  
ANISOU 2849  CD  LYS A 400     3205   3893   3752   -368   -207     75       C  
ATOM   2850  CE  LYS A 400     -61.613  -0.730  60.453  1.00 29.03           C  
ANISOU 2850  CE  LYS A 400     3251   3983   3796   -360   -244     82       C  
ATOM   2851  NZ  LYS A 400     -62.407  -1.452  59.427  1.00 32.19           N  
ANISOU 2851  NZ  LYS A 400     3648   4395   4187   -395   -280     66       N  
ATOM   2852  N   SER A 401     -60.648  -0.397  66.194  1.00 15.56           N  
ANISOU 2852  N   SER A 401     1509   2227   2178   -305   -102    127       N  
ATOM   2853  CA  SER A 401     -61.518   0.578  66.859  1.00 15.29           C  
ANISOU 2853  CA  SER A 401     1434   2213   2162   -288    -98    143       C  
ATOM   2854  C   SER A 401     -60.718   1.545  67.755  1.00 17.87           C  
ANISOU 2854  C   SER A 401     1771   2532   2486   -253    -73    156       C  
ATOM   2855  O   SER A 401     -61.008   2.742  67.772  1.00 17.98           O  
ANISOU 2855  O   SER A 401     1767   2562   2503   -228    -78    167       O  
ATOM   2856  CB  SER A 401     -62.594  -0.131  67.671  1.00 19.73           C  
ANISOU 2856  CB  SER A 401     1962   2780   2753   -312    -88    145       C  
ATOM   2857  OG  SER A 401     -63.443   0.799  68.312  1.00 30.77           O  
ANISOU 2857  OG  SER A 401     3320   4200   4172   -295    -84    159       O  
ATOM   2858  N   GLU A 402     -59.694   1.027  68.483  1.00 12.34           N  
ANISOU 2858  N   GLU A 402     1101   1806   1781   -252    -47    154       N  
ATOM   2859  CA  GLU A 402     -58.837   1.876  69.320  1.00 10.65           C  
ANISOU 2859  CA  GLU A 402      900   1584   1562   -222    -24    165       C  
ATOM   2860  C   GLU A 402     -57.967   2.791  68.458  1.00 14.31           C  
ANISOU 2860  C   GLU A 402     1386   2049   2004   -199    -37    165       C  
ATOM   2861  O   GLU A 402     -57.810   3.972  68.778  1.00 13.49           O  
ANISOU 2861  O   GLU A 402     1276   1950   1899   -172    -32    176       O  
ATOM   2862  CB  GLU A 402     -57.958   1.019  70.256  1.00 11.34           C  
ANISOU 2862  CB  GLU A 402     1014   1645   1650   -229      2    164       C  
ATOM   2863  CG  GLU A 402     -58.721   0.399  71.417  1.00 16.60           C  
ANISOU 2863  CG  GLU A 402     1661   2310   2336   -245     22    169       C  
ATOM   2864  CD  GLU A 402     -59.295   1.392  72.412  1.00 33.89           C  
ANISOU 2864  CD  GLU A 402     3825   4515   4538   -226     38    182       C  
ATOM   2865  OE1 GLU A 402     -58.821   2.551  72.440  1.00 26.27           O  
ANISOU 2865  OE1 GLU A 402     2864   3554   3564   -198     38    187       O  
ATOM   2866  OE2 GLU A 402     -60.173   0.991  73.208  1.00 30.99           O  
ANISOU 2866  OE2 GLU A 402     3434   4153   4188   -241     52    186       O  
ATOM   2867  N   TYR A 403     -57.415   2.246  67.338  1.00 10.76           N  
ANISOU 2867  N   TYR A 403      961   1591   1535   -210    -52    153       N  
ATOM   2868  CA  TYR A 403     -56.594   3.014  66.391  1.00 10.56           C  
ANISOU 2868  CA  TYR A 403      958   1567   1487   -192    -64    153       C  
ATOM   2869  C   TYR A 403     -57.381   4.216  65.811  1.00 15.71           C  
ANISOU 2869  C   TYR A 403     1586   2244   2138   -177    -87    164       C  
ATOM   2870  O   TYR A 403     -56.886   5.348  65.833  1.00 14.26           O  
ANISOU 2870  O   TYR A 403     1408   2062   1948   -151    -84    174       O  
ATOM   2871  CB  TYR A 403     -56.087   2.094  65.251  1.00 11.35           C  
ANISOU 2871  CB  TYR A 403     1088   1658   1568   -212    -76    136       C  
ATOM   2872  CG  TYR A 403     -55.502   2.845  64.070  1.00 11.57           C  
ANISOU 2872  CG  TYR A 403     1135   1692   1570   -198    -91    136       C  
ATOM   2873  CD1 TYR A 403     -54.161   3.221  64.053  1.00 12.36           C  
ANISOU 2873  CD1 TYR A 403     1263   1777   1656   -180    -75    138       C  
ATOM   2874  CD2 TYR A 403     -56.269   3.110  62.935  1.00 12.50           C  
ANISOU 2874  CD2 TYR A 403     1244   1831   1675   -206   -122    134       C  
ATOM   2875  CE1 TYR A 403     -53.607   3.879  62.953  1.00 11.73           C  
ANISOU 2875  CE1 TYR A 403     1202   1702   1551   -170    -86    138       C  
ATOM   2876  CE2 TYR A 403     -55.730   3.783  61.837  1.00 12.83           C  
ANISOU 2876  CE2 TYR A 403     1306   1878   1689   -195   -136    136       C  
ATOM   2877  CZ  TYR A 403     -54.397   4.163  61.848  1.00 15.73           C  
ANISOU 2877  CZ  TYR A 403     1702   2229   2043   -178   -116    137       C  
ATOM   2878  OH  TYR A 403     -53.856   4.805  60.763  1.00 13.56           O  
ANISOU 2878  OH  TYR A 403     1449   1960   1741   -169   -127    139       O  
ATOM   2879  N   GLU A 404     -58.600   3.957  65.286  1.00 13.53           N  
ANISOU 2879  N   GLU A 404     1283   1987   1870   -194   -110    162       N  
ATOM   2880  CA  GLU A 404     -59.437   4.998  64.679  1.00 13.68           C  
ANISOU 2880  CA  GLU A 404     1277   2031   1891   -181   -136    173       C  
ATOM   2881  C   GLU A 404     -59.907   6.023  65.715  1.00 17.94           C  
ANISOU 2881  C   GLU A 404     1787   2577   2453   -155   -121    188       C  
ATOM   2882  O   GLU A 404     -59.952   7.219  65.416  1.00 17.11           O  
ANISOU 2882  O   GLU A 404     1677   2481   2345   -130   -131    200       O  
ATOM   2883  CB  GLU A 404     -60.640   4.375  63.956  1.00 15.45           C  
ANISOU 2883  CB  GLU A 404     1475   2273   2121   -207   -166    166       C  
ATOM   2884  CG  GLU A 404     -60.254   3.505  62.771  1.00 23.04           C  
ANISOU 2884  CG  GLU A 404     2467   3230   3056   -231   -185    149       C  
ATOM   2885  CD  GLU A 404     -61.429   2.946  61.993  1.00 39.03           C  
ANISOU 2885  CD  GLU A 404     4469   5274   5085   -259   -219    142       C  
ATOM   2886  OE1 GLU A 404     -62.505   2.738  62.603  1.00 26.51           O  
ANISOU 2886  OE1 GLU A 404     2844   3700   3528   -269   -219    146       O  
ATOM   2887  OE2 GLU A 404     -61.260   2.667  60.785  1.00 35.28           O  
ANISOU 2887  OE2 GLU A 404     4018   4804   4584   -273   -243    132       O  
ATOM   2888  N   ALA A 405     -60.255   5.556  66.946  1.00 14.23           N  
ANISOU 2888  N   ALA A 405     1300   2101   2004   -162    -96    188       N  
ATOM   2889  CA  ALA A 405     -60.684   6.457  68.030  1.00 13.78           C  
ANISOU 2889  CA  ALA A 405     1219   2050   1968   -139    -77    200       C  
ATOM   2890  C   ALA A 405     -59.541   7.411  68.441  1.00 18.09           C  
ANISOU 2890  C   ALA A 405     1791   2580   2500   -111    -60    206       C  
ATOM   2891  O   ALA A 405     -59.792   8.567  68.784  1.00 17.03           O  
ANISOU 2891  O   ALA A 405     1643   2452   2375    -85    -56    217       O  
ATOM   2892  CB  ALA A 405     -61.152   5.650  69.231  1.00 14.26           C  
ANISOU 2892  CB  ALA A 405     1264   2106   2048   -156    -51    198       C  
ATOM   2893  N   GLY A 406     -58.299   6.927  68.342  1.00 15.23           N  
ANISOU 2893  N   GLY A 406     1468   2199   2119   -115    -51    199       N  
ATOM   2894  CA  GLY A 406     -57.118   7.735  68.618  1.00 14.59           C  
ANISOU 2894  CA  GLY A 406     1414   2104   2026    -92    -38    204       C  
ATOM   2895  C   GLY A 406     -56.873   8.795  67.563  1.00 17.10           C  
ANISOU 2895  C   GLY A 406     1739   2428   2329    -74    -58    211       C  
ATOM   2896  O   GLY A 406     -56.590   9.951  67.893  1.00 16.05           O  
ANISOU 2896  O   GLY A 406     1608   2292   2198    -49    -51    221       O  
ATOM   2897  N   VAL A 407     -56.990   8.410  66.271  1.00 13.84           N  
ANISOU 2897  N   VAL A 407     1333   2023   1902    -88    -84    206       N  
ATOM   2898  CA  VAL A 407     -56.804   9.347  65.145  1.00 13.74           C  
ANISOU 2898  CA  VAL A 407     1331   2018   1872    -73   -106    214       C  
ATOM   2899  C   VAL A 407     -57.916  10.427  65.144  1.00 17.66           C  
ANISOU 2899  C   VAL A 407     1794   2532   2385    -54   -121    228       C  
ATOM   2900  O   VAL A 407     -57.630  11.607  64.930  1.00 17.23           O  
ANISOU 2900  O   VAL A 407     1745   2476   2326    -30   -124    240       O  
ATOM   2901  CB  VAL A 407     -56.730   8.592  63.773  1.00 17.25           C  
ANISOU 2901  CB  VAL A 407     1793   2469   2294    -95   -130    204       C  
ATOM   2902  CG1 VAL A 407     -56.561   9.573  62.611  1.00 17.06           C  
ANISOU 2902  CG1 VAL A 407     1781   2453   2248    -81   -152    214       C  
ATOM   2903  CG2 VAL A 407     -55.609   7.567  63.775  1.00 16.50           C  
ANISOU 2903  CG2 VAL A 407     1732   2354   2185   -110   -112    189       C  
ATOM   2904  N   ARG A 408     -59.174  10.018  65.437  1.00 14.25           N  
ANISOU 2904  N   ARG A 408     1324   2115   1974    -65   -128    227       N  
ATOM   2905  CA  ARG A 408     -60.315  10.942  65.473  1.00 14.09           C  
ANISOU 2905  CA  ARG A 408     1267   2113   1976    -47   -141    241       C  
ATOM   2906  C   ARG A 408     -60.189  11.959  66.609  1.00 17.49           C  
ANISOU 2906  C   ARG A 408     1689   2533   2422    -18   -115    249       C  
ATOM   2907  O   ARG A 408     -60.556  13.117  66.435  1.00 16.87           O  
ANISOU 2907  O   ARG A 408     1598   2460   2351      7   -124    262       O  
ATOM   2908  CB  ARG A 408     -61.643  10.168  65.577  1.00 14.21           C  
ANISOU 2908  CB  ARG A 408     1242   2146   2012    -67   -152    236       C  
ATOM   2909  CG  ARG A 408     -62.006   9.418  64.301  1.00 23.34           C  
ANISOU 2909  CG  ARG A 408     2399   3315   3153    -93   -187    230       C  
ATOM   2910  CD  ARG A 408     -63.329   8.695  64.430  1.00 34.06           C  
ANISOU 2910  CD  ARG A 408     3715   4691   4535   -115   -199    226       C  
ATOM   2911  NE  ARG A 408     -63.695   8.010  63.188  1.00 42.70           N  
ANISOU 2911  NE  ARG A 408     4812   5798   5614   -141   -235    219       N  
ATOM   2912  CZ  ARG A 408     -64.401   8.576  62.216  1.00 60.55           C  
ANISOU 2912  CZ  ARG A 408     7054   8079   7872   -136   -273    228       C  
ATOM   2913  NH1 ARG A 408     -64.831   9.825  62.340  1.00 50.44           N  
ANISOU 2913  NH1 ARG A 408     5751   6808   6607   -103   -279    247       N  
ATOM   2914  NH2 ARG A 408     -64.682   7.897  61.111  1.00 48.70           N  
ANISOU 2914  NH2 ARG A 408     5561   6590   6353   -162   -307    220       N  
ATOM   2915  N   ALA A 409     -59.651  11.531  67.767  1.00 14.27           N  
ANISOU 2915  N   ALA A 409     1292   2110   2018    -23    -82    241       N  
ATOM   2916  CA  ALA A 409     -59.421  12.438  68.899  1.00 14.26           C  
ANISOU 2916  CA  ALA A 409     1291   2099   2028      2    -55    246       C  
ATOM   2917  C   ALA A 409     -58.291  13.438  68.583  1.00 18.12           C  
ANISOU 2917  C   ALA A 409     1812   2572   2499     22    -55    252       C  
ATOM   2918  O   ALA A 409     -58.311  14.565  69.079  1.00 17.93           O  
ANISOU 2918  O   ALA A 409     1785   2543   2485     47    -45    260       O  
ATOM   2919  CB  ALA A 409     -59.082  11.643  70.146  1.00 14.90           C  
ANISOU 2919  CB  ALA A 409     1379   2169   2113    -11    -24    238       C  
ATOM   2920  N   SER A 410     -57.311  13.025  67.734  1.00 14.60           N  
ANISOU 2920  N   SER A 410     1398   2119   2028     11    -65    249       N  
ATOM   2921  CA  SER A 410     -56.190  13.893  67.345  1.00 14.10           C  
ANISOU 2921  CA  SER A 410     1366   2043   1948     26    -65    255       C  
ATOM   2922  C   SER A 410     -56.633  14.940  66.336  1.00 17.42           C  
ANISOU 2922  C   SER A 410     1780   2472   2366     43    -90    269       C  
ATOM   2923  O   SER A 410     -56.250  16.101  66.452  1.00 16.76           O  
ANISOU 2923  O   SER A 410     1706   2379   2284     66    -86    278       O  
ATOM   2924  CB  SER A 410     -55.042  13.067  66.780  1.00 17.47           C  
ANISOU 2924  CB  SER A 410     1826   2459   2351      8    -64    246       C  
ATOM   2925  OG  SER A 410     -53.910  13.880  66.514  1.00 27.10           O  
ANISOU 2925  OG  SER A 410     3074   3666   3557     22    -59    252       O  
ATOM   2926  N   PHE A 411     -57.479  14.542  65.361  1.00 14.08           N  
ANISOU 2926  N   PHE A 411     1342   2069   1941     32   -119    270       N  
ATOM   2927  CA  PHE A 411     -58.045  15.487  64.389  1.00 14.06           C  
ANISOU 2927  CA  PHE A 411     1329   2076   1935     48   -147    286       C  
ATOM   2928  C   PHE A 411     -58.986  16.480  65.081  1.00 18.53           C  
ANISOU 2928  C   PHE A 411     1862   2646   2532     74   -144    297       C  
ATOM   2929  O   PHE A 411     -59.046  17.644  64.689  1.00 18.88           O  
ANISOU 2929  O   PHE A 411     1908   2688   2578     98   -155    312       O  
ATOM   2930  CB  PHE A 411     -58.772  14.738  63.257  1.00 15.65           C  
ANISOU 2930  CB  PHE A 411     1520   2299   2127     27   -180    284       C  
ATOM   2931  CG  PHE A 411     -57.860  14.291  62.136  1.00 16.42           C  
ANISOU 2931  CG  PHE A 411     1657   2394   2189     11   -192    279       C  
ATOM   2932  CD1 PHE A 411     -56.851  13.364  62.365  1.00 18.63           C  
ANISOU 2932  CD1 PHE A 411     1964   2660   2456     -7   -170    263       C  
ATOM   2933  CD2 PHE A 411     -58.058  14.739  60.837  1.00 17.79           C  
ANISOU 2933  CD2 PHE A 411     1838   2579   2342     13   -224    290       C  
ATOM   2934  CE1 PHE A 411     -56.011  12.953  61.330  1.00 18.83           C  
ANISOU 2934  CE1 PHE A 411     2023   2682   2449    -20   -177    257       C  
ATOM   2935  CE2 PHE A 411     -57.223  14.319  59.801  1.00 20.16           C  
ANISOU 2935  CE2 PHE A 411     2176   2877   2607     -2   -231    285       C  
ATOM   2936  CZ  PHE A 411     -56.201  13.436  60.056  1.00 17.60           C  
ANISOU 2936  CZ  PHE A 411     1877   2538   2271    -18   -206    267       C  
ATOM   2937  N   ALA A 412     -59.655  16.040  66.166  1.00 14.89           N  
ANISOU 2937  N   ALA A 412     1373   2189   2095     71   -125    289       N  
ATOM   2938  CA  ALA A 412     -60.490  16.927  66.977  1.00 14.74           C  
ANISOU 2938  CA  ALA A 412     1324   2172   2106     96   -113    296       C  
ATOM   2939  C   ALA A 412     -59.613  17.918  67.730  1.00 18.36           C  
ANISOU 2939  C   ALA A 412     1806   2607   2564    118    -88    298       C  
ATOM   2940  O   ALA A 412     -59.914  19.113  67.755  1.00 17.82           O  
ANISOU 2940  O   ALA A 412     1730   2534   2508    146    -90    309       O  
ATOM   2941  CB  ALA A 412     -61.321  16.113  67.955  1.00 15.29           C  
ANISOU 2941  CB  ALA A 412     1361   2250   2197     83    -95    286       C  
ATOM   2942  N   THR A 413     -58.461  17.436  68.256  1.00 14.19           N  
ANISOU 2942  N   THR A 413     1310   2063   2018    106    -67    287       N  
ATOM   2943  CA  THR A 413     -57.482  18.274  68.952  1.00 13.63           C  
ANISOU 2943  CA  THR A 413     1265   1970   1943    121    -45    287       C  
ATOM   2944  C   THR A 413     -56.926  19.374  68.015  1.00 18.81           C  
ANISOU 2944  C   THR A 413     1942   2617   2588    138    -62    301       C  
ATOM   2945  O   THR A 413     -56.737  20.515  68.447  1.00 17.56           O  
ANISOU 2945  O   THR A 413     1790   2444   2439    161    -51    306       O  
ATOM   2946  CB  THR A 413     -56.355  17.386  69.536  1.00 16.79           C  
ANISOU 2946  CB  THR A 413     1693   2358   2327    101    -25    274       C  
ATOM   2947  OG1 THR A 413     -56.899  16.564  70.577  1.00 11.30           O  
ANISOU 2947  OG1 THR A 413      980   1669   1645     89     -6    265       O  
ATOM   2948  CG2 THR A 413     -55.179  18.201  70.071  1.00 14.56           C  
ANISOU 2948  CG2 THR A 413     1441   2054   2038    113     -8    275       C  
ATOM   2949  N   TRP A 414     -56.704  19.032  66.728  1.00 17.31           N  
ANISOU 2949  N   TRP A 414     1764   2435   2378    126    -87    306       N  
ATOM   2950  CA  TRP A 414     -56.122  19.964  65.763  1.00 17.88           C  
ANISOU 2950  CA  TRP A 414     1859   2499   2435    138   -102    320       C  
ATOM   2951  C   TRP A 414     -57.175  20.673  64.890  1.00 21.68           C  
ANISOU 2951  C   TRP A 414     2320   2994   2925    155   -132    337       C  
ATOM   2952  O   TRP A 414     -56.817  21.400  63.963  1.00 21.14           O  
ANISOU 2952  O   TRP A 414     2270   2920   2842    163   -149    352       O  
ATOM   2953  CB  TRP A 414     -55.071  19.260  64.898  1.00 16.85           C  
ANISOU 2953  CB  TRP A 414     1761   2367   2273    116   -108    316       C  
ATOM   2954  CG  TRP A 414     -53.814  18.945  65.641  1.00 17.78           C  
ANISOU 2954  CG  TRP A 414     1904   2468   2385    108    -80    304       C  
ATOM   2955  CD1 TRP A 414     -53.460  17.742  66.178  1.00 20.53           C  
ANISOU 2955  CD1 TRP A 414     2254   2815   2729     87    -66    289       C  
ATOM   2956  CD2 TRP A 414     -52.822  19.886  66.075  1.00 17.61           C  
ANISOU 2956  CD2 TRP A 414     1905   2425   2362    121    -64    308       C  
ATOM   2957  NE1 TRP A 414     -52.268  17.860  66.858  1.00 20.02           N  
ANISOU 2957  NE1 TRP A 414     2213   2733   2662     87    -44    284       N  
ATOM   2958  CE2 TRP A 414     -51.862  19.170  66.823  1.00 21.57           C  
ANISOU 2958  CE2 TRP A 414     2420   2916   2859    107    -42    295       C  
ATOM   2959  CE3 TRP A 414     -52.642  21.271  65.889  1.00 18.94           C  
ANISOU 2959  CE3 TRP A 414     2081   2580   2534    142    -67    322       C  
ATOM   2960  CZ2 TRP A 414     -50.732  19.789  67.381  1.00 20.81           C  
ANISOU 2960  CZ2 TRP A 414     2346   2801   2762    112    -25    294       C  
ATOM   2961  CZ3 TRP A 414     -51.522  21.879  66.438  1.00 20.45           C  
ANISOU 2961  CZ3 TRP A 414     2296   2751   2724    146    -48    321       C  
ATOM   2962  CH2 TRP A 414     -50.587  21.144  67.180  1.00 20.86           C  
ANISOU 2962  CH2 TRP A 414     2360   2794   2770    131    -28    307       C  
ATOM   2963  N   GLY A 415     -58.453  20.508  65.243  1.00 18.54           N  
ANISOU 2963  N   GLY A 415     1882   2610   2551    160   -138    337       N  
ATOM   2964  CA  GLY A 415     -59.560  21.178  64.557  1.00 18.40           C  
ANISOU 2964  CA  GLY A 415     1837   2606   2548    178   -167    354       C  
ATOM   2965  C   GLY A 415     -59.715  20.790  63.095  1.00 20.97           C  
ANISOU 2965  C   GLY A 415     2169   2948   2850    163   -204    363       C  
ATOM   2966  O   GLY A 415     -60.067  21.631  62.262  1.00 20.82           O  
ANISOU 2966  O   GLY A 415     2148   2933   2830    180   -231    383       O  
ATOM   2967  N   VAL A 416     -59.470  19.508  62.773  1.00 16.14           N  
ANISOU 2967  N   VAL A 416     1566   2347   2219    132   -208    349       N  
ATOM   2968  CA  VAL A 416     -59.625  19.001  61.401  1.00 16.16           C  
ANISOU 2968  CA  VAL A 416     1577   2367   2196    114   -243    353       C  
ATOM   2969  C   VAL A 416     -60.529  17.751  61.359  1.00 19.76           C  
ANISOU 2969  C   VAL A 416     2004   2845   2659     88   -256    340       C  
ATOM   2970  O   VAL A 416     -60.323  16.862  60.529  1.00 19.27           O  
ANISOU 2970  O   VAL A 416     1959   2792   2572     62   -272    331       O  
ATOM   2971  CB  VAL A 416     -58.253  18.760  60.699  1.00 19.79           C  
ANISOU 2971  CB  VAL A 416     2086   2816   2617     99   -238    348       C  
ATOM   2972  CG1 VAL A 416     -57.679  20.062  60.167  1.00 19.53           C  
ANISOU 2972  CG1 VAL A 416     2078   2770   2574    121   -243    369       C  
ATOM   2973  CG2 VAL A 416     -57.262  18.065  61.639  1.00 19.18           C  
ANISOU 2973  CG2 VAL A 416     2027   2723   2539     86   -201    329       C  
ATOM   2974  N   THR A 417     -61.583  17.733  62.210  1.00 16.32           N  
ANISOU 2974  N   THR A 417     1525   2417   2259     96   -249    338       N  
ATOM   2975  CA  THR A 417     -62.538  16.614  62.293  1.00 16.17           C  
ANISOU 2975  CA  THR A 417     1472   2418   2252     72   -259    327       C  
ATOM   2976  C   THR A 417     -63.252  16.360  60.944  1.00 20.35           C  
ANISOU 2976  C   THR A 417     1992   2971   2769     59   -307    335       C  
ATOM   2977  O   THR A 417     -63.499  15.206  60.587  1.00 19.04           O  
ANISOU 2977  O   THR A 417     1822   2817   2593     28   -319    321       O  
ATOM   2978  CB  THR A 417     -63.538  16.865  63.439  1.00 20.68           C  
ANISOU 2978  CB  THR A 417     1998   2994   2866     87   -241    328       C  
ATOM   2979  OG1 THR A 417     -62.822  16.900  64.672  1.00 16.99           O  
ANISOU 2979  OG1 THR A 417     1546   2506   2404     92   -198    318       O  
ATOM   2980  CG2 THR A 417     -64.639  15.802  63.504  1.00 18.06           C  
ANISOU 2980  CG2 THR A 417     1626   2684   2552     62   -252    319       C  
ATOM   2981  N   SER A 418     -63.558  17.438  60.192  1.00 17.68           N  
ANISOU 2981  N   SER A 418     1650   2637   2429     82   -334    357       N  
ATOM   2982  CA  SER A 418     -64.254  17.321  58.904  1.00 18.00           C  
ANISOU 2982  CA  SER A 418     1682   2701   2455     73   -383    367       C  
ATOM   2983  C   SER A 418     -63.412  16.545  57.856  1.00 21.99           C  
ANISOU 2983  C   SER A 418     2234   3208   2913     43   -396    357       C  
ATOM   2984  O   SER A 418     -63.934  16.164  56.808  1.00 21.64           O  
ANISOU 2984  O   SER A 418     2187   3184   2852     26   -436    359       O  
ATOM   2985  CB  SER A 418     -64.621  18.702  58.367  1.00 21.15           C  
ANISOU 2985  CB  SER A 418     2074   3102   2861    107   -408    395       C  
ATOM   2986  OG  SER A 418     -63.466  19.497  58.154  1.00 26.30           O  
ANISOU 2986  OG  SER A 418     2771   3732   3489    121   -394    404       O  
ATOM   2987  N   GLU A 419     -62.122  16.285  58.166  1.00 18.36           N  
ANISOU 2987  N   GLU A 419     1816   2727   2434     36   -363    344       N  
ATOM   2988  CA  GLU A 419     -61.221  15.610  57.230  1.00 17.83           C  
ANISOU 2988  CA  GLU A 419     1794   2658   2324     12   -368    333       C  
ATOM   2989  C   GLU A 419     -60.896  14.161  57.664  1.00 21.84           C  
ANISOU 2989  C   GLU A 419     2309   3162   2829    -20   -347    305       C  
ATOM   2990  O   GLU A 419     -60.359  13.392  56.864  1.00 21.31           O  
ANISOU 2990  O   GLU A 419     2273   3096   2729    -44   -354    292       O  
ATOM   2991  CB  GLU A 419     -59.917  16.419  57.055  1.00 18.64           C  
ANISOU 2991  CB  GLU A 419     1940   2740   2404     28   -348    341       C  
ATOM   2992  CG  GLU A 419     -60.136  17.873  56.644  1.00 30.45           C  
ANISOU 2992  CG  GLU A 419     3433   4234   3902     59   -366    370       C  
ATOM   2993  CD  GLU A 419     -60.722  18.078  55.256  1.00 55.07           C  
ANISOU 2993  CD  GLU A 419     6555   7373   6996     55   -414    386       C  
ATOM   2994  OE1 GLU A 419     -60.520  17.198  54.387  1.00 49.38           O  
ANISOU 2994  OE1 GLU A 419     5857   6663   6241     26   -429    374       O  
ATOM   2995  OE2 GLU A 419     -61.304  19.159  55.015  1.00 51.02           O  
ANISOU 2995  OE2 GLU A 419     6026   6863   6495     81   -436    411       O  
ATOM   2996  N   VAL A 420     -61.191  13.802  58.940  1.00 18.03           N  
ANISOU 2996  N   VAL A 420     1798   2672   2378    -19   -320    296       N  
ATOM   2997  CA  VAL A 420     -60.788  12.497  59.490  1.00 17.59           C  
ANISOU 2997  CA  VAL A 420     1753   2609   2323    -46   -296    273       C  
ATOM   2998  C   VAL A 420     -61.451  11.270  58.768  1.00 22.76           C  
ANISOU 2998  C   VAL A 420     2401   3280   2969    -82   -322    258       C  
ATOM   2999  O   VAL A 420     -60.800  10.239  58.601  1.00 22.55           O  
ANISOU 2999  O   VAL A 420     2402   3244   2924   -106   -311    239       O  
ATOM   3000  CB  VAL A 420     -60.931  12.431  61.045  1.00 20.54           C  
ANISOU 3000  CB  VAL A 420     2102   2971   2731    -38   -260    269       C  
ATOM   3001  CG1 VAL A 420     -62.388  12.212  61.461  1.00 20.55           C  
ANISOU 3001  CG1 VAL A 420     2050   2991   2765    -42   -271    271       C  
ATOM   3002  CG2 VAL A 420     -60.028  11.349  61.631  1.00 19.79           C  
ANISOU 3002  CG2 VAL A 420     2032   2858   2629    -58   -229    249       C  
ATOM   3003  N   ASP A 421     -62.717  11.413  58.313  1.00 20.69           N  
ANISOU 3003  N   ASP A 421     2101   3041   2718    -84   -358    267       N  
ATOM   3004  CA  ASP A 421     -63.424  10.316  57.626  1.00 21.22           C  
ANISOU 3004  CA  ASP A 421     2158   3125   2778   -119   -387    253       C  
ATOM   3005  C   ASP A 421     -62.717   9.906  56.330  1.00 25.68           C  
ANISOU 3005  C   ASP A 421     2771   3690   3296   -138   -406    244       C  
ATOM   3006  O   ASP A 421     -62.459   8.718  56.120  1.00 25.63           O  
ANISOU 3006  O   ASP A 421     2783   3678   3276   -168   -402    221       O  
ATOM   3007  CB  ASP A 421     -64.895  10.693  57.347  1.00 23.51           C  
ANISOU 3007  CB  ASP A 421     2398   3443   3093   -116   -426    267       C  
ATOM   3008  CG  ASP A 421     -65.790  10.660  58.580  1.00 33.16           C  
ANISOU 3008  CG  ASP A 421     3569   4669   4363   -109   -407    269       C  
ATOM   3009  OD1 ASP A 421     -65.312  10.219  59.651  1.00 32.24           O  
ANISOU 3009  OD1 ASP A 421     3457   4534   4259   -113   -366    258       O  
ATOM   3010  OD2 ASP A 421     -66.983  11.012  58.456  1.00 40.50           O  
ANISOU 3010  OD2 ASP A 421     4451   5619   5317   -103   -434    282       O  
ATOM   3011  N   ASP A 422     -62.383  10.893  55.465  1.00 21.67           N  
ANISOU 3011  N   ASP A 422     2285   3186   2763   -119   -425    261       N  
ATOM   3012  CA  ASP A 422     -61.673  10.626  54.208  1.00 21.43           C  
ANISOU 3012  CA  ASP A 422     2302   3157   2684   -134   -440    254       C  
ATOM   3013  C   ASP A 422     -60.230  10.185  54.474  1.00 23.06           C  
ANISOU 3013  C   ASP A 422     2552   3337   2873   -138   -397    238       C  
ATOM   3014  O   ASP A 422     -59.685   9.376  53.726  1.00 23.28           O  
ANISOU 3014  O   ASP A 422     2615   3361   2868   -161   -399    220       O  
ATOM   3015  CB  ASP A 422     -61.695  11.869  53.295  1.00 23.97           C  
ANISOU 3015  CB  ASP A 422     2635   3488   2984   -112   -468    280       C  
ATOM   3016  CG  ASP A 422     -63.088  12.261  52.814  1.00 34.13           C  
ANISOU 3016  CG  ASP A 422     3882   4803   4284   -109   -517    297       C  
ATOM   3017  OD1 ASP A 422     -63.933  11.353  52.635  1.00 34.34           O  
ANISOU 3017  OD1 ASP A 422     3886   4846   4316   -137   -540    284       O  
ATOM   3018  OD2 ASP A 422     -63.295  13.454  52.516  1.00 40.79           O  
ANISOU 3018  OD2 ASP A 422     4719   5652   5129    -81   -534    324       O  
ATOM   3019  N   TYR A 423     -59.617  10.715  55.552  1.00 17.94           N  
ANISOU 3019  N   TYR A 423     1901   2670   2246   -115   -360    244       N  
ATOM   3020  CA  TYR A 423     -58.251  10.360  55.951  1.00 16.81           C  
ANISOU 3020  CA  TYR A 423     1793   2502   2093   -115   -320    231       C  
ATOM   3021  C   TYR A 423     -58.155   8.860  56.292  1.00 19.46           C  
ANISOU 3021  C   TYR A 423     2133   2829   2433   -145   -305    204       C  
ATOM   3022  O   TYR A 423     -57.318   8.156  55.727  1.00 17.76           O  
ANISOU 3022  O   TYR A 423     1954   2603   2191   -161   -296    188       O  
ATOM   3023  CB  TYR A 423     -57.807  11.223  57.162  1.00 17.34           C  
ANISOU 3023  CB  TYR A 423     1849   2552   2187    -86   -288    244       C  
ATOM   3024  CG  TYR A 423     -56.366  11.011  57.584  1.00 18.54           C  
ANISOU 3024  CG  TYR A 423     2034   2680   2330    -84   -250    234       C  
ATOM   3025  CD1 TYR A 423     -55.347  11.812  57.077  1.00 20.65           C  
ANISOU 3025  CD1 TYR A 423     2332   2938   2574    -69   -242    244       C  
ATOM   3026  CD2 TYR A 423     -56.042  10.116  58.599  1.00 18.89           C  
ANISOU 3026  CD2 TYR A 423     2075   2710   2393    -94   -221    218       C  
ATOM   3027  CE1 TYR A 423     -54.027  11.659  57.499  1.00 21.73           C  
ANISOU 3027  CE1 TYR A 423     2495   3054   2707    -67   -207    236       C  
ATOM   3028  CE2 TYR A 423     -54.728   9.966  59.041  1.00 19.30           C  
ANISOU 3028  CE2 TYR A 423     2154   2740   2440    -89   -189    212       C  
ATOM   3029  CZ  TYR A 423     -53.721  10.730  58.479  1.00 26.48           C  
ANISOU 3029  CZ  TYR A 423     3092   3642   3327    -76   -182    220       C  
ATOM   3030  OH  TYR A 423     -52.423  10.578  58.902  1.00 26.70           O  
ANISOU 3030  OH  TYR A 423     3143   3649   3353    -73   -150    214       O  
ATOM   3031  N   LEU A 424     -59.067   8.366  57.171  1.00 16.75           N  
ANISOU 3031  N   LEU A 424     1751   2490   2124   -153   -304    201       N  
ATOM   3032  CA  LEU A 424     -59.063   6.964  57.644  1.00 16.89           C  
ANISOU 3032  CA  LEU A 424     1769   2497   2152   -181   -289    178       C  
ATOM   3033  C   LEU A 424     -59.398   5.940  56.536  1.00 20.32           C  
ANISOU 3033  C   LEU A 424     2219   2940   2562   -214   -316    159       C  
ATOM   3034  O   LEU A 424     -59.064   4.764  56.673  1.00 19.42           O  
ANISOU 3034  O   LEU A 424     2121   2811   2447   -237   -301    138       O  
ATOM   3035  CB  LEU A 424     -60.034   6.791  58.839  1.00 17.44           C  
ANISOU 3035  CB  LEU A 424     1792   2570   2263   -181   -280    182       C  
ATOM   3036  CG  LEU A 424     -59.577   7.403  60.175  1.00 22.14           C  
ANISOU 3036  CG  LEU A 424     2379   3151   2882   -155   -244    192       C  
ATOM   3037  CD1 LEU A 424     -60.670   7.301  61.218  1.00 22.05           C  
ANISOU 3037  CD1 LEU A 424     2322   3148   2909   -156   -238    196       C  
ATOM   3038  CD2 LEU A 424     -58.295   6.727  60.684  1.00 25.83           C  
ANISOU 3038  CD2 LEU A 424     2880   3591   3341   -160   -209    179       C  
ATOM   3039  N   THR A 425     -60.104   6.371  55.478  1.00 16.80           N  
ANISOU 3039  N   THR A 425     1767   2518   2098   -218   -356    167       N  
ATOM   3040  CA  THR A 425     -60.505   5.451  54.399  1.00 16.85           C  
ANISOU 3040  CA  THR A 425     1788   2535   2080   -252   -386    149       C  
ATOM   3041  C   THR A 425     -59.509   5.478  53.215  1.00 21.03           C  
ANISOU 3041  C   THR A 425     2371   3060   2560   -255   -389    141       C  
ATOM   3042  O   THR A 425     -59.692   4.743  52.239  1.00 21.28           O  
ANISOU 3042  O   THR A 425     2423   3099   2564   -283   -411    123       O  
ATOM   3043  CB  THR A 425     -61.947   5.752  53.940  1.00 24.87           C  
ANISOU 3043  CB  THR A 425     2764   3581   3105   -259   -434    160       C  
ATOM   3044  OG1 THR A 425     -62.021   7.104  53.496  1.00 28.72           O  
ANISOU 3044  OG1 THR A 425     3249   4082   3583   -230   -452    186       O  
ATOM   3045  CG2 THR A 425     -62.972   5.508  55.039  1.00 22.50           C  
ANISOU 3045  CG2 THR A 425     2411   3286   2854   -262   -429    164       C  
ATOM   3046  N   SER A 426     -58.450   6.309  53.313  1.00 16.57           N  
ANISOU 3046  N   SER A 426     1829   2483   1985   -228   -364    153       N  
ATOM   3047  CA  SER A 426     -57.488   6.479  52.223  1.00 16.26           C  
ANISOU 3047  CA  SER A 426     1838   2440   1899   -228   -362    149       C  
ATOM   3048  C   SER A 426     -56.360   5.436  52.262  1.00 20.52           C  
ANISOU 3048  C   SER A 426     2414   2955   2427   -242   -326    122       C  
ATOM   3049  O   SER A 426     -55.796   5.168  53.328  1.00 19.55           O  
ANISOU 3049  O   SER A 426     2286   2812   2332   -233   -291    118       O  
ATOM   3050  CB  SER A 426     -56.904   7.884  52.243  1.00 18.51           C  
ANISOU 3050  CB  SER A 426     2130   2724   2180   -195   -353    175       C  
ATOM   3051  OG  SER A 426     -55.917   8.048  51.237  1.00 25.29           O  
ANISOU 3051  OG  SER A 426     3035   3578   2995   -196   -346    172       O  
ATOM   3052  N   THR A 427     -55.968   4.924  51.076  1.00 17.76           N  
ANISOU 3052  N   THR A 427     2105   2607   2036   -261   -334    105       N  
ATOM   3053  CA  THR A 427     -54.873   3.950  50.950  1.00 17.39           C  
ANISOU 3053  CA  THR A 427     2095   2536   1975   -272   -301     79       C  
ATOM   3054  C   THR A 427     -53.562   4.644  50.513  1.00 22.06           C  
ANISOU 3054  C   THR A 427     2721   3119   2540   -253   -275     86       C  
ATOM   3055  O   THR A 427     -52.559   3.968  50.258  1.00 21.51           O  
ANISOU 3055  O   THR A 427     2685   3032   2457   -259   -246     65       O  
ATOM   3056  CB  THR A 427     -55.270   2.821  49.980  1.00 22.46           C  
ANISOU 3056  CB  THR A 427     2760   3183   2590   -308   -322     50       C  
ATOM   3057  OG1 THR A 427     -55.551   3.384  48.703  1.00 21.03           O  
ANISOU 3057  OG1 THR A 427     2599   3026   2366   -313   -355     57       O  
ATOM   3058  CG2 THR A 427     -56.469   2.026  50.471  1.00 20.97           C  
ANISOU 3058  CG2 THR A 427     2537   3000   2431   -331   -343     41       C  
ATOM   3059  N   GLU A 428     -53.575   5.998  50.431  1.00 19.09           N  
ANISOU 3059  N   GLU A 428     2337   2755   2161   -229   -284    115       N  
ATOM   3060  CA  GLU A 428     -52.383   6.770  50.060  1.00 18.41           C  
ANISOU 3060  CA  GLU A 428     2281   2661   2053   -210   -259    125       C  
ATOM   3061  C   GLU A 428     -51.291   6.578  51.092  1.00 21.95           C  
ANISOU 3061  C   GLU A 428     2728   3082   2528   -197   -214    120       C  
ATOM   3062  O   GLU A 428     -51.540   6.732  52.292  1.00 21.78           O  
ANISOU 3062  O   GLU A 428     2675   3055   2547   -185   -206    129       O  
ATOM   3063  CB  GLU A 428     -52.724   8.270  49.905  1.00 19.88           C  
ANISOU 3063  CB  GLU A 428     2456   2863   2237   -188   -279    159       C  
ATOM   3064  CG  GLU A 428     -53.697   8.570  48.763  1.00 29.61           C  
ANISOU 3064  CG  GLU A 428     3691   4121   3437   -199   -327    168       C  
ATOM   3065  CD  GLU A 428     -53.147   8.340  47.365  1.00 44.33           C  
ANISOU 3065  CD  GLU A 428     5605   5992   5246   -215   -331    157       C  
ATOM   3066  OE1 GLU A 428     -51.918   8.486  47.177  1.00 23.60           O  
ANISOU 3066  OE1 GLU A 428     3011   3352   2605   -208   -295    154       O  
ATOM   3067  OE2 GLU A 428     -53.960   8.107  46.441  1.00 44.13           O  
ANISOU 3067  OE2 GLU A 428     5587   5987   5192   -234   -370    154       O  
ATOM   3068  N   LYS A 429     -50.108   6.156  50.648  1.00 17.98           N  
ANISOU 3068  N   LYS A 429     2261   2566   2006   -200   -184    105       N  
ATOM   3069  CA  LYS A 429     -49.000   5.867  51.554  1.00 17.16           C  
ANISOU 3069  CA  LYS A 429     2158   2436   1927   -188   -142     99       C  
ATOM   3070  C   LYS A 429     -48.111   7.074  51.719  1.00 19.79           C  
ANISOU 3070  C   LYS A 429     2494   2765   2261   -163   -123    121       C  
ATOM   3071  O   LYS A 429     -47.834   7.769  50.742  1.00 20.11           O  
ANISOU 3071  O   LYS A 429     2557   2816   2268   -161   -128    131       O  
ATOM   3072  CB  LYS A 429     -48.174   4.676  51.031  1.00 19.76           C  
ANISOU 3072  CB  LYS A 429     2520   2750   2240   -204   -117     69       C  
ATOM   3073  CG  LYS A 429     -48.963   3.375  50.926  1.00 31.08           C  
ANISOU 3073  CG  LYS A 429     3952   4181   3675   -230   -132     43       C  
ATOM   3074  CD  LYS A 429     -48.120   2.265  50.316  1.00 39.45           C  
ANISOU 3074  CD  LYS A 429     5050   5224   4717   -244   -106     12       C  
ATOM   3075  CE  LYS A 429     -48.838   0.940  50.318  1.00 50.81           C  
ANISOU 3075  CE  LYS A 429     6489   6656   6162   -271   -119    -14       C  
ATOM   3076  NZ  LYS A 429     -48.001  -0.139  49.736  1.00 60.28           N  
ANISOU 3076  NZ  LYS A 429     7725   7834   7345   -282    -92    -45       N  
ATOM   3077  N   ASN A 430     -47.593   7.298  52.941  1.00 14.88           N  
ANISOU 3077  N   ASN A 430     1853   2128   1675   -147   -100    129       N  
ATOM   3078  CA  ASN A 430     -46.594   8.337  53.153  1.00 14.31           C  
ANISOU 3078  CA  ASN A 430     1785   2048   1605   -126    -78    147       C  
ATOM   3079  C   ASN A 430     -45.236   7.872  52.581  1.00 18.15           C  
ANISOU 3079  C   ASN A 430     2302   2520   2073   -129    -45    132       C  
ATOM   3080  O   ASN A 430     -45.167   6.805  51.964  1.00 17.38           O  
ANISOU 3080  O   ASN A 430     2224   2420   1958   -147    -41    108       O  
ATOM   3081  CB  ASN A 430     -46.484   8.717  54.663  1.00 14.25           C  
ANISOU 3081  CB  ASN A 430     1747   2027   1639   -109    -66    158       C  
ATOM   3082  CG  ASN A 430     -46.046   7.583  55.575  1.00 29.50           C  
ANISOU 3082  CG  ASN A 430     3672   3940   3597   -113    -43    140       C  
ATOM   3083  OD1 ASN A 430     -45.590   6.524  55.129  1.00 24.17           O  
ANISOU 3083  OD1 ASN A 430     3016   3256   2912   -127    -31    119       O  
ATOM   3084  ND2 ASN A 430     -46.131   7.809  56.879  1.00 15.13           N  
ANISOU 3084  ND2 ASN A 430     1826   2112   1809   -102    -37    150       N  
ATOM   3085  N   GLU A 431     -44.178   8.671  52.750  1.00 14.83           N  
ANISOU 3085  N   GLU A 431     1887   2091   1656   -114    -21    145       N  
ATOM   3086  CA  GLU A 431     -42.880   8.325  52.173  1.00 14.86           C  
ANISOU 3086  CA  GLU A 431     1918   2084   1645   -116     12    133       C  
ATOM   3087  C   GLU A 431     -42.155   7.219  52.959  1.00 18.98           C  
ANISOU 3087  C   GLU A 431     2433   2583   2194   -116     39    113       C  
ATOM   3088  O   GLU A 431     -41.113   6.729  52.516  1.00 18.62           O  
ANISOU 3088  O   GLU A 431     2407   2527   2141   -117     68     99       O  
ATOM   3089  CB  GLU A 431     -42.005   9.571  51.983  1.00 16.06           C  
ANISOU 3089  CB  GLU A 431     2076   2235   1790   -101     27    154       C  
ATOM   3090  CG  GLU A 431     -42.567  10.519  50.927  1.00 26.04           C  
ANISOU 3090  CG  GLU A 431     3356   3518   3019   -103      3    172       C  
ATOM   3091  CD  GLU A 431     -41.682  11.692  50.556  1.00 42.02           C  
ANISOU 3091  CD  GLU A 431     5393   5540   5032    -93     20    193       C  
ATOM   3092  OE1 GLU A 431     -40.827  12.080  51.383  1.00 38.36           O  
ANISOU 3092  OE1 GLU A 431     4917   5062   4598    -81     43    200       O  
ATOM   3093  OE2 GLU A 431     -41.900  12.275  49.468  1.00 30.90           O  
ANISOU 3093  OE2 GLU A 431     4007   4145   3587    -98      7    205       O  
ATOM   3094  N   ALA A 432     -42.786   6.728  54.046  1.00 15.77           N  
ANISOU 3094  N   ALA A 432     2002   2172   1820   -115     29    111       N  
ATOM   3095  CA  ALA A 432     -42.297   5.562  54.785  1.00 15.18           C  
ANISOU 3095  CA  ALA A 432     1922   2076   1771   -118     50     93       C  
ATOM   3096  C   ALA A 432     -43.022   4.286  54.291  1.00 18.24           C  
ANISOU 3096  C   ALA A 432     2320   2463   2147   -139     39     68       C  
ATOM   3097  O   ALA A 432     -42.627   3.168  54.639  1.00 17.42           O  
ANISOU 3097  O   ALA A 432     2220   2340   2059   -144     56     50       O  
ATOM   3098  CB  ALA A 432     -42.532   5.753  56.278  1.00 15.73           C  
ANISOU 3098  CB  ALA A 432     1961   2138   1878   -107     47    106       C  
ATOM   3099  N   GLY A 433     -44.063   4.480  53.466  1.00 14.77           N  
ANISOU 3099  N   GLY A 433     1886   2044   1681   -152      9     69       N  
ATOM   3100  CA  GLY A 433     -44.860   3.385  52.917  1.00 14.26           C  
ANISOU 3100  CA  GLY A 433     1833   1982   1603   -175     -7     46       C  
ATOM   3101  C   GLY A 433     -46.106   3.086  53.732  1.00 16.25           C  
ANISOU 3101  C   GLY A 433     2056   2239   1881   -183    -33     49       C  
ATOM   3102  O   GLY A 433     -46.830   2.128  53.440  1.00 16.26           O  
ANISOU 3102  O   GLY A 433     2061   2241   1877   -205    -47     31       O  
ATOM   3103  N   THR A 434     -46.381   3.915  54.746  1.00 10.34           N  
ANISOU 3103  N   THR A 434     1277   1494   1157   -167    -37     72       N  
ATOM   3104  CA  THR A 434     -47.519   3.695  55.644  1.00  9.79           C  
ANISOU 3104  CA  THR A 434     1176   1428   1114   -172    -56     77       C  
ATOM   3105  C   THR A 434     -48.759   4.448  55.172  1.00 13.15           C  
ANISOU 3105  C   THR A 434     1587   1881   1528   -176    -93     90       C  
ATOM   3106  O   THR A 434     -48.694   5.656  54.934  1.00 11.37           O  
ANISOU 3106  O   THR A 434     1360   1668   1294   -160   -100    111       O  
ATOM   3107  CB  THR A 434     -47.146   4.096  57.082  1.00 13.76           C  
ANISOU 3107  CB  THR A 434     1656   1920   1652   -153    -39     92       C  
ATOM   3108  OG1 THR A 434     -45.822   3.643  57.370  1.00 12.92           O  
ANISOU 3108  OG1 THR A 434     1564   1791   1553   -146     -7     85       O  
ATOM   3109  CG2 THR A 434     -48.129   3.552  58.114  1.00  9.39           C  
ANISOU 3109  CG2 THR A 434     1075   1366   1128   -161    -48     93       C  
ATOM   3110  N   SER A 435     -49.911   3.753  55.119  1.00 11.27           N  
ANISOU 3110  N   SER A 435     1335   1651   1294   -196   -116     81       N  
ATOM   3111  CA  SER A 435     -51.196   4.382  54.808  1.00 11.46           C  
ANISOU 3111  CA  SER A 435     1339   1702   1315   -199   -153     94       C  
ATOM   3112  C   SER A 435     -52.035   4.539  56.090  1.00 14.94           C  
ANISOU 3112  C   SER A 435     1737   2144   1795   -193   -157    106       C  
ATOM   3113  O   SER A 435     -51.765   3.870  57.087  1.00 13.87           O  
ANISOU 3113  O   SER A 435     1594   1991   1684   -194   -135    100       O  
ATOM   3114  CB  SER A 435     -51.961   3.559  53.772  1.00 15.71           C  
ANISOU 3114  CB  SER A 435     1888   2252   1830   -228   -180     75       C  
ATOM   3115  OG  SER A 435     -52.234   2.252  54.247  1.00 23.99           O  
ANISOU 3115  OG  SER A 435     2932   3286   2897   -249   -174     55       O  
ATOM   3116  N   ALA A 436     -53.025   5.441  56.072  1.00 12.21           N  
ANISOU 3116  N   ALA A 436     1366   1819   1454   -185   -183    125       N  
ATOM   3117  CA  ALA A 436     -53.868   5.691  57.243  1.00 12.29           C  
ANISOU 3117  CA  ALA A 436     1336   1834   1501   -177   -185    137       C  
ATOM   3118  C   ALA A 436     -54.924   4.582  57.442  1.00 15.66           C  
ANISOU 3118  C   ALA A 436     1743   2266   1944   -204   -199    123       C  
ATOM   3119  O   ALA A 436     -55.298   4.289  58.580  1.00 14.43           O  
ANISOU 3119  O   ALA A 436     1562   2104   1819   -204   -186    125       O  
ATOM   3120  CB  ALA A 436     -54.544   7.038  57.120  1.00 13.18           C  
ANISOU 3120  CB  ALA A 436     1426   1965   1615   -157   -206    161       C  
ATOM   3121  N   ARG A 437     -55.429   3.991  56.327  1.00 12.57           N  
ANISOU 3121  N   ARG A 437     1361   1885   1528   -228   -225    109       N  
ATOM   3122  CA  ARG A 437     -56.442   2.924  56.388  1.00 12.61           C  
ANISOU 3122  CA  ARG A 437     1349   1895   1548   -257   -241     95       C  
ATOM   3123  C   ARG A 437     -55.892   1.699  57.141  1.00 17.75           C  
ANISOU 3123  C   ARG A 437     2011   2519   2215   -271   -211     77       C  
ATOM   3124  O   ARG A 437     -54.929   1.076  56.686  1.00 17.08           O  
ANISOU 3124  O   ARG A 437     1962   2416   2111   -276   -194     60       O  
ATOM   3125  CB  ARG A 437     -56.901   2.533  54.970  1.00 12.48           C  
ANISOU 3125  CB  ARG A 437     1350   1894   1497   -282   -276     81       C  
ATOM   3126  CG  ARG A 437     -58.136   1.648  54.949  1.00 20.29           C  
ANISOU 3126  CG  ARG A 437     2315   2894   2502   -313   -301     69       C  
ATOM   3127  CD  ARG A 437     -58.480   1.210  53.539  1.00 28.41           C  
ANISOU 3127  CD  ARG A 437     3365   3935   3494   -339   -335     53       C  
ATOM   3128  NE  ARG A 437     -59.694   0.393  53.503  1.00 35.63           N  
ANISOU 3128  NE  ARG A 437     4254   4860   4424   -371   -362     42       N  
ATOM   3129  CZ  ARG A 437     -60.906   0.882  53.261  1.00 47.23           C  
ANISOU 3129  CZ  ARG A 437     5687   6359   5902   -375   -401     56       C  
ATOM   3130  NH1 ARG A 437     -61.069   2.175  53.008  1.00 35.82           N  
ANISOU 3130  NH1 ARG A 437     4229   4932   4449   -348   -417     81       N  
ATOM   3131  NH2 ARG A 437     -61.960   0.078  53.250  1.00 30.75           N  
ANISOU 3131  NH2 ARG A 437     3574   4279   3830   -407   -424     45       N  
ATOM   3132  N   TYR A 438     -56.490   1.376  58.314  1.00 16.16           N  
ANISOU 3132  N   TYR A 438     1778   2313   2049   -274   -201     81       N  
ATOM   3133  CA  TYR A 438     -55.981   0.311  59.192  1.00 16.35           C  
ANISOU 3133  CA  TYR A 438     1811   2310   2091   -283   -171     70       C  
ATOM   3134  C   TYR A 438     -55.974  -1.072  58.530  1.00 21.47           C  
ANISOU 3134  C   TYR A 438     2483   2945   2729   -315   -175     43       C  
ATOM   3135  O   TYR A 438     -55.062  -1.858  58.780  1.00 21.07           O  
ANISOU 3135  O   TYR A 438     2458   2867   2680   -318   -150     31       O  
ATOM   3136  CB  TYR A 438     -56.759   0.269  60.520  1.00 17.06           C  
ANISOU 3136  CB  TYR A 438     1863   2401   2218   -283   -162     82       C  
ATOM   3137  CG  TYR A 438     -56.084  -0.583  61.577  1.00 17.32           C  
ANISOU 3137  CG  TYR A 438     1906   2405   2268   -285   -129     77       C  
ATOM   3138  CD1 TYR A 438     -55.000  -0.097  62.305  1.00 18.76           C  
ANISOU 3138  CD1 TYR A 438     2100   2573   2453   -259   -101     87       C  
ATOM   3139  CD2 TYR A 438     -56.504  -1.885  61.824  1.00 17.81           C  
ANISOU 3139  CD2 TYR A 438     1968   2455   2346   -315   -126     63       C  
ATOM   3140  CE1 TYR A 438     -54.360  -0.881  63.260  1.00 18.29           C  
ANISOU 3140  CE1 TYR A 438     2052   2488   2410   -261    -74     84       C  
ATOM   3141  CE2 TYR A 438     -55.874  -2.679  62.781  1.00 18.47           C  
ANISOU 3141  CE2 TYR A 438     2063   2510   2444   -316    -96     61       C  
ATOM   3142  CZ  TYR A 438     -54.797  -2.174  63.496  1.00 23.45           C  
ANISOU 3142  CZ  TYR A 438     2706   3129   3077   -289    -72     72       C  
ATOM   3143  OH  TYR A 438     -54.165  -2.950  64.436  1.00 20.81           O  
ANISOU 3143  OH  TYR A 438     2383   2767   2758   -289    -46     72       O  
ATOM   3144  N   ASP A 439     -57.012  -1.387  57.722  1.00 19.06           N  
ANISOU 3144  N   ASP A 439     2169   2658   2416   -341   -209     34       N  
ATOM   3145  CA  ASP A 439     -57.129  -2.707  57.075  1.00 19.56           C  
ANISOU 3145  CA  ASP A 439     2254   2709   2469   -375   -216      6       C  
ATOM   3146  C   ASP A 439     -56.129  -2.887  55.924  1.00 23.08           C  
ANISOU 3146  C   ASP A 439     2748   3146   2877   -375   -213    -12       C  
ATOM   3147  O   ASP A 439     -55.811  -4.021  55.559  1.00 23.28           O  
ANISOU 3147  O   ASP A 439     2801   3150   2895   -396   -205    -37       O  
ATOM   3148  CB  ASP A 439     -58.570  -2.954  56.590  1.00 22.26           C  
ANISOU 3148  CB  ASP A 439     2570   3074   2815   -404   -255      2       C  
ATOM   3149  CG  ASP A 439     -59.572  -3.128  57.721  1.00 36.75           C  
ANISOU 3149  CG  ASP A 439     4358   4913   4691   -412   -253     14       C  
ATOM   3150  OD1 ASP A 439     -59.150  -3.520  58.839  1.00 37.17           O  
ANISOU 3150  OD1 ASP A 439     4410   4945   4768   -406   -220     17       O  
ATOM   3151  OD2 ASP A 439     -60.787  -2.958  57.469  1.00 44.62           O  
ANISOU 3151  OD2 ASP A 439     5322   5936   5697   -427   -285     18       O  
ATOM   3152  N   ASP A 440     -55.628  -1.772  55.358  1.00 18.59           N  
ANISOU 3152  N   ASP A 440     2190   2591   2283   -351   -217      1       N  
ATOM   3153  CA  ASP A 440     -54.626  -1.825  54.289  1.00 18.01           C  
ANISOU 3153  CA  ASP A 440     2162   2511   2172   -349   -209    -14       C  
ATOM   3154  C   ASP A 440     -53.221  -2.041  54.887  1.00 21.81           C  
ANISOU 3154  C   ASP A 440     2663   2961   2661   -329   -165    -16       C  
ATOM   3155  O   ASP A 440     -52.472  -1.081  55.078  1.00 20.70           O  
ANISOU 3155  O   ASP A 440     2525   2824   2518   -301   -150      1       O  
ATOM   3156  CB  ASP A 440     -54.670  -0.532  53.439  1.00 19.41           C  
ANISOU 3156  CB  ASP A 440     2341   2714   2319   -333   -230      4       C  
ATOM   3157  CG  ASP A 440     -53.593  -0.461  52.365  1.00 24.82           C  
ANISOU 3157  CG  ASP A 440     3073   3394   2963   -329   -219     -8       C  
ATOM   3158  OD1 ASP A 440     -53.298  -1.511  51.748  1.00 25.45           O  
ANISOU 3158  OD1 ASP A 440     3183   3459   3025   -350   -213    -37       O  
ATOM   3159  OD2 ASP A 440     -53.044   0.641  52.148  1.00 25.82           O  
ANISOU 3159  OD2 ASP A 440     3206   3529   3076   -305   -214     10       O  
ATOM   3160  N   GLN A 441     -52.880  -3.298  55.204  1.00 18.70           N  
ANISOU 3160  N   GLN A 441     2285   2540   2282   -344   -145    -37       N  
ATOM   3161  CA  GLN A 441     -51.594  -3.621  55.837  1.00 17.84           C  
ANISOU 3161  CA  GLN A 441     2191   2401   2185   -326   -106    -38       C  
ATOM   3162  C   GLN A 441     -50.605  -4.271  54.846  1.00 22.78           C  
ANISOU 3162  C   GLN A 441     2861   3009   2784   -331    -89    -64       C  
ATOM   3163  O   GLN A 441     -49.688  -4.988  55.266  1.00 22.09           O  
ANISOU 3163  O   GLN A 441     2789   2892   2711   -324    -59    -74       O  
ATOM   3164  CB  GLN A 441     -51.807  -4.517  57.067  1.00 18.64           C  
ANISOU 3164  CB  GLN A 441     2277   2481   2326   -334    -91    -38       C  
ATOM   3165  CG  GLN A 441     -52.542  -3.811  58.206  1.00 24.35           C  
ANISOU 3165  CG  GLN A 441     2958   3218   3075   -324    -97    -12       C  
ATOM   3166  CD  GLN A 441     -53.007  -4.770  59.275  1.00 34.19           C  
ANISOU 3166  CD  GLN A 441     4188   4447   4355   -339    -88    -13       C  
ATOM   3167  OE1 GLN A 441     -52.515  -5.896  59.397  1.00 31.51           O  
ANISOU 3167  OE1 GLN A 441     3870   4078   4024   -350    -71    -29       O  
ATOM   3168  NE2 GLN A 441     -53.952  -4.327  60.094  1.00 20.12           N  
ANISOU 3168  NE2 GLN A 441     2369   2681   2594   -339    -97      5       N  
ATOM   3169  N   GLN A 442     -50.747  -3.958  53.542  1.00 20.00           N  
ANISOU 3169  N   GLN A 442     2531   2675   2393   -340   -108    -74       N  
ATOM   3170  CA  GLN A 442     -49.865  -4.511  52.511  1.00 19.96           C  
ANISOU 3170  CA  GLN A 442     2570   2657   2358   -345    -91   -100       C  
ATOM   3171  C   GLN A 442     -48.793  -3.504  52.098  1.00 23.38           C  
ANISOU 3171  C   GLN A 442     3018   3097   2770   -318    -72    -88       C  
ATOM   3172  O   GLN A 442     -49.079  -2.314  51.959  1.00 22.69           O  
ANISOU 3172  O   GLN A 442     2916   3034   2671   -306    -89    -65       O  
ATOM   3173  CB  GLN A 442     -50.677  -4.962  51.290  1.00 21.72           C  
ANISOU 3173  CB  GLN A 442     2813   2894   2547   -376   -122   -122       C  
ATOM   3174  N   GLY A 443     -47.568  -3.992  51.906  1.00 20.02           N  
ANISOU 3174  N   GLY A 443     2619   2647   2340   -309    -37   -103       N  
ATOM   3175  CA  GLY A 443     -46.446  -3.161  51.481  1.00 19.67           C  
ANISOU 3175  CA  GLY A 443     2590   2606   2278   -285    -14    -94       C  
ATOM   3176  C   GLY A 443     -45.424  -2.920  52.572  1.00 23.45           C  
ANISOU 3176  C   GLY A 443     3053   3067   2791   -258     17    -79       C  
ATOM   3177  O   GLY A 443     -45.737  -3.045  53.764  1.00 22.67           O  
ANISOU 3177  O   GLY A 443     2926   2960   2728   -253     16    -66       O  
ATOM   3178  N   ALA A 444     -44.188  -2.541  52.174  1.00 19.72           N  
ANISOU 3178  N   ALA A 444     2598   2588   2306   -240     46    -79       N  
ATOM   3179  CA  ALA A 444     -43.105  -2.262  53.121  1.00 18.96           C  
ANISOU 3179  CA  ALA A 444     2487   2476   2241   -214     76    -64       C  
ATOM   3180  C   ALA A 444     -43.398  -1.002  53.949  1.00 22.77           C  
ANISOU 3180  C   ALA A 444     2937   2975   2738   -198     61    -30       C  
ATOM   3181  O   ALA A 444     -43.695   0.061  53.389  1.00 22.58           O  
ANISOU 3181  O   ALA A 444     2913   2975   2690   -196     45    -16       O  
ATOM   3182  CB  ALA A 444     -41.788  -2.104  52.376  1.00 19.68           C  
ANISOU 3182  CB  ALA A 444     2603   2560   2314   -202    108    -72       C  
ATOM   3183  N   GLY A 445     -43.337  -1.144  55.271  1.00 18.63           N  
ANISOU 3183  N   GLY A 445     2389   2439   2252   -188     67    -18       N  
ATOM   3184  CA  GLY A 445     -43.592  -0.045  56.195  1.00 18.01           C  
ANISOU 3184  CA  GLY A 445     2280   2373   2190   -173     57     11       C  
ATOM   3185  C   GLY A 445     -45.065   0.154  56.507  1.00 21.46           C  
ANISOU 3185  C   GLY A 445     2696   2828   2631   -185     24     19       C  
ATOM   3186  O   GLY A 445     -45.434   1.132  57.165  1.00 20.88           O  
ANISOU 3186  O   GLY A 445     2599   2767   2568   -173     14     42       O  
ATOM   3187  N   ASN A 446     -45.918  -0.808  56.089  1.00 17.60           N  
ANISOU 3187  N   ASN A 446     2214   2339   2136   -210      9      1       N  
ATOM   3188  CA  ASN A 446     -47.372  -0.663  56.208  1.00 17.10           C  
ANISOU 3188  CA  ASN A 446     2128   2294   2074   -224    -24      7       C  
ATOM   3189  C   ASN A 446     -48.009  -1.692  57.200  1.00 20.37           C  
ANISOU 3189  C   ASN A 446     2526   2694   2521   -238    -25      2       C  
ATOM   3190  O   ASN A 446     -49.207  -1.955  57.117  1.00 20.69           O  
ANISOU 3190  O   ASN A 446     2551   2746   2562   -258    -50     -1       O  
ATOM   3191  CB  ASN A 446     -48.035  -0.765  54.815  1.00 16.53           C  
ANISOU 3191  CB  ASN A 446     2074   2240   1965   -245    -49     -7       C  
ATOM   3192  CG  ASN A 446     -49.349  -0.022  54.700  1.00 35.10           C  
ANISOU 3192  CG  ASN A 446     4403   4622   4314   -250    -86      8       C  
ATOM   3193  OD1 ASN A 446     -49.690   0.827  55.531  1.00 26.43           O  
ANISOU 3193  OD1 ASN A 446     3274   3532   3235   -235    -91     32       O  
ATOM   3194  ND2 ASN A 446     -50.073  -0.268  53.618  1.00 27.30           N  
ANISOU 3194  ND2 ASN A 446     3427   3649   3298   -272   -113     -4       N  
ATOM   3195  N   THR A 447     -47.220  -2.205  58.169  1.00 15.89           N  
ANISOU 3195  N   THR A 447     1957   2102   1980   -228      1      3       N  
ATOM   3196  CA  THR A 447     -47.752  -3.141  59.180  1.00 15.39           C  
ANISOU 3196  CA  THR A 447     1879   2022   1946   -240      3      1       C  
ATOM   3197  C   THR A 447     -48.679  -2.410  60.176  1.00 19.03           C  
ANISOU 3197  C   THR A 447     2304   2500   2424   -235    -11     25       C  
ATOM   3198  O   THR A 447     -48.597  -1.179  60.310  1.00 18.16           O  
ANISOU 3198  O   THR A 447     2182   2408   2310   -216    -14     43       O  
ATOM   3199  CB  THR A 447     -46.608  -3.877  59.904  1.00 19.02           C  
ANISOU 3199  CB  THR A 447     2350   2450   2427   -228     33     -1       C  
ATOM   3200  OG1 THR A 447     -45.869  -2.943  60.679  1.00 17.72           O  
ANISOU 3200  OG1 THR A 447     2173   2288   2273   -202     46     20       O  
ATOM   3201  CG2 THR A 447     -45.683  -4.617  58.941  1.00 15.33           C  
ANISOU 3201  CG2 THR A 447     1916   1964   1946   -230     50    -26       C  
ATOM   3202  N   ALA A 448     -49.566  -3.175  60.876  1.00 15.60           N  
ANISOU 3202  N   ALA A 448     1854   2061   2012   -253    -16     23       N  
ATOM   3203  CA  ALA A 448     -50.535  -2.611  61.833  1.00 15.48           C  
ANISOU 3203  CA  ALA A 448     1804   2062   2014   -252    -26     43       C  
ATOM   3204  C   ALA A 448     -49.851  -1.808  62.939  1.00 19.57           C  
ANISOU 3204  C   ALA A 448     2313   2577   2547   -225     -8     64       C  
ATOM   3205  O   ALA A 448     -50.329  -0.726  63.299  1.00 19.36           O  
ANISOU 3205  O   ALA A 448     2264   2571   2522   -212    -16     81       O  
ATOM   3206  CB  ALA A 448     -51.376  -3.722  62.438  1.00 16.54           C  
ANISOU 3206  CB  ALA A 448     1928   2186   2171   -277    -27     37       C  
ATOM   3207  N   LEU A 449     -48.717  -2.330  63.479  1.00 15.55           N  
ANISOU 3207  N   LEU A 449     1820   2042   2048   -215     16     63       N  
ATOM   3208  CA  LEU A 449     -47.963  -1.643  64.538  1.00 14.27           C  
ANISOU 3208  CA  LEU A 449     1650   1875   1896   -191     31     81       C  
ATOM   3209  C   LEU A 449     -47.344  -0.333  64.021  1.00 16.52           C  
ANISOU 3209  C   LEU A 449     1937   2174   2164   -169     30     90       C  
ATOM   3210  O   LEU A 449     -47.338   0.671  64.738  1.00 15.62           O  
ANISOU 3210  O   LEU A 449     1808   2069   2056   -153     31    107       O  
ATOM   3211  CB  LEU A 449     -46.867  -2.569  65.116  1.00 14.06           C  
ANISOU 3211  CB  LEU A 449     1640   1817   1884   -186     53     78       C  
ATOM   3212  CG  LEU A 449     -46.037  -1.984  66.279  1.00 18.24           C  
ANISOU 3212  CG  LEU A 449     2163   2341   2426   -164     67     97       C  
ATOM   3213  CD1 LEU A 449     -46.928  -1.577  67.434  1.00 17.87           C  
ANISOU 3213  CD1 LEU A 449     2093   2305   2391   -165     63    113       C  
ATOM   3214  CD2 LEU A 449     -44.984  -2.970  66.745  1.00 21.27           C  
ANISOU 3214  CD2 LEU A 449     2563   2694   2825   -160     85     94       C  
ATOM   3215  N   GLU A 450     -46.855  -0.337  62.764  1.00 12.83           N  
ANISOU 3215  N   GLU A 450     1491   1708   1676   -171     28     77       N  
ATOM   3216  CA  GLU A 450     -46.272   0.858  62.153  1.00 11.79           C  
ANISOU 3216  CA  GLU A 450     1364   1589   1525   -153     28     85       C  
ATOM   3217  C   GLU A 450     -47.309   1.970  61.988  1.00 14.53           C  
ANISOU 3217  C   GLU A 450     1693   1963   1865   -151      5     98       C  
ATOM   3218  O   GLU A 450     -46.997   3.132  62.232  1.00 13.81           O  
ANISOU 3218  O   GLU A 450     1594   1879   1773   -132      7    114       O  
ATOM   3219  CB  GLU A 450     -45.614   0.521  60.816  1.00 13.05           C  
ANISOU 3219  CB  GLU A 450     1552   1745   1662   -158     33     68       C  
ATOM   3220  CG  GLU A 450     -44.268  -0.164  60.972  1.00 19.65           C  
ANISOU 3220  CG  GLU A 450     2405   2554   2506   -150     60     59       C  
ATOM   3221  CD  GLU A 450     -43.665  -0.661  59.677  1.00 24.24           C  
ANISOU 3221  CD  GLU A 450     3014   3129   3065   -156     69     38       C  
ATOM   3222  OE1 GLU A 450     -44.250  -1.580  59.067  1.00 15.22           O  
ANISOU 3222  OE1 GLU A 450     1885   1985   1915   -177     61     19       O  
ATOM   3223  OE2 GLU A 450     -42.568  -0.186  59.312  1.00 11.72           O  
ANISOU 3223  OE2 GLU A 450     1439   1541   1473   -141     86     40       O  
ATOM   3224  N   LYS A 451     -48.576   1.600  61.643  1.00 10.66           N  
ANISOU 3224  N   LYS A 451     1191   1486   1372   -170    -16     92       N  
ATOM   3225  CA  LYS A 451     -49.684   2.568  61.542  1.00 10.35           C  
ANISOU 3225  CA  LYS A 451     1129   1472   1331   -167    -39    105       C  
ATOM   3226  C   LYS A 451     -49.961   3.206  62.897  1.00 13.89           C  
ANISOU 3226  C   LYS A 451     1552   1922   1803   -152    -32    123       C  
ATOM   3227  O   LYS A 451     -50.133   4.426  62.983  1.00 13.76           O  
ANISOU 3227  O   LYS A 451     1524   1919   1786   -135    -38    138       O  
ATOM   3228  CB  LYS A 451     -50.960   1.884  61.033  1.00 12.74           C  
ANISOU 3228  CB  LYS A 451     1421   1788   1632   -192    -62     95       C  
ATOM   3229  CG  LYS A 451     -50.857   1.339  59.636  1.00 18.69           C  
ANISOU 3229  CG  LYS A 451     2200   2543   2358   -209    -74     76       C  
ATOM   3230  CD  LYS A 451     -52.102   0.528  59.285  1.00 26.79           C  
ANISOU 3230  CD  LYS A 451     3215   3578   3386   -237    -98     64       C  
ATOM   3231  CE  LYS A 451     -52.027  -0.065  57.910  1.00 28.88           C  
ANISOU 3231  CE  LYS A 451     3508   3844   3620   -256   -110     43       C  
ATOM   3232  NZ  LYS A 451     -52.127   0.976  56.856  1.00 33.20           N  
ANISOU 3232  NZ  LYS A 451     4063   4415   4138   -248   -131     51       N  
ATOM   3233  N   ILE A 452     -50.075   2.368  63.957  1.00  9.84           N  
ANISOU 3233  N   ILE A 452     1031   1396   1312   -160    -19    121       N  
ATOM   3234  CA  ILE A 452     -50.372   2.839  65.312  1.00  9.97           C  
ANISOU 3234  CA  ILE A 452     1026   1414   1349   -149     -9    136       C  
ATOM   3235  C   ILE A 452     -49.314   3.832  65.798  1.00 15.31           C  
ANISOU 3235  C   ILE A 452     1710   2084   2024   -124      4    148       C  
ATOM   3236  O   ILE A 452     -49.661   4.912  66.278  1.00 14.90           O  
ANISOU 3236  O   ILE A 452     1643   2043   1977   -109      2    161       O  
ATOM   3237  CB  ILE A 452     -50.533   1.637  66.297  1.00 12.87           C  
ANISOU 3237  CB  ILE A 452     1390   1764   1735   -164      4    132       C  
ATOM   3238  CG1 ILE A 452     -51.709   0.724  65.869  1.00 13.29           C  
ANISOU 3238  CG1 ILE A 452     1433   1824   1793   -191    -11    121       C  
ATOM   3239  CG2 ILE A 452     -50.704   2.131  67.757  1.00 12.93           C  
ANISOU 3239  CG2 ILE A 452     1381   1773   1761   -152     17    147       C  
ATOM   3240  CD1 ILE A 452     -51.712  -0.620  66.528  1.00 14.11           C  
ANISOU 3240  CD1 ILE A 452     1542   1908   1912   -210      2    114       C  
ATOM   3241  N   ILE A 453     -48.020   3.472  65.666  1.00 12.18           N  
ANISOU 3241  N   ILE A 453     1336   1669   1623   -120     19    143       N  
ATOM   3242  CA  ILE A 453     -46.931   4.329  66.138  1.00 12.34           C  
ANISOU 3242  CA  ILE A 453     1362   1682   1644    -99     32    153       C  
ATOM   3243  C   ILE A 453     -46.798   5.608  65.290  1.00 17.07           C  
ANISOU 3243  C   ILE A 453     1964   2295   2227    -86     22    160       C  
ATOM   3244  O   ILE A 453     -46.560   6.680  65.843  1.00 16.59           O  
ANISOU 3244  O   ILE A 453     1897   2236   2170    -69     26    173       O  
ATOM   3245  CB  ILE A 453     -45.583   3.543  66.260  1.00 14.97           C  
ANISOU 3245  CB  ILE A 453     1715   1993   1980    -97     50    147       C  
ATOM   3246  CG1 ILE A 453     -45.739   2.297  67.177  1.00 14.62           C  
ANISOU 3246  CG1 ILE A 453     1670   1933   1954   -109     58    143       C  
ATOM   3247  CG2 ILE A 453     -44.458   4.451  66.754  1.00 15.77           C  
ANISOU 3247  CG2 ILE A 453     1820   2088   2084    -78     61    158       C  
ATOM   3248  CD1 ILE A 453     -46.206   2.622  68.676  1.00 17.28           C  
ANISOU 3248  CD1 ILE A 453     1989   2271   2305   -104     62    157       C  
ATOM   3249  N   THR A 454     -47.031   5.507  63.961  1.00 13.57           N  
ANISOU 3249  N   THR A 454     1531   1861   1764    -94     10    152       N  
ATOM   3250  CA  THR A 454     -47.023   6.694  63.086  1.00 13.22           C  
ANISOU 3250  CA  THR A 454     1491   1831   1702    -84     -1    161       C  
ATOM   3251  C   THR A 454     -48.100   7.689  63.540  1.00 16.88           C  
ANISOU 3251  C   THR A 454     1930   2310   2174    -74    -16    176       C  
ATOM   3252  O   THR A 454     -47.817   8.881  63.688  1.00 17.03           O  
ANISOU 3252  O   THR A 454     1948   2331   2194    -57    -15    189       O  
ATOM   3253  CB  THR A 454     -47.219   6.285  61.610  1.00 19.66           C  
ANISOU 3253  CB  THR A 454     2323   2655   2493    -97    -14    150       C  
ATOM   3254  OG1 THR A 454     -46.173   5.398  61.230  1.00 19.79           O  
ANISOU 3254  OG1 THR A 454     2362   2655   2502   -104      3    135       O  
ATOM   3255  CG2 THR A 454     -47.242   7.489  60.668  1.00 19.36           C  
ANISOU 3255  CG2 THR A 454     2292   2632   2434    -88    -27    161       C  
ATOM   3256  N   GLN A 455     -49.317   7.184  63.824  1.00 11.91           N  
ANISOU 3256  N   GLN A 455     1281   1690   1556    -86    -27    173       N  
ATOM   3257  CA  GLN A 455     -50.424   8.026  64.257  1.00 11.16           C  
ANISOU 3257  CA  GLN A 455     1158   1609   1472    -77    -39    185       C  
ATOM   3258  C   GLN A 455     -50.253   8.498  65.699  1.00 15.91           C  
ANISOU 3258  C   GLN A 455     1749   2203   2093    -63    -22    194       C  
ATOM   3259  O   GLN A 455     -50.648   9.618  66.029  1.00 15.73           O  
ANISOU 3259  O   GLN A 455     1712   2187   2077    -46    -25    206       O  
ATOM   3260  CB  GLN A 455     -51.763   7.304  64.069  1.00 12.12           C  
ANISOU 3260  CB  GLN A 455     1260   1745   1600    -95    -57    179       C  
ATOM   3261  CG  GLN A 455     -52.144   7.097  62.595  1.00 12.46           C  
ANISOU 3261  CG  GLN A 455     1312   1801   1621   -108    -81    172       C  
ATOM   3262  CD  GLN A 455     -52.280   8.407  61.850  1.00 19.65           C  
ANISOU 3262  CD  GLN A 455     2223   2726   2519    -91    -98    187       C  
ATOM   3263  OE1 GLN A 455     -52.794   9.402  62.375  1.00 14.67           O  
ANISOU 3263  OE1 GLN A 455     1570   2101   1901    -73   -101    202       O  
ATOM   3264  NE2 GLN A 455     -51.851   8.423  60.600  1.00  5.08           N  
ANISOU 3264  NE2 GLN A 455      425    870    636    -94    -96    184       N  
ATOM   3265  N   LYS A 456     -49.619   7.665  66.551  1.00 11.53           N  
ANISOU 3265  N   LYS A 456     1201   1632   1547    -69     -3    188       N  
ATOM   3266  CA  LYS A 456     -49.331   8.034  67.938  1.00 10.65           C  
ANISOU 3266  CA  LYS A 456     1085   1512   1451    -57     14    195       C  
ATOM   3267  C   LYS A 456     -48.273   9.146  67.981  1.00 12.40           C  
ANISOU 3267  C   LYS A 456     1319   1726   1666    -38     21    203       C  
ATOM   3268  O   LYS A 456     -48.383  10.072  68.782  1.00 11.29           O  
ANISOU 3268  O   LYS A 456     1171   1586   1534    -24     26    212       O  
ATOM   3269  CB  LYS A 456     -48.846   6.808  68.726  1.00 13.10           C  
ANISOU 3269  CB  LYS A 456     1403   1806   1769    -69     29    188       C  
ATOM   3270  CG  LYS A 456     -48.676   7.060  70.207  1.00 18.39           C  
ANISOU 3270  CG  LYS A 456     2067   2469   2450    -61     44    196       C  
ATOM   3271  CD  LYS A 456     -48.052   5.869  70.889  1.00 22.58           C  
ANISOU 3271  CD  LYS A 456     2610   2983   2988    -72     57    192       C  
ATOM   3272  CE  LYS A 456     -47.910   6.079  72.369  1.00 24.20           C  
ANISOU 3272  CE  LYS A 456     2812   3182   3201    -66     70    200       C  
ATOM   3273  NZ  LYS A 456     -47.105   5.003  72.996  1.00 24.71           N  
ANISOU 3273  NZ  LYS A 456     2891   3228   3270    -73     81    199       N  
ATOM   3274  N   TYR A 457     -47.260   9.056  67.095  1.00  8.14           N  
ANISOU 3274  N   TYR A 457      800   1180   1113    -39     22    200       N  
ATOM   3275  CA  TYR A 457     -46.185  10.039  66.998  1.00  7.51           C  
ANISOU 3275  CA  TYR A 457      733   1093   1027    -25     28    207       C  
ATOM   3276  C   TYR A 457     -46.740  11.411  66.576  1.00 12.35           C  
ANISOU 3276  C   TYR A 457     1339   1716   1636    -11     16    219       C  
ATOM   3277  O   TYR A 457     -46.529  12.400  67.281  1.00 11.15           O  
ANISOU 3277  O   TYR A 457     1184   1560   1491      3     22    227       O  
ATOM   3278  CB  TYR A 457     -45.106   9.549  65.988  1.00  8.34           C  
ANISOU 3278  CB  TYR A 457      860   1190   1119    -30     33    200       C  
ATOM   3279  CG  TYR A 457     -43.932  10.487  65.829  1.00  8.19           C  
ANISOU 3279  CG  TYR A 457      852   1164   1095    -18     42    207       C  
ATOM   3280  CD1 TYR A 457     -43.970  11.536  64.910  1.00 10.07           C  
ANISOU 3280  CD1 TYR A 457     1097   1410   1320    -11     34    216       C  
ATOM   3281  CD2 TYR A 457     -42.732  10.252  66.496  1.00  8.66           C  
ANISOU 3281  CD2 TYR A 457      919   1209   1165    -15     58    207       C  
ATOM   3282  CE1 TYR A 457     -42.875  12.377  64.725  1.00 10.02           C  
ANISOU 3282  CE1 TYR A 457     1102   1396   1310     -3     43    223       C  
ATOM   3283  CE2 TYR A 457     -41.616  11.064  66.289  1.00  9.21           C  
ANISOU 3283  CE2 TYR A 457      997   1271   1232     -7     66    213       C  
ATOM   3284  CZ  TYR A 457     -41.692  12.126  65.403  1.00 15.64           C  
ANISOU 3284  CZ  TYR A 457     1817   2092   2033     -1     60    221       C  
ATOM   3285  OH  TYR A 457     -40.600  12.934  65.205  1.00 16.52           O  
ANISOU 3285  OH  TYR A 457     1937   2197   2143      5     69    228       O  
ATOM   3286  N   ILE A 458     -47.488  11.461  65.431  1.00 10.10           N  
ANISOU 3286  N   ILE A 458     1052   1446   1338    -15     -2    219       N  
ATOM   3287  CA  ILE A 458     -48.083  12.718  64.920  1.00 10.46           C  
ANISOU 3287  CA  ILE A 458     1092   1502   1380     -2    -17    232       C  
ATOM   3288  C   ILE A 458     -49.020  13.357  65.969  1.00 16.06           C  
ANISOU 3288  C   ILE A 458     1777   2215   2110     10    -17    239       C  
ATOM   3289  O   ILE A 458     -48.988  14.580  66.164  1.00 15.78           O  
ANISOU 3289  O   ILE A 458     1741   2177   2079     28    -17    250       O  
ATOM   3290  CB  ILE A 458     -48.814  12.482  63.553  1.00 13.86           C  
ANISOU 3290  CB  ILE A 458     1523   1949   1793    -11    -40    231       C  
ATOM   3291  CG1 ILE A 458     -47.850  11.859  62.505  1.00 13.95           C  
ANISOU 3291  CG1 ILE A 458     1563   1957   1783    -23    -36    222       C  
ATOM   3292  CG2 ILE A 458     -49.441  13.797  63.024  1.00 14.89           C  
ANISOU 3292  CG2 ILE A 458     1647   2089   1921      5    -58    248       C  
ATOM   3293  CD1 ILE A 458     -48.568  11.295  61.221  1.00 18.34           C  
ANISOU 3293  CD1 ILE A 458     2123   2528   2317    -39    -58    216       C  
ATOM   3294  N   ALA A 459     -49.800  12.519  66.692  1.00 13.12           N  
ANISOU 3294  N   ALA A 459     1387   1848   1751      1    -15    232       N  
ATOM   3295  CA  ALA A 459     -50.718  13.000  67.733  1.00 13.11           C  
ANISOU 3295  CA  ALA A 459     1362   1851   1769     11    -11    237       C  
ATOM   3296  C   ALA A 459     -49.963  13.571  68.953  1.00 15.16           C  
ANISOU 3296  C   ALA A 459     1629   2095   2036     23     10    239       C  
ATOM   3297  O   ALA A 459     -50.562  14.260  69.779  1.00 14.39           O  
ANISOU 3297  O   ALA A 459     1517   1999   1951     35     16    243       O  
ATOM   3298  CB  ALA A 459     -51.649  11.875  68.173  1.00 14.12           C  
ANISOU 3298  CB  ALA A 459     1471   1987   1907     -5    -10    228       C  
ATOM   3299  N   GLY A 460     -48.656  13.293  69.036  1.00 11.29           N  
ANISOU 3299  N   GLY A 460     1161   1591   1538     19     20    235       N  
ATOM   3300  CA  GLY A 460     -47.827  13.740  70.157  1.00 11.06           C  
ANISOU 3300  CA  GLY A 460     1141   1547   1514     27     36    237       C  
ATOM   3301  C   GLY A 460     -46.924  14.924  69.845  1.00 14.22           C  
ANISOU 3301  C   GLY A 460     1556   1938   1909     40     37    244       C  
ATOM   3302  O   GLY A 460     -46.213  15.405  70.724  1.00 13.99           O  
ANISOU 3302  O   GLY A 460     1534   1897   1884     45     48    245       O  
ATOM   3303  N   ILE A 461     -46.939  15.403  68.585  1.00 10.38           N  
ANISOU 3303  N   ILE A 461     1075   1457   1412     43     24    250       N  
ATOM   3304  CA  ILE A 461     -46.084  16.525  68.174  1.00 10.00           C  
ANISOU 3304  CA  ILE A 461     1042   1399   1358     53     25    259       C  
ATOM   3305  C   ILE A 461     -46.607  17.868  68.726  1.00 13.25           C  
ANISOU 3305  C   ILE A 461     1446   1807   1781     71     24    267       C  
ATOM   3306  O   ILE A 461     -47.736  18.257  68.426  1.00 12.71           O  
ANISOU 3306  O   ILE A 461     1363   1748   1717     80     13    272       O  
ATOM   3307  CB  ILE A 461     -45.927  16.575  66.610  1.00 12.78           C  
ANISOU 3307  CB  ILE A 461     1405   1758   1693     49     13    263       C  
ATOM   3308  CG1 ILE A 461     -45.341  15.254  66.061  1.00 13.42           C  
ANISOU 3308  CG1 ILE A 461     1496   1840   1763     31     17    252       C  
ATOM   3309  CG2 ILE A 461     -45.075  17.791  66.178  1.00 11.29           C  
ANISOU 3309  CG2 ILE A 461     1232   1558   1499     58     15    275       C  
ATOM   3310  CD1 ILE A 461     -45.267  15.187  64.511  1.00 18.90           C  
ANISOU 3310  CD1 ILE A 461     2203   2542   2435     25      6    254       C  
ATOM   3311  N   PRO A 462     -45.764  18.646  69.470  1.00 10.66           N  
ANISOU 3311  N   PRO A 462     1129   1463   1458     78     35    269       N  
ATOM   3312  CA  PRO A 462     -44.369  18.377  69.830  1.00 10.22           C  
ANISOU 3312  CA  PRO A 462     1088   1395   1399     70     46    265       C  
ATOM   3313  C   PRO A 462     -44.177  18.066  71.337  1.00 14.75           C  
ANISOU 3313  C   PRO A 462     1660   1963   1983     68     58    257       C  
ATOM   3314  O   PRO A 462     -43.087  17.651  71.739  1.00 14.04           O  
ANISOU 3314  O   PRO A 462     1578   1864   1892     60     65    254       O  
ATOM   3315  CB  PRO A 462     -43.685  19.692  69.465  1.00 11.86           C  
ANISOU 3315  CB  PRO A 462     1309   1591   1607     78     46    274       C  
ATOM   3316  CG  PRO A 462     -44.794  20.791  69.752  1.00 16.33           C  
ANISOU 3316  CG  PRO A 462     1867   2157   2182     96     41    280       C  
ATOM   3317  CD  PRO A 462     -46.134  20.031  69.816  1.00 12.50           C  
ANISOU 3317  CD  PRO A 462     1360   1688   1700     96     35    276       C  
ATOM   3318  N   ASP A 463     -45.224  18.346  72.180  1.00 10.79           N  
ANISOU 3318  N   ASP A 463     1145   1464   1489     76     60    255       N  
ATOM   3319  CA  ASP A 463     -45.116  18.278  73.657  1.00 10.12           C  
ANISOU 3319  CA  ASP A 463     1062   1374   1410     75     72    249       C  
ATOM   3320  C   ASP A 463     -44.862  16.872  74.194  1.00 14.71           C  
ANISOU 3320  C   ASP A 463     1642   1958   1989     60     77    243       C  
ATOM   3321  O   ASP A 463     -44.412  16.727  75.334  1.00 13.96           O  
ANISOU 3321  O   ASP A 463     1554   1857   1895     57     85    239       O  
ATOM   3322  CB  ASP A 463     -46.359  18.896  74.330  1.00 11.82           C  
ANISOU 3322  CB  ASP A 463     1264   1594   1634     88     77    248       C  
ATOM   3323  CG  ASP A 463     -46.515  20.392  74.085  1.00 16.47           C  
ANISOU 3323  CG  ASP A 463     1856   2173   2228    106     74    253       C  
ATOM   3324  OD1 ASP A 463     -45.512  21.040  73.703  1.00 15.44           O  
ANISOU 3324  OD1 ASP A 463     1742   2031   2094    106     71    258       O  
ATOM   3325  OD2 ASP A 463     -47.613  20.925  74.352  1.00 20.05           O  
ANISOU 3325  OD2 ASP A 463     2297   2631   2692    119     77    253       O  
ATOM   3326  N   LEU A 464     -45.170  15.832  73.395  1.00 11.72           N  
ANISOU 3326  N   LEU A 464     1257   1588   1607     50     72    241       N  
ATOM   3327  CA  LEU A 464     -44.953  14.448  73.820  1.00 10.86           C  
ANISOU 3327  CA  LEU A 464     1148   1479   1497     36     76    236       C  
ATOM   3328  C   LEU A 464     -43.630  13.881  73.237  1.00 13.74           C  
ANISOU 3328  C   LEU A 464     1527   1836   1859     29     76    235       C  
ATOM   3329  O   LEU A 464     -43.499  12.663  73.065  1.00 13.25           O  
ANISOU 3329  O   LEU A 464     1465   1773   1796     18     77    231       O  
ATOM   3330  CB  LEU A 464     -46.162  13.551  73.418  1.00 10.89           C  
ANISOU 3330  CB  LEU A 464     1137   1497   1504     28     72    233       C  
ATOM   3331  CG  LEU A 464     -47.466  13.684  74.293  1.00 15.66           C  
ANISOU 3331  CG  LEU A 464     1724   2111   2117     31     78    232       C  
ATOM   3332  CD1 LEU A 464     -47.192  13.339  75.766  1.00 15.42           C  
ANISOU 3332  CD1 LEU A 464     1700   2073   2087     27     93    230       C  
ATOM   3333  CD2 LEU A 464     -48.095  15.074  74.161  1.00 18.23           C  
ANISOU 3333  CD2 LEU A 464     2042   2440   2447     49     76    237       C  
ATOM   3334  N   ALA A 465     -42.622  14.769  73.016  1.00  9.91           N  
ANISOU 3334  N   ALA A 465     1052   1341   1371     35     76    240       N  
ATOM   3335  CA  ALA A 465     -41.309  14.376  72.460  1.00  9.48           C  
ANISOU 3335  CA  ALA A 465     1007   1279   1315     30     77    239       C  
ATOM   3336  C   ALA A 465     -40.654  13.238  73.263  1.00 13.33           C  
ANISOU 3336  C   ALA A 465     1497   1760   1808     21     83    236       C  
ATOM   3337  O   ALA A 465     -40.030  12.353  72.675  1.00 13.13           O  
ANISOU 3337  O   ALA A 465     1475   1731   1783     15     85    233       O  
ATOM   3338  CB  ALA A 465     -40.381  15.579  72.409  1.00 10.25           C  
ANISOU 3338  CB  ALA A 465     1112   1367   1413     36     78    245       C  
ATOM   3339  N   GLN A 466     -40.807  13.255  74.605  1.00  9.74           N  
ANISOU 3339  N   GLN A 466     1042   1302   1357     22     85    237       N  
ATOM   3340  CA  GLN A 466     -40.234  12.214  75.459  1.00  9.65           C  
ANISOU 3340  CA  GLN A 466     1034   1284   1349     15     88    236       C  
ATOM   3341  C   GLN A 466     -40.844  10.856  75.137  1.00 14.56           C  
ANISOU 3341  C   GLN A 466     1651   1909   1972      6     89    232       C  
ATOM   3342  O   GLN A 466     -40.123   9.868  75.049  1.00 15.05           O  
ANISOU 3342  O   GLN A 466     1717   1963   2039      0     91    232       O  
ATOM   3343  CB  GLN A 466     -40.425  12.560  76.953  1.00 10.84           C  
ANISOU 3343  CB  GLN A 466     1188   1434   1499     16     90    238       C  
ATOM   3344  CG  GLN A 466     -39.693  11.593  77.914  1.00 13.60           C  
ANISOU 3344  CG  GLN A 466     1542   1774   1850      9     90    241       C  
ATOM   3345  CD  GLN A 466     -38.196  11.566  77.667  1.00 20.61           C  
ANISOU 3345  CD  GLN A 466     2434   2652   2744     10     85    244       C  
ATOM   3346  OE1 GLN A 466     -37.506  12.595  77.734  1.00 10.18           O  
ANISOU 3346  OE1 GLN A 466     1116   1328   1424     14     82    246       O  
ATOM   3347  NE2 GLN A 466     -37.664  10.385  77.394  1.00  9.19           N  
ANISOU 3347  NE2 GLN A 466      987   1200   1305      6     86    245       N  
ATOM   3348  N   GLU A 467     -42.166  10.818  74.891  1.00 11.75           N  
ANISOU 3348  N   GLU A 467     1286   1564   1613      4     89    230       N  
ATOM   3349  CA  GLU A 467     -42.849   9.588  74.492  1.00 11.62           C  
ANISOU 3349  CA  GLU A 467     1266   1551   1599     -8     89    225       C  
ATOM   3350  C   GLU A 467     -42.506   9.203  73.061  1.00 16.32           C  
ANISOU 3350  C   GLU A 467     1864   2146   2191    -11     85    220       C  
ATOM   3351  O   GLU A 467     -42.453   8.015  72.736  1.00 15.34           O  
ANISOU 3351  O   GLU A 467     1743   2017   2069    -21     86    214       O  
ATOM   3352  CB  GLU A 467     -44.365   9.716  74.677  1.00 12.88           C  
ANISOU 3352  CB  GLU A 467     1411   1723   1758    -10     88    224       C  
ATOM   3353  CG  GLU A 467     -44.790   9.690  76.135  1.00 21.62           C  
ANISOU 3353  CG  GLU A 467     2516   2831   2868    -11     96    227       C  
ATOM   3354  CD  GLU A 467     -44.272   8.488  76.908  1.00 38.37           C  
ANISOU 3354  CD  GLU A 467     4646   4941   4991    -21    102    229       C  
ATOM   3355  OE1 GLU A 467     -44.517   7.343  76.462  1.00 40.18           O  
ANISOU 3355  OE1 GLU A 467     4874   5168   5225    -33    101    226       O  
ATOM   3356  OE2 GLU A 467     -43.602   8.693  77.944  1.00 23.52           O  
ANISOU 3356  OE2 GLU A 467     2775   3054   3109    -18    105    234       O  
ATOM   3357  N   GLY A 468     -42.219  10.207  72.229  1.00 13.68           N  
ANISOU 3357  N   GLY A 468     1532   1815   1850     -3     81    221       N  
ATOM   3358  CA  GLY A 468     -41.733   9.985  70.874  1.00 13.51           C  
ANISOU 3358  CA  GLY A 468     1518   1794   1823     -5     80    217       C  
ATOM   3359  C   GLY A 468     -40.353   9.355  70.865  1.00 16.20           C  
ANISOU 3359  C   GLY A 468     1867   2120   2168     -6     88    215       C  
ATOM   3360  O   GLY A 468     -40.104   8.405  70.115  1.00 15.71           O  
ANISOU 3360  O   GLY A 468     1811   2054   2105    -13     92    207       O  
ATOM   3361  N   TRP A 469     -39.461   9.832  71.769  1.00 11.02           N  
ANISOU 3361  N   TRP A 469     1211   1455   1519      0     91    221       N  
ATOM   3362  CA  TRP A 469     -38.113   9.265  71.918  1.00 10.60           C  
ANISOU 3362  CA  TRP A 469     1162   1389   1475      1     98    222       C  
ATOM   3363  C   TRP A 469     -38.175   7.888  72.589  1.00 13.64           C  
ANISOU 3363  C   TRP A 469     1548   1766   1869     -5    100    219       C  
ATOM   3364  O   TRP A 469     -37.422   6.988  72.215  1.00 12.80           O  
ANISOU 3364  O   TRP A 469     1446   1649   1770     -7    106    215       O  
ATOM   3365  CB  TRP A 469     -37.202  10.230  72.722  1.00  8.96           C  
ANISOU 3365  CB  TRP A 469      955   1177   1274      8     97    230       C  
ATOM   3366  CG  TRP A 469     -35.773   9.768  72.859  1.00  9.53           C  
ANISOU 3366  CG  TRP A 469     1027   1238   1358      9    101    232       C  
ATOM   3367  CD1 TRP A 469     -35.049   9.060  71.942  1.00 12.40           C  
ANISOU 3367  CD1 TRP A 469     1391   1595   1726      9    110    226       C  
ATOM   3368  CD2 TRP A 469     -34.844  10.166  73.882  1.00  9.11           C  
ANISOU 3368  CD2 TRP A 469      971   1178   1314     12     98    239       C  
ATOM   3369  NE1 TRP A 469     -33.748   8.915  72.376  1.00 11.70           N  
ANISOU 3369  NE1 TRP A 469     1298   1496   1652     13    113    231       N  
ATOM   3370  CE2 TRP A 469     -33.597   9.582  73.567  1.00 12.61           C  
ANISOU 3370  CE2 TRP A 469     1410   1611   1769     14    103    239       C  
ATOM   3371  CE3 TRP A 469     -34.952  10.940  75.053  1.00  9.81           C  
ANISOU 3371  CE3 TRP A 469     1061   1267   1401     13     90    245       C  
ATOM   3372  CZ2 TRP A 469     -32.472   9.727  74.391  1.00 11.42           C  
ANISOU 3372  CZ2 TRP A 469     1255   1453   1632     17     98    246       C  
ATOM   3373  CZ3 TRP A 469     -33.832  11.095  75.860  1.00 10.62           C  
ANISOU 3373  CZ3 TRP A 469     1161   1362   1513     14     85    251       C  
ATOM   3374  CH2 TRP A 469     -32.614  10.491  75.532  1.00 11.06           C  
ANISOU 3374  CH2 TRP A 469     1211   1410   1583     16     88    252       C  
ATOM   3375  N   ASN A 470     -39.132   7.704  73.539  1.00 10.69           N  
ANISOU 3375  N   ASN A 470     1171   1396   1495    -10     97    222       N  
ATOM   3376  CA  ASN A 470     -39.329   6.416  74.226  1.00  9.51           C  
ANISOU 3376  CA  ASN A 470     1024   1238   1352    -17     99    222       C  
ATOM   3377  C   ASN A 470     -39.732   5.315  73.246  1.00 13.58           C  
ANISOU 3377  C   ASN A 470     1541   1750   1868    -26    101    211       C  
ATOM   3378  O   ASN A 470     -39.153   4.236  73.275  1.00 14.19           O  
ANISOU 3378  O   ASN A 470     1624   1813   1954    -29    106    209       O  
ATOM   3379  CB  ASN A 470     -40.380   6.546  75.338  1.00  7.06           C  
ANISOU 3379  CB  ASN A 470      709    934   1039    -21     97    226       C  
ATOM   3380  CG  ASN A 470     -39.893   7.278  76.572  1.00 19.07           C  
ANISOU 3380  CG  ASN A 470     2232   2453   2559    -15     96    235       C  
ATOM   3381  OD1 ASN A 470     -38.694   7.367  76.846  1.00  9.53           O  
ANISOU 3381  OD1 ASN A 470     1029   1237   1356    -10     94    240       O  
ATOM   3382  ND2 ASN A 470     -40.818   7.764  77.366  1.00 12.23           N  
ANISOU 3382  ND2 ASN A 470     1364   1597   1687    -16     97    237       N  
ATOM   3383  N   ASP A 471     -40.740   5.591  72.367  1.00  9.54           N  
ANISOU 3383  N   ASP A 471     1026   1252   1347    -31     97    205       N  
ATOM   3384  CA  ASP A 471     -41.219   4.596  71.390  1.00  9.37           C  
ANISOU 3384  CA  ASP A 471     1009   1229   1323    -42     97    193       C  
ATOM   3385  C   ASP A 471     -40.195   4.345  70.278  1.00 12.70           C  
ANISOU 3385  C   ASP A 471     1440   1642   1742    -39    103    185       C  
ATOM   3386  O   ASP A 471     -40.182   3.262  69.689  1.00 12.80           O  
ANISOU 3386  O   ASP A 471     1460   1647   1757    -48    107    174       O  
ATOM   3387  CB  ASP A 471     -42.580   5.016  70.794  1.00 11.46           C  
ANISOU 3387  CB  ASP A 471     1265   1512   1578    -49     88    190       C  
ATOM   3388  CG  ASP A 471     -43.746   4.926  71.780  1.00 16.71           C  
ANISOU 3388  CG  ASP A 471     1917   2184   2248    -55     86    194       C  
ATOM   3389  OD1 ASP A 471     -43.656   4.120  72.733  1.00 15.64           O  
ANISOU 3389  OD1 ASP A 471     1784   2037   2121    -61     92    198       O  
ATOM   3390  OD2 ASP A 471     -44.775   5.595  71.543  1.00 19.31           O  
ANISOU 3390  OD2 ASP A 471     2235   2529   2572    -55     79    195       O  
ATOM   3391  N   LYS A 472     -39.331   5.347  69.987  1.00  9.43           N  
ANISOU 3391  N   LYS A 472     1027   1232   1325    -28    105    190       N  
ATOM   3392  CA  LYS A 472     -38.267   5.189  68.989  1.00  9.44           C  
ANISOU 3392  CA  LYS A 472     1037   1226   1325    -25    115    183       C  
ATOM   3393  C   LYS A 472     -37.162   4.257  69.524  1.00 14.60           C  
ANISOU 3393  C   LYS A 472     1691   1859   1995    -20    125    183       C  
ATOM   3394  O   LYS A 472     -36.589   3.479  68.764  1.00 15.02           O  
ANISOU 3394  O   LYS A 472     1753   1903   2052    -21    135    173       O  
ATOM   3395  CB  LYS A 472     -37.681   6.564  68.585  1.00 10.56           C  
ANISOU 3395  CB  LYS A 472     1178   1376   1460    -15    116    190       C  
ATOM   3396  CG  LYS A 472     -36.590   6.482  67.488  1.00 15.68           C  
ANISOU 3396  CG  LYS A 472     1833   2019   2104    -13    129    184       C  
ATOM   3397  CD  LYS A 472     -37.117   5.821  66.211  1.00 15.43           C  
ANISOU 3397  CD  LYS A 472     1814   1992   2057    -22    131    169       C  
ATOM   3398  CE  LYS A 472     -36.077   5.749  65.136  1.00 15.03           C  
ANISOU 3398  CE  LYS A 472     1773   1937   2001    -19    147    162       C  
ATOM   3399  NZ  LYS A 472     -36.576   5.008  63.943  1.00 20.94           N  
ANISOU 3399  NZ  LYS A 472     2537   2688   2732    -30    149    146       N  
ATOM   3400  N   ARG A 473     -36.903   4.309  70.833  1.00 10.67           N  
ANISOU 3400  N   ARG A 473     1187   1356   1509    -16    121    194       N  
ATOM   3401  CA  ARG A 473     -35.939   3.415  71.468  1.00 10.65           C  
ANISOU 3401  CA  ARG A 473     1185   1335   1525    -12    126    198       C  
ATOM   3402  C   ARG A 473     -36.545   2.040  71.695  1.00 13.99           C  
ANISOU 3402  C   ARG A 473     1614   1746   1955    -21    127    193       C  
ATOM   3403  O   ARG A 473     -35.837   1.041  71.637  1.00 13.93           O  
ANISOU 3403  O   ARG A 473     1612   1721   1962    -18    134    189       O  
ATOM   3404  CB  ARG A 473     -35.457   4.001  72.804  1.00 11.34           C  
ANISOU 3404  CB  ARG A 473     1266   1422   1620     -5    119    213       C  
ATOM   3405  CG  ARG A 473     -34.409   5.068  72.655  1.00 14.66           C  
ANISOU 3405  CG  ARG A 473     1681   1846   2043      4    120    218       C  
ATOM   3406  CD  ARG A 473     -34.063   5.676  73.979  1.00 15.55           C  
ANISOU 3406  CD  ARG A 473     1790   1960   2161      7    110    231       C  
ATOM   3407  NE  ARG A 473     -35.139   6.532  74.491  1.00 18.42           N  
ANISOU 3407  NE  ARG A 473     2154   2336   2510      3    103    233       N  
ATOM   3408  CZ  ARG A 473     -35.093   7.149  75.667  1.00 26.62           C  
ANISOU 3408  CZ  ARG A 473     3192   3377   3547      5     95    242       C  
ATOM   3409  NH1 ARG A 473     -34.038   7.008  76.456  1.00 14.93           N  
ANISOU 3409  NH1 ARG A 473     1710   1888   2077      8     90    250       N  
ATOM   3410  NH2 ARG A 473     -36.104   7.907  76.063  1.00 17.71           N  
ANISOU 3410  NH2 ARG A 473     2064   2258   2405      2     92    242       N  
ATOM   3411  N   ARG A 474     -37.851   1.987  71.992  1.00  9.78           N  
ANISOU 3411  N   ARG A 474     1080   1222   1413    -32    120    192       N  
ATOM   3412  CA  ARG A 474     -38.520   0.739  72.340  1.00  9.36           C  
ANISOU 3412  CA  ARG A 474     1031   1157   1366    -43    121    190       C  
ATOM   3413  C   ARG A 474     -38.847  -0.121  71.093  1.00 12.52           C  
ANISOU 3413  C   ARG A 474     1440   1552   1763    -53    126    172       C  
ATOM   3414  O   ARG A 474     -38.708  -1.338  71.142  1.00 12.28           O  
ANISOU 3414  O   ARG A 474     1419   1502   1745    -58    131    166       O  
ATOM   3415  CB  ARG A 474     -39.789   1.026  73.158  1.00  9.29           C  
ANISOU 3415  CB  ARG A 474     1017   1162   1351    -52    114    196       C  
ATOM   3416  CG  ARG A 474     -40.486  -0.225  73.688  1.00 13.93           C  
ANISOU 3416  CG  ARG A 474     1609   1738   1947    -66    115    197       C  
ATOM   3417  CD  ARG A 474     -41.654   0.130  74.597  1.00 14.12           C  
ANISOU 3417  CD  ARG A 474     1624   1775   1966    -75    112    205       C  
ATOM   3418  NE  ARG A 474     -42.619   1.019  73.937  1.00 19.23           N  
ANISOU 3418  NE  ARG A 474     2260   2445   2601    -78    107    199       N  
ATOM   3419  CZ  ARG A 474     -43.682   0.589  73.266  1.00 28.96           C  
ANISOU 3419  CZ  ARG A 474     3489   3684   3832    -92    103    189       C  
ATOM   3420  NH1 ARG A 474     -43.945  -0.708  73.189  1.00 10.61           N  
ANISOU 3420  NH1 ARG A 474     1171   1345   1515   -107    106    183       N  
ATOM   3421  NH2 ARG A 474     -44.498   1.455  72.681  1.00 19.48           N  
ANISOU 3421  NH2 ARG A 474     2277   2505   2622    -92     96    186       N  
ATOM   3422  N   LEU A 475     -39.280   0.516  69.992  1.00  9.66           N  
ANISOU 3422  N   LEU A 475     1079   1206   1385    -56    123    162       N  
ATOM   3423  CA  LEU A 475     -39.734  -0.218  68.801  1.00 10.60           C  
ANISOU 3423  CA  LEU A 475     1208   1323   1496    -68    125    144       C  
ATOM   3424  C   LEU A 475     -38.989   0.210  67.514  1.00 14.87           C  
ANISOU 3424  C   LEU A 475     1757   1868   2025    -61    132    134       C  
ATOM   3425  O   LEU A 475     -39.247  -0.351  66.442  1.00 14.35           O  
ANISOU 3425  O   LEU A 475     1704   1801   1949    -71    134    117       O  
ATOM   3426  CB  LEU A 475     -41.261  -0.029  68.611  1.00 10.82           C  
ANISOU 3426  CB  LEU A 475     1229   1368   1512    -83    112    141       C  
ATOM   3427  CG  LEU A 475     -42.151  -0.433  69.808  1.00 16.00           C  
ANISOU 3427  CG  LEU A 475     1876   2023   2179    -92    107    150       C  
ATOM   3428  CD1 LEU A 475     -43.572   0.037  69.607  1.00 16.25           C  
ANISOU 3428  CD1 LEU A 475     1896   2078   2202   -104     95    150       C  
ATOM   3429  CD2 LEU A 475     -42.118  -1.940  70.038  1.00 18.42           C  
ANISOU 3429  CD2 LEU A 475     2193   2307   2500   -104    113    144       C  
ATOM   3430  N   ASN A 476     -38.083   1.224  67.617  1.00 11.65           N  
ANISOU 3430  N   ASN A 476     1344   1466   1617    -47    136    144       N  
ATOM   3431  CA  ASN A 476     -37.427   1.844  66.437  1.00 11.26           C  
ANISOU 3431  CA  ASN A 476     1301   1423   1555    -41    144    138       C  
ATOM   3432  C   ASN A 476     -38.495   2.467  65.501  1.00 15.41           C  
ANISOU 3432  C   ASN A 476     1831   1970   2056    -51    132    133       C  
ATOM   3433  O   ASN A 476     -38.268   2.613  64.295  1.00 16.47           O  
ANISOU 3433  O   ASN A 476     1977   2109   2173    -53    137    123       O  
ATOM   3434  CB  ASN A 476     -36.538   0.819  65.675  1.00  8.45           C  
ANISOU 3434  CB  ASN A 476      958   1049   1204    -40    162    122       C  
ATOM   3435  CG  ASN A 476     -35.611   1.460  64.655  1.00 23.60           C  
ANISOU 3435  CG  ASN A 476     2882   2973   3112    -32    175    118       C  
ATOM   3436  OD1 ASN A 476     -35.153   2.600  64.818  1.00 20.59           O  
ANISOU 3436  OD1 ASN A 476     2492   2602   2729    -24    174    131       O  
ATOM   3437  ND2 ASN A 476     -35.291   0.728  63.602  1.00 10.99           N  
ANISOU 3437  ND2 ASN A 476     1300   1368   1508    -35    190    100       N  
ATOM   3438  N   LEU A 477     -39.646   2.848  66.076  1.00  9.73           N  
ANISOU 3438  N   LEU A 477     1101   1263   1334    -56    116    141       N  
ATOM   3439  CA  LEU A 477     -40.743   3.410  65.316  1.00  8.83           C  
ANISOU 3439  CA  LEU A 477      986   1169   1201    -64    102    139       C  
ATOM   3440  C   LEU A 477     -41.070   4.837  65.788  1.00 11.93           C  
ANISOU 3440  C   LEU A 477     1365   1576   1591    -54     92    155       C  
ATOM   3441  O   LEU A 477     -40.928   5.148  66.969  1.00 10.67           O  
ANISOU 3441  O   LEU A 477     1196   1413   1445    -47     94    166       O  
ATOM   3442  CB  LEU A 477     -41.990   2.509  65.426  1.00  8.42           C  
ANISOU 3442  CB  LEU A 477      931   1119   1151    -81     91    131       C  
ATOM   3443  CG  LEU A 477     -41.905   1.157  64.729  1.00 12.40           C  
ANISOU 3443  CG  LEU A 477     1451   1609   1653    -94     97    111       C  
ATOM   3444  CD1 LEU A 477     -43.125   0.319  65.033  1.00 12.79           C  
ANISOU 3444  CD1 LEU A 477     1494   1658   1708   -113     86    106       C  
ATOM   3445  CD2 LEU A 477     -41.755   1.323  63.240  1.00 15.04           C  
ANISOU 3445  CD2 LEU A 477     1801   1951   1963    -98     97     99       C  
ATOM   3446  N   PRO A 478     -41.538   5.721  64.876  1.00  9.38           N  
ANISOU 3446  N   PRO A 478     1045   1270   1250    -54     82    158       N  
ATOM   3447  CA  PRO A 478     -41.742   5.498  63.438  1.00  9.43           C  
ANISOU 3447  CA  PRO A 478     1065   1284   1234    -63     78    146       C  
ATOM   3448  C   PRO A 478     -40.429   5.553  62.666  1.00 15.12           C  
ANISOU 3448  C   PRO A 478     1802   1997   1946    -57     96    142       C  
ATOM   3449  O   PRO A 478     -39.359   5.747  63.267  1.00 14.56           O  
ANISOU 3449  O   PRO A 478     1728   1915   1890    -47    110    148       O  
ATOM   3450  CB  PRO A 478     -42.683   6.644  63.056  1.00 11.19           C  
ANISOU 3450  CB  PRO A 478     1281   1527   1443    -60     60    157       C  
ATOM   3451  CG  PRO A 478     -42.270   7.764  63.959  1.00 15.12           C  
ANISOU 3451  CG  PRO A 478     1769   2024   1954    -45     63    174       C  
ATOM   3452  CD  PRO A 478     -41.868   7.109  65.262  1.00 10.58           C  
ANISOU 3452  CD  PRO A 478     1185   1433   1401    -43     74    173       C  
ATOM   3453  N   ARG A 479     -40.493   5.370  61.340  1.00 12.68           N  
ANISOU 3453  N   ARG A 479     1510   1694   1613    -66     95    131       N  
ATOM   3454  CA  ARG A 479     -39.318   5.506  60.496  1.00 11.91           C  
ANISOU 3454  CA  ARG A 479     1429   1592   1505    -61    114    126       C  
ATOM   3455  C   ARG A 479     -38.772   6.927  60.599  1.00 15.19           C  
ANISOU 3455  C   ARG A 479     1838   2013   1919    -49    117    145       C  
ATOM   3456  O   ARG A 479     -39.528   7.887  60.457  1.00 14.01           O  
ANISOU 3456  O   ARG A 479     1685   1878   1759    -47    100    157       O  
ATOM   3457  CB  ARG A 479     -39.661   5.178  59.033  1.00 11.80           C  
ANISOU 3457  CB  ARG A 479     1437   1588   1460    -74    111    112       C  
ATOM   3458  CG  ARG A 479     -38.442   5.192  58.112  1.00 17.72           C  
ANISOU 3458  CG  ARG A 479     2205   2331   2196    -71    136    105       C  
ATOM   3459  CD  ARG A 479     -38.779   5.719  56.730  1.00 16.27           C  
ANISOU 3459  CD  ARG A 479     2041   2165   1974    -78    128    103       C  
ATOM   3460  NE  ARG A 479     -37.574   5.916  55.918  1.00 15.98           N  
ANISOU 3460  NE  ARG A 479     2021   2125   1925    -75    155    100       N  
ATOM   3461  CZ  ARG A 479     -36.819   7.009  55.972  1.00 27.21           C  
ANISOU 3461  CZ  ARG A 479     3440   3550   3350    -64    165    118       C  
ATOM   3462  NH1 ARG A 479     -37.132   7.999  56.800  1.00 12.53           N  
ANISOU 3462  NH1 ARG A 479     1561   1694   1504    -56    150    139       N  
ATOM   3463  NH2 ARG A 479     -35.734   7.112  55.214  1.00 11.39           N  
ANISOU 3463  NH2 ARG A 479     1450   1543   1335    -62    192    114       N  
ATOM   3464  N   LEU A 480     -37.491   7.061  60.928  1.00 12.43           N  
ANISOU 3464  N   LEU A 480     1487   1651   1584    -39    137    148       N  
ATOM   3465  CA  LEU A 480     -36.826   8.360  60.953  1.00 12.74           C  
ANISOU 3465  CA  LEU A 480     1524   1695   1623    -30    141    165       C  
ATOM   3466  C   LEU A 480     -35.547   8.291  60.147  1.00 16.18           C  
ANISOU 3466  C   LEU A 480     1971   2124   2054    -28    166    160       C  
ATOM   3467  O   LEU A 480     -34.933   7.226  60.060  1.00 15.22           O  
ANISOU 3467  O   LEU A 480     1852   1990   1940    -29    183    145       O  
ATOM   3468  CB  LEU A 480     -36.510   8.795  62.414  1.00 12.94           C  
ANISOU 3468  CB  LEU A 480     1530   1712   1676    -20    139    177       C  
ATOM   3469  CG  LEU A 480     -37.722   8.979  63.362  1.00 17.83           C  
ANISOU 3469  CG  LEU A 480     2136   2336   2302    -20    119    183       C  
ATOM   3470  CD1 LEU A 480     -37.265   9.336  64.758  1.00 17.72           C  
ANISOU 3470  CD1 LEU A 480     2108   2313   2311    -12    120    193       C  
ATOM   3471  CD2 LEU A 480     -38.671  10.045  62.842  1.00 20.23           C  
ANISOU 3471  CD2 LEU A 480     2441   2655   2588    -19    102    193       C  
ATOM   3472  N   ASP A 481     -35.144   9.415  59.533  1.00 14.04           N  
ANISOU 3472  N   ASP A 481     1706   1861   1770    -26    171    172       N  
ATOM   3473  CA  ASP A 481     -33.865   9.483  58.826  1.00 13.84           C  
ANISOU 3473  CA  ASP A 481     1688   1830   1740    -25    198    169       C  
ATOM   3474  C   ASP A 481     -32.735   9.414  59.819  1.00 16.68           C  
ANISOU 3474  C   ASP A 481     2029   2176   2134    -16    212    173       C  
ATOM   3475  O   ASP A 481     -32.835   9.991  60.911  1.00 15.27           O  
ANISOU 3475  O   ASP A 481     1835   1994   1973    -10    199    186       O  
ATOM   3476  CB  ASP A 481     -33.756  10.789  58.014  1.00 15.55           C  
ANISOU 3476  CB  ASP A 481     1915   2057   1935    -26    199    184       C  
ATOM   3477  CG  ASP A 481     -34.698  10.875  56.834  1.00 23.89           C  
ANISOU 3477  CG  ASP A 481     2994   3129   2955    -35    186    182       C  
ATOM   3478  OD1 ASP A 481     -35.262   9.828  56.446  1.00 24.19           O  
ANISOU 3478  OD1 ASP A 481     3041   3169   2982    -42    182    164       O  
ATOM   3479  OD2 ASP A 481     -34.794  11.965  56.234  1.00 27.83           O  
ANISOU 3479  OD2 ASP A 481     3502   3637   3436    -35    182    197       O  
ATOM   3480  N   VAL A 482     -31.656   8.715  59.466  1.00 13.48           N  
ANISOU 3480  N   VAL A 482     1625   1761   1737    -14    237    162       N  
ATOM   3481  CA  VAL A 482     -30.460   8.693  60.297  1.00 12.69           C  
ANISOU 3481  CA  VAL A 482     1504   1647   1669     -5    250    168       C  
ATOM   3482  C   VAL A 482     -29.750  10.046  60.175  1.00 15.60           C  
ANISOU 3482  C   VAL A 482     1868   2022   2039     -4    257    185       C  
ATOM   3483  O   VAL A 482     -29.731  10.630  59.087  1.00 14.27           O  
ANISOU 3483  O   VAL A 482     1715   1861   1845    -10    266    187       O  
ATOM   3484  CB  VAL A 482     -29.521   7.505  59.920  1.00 16.58           C  
ANISOU 3484  CB  VAL A 482     1997   2128   2174     -1    277    151       C  
ATOM   3485  CG1 VAL A 482     -28.201   7.583  60.685  1.00 16.40           C  
ANISOU 3485  CG1 VAL A 482     1951   2094   2187      8    290    159       C  
ATOM   3486  CG2 VAL A 482     -30.211   6.165  60.169  1.00 16.36           C  
ANISOU 3486  CG2 VAL A 482     1975   2092   2150     -3    270    135       C  
ATOM   3487  N   ALA A 483     -29.269  10.604  61.315  1.00 12.72           N  
ANISOU 3487  N   ALA A 483     1483   1650   1700      1    249    197       N  
ATOM   3488  CA  ALA A 483     -28.587  11.905  61.316  1.00 12.59           C  
ANISOU 3488  CA  ALA A 483     1461   1636   1688      0    254    213       C  
ATOM   3489  C   ALA A 483     -27.396  11.900  60.359  1.00 17.03           C  
ANISOU 3489  C   ALA A 483     2023   2196   2250     -2    285    211       C  
ATOM   3490  O   ALA A 483     -26.685  10.897  60.266  1.00 16.75           O  
ANISOU 3490  O   ALA A 483     1981   2154   2229      3    303    199       O  
ATOM   3491  CB  ALA A 483     -28.129  12.256  62.721  1.00 13.10           C  
ANISOU 3491  CB  ALA A 483     1504   1692   1782      5    242    223       C  
ATOM   3492  N   VAL A 484     -27.208  13.009  59.602  1.00 13.56           N  
ANISOU 3492  N   VAL A 484     1594   1764   1794     -8    293    222       N  
ATOM   3493  CA  VAL A 484     -26.106  13.126  58.630  1.00 13.24           C  
ANISOU 3493  CA  VAL A 484     1555   1724   1750    -12    326    222       C  
ATOM   3494  C   VAL A 484     -24.753  12.909  59.317  1.00 16.32           C  
ANISOU 3494  C   VAL A 484     1917   2104   2180     -7    341    222       C  
ATOM   3495  O   VAL A 484     -23.953  12.088  58.860  1.00 15.49           O  
ANISOU 3495  O   VAL A 484     1806   1995   2084     -3    367    211       O  
ATOM   3496  CB  VAL A 484     -26.156  14.481  57.869  1.00 16.88           C  
ANISOU 3496  CB  VAL A 484     2031   2192   2190    -20    329    238       C  
ATOM   3497  CG1 VAL A 484     -25.011  14.588  56.861  1.00 16.99           C  
ANISOU 3497  CG1 VAL A 484     2047   2208   2199    -26    366    238       C  
ATOM   3498  CG2 VAL A 484     -27.502  14.668  57.179  1.00 16.64           C  
ANISOU 3498  CG2 VAL A 484     2028   2173   2122    -24    310    239       C  
ATOM   3499  N   TYR A 485     -24.528  13.592  60.449  1.00 12.89           N  
ANISOU 3499  N   TYR A 485     1464   1665   1770     -6    323    235       N  
ATOM   3500  CA  TYR A 485     -23.318  13.410  61.237  1.00 13.14           C  
ANISOU 3500  CA  TYR A 485     1466   1687   1839     -2    330    238       C  
ATOM   3501  C   TYR A 485     -23.647  13.113  62.693  1.00 15.62           C  
ANISOU 3501  C   TYR A 485     1766   1995   2173      4    301    239       C  
ATOM   3502  O   TYR A 485     -24.502  13.775  63.285  1.00 13.84           O  
ANISOU 3502  O   TYR A 485     1548   1771   1938      2    276    246       O  
ATOM   3503  CB  TYR A 485     -22.390  14.639  61.128  1.00 15.51           C  
ANISOU 3503  CB  TYR A 485     1755   1987   2150    -10    340    253       C  
ATOM   3504  CG  TYR A 485     -21.189  14.564  62.053  1.00 18.87           C  
ANISOU 3504  CG  TYR A 485     2148   2405   2617     -8    341    257       C  
ATOM   3505  CD1 TYR A 485     -20.084  13.779  61.731  1.00 21.31           C  
ANISOU 3505  CD1 TYR A 485     2437   2712   2949     -3    368    250       C  
ATOM   3506  CD2 TYR A 485     -21.194  15.208  63.288  1.00 19.70           C  
ANISOU 3506  CD2 TYR A 485     2240   2505   2739    -10    313    267       C  
ATOM   3507  CE1 TYR A 485     -19.013  13.642  62.611  1.00 22.84           C  
ANISOU 3507  CE1 TYR A 485     2597   2899   3182      1    365    255       C  
ATOM   3508  CE2 TYR A 485     -20.129  15.076  64.178  1.00 20.89           C  
ANISOU 3508  CE2 TYR A 485     2361   2651   2927     -8    309    271       C  
ATOM   3509  CZ  TYR A 485     -19.035  14.300  63.832  1.00 31.06           C  
ANISOU 3509  CZ  TYR A 485     3626   3936   4238     -3    334    266       C  
ATOM   3510  OH  TYR A 485     -17.970  14.188  64.697  1.00 34.80           O  
ANISOU 3510  OH  TYR A 485     4068   4405   4750     -1    327    271       O  
ATOM   3511  N   ARG A 486     -22.959  12.128  63.277  1.00 12.43           N  
ANISOU 3511  N   ARG A 486     1343   1583   1796     13    304    233       N  
ATOM   3512  CA  ARG A 486     -23.111  11.785  64.689  1.00 12.05           C  
ANISOU 3512  CA  ARG A 486     1282   1528   1768     18    278    236       C  
ATOM   3513  C   ARG A 486     -21.737  11.675  65.348  1.00 15.63           C  
ANISOU 3513  C   ARG A 486     1705   1975   2259     22    282    242       C  
ATOM   3514  O   ARG A 486     -20.748  11.382  64.664  1.00 15.09           O  
ANISOU 3514  O   ARG A 486     1623   1904   2204     25    309    239       O  
ATOM   3515  CB  ARG A 486     -23.884  10.463  64.848  1.00 10.97           C  
ANISOU 3515  CB  ARG A 486     1155   1387   1626     26    272    223       C  
ATOM   3516  CG  ARG A 486     -25.341  10.544  64.406  1.00 12.78           C  
ANISOU 3516  CG  ARG A 486     1410   1624   1821     21    262    218       C  
ATOM   3517  CD  ARG A 486     -25.882   9.174  64.060  1.00 20.87           C  
ANISOU 3517  CD  ARG A 486     2445   2644   2839     25    267    202       C  
ATOM   3518  NE  ARG A 486     -25.231   8.625  62.868  1.00 21.36           N  
ANISOU 3518  NE  ARG A 486     2512   2705   2898     26    298    190       N  
ATOM   3519  CZ  ARG A 486     -25.230   7.335  62.552  1.00 29.89           C  
ANISOU 3519  CZ  ARG A 486     3599   3777   3982     31    310    175       C  
ATOM   3520  NH1 ARG A 486     -25.808   6.447  63.352  1.00 12.19           N  
ANISOU 3520  NH1 ARG A 486     1357   1527   1749     35    293    171       N  
ATOM   3521  NH2 ARG A 486     -24.618   6.917  61.453  1.00 13.16           N  
ANISOU 3521  NH2 ARG A 486     1486   1656   1859     33    340    162       N  
ATOM   3522  N   ASP A 487     -21.670  11.914  66.681  1.00 12.62           N  
ANISOU 3522  N   ASP A 487     1311   1590   1894     22    255    251       N  
ATOM   3523  CA  ASP A 487     -20.415  11.844  67.454  1.00 12.80           C  
ANISOU 3523  CA  ASP A 487     1303   1606   1952     25    251    258       C  
ATOM   3524  C   ASP A 487     -19.533  10.664  66.970  1.00 17.81           C  
ANISOU 3524  C   ASP A 487     1922   2236   2611     37    275    251       C  
ATOM   3525  O   ASP A 487     -19.847   9.506  67.248  1.00 17.92           O  
ANISOU 3525  O   ASP A 487     1939   2242   2629     48    271    244       O  
ATOM   3526  CB  ASP A 487     -20.730  11.711  68.970  1.00 14.24           C  
ANISOU 3526  CB  ASP A 487     1483   1786   2143     27    217    264       C  
ATOM   3527  CG  ASP A 487     -19.513  11.836  69.886  1.00 18.00           C  
ANISOU 3527  CG  ASP A 487     1929   2257   2652     27    205    274       C  
ATOM   3528  OD1 ASP A 487     -18.386  11.953  69.364  1.00 16.29           O  
ANISOU 3528  OD1 ASP A 487     1690   2041   2458     27    223    277       O  
ATOM   3529  OD2 ASP A 487     -19.700  11.838  71.122  1.00 23.52           O  
ANISOU 3529  OD2 ASP A 487     2627   2955   3356     27    176    280       O  
ATOM   3530  N   GLN A 488     -18.455  10.970  66.200  1.00 14.03           N  
ANISOU 3530  N   GLN A 488     1426   1758   2146     35    302    252       N  
ATOM   3531  CA  GLN A 488     -17.589   9.935  65.597  1.00 14.06           C  
ANISOU 3531  CA  GLN A 488     1414   1756   2173     48    331    243       C  
ATOM   3532  C   GLN A 488     -16.833   9.091  66.647  1.00 19.23           C  
ANISOU 3532  C   GLN A 488     2040   2401   2866     61    316    248       C  
ATOM   3533  O   GLN A 488     -16.368   7.989  66.333  1.00 18.72           O  
ANISOU 3533  O   GLN A 488     1965   2327   2820     75    335    239       O  
ATOM   3534  CB  GLN A 488     -16.614  10.552  64.569  1.00 15.27           C  
ANISOU 3534  CB  GLN A 488     1554   1915   2333     41    365    244       C  
ATOM   3535  CG  GLN A 488     -15.701  11.632  65.141  1.00 26.52           C  
ANISOU 3535  CG  GLN A 488     2952   3342   3781     31    355    260       C  
ATOM   3536  CD  GLN A 488     -14.772  12.191  64.082  1.00 48.98           C  
ANISOU 3536  CD  GLN A 488     5784   6192   6633     23    391    262       C  
ATOM   3537  OE1 GLN A 488     -14.081  11.450  63.366  1.00 47.85           O  
ANISOU 3537  OE1 GLN A 488     5626   6047   6506     33    424    253       O  
ATOM   3538  NE2 GLN A 488     -14.697  13.512  63.997  1.00 36.97           N  
ANISOU 3538  NE2 GLN A 488     4267   4677   5103      5    388    273       N  
ATOM   3539  N   ALA A 489     -16.747   9.589  67.896  1.00 16.46           N  
ANISOU 3539  N   ALA A 489     1678   2050   2527     56    282    261       N  
ATOM   3540  CA  ALA A 489     -16.138   8.834  68.992  1.00 16.53           C  
ANISOU 3540  CA  ALA A 489     1662   2050   2567     68    262    268       C  
ATOM   3541  C   ALA A 489     -17.110   7.768  69.507  1.00 20.30           C  
ANISOU 3541  C   ALA A 489     2161   2519   3033     77    247    263       C  
ATOM   3542  O   ALA A 489     -16.718   6.894  70.285  1.00 20.09           O  
ANISOU 3542  O   ALA A 489     2120   2484   3031     89    233    268       O  
ATOM   3543  CB  ALA A 489     -15.752   9.777  70.123  1.00 17.23           C  
ANISOU 3543  CB  ALA A 489     1736   2144   2667     57    230    283       C  
ATOM   3544  N   VAL A 490     -18.386   7.845  69.078  1.00 16.95           N  
ANISOU 3544  N   VAL A 490     1770   2099   2571     71    248    254       N  
ATOM   3545  CA  VAL A 490     -19.429   6.926  69.538  1.00 16.50           C  
ANISOU 3545  CA  VAL A 490     1734   2035   2500     76    234    249       C  
ATOM   3546  C   VAL A 490     -20.082   6.184  68.342  1.00 19.22           C  
ANISOU 3546  C   VAL A 490     2101   2377   2826     79    260    231       C  
ATOM   3547  O   VAL A 490     -20.476   5.020  68.477  1.00 17.80           O  
ANISOU 3547  O   VAL A 490     1929   2185   2648     87    260    225       O  
ATOM   3548  CB  VAL A 490     -20.503   7.680  70.398  1.00 20.57           C  
ANISOU 3548  CB  VAL A 490     2268   2558   2990     64    205    256       C  
ATOM   3549  CG1 VAL A 490     -21.557   6.719  70.928  1.00 20.60           C  
ANISOU 3549  CG1 VAL A 490     2290   2555   2981     68    192    252       C  
ATOM   3550  CG2 VAL A 490     -19.848   8.448  71.545  1.00 20.52           C  
ANISOU 3550  CG2 VAL A 490     2243   2554   2999     60    179    271       C  
ATOM   3551  N   TYR A 491     -20.188   6.859  67.177  1.00 15.44           N  
ANISOU 3551  N   TYR A 491     1632   1907   2326     71    282    224       N  
ATOM   3552  CA  TYR A 491     -20.922   6.319  66.032  1.00 15.21           C  
ANISOU 3552  CA  TYR A 491     1629   1879   2273     70    303    207       C  
ATOM   3553  C   TYR A 491     -20.060   6.139  64.796  1.00 19.61           C  
ANISOU 3553  C   TYR A 491     2181   2435   2836     74    341    197       C  
ATOM   3554  O   TYR A 491     -19.162   6.943  64.538  1.00 18.53           O  
ANISOU 3554  O   TYR A 491     2026   2304   2710     71    354    204       O  
ATOM   3555  CB  TYR A 491     -22.137   7.205  65.701  1.00 15.66           C  
ANISOU 3555  CB  TYR A 491     1711   1949   2290     56    292    207       C  
ATOM   3556  CG  TYR A 491     -23.174   7.241  66.798  1.00 16.98           C  
ANISOU 3556  CG  TYR A 491     1887   2116   2448     53    260    214       C  
ATOM   3557  CD1 TYR A 491     -24.204   6.305  66.842  1.00 18.91           C  
ANISOU 3557  CD1 TYR A 491     2149   2356   2679     53    253    204       C  
ATOM   3558  CD2 TYR A 491     -23.149   8.231  67.777  1.00 17.71           C  
ANISOU 3558  CD2 TYR A 491     1971   2214   2544     47    237    228       C  
ATOM   3559  CE1 TYR A 491     -25.165   6.332  67.852  1.00 19.26           C  
ANISOU 3559  CE1 TYR A 491     2200   2401   2715     50    227    210       C  
ATOM   3560  CE2 TYR A 491     -24.106   8.270  68.791  1.00 18.39           C  
ANISOU 3560  CE2 TYR A 491     2066   2301   2620     45    210    233       C  
ATOM   3561  CZ  TYR A 491     -25.107   7.311  68.832  1.00 25.31           C  
ANISOU 3561  CZ  TYR A 491     2958   3174   3485     46    206    224       C  
ATOM   3562  OH  TYR A 491     -26.050   7.343  69.827  1.00 27.68           O  
ANISOU 3562  OH  TYR A 491     3266   3476   3775     42    184    229       O  
ATOM   3563  N   ASN A 492     -20.406   5.132  63.966  1.00 17.59           N  
ANISOU 3563  N   ASN A 492     1943   2172   2569     79    361    179       N  
ATOM   3564  CA  ASN A 492     -19.814   4.943  62.651  1.00 17.90           C  
ANISOU 3564  CA  ASN A 492     1986   2212   2604     81    401    165       C  
ATOM   3565  C   ASN A 492     -20.707   5.635  61.611  1.00 22.64           C  
ANISOU 3565  C   ASN A 492     2617   2827   3158     65    406    159       C  
ATOM   3566  O   ASN A 492     -21.822   5.178  61.355  1.00 21.69           O  
ANISOU 3566  O   ASN A 492     2524   2708   3012     61    397    148       O  
ATOM   3567  CB  ASN A 492     -19.676   3.434  62.335  1.00 18.62           C  
ANISOU 3567  CB  ASN A 492     2082   2285   2709     95    420    146       C  
ATOM   3568  CG  ASN A 492     -19.088   3.127  60.968  1.00 33.78           C  
ANISOU 3568  CG  ASN A 492     4009   4204   4622     98    464    128       C  
ATOM   3569  OD1 ASN A 492     -18.656   4.018  60.227  1.00 23.24           O  
ANISOU 3569  OD1 ASN A 492     2673   2883   3275     90    483    131       O  
ATOM   3570  ND2 ASN A 492     -19.058   1.853  60.615  1.00 29.60           N  
ANISOU 3570  ND2 ASN A 492     3488   3657   4100    109    481    109       N  
ATOM   3571  N   ASN A 493     -20.246   6.783  61.072  1.00 20.26           N  
ANISOU 3571  N   ASN A 493     2312   2538   2847     56    419    168       N  
ATOM   3572  CA  ASN A 493     -21.047   7.611  60.158  1.00 20.55           C  
ANISOU 3572  CA  ASN A 493     2377   2590   2841     42    420    167       C  
ATOM   3573  C   ASN A 493     -21.398   6.907  58.826  1.00 26.12           C  
ANISOU 3573  C   ASN A 493     3111   3296   3517     40    446    146       C  
ATOM   3574  O   ASN A 493     -22.358   7.300  58.164  1.00 25.98           O  
ANISOU 3574  O   ASN A 493     3121   3290   3460     29    439    144       O  
ATOM   3575  CB  ASN A 493     -20.362   8.955  59.904  1.00 20.70           C  
ANISOU 3575  CB  ASN A 493     2385   2618   2861     33    429    183       C  
ATOM   3576  CG  ASN A 493     -20.422   9.884  61.092  1.00 35.69           C  
ANISOU 3576  CG  ASN A 493     4268   4519   4774     29    397    203       C  
ATOM   3577  OD1 ASN A 493     -21.485  10.396  61.457  1.00 23.30           O  
ANISOU 3577  OD1 ASN A 493     2714   2954   3183     23    370    208       O  
ATOM   3578  ND2 ASN A 493     -19.280  10.133  61.710  1.00 30.47           N  
ANISOU 3578  ND2 ASN A 493     3575   3853   4149     32    399    212       N  
ATOM   3579  N   ASN A 494     -20.643   5.851  58.457  1.00 23.58           N  
ANISOU 3579  N   ASN A 494     2782   2963   3214     51    475    130       N  
ATOM   3580  CA  ASN A 494     -20.936   5.080  57.240  1.00 23.72           C  
ANISOU 3580  CA  ASN A 494     2830   2980   3205     50    502    107       C  
ATOM   3581  C   ASN A 494     -22.180   4.191  57.432  1.00 27.36           C  
ANISOU 3581  C   ASN A 494     3314   3434   3649     48    478     94       C  
ATOM   3582  O   ASN A 494     -22.816   3.797  56.452  1.00 26.80           O  
ANISOU 3582  O   ASN A 494     3273   3366   3543     40    487     76       O  
ATOM   3583  CB  ASN A 494     -19.723   4.233  56.829  1.00 24.55           C  
ANISOU 3583  CB  ASN A 494     2919   3071   3337     64    542     92       C  
ATOM   3584  CG  ASN A 494     -18.523   5.055  56.394  1.00 48.24           C  
ANISOU 3584  CG  ASN A 494     5899   6080   6350     63    573    102       C  
ATOM   3585  OD1 ASN A 494     -18.627   6.255  56.097  1.00 37.35           O  
ANISOU 3585  OD1 ASN A 494     4526   4717   4950     49    569    117       O  
ATOM   3586  ND2 ASN A 494     -17.367   4.411  56.296  1.00 42.63           N  
ANISOU 3586  ND2 ASN A 494     5166   5359   5675     78    605     94       N  
ATOM   3587  N   ASP A 495     -22.549   3.919  58.698  1.00 23.78           N  
ANISOU 3587  N   ASP A 495     2846   2972   3218     53    447    103       N  
ATOM   3588  CA  ASP A 495     -23.720   3.104  59.020  1.00 23.33           C  
ANISOU 3588  CA  ASP A 495     2806   2908   3149     50    423     94       C  
ATOM   3589  C   ASP A 495     -24.978   3.989  59.133  1.00 26.13           C  
ANISOU 3589  C   ASP A 495     3176   3281   3473     35    392    104       C  
ATOM   3590  O   ASP A 495     -25.189   4.635  60.163  1.00 26.14           O  
ANISOU 3590  O   ASP A 495     3161   3285   3484     35    366    122       O  
ATOM   3591  CB  ASP A 495     -23.480   2.316  60.336  1.00 25.09           C  
ANISOU 3591  CB  ASP A 495     3007   3112   3412     63    408     99       C  
ATOM   3592  CG  ASP A 495     -24.572   1.305  60.682  1.00 35.72           C  
ANISOU 3592  CG  ASP A 495     4372   4449   4753     59    389     89       C  
ATOM   3593  OD1 ASP A 495     -25.539   1.176  59.893  1.00 35.92           O  
ANISOU 3593  OD1 ASP A 495     4424   4481   4743     47    387     76       O  
ATOM   3594  OD2 ASP A 495     -24.443   0.630  61.722  1.00 43.31           O  
ANISOU 3594  OD2 ASP A 495     5319   5394   5742     69    376     95       O  
ATOM   3595  N   LYS A 496     -25.788   4.049  58.055  1.00 21.48           N  
ANISOU 3595  N   LYS A 496     2616   2701   2843     23    394     92       N  
ATOM   3596  CA  LYS A 496     -27.018   4.852  58.050  1.00 20.63           C  
ANISOU 3596  CA  LYS A 496     2521   2610   2706     11    365    102       C  
ATOM   3597  C   LYS A 496     -28.266   3.979  57.819  1.00 22.78           C  
ANISOU 3597  C   LYS A 496     2815   2882   2958      2    349     86       C  
ATOM   3598  O   LYS A 496     -29.281   4.469  57.301  1.00 22.92           O  
ANISOU 3598  O   LYS A 496     2850   2915   2943     -9    332     88       O  
ATOM   3599  CB  LYS A 496     -26.933   5.985  56.998  1.00 23.69           C  
ANISOU 3599  CB  LYS A 496     2923   3016   3062      2    375    109       C  
ATOM   3600  CG  LYS A 496     -25.873   7.034  57.321  1.00 38.64           C  
ANISOU 3600  CG  LYS A 496     4794   4911   4975      7    385    129       C  
ATOM   3601  CD  LYS A 496     -26.035   8.281  56.461  1.00 48.99           C  
ANISOU 3601  CD  LYS A 496     6121   6239   6254     -4    387    141       C  
ATOM   3602  CE  LYS A 496     -25.209   9.430  56.982  1.00 57.03           C  
ANISOU 3602  CE  LYS A 496     7117   7259   7294     -2    389    162       C  
ATOM   3603  NZ  LYS A 496     -23.753   9.180  56.843  1.00 63.48           N  
ANISOU 3603  NZ  LYS A 496     7915   8068   8137      4    423    159       N  
ATOM   3604  N   ASP A 497     -28.207   2.693  58.240  1.00 17.28           N  
ANISOU 3604  N   ASP A 497     2117   2167   2283      8    352     72       N  
ATOM   3605  CA  ASP A 497     -29.342   1.775  58.108  1.00 16.04           C  
ANISOU 3605  CA  ASP A 497     1978   2005   2111     -2    337     57       C  
ATOM   3606  C   ASP A 497     -30.481   2.197  59.044  1.00 18.50           C  
ANISOU 3606  C   ASP A 497     2281   2325   2422     -8    301     72       C  
ATOM   3607  O   ASP A 497     -30.311   2.199  60.266  1.00 17.43           O  
ANISOU 3607  O   ASP A 497     2126   2182   2315      0    290     85       O  
ATOM   3608  CB  ASP A 497     -28.904   0.323  58.405  1.00 17.35           C  
ANISOU 3608  CB  ASP A 497     2144   2145   2305      6    352     40       C  
ATOM   3609  CG  ASP A 497     -29.914  -0.737  57.966  1.00 22.70           C  
ANISOU 3609  CG  ASP A 497     2845   2815   2966     -6    345     18       C  
ATOM   3610  OD1 ASP A 497     -31.112  -0.395  57.817  1.00 22.47           O  
ANISOU 3610  OD1 ASP A 497     2826   2801   2911    -21    320     20       O  
ATOM   3611  OD2 ASP A 497     -29.511  -1.902  57.803  1.00 27.33           O  
ANISOU 3611  OD2 ASP A 497     3438   3378   3566     -1    363      0       O  
ATOM   3612  N   ILE A 498     -31.641   2.577  58.463  1.00 13.97           N  
ANISOU 3612  N   ILE A 498     1724   1769   1816    -22    283     70       N  
ATOM   3613  CA  ILE A 498     -32.808   3.041  59.237  1.00 12.98           C  
ANISOU 3613  CA  ILE A 498     1591   1653   1689    -28    250     84       C  
ATOM   3614  C   ILE A 498     -33.414   1.912  60.087  1.00 17.05           C  
ANISOU 3614  C   ILE A 498     2102   2154   2223    -31    239     77       C  
ATOM   3615  O   ILE A 498     -34.128   2.184  61.057  1.00 16.24           O  
ANISOU 3615  O   ILE A 498     1985   2055   2128    -32    217     90       O  
ATOM   3616  CB  ILE A 498     -33.873   3.691  58.305  1.00 15.60           C  
ANISOU 3616  CB  ILE A 498     1939   2007   1983    -41    234     83       C  
ATOM   3617  CG1 ILE A 498     -34.361   2.680  57.222  1.00 15.93           C  
ANISOU 3617  CG1 ILE A 498     2006   2047   2000    -54    238     58       C  
ATOM   3618  CG2 ILE A 498     -33.327   4.984  57.669  1.00 16.25           C  
ANISOU 3618  CG2 ILE A 498     2024   2103   2048    -37    242     97       C  
ATOM   3619  CD1 ILE A 498     -35.686   3.043  56.573  1.00 22.93           C  
ANISOU 3619  CD1 ILE A 498     2905   2954   2854    -69    211     58       C  
ATOM   3620  N   LEU A 499     -33.125   0.648  59.725  1.00 13.76           N  
ANISOU 3620  N   LEU A 499     1697   1720   1813    -32    255     57       N  
ATOM   3621  CA  LEU A 499     -33.673  -0.508  60.428  1.00 13.50           C  
ANISOU 3621  CA  LEU A 499     1663   1669   1797    -36    246     50       C  
ATOM   3622  C   LEU A 499     -32.838  -0.865  61.668  1.00 17.78           C  
ANISOU 3622  C   LEU A 499     2186   2193   2378    -21    251     62       C  
ATOM   3623  O   LEU A 499     -33.241  -1.723  62.452  1.00 17.85           O  
ANISOU 3623  O   LEU A 499     2192   2186   2403    -23    242     62       O  
ATOM   3624  CB  LEU A 499     -33.773  -1.721  59.476  1.00 13.89           C  
ANISOU 3624  CB  LEU A 499     1737   1705   1837    -45    260     21       C  
ATOM   3625  CG  LEU A 499     -34.516  -1.471  58.146  1.00 18.59           C  
ANISOU 3625  CG  LEU A 499     2354   2318   2390    -61    254      7       C  
ATOM   3626  CD1 LEU A 499     -34.538  -2.719  57.298  1.00 18.97           C  
ANISOU 3626  CD1 LEU A 499     2429   2350   2430    -71    269    -23       C  
ATOM   3627  CD2 LEU A 499     -35.935  -0.970  58.391  1.00 20.55           C  
ANISOU 3627  CD2 LEU A 499     2598   2586   2624    -75    221     17       C  
ATOM   3628  N   LYS A 500     -31.677  -0.200  61.848  1.00 14.38           N  
ANISOU 3628  N   LYS A 500     1741   1763   1961     -6    264     73       N  
ATOM   3629  CA  LYS A 500     -30.831  -0.422  63.022  1.00 14.10           C  
ANISOU 3629  CA  LYS A 500     1685   1712   1959      8    265     87       C  
ATOM   3630  C   LYS A 500     -31.129   0.616  64.094  1.00 17.49           C  
ANISOU 3630  C   LYS A 500     2099   2156   2393      9    243    110       C  
ATOM   3631  O   LYS A 500     -30.854   1.802  63.901  1.00 16.64           O  
ANISOU 3631  O   LYS A 500     1984   2063   2275     10    242    120       O  
ATOM   3632  CB  LYS A 500     -29.335  -0.396  62.640  1.00 16.50           C  
ANISOU 3632  CB  LYS A 500     1980   2008   2281     23    292     85       C  
ATOM   3633  CG  LYS A 500     -28.921  -1.535  61.714  1.00 28.56           C  
ANISOU 3633  CG  LYS A 500     3523   3517   3810     26    318     61       C  
ATOM   3634  CD  LYS A 500     -27.407  -1.525  61.423  1.00 40.89           C  
ANISOU 3634  CD  LYS A 500     5072   5071   5395     43    347     60       C  
ATOM   3635  CE  LYS A 500     -26.582  -1.939  62.625  1.00 47.03           C  
ANISOU 3635  CE  LYS A 500     5825   5831   6215     60    343     74       C  
ATOM   3636  NZ  LYS A 500     -25.133  -1.979  62.308  1.00 54.08           N  
ANISOU 3636  NZ  LYS A 500     6701   6715   7132     77    372     73       N  
ATOM   3637  N   SER A 501     -31.730   0.178  65.219  1.00 14.61           N  
ANISOU 3637  N   SER A 501     1728   1784   2040      7    225    119       N  
ATOM   3638  CA  SER A 501     -32.103   1.072  66.323  1.00 14.24           C  
ANISOU 3638  CA  SER A 501     1669   1749   1994      7    205    139       C  
ATOM   3639  C   SER A 501     -30.859   1.695  66.995  1.00 17.72           C  
ANISOU 3639  C   SER A 501     2091   2187   2455     20    208    154       C  
ATOM   3640  O   SER A 501     -30.960   2.762  67.614  1.00 16.72           O  
ANISOU 3640  O   SER A 501     1956   2073   2325     20    195    168       O  
ATOM   3641  CB  SER A 501     -32.937   0.319  67.354  1.00 17.53           C  
ANISOU 3641  CB  SER A 501     2085   2157   2418      1    190    143       C  
ATOM   3642  OG  SER A 501     -33.474   1.197  68.326  1.00 29.89           O  
ANISOU 3642  OG  SER A 501     3641   3735   3980     -1    173    159       O  
ATOM   3643  N   ALA A 502     -29.676   1.051  66.826  1.00 15.04           N  
ANISOU 3643  N   ALA A 502     1746   1832   2137     31    225    150       N  
ATOM   3644  CA  ALA A 502     -28.414   1.544  67.395  1.00 14.92           C  
ANISOU 3644  CA  ALA A 502     1710   1814   2144     44    227    164       C  
ATOM   3645  C   ALA A 502     -27.889   2.802  66.647  1.00 18.49           C  
ANISOU 3645  C   ALA A 502     2157   2282   2585     43    237    166       C  
ATOM   3646  O   ALA A 502     -26.955   3.453  67.122  1.00 18.71           O  
ANISOU 3646  O   ALA A 502     2168   2312   2629     49    236    178       O  
ATOM   3647  CB  ALA A 502     -27.363   0.442  67.375  1.00 15.69           C  
ANISOU 3647  CB  ALA A 502     1801   1890   2272     57    243    159       C  
ATOM   3648  N   ASN A 503     -28.520   3.159  65.501  1.00 13.63           N  
ANISOU 3648  N   ASN A 503     1559   1679   1942     34    244    155       N  
ATOM   3649  CA  ASN A 503     -28.155   4.378  64.763  1.00 12.99           C  
ANISOU 3649  CA  ASN A 503     1477   1613   1846     31    252    159       C  
ATOM   3650  C   ASN A 503     -28.829   5.616  65.362  1.00 15.99           C  
ANISOU 3650  C   ASN A 503     1854   2007   2214     26    230    174       C  
ATOM   3651  O   ASN A 503     -28.506   6.743  64.979  1.00 14.94           O  
ANISOU 3651  O   ASN A 503     1719   1884   2073     24    234    181       O  
ATOM   3652  CB  ASN A 503     -28.496   4.237  63.278  1.00 12.81           C  
ANISOU 3652  CB  ASN A 503     1474   1596   1796     24    269    142       C  
ATOM   3653  CG  ASN A 503     -27.496   3.402  62.512  1.00 27.96           C  
ANISOU 3653  CG  ASN A 503     3395   3503   3727     32    299    128       C  
ATOM   3654  OD1 ASN A 503     -26.280   3.484  62.732  1.00 18.19           O  
ANISOU 3654  OD1 ASN A 503     2139   2258   2514     42    313    134       O  
ATOM   3655  ND2 ASN A 503     -27.978   2.646  61.537  1.00 17.74           N  
ANISOU 3655  ND2 ASN A 503     2122   2206   2413     26    310    108       N  
ATOM   3656  N   PHE A 504     -29.710   5.409  66.345  1.00 12.85           N  
ANISOU 3656  N   PHE A 504     1456   1608   1817     23    209    179       N  
ATOM   3657  CA  PHE A 504     -30.422   6.498  67.005  1.00 12.97           C  
ANISOU 3657  CA  PHE A 504     1470   1636   1823     19    190    191       C  
ATOM   3658  C   PHE A 504     -30.071   6.547  68.490  1.00 17.37           C  
ANISOU 3658  C   PHE A 504     2013   2186   2399     24    176    203       C  
ATOM   3659  O   PHE A 504     -29.894   5.497  69.116  1.00 17.48           O  
ANISOU 3659  O   PHE A 504     2024   2188   2429     27    175    202       O  
ATOM   3660  CB  PHE A 504     -31.940   6.347  66.799  1.00 14.99           C  
ANISOU 3660  CB  PHE A 504     1737   1900   2056     11    178    185       C  
ATOM   3661  CG  PHE A 504     -32.349   6.358  65.340  1.00 16.42           C  
ANISOU 3661  CG  PHE A 504     1934   2090   2214      4    186    174       C  
ATOM   3662  CD1 PHE A 504     -32.603   7.556  64.681  1.00 19.22           C  
ANISOU 3662  CD1 PHE A 504     2294   2460   2551      2    184    180       C  
ATOM   3663  CD2 PHE A 504     -32.407   5.174  64.605  1.00 19.04           C  
ANISOU 3663  CD2 PHE A 504     2276   2414   2543      1    198    157       C  
ATOM   3664  CE1 PHE A 504     -32.935   7.570  63.319  1.00 20.55           C  
ANISOU 3664  CE1 PHE A 504     2478   2636   2694     -4    190    171       C  
ATOM   3665  CE2 PHE A 504     -32.735   5.190  63.243  1.00 22.07           C  
ANISOU 3665  CE2 PHE A 504     2677   2807   2901     -6    205    146       C  
ATOM   3666  CZ  PHE A 504     -32.997   6.388  62.610  1.00 20.02           C  
ANISOU 3666  CZ  PHE A 504     2422   2563   2621     -9    201    153       C  
ATOM   3667  N   ILE A 505     -29.882   7.775  69.040  1.00 13.81           N  
ANISOU 3667  N   ILE A 505     1556   1743   1949     24    167    215       N  
ATOM   3668  CA  ILE A 505     -29.445   7.969  70.437  1.00 13.52           C  
ANISOU 3668  CA  ILE A 505     1507   1701   1927     27    153    227       C  
ATOM   3669  C   ILE A 505     -30.281   7.132  71.436  1.00 16.23           C  
ANISOU 3669  C   ILE A 505     1855   2040   2271     25    140    227       C  
ATOM   3670  O   ILE A 505     -31.506   7.051  71.306  1.00 15.93           O  
ANISOU 3670  O   ILE A 505     1828   2009   2217     20    136    223       O  
ATOM   3671  CB  ILE A 505     -29.400   9.485  70.810  1.00 16.66           C  
ANISOU 3671  CB  ILE A 505     1904   2108   2320     24    143    236       C  
ATOM   3672  CG1 ILE A 505     -28.689   9.713  72.171  1.00 17.29           C  
ANISOU 3672  CG1 ILE A 505     1972   2182   2416     26    129    246       C  
ATOM   3673  CG2 ILE A 505     -30.792  10.099  70.790  1.00 17.01           C  
ANISOU 3673  CG2 ILE A 505     1958   2161   2342     20    135    235       C  
ATOM   3674  CD1 ILE A 505     -28.358  11.200  72.485  1.00 23.63           C  
ANISOU 3674  CD1 ILE A 505     2773   2990   3217     22    122    254       C  
ATOM   3675  N   LYS A 506     -29.598   6.446  72.371  1.00 11.47           N  
ANISOU 3675  N   LYS A 506     1245   1426   1687     30    135    234       N  
ATOM   3676  CA  LYS A 506     -30.253   5.546  73.323  1.00 10.98           C  
ANISOU 3676  CA  LYS A 506     1188   1357   1626     28    125    237       C  
ATOM   3677  C   LYS A 506     -30.535   6.246  74.650  1.00 14.70           C  
ANISOU 3677  C   LYS A 506     1659   1835   2092     26    107    248       C  
ATOM   3678  O   LYS A 506     -31.502   5.907  75.329  1.00 14.20           O  
ANISOU 3678  O   LYS A 506     1604   1773   2019     21    101    250       O  
ATOM   3679  CB  LYS A 506     -29.383   4.283  73.565  1.00 13.12           C  
ANISOU 3679  CB  LYS A 506     1453   1611   1920     36    128    239       C  
ATOM   3680  CG  LYS A 506     -29.054   3.480  72.289  1.00 16.52           C  
ANISOU 3680  CG  LYS A 506     1886   2033   2358     40    148    225       C  
ATOM   3681  CD  LYS A 506     -30.119   2.426  71.959  1.00 18.71           C  
ANISOU 3681  CD  LYS A 506     2178   2304   2627     34    152    215       C  
ATOM   3682  CE  LYS A 506     -31.178   2.946  71.015  1.00 25.42           C  
ANISOU 3682  CE  LYS A 506     3038   3169   3451     24    156    204       C  
ATOM   3683  NZ  LYS A 506     -32.206   1.909  70.721  1.00 29.09           N  
ANISOU 3683  NZ  LYS A 506     3516   3629   3909     15    157    193       N  
ATOM   3684  N   ARG A 507     -29.659   7.177  75.055  1.00 11.27           N  
ANISOU 3684  N   ARG A 507     1216   1403   1664     28    101    256       N  
ATOM   3685  CA  ARG A 507     -29.802   7.856  76.350  1.00 10.68           C  
ANISOU 3685  CA  ARG A 507     1144   1332   1583     24     84    264       C  
ATOM   3686  C   ARG A 507     -28.973   9.130  76.411  1.00 12.88           C  
ANISOU 3686  C   ARG A 507     1414   1614   1864     24     79    268       C  
ATOM   3687  O   ARG A 507     -28.079   9.333  75.585  1.00 12.23           O  
ANISOU 3687  O   ARG A 507     1322   1531   1795     26     88    267       O  
ATOM   3688  CB  ARG A 507     -29.391   6.897  77.519  1.00 10.35           C  
ANISOU 3688  CB  ARG A 507     1101   1280   1552     27     72    275       C  
ATOM   3689  CG  ARG A 507     -27.929   6.410  77.428  1.00 17.99           C  
ANISOU 3689  CG  ARG A 507     2052   2237   2544     35     71    280       C  
ATOM   3690  CD  ARG A 507     -27.528   5.536  78.616  1.00 22.55           C  
ANISOU 3690  CD  ARG A 507     2629   2805   3132     38     56    293       C  
ATOM   3691  NE  ARG A 507     -27.477   6.295  79.873  1.00 19.95           N  
ANISOU 3691  NE  ARG A 507     2305   2483   2793     32     36    303       N  
ATOM   3692  CZ  ARG A 507     -26.400   6.950  80.299  1.00 30.94           C  
ANISOU 3692  CZ  ARG A 507     3684   3876   4195     33     22    309       C  
ATOM   3693  NH1 ARG A 507     -25.289   6.960  79.571  1.00 16.12           N  
ANISOU 3693  NH1 ARG A 507     1788   1995   2341     39     28    309       N  
ATOM   3694  NH2 ARG A 507     -26.426   7.601  81.452  1.00 21.22           N  
ANISOU 3694  NH2 ARG A 507     2460   2650   2951     26      4    316       N  
HETATM 3695  N   MSE A 508     -29.224   9.960  77.429  1.00  9.03           N  
ANISOU 3695  N   MSE A 508      932   1131   1367     19     66    273       N  
HETATM 3696  CA  MSE A 508     -28.376  11.102  77.740  1.00  7.92           C  
ANISOU 3696  CA  MSE A 508      786    992   1232     17     57    277       C  
HETATM 3697  C   MSE A 508     -27.349  10.680  78.792  1.00 13.31           C  
ANISOU 3697  C   MSE A 508     1460   1669   1929     17     41    286       C  
HETATM 3698  O   MSE A 508     -27.664   9.859  79.657  1.00 13.16           O  
ANISOU 3698  O   MSE A 508     1448   1647   1906     18     32    291       O  
HETATM 3699  CB  MSE A 508     -29.222  12.276  78.254  1.00  9.17           C  
ANISOU 3699  CB  MSE A 508      956   1156   1371     12     52    274       C  
HETATM 3700  CG  MSE A 508     -30.040  12.966  77.150  1.00 14.91           C  
ANISOU 3700  CG  MSE A 508     1689   1889   2088     12     65    267       C  
HETATM 3701 SE   MSE A 508     -31.495  14.086  77.846  0.75 21.07          SE  
ANISOU 3701 SE   MSE A 508     2484   2675   2845     11     61    263      SE  
HETATM 3702  CE  MSE A 508     -30.479  15.186  79.090  1.00 17.43           C  
ANISOU 3702  CE  MSE A 508     2026   2208   2387      5     45    266       C  
ATOM   3703  N   ARG A 509     -26.098  11.157  78.668  1.00 10.89           N  
ANISOU 3703  N   ARG A 509     1139   1360   1640     16     37    290       N  
ATOM   3704  CA  ARG A 509     -25.045  10.788  79.627  1.00 10.51           C  
ANISOU 3704  CA  ARG A 509     1078   1307   1607     16     18    301       C  
ATOM   3705  C   ARG A 509     -25.307  11.400  80.978  1.00 14.67           C  
ANISOU 3705  C   ARG A 509     1619   1838   2118      8     -3    305       C  
ATOM   3706  O   ARG A 509     -25.926  12.461  81.062  1.00 14.55           O  
ANISOU 3706  O   ARG A 509     1616   1827   2086      2     -2    298       O  
ATOM   3707  CB  ARG A 509     -23.657  11.215  79.120  1.00  8.26           C  
ANISOU 3707  CB  ARG A 509      771   1021   1347     16     19    304       C  
ATOM   3708  CG  ARG A 509     -23.212  10.493  77.863  1.00 18.14           C  
ANISOU 3708  CG  ARG A 509     2009   2268   2617     25     42    301       C  
ATOM   3709  CD  ARG A 509     -21.718  10.690  77.587  1.00 31.84           C  
ANISOU 3709  CD  ARG A 509     3716   4001   4382     26     42    306       C  
ATOM   3710  NE  ARG A 509     -21.375  12.097  77.352  1.00 49.52           N  
ANISOU 3710  NE  ARG A 509     5952   6246   6619     15     42    305       N  
ATOM   3711  CZ  ARG A 509     -20.782  12.877  78.256  1.00 67.10           C  
ANISOU 3711  CZ  ARG A 509     8171   8473   8850      5     20    311       C  
ATOM   3712  NH1 ARG A 509     -20.451  12.391  79.446  1.00 54.46           N  
ANISOU 3712  NH1 ARG A 509     6567   6870   7254      6     -5    319       N  
ATOM   3713  NH2 ARG A 509     -20.503  14.142  77.968  1.00 54.47           N  
ANISOU 3713  NH2 ARG A 509     6571   6875   7250     -6     22    309       N  
ATOM   3714  N   TYR A 510     -24.815  10.745  82.057  1.00 12.27           N  
ANISOU 3714  N   TYR A 510     1313   1531   1819      9    -23    315       N  
ATOM   3715  CA  TYR A 510     -24.882  11.301  83.405  1.00 11.77           C  
ANISOU 3715  CA  TYR A 510     1263   1471   1738      0    -46    319       C  
ATOM   3716  C   TYR A 510     -24.035  12.574  83.467  1.00 15.94           C  
ANISOU 3716  C   TYR A 510     1783   2001   2273    -10    -56    317       C  
ATOM   3717  O   TYR A 510     -23.024  12.675  82.757  1.00 15.43           O  
ANISOU 3717  O   TYR A 510     1695   1934   2233     -8    -53    319       O  
ATOM   3718  CB  TYR A 510     -24.334  10.284  84.445  1.00 12.67           C  
ANISOU 3718  CB  TYR A 510     1375   1581   1858      2    -67    334       C  
ATOM   3719  CG  TYR A 510     -25.098   8.983  84.531  1.00 12.69           C  
ANISOU 3719  CG  TYR A 510     1388   1579   1855      9    -59    338       C  
ATOM   3720  CD1 TYR A 510     -26.470   8.975  84.779  1.00 14.13           C  
ANISOU 3720  CD1 TYR A 510     1592   1765   2011      5    -48    332       C  
ATOM   3721  CD2 TYR A 510     -24.428   7.765  84.586  1.00 13.09           C  
ANISOU 3721  CD2 TYR A 510     1426   1620   1927     19    -65    350       C  
ATOM   3722  CE1 TYR A 510     -27.166   7.783  84.961  1.00 15.23           C  
ANISOU 3722  CE1 TYR A 510     1742   1900   2147      9    -42    337       C  
ATOM   3723  CE2 TYR A 510     -25.109   6.570  84.798  1.00 13.61           C  
ANISOU 3723  CE2 TYR A 510     1504   1678   1988     23    -60    355       C  
ATOM   3724  CZ  TYR A 510     -26.481   6.581  84.966  1.00 21.64           C  
ANISOU 3724  CZ  TYR A 510     2542   2700   2978     17    -48    349       C  
ATOM   3725  OH  TYR A 510     -27.157   5.401  85.147  1.00 23.66           O  
ANISOU 3725  OH  TYR A 510     2810   2949   3232     20    -42    354       O  
ATOM   3726  N   PRO A 511     -24.323  13.499  84.418  1.00 12.54           N  
ANISOU 3726  N   PRO A 511     1369   1574   1822    -20    -70    313       N  
ATOM   3727  CA  PRO A 511     -23.394  14.620  84.634  1.00 12.32           C  
ANISOU 3727  CA  PRO A 511     1334   1546   1802    -31    -85    312       C  
ATOM   3728  C   PRO A 511     -22.028  14.097  85.081  1.00 17.97           C  
ANISOU 3728  C   PRO A 511     2027   2260   2541    -32   -108    325       C  
ATOM   3729  O   PRO A 511     -21.967  13.192  85.916  1.00 18.33           O  
ANISOU 3729  O   PRO A 511     2076   2306   2582    -29   -124    335       O  
ATOM   3730  CB  PRO A 511     -24.076  15.441  85.745  1.00 13.74           C  
ANISOU 3730  CB  PRO A 511     1540   1727   1952    -41    -96    305       C  
ATOM   3731  CG  PRO A 511     -25.476  14.922  85.817  1.00 18.11           C  
ANISOU 3731  CG  PRO A 511     2114   2284   2485    -34    -80    301       C  
ATOM   3732  CD  PRO A 511     -25.425  13.510  85.396  1.00 13.76           C  
ANISOU 3732  CD  PRO A 511     1550   1731   1946    -23    -73    310       C  
ATOM   3733  N   THR A 512     -20.931  14.583  84.447  1.00 14.92           N  
ANISOU 3733  N   THR A 512     1616   1872   2181    -36   -108    326       N  
ATOM   3734  CA  THR A 512     -19.570  14.088  84.749  1.00 15.72           C  
ANISOU 3734  CA  THR A 512     1689   1973   2311    -36   -128    339       C  
ATOM   3735  C   THR A 512     -19.152  14.384  86.198  1.00 21.11           C  
ANISOU 3735  C   THR A 512     2380   2659   2982    -48   -166    345       C  
ATOM   3736  O   THR A 512     -18.239  13.739  86.715  1.00 21.53           O  
ANISOU 3736  O   THR A 512     2415   2713   3053    -46   -189    358       O  
ATOM   3737  CB  THR A 512     -18.543  14.637  83.735  1.00 24.68           C  
ANISOU 3737  CB  THR A 512     2794   3106   3476    -39   -117    338       C  
ATOM   3738  OG1 THR A 512     -18.533  16.058  83.803  1.00 28.48           O  
ANISOU 3738  OG1 THR A 512     3284   3587   3949    -55   -120    330       O  
ATOM   3739  CG2 THR A 512     -18.826  14.180  82.310  1.00 22.88           C  
ANISOU 3739  CG2 THR A 512     2558   2876   3259    -26    -82    334       C  
ATOM   3740  N   LYS A 513     -19.837  15.347  86.863  1.00 17.68           N  
ANISOU 3740  N   LYS A 513     1974   2226   2517    -61   -172    334       N  
ATOM   3741  CA  LYS A 513     -19.533  15.682  88.256  1.00 17.70           C  
ANISOU 3741  CA  LYS A 513     1990   2232   2503    -74   -206    337       C  
ATOM   3742  C   LYS A 513     -19.952  14.545  89.210  1.00 22.26           C  
ANISOU 3742  C   LYS A 513     2584   2813   3062    -67   -220    348       C  
ATOM   3743  O   LYS A 513     -19.454  14.469  90.332  1.00 22.33           O  
ANISOU 3743  O   LYS A 513     2598   2825   3062    -76   -252    356       O  
ATOM   3744  CB  LYS A 513     -20.186  17.038  88.662  1.00 19.72           C  
ANISOU 3744  CB  LYS A 513     2275   2487   2732    -89   -205    320       C  
ATOM   3745  CG  LYS A 513     -21.723  17.016  88.732  1.00 23.47           C  
ANISOU 3745  CG  LYS A 513     2781   2962   3175    -82   -182    310       C  
ATOM   3746  CD  LYS A 513     -22.223  16.800  90.174  1.00 27.39           C  
ANISOU 3746  CD  LYS A 513     3308   3463   3637    -88   -200    310       C  
ATOM   3747  CE  LYS A 513     -23.726  16.938  90.296  1.00 30.07           C  
ANISOU 3747  CE  LYS A 513     3675   3802   3946    -83   -176    299       C  
ATOM   3748  NZ  LYS A 513     -24.445  15.933  89.469  1.00 35.13           N  
ANISOU 3748  NZ  LYS A 513     4308   4444   4595    -67   -151    304       N  
ATOM   3749  N   GLU A 514     -20.824  13.621  88.726  1.00 18.80           N  
ANISOU 3749  N   GLU A 514     2152   2372   2620    -52   -196    349       N  
ATOM   3750  CA  GLU A 514     -21.254  12.457  89.510  1.00 18.66           C  
ANISOU 3750  CA  GLU A 514     2148   2354   2587    -45   -205    362       C  
ATOM   3751  C   GLU A 514     -20.117  11.460  89.693  1.00 24.66           C  
ANISOU 3751  C   GLU A 514     2883   3112   3376    -37   -227    381       C  
ATOM   3752  O   GLU A 514     -20.067  10.770  90.706  1.00 24.25           O  
ANISOU 3752  O   GLU A 514     2842   3061   3311    -37   -249    395       O  
ATOM   3753  CB  GLU A 514     -22.470  11.770  88.853  1.00 19.21           C  
ANISOU 3753  CB  GLU A 514     2229   2422   2649    -34   -172    357       C  
ATOM   3754  CG  GLU A 514     -23.776  12.519  89.057  1.00 25.14           C  
ANISOU 3754  CG  GLU A 514     3009   3177   3367    -40   -156    342       C  
ATOM   3755  CD  GLU A 514     -24.261  12.547  90.494  1.00 41.51           C  
ANISOU 3755  CD  GLU A 514     5111   5254   5405    -49   -172    344       C  
ATOM   3756  OE1 GLU A 514     -24.491  11.457  91.066  1.00 29.18           O  
ANISOU 3756  OE1 GLU A 514     3559   3693   3836    -45   -178    357       O  
ATOM   3757  OE2 GLU A 514     -24.446  13.660  91.036  1.00 38.49           O  
ANISOU 3757  OE2 GLU A 514     4746   4875   5003    -61   -178    332       O  
ATOM   3758  N   SER A 515     -19.183  11.403  88.726  1.00 22.50           N  
ANISOU 3758  N   SER A 515     2574   2835   3139    -30   -220    383       N  
ATOM   3759  CA  SER A 515     -18.033  10.501  88.813  1.00 23.28           C  
ANISOU 3759  CA  SER A 515     2644   2930   3271    -20   -239    401       C  
ATOM   3760  C   SER A 515     -16.961  11.047  89.775  1.00 28.44           C  
ANISOU 3760  C   SER A 515     3286   3589   3929    -33   -280    410       C  
ATOM   3761  O   SER A 515     -16.032  10.323  90.138  1.00 27.60           O  
ANISOU 3761  O   SER A 515     3158   3483   3847    -26   -305    428       O  
ATOM   3762  CB  SER A 515     -17.428  10.271  87.429  1.00 27.27           C  
ANISOU 3762  CB  SER A 515     3116   3431   3816     -8   -213    399       C  
ATOM   3763  OG  SER A 515     -16.973  11.485  86.854  1.00 35.85           O  
ANISOU 3763  OG  SER A 515     4188   4521   4912    -20   -207    387       O  
ATOM   3764  N   LEU A 516     -17.101  12.322  90.197  1.00 26.63           N  
ANISOU 3764  N   LEU A 516     3073   3367   3678    -53   -289    397       N  
ATOM   3765  CA  LEU A 516     -16.096  12.977  91.032  1.00 27.27           C  
ANISOU 3765  CA  LEU A 516     3144   3453   3762    -70   -328    402       C  
ATOM   3766  C   LEU A 516     -16.554  13.133  92.489  1.00 31.16           C  
ANISOU 3766  C   LEU A 516     3674   3952   4212    -83   -357    404       C  
ATOM   3767  O   LEU A 516     -15.790  12.826  93.405  1.00 31.50           O  
ANISOU 3767  O   LEU A 516     3713   4000   4257    -87   -396    419       O  
ATOM   3768  CB  LEU A 516     -15.713  14.351  90.436  1.00 27.68           C  
ANISOU 3768  CB  LEU A 516     3185   3506   3826    -85   -320    387       C  
ATOM   3769  CG  LEU A 516     -15.122  14.322  89.008  1.00 32.90           C  
ANISOU 3769  CG  LEU A 516     3809   4164   4529    -76   -292    386       C  
ATOM   3770  CD1 LEU A 516     -15.144  15.693  88.385  1.00 33.02           C  
ANISOU 3770  CD1 LEU A 516     3825   4177   4545    -91   -276    369       C  
ATOM   3771  CD2 LEU A 516     -13.703  13.752  89.007  1.00 36.30           C  
ANISOU 3771  CD2 LEU A 516     4195   4596   5002    -70   -315    403       C  
ATOM   3772  N   ILE A 517     -17.784  13.646  92.708  1.00 26.52           N  
ANISOU 3772  N   ILE A 517     3125   3365   3586    -89   -338    388       N  
ATOM   3773  CA  ILE A 517     -18.279  13.900  94.075  1.00 25.99           C  
ANISOU 3773  CA  ILE A 517     3097   3304   3475   -102   -360    386       C  
ATOM   3774  C   ILE A 517     -19.296  12.835  94.548  1.00 29.80           C  
ANISOU 3774  C   ILE A 517     3606   3786   3931    -91   -349    395       C  
ATOM   3775  O   ILE A 517     -19.732  12.870  95.704  1.00 29.78           O  
ANISOU 3775  O   ILE A 517     3637   3789   3890   -101   -365    396       O  
ATOM   3776  CB  ILE A 517     -18.826  15.356  94.231  1.00 28.46           C  
ANISOU 3776  CB  ILE A 517     3435   3617   3762   -120   -351    362       C  
ATOM   3777  CG1 ILE A 517     -20.100  15.577  93.377  1.00 28.26           C  
ANISOU 3777  CG1 ILE A 517     3423   3587   3728   -110   -305    346       C  
ATOM   3778  CG2 ILE A 517     -17.733  16.392  93.905  1.00 28.86           C  
ANISOU 3778  CG2 ILE A 517     3461   3666   3838   -134   -366    355       C  
ATOM   3779  CD1 ILE A 517     -20.852  16.905  93.684  1.00 33.50           C  
ANISOU 3779  CD1 ILE A 517     4118   4249   4362   -123   -294    323       C  
ATOM   3780  N   ASN A 518     -19.642  11.877  93.665  1.00 25.18           N  
ANISOU 3780  N   ASN A 518     3007   3194   3367    -72   -322    402       N  
ATOM   3781  CA  ASN A 518     -20.569  10.790  94.001  1.00 24.19           C  
ANISOU 3781  CA  ASN A 518     2902   3066   3221    -63   -310    411       C  
ATOM   3782  C   ASN A 518     -20.090   9.479  93.324  1.00 26.81           C  
ANISOU 3782  C   ASN A 518     3206   3389   3590    -43   -306    428       C  
ATOM   3783  O   ASN A 518     -20.900   8.731  92.761  1.00 26.17           O  
ANISOU 3783  O   ASN A 518     3130   3301   3511    -31   -277    428       O  
ATOM   3784  CB  ASN A 518     -22.006  11.153  93.545  1.00 22.97           C  
ANISOU 3784  CB  ASN A 518     2770   2911   3045    -62   -271    392       C  
ATOM   3785  CG  ASN A 518     -23.096  10.337  94.219  1.00 33.21           C  
ANISOU 3785  CG  ASN A 518     4097   4209   4312    -60   -261    399       C  
ATOM   3786  OD1 ASN A 518     -22.894   9.735  95.284  1.00 28.58           O  
ANISOU 3786  OD1 ASN A 518     3526   3625   3708    -64   -285    415       O  
ATOM   3787  ND2 ASN A 518     -24.305  10.389  93.665  1.00 12.56           N  
ANISOU 3787  ND2 ASN A 518     1493   1593   1687    -56   -225    385       N  
ATOM   3788  N   ALA A 519     -18.748   9.231  93.356  1.00 22.32           N  
ANISOU 3788  N   ALA A 519     2607   2819   3054    -39   -334    443       N  
ATOM   3789  CA  ALA A 519     -18.092   8.133  92.621  1.00 21.59           C  
ANISOU 3789  CA  ALA A 519     2482   2717   3004    -18   -329    457       C  
ATOM   3790  C   ALA A 519     -18.701   6.749  92.897  1.00 23.97           C  
ANISOU 3790  C   ALA A 519     2800   3009   3299     -5   -323    473       C  
ATOM   3791  O   ALA A 519     -18.985   6.012  91.953  1.00 23.35           O  
ANISOU 3791  O   ALA A 519     2711   2919   3242     10   -294    471       O  
ATOM   3792  CB  ALA A 519     -16.600   8.120  92.920  1.00 22.70           C  
ANISOU 3792  CB  ALA A 519     2590   2860   3176    -18   -366    473       C  
ATOM   3793  N   THR A 520     -18.854   6.376  94.189  1.00 20.20           N  
ANISOU 3793  N   THR A 520     2349   2534   2793    -12   -351    489       N  
ATOM   3794  CA  THR A 520     -19.383   5.052  94.567  1.00 19.86           C  
ANISOU 3794  CA  THR A 520     2324   2481   2743     -1   -348    507       C  
ATOM   3795  C   THR A 520     -20.737   4.770  93.895  1.00 23.02           C  
ANISOU 3795  C   THR A 520     2741   2875   3130      1   -304    493       C  
ATOM   3796  O   THR A 520     -20.904   3.724  93.256  1.00 22.05           O  
ANISOU 3796  O   THR A 520     2609   2738   3029     16   -286    498       O  
ATOM   3797  CB  THR A 520     -19.457   4.921  96.105  1.00 26.91           C  
ANISOU 3797  CB  THR A 520     3248   3380   3596    -13   -382    525       C  
ATOM   3798  OG1 THR A 520     -18.144   5.067  96.646  1.00 24.17           O  
ANISOU 3798  OG1 THR A 520     2880   3037   3265    -14   -427    541       O  
ATOM   3799  CG2 THR A 520     -20.061   3.581  96.554  1.00 24.96           C  
ANISOU 3799  CG2 THR A 520     3023   3122   3340     -5   -379    546       C  
ATOM   3800  N   GLU A 521     -21.682   5.714  94.005  1.00 19.75           N  
ANISOU 3800  N   GLU A 521     2350   2472   2683    -13   -287    473       N  
ATOM   3801  CA  GLU A 521     -23.016   5.548  93.428  1.00 19.45           C  
ANISOU 3801  CA  GLU A 521     2327   2431   2632    -13   -248    458       C  
ATOM   3802  C   GLU A 521     -23.005   5.675  91.895  1.00 22.90           C  
ANISOU 3802  C   GLU A 521     2737   2863   3100     -2   -218    442       C  
ATOM   3803  O   GLU A 521     -23.797   5.014  91.218  1.00 22.05           O  
ANISOU 3803  O   GLU A 521     2633   2748   2997      4   -191    438       O  
ATOM   3804  CB  GLU A 521     -24.009   6.539  94.056  1.00 20.72           C  
ANISOU 3804  CB  GLU A 521     2519   2606   2750    -29   -239    443       C  
ATOM   3805  CG  GLU A 521     -24.266   6.287  95.540  1.00 32.73           C  
ANISOU 3805  CG  GLU A 521     4073   4132   4232    -40   -260    458       C  
ATOM   3806  CD  GLU A 521     -24.909   4.946  95.871  1.00 47.84           C  
ANISOU 3806  CD  GLU A 521     6002   6036   6138    -35   -252    476       C  
ATOM   3807  OE1 GLU A 521     -25.479   4.312  94.951  1.00 29.72           O  
ANISOU 3807  OE1 GLU A 521     3698   3732   3862    -26   -223    471       O  
ATOM   3808  OE2 GLU A 521     -24.906   4.568  97.065  1.00 42.21           O  
ANISOU 3808  OE2 GLU A 521     5314   5325   5398    -43   -273    493       O  
ATOM   3809  N   TYR A 522     -22.079   6.493  91.346  1.00 19.24           N  
ANISOU 3809  N   TYR A 522     2248   2403   2658     -2   -225    434       N  
ATOM   3810  CA  TYR A 522     -21.942   6.653  89.890  1.00 18.76           C  
ANISOU 3810  CA  TYR A 522     2163   2339   2627      7   -198    421       C  
ATOM   3811  C   TYR A 522     -21.490   5.346  89.236  1.00 22.60           C  
ANISOU 3811  C   TYR A 522     2629   2810   3147     25   -190    431       C  
ATOM   3812  O   TYR A 522     -22.008   4.978  88.179  1.00 21.85           O  
ANISOU 3812  O   TYR A 522     2531   2709   3063     32   -159    420       O  
ATOM   3813  CB  TYR A 522     -20.960   7.799  89.554  1.00 19.41           C  
ANISOU 3813  CB  TYR A 522     2222   2427   2725      1   -207    413       C  
ATOM   3814  CG  TYR A 522     -20.613   7.890  88.082  1.00 20.33           C  
ANISOU 3814  CG  TYR A 522     2312   2540   2874     10   -181    402       C  
ATOM   3815  CD1 TYR A 522     -21.415   8.608  87.200  1.00 21.65           C  
ANISOU 3815  CD1 TYR A 522     2485   2709   3030      6   -152    383       C  
ATOM   3816  CD2 TYR A 522     -19.469   7.279  87.574  1.00 21.22           C  
ANISOU 3816  CD2 TYR A 522     2392   2645   3026     23   -185    412       C  
ATOM   3817  CE1 TYR A 522     -21.097   8.703  85.846  1.00 22.19           C  
ANISOU 3817  CE1 TYR A 522     2532   2775   3123     13   -128    374       C  
ATOM   3818  CE2 TYR A 522     -19.148   7.354  86.221  1.00 22.03           C  
ANISOU 3818  CE2 TYR A 522     2471   2744   3154     31   -158    401       C  
ATOM   3819  CZ  TYR A 522     -19.958   8.075  85.360  1.00 29.50           C  
ANISOU 3819  CZ  TYR A 522     3427   3694   4086     25   -130    383       C  
ATOM   3820  OH  TYR A 522     -19.631   8.167  84.027  1.00 30.72           O  
ANISOU 3820  OH  TYR A 522     3562   3846   4262     32   -103    373       O  
ATOM   3821  N   GLU A 523     -20.515   4.642  89.862  1.00 19.74           N  
ANISOU 3821  N   GLU A 523     2255   2441   2803     32   -218    453       N  
ATOM   3822  CA  GLU A 523     -20.031   3.351  89.350  1.00 20.41           C  
ANISOU 3822  CA  GLU A 523     2322   2510   2924     52   -212    464       C  
ATOM   3823  C   GLU A 523     -21.134   2.288  89.412  1.00 24.70           C  
ANISOU 3823  C   GLU A 523     2891   3042   3453     55   -195    468       C  
ATOM   3824  O   GLU A 523     -21.209   1.427  88.531  1.00 24.74           O  
ANISOU 3824  O   GLU A 523     2888   3033   3482     68   -173    464       O  
ATOM   3825  CB  GLU A 523     -18.776   2.884  90.121  1.00 22.34           C  
ANISOU 3825  CB  GLU A 523     2547   2749   3190     60   -249    489       C  
ATOM   3826  CG  GLU A 523     -17.554   3.776  89.904  1.00 34.69           C  
ANISOU 3826  CG  GLU A 523     4078   4323   4779     58   -265    486       C  
ATOM   3827  CD  GLU A 523     -17.024   3.816  88.478  1.00 59.72           C  
ANISOU 3827  CD  GLU A 523     7215   7488   7987     70   -236    473       C  
ATOM   3828  OE1 GLU A 523     -17.121   2.783  87.775  1.00 53.53           O  
ANISOU 3828  OE1 GLU A 523     6425   6689   7224     87   -214    474       O  
ATOM   3829  OE2 GLU A 523     -16.435   4.853  88.095  1.00 57.39           O  
ANISOU 3829  OE2 GLU A 523     6900   7203   7701     62   -236    463       O  
ATOM   3830  N   LYS A 524     -22.016   2.367  90.453  1.00 21.36           N  
ANISOU 3830  N   LYS A 524     2501   2625   2991     42   -203    473       N  
ATOM   3831  CA ALYS A 524     -23.158   1.456  90.574  0.50 21.06           C  
ANISOU 3831  CA ALYS A 524     2488   2578   2936     41   -185    476       C  
ATOM   3832  CA BLYS A 524     -23.161   1.462  90.591  0.50 21.06           C  
ANISOU 3832  CA BLYS A 524     2489   2578   2936     41   -186    476       C  
ATOM   3833  C   LYS A 524     -24.135   1.661  89.415  1.00 24.11           C  
ANISOU 3833  C   LYS A 524     2875   2965   3320     39   -147    451       C  
ATOM   3834  O   LYS A 524     -24.619   0.689  88.838  1.00 24.46           O  
ANISOU 3834  O   LYS A 524     2922   2995   3376     46   -128    450       O  
ATOM   3835  CB ALYS A 524     -23.873   1.650  91.925  0.50 23.83           C  
ANISOU 3835  CB ALYS A 524     2872   2938   3243     25   -200    485       C  
ATOM   3836  CB BLYS A 524     -23.880   1.710  91.939  0.50 23.82           C  
ANISOU 3836  CB BLYS A 524     2872   2938   3242     25   -200    484       C  
ATOM   3837  CG ALYS A 524     -23.069   1.147  93.119  0.50 39.38           C  
ANISOU 3837  CG ALYS A 524     4847   4903   5210     27   -238    513       C  
ATOM   3838  CG BLYS A 524     -25.062   0.770  92.193  0.50 38.96           C  
ANISOU 3838  CG BLYS A 524     4815   4846   5141     21   -182    489       C  
ATOM   3839  CD ALYS A 524     -23.804   1.392  94.434  0.50 49.35           C  
ANISOU 3839  CD ALYS A 524     6147   6177   6425     10   -249    520       C  
ATOM   3840  CD BLYS A 524     -25.851   1.159  93.466  0.50 49.26           C  
ANISOU 3840  CD BLYS A 524     6153   6164   6399      3   -189    494       C  
ATOM   3841  CE ALYS A 524     -23.026   0.889  95.630  0.50 60.92           C  
ANISOU 3841  CE ALYS A 524     7622   7640   7884     10   -289    550       C  
ATOM   3842  CE BLYS A 524     -25.118   0.805  94.747  0.50 62.54           C  
ANISOU 3842  CE BLYS A 524     7848   7845   8069      2   -226    522       C  
ATOM   3843  NZ ALYS A 524     -22.906  -0.595  95.631  0.50 71.68           N  
ANISOU 3843  NZ ALYS A 524     8985   8982   9269     24   -291    573       N  
ATOM   3844  NZ BLYS A 524     -25.003  -0.669  94.932  0.50 72.51           N  
ANISOU 3844  NZ BLYS A 524     9116   9087   9348     12   -230    546       N  
ATOM   3845  N   GLY A 525     -24.371   2.924  89.053  1.00 18.99           N  
ANISOU 3845  N   GLY A 525     2225   2332   2660     30   -139    433       N  
ATOM   3846  CA  GLY A 525     -25.231   3.272  87.930  1.00 18.19           C  
ANISOU 3846  CA  GLY A 525     2123   2234   2556     29   -107    411       C  
ATOM   3847  C   GLY A 525     -24.628   2.868  86.603  1.00 20.69           C  
ANISOU 3847  C   GLY A 525     2414   2541   2907     42    -91    403       C  
ATOM   3848  O   GLY A 525     -25.334   2.378  85.720  1.00 19.19           O  
ANISOU 3848  O   GLY A 525     2226   2344   2720     45    -66    392       O  
ATOM   3849  N   LYS A 526     -23.290   3.012  86.476  1.00 17.85           N  
ANISOU 3849  N   LYS A 526     2029   2179   2575     51   -105    410       N  
ATOM   3850  CA  LYS A 526     -22.558   2.582  85.283  1.00 17.29           C  
ANISOU 3850  CA  LYS A 526     1933   2098   2539     65    -89    404       C  
ATOM   3851  C   LYS A 526     -22.637   1.054  85.133  1.00 20.44           C  
ANISOU 3851  C   LYS A 526     2335   2476   2956     78    -81    413       C  
ATOM   3852  O   LYS A 526     -22.880   0.560  84.041  1.00 19.93           O  
ANISOU 3852  O   LYS A 526     2267   2403   2904     84    -55    400       O  
ATOM   3853  CB  LYS A 526     -21.087   3.044  85.358  1.00 19.50           C  
ANISOU 3853  CB  LYS A 526     2184   2381   2846     70   -107    412       C  
ATOM   3854  CG  LYS A 526     -20.291   2.771  84.089  1.00 28.89           C  
ANISOU 3854  CG  LYS A 526     3344   3562   4071     84    -86    404       C  
ATOM   3855  CD  LYS A 526     -18.861   3.290  84.205  1.00 38.50           C  
ANISOU 3855  CD  LYS A 526     4529   4783   5316     88   -104    412       C  
ATOM   3856  N   SER A 527     -22.506   0.313  86.257  1.00 16.52           N  
ANISOU 3856  N   SER A 527     1849   1971   2458     80   -104    434       N  
ATOM   3857  CA  SER A 527     -22.594  -1.151  86.240  1.00 16.41           C  
ANISOU 3857  CA  SER A 527     1841   1934   2461     92    -99    445       C  
ATOM   3858  C   SER A 527     -23.998  -1.616  85.840  1.00 18.85           C  
ANISOU 3858  C   SER A 527     2174   2239   2750     83    -74    432       C  
ATOM   3859  O   SER A 527     -24.135  -2.581  85.083  1.00 18.72           O  
ANISOU 3859  O   SER A 527     2156   2203   2752     92    -55    427       O  
ATOM   3860  CB  SER A 527     -22.217  -1.725  87.600  1.00 20.46           C  
ANISOU 3860  CB  SER A 527     2362   2440   2971     94   -132    473       C  
ATOM   3861  OG  SER A 527     -20.887  -1.383  87.947  1.00 28.99           O  
ANISOU 3861  OG  SER A 527     3417   3524   4073    102   -158    485       O  
HETATM 3862  N   MSE A 528     -25.048  -0.909  86.328  1.00 13.27           N  
ANISOU 3862  N   MSE A 528     1487   1548   2007     65    -73    427       N  
HETATM 3863  CA  MSE A 528     -26.439  -1.217  85.972  1.00 11.68           C  
ANISOU 3863  CA  MSE A 528     1305   1347   1787     55    -50    415       C  
HETATM 3864  C   MSE A 528     -26.685  -1.012  84.478  1.00 16.87           C  
ANISOU 3864  C   MSE A 528     1951   2004   2454     57    -23    391       C  
HETATM 3865  O   MSE A 528     -27.369  -1.824  83.852  1.00 16.03           O  
ANISOU 3865  O   MSE A 528     1852   1886   2351     56     -5    382       O  
HETATM 3866  CB  MSE A 528     -27.411  -0.365  86.796  1.00 12.95           C  
ANISOU 3866  CB  MSE A 528     1485   1526   1909     38    -54    413       C  
HETATM 3867  CG  MSE A 528     -27.495  -0.788  88.259  1.00 18.81           C  
ANISOU 3867  CG  MSE A 528     2247   2266   2634     32    -75    436       C  
HETATM 3868 SE   MSE A 528     -28.368   0.548  89.354  0.75 25.44          SE  
ANISOU 3868 SE   MSE A 528     3108   3132   3425     12    -80    432      SE  
HETATM 3869  CE  MSE A 528     -28.376  -0.394  91.026  1.00 22.10           C  
ANISOU 3869  CE  MSE A 528     2713   2702   2984      7   -103    463       C  
ATOM   3870  N   LEU A 529     -26.102   0.066  83.894  1.00 14.93           N  
ANISOU 3870  N   LEU A 529     1688   1772   2213     59    -22    380       N  
ATOM   3871  CA  LEU A 529     -26.207   0.331  82.450  1.00 14.75           C  
ANISOU 3871  CA  LEU A 529     1656   1752   2198     62      3    359       C  
ATOM   3872  C   LEU A 529     -25.588  -0.793  81.644  1.00 18.72           C  
ANISOU 3872  C   LEU A 529     2148   2233   2732     76     16    356       C  
ATOM   3873  O   LEU A 529     -26.158  -1.218  80.639  1.00 18.41           O  
ANISOU 3873  O   LEU A 529     2113   2188   2692     76     38    341       O  
ATOM   3874  CB  LEU A 529     -25.525   1.664  82.090  1.00 14.66           C  
ANISOU 3874  CB  LEU A 529     1627   1756   2187     61      1    352       C  
ATOM   3875  CG  LEU A 529     -26.310   2.932  82.395  1.00 19.06           C  
ANISOU 3875  CG  LEU A 529     2196   2333   2714     47     -2    345       C  
ATOM   3876  CD1 LEU A 529     -25.441   4.145  82.232  1.00 18.81           C  
ANISOU 3876  CD1 LEU A 529     2147   2311   2687     47     -9    343       C  
ATOM   3877  CD2 LEU A 529     -27.540   3.047  81.498  1.00 21.48           C  
ANISOU 3877  CD2 LEU A 529     2513   2645   3005     41     20    328       C  
ATOM   3878  N   GLY A 530     -24.403  -1.243  82.070  1.00 16.15           N  
ANISOU 3878  N   GLY A 530     1808   1897   2433     90      1    372       N  
ATOM   3879  CA  GLY A 530     -23.663  -2.293  81.381  1.00 16.67           C  
ANISOU 3879  CA  GLY A 530     1861   1941   2533    107     14    370       C  
ATOM   3880  C   GLY A 530     -23.138  -1.858  80.028  1.00 20.91           C  
ANISOU 3880  C   GLY A 530     2380   2482   3084    114     37    351       C  
ATOM   3881  O   GLY A 530     -23.117  -0.662  79.716  1.00 19.73           O  
ANISOU 3881  O   GLY A 530     2224   2352   2921    105     39    343       O  
ATOM   3882  N   GLY A 531     -22.720  -2.832  79.223  1.00 19.26           N  
ANISOU 3882  N   GLY A 531     2164   2253   2901    128     56    344       N  
ATOM   3883  CA  GLY A 531     -22.211  -2.582  77.879  1.00 19.72           C  
ANISOU 3883  CA  GLY A 531     2208   2312   2971    134     82    325       C  
ATOM   3884  C   GLY A 531     -20.965  -1.723  77.855  1.00 24.25           C  
ANISOU 3884  C   GLY A 531     2752   2898   3564    141     76    330       C  
ATOM   3885  O   GLY A 531     -20.004  -1.995  78.583  1.00 24.31           O  
ANISOU 3885  O   GLY A 531     2741   2899   3597    153     58    348       O  
ATOM   3886  N   LYS A 532     -20.981  -0.652  77.022  1.00 20.84           N  
ANISOU 3886  N   LYS A 532     2316   2485   3120    132     91    316       N  
ATOM   3887  CA ALYS A 532     -19.826   0.240  76.881  0.50 20.83           C  
ANISOU 3887  CA ALYS A 532     2285   2494   3135    135     89    320       C  
ATOM   3888  CA BLYS A 532     -19.834   0.244  76.867  0.50 20.76           C  
ANISOU 3888  CA BLYS A 532     2276   2485   3126    135     90    320       C  
ATOM   3889  C   LYS A 532     -19.755   1.289  78.000  1.00 24.45           C  
ANISOU 3889  C   LYS A 532     2741   2970   3581    123     58    335       C  
ATOM   3890  O   LYS A 532     -18.741   1.968  78.144  1.00 25.43           O  
ANISOU 3890  O   LYS A 532     2840   3101   3721    124     50    342       O  
ATOM   3891  CB ALYS A 532     -19.814   0.909  75.500  0.50 23.47           C  
ANISOU 3891  CB ALYS A 532     2617   2839   3462    131    120    301       C  
ATOM   3892  CB BLYS A 532     -19.865   0.931  75.491  0.50 23.25           C  
ANISOU 3892  CB BLYS A 532     2590   2812   3433    130    120    300       C  
ATOM   3893  CG ALYS A 532     -19.431  -0.040  74.369  0.50 38.14           C  
ANISOU 3893  CG ALYS A 532     4471   4681   5341    145    152    286       C  
ATOM   3894  CG BLYS A 532     -19.686  -0.045  74.318  0.50 35.95           C  
ANISOU 3894  CG BLYS A 532     4198   4404   5056    143    152    284       C  
ATOM   3895  CD ALYS A 532     -19.326   0.689  73.032  0.50 46.95           C  
ANISOU 3895  CD ALYS A 532     5584   5809   6447    140    181    269       C  
ATOM   3896  CD BLYS A 532     -19.848   0.651  72.949  0.50 43.69           C  
ANISOU 3896  CD BLYS A 532     5184   5396   6019    135    181    265       C  
ATOM   3897  CE ALYS A 532     -18.807  -0.209  71.931  0.50 55.52           C  
ANISOU 3897  CE ALYS A 532     6664   6879   7552    154    215    254       C  
ATOM   3898  CE BLYS A 532     -21.274   0.589  72.417  0.50 50.81           C  
ANISOU 3898  CE BLYS A 532     6118   6303   6885    122    189    250       C  
ATOM   3899  NZ ALYS A 532     -17.399  -0.633  72.177  0.50 63.04           N  
ANISOU 3899  NZ ALYS A 532     7582   7820   8550    174    217    264       N  
ATOM   3900  NZ BLYS A 532     -22.211   1.421  73.218  0.50 56.30           N  
ANISOU 3900  NZ BLYS A 532     6828   7013   7552    106    164    259       N  
ATOM   3901  N   GLY A 533     -20.814   1.385  78.801  1.00 19.22           N  
ANISOU 3901  N   GLY A 533     2103   2311   2888    112     42    339       N  
ATOM   3902  CA  GLY A 533     -20.821   2.275  79.957  1.00 17.88           C  
ANISOU 3902  CA  GLY A 533     1936   2155   2702    100     13    352       C  
ATOM   3903  C   GLY A 533     -21.692   3.504  79.826  1.00 17.61           C  
ANISOU 3903  C   GLY A 533     1917   2139   2635     83     16    341       C  
ATOM   3904  O   GLY A 533     -22.789   3.442  79.262  1.00 16.44           O  
ANISOU 3904  O   GLY A 533     1788   1992   2466     78     33    329       O  
ATOM   3905  N   ASP A 534     -21.233   4.627  80.421  1.00 11.92           N  
ANISOU 3905  N   ASP A 534     1189   1430   1910     74     -2    347       N  
ATOM   3906  CA  ASP A 534     -21.987   5.878  80.472  1.00 10.84           C  
ANISOU 3906  CA  ASP A 534     1066   1308   1743     59     -3    338       C  
ATOM   3907  C   ASP A 534     -21.794   6.700  79.182  1.00 14.55           C  
ANISOU 3907  C   ASP A 534     1528   1785   2217     56     21    325       C  
ATOM   3908  O   ASP A 534     -21.124   7.740  79.195  1.00 13.26           O  
ANISOU 3908  O   ASP A 534     1351   1628   2059     50     15    326       O  
ATOM   3909  CB  ASP A 534     -21.581   6.698  81.720  1.00 12.43           C  
ANISOU 3909  CB  ASP A 534     1268   1518   1937     49    -33    349       C  
ATOM   3910  CG  ASP A 534     -22.336   8.012  81.896  1.00 18.80           C  
ANISOU 3910  CG  ASP A 534     2092   2337   2716     34    -34    340       C  
ATOM   3911  OD1 ASP A 534     -23.453   8.140  81.332  1.00 18.95           O  
ANISOU 3911  OD1 ASP A 534     2127   2358   2714     32    -16    329       O  
ATOM   3912  OD2 ASP A 534     -21.854   8.873  82.659  1.00 21.93           O  
ANISOU 3912  OD2 ASP A 534     2486   2739   3108     25    -55    345       O  
ATOM   3913  N   ILE A 535     -22.350   6.207  78.066  1.00 11.10           N  
ANISOU 3913  N   ILE A 535     1097   1344   1776     61     47    313       N  
ATOM   3914  CA  ILE A 535     -22.332   6.925  76.791  1.00 10.58           C  
ANISOU 3914  CA  ILE A 535     1028   1284   1707     58     70    301       C  
ATOM   3915  C   ILE A 535     -23.732   6.952  76.189  1.00 14.88           C  
ANISOU 3915  C   ILE A 535     1597   1833   2223     53     83    289       C  
ATOM   3916  O   ILE A 535     -24.649   6.315  76.730  1.00 14.09           O  
ANISOU 3916  O   ILE A 535     1513   1731   2111     52     76    289       O  
ATOM   3917  CB  ILE A 535     -21.265   6.345  75.797  1.00 13.29           C  
ANISOU 3917  CB  ILE A 535     1349   1620   2079     69     92    297       C  
ATOM   3918  CG1 ILE A 535     -21.509   4.846  75.513  1.00 13.23           C  
ANISOU 3918  CG1 ILE A 535     1347   1597   2080     81    103    293       C  
ATOM   3919  CG2 ILE A 535     -19.823   6.604  76.307  1.00 13.93           C  
ANISOU 3919  CG2 ILE A 535     1401   1701   2192     73     78    310       C  
ATOM   3920  CD1 ILE A 535     -20.626   4.285  74.417  1.00 14.71           C  
ANISOU 3920  CD1 ILE A 535     1518   1777   2293     93    130    285       C  
ATOM   3921  N   VAL A 536     -23.918   7.711  75.096  1.00 11.28           N  
ANISOU 3921  N   VAL A 536     1143   1385   1757     48    101    279       N  
ATOM   3922  CA  VAL A 536     -25.247   7.907  74.494  1.00 11.55           C  
ANISOU 3922  CA  VAL A 536     1198   1425   1764     43    110    269       C  
ATOM   3923  C   VAL A 536     -25.776   6.661  73.761  1.00 16.00           C  
ANISOU 3923  C   VAL A 536     1771   1983   2327     48    125    259       C  
ATOM   3924  O   VAL A 536     -26.964   6.603  73.445  1.00 16.27           O  
ANISOU 3924  O   VAL A 536     1821   2020   2339     42    127    252       O  
ATOM   3925  CB  VAL A 536     -25.292   9.163  73.581  1.00 15.33           C  
ANISOU 3925  CB  VAL A 536     1679   1914   2231     36    120    265       C  
ATOM   3926  CG1 VAL A 536     -25.035  10.425  74.380  1.00 14.96           C  
ANISOU 3926  CG1 VAL A 536     1630   1873   2183     29    104    273       C  
ATOM   3927  CG2 VAL A 536     -24.303   9.039  72.421  1.00 15.53           C  
ANISOU 3927  CG2 VAL A 536     1691   1937   2271     40    143    261       C  
ATOM   3928  N   SER A 537     -24.891   5.700  73.440  1.00 12.13           N  
ANISOU 3928  N   SER A 537     1269   1480   1859     58    136    258       N  
ATOM   3929  CA  SER A 537     -25.275   4.536  72.637  1.00 11.58           C  
ANISOU 3929  CA  SER A 537     1209   1401   1790     62    153    246       C  
ATOM   3930  C   SER A 537     -25.640   3.297  73.491  1.00 14.65           C  
ANISOU 3930  C   SER A 537     1603   1775   2186     66    142    250       C  
ATOM   3931  O   SER A 537     -26.021   2.266  72.937  1.00 13.75           O  
ANISOU 3931  O   SER A 537     1499   1651   2073     68    154    240       O  
ATOM   3932  CB  SER A 537     -24.178   4.191  71.636  1.00 13.86           C  
ANISOU 3932  CB  SER A 537     1484   1683   2099     71    176    239       C  
ATOM   3933  OG  SER A 537     -22.953   3.919  72.294  1.00 18.54           O  
ANISOU 3933  OG  SER A 537     2055   2267   2723     82    170    250       O  
ATOM   3934  N   THR A 538     -25.546   3.408  74.829  1.00 11.11           N  
ANISOU 3934  N   THR A 538     1152   1327   1742     66    119    266       N  
ATOM   3935  CA  THR A 538     -25.887   2.288  75.710  1.00 10.35           C  
ANISOU 3935  CA  THR A 538     1064   1217   1651     68    108    273       C  
ATOM   3936  C   THR A 538     -27.416   2.154  75.857  1.00 13.04           C  
ANISOU 3936  C   THR A 538     1426   1563   1965     56    106    268       C  
ATOM   3937  O   THR A 538     -28.074   3.071  76.353  1.00 11.82           O  
ANISOU 3937  O   THR A 538     1277   1423   1791     47     96    271       O  
ATOM   3938  CB  THR A 538     -25.176   2.432  77.065  1.00 21.08           C  
ANISOU 3938  CB  THR A 538     2413   2575   3022     71     84    292       C  
ATOM   3939  OG1 THR A 538     -23.776   2.588  76.840  1.00 19.54           O  
ANISOU 3939  OG1 THR A 538     2194   2377   2854     82     86    296       O  
ATOM   3940  CG2 THR A 538     -25.425   1.230  77.990  1.00 21.06           C  
ANISOU 3940  CG2 THR A 538     2420   2558   3026     75     72    303       C  
ATOM   3941  N   PRO A 539     -28.013   1.022  75.387  1.00 10.39           N  
ANISOU 3941  N   PRO A 539     1102   1216   1631     56    117    259       N  
ATOM   3942  CA  PRO A 539     -29.475   0.876  75.492  1.00 10.08           C  
ANISOU 3942  CA  PRO A 539     1079   1182   1569     43    116    254       C  
ATOM   3943  C   PRO A 539     -29.929   0.717  76.936  1.00 13.79           C  
ANISOU 3943  C   PRO A 539     1555   1651   2033     38     98    269       C  
ATOM   3944  O   PRO A 539     -29.260   0.048  77.726  1.00 14.02           O  
ANISOU 3944  O   PRO A 539     1582   1667   2079     45     89    283       O  
ATOM   3945  CB  PRO A 539     -29.771  -0.390  74.660  1.00 12.15           C  
ANISOU 3945  CB  PRO A 539     1351   1428   1839     43    131    241       C  
ATOM   3946  CG  PRO A 539     -28.486  -0.692  73.919  1.00 16.65           C  
ANISOU 3946  CG  PRO A 539     1909   1986   2431     57    145    236       C  
ATOM   3947  CD  PRO A 539     -27.396  -0.156  74.755  1.00 12.29           C  
ANISOU 3947  CD  PRO A 539     1340   1436   1894     66    132    252       C  
ATOM   3948  N   LEU A 540     -31.055   1.348  77.293  1.00  9.02           N  
ANISOU 3948  N   LEU A 540      959   1061   1406     26     93    269       N  
ATOM   3949  CA  LEU A 540     -31.588   1.271  78.647  1.00  8.22           C  
ANISOU 3949  CA  LEU A 540      866    962   1295     20     80    282       C  
ATOM   3950  C   LEU A 540     -32.220  -0.087  78.913  1.00 14.37           C  
ANISOU 3950  C   LEU A 540     1656   1726   2078     15     84    284       C  
ATOM   3951  O   LEU A 540     -32.381  -0.885  77.987  1.00 13.57           O  
ANISOU 3951  O   LEU A 540     1557   1614   1985     15     96    273       O  
ATOM   3952  CB  LEU A 540     -32.609   2.403  78.896  1.00  7.70           C  
ANISOU 3952  CB  LEU A 540      804    917   1206     11     78    279       C  
ATOM   3953  CG  LEU A 540     -32.052   3.844  78.831  1.00 10.84           C  
ANISOU 3953  CG  LEU A 540     1193   1327   1598     15     73    278       C  
ATOM   3954  CD1 LEU A 540     -33.123   4.853  79.175  1.00 10.21           C  
ANISOU 3954  CD1 LEU A 540     1119   1263   1496      8     72    275       C  
ATOM   3955  CD2 LEU A 540     -30.852   4.015  79.761  1.00 12.85           C  
ANISOU 3955  CD2 LEU A 540     1442   1576   1862     21     59    292       C  
ATOM   3956  N   TRP A 541     -32.559  -0.367  80.197  1.00 13.16           N  
ANISOU 3956  N   TRP A 541     1512   1570   1918     10     73    300       N  
ATOM   3957  CA  TRP A 541     -33.129  -1.659  80.617  1.00 12.84           C  
ANISOU 3957  CA  TRP A 541     1484   1514   1882      3     76    306       C  
ATOM   3958  C   TRP A 541     -34.313  -2.100  79.731  1.00 16.16           C  
ANISOU 3958  C   TRP A 541     1908   1934   2296     -9     90    290       C  
ATOM   3959  O   TRP A 541     -34.307  -3.221  79.215  1.00 15.55           O  
ANISOU 3959  O   TRP A 541     1836   1839   2234    -10     97    285       O  
ATOM   3960  CB  TRP A 541     -33.537  -1.610  82.099  1.00 11.67           C  
ANISOU 3960  CB  TRP A 541     1345   1369   1718     -4     64    324       C  
ATOM   3961  CG  TRP A 541     -34.276  -2.827  82.572  1.00 13.15           C  
ANISOU 3961  CG  TRP A 541     1547   1543   1907    -15     69    331       C  
ATOM   3962  CD1 TRP A 541     -33.755  -4.071  82.789  1.00 16.24           C  
ANISOU 3962  CD1 TRP A 541     1945   1909   2318    -10     66    343       C  
ATOM   3963  CD2 TRP A 541     -35.637  -2.880  83.011  1.00 13.30           C  
ANISOU 3963  CD2 TRP A 541     1575   1571   1909    -32     76    331       C  
ATOM   3964  NE1 TRP A 541     -34.727  -4.911  83.277  1.00 15.84           N  
ANISOU 3964  NE1 TRP A 541     1909   1849   2261    -24     72    349       N  
ATOM   3965  CE2 TRP A 541     -35.893  -4.205  83.425  1.00 17.56           C  
ANISOU 3965  CE2 TRP A 541     2127   2089   2457    -39     78    342       C  
ATOM   3966  CE3 TRP A 541     -36.680  -1.939  83.070  1.00 14.64           C  
ANISOU 3966  CE3 TRP A 541     1742   1764   2058    -41     82    323       C  
ATOM   3967  CZ2 TRP A 541     -37.157  -4.620  83.867  1.00 17.22           C  
ANISOU 3967  CZ2 TRP A 541     2092   2048   2402    -57     87    345       C  
ATOM   3968  CZ3 TRP A 541     -37.920  -2.344  83.545  1.00 16.42           C  
ANISOU 3968  CZ3 TRP A 541     1974   1992   2272    -57     90    326       C  
ATOM   3969  CH2 TRP A 541     -38.153  -3.669  83.923  1.00 17.14           C  
ANISOU 3969  CH2 TRP A 541     2077   2064   2373    -66     94    336       C  
ATOM   3970  N   TRP A 542     -35.296  -1.202  79.513  1.00 12.86           N  
ANISOU 3970  N   TRP A 542     1488   1538   1860    -18     93    281       N  
ATOM   3971  CA  TRP A 542     -36.482  -1.525  78.702  1.00 12.31           C  
ANISOU 3971  CA  TRP A 542     1420   1472   1784    -30    103    267       C  
ATOM   3972  C   TRP A 542     -36.192  -1.504  77.187  1.00 16.54           C  
ANISOU 3972  C   TRP A 542     1952   2008   2326    -26    111    248       C  
ATOM   3973  O   TRP A 542     -37.060  -1.863  76.392  1.00 16.92           O  
ANISOU 3973  O   TRP A 542     2002   2058   2370    -37    117    235       O  
ATOM   3974  CB  TRP A 542     -37.660  -0.587  79.049  1.00 10.59           C  
ANISOU 3974  CB  TRP A 542     1199   1278   1547    -40    103    265       C  
ATOM   3975  CG  TRP A 542     -37.290   0.869  79.105  1.00 10.99           C  
ANISOU 3975  CG  TRP A 542     1242   1345   1587    -31     98    265       C  
ATOM   3976  CD1 TRP A 542     -36.961   1.590  80.217  1.00 13.73           C  
ANISOU 3976  CD1 TRP A 542     1591   1699   1926    -27     90    277       C  
ATOM   3977  CD2 TRP A 542     -37.268   1.790  78.006  1.00 10.46           C  
ANISOU 3977  CD2 TRP A 542     1168   1291   1517    -26    100    253       C  
ATOM   3978  NE1 TRP A 542     -36.726   2.902  79.878  1.00 13.05           N  
ANISOU 3978  NE1 TRP A 542     1498   1627   1834    -20     87    272       N  
ATOM   3979  CE2 TRP A 542     -36.896   3.051  78.523  1.00 14.45           C  
ANISOU 3979  CE2 TRP A 542     1670   1808   2014    -19     94    258       C  
ATOM   3980  CE3 TRP A 542     -37.513   1.670  76.624  1.00 11.42           C  
ANISOU 3980  CE3 TRP A 542     1286   1414   1638    -28    106    238       C  
ATOM   3981  CZ2 TRP A 542     -36.747   4.186  77.704  1.00 13.63           C  
ANISOU 3981  CZ2 TRP A 542     1559   1715   1905    -14     94    251       C  
ATOM   3982  CZ3 TRP A 542     -37.372   2.796  75.818  1.00 12.80           C  
ANISOU 3982  CZ3 TRP A 542     1455   1602   1805    -22    106    232       C  
ATOM   3983  CH2 TRP A 542     -37.000   4.034  76.359  1.00 13.31           C  
ANISOU 3983  CH2 TRP A 542     1516   1676   1864    -15    100    239       C  
ATOM   3984  N   ASP A 543     -34.959  -1.117  76.796  1.00 12.41           N  
ANISOU 3984  N   ASP A 543     1422   1481   1811    -12    111    248       N  
ATOM   3985  CA  ASP A 543     -34.573  -1.029  75.383  1.00 11.61           C  
ANISOU 3985  CA  ASP A 543     1318   1380   1713     -7    121    231       C  
ATOM   3986  C   ASP A 543     -33.743  -2.264  74.961  1.00 15.30           C  
ANISOU 3986  C   ASP A 543     1789   1821   2201      0    129    227       C  
ATOM   3987  O   ASP A 543     -32.597  -2.419  75.393  1.00 14.50           O  
ANISOU 3987  O   ASP A 543     1683   1710   2118     14    127    237       O  
ATOM   3988  CB  ASP A 543     -33.783   0.279  75.126  1.00 12.83           C  
ANISOU 3988  CB  ASP A 543     1463   1549   1864      3    119    233       C  
ATOM   3989  CG  ASP A 543     -33.481   0.568  73.659  1.00 17.09           C  
ANISOU 3989  CG  ASP A 543     2000   2092   2400      5    131    217       C  
ATOM   3990  OD1 ASP A 543     -33.605  -0.363  72.830  1.00 18.43           O  
ANISOU 3990  OD1 ASP A 543     2177   2251   2574      3    141    204       O  
ATOM   3991  OD2 ASP A 543     -33.080   1.705  73.353  1.00 16.17           O  
ANISOU 3991  OD2 ASP A 543     1877   1989   2278     10    130    218       O  
ATOM   3992  N   LYS A 544     -34.329  -3.135  74.126  1.00 11.66           N  
ANISOU 3992  N   LYS A 544     1338   1351   1741     -8    139    212       N  
ATOM   3993  CA  LYS A 544     -33.647  -4.337  73.638  1.00 11.84           C  
ANISOU 3993  CA  LYS A 544     1368   1348   1784     -2    150    204       C  
ATOM   3994  C   LYS A 544     -33.176  -4.139  72.180  1.00 16.96           C  
ANISOU 3994  C   LYS A 544     2016   1999   2430      3    164    184       C  
ATOM   3995  O   LYS A 544     -32.831  -5.115  71.501  1.00 17.75           O  
ANISOU 3995  O   LYS A 544     2124   2078   2542      6    177    170       O  
ATOM   3996  CB  LYS A 544     -34.584  -5.568  73.735  1.00 13.70           C  
ANISOU 3996  CB  LYS A 544     1617   1566   2023    -16    152    199       C  
ATOM   3997  CG  LYS A 544     -34.974  -5.950  75.170  1.00 19.89           C  
ANISOU 3997  CG  LYS A 544     2404   2343   2810    -22    141    220       C  
ATOM   3998  CD  LYS A 544     -33.806  -6.573  75.932  1.00 22.49           C  
ANISOU 3998  CD  LYS A 544     2733   2649   3163     -5    138    237       C  
ATOM   3999  CE  LYS A 544     -34.218  -7.021  77.308  1.00 24.08           C  
ANISOU 3999  CE  LYS A 544     2941   2844   3365    -12    127    258       C  
ATOM   4000  NZ  LYS A 544     -33.089  -7.629  78.049  1.00 27.09           N  
ANISOU 4000  NZ  LYS A 544     3321   3202   3768      5    121    277       N  
ATOM   4001  N   ASN A 545     -33.153  -2.857  71.705  1.00 12.75           N  
ANISOU 4001  N   ASN A 545     1475   1490   1880      4    163    182       N  
ATOM   4002  CA  ASN A 545     -32.842  -2.510  70.305  1.00 11.97           C  
ANISOU 4002  CA  ASN A 545     1378   1397   1772      6    177    164       C  
ATOM   4003  C   ASN A 545     -33.755  -3.255  69.330  1.00 14.41           C  
ANISOU 4003  C   ASN A 545     1703   1702   2068     -8    183    144       C  
ATOM   4004  O   ASN A 545     -33.329  -3.624  68.230  1.00 13.92           O  
ANISOU 4004  O   ASN A 545     1650   1633   2005     -6    198    126       O  
ATOM   4005  CB  ASN A 545     -31.353  -2.745  69.985  1.00 13.50           C  
ANISOU 4005  CB  ASN A 545     1565   1577   1986     24    191    163       C  
ATOM   4006  CG  ASN A 545     -30.429  -1.778  70.688  1.00 34.34           C  
ANISOU 4006  CG  ASN A 545     4186   4225   4635     35    184    181       C  
ATOM   4007  OD1 ASN A 545     -30.861  -0.786  71.287  1.00 29.02           O  
ANISOU 4007  OD1 ASN A 545     3507   3569   3948     30    170    192       O  
ATOM   4008  ND2 ASN A 545     -29.142  -2.041  70.624  1.00 28.37           N  
ANISOU 4008  ND2 ASN A 545     3419   3457   3902     51    194    183       N  
ATOM   4009  N   SER A 546     -35.027  -3.468  69.735  1.00 10.61           N  
ANISOU 4009  N   SER A 546     1226   1227   1578    -24    171    145       N  
ATOM   4010  CA  SER A 546     -36.022  -4.132  68.904  1.00  9.99           C  
ANISOU 4010  CA  SER A 546     1161   1146   1487    -42    172    127       C  
ATOM   4011  C   SER A 546     -36.378  -3.269  67.719  1.00 14.57           C  
ANISOU 4011  C   SER A 546     1744   1750   2043    -47    172    115       C  
ATOM   4012  O   SER A 546     -36.621  -2.064  67.879  1.00 14.41           O  
ANISOU 4012  O   SER A 546     1714   1752   2010    -45    163    125       O  
ATOM   4013  CB  SER A 546     -37.278  -4.432  69.716  1.00 11.49           C  
ANISOU 4013  CB  SER A 546     1350   1340   1675    -58    159    134       C  
ATOM   4014  OG  SER A 546     -37.002  -5.279  70.818  1.00 18.09           O  
ANISOU 4014  OG  SER A 546     2187   2153   2532    -55    159    147       O  
ATOM   4015  N   ASN A 547     -36.393  -3.857  66.525  1.00 11.08           N  
ANISOU 4015  N   ASN A 547     1316   1301   1592    -53    182     93       N  
ATOM   4016  CA  ASN A 547     -36.783  -3.141  65.325  1.00 10.92           C  
ANISOU 4016  CA  ASN A 547     1302   1302   1544    -60    181     81       C  
ATOM   4017  C   ASN A 547     -38.094  -3.659  64.798  1.00 15.68           C  
ANISOU 4017  C   ASN A 547     1916   1911   2133    -82    169     67       C  
ATOM   4018  O   ASN A 547     -38.202  -4.842  64.460  1.00 15.38           O  
ANISOU 4018  O   ASN A 547     1891   1852   2100    -91    176     51       O  
ATOM   4019  CB  ASN A 547     -35.705  -3.248  64.251  1.00 10.34           C  
ANISOU 4019  CB  ASN A 547     1240   1221   1467    -50    202     67       C  
ATOM   4020  CG  ASN A 547     -36.144  -2.701  62.903  1.00 26.53           C  
ANISOU 4020  CG  ASN A 547     3303   3291   3485    -60    201     53       C  
ATOM   4021  OD1 ASN A 547     -36.588  -1.558  62.785  1.00 20.13           O  
ANISOU 4021  OD1 ASN A 547     2485   2505   2658    -62    188     64       O  
ATOM   4022  ND2 ASN A 547     -36.031  -3.515  61.863  1.00 13.47           N  
ANISOU 4022  ND2 ASN A 547     1669   1627   1822    -67    214     30       N  
ATOM   4023  N   TYR A 548     -39.094  -2.779  64.692  1.00 12.56           N  
ANISOU 4023  N   TYR A 548     1512   1540   1719    -91    152     74       N  
ATOM   4024  CA  TYR A 548     -40.374  -3.137  64.098  1.00 13.15           C  
ANISOU 4024  CA  TYR A 548     1593   1625   1779   -112    138     61       C  
ATOM   4025  C   TYR A 548     -40.647  -2.312  62.839  1.00 16.89           C  
ANISOU 4025  C   TYR A 548     2073   2121   2222   -116    131     54       C  
ATOM   4026  O   TYR A 548     -41.741  -2.388  62.269  1.00 16.26           O  
ANISOU 4026  O   TYR A 548     1995   2055   2127   -133    115     45       O  
ATOM   4027  CB  TYR A 548     -41.509  -2.998  65.118  1.00 14.85           C  
ANISOU 4027  CB  TYR A 548     1791   1850   2002   -122    122     75       C  
ATOM   4028  CG  TYR A 548     -41.603  -4.172  66.064  1.00 18.27           C  
ANISOU 4028  CG  TYR A 548     2224   2258   2458   -128    127     77       C  
ATOM   4029  CD1 TYR A 548     -42.288  -5.329  65.705  1.00 20.85           C  
ANISOU 4029  CD1 TYR A 548     2562   2572   2787   -149    124     61       C  
ATOM   4030  CD2 TYR A 548     -40.985  -4.140  67.310  1.00 19.60           C  
ANISOU 4030  CD2 TYR A 548     2385   2416   2646   -115    133     95       C  
ATOM   4031  CE1 TYR A 548     -42.376  -6.417  66.572  1.00 22.87           C  
ANISOU 4031  CE1 TYR A 548     2820   2803   3065   -156    129     64       C  
ATOM   4032  CE2 TYR A 548     -41.059  -5.225  68.184  1.00 20.93           C  
ANISOU 4032  CE2 TYR A 548     2557   2562   2835   -121    136     99       C  
ATOM   4033  CZ  TYR A 548     -41.756  -6.364  67.810  1.00 30.68           C  
ANISOU 4033  CZ  TYR A 548     3802   3782   4072   -141    136     84       C  
ATOM   4034  OH  TYR A 548     -41.837  -7.436  68.667  1.00 34.52           O  
ANISOU 4034  OH  TYR A 548     4294   4244   4580   -148    140     90       O  
ATOM   4035  N   CYS A 549     -39.618  -1.589  62.354  1.00 13.73           N  
ANISOU 4035  N   CYS A 549     1677   1726   1815   -101    144     56       N  
ATOM   4036  CA  CYS A 549     -39.704  -0.844  61.105  1.00 13.44           C  
ANISOU 4036  CA  CYS A 549     1650   1708   1747   -103    141     50       C  
ATOM   4037  C   CYS A 549     -39.430  -1.771  59.920  1.00 17.92           C  
ANISOU 4037  C   CYS A 549     2244   2265   2300   -113    153     24       C  
ATOM   4038  O   CYS A 549     -38.432  -2.493  59.920  1.00 17.85           O  
ANISOU 4038  O   CYS A 549     2244   2234   2305   -105    176     14       O  
ATOM   4039  CB  CYS A 549     -38.747   0.348  61.118  1.00 13.15           C  
ANISOU 4039  CB  CYS A 549     1608   1680   1709    -85    150     66       C  
ATOM   4040  SG  CYS A 549     -38.752   1.322  59.593  1.00 16.70           S  
ANISOU 4040  SG  CYS A 549     2073   2152   2121    -88    148     62       S  
ATOM   4041  N   THR A 550     -40.354  -1.809  58.948  1.00 15.12           N  
ANISOU 4041  N   THR A 550     1901   1924   1918   -131    137     12       N  
ATOM   4042  CA  THR A 550     -40.216  -2.668  57.769  1.00 15.47           C  
ANISOU 4042  CA  THR A 550     1974   1961   1943   -143    147    -16       C  
ATOM   4043  C   THR A 550     -40.110  -1.824  56.479  1.00 19.59           C  
ANISOU 4043  C   THR A 550     2512   2504   2427   -145    146    -19       C  
ATOM   4044  O   THR A 550     -40.261  -2.360  55.376  1.00 18.25           O  
ANISOU 4044  O   THR A 550     2368   2335   2232   -159    147    -41       O  
ATOM   4045  CB  THR A 550     -41.385  -3.690  57.699  1.00 23.16           C  
ANISOU 4045  CB  THR A 550     2954   2929   2917   -168    129    -32       C  
ATOM   4046  OG1 THR A 550     -42.616  -2.985  57.538  1.00 23.41           O  
ANISOU 4046  OG1 THR A 550     2974   2989   2933   -180     99    -22       O  
ATOM   4047  CG2 THR A 550     -41.452  -4.589  58.930  1.00 20.08           C  
ANISOU 4047  CG2 THR A 550     2551   2515   2563   -168    133    -28       C  
ATOM   4048  N   SER A 551     -39.842  -0.497  56.623  1.00 16.93           N  
ANISOU 4048  N   SER A 551     2163   2185   2086   -131    143      4       N  
ATOM   4049  CA  SER A 551     -39.697   0.399  55.470  1.00 17.12           C  
ANISOU 4049  CA  SER A 551     2201   2228   2074   -131    142      6       C  
ATOM   4050  C   SER A 551     -38.518  -0.026  54.588  1.00 22.18           C  
ANISOU 4050  C   SER A 551     2867   2857   2703   -127    175    -12       C  
ATOM   4051  O   SER A 551     -37.449  -0.371  55.104  1.00 21.40           O  
ANISOU 4051  O   SER A 551     2762   2739   2630   -113    201    -13       O  
ATOM   4052  CB  SER A 551     -39.517   1.843  55.930  1.00 20.13           C  
ANISOU 4052  CB  SER A 551     2564   2624   2459   -116    136     35       C  
ATOM   4053  OG  SER A 551     -40.689   2.335  56.564  1.00 27.41           O  
ANISOU 4053  OG  SER A 551     3467   3561   3388   -119    107     50       O  
ATOM   4054  N   SER A 552     -38.723  -0.038  53.261  1.00 19.13           N  
ANISOU 4054  N   SER A 552     2508   2483   2276   -140    173    -27       N  
ATOM   4055  CA  SER A 552     -37.692  -0.455  52.311  1.00 19.02           C  
ANISOU 4055  CA  SER A 552     2521   2459   2246   -138    206    -47       C  
ATOM   4056  C   SER A 552     -36.647   0.650  52.082  1.00 22.98           C  
ANISOU 4056  C   SER A 552     3020   2969   2742   -122    227    -29       C  
ATOM   4057  O   SER A 552     -35.507   0.352  51.721  1.00 23.07           O  
ANISOU 4057  O   SER A 552     3042   2968   2757   -114    263    -40       O  
ATOM   4058  CB  SER A 552     -38.325  -0.865  50.984  1.00 22.78           C  
ANISOU 4058  CB  SER A 552     3031   2946   2678   -160    197    -70       C  
ATOM   4059  OG  SER A 552     -39.096   0.192  50.437  1.00 31.74           O  
ANISOU 4059  OG  SER A 552     4168   4110   3781   -167    168    -53       O  
ATOM   4060  N   LYS A 553     -37.041   1.928  52.278  1.00 19.18           N  
ANISOU 4060  N   LYS A 553     2525   2508   2254   -118    207     -2       N  
ATOM   4061  CA  LYS A 553     -36.137   3.069  52.074  1.00 19.97           C  
ANISOU 4061  CA  LYS A 553     2623   2616   2350   -106    224     17       C  
ATOM   4062  C   LYS A 553     -36.252   4.075  53.237  1.00 23.83           C  
ANISOU 4062  C   LYS A 553     3080   3108   2866    -93    208     46       C  
ATOM   4063  O   LYS A 553     -37.368   4.239  53.778  1.00 24.68           O  
ANISOU 4063  O   LYS A 553     3174   3224   2979    -97    177     55       O  
ATOM   4064  CB  LYS A 553     -36.441   3.762  50.727  1.00 22.43           C  
ANISOU 4064  CB  LYS A 553     2962   2950   2612   -117    217     19       C  
ATOM   4065  CG  LYS A 553     -35.405   4.808  50.325  1.00 36.84           C  
ANISOU 4065  CG  LYS A 553     4789   4779   4427   -107    241     35       C  
ATOM   4066  NZ  LYS A 553     -35.262   7.526  44.623  1.00 21.59           N  
ANISOU 4066  NZ  LYS A 553     3000   2926   2277   -149    256     58       N  
ATOM   4067  OXT LYS A 553     -35.218   4.659  53.625  1.00 39.17           O  
ANISOU 4067  OXT LYS A 553     5010   5045   4827    -79    229     59       O  
TER    4068      LYS A 553                                                      
ATOM   4069  N   ASN B  39     -47.492 -19.130  93.458  1.00 36.27           N  
ANISOU 4069  N   ASN B  39     4799   4703   4280    395   -674   -147       N  
ATOM   4070  CA  ASN B  39     -47.347 -18.224  94.590  1.00 35.10           C  
ANISOU 4070  CA  ASN B  39     4603   4556   4176    366   -625   -105       C  
ATOM   4071  C   ASN B  39     -48.221 -18.677  95.782  1.00 37.70           C  
ANISOU 4071  C   ASN B  39     4884   4850   4592    332   -652   -102       C  
ATOM   4072  O   ASN B  39     -49.273 -18.074  96.055  1.00 37.30           O  
ANISOU 4072  O   ASN B  39     4807   4787   4577    313   -674    -77       O  
ATOM   4073  CB  ASN B  39     -47.681 -16.786  94.182  1.00 35.51           C  
ANISOU 4073  CB  ASN B  39     4659   4628   4205    366   -612    -64       C  
HETATM 4074  N   MSE B  40     -47.794 -19.753  96.477  1.00 33.34           N  
ANISOU 4074  N   MSE B  40     4318   4279   4071    325   -649   -126       N  
HETATM 4075  CA  MSE B  40     -48.514 -20.268  97.654  1.00 32.44           C  
ANISOU 4075  CA  MSE B  40     4158   4131   4035    293   -669   -122       C  
HETATM 4076  C   MSE B  40     -48.055 -19.540  98.931  1.00 34.66           C  
ANISOU 4076  C   MSE B  40     4399   4418   4353    270   -608    -87       C  
HETATM 4077  O   MSE B  40     -47.269 -20.091  99.722  1.00 34.28           O  
ANISOU 4077  O   MSE B  40     4338   4364   4323    264   -579    -95       O  
HETATM 4078  CB  MSE B  40     -48.317 -21.792  97.794  1.00 34.90           C  
ANISOU 4078  CB  MSE B  40     4477   4418   4366    297   -699   -164       C  
ATOM   4079  N   ASN B  41     -48.540 -18.301  99.128  1.00 29.42           N  
ANISOU 4079  N   ASN B  41     3718   3763   3698    258   -592    -49       N  
ATOM   4080  CA  ASN B  41     -48.133 -17.458 100.252  1.00 27.84           C  
ANISOU 4080  CA  ASN B  41     3485   3568   3525    238   -536    -16       C  
ATOM   4081  C   ASN B  41     -48.935 -17.760 101.522  1.00 29.95           C  
ANISOU 4081  C   ASN B  41     3707   3806   3866    208   -546     -5       C  
ATOM   4082  O   ASN B  41     -48.513 -17.373 102.613  1.00 29.52           O  
ANISOU 4082  O   ASN B  41     3628   3752   3837    191   -502     15       O  
ATOM   4083  CB  ASN B  41     -48.274 -15.965  99.888  1.00 28.08           C  
ANISOU 4083  CB  ASN B  41     3518   3619   3531    241   -512     19       C  
ATOM   4084  CG  ASN B  41     -47.510 -15.557  98.651  1.00 44.00           C  
ANISOU 4084  CG  ASN B  41     5578   5667   5474    269   -498     15       C  
ATOM   4085  OD1 ASN B  41     -48.087 -15.084  97.666  1.00 34.78           O  
ANISOU 4085  OD1 ASN B  41     4433   4506   4274    283   -526     21       O  
ATOM   4086  ND2 ASN B  41     -46.192 -15.701  98.688  1.00 34.63           N  
ANISOU 4086  ND2 ASN B  41     4402   4498   4259    279   -452      8       N  
ATOM   4087  N   GLU B  42     -50.133 -18.378 101.380  1.00 24.95           N  
ANISOU 4087  N   GLU B  42     3065   3148   3268    200   -603    -15       N  
ATOM   4088  CA  GLU B  42     -51.008 -18.613 102.538  1.00 23.68           C  
ANISOU 4088  CA  GLU B  42     2859   2959   3178    172   -611      1       C  
ATOM   4089  C   GLU B  42     -50.376 -19.537 103.614  1.00 25.44           C  
ANISOU 4089  C   GLU B  42     3067   3168   3432    158   -589     -9       C  
ATOM   4090  O   GLU B  42     -50.289 -19.135 104.774  1.00 24.39           O  
ANISOU 4090  O   GLU B  42     2905   3032   3330    140   -551     14       O  
ATOM   4091  CB  GLU B  42     -52.398 -19.106 102.114  1.00 25.20           C  
ANISOU 4091  CB  GLU B  42     3042   3128   3406    166   -678     -6       C  
ATOM   4092  CG  GLU B  42     -53.332 -19.322 103.292  1.00 31.65           C  
ANISOU 4092  CG  GLU B  42     3810   3918   4299    137   -682     13       C  
ATOM   4093  CD  GLU B  42     -54.796 -19.177 102.961  1.00 43.17           C  
ANISOU 4093  CD  GLU B  42     5247   5361   5796    129   -732     24       C  
ATOM   4094  OE1 GLU B  42     -55.470 -20.215 102.783  1.00 31.80           O  
ANISOU 4094  OE1 GLU B  42     3799   3894   4390    121   -785      6       O  
ATOM   4095  OE2 GLU B  42     -55.278 -18.022 102.895  1.00 33.74           O  
ANISOU 4095  OE2 GLU B  42     4042   4178   4601    130   -720     52       O  
ATOM   4096  N   PRO B  43     -49.901 -20.775 103.255  1.00 21.02           N  
ANISOU 4096  N   PRO B  43     2528   2598   2861    169   -613    -45       N  
ATOM   4097  CA  PRO B  43     -49.258 -21.626 104.277  1.00 20.16           C  
ANISOU 4097  CA  PRO B  43     2404   2475   2780    158   -593    -52       C  
ATOM   4098  C   PRO B  43     -48.024 -20.952 104.882  1.00 21.85           C  
ANISOU 4098  C   PRO B  43     2618   2713   2972    160   -528    -38       C  
ATOM   4099  O   PRO B  43     -47.757 -21.108 106.072  1.00 21.31           O  
ANISOU 4099  O   PRO B  43     2525   2635   2936    143   -502    -25       O  
ATOM   4100  CB  PRO B  43     -48.888 -22.902 103.499  1.00 22.44           C  
ANISOU 4100  CB  PRO B  43     2724   2752   3049    177   -630    -95       C  
ATOM   4101  CG  PRO B  43     -49.727 -22.860 102.261  1.00 27.31           C  
ANISOU 4101  CG  PRO B  43     3362   3368   3645    190   -683   -109       C  
ATOM   4102  CD  PRO B  43     -49.893 -21.425 101.929  1.00 22.94           C  
ANISOU 4102  CD  PRO B  43     2810   2843   3064    194   -659    -80       C  
ATOM   4103  N   ARG B  44     -47.309 -20.140 104.067  1.00 17.76           N  
ANISOU 4103  N   ARG B  44     2124   2225   2397    180   -503    -36       N  
ATOM   4104  CA  ARG B  44     -46.141 -19.383 104.517  1.00 16.78           C  
ANISOU 4104  CA  ARG B  44     1998   2125   2252    182   -444    -20       C  
ATOM   4105  C   ARG B  44     -46.547 -18.322 105.549  1.00 20.26           C  
ANISOU 4105  C   ARG B  44     2409   2565   2725    158   -415     17       C  
ATOM   4106  O   ARG B  44     -45.986 -18.285 106.645  1.00 19.07           O  
ANISOU 4106  O   ARG B  44     2239   2411   2594    145   -382     28       O  
ATOM   4107  CB  ARG B  44     -45.436 -18.722 103.318  1.00 17.34           C  
ANISOU 4107  CB  ARG B  44     2101   2227   2258    208   -427    -23       C  
ATOM   4108  CG  ARG B  44     -44.219 -17.893 103.715  1.00 28.06           C  
ANISOU 4108  CG  ARG B  44     3455   3609   3598    208   -366     -4       C  
ATOM   4109  CD  ARG B  44     -43.602 -17.178 102.528  1.00 38.13           C  
ANISOU 4109  CD  ARG B  44     4760   4916   4813    231   -346     -2       C  
ATOM   4110  NE  ARG B  44     -42.897 -18.099 101.637  1.00 49.75           N  
ANISOU 4110  NE  ARG B  44     6262   6397   6245    259   -354    -35       N  
ATOM   4111  CZ  ARG B  44     -41.617 -18.429 101.779  1.00 66.25           C  
ANISOU 4111  CZ  ARG B  44     8351   8499   8320    269   -317    -45       C  
ATOM   4112  NH1 ARG B  44     -40.907 -17.942 102.790  1.00 53.54           N  
ANISOU 4112  NH1 ARG B  44     6714   6893   6735    252   -276    -24       N  
ATOM   4113  NH2 ARG B  44     -41.043 -19.262 100.924  1.00 55.26           N  
ANISOU 4113  NH2 ARG B  44     6988   7116   6893    298   -324    -77       N  
ATOM   4114  N   LEU B  45     -47.549 -17.474 105.204  1.00 16.82           N  
ANISOU 4114  N   LEU B  45     1968   2130   2293    155   -429     37       N  
ATOM   4115  CA  LEU B  45     -48.050 -16.430 106.107  1.00 16.33           C  
ANISOU 4115  CA  LEU B  45     1878   2065   2261    136   -403     70       C  
ATOM   4116  C   LEU B  45     -48.668 -17.041 107.375  1.00 19.86           C  
ANISOU 4116  C   LEU B  45     2293   2485   2767    113   -408     76       C  
ATOM   4117  O   LEU B  45     -48.565 -16.455 108.452  1.00 19.12           O  
ANISOU 4117  O   LEU B  45     2180   2390   2694     98   -373     98       O  
ATOM   4118  CB  LEU B  45     -49.084 -15.552 105.381  1.00 16.71           C  
ANISOU 4118  CB  LEU B  45     1928   2117   2306    140   -425     87       C  
ATOM   4119  CG  LEU B  45     -49.630 -14.362 106.178  1.00 21.42           C  
ANISOU 4119  CG  LEU B  45     2499   2710   2930    126   -398    121       C  
ATOM   4120  CD1 LEU B  45     -48.543 -13.314 106.422  1.00 21.35           C  
ANISOU 4120  CD1 LEU B  45     2499   2721   2892    128   -346    137       C  
ATOM   4121  CD2 LEU B  45     -50.791 -13.744 105.477  1.00 22.91           C  
ANISOU 4121  CD2 LEU B  45     2686   2897   3124    131   -430    134       C  
ATOM   4122  N   ALA B  46     -49.316 -18.223 107.241  1.00 16.76           N  
ANISOU 4122  N   ALA B  46     1897   2071   2400    110   -452     57       N  
ATOM   4123  CA  ALA B  46     -49.916 -18.929 108.383  1.00 16.25           C  
ANISOU 4123  CA  ALA B  46     1802   1980   2392     88   -458     64       C  
ATOM   4124  C   ALA B  46     -48.843 -19.400 109.364  1.00 18.91           C  
ANISOU 4124  C   ALA B  46     2137   2315   2731     82   -424     61       C  
ATOM   4125  O   ALA B  46     -49.051 -19.349 110.574  1.00 18.78           O  
ANISOU 4125  O   ALA B  46     2099   2289   2750     64   -403     79       O  
ATOM   4126  CB  ALA B  46     -50.728 -20.118 107.894  1.00 17.32           C  
ANISOU 4126  CB  ALA B  46     1936   2090   2553     87   -515     43       C  
ATOM   4127  N   SER B  47     -47.686 -19.846 108.841  1.00 15.06           N  
ANISOU 4127  N   SER B  47     1676   1840   2206     99   -419     37       N  
ATOM   4128  CA  SER B  47     -46.592 -20.351 109.674  1.00 14.70           C  
ANISOU 4128  CA  SER B  47     1628   1793   2162     96   -391     32       C  
ATOM   4129  C   SER B  47     -45.858 -19.217 110.426  1.00 17.38           C  
ANISOU 4129  C   SER B  47     1962   2152   2490     90   -340     55       C  
ATOM   4130  O   SER B  47     -45.101 -19.495 111.356  1.00 17.00           O  
ANISOU 4130  O   SER B  47     1908   2101   2452     83   -317     57       O  
ATOM   4131  CB  SER B  47     -45.603 -21.154 108.831  1.00 18.90           C  
ANISOU 4131  CB  SER B  47     2188   2333   2660    119   -402     -1       C  
ATOM   4132  OG  SER B  47     -44.965 -20.338 107.863  1.00 27.91           O  
ANISOU 4132  OG  SER B  47     3351   3504   3751    138   -383     -3       O  
ATOM   4133  N   THR B  48     -46.092 -17.935 110.026  1.00 13.02           N  
ANISOU 4133  N   THR B  48     1412   1617   1920     93   -324     73       N  
ATOM   4134  CA  THR B  48     -45.434 -16.785 110.680  1.00 11.96           C  
ANISOU 4134  CA  THR B  48     1272   1497   1776     86   -279     95       C  
ATOM   4135  C   THR B  48     -46.176 -16.348 111.947  1.00 16.48           C  
ANISOU 4135  C   THR B  48     1820   2055   2387     66   -265    119       C  
ATOM   4136  O   THR B  48     -45.657 -15.531 112.712  1.00 16.55           O  
ANISOU 4136  O   THR B  48     1825   2069   2393     58   -230    134       O  
ATOM   4137  CB  THR B  48     -45.243 -15.611 109.685  1.00 16.40           C  
ANISOU 4137  CB  THR B  48     1849   2082   2300     99   -266    104       C  
ATOM   4138  OG1 THR B  48     -46.521 -15.101 109.300  1.00 14.85           O  
ANISOU 4138  OG1 THR B  48     1648   1880   2116     97   -288    117       O  
ATOM   4139  CG2 THR B  48     -44.441 -16.011 108.452  1.00 15.47           C  
ANISOU 4139  CG2 THR B  48     1758   1982   2139    122   -273     82       C  
ATOM   4140  N   LEU B  49     -47.393 -16.891 112.175  1.00 13.90           N  
ANISOU 4140  N   LEU B  49     1477   1707   2096     56   -292    122       N  
ATOM   4141  CA  LEU B  49     -48.177 -16.558 113.371  1.00 13.49           C  
ANISOU 4141  CA  LEU B  49     1402   1641   2082     39   -276    145       C  
ATOM   4142  C   LEU B  49     -47.521 -17.117 114.633  1.00 16.13           C  
ANISOU 4142  C   LEU B  49     1731   1967   2429     27   -256    146       C  
ATOM   4143  O   LEU B  49     -47.016 -16.344 115.452  1.00 14.96           O  
ANISOU 4143  O   LEU B  49     1584   1826   2276     22   -221    160       O  
ATOM   4144  CB  LEU B  49     -49.627 -17.059 113.233  1.00 13.96           C  
ANISOU 4144  CB  LEU B  49     1442   1682   2181     32   -310    150       C  
ATOM   4145  CG  LEU B  49     -50.534 -16.191 112.344  1.00 18.67           C  
ANISOU 4145  CG  LEU B  49     2036   2284   2775     39   -326    159       C  
ATOM   4146  CD1 LEU B  49     -51.704 -16.987 111.814  1.00 18.85           C  
ANISOU 4146  CD1 LEU B  49     2045   2289   2829     37   -374    153       C  
ATOM   4147  CD2 LEU B  49     -51.012 -14.952 113.092  1.00 20.72           C  
ANISOU 4147  CD2 LEU B  49     2280   2545   3047     33   -293    187       C  
ATOM   4148  N   ARG B  50     -47.438 -18.464 114.750  1.00 12.37           N  
ANISOU 4148  N   ARG B  50     1255   1476   1970     25   -278    131       N  
ATOM   4149  CA  ARG B  50     -46.739 -19.090 115.874  1.00 11.87           C  
ANISOU 4149  CA  ARG B  50     1190   1404   1916     16   -263    132       C  
ATOM   4150  C   ARG B  50     -45.233 -18.932 115.721  1.00 15.95           C  
ANISOU 4150  C   ARG B  50     1724   1938   2397     27   -245    119       C  
ATOM   4151  O   ARG B  50     -44.519 -18.756 116.719  1.00 15.30           O  
ANISOU 4151  O   ARG B  50     1642   1858   2314     20   -220    127       O  
ATOM   4152  CB  ARG B  50     -47.107 -20.578 115.999  1.00 10.58           C  
ANISOU 4152  CB  ARG B  50     1022   1216   1782     11   -295    121       C  
ATOM   4153  CG  ARG B  50     -48.531 -20.817 116.459  1.00 14.93           C  
ANISOU 4153  CG  ARG B  50     1549   1746   2377     -5   -307    139       C  
ATOM   4154  CD  ARG B  50     -48.699 -22.213 117.015  1.00 16.26           C  
ANISOU 4154  CD  ARG B  50     1711   1889   2579    -16   -327    136       C  
ATOM   4155  NE  ARG B  50     -50.087 -22.497 117.369  1.00 13.95           N  
ANISOU 4155  NE  ARG B  50     1392   1575   2333    -32   -339    155       N  
ATOM   4156  CZ  ARG B  50     -50.933 -23.139 116.574  1.00 21.34           C  
ANISOU 4156  CZ  ARG B  50     2319   2495   3293    -33   -381    146       C  
ATOM   4157  NH1 ARG B  50     -50.533 -23.582 115.387  1.00 10.17           N  
ANISOU 4157  NH1 ARG B  50      924   1083   1858    -19   -415    116       N  
ATOM   4158  NH2 ARG B  50     -52.182 -23.354 116.961  1.00  5.75           N  
ANISOU 4158  NH2 ARG B  50      484    415   1285    -53   -297    160       N  
ATOM   4159  N   GLY B  51     -44.761 -18.986 114.470  1.00 12.48           N  
ANISOU 4159  N   GLY B  51     1300   1512   1928     45   -258    100       N  
ATOM   4160  CA  GLY B  51     -43.343 -18.866 114.149  1.00 12.15           C  
ANISOU 4160  CA  GLY B  51     1272   1490   1854     57   -240     88       C  
ATOM   4161  C   GLY B  51     -42.733 -17.558 114.602  1.00 14.58           C  
ANISOU 4161  C   GLY B  51     1578   1814   2147     53   -202    106       C  
ATOM   4162  O   GLY B  51     -41.676 -17.551 115.242  1.00 13.85           O  
ANISOU 4162  O   GLY B  51     1485   1726   2050     51   -183    106       O  
ATOM   4163  N   GLY B  52     -43.400 -16.445 114.262  1.00  9.45           N  
ANISOU 4163  N   GLY B  52      928   1172   1492     51   -195    121       N  
ATOM   4164  CA  GLY B  52     -42.940 -15.103 114.621  1.00  8.80           C  
ANISOU 4164  CA  GLY B  52      844   1101   1397     46   -162    139       C  
ATOM   4165  C   GLY B  52     -42.954 -14.839 116.112  1.00 11.89           C  
ANISOU 4165  C   GLY B  52     1226   1481   1810     30   -143    154       C  
ATOM   4166  O   GLY B  52     -42.119 -14.087 116.620  1.00 10.80           O  
ANISOU 4166  O   GLY B  52     1091   1351   1663     25   -118    161       O  
ATOM   4167  N   LEU B  53     -43.900 -15.459 116.828  1.00  9.37           N  
ANISOU 4167  N   LEU B  53      897   1143   1521     20   -154    159       N  
ATOM   4168  CA  LEU B  53     -44.000 -15.316 118.277  1.00  9.53           C  
ANISOU 4168  CA  LEU B  53      911   1153   1559      6   -136    172       C  
ATOM   4169  C   LEU B  53     -42.909 -16.148 118.983  1.00 14.17           C  
ANISOU 4169  C   LEU B  53     1502   1736   2144      4   -135    163       C  
ATOM   4170  O   LEU B  53     -42.501 -15.812 120.096  1.00 13.15           O  
ANISOU 4170  O   LEU B  53     1374   1604   2016     -5   -116    172       O  
ATOM   4171  CB  LEU B  53     -45.398 -15.762 118.755  1.00  9.75           C  
ANISOU 4171  CB  LEU B  53      924   1161   1619     -2   -146    183       C  
ATOM   4172  CG  LEU B  53     -45.744 -15.426 120.211  1.00 14.49           C  
ANISOU 4172  CG  LEU B  53     1519   1751   2234    -14   -122    202       C  
ATOM   4173  CD1 LEU B  53     -45.889 -13.920 120.406  1.00 14.75           C  
ANISOU 4173  CD1 LEU B  53     1555   1792   2257    -14    -96    215       C  
ATOM   4174  CD2 LEU B  53     -46.998 -16.118 120.634  1.00 14.88           C  
ANISOU 4174  CD2 LEU B  53     1552   1783   2318    -22   -132    212       C  
ATOM   4175  N   ILE B  54     -42.415 -17.225 118.304  1.00 11.45           N  
ANISOU 4175  N   ILE B  54     1162   1393   1796     13   -156    143       N  
ATOM   4176  CA  ILE B  54     -41.427 -18.164 118.865  1.00 11.12           C  
ANISOU 4176  CA  ILE B  54     1123   1346   1757     14   -160    133       C  
ATOM   4177  C   ILE B  54     -41.983 -18.889 120.120  1.00 16.09           C  
ANISOU 4177  C   ILE B  54     1747   1954   2413      0   -164    144       C  
ATOM   4178  O   ILE B  54     -41.657 -18.519 121.255  1.00 15.93           O  
ANISOU 4178  O   ILE B  54     1728   1932   2393     -9   -146    156       O  
ATOM   4179  CB  ILE B  54     -40.022 -17.497 119.124  1.00 13.73           C  
ANISOU 4179  CB  ILE B  54     1458   1693   2067     16   -138    133       C  
ATOM   4180  CG1 ILE B  54     -39.547 -16.689 117.889  1.00 13.80           C  
ANISOU 4180  CG1 ILE B  54     1470   1723   2050     28   -129    127       C  
ATOM   4181  CG2 ILE B  54     -38.976 -18.563 119.535  1.00 14.35           C  
ANISOU 4181  CG2 ILE B  54     1536   1766   2149     20   -147    120       C  
ATOM   4182  CD1 ILE B  54     -38.176 -15.937 118.098  1.00 16.44           C  
ANISOU 4182  CD1 ILE B  54     1804   2072   2369     27   -106    130       C  
ATOM   4183  N   ILE B  55     -42.865 -19.867 119.903  1.00 12.57           N  
ANISOU 4183  N   ILE B  55     1295   1491   1990     -1   -188    141       N  
ATOM   4184  CA  ILE B  55     -43.423 -20.682 120.987  1.00 12.16           C  
ANISOU 4184  CA  ILE B  55     1238   1418   1967    -14   -192    153       C  
ATOM   4185  C   ILE B  55     -43.194 -22.181 120.703  1.00 15.04           C  
ANISOU 4185  C   ILE B  55     1604   1765   2346    -10   -223    137       C  
ATOM   4186  O   ILE B  55     -44.076 -23.008 120.953  1.00 15.05           O  
ANISOU 4186  O   ILE B  55     1597   1745   2377    -19   -239    144       O  
ATOM   4187  CB  ILE B  55     -44.935 -20.341 121.245  1.00 15.20           C  
ANISOU 4187  CB  ILE B  55     1609   1793   2375    -25   -189    173       C  
ATOM   4188  CG1 ILE B  55     -45.762 -20.400 119.926  1.00 15.42           C  
ANISOU 4188  CG1 ILE B  55     1629   1820   2409    -19   -214    163       C  
ATOM   4189  CG2 ILE B  55     -45.072 -18.971 121.935  1.00 15.77           C  
ANISOU 4189  CG2 ILE B  55     1681   1876   2435    -30   -155    191       C  
ATOM   4190  CD1 ILE B  55     -47.293 -20.360 120.131  1.00 21.64           C  
ANISOU 4190  CD1 ILE B  55     2397   2594   3231    -30   -218    182       C  
ATOM   4191  N   GLU B  56     -41.991 -22.523 120.193  1.00 10.85           N  
ANISOU 4191  N   GLU B  56     1083   1243   1796      5   -229    116       N  
ATOM   4192  CA  GLU B  56     -41.642 -23.901 119.833  1.00 10.30           C  
ANISOU 4192  CA  GLU B  56     1017   1158   1738     13   -257     96       C  
ATOM   4193  C   GLU B  56     -40.869 -24.639 120.963  1.00 12.53           C  
ANISOU 4193  C   GLU B  56     1302   1427   2031      9   -256    101       C  
ATOM   4194  O   GLU B  56     -40.329 -25.722 120.735  1.00 12.07           O  
ANISOU 4194  O   GLU B  56     1248   1357   1980     19   -276     84       O  
ATOM   4195  CB  GLU B  56     -40.854 -23.943 118.489  1.00 11.63           C  
ANISOU 4195  CB  GLU B  56     1195   1342   1880     36   -265     68       C  
ATOM   4196  CG  GLU B  56     -39.901 -22.764 118.278  1.00 17.26           C  
ANISOU 4196  CG  GLU B  56     1911   2085   2562     43   -236     70       C  
ATOM   4197  CD  GLU B  56     -38.762 -22.669 119.275  1.00 26.54           C  
ANISOU 4197  CD  GLU B  56     3085   3265   3735     40   -218     76       C  
ATOM   4198  OE1 GLU B  56     -39.005 -22.203 120.413  1.00 10.36           O  
ANISOU 4198  OE1 GLU B  56     1032   1211   1694     24   -205     98       O  
ATOM   4199  OE2 GLU B  56     -37.608 -22.954 118.883  1.00 11.08           O  
ANISOU 4199  OE2 GLU B  56     1129   1317   1765     56   -217     60       O  
ATOM   4200  N   GLY B  57     -40.844 -24.039 122.161  1.00  8.64           N  
ANISOU 4200  N   GLY B  57      808    938   1537     -4   -233    124       N  
ATOM   4201  CA  GLY B  57     -40.270 -24.659 123.364  1.00  8.11           C  
ANISOU 4201  CA  GLY B  57      745    857   1479     -9   -232    134       C  
ATOM   4202  C   GLY B  57     -38.753 -24.808 123.364  1.00 11.35           C  
ANISOU 4202  C   GLY B  57     1161   1277   1873      4   -233    120       C  
ATOM   4203  O   GLY B  57     -38.182 -25.352 124.318  1.00  9.99           O  
ANISOU 4203  O   GLY B  57      993   1095   1708      2   -236    127       O  
ATOM   4204  N   ASN B  58     -38.088 -24.344 122.296  1.00  7.82           N  
ANISOU 4204  N   ASN B  58      713    851   1406     19   -229    101       N  
ATOM   4205  CA  ASN B  58     -36.634 -24.477 122.169  1.00  7.76           C  
ANISOU 4205  CA  ASN B  58      706    855   1388     33   -227     87       C  
ATOM   4206  C   ASN B  58     -35.968 -23.101 122.229  1.00 11.46           C  
ANISOU 4206  C   ASN B  58     1171   1348   1834     31   -201     93       C  
ATOM   4207  O   ASN B  58     -35.410 -22.736 123.263  1.00 11.39           O  
ANISOU 4207  O   ASN B  58     1163   1341   1825     23   -192    105       O  
ATOM   4208  CB  ASN B  58     -36.274 -25.218 120.854  1.00  6.20           C  
ANISOU 4208  CB  ASN B  58      510    659   1188     55   -244     58       C  
ATOM   4209  CG  ASN B  58     -34.795 -25.468 120.655  1.00 17.62           C  
ANISOU 4209  CG  ASN B  58     1953   2116   2626     73   -240     43       C  
ATOM   4210  OD1 ASN B  58     -33.951 -25.065 121.462  1.00 12.18           O  
ANISOU 4210  OD1 ASN B  58     1258   1434   1935     69   -229     54       O  
ATOM   4211  ND2 ASN B  58     -34.453 -26.151 119.573  1.00  6.68           N  
ANISOU 4211  ND2 ASN B  58      570    732   1236     95   -252     18       N  
ATOM   4212  N   VAL B  59     -36.074 -22.311 121.138  1.00  7.84           N  
ANISOU 4212  N   VAL B  59      711    909   1358     38   -190     86       N  
ATOM   4213  CA  VAL B  59     -35.585 -20.926 121.131  1.00  7.01           C  
ANISOU 4213  CA  VAL B  59      603    825   1235     34   -164     95       C  
ATOM   4214  C   VAL B  59     -36.444 -20.086 122.091  1.00 10.40           C  
ANISOU 4214  C   VAL B  59     1036   1249   1668     14   -152    117       C  
ATOM   4215  O   VAL B  59     -35.930 -19.167 122.740  1.00  8.57           O  
ANISOU 4215  O   VAL B  59      804   1024   1428      6   -137    128       O  
ATOM   4216  CB  VAL B  59     -35.564 -20.329 119.691  1.00 10.05           C  
ANISOU 4216  CB  VAL B  59      988   1231   1601     46   -155     85       C  
ATOM   4217  CG1 VAL B  59     -35.122 -18.864 119.707  1.00  9.34           C  
ANISOU 4217  CG1 VAL B  59      894   1159   1495     39   -129     98       C  
ATOM   4218  CG2 VAL B  59     -34.663 -21.158 118.771  1.00  9.71           C  
ANISOU 4218  CG2 VAL B  59      944   1195   1551     69   -163     62       C  
ATOM   4219  N   GLU B  60     -37.722 -20.509 122.291  1.00  7.46           N  
ANISOU 4219  N   GLU B  60      666    861   1309      7   -161    125       N  
ATOM   4220  CA  GLU B  60     -38.630 -19.880 123.249  1.00  7.45           C  
ANISOU 4220  CA  GLU B  60      665    851   1312     -9   -148    146       C  
ATOM   4221  C   GLU B  60     -38.043 -19.915 124.663  1.00 11.76           C  
ANISOU 4221  C   GLU B  60     1218   1390   1859    -17   -143    157       C  
ATOM   4222  O   GLU B  60     -38.059 -18.898 125.358  1.00 11.09           O  
ANISOU 4222  O   GLU B  60     1138   1310   1764    -25   -125    168       O  
ATOM   4223  CB  GLU B  60     -39.999 -20.581 123.233  1.00  8.90           C  
ANISOU 4223  CB  GLU B  60      846   1017   1517    -14   -161    152       C  
ATOM   4224  CG  GLU B  60     -40.986 -19.992 124.228  1.00 15.13           C  
ANISOU 4224  CG  GLU B  60     1634   1799   2314    -28   -143    175       C  
ATOM   4225  CD  GLU B  60     -42.188 -20.862 124.524  1.00 18.45           C  
ANISOU 4225  CD  GLU B  60     2048   2199   2762    -36   -154    187       C  
ATOM   4226  OE1 GLU B  60     -42.269 -21.978 123.964  1.00 17.23           O  
ANISOU 4226  OE1 GLU B  60     1890   2034   2623    -32   -179    175       O  
ATOM   4227  OE2 GLU B  60     -43.020 -20.454 125.363  1.00  4.76           O  
ANISOU 4227  OE2 GLU B  60      455    485    870    -26    -79    139       O  
ATOM   4228  N   GLN B  61     -37.540 -21.101 125.100  1.00  8.97           N  
ANISOU 4228  N   GLN B  61      866   1024   1516    -14   -161    152       N  
ATOM   4229  CA  GLN B  61     -36.957 -21.254 126.440  1.00  9.19           C  
ANISOU 4229  CA  GLN B  61      903   1045   1543    -21   -161    163       C  
ATOM   4230  C   GLN B  61     -35.763 -20.317 126.623  1.00 14.92           C  
ANISOU 4230  C   GLN B  61     1630   1787   2253    -20   -152    159       C  
ATOM   4231  O   GLN B  61     -35.606 -19.713 127.682  1.00 15.03           O  
ANISOU 4231  O   GLN B  61     1654   1799   2258    -29   -144    171       O  
ATOM   4232  CB  GLN B  61     -36.526 -22.718 126.685  1.00 10.18           C  
ANISOU 4232  CB  GLN B  61     1029   1154   1685    -15   -185    158       C  
ATOM   4233  CG  GLN B  61     -36.159 -23.009 128.147  1.00 16.17           C  
ANISOU 4233  CG  GLN B  61     1800   1901   2443    -23   -188    173       C  
ATOM   4234  CD  GLN B  61     -35.499 -24.366 128.328  1.00 24.94           C  
ANISOU 4234  CD  GLN B  61     2911   2996   3569    -15   -213    167       C  
ATOM   4235  OE1 GLN B  61     -34.904 -24.935 127.398  1.00 15.84           O  
ANISOU 4235  OE1 GLN B  61     1749   1845   2423      0   -226    148       O  
ATOM   4236  NE2 GLN B  61     -35.481 -24.848 129.558  1.00 15.17           N  
ANISOU 4236  NE2 GLN B  61     1686   1744   2333    -21   -219    185       N  
ATOM   4237  N   ARG B  62     -34.975 -20.136 125.561  1.00 11.84           N  
ANISOU 4237  N   ARG B  62     1229   1412   1858     -9   -152    144       N  
ATOM   4238  CA  ARG B  62     -33.727 -19.379 125.612  1.00 11.50           C  
ANISOU 4238  CA  ARG B  62     1181   1383   1805     -8   -145    140       C  
ATOM   4239  C   ARG B  62     -33.917 -17.854 125.491  1.00 16.25           C  
ANISOU 4239  C   ARG B  62     1784   1997   2394    -17   -124    148       C  
ATOM   4240  O   ARG B  62     -32.950 -17.109 125.655  1.00 16.35           O  
ANISOU 4240  O   ARG B  62     1793   2019   2402    -20   -118    148       O  
ATOM   4241  CB  ARG B  62     -32.751 -19.901 124.563  1.00  9.05           C  
ANISOU 4241  CB  ARG B  62      857   1084   1498      9   -151    123       C  
ATOM   4242  CG  ARG B  62     -32.271 -21.296 124.879  1.00 12.84           C  
ANISOU 4242  CG  ARG B  62     1336   1550   1992     18   -173    115       C  
ATOM   4243  CD  ARG B  62     -31.973 -22.105 123.641  1.00 19.17           C  
ANISOU 4243  CD  ARG B  62     2129   2356   2798     38   -180     95       C  
ATOM   4244  NE  ARG B  62     -31.335 -23.380 123.984  1.00 22.33           N  
ANISOU 4244  NE  ARG B  62     2528   2742   3215     49   -202     86       N  
ATOM   4245  CZ  ARG B  62     -31.999 -24.452 124.409  1.00 27.46           C  
ANISOU 4245  CZ  ARG B  62     3187   3368   3878     48   -221     88       C  
ATOM   4246  NH1 ARG B  62     -33.324 -24.419 124.524  1.00 10.62           N  
ANISOU 4246  NH1 ARG B  62     1064   1226   1747     36   -220     98       N  
ATOM   4247  NH2 ARG B  62     -31.346 -25.562 124.726  1.00 12.70           N  
ANISOU 4247  NH2 ARG B  62     1316   1485   2025     59   -241     81       N  
ATOM   4248  N   LEU B  63     -35.168 -17.386 125.262  1.00 12.20           N  
ANISOU 4248  N   LEU B  63     1275   1481   1877    -21   -113    155       N  
ATOM   4249  CA  LEU B  63     -35.445 -15.940 125.220  1.00 11.51           C  
ANISOU 4249  CA  LEU B  63     1192   1401   1780    -29    -94    164       C  
ATOM   4250  C   LEU B  63     -36.489 -15.520 126.267  1.00 12.45           C  
ANISOU 4250  C   LEU B  63     1324   1508   1898    -39    -84    178       C  
ATOM   4251  O   LEU B  63     -36.447 -14.391 126.755  1.00 10.47           O  
ANISOU 4251  O   LEU B  63     1080   1258   1638    -46    -71    184       O  
ATOM   4252  CB  LEU B  63     -35.877 -15.486 123.789  1.00 11.95           C  
ANISOU 4252  CB  LEU B  63     1240   1469   1830    -21    -86    160       C  
ATOM   4253  CG  LEU B  63     -37.267 -15.948 123.300  1.00 17.11           C  
ANISOU 4253  CG  LEU B  63     1894   2116   2491    -18    -91    161       C  
ATOM   4254  CD1 LEU B  63     -38.360 -14.944 123.714  1.00 17.46           C  
ANISOU 4254  CD1 LEU B  63     1944   2156   2535    -26    -75    176       C  
ATOM   4255  CD2 LEU B  63     -37.281 -16.103 121.806  1.00 18.75           C  
ANISOU 4255  CD2 LEU B  63     2095   2336   2692     -5    -95    150       C  
ATOM   4256  N   LYS B  64     -37.435 -16.425 126.597  1.00  8.07           N  
ANISOU 4256  N   LYS B  64      771    941   1354    -39    -90    183       N  
ATOM   4257  CA  LYS B  64     -38.524 -16.092 127.511  1.00  7.22           C  
ANISOU 4257  CA  LYS B  64      673    822   1247    -47    -77    198       C  
ATOM   4258  C   LYS B  64     -38.172 -16.436 128.994  1.00  9.33           C  
ANISOU 4258  C   LYS B  64      956   1080   1509    -52    -79    206       C  
ATOM   4259  O   LYS B  64     -37.701 -15.558 129.715  1.00  7.89           O  
ANISOU 4259  O   LYS B  64      786    898   1311    -57    -71    208       O  
ATOM   4260  CB  LYS B  64     -39.867 -16.748 127.050  1.00  8.23           C  
ANISOU 4260  CB  LYS B  64      792    943   1392    -45    -79    204       C  
ATOM   4261  CG  LYS B  64     -41.111 -16.263 127.814  1.00  7.16           C  
ANISOU 4261  CG  LYS B  64      660    799   1260    -51    -59    222       C  
ATOM   4262  CD  LYS B  64     -41.404 -14.775 127.568  1.00 13.64           C  
ANISOU 4262  CD  LYS B  64     1483   1629   2072    -50    -40    224       C  
ATOM   4263  CE  LYS B  64     -42.748 -14.351 128.128  1.00 13.76           C  
ANISOU 4263  CE  LYS B  64     1498   1636   2095    -52    -19    240       C  
ATOM   4264  NZ  LYS B  64     -42.878 -14.684 129.571  1.00  8.86           N  
ANISOU 4264  NZ  LYS B  64      892   1006   1470    -56     -8    252       N  
ATOM   4265  N   PRO B  65     -38.306 -17.725 129.450  1.00  6.11           N  
ANISOU 4265  N   PRO B  65      558    657   1107    -48    -92    211       N  
ATOM   4266  CA  PRO B  65     -38.008 -18.023 130.869  1.00  5.98           C  
ANISOU 4266  CA  PRO B  65      578    645   1050    -37    -90    202       C  
ATOM   4267  C   PRO B  65     -36.553 -17.756 131.264  1.00 11.22           C  
ANISOU 4267  C   PRO B  65     1223   1303   1738    -57   -107    211       C  
ATOM   4268  O   PRO B  65     -36.293 -17.273 132.370  1.00 11.46           O  
ANISOU 4268  O   PRO B  65     1273   1330   1752    -61   -104    217       O  
ATOM   4269  CB  PRO B  65     -38.375 -19.512 131.009  1.00  7.25           C  
ANISOU 4269  CB  PRO B  65      709    780   1265    -57   -109    228       C  
ATOM   4270  CG  PRO B  65     -38.403 -20.038 129.621  1.00 11.72           C  
ANISOU 4270  CG  PRO B  65     1256   1350   1848    -50   -122    213       C  
ATOM   4271  CD  PRO B  65     -38.830 -18.915 128.747  1.00  7.15           C  
ANISOU 4271  CD  PRO B  65      669    785   1264    -49   -107    208       C  
ATOM   4272  N   LEU B  66     -35.604 -18.060 130.370  1.00  7.12           N  
ANISOU 4272  N   LEU B  66      688    791   1226    -50   -122    197       N  
ATOM   4273  CA  LEU B  66     -34.190 -17.967 130.714  1.00  6.73           C  
ANISOU 4273  CA  LEU B  66      638    746   1172    -50   -137    189       C  
ATOM   4274  C   LEU B  66     -33.551 -16.622 130.336  1.00 11.59           C  
ANISOU 4274  C   LEU B  66     1249   1375   1780    -53   -128    183       C  
ATOM   4275  O   LEU B  66     -32.352 -16.442 130.539  1.00 10.69           O  
ANISOU 4275  O   LEU B  66     1131   1264   1666    -54   -140    177       O  
ATOM   4276  CB  LEU B  66     -33.399 -19.147 130.120  1.00  6.64           C  
ANISOU 4276  CB  LEU B  66      612    734   1177    -39   -158    179       C  
ATOM   4277  CG  LEU B  66     -33.956 -20.563 130.465  1.00 11.71           C  
ANISOU 4277  CG  LEU B  66     1259   1359   1830    -36   -171    185       C  
ATOM   4278  CD1 LEU B  66     -33.090 -21.650 129.866  1.00 12.06           C  
ANISOU 4278  CD1 LEU B  66     1290   1402   1891    -24   -192    172       C  
ATOM   4279  CD2 LEU B  66     -34.088 -20.754 131.972  1.00 13.02           C  
ANISOU 4279  CD2 LEU B  66     1448   1513   1987    -44   -175    202       C  
ATOM   4280  N   GLN B  67     -34.367 -15.640 129.877  1.00  8.87           N  
ANISOU 4280  N   GLN B  67      906   1035   1430    -56   -107    186       N  
ATOM   4281  CA  GLN B  67     -33.855 -14.285 129.618  1.00  8.78           C  
ANISOU 4281  CA  GLN B  67      892   1031   1412    -61    -97    182       C  
ATOM   4282  C   GLN B  67     -34.823 -13.164 130.082  1.00 12.54           C  
ANISOU 4282  C   GLN B  67     1385   1503   1878    -67    -78    190       C  
ATOM   4283  O   GLN B  67     -34.682 -12.676 131.197  1.00 11.97           O  
ANISOU 4283  O   GLN B  67     1332   1422   1793    -73    -78    193       O  
ATOM   4284  CB  GLN B  67     -33.425 -14.102 128.145  1.00  9.98           C  
ANISOU 4284  CB  GLN B  67     1021   1198   1571    -55    -93    175       C  
ATOM   4285  CG  GLN B  67     -32.144 -14.872 127.790  1.00 16.24           C  
ANISOU 4285  CG  GLN B  67     1798   1998   2374    -49   -109    165       C  
ATOM   4286  CD  GLN B  67     -31.381 -14.230 126.659  1.00 18.00           C  
ANISOU 4286  CD  GLN B  67     2002   2237   2599    -46   -100    161       C  
ATOM   4287  OE1 GLN B  67     -30.756 -13.179 126.822  1.00 10.71           O  
ANISOU 4287  OE1 GLN B  67     1077   1317   1676    -55    -95    164       O  
ATOM   4288  NE2 GLN B  67     -31.276 -14.935 125.541  1.00  3.93           N  
ANISOU 4288  NE2 GLN B  67      435    454    604    -10    -28     64       N  
ATOM   4289  N   ILE B  68     -35.815 -12.766 129.222  1.00  8.96           N  
ANISOU 4289  N   ILE B  68      925   1054   1427    -64    -61    194       N  
ATOM   4290  CA  ILE B  68     -36.705 -11.622 129.546  1.00  8.74           C  
ANISOU 4290  CA  ILE B  68      909   1020   1392    -67    -41    201       C  
ATOM   4291  C   ILE B  68     -37.545 -11.832 130.825  1.00 12.04           C  
ANISOU 4291  C   ILE B  68     1347   1426   1802    -67    -33    210       C  
ATOM   4292  O   ILE B  68     -37.918 -10.850 131.478  1.00 10.89           O  
ANISOU 4292  O   ILE B  68     1218   1274   1645    -69    -19    212       O  
ATOM   4293  CB  ILE B  68     -37.559 -11.151 128.332  1.00 11.85           C  
ANISOU 4293  CB  ILE B  68     1290   1421   1793    -62    -28    203       C  
ATOM   4294  CG1 ILE B  68     -38.625 -12.204 127.936  1.00 12.63           C  
ANISOU 4294  CG1 ILE B  68     1378   1517   1902    -56    -30    208       C  
ATOM   4295  CG2 ILE B  68     -36.665 -10.775 127.150  1.00 13.30           C  
ANISOU 4295  CG2 ILE B  68     1459   1618   1978    -60    -32    197       C  
ATOM   4296  CD1 ILE B  68     -39.653 -11.699 126.840  1.00 17.32           C  
ANISOU 4296  CD1 ILE B  68     1961   2116   2503    -50    -20    212       C  
ATOM   4297  N   ASP B  69     -37.797 -13.111 131.213  1.00  8.17           N  
ANISOU 4297  N   ASP B  69      857    932   1317    -65    -41    214       N  
ATOM   4298  CA  ASP B  69     -38.452 -13.408 132.497  1.00  7.13           C  
ANISOU 4298  CA  ASP B  69      745    789   1175    -66    -32    226       C  
ATOM   4299  C   ASP B  69     -37.543 -13.034 133.642  1.00  9.99           C  
ANISOU 4299  C   ASP B  69     1132   1147   1517    -70    -41    222       C  
ATOM   4300  O   ASP B  69     -38.000 -12.451 134.617  1.00  8.91           O  
ANISOU 4300  O   ASP B  69     1018   1004   1363    -70    -26    227       O  
ATOM   4301  CB  ASP B  69     -38.841 -14.888 132.592  1.00  8.38           C  
ANISOU 4301  CB  ASP B  69      896    942   1347    -65    -41    234       C  
ATOM   4302  CG  ASP B  69     -40.099 -15.244 131.829  1.00 13.38           C  
ANISOU 4302  CG  ASP B  69     1511   1574   2000    -63    -31    242       C  
ATOM   4303  OD1 ASP B  69     -40.536 -14.427 130.992  1.00 13.18           O  
ANISOU 4303  OD1 ASP B  69     1474   1555   1979    -61    -21    238       O  
ATOM   4304  OD2 ASP B  69     -40.636 -16.352 132.056  1.00 15.67           O  
ANISOU 4304  OD2 ASP B  69     1796   1855   2302    -64    -35    252       O  
ATOM   4305  N   PHE B  70     -36.218 -13.348 133.516  1.00  7.06           N  
ANISOU 4305  N   PHE B  70      755    779   1148    -72    -66    212       N  
ATOM   4306  CA  PHE B  70     -35.225 -12.973 134.529  1.00  7.59           C  
ANISOU 4306  CA  PHE B  70      843    842   1199    -77    -81    207       C  
ATOM   4307  C   PHE B  70     -35.054 -11.452 134.578  1.00 12.23           C  
ANISOU 4307  C   PHE B  70     1440   1429   1778    -81    -73    200       C  
ATOM   4308  O   PHE B  70     -34.869 -10.887 135.654  1.00 12.05           O  
ANISOU 4308  O   PHE B  70     1445   1398   1736    -84    -76    198       O  
ATOM   4309  CB  PHE B  70     -33.855 -13.637 134.234  1.00  9.32           C  
ANISOU 4309  CB  PHE B  70     1047   1066   1430    -78   -110    199       C  
ATOM   4310  CG  PHE B  70     -33.792 -15.136 134.416  1.00 10.60           C  
ANISOU 4310  CG  PHE B  70     1204   1224   1599    -73   -125    205       C  
ATOM   4311  CD1 PHE B  70     -34.561 -15.767 135.389  1.00 13.69           C  
ANISOU 4311  CD1 PHE B  70     1617   1605   1980    -72   -120    218       C  
ATOM   4312  CD2 PHE B  70     -32.833 -15.893 133.748  1.00 12.20           C  
ANISOU 4312  CD2 PHE B  70     1384   1431   1820    -69   -145    197       C  
ATOM   4313  CE1 PHE B  70     -34.461 -17.147 135.596  1.00 14.54           C  
ANISOU 4313  CE1 PHE B  70     1721   1706   2096    -68   -136    226       C  
ATOM   4314  CE2 PHE B  70     -32.719 -17.270 133.973  1.00 15.05           C  
ANISOU 4314  CE2 PHE B  70     1744   1786   2190    -63   -162    202       C  
ATOM   4315  CZ  PHE B  70     -33.539 -17.888 134.889  1.00 13.14           C  
ANISOU 4315  CZ  PHE B  70     1523   1532   1938    -64   -158    216       C  
ATOM   4316  N   TYR B  71     -35.054 -10.797 133.401  1.00  8.00           N  
ANISOU 4316  N   TYR B  71      883    900   1256    -82    -65    196       N  
ATOM   4317  CA  TYR B  71     -34.811  -9.354 133.309  1.00  7.00           C  
ANISOU 4317  CA  TYR B  71      763    771   1126    -88    -58    191       C  
ATOM   4318  C   TYR B  71     -35.963  -8.544 133.934  1.00 12.75           C  
ANISOU 4318  C   TYR B  71     1514   1489   1840    -84    -35    195       C  
ATOM   4319  O   TYR B  71     -35.715  -7.621 134.715  1.00 12.61           O  
ANISOU 4319  O   TYR B  71     1521   1462   1809    -87    -37    188       O  
ATOM   4320  CB  TYR B  71     -34.564  -8.933 131.843  1.00  6.48           C  
ANISOU 4320  CB  TYR B  71      668    715   1077    -89    -53    189       C  
ATOM   4321  CG  TYR B  71     -33.473  -9.743 131.145  1.00  7.07           C  
ANISOU 4321  CG  TYR B  71      718    801   1166    -89    -71    185       C  
ATOM   4322  CD1 TYR B  71     -32.468 -10.378 131.877  1.00  8.51           C  
ANISOU 4322  CD1 TYR B  71      904    982   1348    -92    -95    181       C  
ATOM   4323  CD2 TYR B  71     -33.397  -9.797 129.758  1.00  7.45           C  
ANISOU 4323  CD2 TYR B  71      742    862   1226    -85    -64    185       C  
ATOM   4324  CE1 TYR B  71     -31.481 -11.133 131.247  1.00  7.29           C  
ANISOU 4324  CE1 TYR B  71      724    836   1208    -89   -109    177       C  
ATOM   4325  CE2 TYR B  71     -32.394 -10.524 129.114  1.00  7.90           C  
ANISOU 4325  CE2 TYR B  71      777    931   1294    -82    -77    180       C  
ATOM   4326  CZ  TYR B  71     -31.433 -11.186 129.863  1.00 12.76           C  
ANISOU 4326  CZ  TYR B  71     1393   1543   1913    -84    -98    176       C  
ATOM   4327  OH  TYR B  71     -30.447 -11.908 129.232  1.00 10.67           O  
ANISOU 4327  OH  TYR B  71     1105   1289   1661    -79   -109    171       O  
ATOM   4328  N   SER B  72     -37.218  -8.939 133.647  1.00  9.58           N  
ANISOU 4328  N   SER B  72     1106   1090   1443    -76    -14    204       N  
ATOM   4329  CA  SER B  72     -38.395  -8.305 134.247  1.00  9.30           C  
ANISOU 4329  CA  SER B  72     1089   1047   1397    -69     12    210       C  
ATOM   4330  C   SER B  72     -38.655  -8.873 135.654  1.00 12.33           C  
ANISOU 4330  C   SER B  72     1500   1423   1760    -66     15    215       C  
ATOM   4331  O   SER B  72     -39.392  -8.270 136.436  1.00 12.17           O  
ANISOU 4331  O   SER B  72     1502   1396   1724    -59     36    218       O  
ATOM   4332  CB  SER B  72     -39.623  -8.520 133.363  1.00 12.96           C  
ANISOU 4332  CB  SER B  72     1530   1515   1878    -63     31    220       C  
ATOM   4333  OG  SER B  72     -39.903  -9.904 133.201  1.00 20.39           O  
ANISOU 4333  OG  SER B  72     2457   2460   2829    -62     24    228       O  
ATOM   4334  N   GLN B  73     -38.061 -10.059 135.959  1.00  9.01           N  
ANISOU 4334  N   GLN B  73     1079   1006   1339    -69     -5    218       N  
ATOM   4335  CA  GLN B  73     -38.250 -10.777 137.243  1.00  8.62           C  
ANISOU 4335  CA  GLN B  73     1055    951   1270    -66     -4    226       C  
ATOM   4336  C   GLN B  73     -39.705 -11.258 137.443  1.00 10.95           C  
ANISOU 4336  C   GLN B  73     1347   1245   1568    -59     26    244       C  
ATOM   4337  O   GLN B  73     -40.118 -11.515 138.577  1.00 10.74           O  
ANISOU 4337  O   GLN B  73     1346   1213   1520    -55     39    254       O  
ATOM   4338  CB  GLN B  73     -37.762  -9.932 138.448  1.00 10.00           C  
ANISOU 4338  CB  GLN B  73     1269   1118   1414    -65     -9    217       C  
ATOM   4339  CG  GLN B  73     -36.248  -9.720 138.468  1.00 14.22           C  
ANISOU 4339  CG  GLN B  73     1804   1650   1947    -74    -45    203       C  
ATOM   4340  CD  GLN B  73     -35.788  -9.023 139.724  1.00 21.87           C  
ANISOU 4340  CD  GLN B  73     2815   2608   2885    -74    -56    193       C  
ATOM   4341  OE1 GLN B  73     -36.218  -9.341 140.833  1.00 17.13           O  
ANISOU 4341  OE1 GLN B  73     2247   2005   2258    -67    -48    200       O  
ATOM   4342  NE2 GLN B  73     -34.817  -8.140 139.585  1.00 12.82           N  
ANISOU 4342  NE2 GLN B  73     1670   1458   1743    -83    -78    178       N  
HETATM 4343  N   MSE B  74     -40.451 -11.470 136.327  1.00  5.29           N  
ANISOU 4343  N   MSE B  74      570    578    862    -28     20    205       N  
HETATM 4344  CA  MSE B  74     -41.825 -12.002 136.402  1.00  3.92           C  
ANISOU 4344  CA  MSE B  74      389    457    642     10     19    133       C  
HETATM 4345  C   MSE B  74     -41.835 -13.483 136.782  1.00  9.55           C  
ANISOU 4345  C   MSE B  74     1125   1067   1436    -57     51    281       C  
HETATM 4346  O   MSE B  74     -42.730 -13.927 137.503  1.00 10.08           O  
ANISOU 4346  O   MSE B  74     1198   1130   1501    -55     73    300       O  
HETATM 4347  CB  MSE B  74     -42.575 -11.770 135.098  1.00  4.06           C  
ANISOU 4347  CB  MSE B  74      390    465    689     13     25    152       C  
HETATM 4348  CG  MSE B  74     -42.962 -10.333 134.890  1.00  7.06           C  
ANISOU 4348  CG  MSE B  74      783    759   1139    -47     87    263       C  
HETATM 4349 SE   MSE B  74     -44.212 -10.119 133.458  0.75 11.67          SE  
ANISOU 4349 SE   MSE B  74     1329   1347   1757    -43     98    270      SE  
HETATM 4350  CE  MSE B  74     -44.539  -8.249 133.633  1.00  9.02           C  
ANISOU 4350  CE  MSE B  74     1009   1006   1410    -33    121    263       C  
ATOM   4351  N   THR B  75     -40.851 -14.256 136.281  1.00  7.67           N  
ANISOU 4351  N   THR B  75      876    831   1207    -62     20    274       N  
ATOM   4352  CA  THR B  75     -40.629 -15.640 136.732  1.00  8.22           C  
ANISOU 4352  CA  THR B  75      947    894   1280    -65      4    284       C  
ATOM   4353  C   THR B  75     -39.141 -15.885 136.897  1.00 13.09           C  
ANISOU 4353  C   THR B  75     1574   1512   1888    -67    -28    271       C  
ATOM   4354  O   THR B  75     -38.332 -15.241 136.217  1.00 12.85           O  
ANISOU 4354  O   THR B  75     1534   1489   1860    -68    -41    254       O  
ATOM   4355  CB  THR B  75     -41.263 -16.674 135.754  1.00 15.90           C  
ANISOU 4355  CB  THR B  75     1888   1865   2288    -68     -1    291       C  
ATOM   4356  OG1 THR B  75     -40.436 -16.822 134.608  1.00 13.80           O  
ANISOU 4356  OG1 THR B  75     1603   1604   2035    -68    -26    273       O  
ATOM   4357  CG2 THR B  75     -42.681 -16.320 135.353  1.00 14.25           C  
ANISOU 4357  CG2 THR B  75     1663   1656   2096    -66     26    302       C  
ATOM   4358  N   VAL B  76     -38.762 -16.804 137.800  1.00  9.40           N  
ANISOU 4358  N   VAL B  76     1123   1037   1410    -68    -42    281       N  
ATOM   4359  CA  VAL B  76     -37.349 -17.120 138.020  1.00  9.31           C  
ANISOU 4359  CA  VAL B  76     1119   1026   1393    -69    -76    270       C  
ATOM   4360  C   VAL B  76     -37.117 -18.630 138.038  1.00 13.94           C  
ANISOU 4360  C   VAL B  76     1697   1604   1995    -68    -96    280       C  
ATOM   4361  O   VAL B  76     -37.340 -19.282 139.064  1.00 13.48           O  
ANISOU 4361  O   VAL B  76     1661   1537   1925    -68    -96    298       O  
ATOM   4362  CB  VAL B  76     -36.776 -16.428 139.305  1.00 12.72           C  
ANISOU 4362  CB  VAL B  76     1588   1456   1788    -68    -81    268       C  
ATOM   4363  CG1 VAL B  76     -35.287 -16.716 139.460  1.00 12.49           C  
ANISOU 4363  CG1 VAL B  76     1561   1426   1758    -69   -120    257       C  
ATOM   4364  CG2 VAL B  76     -37.032 -14.923 139.280  1.00 12.22           C  
ANISOU 4364  CG2 VAL B  76     1535   1397   1712    -68    -62    257       C  
ATOM   4365  N   ASP B  77     -36.668 -19.189 136.904  1.00 10.78           N  
ANISOU 4365  N   ASP B  77     1268   1205   1622    -67   -114    269       N  
ATOM   4366  CA  ASP B  77     -36.265 -20.585 136.839  1.00 10.78           C  
ANISOU 4366  CA  ASP B  77     1261   1196   1639    -65   -138    273       C  
ATOM   4367  C   ASP B  77     -35.154 -20.827 137.867  1.00 15.87           C  
ANISOU 4367  C   ASP B  77     1928   1837   2267    -63   -163    274       C  
ATOM   4368  O   ASP B  77     -34.229 -20.023 137.972  1.00 16.40           O  
ANISOU 4368  O   ASP B  77     1999   1912   2322    -63   -175    261       O  
ATOM   4369  CB  ASP B  77     -35.775 -20.935 135.418  1.00 12.25           C  
ANISOU 4369  CB  ASP B  77     1415   1386   1852    -61   -153    255       C  
ATOM   4370  CG  ASP B  77     -35.461 -22.406 135.221  1.00 19.08           C  
ANISOU 4370  CG  ASP B  77     2271   2238   2738    -56   -177    256       C  
ATOM   4371  OD1 ASP B  77     -34.480 -22.890 135.830  1.00 19.22           O  
ANISOU 4371  OD1 ASP B  77     2298   2251   2752    -53   -201    256       O  
ATOM   4372  OD2 ASP B  77     -36.125 -23.044 134.379  1.00 25.02           O  
ANISOU 4372  OD2 ASP B  77     3007   2986   3514    -55   -176    255       O  
ATOM   4373  N   GLY B  78     -35.309 -21.872 138.675  1.00 13.12           N  
ANISOU 4373  N   GLY B  78     1595   1475   1917    -63   -172    293       N  
ATOM   4374  CA  GLY B  78     -34.391 -22.154 139.779  1.00 13.18           C  
ANISOU 4374  CA  GLY B  78     1628   1476   1904    -61   -196    299       C  
ATOM   4375  C   GLY B  78     -32.985 -22.556 139.361  1.00 17.42           C  
ANISOU 4375  C   GLY B  78     2148   2013   2457    -55   -233    282       C  
ATOM   4376  O   GLY B  78     -32.081 -22.620 140.201  1.00 16.71           O  
ANISOU 4376  O   GLY B  78     2075   1920   2352    -53   -259    284       O  
ATOM   4377  N   GLY B  79     -32.801 -22.826 138.063  1.00 14.67           N  
ANISOU 4377  N   GLY B  79     1766   1669   2138    -52   -237    267       N  
ATOM   4378  CA  GLY B  79     -31.517 -23.278 137.520  1.00 14.68           C  
ANISOU 4378  CA  GLY B  79     1746   1672   2158    -44   -266    251       C  
ATOM   4379  C   GLY B  79     -30.398 -22.253 137.624  1.00 18.44           C  
ANISOU 4379  C   GLY B  79     2221   2161   2626    -45   -278    237       C  
ATOM   4380  O   GLY B  79     -30.654 -21.051 137.754  1.00 17.59           O  
ANISOU 4380  O   GLY B  79     2121   2062   2500    -52   -261    233       O  
ATOM   4381  N   GLY B  80     -29.154 -22.735 137.535  1.00 15.54           N  
ANISOU 4381  N   GLY B  80     1838   1792   2273    -37   -308    228       N  
ATOM   4382  CA  GLY B  80     -27.970 -21.886 137.615  1.00 14.92           C  
ANISOU 4382  CA  GLY B  80     1751   1724   2194    -39   -324    216       C  
ATOM   4383  C   GLY B  80     -27.585 -21.277 136.284  1.00 19.18           C  
ANISOU 4383  C   GLY B  80     2256   2280   2753    -38   -311    198       C  
ATOM   4384  O   GLY B  80     -26.460 -21.473 135.807  1.00 19.46           O  
ANISOU 4384  O   GLY B  80     2264   2320   2808    -31   -328    188       O  
ATOM   4385  N   TRP B  81     -28.517 -20.526 135.666  1.00 14.92           N  
ANISOU 4385  N   TRP B  81     1715   1748   2205    -43   -280    196       N  
ATOM   4386  CA  TRP B  81     -28.267 -19.884 134.374  1.00 13.89           C  
ANISOU 4386  CA  TRP B  81     1556   1633   2089    -42   -264    182       C  
ATOM   4387  C   TRP B  81     -27.574 -18.534 134.563  1.00 15.56           C  
ANISOU 4387  C   TRP B  81     1765   1852   2293    -52   -264    177       C  
ATOM   4388  O   TRP B  81     -27.993 -17.735 135.396  1.00 14.20           O  
ANISOU 4388  O   TRP B  81     1619   1676   2099    -62   -260    182       O  
ATOM   4389  CB  TRP B  81     -29.575 -19.716 133.589  1.00 12.46           C  
ANISOU 4389  CB  TRP B  81     1374   1455   1904    -43   -234    184       C  
ATOM   4390  CG  TRP B  81     -30.322 -21.000 133.382  1.00 13.51           C  
ANISOU 4390  CG  TRP B  81     1508   1577   2047    -36   -235    189       C  
ATOM   4391  CD1 TRP B  81     -31.396 -21.448 134.095  1.00 16.41           C  
ANISOU 4391  CD1 TRP B  81     1898   1932   2407    -40   -229    204       C  
ATOM   4392  CD2 TRP B  81     -29.997 -22.038 132.450  1.00 13.36           C  
ANISOU 4392  CD2 TRP B  81     1469   1557   2051    -23   -245    178       C  
ATOM   4393  NE1 TRP B  81     -31.792 -22.681 133.628  1.00 15.99           N  
ANISOU 4393  NE1 TRP B  81     1836   1868   2372    -33   -236    205       N  
ATOM   4394  CE2 TRP B  81     -30.946 -23.071 132.622  1.00 17.38           C  
ANISOU 4394  CE2 TRP B  81     1988   2049   2565    -22   -247    188       C  
ATOM   4395  CE3 TRP B  81     -28.981 -22.206 131.490  1.00 14.60           C  
ANISOU 4395  CE3 TRP B  81     1599   1724   2223    -11   -251    162       C  
ATOM   4396  CZ2 TRP B  81     -30.926 -24.244 131.856  1.00 16.87           C  
ANISOU 4396  CZ2 TRP B  81     1911   1977   2523     -9   -259    179       C  
ATOM   4397  CZ3 TRP B  81     -28.972 -23.361 130.720  1.00 16.34           C  
ANISOU 4397  CZ3 TRP B  81     1808   1938   2461      4   -259    153       C  
ATOM   4398  CH2 TRP B  81     -29.933 -24.364 130.908  1.00 17.03           C  
ANISOU 4398  CH2 TRP B  81     1908   2007   2555      4   -265    160       C  
ATOM   4399  N   GLY B  82     -26.516 -18.299 133.784  1.00 11.93           N  
ANISOU 4399  N   GLY B  82     1275   1404   1854    -50   -269    167       N  
ATOM   4400  CA  GLY B  82     -25.714 -17.077 133.869  1.00 11.20           C  
ANISOU 4400  CA  GLY B  82     1173   1318   1763    -61   -273    163       C  
ATOM   4401  C   GLY B  82     -26.456 -15.819 133.458  1.00 12.69           C  
ANISOU 4401  C   GLY B  82     1369   1512   1940    -71   -244    163       C  
ATOM   4402  O   GLY B  82     -26.092 -14.718 133.881  1.00 11.99           O  
ANISOU 4402  O   GLY B  82     1287   1422   1847    -83   -249    162       O  
ATOM   4403  N   THR B  83     -27.517 -15.969 132.626  1.00  8.12           N  
ANISOU 4403  N   THR B  83      789    938   1357    -66   -218    164       N  
ATOM   4404  CA  THR B  83     -28.345 -14.831 132.186  1.00  7.21           C  
ANISOU 4404  CA  THR B  83      681    828   1232    -73   -191    166       C  
ATOM   4405  C   THR B  83     -29.072 -14.196 133.361  1.00 12.35           C  
ANISOU 4405  C   THR B  83     1367   1466   1859    -81   -189    172       C  
ATOM   4406  O   THR B  83     -29.433 -13.020 133.300  1.00 11.79           O  
ANISOU 4406  O   THR B  83     1304   1396   1781    -89   -173    172       O  
ATOM   4407  CB  THR B  83     -29.314 -15.262 131.090  1.00  9.60           C  
ANISOU 4407  CB  THR B  83      975   1137   1536    -64   -169    166       C  
ATOM   4408  OG1 THR B  83     -29.987 -16.448 131.505  1.00 11.86           O  
ANISOU 4408  OG1 THR B  83     1273   1413   1820    -57   -176    170       O  
ATOM   4409  CG2 THR B  83     -28.617 -15.495 129.752  1.00  5.75           C  
ANISOU 4409  CG2 THR B  83      531    623   1031    -47   -137    160       C  
ATOM   4410  N   LYS B  84     -29.268 -14.974 134.454  1.00  9.20           N  
ANISOU 4410  N   LYS B  84      991   1056   1449    -79   -203    177       N  
ATOM   4411  CA  LYS B  84     -29.834 -14.469 135.705  1.00  8.91           C  
ANISOU 4411  CA  LYS B  84      991   1009   1386    -84   -202    183       C  
ATOM   4412  C   LYS B  84     -28.896 -13.386 136.287  1.00 13.41           C  
ANISOU 4412  C   LYS B  84     1570   1576   1951    -95   -220    175       C  
ATOM   4413  O   LYS B  84     -29.365 -12.392 136.850  1.00 13.92           O  
ANISOU 4413  O   LYS B  84     1659   1633   1997   -100   -211    174       O  
ATOM   4414  CB  LYS B  84     -30.003 -15.627 136.708  1.00 11.09           C  
ANISOU 4414  CB  LYS B  84     1287   1274   1651    -79   -217    192       C  
ATOM   4415  CG  LYS B  84     -30.978 -15.334 137.837  1.00 23.26           C  
ANISOU 4415  CG  LYS B  84     2868   2807   3162    -80   -204    202       C  
ATOM   4416  CD  LYS B  84     -31.133 -16.540 138.787  1.00 28.23           C  
ANISOU 4416  CD  LYS B  84     3518   3428   3781    -75   -216    216       C  
ATOM   4417  CE  LYS B  84     -31.764 -17.740 138.108  1.00 27.43           C  
ANISOU 4417  CE  LYS B  84     3398   3326   3700    -69   -207    225       C  
ATOM   4418  NZ  LYS B  84     -31.888 -18.897 139.033  1.00 26.49           N  
ANISOU 4418  NZ  LYS B  84     3298   3195   3572    -65   -220    241       N  
ATOM   4419  N   ASN B  85     -27.577 -13.548 136.061  1.00  9.18           N  
ANISOU 4419  N   ASN B  85     1010   1043   1436    -97   -245    169       N  
ATOM   4420  CA  ASN B  85     -26.560 -12.593 136.500  1.00  9.15           C  
ANISOU 4420  CA  ASN B  85     1006   1035   1436   -108   -267    162       C  
ATOM   4421  C   ASN B  85     -26.206 -11.621 135.352  1.00 13.00           C  
ANISOU 4421  C   ASN B  85     1464   1532   1945   -116   -251    159       C  
ATOM   4422  O   ASN B  85     -25.151 -10.976 135.385  1.00 12.80           O  
ANISOU 4422  O   ASN B  85     1423   1504   1935   -126   -270    154       O  
ATOM   4423  CB  ASN B  85     -25.306 -13.340 136.970  1.00  8.27           C  
ANISOU 4423  CB  ASN B  85      883    922   1339   -107   -306    161       C  
ATOM   4424  CG  ASN B  85     -25.604 -14.444 137.943  1.00 18.53           C  
ANISOU 4424  CG  ASN B  85     2209   2213   2620    -98   -322    168       C  
ATOM   4425  OD1 ASN B  85     -25.478 -15.630 137.627  1.00  9.26           O  
ANISOU 4425  OD1 ASN B  85     1019   1041   1459    -87   -327    172       O  
ATOM   4426  ND2 ASN B  85     -26.132 -14.084 139.105  1.00  9.07           N  
ANISOU 4426  ND2 ASN B  85     1053   1004   1389   -100   -326    171       N  
ATOM   4427  N   TYR B  86     -27.088 -11.549 134.320  1.00  9.58           N  
ANISOU 4427  N   TYR B  86     1021   1107   1513   -111   -218    162       N  
ATOM   4428  CA  TYR B  86     -26.920 -10.673 133.139  1.00  9.00           C  
ANISOU 4428  CA  TYR B  86      922   1043   1455   -116   -198    161       C  
ATOM   4429  C   TYR B  86     -25.708 -11.070 132.252  1.00 13.39           C  
ANISOU 4429  C   TYR B  86     1436   1612   2039   -113   -205    160       C  
ATOM   4430  O   TYR B  86     -25.337 -10.317 131.346  1.00 13.52           O  
ANISOU 4430  O   TYR B  86     1431   1637   2070   -119   -190    162       O  
ATOM   4431  CB  TYR B  86     -26.856  -9.173 133.542  1.00 10.09           C  
ANISOU 4431  CB  TYR B  86     1075   1171   1589   -130   -198    159       C  
ATOM   4432  CG  TYR B  86     -28.024  -8.706 134.394  1.00 11.61           C  
ANISOU 4432  CG  TYR B  86     1309   1351   1753   -130   -188    159       C  
ATOM   4433  CD1 TYR B  86     -29.287  -9.279 134.257  1.00 12.95           C  
ANISOU 4433  CD1 TYR B  86     1489   1523   1908   -118   -165    164       C  
ATOM   4434  CD2 TYR B  86     -27.901  -7.604 135.234  1.00 12.75           C  
ANISOU 4434  CD2 TYR B  86     1478   1479   1887   -140   -198    153       C  
ATOM   4435  CE1 TYR B  86     -30.366  -8.841 135.018  1.00 12.77           C  
ANISOU 4435  CE1 TYR B  86     1499   1490   1861   -116   -151    165       C  
ATOM   4436  CE2 TYR B  86     -28.979  -7.141 135.985  1.00 13.58           C  
ANISOU 4436  CE2 TYR B  86     1622   1574   1966   -136   -185    152       C  
ATOM   4437  CZ  TYR B  86     -30.212  -7.762 135.873  1.00 21.23           C  
ANISOU 4437  CZ  TYR B  86     2598   2547   2920   -123   -159    159       C  
ATOM   4438  OH  TYR B  86     -31.278  -7.308 136.611  1.00 23.19           O  
ANISOU 4438  OH  TYR B  86     2881   2786   3144   -118   -141    159       O  
ATOM   4439  N   ILE B  87     -25.133 -12.276 132.478  1.00  9.70           N  
ANISOU 4439  N   ILE B  87      958   1146   1580   -104   -224    158       N  
ATOM   4440  CA  ILE B  87     -24.070 -12.798 131.606  1.00  8.94           C  
ANISOU 4440  CA  ILE B  87      823   1064   1512    -96   -227    156       C  
ATOM   4441  C   ILE B  87     -24.713 -13.390 130.354  1.00 12.22           C  
ANISOU 4441  C   ILE B  87     1226   1493   1925    -82   -199    155       C  
ATOM   4442  O   ILE B  87     -25.582 -14.258 130.463  1.00 12.30           O  
ANISOU 4442  O   ILE B  87     1253   1499   1923    -72   -198    155       O  
ATOM   4443  CB  ILE B  87     -23.174 -13.843 132.354  1.00 12.02           C  
ANISOU 4443  CB  ILE B  87     1206   1449   1913    -90   -261    154       C  
ATOM   4444  CG1 ILE B  87     -22.630 -13.259 133.694  1.00 12.91           C  
ANISOU 4444  CG1 ILE B  87     1336   1546   2021   -104   -294    154       C  
ATOM   4445  CG2 ILE B  87     -22.017 -14.336 131.440  1.00 11.92           C  
ANISOU 4445  CG2 ILE B  87     1148   1450   1931    -80   -261    151       C  
ATOM   4446  CD1 ILE B  87     -21.901 -14.309 134.612  1.00 17.32           C  
ANISOU 4446  CD1 ILE B  87     1897   2097   2586    -97   -332    154       C  
ATOM   4447  N   GLN B  88     -24.379 -12.849 129.178  1.00  7.82           N  
ANISOU 4447  N   GLN B  88      643    950   1379    -81   -178    157       N  
ATOM   4448  CA  GLN B  88     -25.034 -13.257 127.935  1.00  7.12           C  
ANISOU 4448  CA  GLN B  88      548    874   1284    -67   -152    155       C  
ATOM   4449  C   GLN B  88     -24.566 -14.609 127.439  1.00 11.23           C  
ANISOU 4449  C   GLN B  88     1050   1401   1814    -47   -158    147       C  
ATOM   4450  O   GLN B  88     -23.371 -14.912 127.487  1.00 10.75           O  
ANISOU 4450  O   GLN B  88      965   1345   1775    -43   -170    145       O  
ATOM   4451  CB  GLN B  88     -24.847 -12.194 126.838  1.00  8.18           C  
ANISOU 4451  CB  GLN B  88      666   1022   1422    -72   -126    161       C  
ATOM   4452  CG  GLN B  88     -25.507 -10.860 127.154  1.00 13.76           C  
ANISOU 4452  CG  GLN B  88     1392   1719   2117    -88   -117    168       C  
ATOM   4453  CD  GLN B  88     -27.010 -10.965 127.207  1.00 22.02           C  
ANISOU 4453  CD  GLN B  88     2467   2760   3142    -84   -107    168       C  
ATOM   4454  OE1 GLN B  88     -27.694 -10.936 126.183  1.00 16.70           O  
ANISOU 4454  OE1 GLN B  88     1790   2094   2459    -76    -87    169       O  
ATOM   4455  NE2 GLN B  88     -27.559 -11.005 128.413  1.00 10.55           N  
ANISOU 4455  NE2 GLN B  88     1040   1291   1679    -89   -121    167       N  
ATOM   4456  N   ASP B  89     -25.501 -15.409 126.910  1.00  7.58           N  
ANISOU 4456  N   ASP B  89      600    941   1341    -34   -150    142       N  
ATOM   4457  CA  ASP B  89     -25.172 -16.628 126.196  1.00  6.89           C  
ANISOU 4457  CA  ASP B  89      498    859   1262    -12   -152    131       C  
ATOM   4458  C   ASP B  89     -25.265 -16.338 124.699  1.00 11.28           C  
ANISOU 4458  C   ASP B  89     1041   1434   1812     -2   -124    128       C  
ATOM   4459  O   ASP B  89     -26.369 -16.207 124.164  1.00  9.77           O  
ANISOU 4459  O   ASP B  89      864   1243   1604     -1   -112    128       O  
ATOM   4460  CB  ASP B  89     -26.130 -17.778 126.598  1.00  7.65           C  
ANISOU 4460  CB  ASP B  89      615    940   1351     -5   -165    127       C  
ATOM   4461  CG  ASP B  89     -25.790 -19.122 125.952  1.00 11.25           C  
ANISOU 4461  CG  ASP B  89     1060   1398   1818     18   -173    115       C  
ATOM   4462  OD1 ASP B  89     -25.568 -19.151 124.718  1.00  9.72           O  
ANISOU 4462  OD1 ASP B  89      851   1220   1624     31   -155    106       O  
ATOM   4463  OD2 ASP B  89     -25.846 -20.148 126.658  1.00 17.53           O  
ANISOU 4463  OD2 ASP B  89     1863   2176   2620     23   -195    113       O  
ATOM   4464  N   ASP B  90     -24.105 -16.111 124.047  1.00  8.83           N  
ANISOU 4464  N   ASP B  90      701   1139   1515      4   -113    128       N  
ATOM   4465  CA  ASP B  90     -24.057 -15.718 122.636  1.00  8.58           C  
ANISOU 4465  CA  ASP B  90      658   1128   1475     14    -83    128       C  
ATOM   4466  C   ASP B  90     -24.741 -16.742 121.718  1.00 11.68           C  
ANISOU 4466  C   ASP B  90     1060   1524   1852     37    -79    113       C  
ATOM   4467  O   ASP B  90     -25.339 -16.359 120.708  1.00 10.12           O  
ANISOU 4467  O   ASP B  90      871   1339   1637     42    -59    113       O  
ATOM   4468  CB  ASP B  90     -22.615 -15.486 122.192  1.00 10.97           C  
ANISOU 4468  CB  ASP B  90      925   1447   1797     19    -71    131       C  
ATOM   4469  CG  ASP B  90     -22.511 -14.866 120.821  1.00 18.68           C  
ANISOU 4469  CG  ASP B  90     1891   2445   2762     26    -36    136       C  
ATOM   4470  OD1 ASP B  90     -23.002 -13.730 120.646  1.00 17.96           O  
ANISOU 4470  OD1 ASP B  90     1808   2355   2660     10    -22    149       O  
ATOM   4471  OD2 ASP B  90     -21.965 -15.526 119.912  1.00 24.70           O  
ANISOU 4471  OD2 ASP B  90     2637   3223   3524     49    -21    127       O  
ATOM   4472  N   GLU B  91     -24.646 -18.044 122.062  1.00  8.89           N  
ANISOU 4472  N   GLU B  91      710   1161   1508     51   -100    101       N  
ATOM   4473  CA  GLU B  91     -25.277 -19.108 121.273  1.00  8.78           C  
ANISOU 4473  CA  GLU B  91      707   1145   1484     72   -102     84       C  
ATOM   4474  C   GLU B  91     -26.815 -18.964 121.297  1.00 12.68           C  
ANISOU 4474  C   GLU B  91     1229   1628   1961     63   -105     87       C  
ATOM   4475  O   GLU B  91     -27.463 -19.152 120.268  1.00 12.30           O  
ANISOU 4475  O   GLU B  91     1189   1586   1897     74    -97     79       O  
ATOM   4476  CB  GLU B  91     -24.834 -20.500 121.788  1.00 10.16           C  
ANISOU 4476  CB  GLU B  91      879   1305   1677     87   -127     72       C  
ATOM   4477  CG  GLU B  91     -25.266 -21.660 120.897  1.00 16.81           C  
ANISOU 4477  CG  GLU B  91     1731   2145   2513    111   -131     52       C  
ATOM   4478  CD  GLU B  91     -26.612 -22.269 121.247  1.00 25.90           C  
ANISOU 4478  CD  GLU B  91     2909   3274   3660    105   -150     50       C  
ATOM   4479  OE1 GLU B  91     -27.020 -22.173 122.426  1.00 14.38           O  
ANISOU 4479  OE1 GLU B  91     1459   1799   2207     86   -165     64       O  
ATOM   4480  OE2 GLU B  91     -27.201 -22.941 120.372  1.00 16.23           O  
ANISOU 4480  OE2 GLU B  91     1694   2046   2425    120   -153     35       O  
ATOM   4481  N   TRP B  92     -27.381 -18.524 122.457  1.00  9.31           N  
ANISOU 4481  N   TRP B  92      815   1187   1536     41   -116    100       N  
ATOM   4482  CA  TRP B  92     -28.823 -18.257 122.577  1.00  9.26           C  
ANISOU 4482  CA  TRP B  92      830   1171   1517     31   -115    106       C  
ATOM   4483  C   TRP B  92     -29.214 -17.034 121.752  1.00 13.06           C  
ANISOU 4483  C   TRP B  92     1313   1667   1983     26    -92    113       C  
ATOM   4484  O   TRP B  92     -30.143 -17.105 120.948  1.00 12.67           O  
ANISOU 4484  O   TRP B  92     1273   1620   1922     32    -88    110       O  
ATOM   4485  CB  TRP B  92     -29.215 -18.028 124.048  1.00  7.71           C  
ANISOU 4485  CB  TRP B  92      648    957   1325     12   -127    118       C  
ATOM   4486  CG  TRP B  92     -29.174 -19.254 124.912  1.00  8.56           C  
ANISOU 4486  CG  TRP B  92      761   1047   1445     16   -151    115       C  
ATOM   4487  CD1 TRP B  92     -28.815 -20.518 124.538  1.00 11.42           C  
ANISOU 4487  CD1 TRP B  92     1117   1404   1817     33   -165    102       C  
ATOM   4488  CD2 TRP B  92     -29.513 -19.326 126.298  1.00  8.43           C  
ANISOU 4488  CD2 TRP B  92      761   1014   1429      2   -164    126       C  
ATOM   4489  NE1 TRP B  92     -28.920 -21.374 125.608  1.00 10.90           N  
ANISOU 4489  NE1 TRP B  92     1061   1319   1762     30   -187    106       N  
ATOM   4490  CE2 TRP B  92     -29.340 -20.666 126.704  1.00 12.48           C  
ANISOU 4490  CE2 TRP B  92     1275   1511   1954     11   -186    122       C  
ATOM   4491  CE3 TRP B  92     -29.943 -18.380 127.247  1.00  9.64           C  
ANISOU 4491  CE3 TRP B  92      928   1161   1572    -15   -159    140       C  
ATOM   4492  CZ2 TRP B  92     -29.600 -21.090 128.013  1.00 11.92           C  
ANISOU 4492  CZ2 TRP B  92     1221   1424   1885      3   -201    133       C  
ATOM   4493  CZ3 TRP B  92     -30.192 -18.800 128.542  1.00 11.10           C  
ANISOU 4493  CZ3 TRP B  92     1130   1330   1756    -22   -173    148       C  
ATOM   4494  CH2 TRP B  92     -30.003 -20.134 128.919  1.00 11.97           C  
ANISOU 4494  CH2 TRP B  92     1243   1428   1878    -14   -194    147       C  
ATOM   4495  N   ASN B  93     -28.515 -15.886 121.980  1.00  9.84           N  
ANISOU 4495  N   ASN B  93      894   1266   1577     13    -79    124       N  
ATOM   4496  CA  ASN B  93     -28.816 -14.614 121.302  1.00  9.67           C  
ANISOU 4496  CA  ASN B  93      874   1256   1543      6    -57    135       C  
ATOM   4497  C   ASN B  93     -28.782 -14.748 119.788  1.00 13.28           C  
ANISOU 4497  C   ASN B  93     1327   1733   1987     25    -41    129       C  
ATOM   4498  O   ASN B  93     -29.598 -14.133 119.103  1.00 12.89           O  
ANISOU 4498  O   ASN B  93     1288   1688   1922     24    -30    135       O  
ATOM   4499  CB  ASN B  93     -27.861 -13.509 121.767  1.00  8.39           C  
ANISOU 4499  CB  ASN B  93      700   1097   1392    -10    -49    147       C  
ATOM   4500  CG  ASN B  93     -28.023 -13.131 123.226  1.00 30.26           C  
ANISOU 4500  CG  ASN B  93     3481   3848   4168    -28    -65    153       C  
ATOM   4501  OD1 ASN B  93     -28.779 -13.756 123.980  1.00 24.82           O  
ANISOU 4501  OD1 ASN B  93     2809   3145   3476    -29    -79    150       O  
ATOM   4502  ND2 ASN B  93     -27.317 -12.094 123.651  1.00 21.99           N  
ANISOU 4502  ND2 ASN B  93     2426   2799   3129    -44    -62    162       N  
ATOM   4503  N   ASN B  94     -27.844 -15.568 119.253  1.00 10.10           N  
ANISOU 4503  N   ASN B  94      909   1340   1588     43    -40    117       N  
ATOM   4504  CA  ASN B  94     -27.761 -15.806 117.811  1.00  9.75           C  
ANISOU 4504  CA  ASN B  94      864   1315   1527     64    -24    109       C  
ATOM   4505  C   ASN B  94     -29.008 -16.541 117.298  1.00 14.04           C  
ANISOU 4505  C   ASN B  94     1429   1850   2054     75    -38     96       C  
ATOM   4506  O   ASN B  94     -29.555 -16.165 116.260  1.00 14.75           O  
ANISOU 4506  O   ASN B  94     1529   1951   2123     83    -27     97       O  
ATOM   4507  CB  ASN B  94     -26.493 -16.590 117.457  1.00  9.49           C  
ANISOU 4507  CB  ASN B  94      810   1293   1502     84    -19     97       C  
ATOM   4508  CG  ASN B  94     -26.330 -16.815 115.970  1.00 24.57           C  
ANISOU 4508  CG  ASN B  94     2721   3223   3389    109      1     87       C  
ATOM   4509  OD1 ASN B  94     -26.385 -15.880 115.166  1.00 19.74           O  
ANISOU 4509  OD1 ASN B  94     2111   2628   2760    107     25    100       O  
ATOM   4510  ND2 ASN B  94     -26.164 -18.064 115.572  1.00 14.76           N  
ANISOU 4510  ND2 ASN B  94     1482   1980   2146    133     -8     65       N  
ATOM   4511  N   LEU B  95     -29.470 -17.582 118.038  1.00 10.00           N  
ANISOU 4511  N   LEU B  95      925   1319   1556     75    -64     86       N  
ATOM   4512  CA  LEU B  95     -30.684 -18.329 117.667  1.00  9.15           C  
ANISOU 4512  CA  LEU B  95      835   1199   1441     82    -81     75       C  
ATOM   4513  C   LEU B  95     -31.901 -17.406 117.659  1.00 10.97           C  
ANISOU 4513  C   LEU B  95     1078   1427   1664     67    -78     89       C  
ATOM   4514  O   LEU B  95     -32.699 -17.443 116.721  1.00 10.22           O  
ANISOU 4514  O   LEU B  95      993   1335   1554     76    -80     84       O  
ATOM   4515  CB  LEU B  95     -30.924 -19.509 118.644  1.00  9.12           C  
ANISOU 4515  CB  LEU B  95      835   1172   1458     80   -108     68       C  
ATOM   4516  CG  LEU B  95     -29.905 -20.654 118.592  1.00 13.91           C  
ANISOU 4516  CG  LEU B  95     1433   1777   2076     99   -117     51       C  
ATOM   4517  CD1 LEU B  95     -30.142 -21.630 119.711  1.00 13.89           C  
ANISOU 4517  CD1 LEU B  95     1434   1748   2095     93   -143     50       C  
ATOM   4518  CD2 LEU B  95     -29.952 -21.378 117.241  1.00 16.51           C  
ANISOU 4518  CD2 LEU B  95     1768   2113   2390    125   -118     29       C  
ATOM   4519  N   VAL B  96     -32.033 -16.568 118.701  1.00  7.38           N  
ANISOU 4519  N   VAL B  96      621    964   1218     46    -73    107       N  
ATOM   4520  CA  VAL B  96     -33.135 -15.604 118.828  1.00  7.55           C  
ANISOU 4520  CA  VAL B  96      653    982   1234     33    -67    121       C  
ATOM   4521  C   VAL B  96     -33.098 -14.584 117.671  1.00 11.47           C  
ANISOU 4521  C   VAL B  96     1149   1496   1711     38    -48    128       C  
ATOM   4522  O   VAL B  96     -34.106 -14.389 116.984  1.00 10.09           O  
ANISOU 4522  O   VAL B  96      985   1323   1527     42    -50    129       O  
ATOM   4523  CB  VAL B  96     -33.093 -14.898 120.213  1.00 11.30           C  
ANISOU 4523  CB  VAL B  96     1127   1444   1720     12    -65    135       C  
ATOM   4524  CG1 VAL B  96     -34.132 -13.787 120.298  1.00 10.46           C  
ANISOU 4524  CG1 VAL B  96     1030   1334   1609      2    -55    150       C  
ATOM   4525  CG2 VAL B  96     -33.281 -15.905 121.343  1.00 11.24           C  
ANISOU 4525  CG2 VAL B  96     1124   1418   1728      8    -84    132       C  
ATOM   4526  N   TRP B  97     -31.916 -13.979 117.434  1.00  9.05           N  
ANISOU 4526  N   TRP B  97      831   1205   1402     38    -29    133       N  
ATOM   4527  CA  TRP B  97     -31.694 -13.006 116.359  1.00  9.39           C  
ANISOU 4527  CA  TRP B  97      873   1266   1427     42     -7    144       C  
ATOM   4528  C   TRP B  97     -32.077 -13.593 114.998  1.00 13.87           C  
ANISOU 4528  C   TRP B  97     1451   1846   1972     64     -9    131       C  
ATOM   4529  O   TRP B  97     -32.881 -12.998 114.276  1.00 13.84           O  
ANISOU 4529  O   TRP B  97     1460   1848   1952     66     -6    139       O  
ATOM   4530  CB  TRP B  97     -30.221 -12.566 116.359  1.00  8.55           C  
ANISOU 4530  CB  TRP B  97      749   1173   1328     39     12    150       C  
ATOM   4531  CG  TRP B  97     -29.827 -11.667 115.222  1.00  9.97           C  
ANISOU 4531  CG  TRP B  97      924   1372   1490     44     38    163       C  
ATOM   4532  CD1 TRP B  97     -29.382 -12.058 113.992  1.00 13.08           C  
ANISOU 4532  CD1 TRP B  97     1318   1788   1864     66     53    157       C  
ATOM   4533  CD2 TRP B  97     -29.588 -10.257 115.304  1.00  9.98           C  
ANISOU 4533  CD2 TRP B  97      922   1375   1496     27     56    186       C  
ATOM   4534  NE1 TRP B  97     -28.946 -10.967 113.278  1.00 12.92           N  
ANISOU 4534  NE1 TRP B  97     1293   1783   1833     63     80    177       N  
ATOM   4535  CE2 TRP B  97     -29.059  -9.847 114.060  1.00 14.41           C  
ANISOU 4535  CE2 TRP B  97     1478   1958   2038     38     81    196       C  
ATOM   4536  CE3 TRP B  97     -29.779  -9.291 116.309  1.00 11.33           C  
ANISOU 4536  CE3 TRP B  97     1093   1529   1683      3     53    199       C  
ATOM   4537  CZ2 TRP B  97     -28.757  -8.509 113.779  1.00 14.22           C  
ANISOU 4537  CZ2 TRP B  97     1450   1939   2015     25    103    220       C  
ATOM   4538  CZ3 TRP B  97     -29.485  -7.965 116.027  1.00 13.02           C  
ANISOU 4538  CZ3 TRP B  97     1304   1746   1899     -9     72    221       C  
ATOM   4539  CH2 TRP B  97     -28.968  -7.587 114.781  1.00 13.99           C  
ANISOU 4539  CH2 TRP B  97     1420   1889   2006      1     96    232       C  
ATOM   4540  N   GLU B  98     -31.533 -14.785 114.666  1.00 10.53           N  
ANISOU 4540  N   GLU B  98     1025   1428   1547     83    -16    111       N  
ATOM   4541  CA  GLU B  98     -31.790 -15.437 113.379  1.00 10.19           C  
ANISOU 4541  CA  GLU B  98      996   1396   1481    107    -20     95       C  
ATOM   4542  C   GLU B  98     -33.258 -15.818 113.197  1.00 13.19           C  
ANISOU 4542  C   GLU B  98     1393   1762   1857    107    -46     88       C  
ATOM   4543  O   GLU B  98     -33.776 -15.713 112.092  1.00 12.74           O  
ANISOU 4543  O   GLU B  98     1351   1715   1776    120    -48     85       O  
ATOM   4544  CB  GLU B  98     -30.884 -16.673 113.197  1.00 11.69           C  
ANISOU 4544  CB  GLU B  98     1179   1589   1673    127    -24     73       C  
ATOM   4545  CG  GLU B  98     -29.422 -16.325 112.964  1.00 21.20           C  
ANISOU 4545  CG  GLU B  98     2364   2814   2878    134      5     78       C  
ATOM   4546  CD  GLU B  98     -29.141 -15.646 111.637  1.00 38.35           C  
ANISOU 4546  CD  GLU B  98     4541   5012   5018    148     34     86       C  
ATOM   4547  OE1 GLU B  98     -29.457 -16.244 110.584  1.00 38.30           O  
ANISOU 4547  OE1 GLU B  98     4553   5015   4986    172     30     68       O  
ATOM   4548  OE2 GLU B  98     -28.539 -14.549 111.650  1.00 27.31           O  
ANISOU 4548  OE2 GLU B  98     3129   3626   3622    136     60    108       O  
ATOM   4549  N   GLU B  99     -33.937 -16.253 114.287  1.00  9.54           N  
ANISOU 4549  N   GLU B  99      929   1276   1419     93    -67     88       N  
ATOM   4550  CA  GLU B  99     -35.342 -16.687 114.200  1.00  9.51           C  
ANISOU 4550  CA  GLU B  99      937   1257   1421     91    -92     84       C  
ATOM   4551  C   GLU B  99     -36.301 -15.521 113.897  1.00 13.02           C  
ANISOU 4551  C   GLU B  99     1386   1703   1856     82    -86    102       C  
ATOM   4552  O   GLU B  99     -37.169 -15.659 113.037  1.00 13.50           O  
ANISOU 4552  O   GLU B  99     1459   1766   1906     91   -101     97       O  
ATOM   4553  CB  GLU B  99     -35.774 -17.442 115.472  1.00 10.89           C  
ANISOU 4553  CB  GLU B  99     1106   1406   1624     77   -110     83       C  
ATOM   4554  CG  GLU B  99     -37.127 -18.147 115.336  1.00 20.22           C  
ANISOU 4554  CG  GLU B  99     2295   2570   2817     77   -138     77       C  
ATOM   4555  CD  GLU B  99     -37.194 -19.229 114.268  1.00 33.23           C  
ANISOU 4555  CD  GLU B  99     3953   4217   4454     98   -160     51       C  
ATOM   4556  OE1 GLU B  99     -36.192 -19.962 114.097  1.00 22.08           O  
ANISOU 4556  OE1 GLU B  99     2541   2810   3039    112   -159     35       O  
ATOM   4557  OE2 GLU B  99     -38.282 -19.405 113.675  1.00 23.24           O  
ANISOU 4557  OE2 GLU B  99     2695   2945   3188    100   -181     47       O  
ATOM   4558  N   TYR B 100     -36.130 -14.363 114.587  1.00  9.65           N  
ANISOU 4558  N   TYR B 100      954   1278   1436     65    -66    123       N  
ATOM   4559  CA  TYR B 100     -36.970 -13.175 114.320  1.00  9.04           C  
ANISOU 4559  CA  TYR B 100      881   1202   1353     58    -59    141       C  
ATOM   4560  C   TYR B 100     -36.798 -12.686 112.887  1.00 12.73           C  
ANISOU 4560  C   TYR B 100     1358   1689   1789     74    -50    143       C  
ATOM   4561  O   TYR B 100     -37.785 -12.441 112.202  1.00 12.48           O  
ANISOU 4561  O   TYR B 100     1337   1658   1749     79    -62    146       O  
ATOM   4562  CB  TYR B 100     -36.657 -12.033 115.309  1.00  9.77           C  
ANISOU 4562  CB  TYR B 100      966   1289   1457     40    -39    160       C  
ATOM   4563  CG  TYR B 100     -37.217 -12.250 116.700  1.00 10.58           C  
ANISOU 4563  CG  TYR B 100     1065   1370   1583     25    -48    163       C  
ATOM   4564  CD1 TYR B 100     -38.587 -12.401 116.905  1.00 11.91           C  
ANISOU 4564  CD1 TYR B 100     1237   1526   1763     22    -61    166       C  
ATOM   4565  CD2 TYR B 100     -36.405 -12.130 117.823  1.00 10.91           C  
ANISOU 4565  CD2 TYR B 100     1102   1407   1637     13    -40    166       C  
ATOM   4566  CE1 TYR B 100     -39.116 -12.544 118.186  1.00 12.07           C  
ANISOU 4566  CE1 TYR B 100     1254   1527   1803     10    -63    172       C  
ATOM   4567  CE2 TYR B 100     -36.928 -12.238 119.111  1.00 11.61           C  
ANISOU 4567  CE2 TYR B 100     1192   1477   1742      1    -45    170       C  
ATOM   4568  CZ  TYR B 100     -38.281 -12.469 119.287  1.00 15.70           C  
ANISOU 4568  CZ  TYR B 100     1713   1983   2269      0    -54    173       C  
ATOM   4569  OH  TYR B 100     -38.792 -12.603 120.553  1.00 12.44           O  
ANISOU 4569  OH  TYR B 100     1302   1555   1872    -11    -55    179       O  
ATOM   4570  N   LEU B 101     -35.538 -12.551 112.425  1.00  9.99           N  
ANISOU 4570  N   LEU B 101     1008   1361   1428     82    -29    143       N  
ATOM   4571  CA  LEU B 101     -35.259 -12.076 111.062  1.00 10.05           C  
ANISOU 4571  CA  LEU B 101     1026   1391   1403     97    -14    147       C  
ATOM   4572  C   LEU B 101     -35.726 -13.081 110.004  1.00 13.49           C  
ANISOU 4572  C   LEU B 101     1478   1831   1816    120    -36    125       C  
ATOM   4573  O   LEU B 101     -36.214 -12.677 108.949  1.00 11.96           O  
ANISOU 4573  O   LEU B 101     1300   1648   1596    132    -38    130       O  
ATOM   4574  CB  LEU B 101     -33.766 -11.749 110.887  1.00 10.29           C  
ANISOU 4574  CB  LEU B 101     1045   1439   1427    100     17    153       C  
ATOM   4575  CG  LEU B 101     -33.265 -10.501 111.648  1.00 14.81           C  
ANISOU 4575  CG  LEU B 101     1603   2007   2017     77     38    178       C  
ATOM   4576  CD1 LEU B 101     -31.783 -10.344 111.503  1.00 15.12           C  
ANISOU 4576  CD1 LEU B 101     1626   2063   2057     79     64    183       C  
ATOM   4577  CD2 LEU B 101     -33.981  -9.234 111.166  1.00 17.13           C  
ANISOU 4577  CD2 LEU B 101     1908   2302   2300     71     45    201       C  
ATOM   4578  N   LYS B 102     -35.647 -14.399 110.324  1.00 10.96           N  
ANISOU 4578  N   LYS B 102     1156   1501   1508    127    -55    101       N  
ATOM   4579  CA  LYS B 102     -36.169 -15.463 109.455  1.00 11.33           C  
ANISOU 4579  CA  LYS B 102     1220   1546   1539    148    -83     76       C  
ATOM   4580  C   LYS B 102     -37.697 -15.308 109.287  1.00 15.93           C  
ANISOU 4580  C   LYS B 102     1812   2115   2126    141   -111     80       C  
ATOM   4581  O   LYS B 102     -38.209 -15.392 108.166  1.00 15.97           O  
ANISOU 4581  O   LYS B 102     1836   2128   2105    157   -126     72       O  
ATOM   4582  CB  LYS B 102     -35.825 -16.853 110.047  1.00 13.77           C  
ANISOU 4582  CB  LYS B 102     1523   1840   1869    152   -100     52       C  
ATOM   4583  CG  LYS B 102     -36.536 -18.021 109.370  1.00 26.05           C  
ANISOU 4583  CG  LYS B 102     3095   3385   3418    168   -136     25       C  
ATOM   4584  CD  LYS B 102     -36.187 -19.354 110.048  1.00 32.06           C  
ANISOU 4584  CD  LYS B 102     3850   4127   4204    170   -153      5       C  
ATOM   4585  CE  LYS B 102     -36.996 -20.509 109.502  1.00 40.30           C  
ANISOU 4585  CE  LYS B 102     4909   5153   5249    182   -193    -21       C  
ATOM   4586  NZ  LYS B 102     -38.440 -20.387 109.846  1.00 46.04           N  
ANISOU 4586  NZ  LYS B 102     5634   5860   5999    163   -219    -10       N  
ATOM   4587  N   GLN B 103     -38.408 -15.004 110.394  1.00 12.56           N  
ANISOU 4587  N   GLN B 103     1371   1669   1732    119   -117     94       N  
ATOM   4588  CA  GLN B 103     -39.863 -14.830 110.367  1.00 12.62           C  
ANISOU 4588  CA  GLN B 103     1381   1662   1752    112   -142    101       C  
ATOM   4589  C   GLN B 103     -40.278 -13.511 109.675  1.00 16.72           C  
ANISOU 4589  C   GLN B 103     1907   2194   2252    113   -131    122       C  
ATOM   4590  O   GLN B 103     -41.285 -13.484 108.962  1.00 15.64           O  
ANISOU 4590  O   GLN B 103     1780   2054   2108    120   -155    121       O  
ATOM   4591  CB  GLN B 103     -40.449 -14.914 111.786  1.00 13.69           C  
ANISOU 4591  CB  GLN B 103     1498   1775   1927     90   -145    111       C  
ATOM   4592  CG  GLN B 103     -40.228 -16.287 112.464  1.00 23.20           C  
ANISOU 4592  CG  GLN B 103     2697   2964   3153     88   -161     93       C  
ATOM   4593  CD  GLN B 103     -40.970 -17.419 111.764  1.00 27.13           C  
ANISOU 4593  CD  GLN B 103     3203   3450   3653     99   -199     71       C  
ATOM   4594  OE1 GLN B 103     -41.976 -17.212 111.074  1.00 17.45           O  
ANISOU 4594  OE1 GLN B 103     1983   2223   2424    102   -219     73       O  
ATOM   4595  NE2 GLN B 103     -40.557 -18.643 112.031  1.00 19.85           N  
ANISOU 4595  NE2 GLN B 103     2282   2517   2743    103   -213     52       N  
ATOM   4596  N   ILE B 104     -39.503 -12.415 109.896  1.00 13.49           N  
ANISOU 4596  N   ILE B 104     1494   1796   1836    106    -97    142       N  
ATOM   4597  CA  ILE B 104     -39.749 -11.127 109.215  1.00 13.33           C  
ANISOU 4597  CA  ILE B 104     1481   1786   1796    108    -84    164       C  
ATOM   4598  C   ILE B 104     -39.562 -11.284 107.697  1.00 18.51           C  
ANISOU 4598  C   ILE B 104     2160   2463   2410    131    -88    156       C  
ATOM   4599  O   ILE B 104     -40.419 -10.853 106.921  1.00 18.90           O  
ANISOU 4599  O   ILE B 104     2222   2514   2445    138   -104    164       O  
ATOM   4600  CB  ILE B 104     -38.832  -9.996 109.792  1.00 15.62           C  
ANISOU 4600  CB  ILE B 104     1762   2081   2092     94    -47    185       C  
ATOM   4601  CG1 ILE B 104     -39.142  -9.715 111.295  1.00 15.20           C  
ANISOU 4601  CG1 ILE B 104     1694   2007   2076     72    -45    193       C  
ATOM   4602  CG2 ILE B 104     -38.931  -8.706 108.940  1.00 16.43           C  
ANISOU 4602  CG2 ILE B 104     1875   2195   2172     97    -32    209       C  
ATOM   4603  CD1 ILE B 104     -40.575  -9.174 111.579  1.00 23.79           C  
ANISOU 4603  CD1 ILE B 104     2780   3078   3181     66    -59    205       C  
ATOM   4604  N   ALA B 105     -38.441 -11.922 107.278  1.00 15.37           N  
ANISOU 4604  N   ALA B 105     1766   2080   1992    145    -75    141       N  
ATOM   4605  CA  ALA B 105     -38.158 -12.172 105.860  1.00 15.32           C  
ANISOU 4605  CA  ALA B 105     1784   2096   1941    171    -75    130       C  
ATOM   4606  C   ALA B 105     -39.278 -12.980 105.223  1.00 17.15           C  
ANISOU 4606  C   ALA B 105     2033   2318   2164    184   -119    110       C  
ATOM   4607  O   ALA B 105     -39.658 -12.713 104.087  1.00 17.01           O  
ANISOU 4607  O   ALA B 105     2038   2313   2111    200   -129    111       O  
ATOM   4608  CB  ALA B 105     -36.833 -12.911 105.714  1.00 16.23           C  
ANISOU 4608  CB  ALA B 105     1898   2226   2044    185    -54    113       C  
ATOM   4609  N   SER B 106     -39.834 -13.949 105.973  1.00 12.75           N  
ANISOU 4609  N   SER B 106     1466   1739   1641    175   -148     92       N  
ATOM   4610  CA  SER B 106     -40.933 -14.781 105.491  1.00 12.98           C  
ANISOU 4610  CA  SER B 106     1506   1754   1672    183   -194     72       C  
ATOM   4611  C   SER B 106     -42.206 -13.943 105.253  1.00 17.33           C  
ANISOU 4611  C   SER B 106     2057   2298   2228    176   -213     92       C  
ATOM   4612  O   SER B 106     -42.843 -14.078 104.204  1.00 18.58           O  
ANISOU 4612  O   SER B 106     2236   2460   2362    191   -243     84       O  
ATOM   4613  CB  SER B 106     -41.215 -15.910 106.474  1.00 15.37           C  
ANISOU 4613  CB  SER B 106     1793   2032   2016    171   -216     56       C  
ATOM   4614  OG  SER B 106     -42.229 -16.767 105.988  1.00 21.01           O  
ANISOU 4614  OG  SER B 106     2517   2730   2736    178   -262     36       O  
ATOM   4615  N   ILE B 107     -42.543 -13.030 106.207  1.00 13.01           N  
ANISOU 4615  N   ILE B 107     1490   1742   1712    155   -197    118       N  
ATOM   4616  CA  ILE B 107     -43.697 -12.124 106.050  1.00 12.27           C  
ANISOU 4616  CA  ILE B 107     1393   1641   1626    149   -210    140       C  
ATOM   4617  C   ILE B 107     -43.485 -11.191 104.851  1.00 16.35           C  
ANISOU 4617  C   ILE B 107     1933   2180   2099    165   -200    154       C  
ATOM   4618  O   ILE B 107     -44.432 -10.913 104.117  1.00 16.34           O  
ANISOU 4618  O   ILE B 107     1943   2178   2089    172   -228    159       O  
ATOM   4619  CB  ILE B 107     -43.976 -11.324 107.360  1.00 14.47           C  
ANISOU 4619  CB  ILE B 107     1647   1906   1945    126   -189    163       C  
ATOM   4620  CG1 ILE B 107     -44.182 -12.273 108.556  1.00 14.16           C  
ANISOU 4620  CG1 ILE B 107     1588   1847   1946    111   -197    151       C  
ATOM   4621  CG2 ILE B 107     -45.184 -10.376 107.178  1.00 14.08           C  
ANISOU 4621  CG2 ILE B 107     1594   1849   1907    123   -202    184       C  
ATOM   4622  CD1 ILE B 107     -44.201 -11.575 109.925  1.00 20.15           C  
ANISOU 4622  CD1 ILE B 107     2327   2594   2736     91   -171    170       C  
ATOM   4623  N   ASN B 108     -42.217 -10.743 104.625  1.00 12.26           N  
ANISOU 4623  N   ASN B 108     1423   1683   1554    170   -161    161       N  
ATOM   4624  CA  ASN B 108     -41.883  -9.879 103.482  1.00 12.66           C  
ANISOU 4624  CA  ASN B 108     1495   1754   1559    184   -145    178       C  
ATOM   4625  C   ASN B 108     -42.185 -10.576 102.148  1.00 18.27           C  
ANISOU 4625  C   ASN B 108     2238   2477   2228    210   -176    158       C  
ATOM   4626  O   ASN B 108     -42.769  -9.965 101.258  1.00 18.54           O  
ANISOU 4626  O   ASN B 108     2291   2518   2237    221   -190    171       O  
ATOM   4627  CB  ASN B 108     -40.409  -9.436 103.540  1.00 12.64           C  
ANISOU 4627  CB  ASN B 108     1491   1771   1542    184    -96    189       C  
ATOM   4628  CG  ASN B 108     -40.103  -8.480 104.675  1.00 27.37           C  
ANISOU 4628  CG  ASN B 108     3331   3625   3441    159    -68    213       C  
ATOM   4629  OD1 ASN B 108     -40.997  -7.851 105.254  1.00 19.66           O  
ANISOU 4629  OD1 ASN B 108     2346   2632   2494    145    -78    227       O  
ATOM   4630  ND2 ASN B 108     -38.822  -8.282 104.952  1.00 16.04           N  
ANISOU 4630  ND2 ASN B 108     1887   2202   2005    154    -31    218       N  
ATOM   4631  N   ILE B 109     -41.820 -11.873 102.028  1.00 15.75           N  
ANISOU 4631  N   ILE B 109     1924   2158   1902    222   -189    124       N  
ATOM   4632  CA  ILE B 109     -42.111 -12.668 100.818  1.00 16.70           C  
ANISOU 4632  CA  ILE B 109     2077   2286   1983    248   -223     98       C  
ATOM   4633  C   ILE B 109     -43.634 -12.659 100.515  1.00 22.18           C  
ANISOU 4633  C   ILE B 109     2775   2963   2689    246   -275     98       C  
ATOM   4634  O   ILE B 109     -44.030 -12.477  99.363  1.00 22.41           O  
ANISOU 4634  O   ILE B 109     2834   3003   2678    265   -297     97       O  
ATOM   4635  CB  ILE B 109     -41.552 -14.141 100.963  1.00 19.59           C  
ANISOU 4635  CB  ILE B 109     2445   2647   2352    258   -232     60       C  
ATOM   4636  CG1 ILE B 109     -39.986 -14.154 101.169  1.00 19.91           C  
ANISOU 4636  CG1 ILE B 109     2480   2707   2380    263   -180     60       C  
ATOM   4637  CG2 ILE B 109     -41.975 -15.027  99.768  1.00 20.11           C  
ANISOU 4637  CG2 ILE B 109     2546   2715   2380    285   -274     28       C  
ATOM   4638  CD1 ILE B 109     -39.140 -13.630  99.937  1.00 26.79           C  
ANISOU 4638  CD1 ILE B 109     3379   3612   3190    289   -147     68       C  
ATOM   4639  N   VAL B 110     -44.477 -12.794 101.573  1.00 19.17           N  
ANISOU 4639  N   VAL B 110     2364   2555   2364    223   -294    102       N  
ATOM   4640  CA  VAL B 110     -45.945 -12.807 101.426  1.00 19.24           C  
ANISOU 4640  CA  VAL B 110     2368   2546   2397    218   -342    104       C  
ATOM   4641  C   VAL B 110     -46.469 -11.447 100.940  1.00 23.03           C  
ANISOU 4641  C   VAL B 110     2854   3034   2863    220   -339    137       C  
ATOM   4642  O   VAL B 110     -47.274 -11.398 100.009  1.00 23.50           O  
ANISOU 4642  O   VAL B 110     2932   3094   2903    233   -378    135       O  
ATOM   4643  CB  VAL B 110     -46.652 -13.258 102.738  1.00 23.12           C  
ANISOU 4643  CB  VAL B 110     2822   3009   2954    194   -354    104       C  
ATOM   4644  CG1 VAL B 110     -48.173 -13.251 102.572  1.00 23.27           C  
ANISOU 4644  CG1 VAL B 110     2831   3010   3002    189   -402    109       C  
ATOM   4645  CG2 VAL B 110     -46.162 -14.636 103.177  1.00 22.79           C  
ANISOU 4645  CG2 VAL B 110     2777   2957   2926    192   -361     73       C  
ATOM   4646  N   ILE B 111     -45.990 -10.340 101.553  1.00 18.94           N  
ANISOU 4646  N   ILE B 111     2321   2520   2354    208   -294    166       N  
ATOM   4647  CA  ILE B 111     -46.402  -8.987 101.147  1.00 18.31           C  
ANISOU 4647  CA  ILE B 111     2247   2446   2264    209   -286    199       C  
ATOM   4648  C   ILE B 111     -45.955  -8.684  99.707  1.00 22.70           C  
ANISOU 4648  C   ILE B 111     2843   3028   2755    234   -285    203       C  
ATOM   4649  O   ILE B 111     -46.788  -8.363  98.865  1.00 22.01           O  
ANISOU 4649  O   ILE B 111     2773   2941   2650    246   -318    210       O  
ATOM   4650  CB  ILE B 111     -45.891  -7.904 102.151  1.00 20.16           C  
ANISOU 4650  CB  ILE B 111     2460   2677   2524    190   -239    227       C  
ATOM   4651  CG1 ILE B 111     -46.330  -8.228 103.586  1.00 19.20           C  
ANISOU 4651  CG1 ILE B 111     2303   2532   2460    168   -238    223       C  
ATOM   4652  CG2 ILE B 111     -46.362  -6.492 101.725  1.00 20.99           C  
ANISOU 4652  CG2 ILE B 111     2571   2783   2621    192   -234    262       C  
ATOM   4653  CD1 ILE B 111     -45.670  -7.340 104.672  1.00 23.29           C  
ANISOU 4653  CD1 ILE B 111     2804   3046   3001    150   -192    243       C  
ATOM   4654  N   ARG B 112     -44.636  -8.846  99.416  1.00 20.01           N  
ANISOU 4654  N   ARG B 112     2516   2708   2378    243   -247    197       N  
ATOM   4655  CA  ARG B 112     -44.076  -8.538  98.087  1.00 20.53           C  
ANISOU 4655  CA  ARG B 112     2621   2801   2379    267   -236    203       C  
ATOM   4656  C   ARG B 112     -44.805  -9.297  96.947  1.00 25.23           C  
ANISOU 4656  C   ARG B 112     3249   3399   2937    291   -289    178       C  
ATOM   4657  O   ARG B 112     -45.084  -8.706  95.899  1.00 23.98           O  
ANISOU 4657  O   ARG B 112     3121   3254   2735    308   -300    194       O  
ATOM   4658  CB  ARG B 112     -42.561  -8.829  98.051  1.00 19.62           C  
ANISOU 4658  CB  ARG B 112     2510   2707   2239    274   -187    196       C  
ATOM   4659  CG  ARG B 112     -41.830  -8.118  96.900  1.00 28.29           C  
ANISOU 4659  CG  ARG B 112     3638   3834   3275    294   -155    217       C  
ATOM   4660  CD  ARG B 112     -40.332  -8.396  96.912  1.00 37.83           C  
ANISOU 4660  CD  ARG B 112     4844   5063   4465    300   -104    212       C  
ATOM   4661  NE  ARG B 112     -40.007  -9.697  96.323  1.00 43.37           N  
ANISOU 4661  NE  ARG B 112     5569   5776   5134    325   -118    171       N  
ATOM   4662  CZ  ARG B 112     -39.680  -9.868  95.044  1.00 61.84           C  
ANISOU 4662  CZ  ARG B 112     7948   8141   7409    355   -113    165       C  
ATOM   4663  NH1 ARG B 112     -39.650  -8.830  94.215  1.00 49.23           N  
ANISOU 4663  NH1 ARG B 112     6372   6560   5771    364    -94    199       N  
ATOM   4664  NH2 ARG B 112     -39.396 -11.078  94.581  1.00 50.97           N  
ANISOU 4664  NH2 ARG B 112     6592   6770   6005    379   -127    125       N  
ATOM   4665  N   SER B 113     -45.119 -10.611  97.166  1.00 23.38           N  
ANISOU 4665  N   SER B 113     3011   3152   2721    293   -324    141       N  
ATOM   4666  CA ASER B 113     -45.783 -11.441  96.153  0.50 23.83           C  
ANISOU 4666  CA ASER B 113     3100   3208   2748    314   -380    112       C  
ATOM   4667  CA BSER B 113     -45.782 -11.438  96.151  0.50 23.84           C  
ANISOU 4667  CA BSER B 113     3101   3208   2748    314   -379    112       C  
ATOM   4668  C   SER B 113     -47.223 -10.974  95.880  1.00 28.66           C  
ANISOU 4668  C   SER B 113     3710   3804   3377    310   -431    126       C  
ATOM   4669  O   SER B 113     -47.615 -10.833  94.719  1.00 28.52           O  
ANISOU 4669  O   SER B 113     3727   3796   3313    332   -462    124       O  
ATOM   4670  CB ASER B 113     -45.774 -12.907  96.573  0.50 27.08           C  
ANISOU 4670  CB ASER B 113     3503   3602   3183    313   -405     70       C  
ATOM   4671  CB BSER B 113     -45.768 -12.905  96.564  0.50 27.10           C  
ANISOU 4671  CB BSER B 113     3506   3605   3186    313   -405     70       C  
ATOM   4672  OG ASER B 113     -46.430 -13.723  95.618  0.50 35.16           O  
ANISOU 4672  OG ASER B 113     4557   4620   4180    332   -463     40       O  
ATOM   4673  OG BSER B 113     -44.442 -13.371  96.756  0.50 34.71           O  
ANISOU 4673  OG BSER B 113     4472   4583   4133    320   -361     57       O  
ATOM   4674  N   LEU B 114     -48.018 -10.750  96.953  1.00 26.10           N  
ANISOU 4674  N   LEU B 114     3343   3455   3119    285   -440    139       N  
ATOM   4675  CA  LEU B 114     -49.425 -10.337  96.811  1.00 25.95           C  
ANISOU 4675  CA  LEU B 114     3314   3419   3128    280   -487    152       C  
ATOM   4676  C   LEU B 114     -49.559  -8.918  96.246  1.00 31.46           C  
ANISOU 4676  C   LEU B 114     4025   4130   3799    287   -473    191       C  
ATOM   4677  O   LEU B 114     -50.443  -8.670  95.427  1.00 31.33           O  
ANISOU 4677  O   LEU B 114     4024   4111   3769    299   -518    197       O  
ATOM   4678  CB  LEU B 114     -50.171 -10.454  98.157  1.00 25.14           C  
ANISOU 4678  CB  LEU B 114     3161   3288   3103    252   -492    158       C  
ATOM   4679  CG  LEU B 114     -50.273 -11.868  98.750  1.00 28.34           C  
ANISOU 4679  CG  LEU B 114     3550   3675   3542    243   -514    124       C  
ATOM   4680  CD1 LEU B 114     -50.855 -11.828 100.129  1.00 27.77           C  
ANISOU 4680  CD1 LEU B 114     3430   3580   3542    216   -505    136       C  
ATOM   4681  CD2 LEU B 114     -51.093 -12.789  97.851  1.00 28.93           C  
ANISOU 4681  CD2 LEU B 114     3643   3740   3607    256   -583     96       C  
ATOM   4682  N   THR B 115     -48.684  -7.979  96.690  1.00 28.98           N  
ANISOU 4682  N   THR B 115     3704   3826   3481    279   -413    218       N  
ATOM   4683  CA  THR B 115     -48.699  -6.593  96.182  1.00 29.48           C  
ANISOU 4683  CA  THR B 115     3781   3900   3521    285   -395    257       C  
ATOM   4684  C   THR B 115     -48.376  -6.555  94.687  1.00 33.95           C  
ANISOU 4684  C   THR B 115     4399   4492   4011    314   -405    257       C  
ATOM   4685  O   THR B 115     -48.960  -5.761  93.952  1.00 33.46           O  
ANISOU 4685  O   THR B 115     4354   4432   3927    324   -425    281       O  
ATOM   4686  CB  THR B 115     -47.728  -5.705  96.986  1.00 40.13           C  
ANISOU 4686  CB  THR B 115     5111   5252   4884    269   -330    283       C  
ATOM   4687  OG1 THR B 115     -46.449  -6.335  97.032  1.00 42.69           O  
ANISOU 4687  OG1 THR B 115     5444   5593   5184    271   -293    265       O  
ATOM   4688  CG2 THR B 115     -48.222  -5.426  98.396  1.00 39.25           C  
ANISOU 4688  CG2 THR B 115     4955   5114   4843    243   -322    291       C  
ATOM   4689  N   GLU B 116     -47.451  -7.429  94.235  1.00 31.38           N  
ANISOU 4689  N   GLU B 116     4097   4184   3642    328   -391    229       N  
ATOM   4690  CA  GLU B 116     -47.071  -7.510  92.826  1.00 31.97           C  
ANISOU 4690  CA  GLU B 116     4224   4285   3639    359   -397    225       C  
ATOM   4691  C   GLU B 116     -48.162  -8.207  91.996  1.00 35.12           C  
ANISOU 4691  C   GLU B 116     4647   4675   4019    376   -472    199       C  
ATOM   4692  O   GLU B 116     -48.495  -7.739  90.904  1.00 35.64           O  
ANISOU 4692  O   GLU B 116     4751   4754   4035    396   -495    212       O  
ATOM   4693  CB  GLU B 116     -45.714  -8.240  92.668  1.00 33.51           C  
ANISOU 4693  CB  GLU B 116     4434   4501   3796    371   -354    202       C  
ATOM   4694  CG  GLU B 116     -45.230  -8.342  91.223  1.00 45.71           C  
ANISOU 4694  CG  GLU B 116     6036   6077   5257    405   -352    196       C  
ATOM   4695  CD  GLU B 116     -45.017  -7.010  90.524  1.00 74.06           C  
ANISOU 4695  CD  GLU B 116     9649   9686   8806    413   -324    243       C  
ATOM   4696  OE1 GLU B 116     -44.363  -6.123  91.119  1.00 73.45           O  
ANISOU 4696  OE1 GLU B 116     9547   9612   8749    396   -270    276       O  
ATOM   4697  OE2 GLU B 116     -45.450  -6.878  89.356  1.00 71.25           O  
ANISOU 4697  OE2 GLU B 116     9337   9342   8395    437   -356    246       O  
ATOM   4698  N   LYS B 117     -48.728  -9.323  92.522  1.00 30.32           N  
ANISOU 4698  N   LYS B 117     4019   4046   3454    367   -513    164       N  
ATOM   4699  CA  LYS B 117     -49.773 -10.083  91.818  1.00 30.09           C  
ANISOU 4699  CA  LYS B 117     4010   4005   3419    379   -589    137       C  
ATOM   4700  C   LYS B 117     -51.070  -9.263  91.694  1.00 32.75           C  
ANISOU 4700  C   LYS B 117     4334   4327   3783    373   -632    164       C  
ATOM   4701  O   LYS B 117     -51.478  -8.926  90.582  1.00 33.31           O  
ANISOU 4701  O   LYS B 117     4442   4408   3805    394   -666    172       O  
ATOM   4702  CB  LYS B 117     -50.041 -11.428  92.526  1.00 32.30           C  
ANISOU 4702  CB  LYS B 117     4264   4260   3747    366   -618     97       C  
ATOM   4703  N   ASP B 118     -51.700  -8.919  92.844  1.00 27.26           N  
ANISOU 4703  N   ASP B 118     3586   3608   3164    346   -628    181       N  
ATOM   4704  CA  ASP B 118     -52.914  -8.089  92.870  1.00 26.65           C  
ANISOU 4704  CA  ASP B 118     3489   3516   3123    340   -663    210       C  
ATOM   4705  C   ASP B 118     -53.111  -7.498  94.269  1.00 30.73           C  
ANISOU 4705  C   ASP B 118     3950   4014   3712    312   -626    233       C  
ATOM   4706  O   ASP B 118     -53.767  -8.114  95.116  1.00 30.10           O  
ANISOU 4706  O   ASP B 118     3831   3911   3694    294   -646    220       O  
ATOM   4707  CB  ASP B 118     -54.158  -8.916  92.443  1.00 28.03           C  
ANISOU 4707  CB  ASP B 118     3662   3671   3319    344   -746    185       C  
ATOM   4708  CG  ASP B 118     -55.419  -8.078  92.193  1.00 25.83           C  
ANISOU 4708  CG  ASP B 118     3368   3379   3066    344   -790    214       C  
ATOM   4709  OD1 ASP B 118     -55.455  -6.903  92.642  1.00 21.03           O  
ANISOU 4709  OD1 ASP B 118     2741   2771   2479    337   -753    252       O  
ATOM   4710  OD2 ASP B 118     -56.386  -8.621  91.618  1.00 29.99           O  
ANISOU 4710  OD2 ASP B 118     3901   3894   3601    351   -862    197       O  
ATOM   4711  N   LYS B 119     -52.505  -6.316  94.525  1.00 27.65           N  
ANISOU 4711  N   LYS B 119     3559   3634   3313    309   -571    268       N  
ATOM   4712  CA  LYS B 119     -52.568  -5.657  95.840  1.00 27.06           C  
ANISOU 4712  CA  LYS B 119     3439   3543   3300    285   -531    290       C  
ATOM   4713  C   LYS B 119     -54.005  -5.380  96.269  1.00 29.41           C  
ANISOU 4713  C   LYS B 119     3700   3815   3659    276   -571    302       C  
ATOM   4714  O   LYS B 119     -54.322  -5.476  97.451  1.00 27.98           O  
ANISOU 4714  O   LYS B 119     3478   3616   3539    256   -556    302       O  
ATOM   4715  CB  LYS B 119     -51.756  -4.351  95.828  1.00 30.08           C  
ANISOU 4715  CB  LYS B 119     3833   3938   3658    285   -476    326       C  
ATOM   4716  N   ASP B 120     -54.879  -5.057  95.304  1.00 26.01           N  
ANISOU 4716  N   ASP B 120     3287   3384   3213    292   -622    312       N  
ATOM   4717  CA  ASP B 120     -56.268  -4.714  95.581  1.00 25.56           C  
ANISOU 4717  CA  ASP B 120     3194   3304   3214    288   -662    326       C  
ATOM   4718  C   ASP B 120     -57.093  -5.932  96.049  1.00 28.40           C  
ANISOU 4718  C   ASP B 120     3522   3645   3626    276   -706    297       C  
ATOM   4719  O   ASP B 120     -57.895  -5.803  96.971  1.00 28.04           O  
ANISOU 4719  O   ASP B 120     3428   3577   3648    261   -706    307       O  
ATOM   4720  CB  ASP B 120     -56.917  -4.053  94.351  1.00 27.89           C  
ANISOU 4720  CB  ASP B 120     3518   3604   3474    310   -708    346       C  
ATOM   4721  CG  ASP B 120     -56.248  -2.743  93.933  1.00 38.81           C  
ANISOU 4721  CG  ASP B 120     4930   5002   4814    320   -666    382       C  
ATOM   4722  OD1 ASP B 120     -55.004  -2.634  94.078  1.00 38.07           O  
ANISOU 4722  OD1 ASP B 120     4854   4925   4686    317   -610    382       O  
ATOM   4723  OD2 ASP B 120     -56.952  -1.866  93.389  1.00 46.64           O  
ANISOU 4723  OD2 ASP B 120     5927   5988   5804    332   -692    410       O  
ATOM   4724  N   ALA B 121     -56.890  -7.110  95.414  1.00 24.47           N  
ANISOU 4724  N   ALA B 121     3049   3152   3097    283   -741    262       N  
ATOM   4725  CA  ALA B 121     -57.651  -8.329  95.760  1.00 23.98           C  
ANISOU 4725  CA  ALA B 121     2959   3069   3084    271   -787    233       C  
ATOM   4726  C   ALA B 121     -57.223  -8.919  97.115  1.00 27.22           C  
ANISOU 4726  C   ALA B 121     3334   3469   3541    247   -743    223       C  
ATOM   4727  O   ALA B 121     -58.054  -9.483  97.829  1.00 26.51           O  
ANISOU 4727  O   ALA B 121     3202   3356   3515    231   -765    218       O  
ATOM   4728  CB  ALA B 121     -57.501  -9.369  94.667  1.00 24.96           C  
ANISOU 4728  CB  ALA B 121     3126   3200   3158    287   -838    197       C  
ATOM   4729  N   TYR B 122     -55.927  -8.800  97.462  1.00 23.45           N  
ANISOU 4729  N   TYR B 122     2873   3008   3030    246   -683    221       N  
ATOM   4730  CA  TYR B 122     -55.413  -9.327  98.733  1.00 23.06           C  
ANISOU 4730  CA  TYR B 122     2795   2949   3017    225   -641    212       C  
ATOM   4731  C   TYR B 122     -55.111  -8.196  99.728  1.00 24.66           C  
ANISOU 4731  C   TYR B 122     2974   3152   3242    213   -580    243       C  
ATOM   4732  O   TYR B 122     -54.201  -8.322 100.543  1.00 23.46           O  
ANISOU 4732  O   TYR B 122     2818   3005   3093    203   -532    239       O  
ATOM   4733  CB  TYR B 122     -54.157 -10.203  98.494  1.00 25.09           C  
ANISOU 4733  CB  TYR B 122     3083   3221   3227    231   -622    182       C  
ATOM   4734  CG  TYR B 122     -54.449 -11.473  97.720  1.00 28.90           C  
ANISOU 4734  CG  TYR B 122     3586   3699   3695    241   -681    145       C  
ATOM   4735  CD1 TYR B 122     -54.859 -12.633  98.372  1.00 31.30           C  
ANISOU 4735  CD1 TYR B 122     3864   3980   4049    225   -705    123       C  
ATOM   4736  CD2 TYR B 122     -54.315 -11.516  96.335  1.00 30.63           C  
ANISOU 4736  CD2 TYR B 122     3854   3934   3850    267   -713    133       C  
ATOM   4737  CE1 TYR B 122     -55.137 -13.803  97.665  1.00 33.26           C  
ANISOU 4737  CE1 TYR B 122     4132   4219   4287    233   -762     88       C  
ATOM   4738  CE2 TYR B 122     -54.598 -12.678  95.615  1.00 32.24           C  
ANISOU 4738  CE2 TYR B 122     4079   4130   4039    277   -770     96       C  
ATOM   4739  CZ  TYR B 122     -55.010 -13.820  96.285  1.00 41.22           C  
ANISOU 4739  CZ  TYR B 122     5189   5243   5230    260   -796     73       C  
ATOM   4740  OH  TYR B 122     -55.284 -14.970  95.582  1.00 44.91           O  
ANISOU 4740  OH  TYR B 122     5679   5699   5685    269   -855     35       O  
ATOM   4741  N   ALA B 123     -55.928  -7.113  99.701  1.00 20.77           N  
ANISOU 4741  N   ALA B 123     2467   2653   2772    216   -586    273       N  
ATOM   4742  CA  ALA B 123     -55.716  -5.939 100.563  1.00 19.75           C  
ANISOU 4742  CA  ALA B 123     2320   2521   2663    208   -533    303       C  
ATOM   4743  C   ALA B 123     -55.865  -6.266 102.060  1.00 22.94           C  
ANISOU 4743  C   ALA B 123     2682   2908   3126    186   -504    300       C  
ATOM   4744  O   ALA B 123     -55.179  -5.666 102.880  1.00 22.01           O  
ANISOU 4744  O   ALA B 123     2560   2792   3011    177   -452    311       O  
ATOM   4745  CB  ALA B 123     -56.667  -4.821 100.173  1.00 20.41           C  
ANISOU 4745  CB  ALA B 123     2396   2597   2761    218   -552    333       C  
ATOM   4746  N   ASN B 124     -56.769  -7.216 102.414  1.00 19.33           N  
ANISOU 4746  N   ASN B 124     2195   2434   2716    177   -539    287       N  
ATOM   4747  CA  ASN B 124     -56.971  -7.616 103.823  1.00 18.30           C  
ANISOU 4747  CA  ASN B 124     2026   2287   2640    157   -512    286       C  
ATOM   4748  C   ASN B 124     -55.844  -8.522 104.306  1.00 21.25           C  
ANISOU 4748  C   ASN B 124     2411   2667   2994    147   -486    262       C  
ATOM   4749  O   ASN B 124     -55.468  -8.471 105.482  1.00 21.10           O  
ANISOU 4749  O   ASN B 124     2376   2643   2998    134   -443    267       O  
ATOM   4750  CB  ASN B 124     -58.328  -8.301 104.006  1.00 18.02           C  
ANISOU 4750  CB  ASN B 124     1952   2231   2664    150   -556    284       C  
ATOM   4751  CG  ASN B 124     -59.505  -7.399 103.702  1.00 24.79           C  
ANISOU 4751  CG  ASN B 124     2788   3080   3550    158   -580    309       C  
ATOM   4752  OD1 ASN B 124     -59.572  -6.253 104.150  1.00 15.47           O  
ANISOU 4752  OD1 ASN B 124     1600   1899   2380    162   -544    333       O  
ATOM   4753  ND2 ASN B 124     -60.488  -7.925 102.984  1.00 16.39           N  
ANISOU 4753  ND2 ASN B 124     1714   2007   2507    162   -641    303       N  
ATOM   4754  N   THR B 125     -55.303  -9.354 103.405  1.00 16.58           N  
ANISOU 4754  N   THR B 125     1851   2086   2362    156   -512    237       N  
ATOM   4755  CA  THR B 125     -54.177 -10.231 103.722  1.00 15.30           C  
ANISOU 4755  CA  THR B 125     1703   1931   2179    151   -490    214       C  
ATOM   4756  C   THR B 125     -52.889  -9.400 103.884  1.00 17.86           C  
ANISOU 4756  C   THR B 125     2048   2275   2465    154   -434    224       C  
ATOM   4757  O   THR B 125     -52.105  -9.648 104.801  1.00 16.41           O  
ANISOU 4757  O   THR B 125     1857   2091   2288    143   -397    219       O  
ATOM   4758  CB  THR B 125     -54.022 -11.306 102.627  1.00 17.22           C  
ANISOU 4758  CB  THR B 125     1975   2179   2388    164   -535    183       C  
ATOM   4759  OG1 THR B 125     -55.290 -11.907 102.379  1.00 16.38           O  
ANISOU 4759  OG1 THR B 125     1850   2053   2320    161   -593    176       O  
ATOM   4760  CG2 THR B 125     -53.019 -12.359 102.996  1.00 14.00           C  
ANISOU 4760  CG2 THR B 125     1576   1773   1969    160   -519    157       C  
ATOM   4761  N   ILE B 126     -52.695  -8.392 103.001  1.00 14.05           N  
ANISOU 4761  N   ILE B 126     1590   1807   1943    169   -430    241       N  
ATOM   4762  CA  ILE B 126     -51.525  -7.510 103.049  1.00 13.28           C  
ANISOU 4762  CA  ILE B 126     1510   1726   1810    171   -379    255       C  
ATOM   4763  C   ILE B 126     -51.573  -6.612 104.277  1.00 16.25           C  
ANISOU 4763  C   ILE B 126     1859   2090   2224    155   -339    277       C  
ATOM   4764  O   ILE B 126     -50.565  -6.472 104.974  1.00 15.51           O  
ANISOU 4764  O   ILE B 126     1767   2002   2126    146   -297    277       O  
ATOM   4765  CB  ILE B 126     -51.399  -6.693 101.734  1.00 16.61           C  
ANISOU 4765  CB  ILE B 126     1965   2165   2181    191   -388    269       C  
ATOM   4766  CG1 ILE B 126     -51.167  -7.639 100.519  1.00 17.70           C  
ANISOU 4766  CG1 ILE B 126     2136   2317   2271    209   -423    243       C  
ATOM   4767  CG2 ILE B 126     -50.283  -5.642 101.844  1.00 16.76           C  
ANISOU 4767  CG2 ILE B 126     1996   2197   2173    189   -334    290       C  
ATOM   4768  CD1 ILE B 126     -51.433  -6.996  99.149  1.00 24.79           C  
ANISOU 4768  CD1 ILE B 126     3068   3229   3121    230   -446    256       C  
ATOM   4769  N   ALA B 127     -52.765  -6.037 104.578  1.00 12.59           N  
ANISOU 4769  N   ALA B 127     1372   1610   1801    153   -353    294       N  
ATOM   4770  CA  ALA B 127     -52.952  -5.178 105.757  1.00 11.97           C  
ANISOU 4770  CA  ALA B 127     1270   1519   1761    142   -317    314       C  
ATOM   4771  C   ALA B 127     -52.609  -5.933 107.054  1.00 15.84           C  
ANISOU 4771  C   ALA B 127     1740   2000   2278    124   -293    300       C  
ATOM   4772  O   ALA B 127     -51.922  -5.388 107.917  1.00 14.96           O  
ANISOU 4772  O   ALA B 127     1628   1888   2169    115   -252    306       O  
ATOM   4773  CB  ALA B 127     -54.383  -4.666 105.811  1.00 12.84           C  
ANISOU 4773  CB  ALA B 127     1355   1612   1912    145   -340    331       C  
ATOM   4774  N   PHE B 128     -53.049  -7.213 107.164  1.00 12.45           N  
ANISOU 4774  N   PHE B 128     1298   1564   1869    119   -322    280       N  
ATOM   4775  CA  PHE B 128     -52.727  -8.053 108.328  1.00 12.23           C  
ANISOU 4775  CA  PHE B 128     1255   1528   1865    104   -303    267       C  
ATOM   4776  C   PHE B 128     -51.230  -8.373 108.380  1.00 13.87           C  
ANISOU 4776  C   PHE B 128     1485   1750   2035    102   -277    253       C  
ATOM   4777  O   PHE B 128     -50.637  -8.360 109.455  1.00 12.10           O  
ANISOU 4777  O   PHE B 128     1253   1523   1822     90   -244    253       O  
ATOM   4778  CB  PHE B 128     -53.557  -9.359 108.309  1.00 14.76           C  
ANISOU 4778  CB  PHE B 128     1556   1835   2216     99   -344    252       C  
ATOM   4779  CG  PHE B 128     -52.872 -10.526 108.988  1.00 16.86           C  
ANISOU 4779  CG  PHE B 128     1821   2098   2486     88   -335    232       C  
ATOM   4780  CD1 PHE B 128     -52.873 -10.646 110.372  1.00 20.00           C  
ANISOU 4780  CD1 PHE B 128     2199   2485   2916     72   -305    238       C  
ATOM   4781  CD2 PHE B 128     -52.163 -11.465 108.245  1.00 19.67           C  
ANISOU 4781  CD2 PHE B 128     2200   2462   2810     94   -355    206       C  
ATOM   4782  CE1 PHE B 128     -52.172 -11.679 111.000  1.00 21.04           C  
ANISOU 4782  CE1 PHE B 128     2331   2613   3049     63   -297    222       C  
ATOM   4783  CE2 PHE B 128     -51.471 -12.501 108.877  1.00 22.62           C  
ANISOU 4783  CE2 PHE B 128     2573   2831   3188     86   -347    189       C  
ATOM   4784  CZ  PHE B 128     -51.493 -12.609 110.247  1.00 20.46           C  
ANISOU 4784  CZ  PHE B 128     2278   2546   2948     70   -319    198       C  
ATOM   4785  N   ALA B 129     -50.642  -8.742 107.226  1.00 10.84           N  
ANISOU 4785  N   ALA B 129     1129   1383   1609    115   -294    239       N  
ATOM   4786  CA  ALA B 129     -49.230  -9.092 107.147  1.00 10.44           C  
ANISOU 4786  CA  ALA B 129     1096   1347   1523    117   -271    225       C  
ATOM   4787  C   ALA B 129     -48.359  -7.928 107.614  1.00 13.92           C  
ANISOU 4787  C   ALA B 129     1541   1795   1952    112   -224    244       C  
ATOM   4788  O   ALA B 129     -47.438  -8.133 108.402  1.00 14.50           O  
ANISOU 4788  O   ALA B 129     1612   1871   2027    102   -196    238       O  
ATOM   4789  CB  ALA B 129     -48.867  -9.486 105.721  1.00 11.15           C  
ANISOU 4789  CB  ALA B 129     1216   1454   1565    136   -294    210       C  
ATOM   4790  N   ARG B 130     -48.732  -6.687 107.224  1.00  9.84           N  
ANISOU 4790  N   ARG B 130     1029   1279   1430    117   -218    268       N  
ATOM   4791  CA  ARG B 130     -48.047  -5.465 107.663  1.00  9.85           C  
ANISOU 4791  CA  ARG B 130     1033   1282   1426    110   -178    288       C  
ATOM   4792  C   ARG B 130     -48.065  -5.329 109.189  1.00 15.41           C  
ANISOU 4792  C   ARG B 130     1716   1970   2169     93   -154    290       C  
ATOM   4793  O   ARG B 130     -47.043  -4.979 109.789  1.00 15.33           O  
ANISOU 4793  O   ARG B 130     1709   1963   2153     84   -122    292       O  
ATOM   4794  CB  ARG B 130     -48.688  -4.229 107.020  1.00  8.36           C  
ANISOU 4794  CB  ARG B 130      851   1092   1234    119   -183    314       C  
ATOM   4795  CG  ARG B 130     -48.022  -3.790 105.729  1.00 20.52           C  
ANISOU 4795  CG  ARG B 130     2420   2652   2724    133   -181    322       C  
ATOM   4796  CD  ARG B 130     -48.672  -2.526 105.189  1.00 26.73           C  
ANISOU 4796  CD  ARG B 130     3213   3433   3509    140   -185    351       C  
ATOM   4797  NE  ARG B 130     -47.817  -1.826 104.229  1.00 30.37           N  
ANISOU 4797  NE  ARG B 130     3701   3912   3926    149   -168    368       N  
ATOM   4798  CZ  ARG B 130     -48.208  -0.761 103.532  1.00 36.49           C  
ANISOU 4798  CZ  ARG B 130     4489   4685   4689    158   -173    394       C  
ATOM   4799  NH1 ARG B 130     -49.450  -0.307 103.644  1.00 23.79           N  
ANISOU 4799  NH1 ARG B 130     2868   3059   3110    162   -197    405       N  
ATOM   4800  NH2 ARG B 130     -47.370  -0.168 102.687  1.00  9.78           N  
ANISOU 4800  NH2 ARG B 130     1132   1319   1266    164   -154    412       N  
ATOM   4801  N   ILE B 131     -49.238  -5.573 109.814  1.00 12.76           N  
ANISOU 4801  N   ILE B 131     1359   1618   1872     90   -169    291       N  
ATOM   4802  CA  ILE B 131     -49.405  -5.474 111.270  1.00 12.91           C  
ANISOU 4802  CA  ILE B 131     1359   1621   1925     76   -146    294       C  
ATOM   4803  C   ILE B 131     -48.541  -6.512 111.989  1.00 17.10           C  
ANISOU 4803  C   ILE B 131     1889   2154   2454     66   -136    275       C  
ATOM   4804  O   ILE B 131     -47.836  -6.171 112.940  1.00 16.71           O  
ANISOU 4804  O   ILE B 131     1841   2102   2408     56   -107    277       O  
ATOM   4805  CB  ILE B 131     -50.914  -5.608 111.664  1.00 16.26           C  
ANISOU 4805  CB  ILE B 131     1759   2029   2391     76   -163    301       C  
ATOM   4806  CG1 ILE B 131     -51.746  -4.454 111.066  1.00 17.06           C  
ANISOU 4806  CG1 ILE B 131     1858   2125   2497     88   -171    321       C  
ATOM   4807  CG2 ILE B 131     -51.084  -5.686 113.201  1.00 17.04           C  
ANISOU 4807  CG2 ILE B 131     1839   2113   2521     64   -137    302       C  
ATOM   4808  CD1 ILE B 131     -53.264  -4.718 111.023  1.00 23.57           C  
ANISOU 4808  CD1 ILE B 131     2657   2937   3361     92   -199    327       C  
ATOM   4809  N   TRP B 132     -48.594  -7.787 111.532  1.00 14.18           N  
ANISOU 4809  N   TRP B 132     1520   1788   2081     69   -163    256       N  
ATOM   4810  CA  TRP B 132     -47.834  -8.870 112.155  1.00 14.22           C  
ANISOU 4810  CA  TRP B 132     1523   1793   2086     61   -158    238       C  
ATOM   4811  C   TRP B 132     -46.327  -8.703 111.943  1.00 16.27           C  
ANISOU 4811  C   TRP B 132     1801   2069   2313     62   -137    232       C  
ATOM   4812  O   TRP B 132     -45.538  -9.072 112.816  1.00 16.72           O  
ANISOU 4812  O   TRP B 132     1854   2124   2374     53   -120    225       O  
ATOM   4813  CB  TRP B 132     -48.309 -10.235 111.647  1.00 13.72           C  
ANISOU 4813  CB  TRP B 132     1457   1726   2030     65   -196    220       C  
ATOM   4814  CG  TRP B 132     -47.944 -11.365 112.558  1.00 15.23           C  
ANISOU 4814  CG  TRP B 132     1640   1908   2237     54   -194    206       C  
ATOM   4815  CD1 TRP B 132     -47.025 -12.344 112.320  1.00 18.39           C  
ANISOU 4815  CD1 TRP B 132     2052   2316   2621     58   -200    185       C  
ATOM   4816  CD2 TRP B 132     -48.374 -11.539 113.914  1.00 15.21           C  
ANISOU 4816  CD2 TRP B 132     1619   1890   2270     40   -180    214       C  
ATOM   4817  NE1 TRP B 132     -46.916 -13.167 113.420  1.00 17.81           N  
ANISOU 4817  NE1 TRP B 132     1966   2228   2571     46   -196    180       N  
ATOM   4818  CE2 TRP B 132     -47.713 -12.679 114.422  1.00 19.21           C  
ANISOU 4818  CE2 TRP B 132     2127   2393   2779     35   -182    199       C  
ATOM   4819  CE3 TRP B 132     -49.266 -10.844 114.752  1.00 16.70           C  
ANISOU 4819  CE3 TRP B 132     1791   2067   2486     33   -164    233       C  
ATOM   4820  CZ2 TRP B 132     -47.917 -13.143 115.726  1.00 18.69           C  
ANISOU 4820  CZ2 TRP B 132     2049   2313   2741     21   -170    204       C  
ATOM   4821  CZ3 TRP B 132     -49.465 -11.304 116.042  1.00 18.38           C  
ANISOU 4821  CZ3 TRP B 132     1991   2266   2725     21   -150    237       C  
ATOM   4822  CH2 TRP B 132     -48.801 -12.445 116.515  1.00 19.02           C  
ANISOU 4822  CH2 TRP B 132     2076   2346   2807     15   -154    224       C  
ATOM   4823  N   ARG B 133     -45.930  -8.100 110.807  1.00 10.67           N  
ANISOU 4823  N   ARG B 133     1107   1375   1571     74   -136    238       N  
ATOM   4824  CA  ARG B 133     -44.526  -7.781 110.529  1.00  9.83           C  
ANISOU 4824  CA  ARG B 133     1015   1286   1436     75   -111    237       C  
ATOM   4825  C   ARG B 133     -44.010  -6.737 111.545  1.00 12.33           C  
ANISOU 4825  C   ARG B 133     1326   1595   1765     61    -78    253       C  
ATOM   4826  O   ARG B 133     -42.894  -6.867 112.054  1.00 11.00           O  
ANISOU 4826  O   ARG B 133     1156   1431   1592     54    -59    248       O  
ATOM   4827  CB  ARG B 133     -44.377  -7.256 109.087  1.00 10.64           C  
ANISOU 4827  CB  ARG B 133     1136   1405   1501     91   -115    245       C  
ATOM   4828  CG  ARG B 133     -42.962  -6.834 108.708  1.00 17.88           C  
ANISOU 4828  CG  ARG B 133     2064   2341   2389     93    -85    249       C  
ATOM   4829  CD  ARG B 133     -42.928  -6.295 107.293  1.00 24.35           C  
ANISOU 4829  CD  ARG B 133     2904   3177   3170    109    -87    261       C  
ATOM   4830  NE  ARG B 133     -41.631  -5.709 106.957  1.00 28.02           N  
ANISOU 4830  NE  ARG B 133     3376   3658   3611    109    -53    272       N  
ATOM   4831  CZ  ARG B 133     -41.359  -4.412 107.057  1.00 38.36           C  
ANISOU 4831  CZ  ARG B 133     4686   4966   4924    100    -29    299       C  
ATOM   4832  NH1 ARG B 133     -42.287  -3.563 107.483  1.00 20.61           N  
ANISOU 4832  NH1 ARG B 133     2433   2699   2699     93    -36    315       N  
ATOM   4833  NH2 ARG B 133     -40.160  -3.954 106.727  1.00 27.20           N  
ANISOU 4833  NH2 ARG B 133     3276   3567   3492     99      1    310       N  
ATOM   4834  N   VAL B 134     -44.858  -5.748 111.889  1.00  9.29           N  
ANISOU 4834  N   VAL B 134      935   1197   1398     58    -74    271       N  
ATOM   4835  CA  VAL B 134     -44.522  -4.747 112.900  1.00  9.06           C  
ANISOU 4835  CA  VAL B 134      903   1157   1383     46    -47    283       C  
ATOM   4836  C   VAL B 134     -44.388  -5.397 114.284  1.00 14.09           C  
ANISOU 4836  C   VAL B 134     1530   1783   2042     34    -40    271       C  
ATOM   4837  O   VAL B 134     -43.350  -5.254 114.929  1.00 14.12           O  
ANISOU 4837  O   VAL B 134     1535   1787   2042     24    -23    269       O  
ATOM   4838  CB  VAL B 134     -45.549  -3.574 112.908  1.00 12.60           C  
ANISOU 4838  CB  VAL B 134     1350   1592   1846     48    -45    303       C  
ATOM   4839  CG1 VAL B 134     -45.431  -2.741 114.188  1.00 11.83           C  
ANISOU 4839  CG1 VAL B 134     1249   1477   1768     37    -21    310       C  
ATOM   4840  CG2 VAL B 134     -45.381  -2.699 111.675  1.00 12.78           C  
ANISOU 4840  CG2 VAL B 134     1387   1625   1844     58    -45    319       C  
ATOM   4841  N   TYR B 135     -45.419  -6.182 114.705  1.00 10.83           N  
ANISOU 4841  N   TYR B 135     1105   1360   1650     34    -57    265       N  
ATOM   4842  CA  TYR B 135     -45.446  -6.819 116.030  1.00  9.99           C  
ANISOU 4842  CA  TYR B 135      990   1242   1564     24    -50    258       C  
ATOM   4843  C   TYR B 135     -44.241  -7.732 116.271  1.00 13.00           C  
ANISOU 4843  C   TYR B 135     1375   1632   1934     19    -49    242       C  
ATOM   4844  O   TYR B 135     -43.605  -7.637 117.321  1.00 11.23           O  
ANISOU 4844  O   TYR B 135     1152   1402   1714      9    -34    241       O  
ATOM   4845  CB  TYR B 135     -46.766  -7.589 116.245  1.00 10.93           C  
ANISOU 4845  CB  TYR B 135     1093   1350   1709     25    -68    257       C  
ATOM   4846  CG  TYR B 135     -46.827  -8.314 117.574  1.00 11.69           C  
ANISOU 4846  CG  TYR B 135     1181   1435   1824     15    -60    253       C  
ATOM   4847  CD1 TYR B 135     -46.970  -7.614 118.768  1.00 13.49           C  
ANISOU 4847  CD1 TYR B 135     1409   1652   2063      9    -35    262       C  
ATOM   4848  CD2 TYR B 135     -46.740  -9.701 117.638  1.00 12.15           C  
ANISOU 4848  CD2 TYR B 135     1235   1492   1889     12    -78    240       C  
ATOM   4849  CE1 TYR B 135     -46.997  -8.274 119.996  1.00 13.57           C  
ANISOU 4849  CE1 TYR B 135     1416   1653   2085      0    -27    260       C  
ATOM   4850  CE2 TYR B 135     -46.788 -10.374 118.859  1.00 12.67           C  
ANISOU 4850  CE2 TYR B 135     1295   1547   1971      3    -70    239       C  
ATOM   4851  CZ  TYR B 135     -46.915  -9.654 120.037  1.00 18.04           C  
ANISOU 4851  CZ  TYR B 135     1977   2219   2658     -3    -44    250       C  
ATOM   4852  OH  TYR B 135     -46.957 -10.307 121.242  1.00 18.59           O  
ANISOU 4852  OH  TYR B 135     2044   2279   2739    -11    -35    251       O  
ATOM   4853  N   VAL B 136     -43.944  -8.640 115.315  1.00 10.49           N  
ANISOU 4853  N   VAL B 136     1059   1325   1601     27    -68    229       N  
ATOM   4854  CA  VAL B 136     -42.814  -9.578 115.457  1.00 10.32           C  
ANISOU 4854  CA  VAL B 136     1040   1310   1570     26    -68    213       C  
ATOM   4855  C   VAL B 136     -41.469  -8.824 115.587  1.00 14.48           C  
ANISOU 4855  C   VAL B 136     1572   1847   2082     22    -44    217       C  
ATOM   4856  O   VAL B 136     -40.639  -9.189 116.428  1.00 14.04           O  
ANISOU 4856  O   VAL B 136     1514   1789   2031     14    -37    211       O  
ATOM   4857  CB  VAL B 136     -42.783 -10.633 114.302  1.00 14.53           C  
ANISOU 4857  CB  VAL B 136     1578   1853   2089     40    -92    196       C  
ATOM   4858  CG1 VAL B 136     -41.529 -11.508 114.386  1.00 14.29           C  
ANISOU 4858  CG1 VAL B 136     1551   1831   2049     42    -90    179       C  
ATOM   4859  CG2 VAL B 136     -44.040 -11.492 114.316  1.00 14.49           C  
ANISOU 4859  CG2 VAL B 136     1565   1834   2105     41   -120    191       C  
ATOM   4860  N   HIS B 137     -41.283  -7.729 114.797  1.00 11.32           N  
ANISOU 4860  N   HIS B 137     1179   1456   1666     26    -33    230       N  
ATOM   4861  CA  HIS B 137     -40.035  -6.957 114.843  1.00 10.77           C  
ANISOU 4861  CA  HIS B 137     1111   1394   1586     20    -11    237       C  
ATOM   4862  C   HIS B 137     -39.857  -6.205 116.176  1.00 14.25           C  
ANISOU 4862  C   HIS B 137     1549   1818   2045      4      4    245       C  
ATOM   4863  O   HIS B 137     -38.722  -6.025 116.625  1.00 14.75           O  
ANISOU 4863  O   HIS B 137     1611   1884   2109     -5     15    244       O  
ATOM   4864  CB  HIS B 137     -39.930  -5.992 113.653  1.00 11.31           C  
ANISOU 4864  CB  HIS B 137     1188   1474   1634     27     -2    253       C  
ATOM   4865  CG  HIS B 137     -38.563  -5.385 113.497  1.00 14.17           C  
ANISOU 4865  CG  HIS B 137     1550   1847   1987     21     21    261       C  
ATOM   4866  ND1 HIS B 137     -38.243  -4.169 114.076  1.00 15.31           N  
ANISOU 4866  ND1 HIS B 137     1694   1981   2143      7     38    277       N  
ATOM   4867  CD2 HIS B 137     -37.453  -5.894 112.914  1.00 15.31           C  
ANISOU 4867  CD2 HIS B 137     1692   2010   2115     27     29    254       C  
ATOM   4868  CE1 HIS B 137     -36.968  -3.959 113.790  1.00 14.35           C  
ANISOU 4868  CE1 HIS B 137     1567   1871   2014      3     54    281       C  
ATOM   4869  NE2 HIS B 137     -36.452  -4.965 113.088  1.00 14.79           N  
ANISOU 4869  NE2 HIS B 137     1621   1945   2053     16     52    269       N  
ATOM   4870  N   THR B 138     -40.984  -5.786 116.831  1.00  9.45           N  
ANISOU 4870  N   THR B 138      942   1195   1454      1      2    251       N  
ATOM   4871  CA  THR B 138     -40.901  -5.110 118.147  1.00  9.02           C  
ANISOU 4871  CA  THR B 138      890   1124   1414    -11     15    255       C  
ATOM   4872  C   THR B 138     -40.249  -6.032 119.171  1.00 11.71           C  
ANISOU 4872  C   THR B 138     1228   1462   1759    -19     12    242       C  
ATOM   4873  O   THR B 138     -39.397  -5.593 119.936  1.00 10.31           O  
ANISOU 4873  O   THR B 138     1054   1279   1583    -29     21    242       O  
ATOM   4874  CB  THR B 138     -42.307  -4.629 118.632  1.00 13.44           C  
ANISOU 4874  CB  THR B 138     1450   1668   1990     -9     16    264       C  
ATOM   4875  OG1 THR B 138     -43.118  -5.763 118.966  1.00 10.92           O  
ANISOU 4875  OG1 THR B 138     1123   1346   1682     -6      4    256       O  
ATOM   4876  CG2 THR B 138     -43.011  -3.750 117.614  1.00  8.10           C  
ANISOU 4876  CG2 THR B 138      775    992   1310      0     16    278       C  
ATOM   4877  N   LEU B 139     -40.595  -7.342 119.127  1.00  8.78           N  
ANISOU 4877  N   LEU B 139      851   1093   1390    -14     -3    231       N  
ATOM   4878  CA  LEU B 139     -40.035  -8.347 120.048  1.00  8.23           C  
ANISOU 4878  CA  LEU B 139      779   1020   1326    -19     -9    220       C  
ATOM   4879  C   LEU B 139     -38.523  -8.491 119.864  1.00 11.77           C  
ANISOU 4879  C   LEU B 139     1226   1480   1765    -21     -7    213       C  
ATOM   4880  O   LEU B 139     -37.820  -8.799 120.816  1.00 11.49           O  
ANISOU 4880  O   LEU B 139     1192   1440   1736    -29     -8    208       O  
ATOM   4881  CB  LEU B 139     -40.729  -9.714 119.845  1.00  8.02           C  
ANISOU 4881  CB  LEU B 139      748    993   1308    -12    -27    211       C  
ATOM   4882  CG  LEU B 139     -42.268  -9.700 119.881  1.00 12.40           C  
ANISOU 4882  CG  LEU B 139     1298   1537   1878    -10    -32    219       C  
ATOM   4883  CD1 LEU B 139     -42.834 -11.040 119.455  1.00 12.40           C  
ANISOU 4883  CD1 LEU B 139     1291   1536   1887     -5    -55    210       C  
ATOM   4884  CD2 LEU B 139     -42.786  -9.309 121.266  1.00 14.36           C  
ANISOU 4884  CD2 LEU B 139     1548   1769   2138    -18    -18    227       C  
ATOM   4885  N   ALA B 140     -38.019  -8.238 118.635  1.00  7.63           N  
ANISOU 4885  N   ALA B 140      700    972   1228    -14     -3    214       N  
ATOM   4886  CA  ALA B 140     -36.583  -8.292 118.358  1.00  6.72           C  
ANISOU 4886  CA  ALA B 140      579    869   1106    -15      4    210       C  
ATOM   4887  C   ALA B 140     -35.898  -6.959 118.716  1.00 10.15           C  
ANISOU 4887  C   ALA B 140     1014   1300   1544    -28     20    224       C  
ATOM   4888  O   ALA B 140     -34.869  -6.957 119.402  1.00  9.45           O  
ANISOU 4888  O   ALA B 140      920   1210   1463    -37     21    221       O  
ATOM   4889  CB  ALA B 140     -36.347  -8.623 116.893  1.00  7.28           C  
ANISOU 4889  CB  ALA B 140      648    959   1158      1      4    207       C  
ATOM   4890  N   ALA B 141     -36.483  -5.820 118.260  1.00  6.20           N  
ANISOU 4890  N   ALA B 141      533    790   1033    -24     26    237       N  
ATOM   4891  CA  ALA B 141     -35.897  -4.485 118.452  1.00  6.19           C  
ANISOU 4891  CA  ALA B 141      557    771   1023    -20     29    247       C  
ATOM   4892  C   ALA B 141     -35.875  -4.052 119.923  1.00  9.92           C  
ANISOU 4892  C   ALA B 141      998   1240   1530    -55     41    249       C  
ATOM   4893  O   ALA B 141     -34.967  -3.339 120.334  1.00  9.96           O  
ANISOU 4893  O   ALA B 141     1002   1240   1543    -67     46    253       O  
ATOM   4894  CB  ALA B 141     -36.646  -3.460 117.617  1.00  6.82           C  
ANISOU 4894  CB  ALA B 141      607    867   1117    -37     51    268       C  
ATOM   4895  N   ASP B 142     -36.881  -4.465 120.711  1.00  7.19           N  
ANISOU 4895  N   ASP B 142      660    883   1189    -52     34    243       N  
ATOM   4896  CA  ASP B 142     -36.926  -4.114 122.137  1.00  6.49           C  
ANISOU 4896  CA  ASP B 142      583    776   1109    -61     33    239       C  
ATOM   4897  C   ASP B 142     -35.921  -4.941 122.938  1.00  9.69           C  
ANISOU 4897  C   ASP B 142      984   1183   1515    -68     23    228       C  
ATOM   4898  O   ASP B 142     -35.638  -4.617 124.091  1.00  9.64           O  
ANISOU 4898  O   ASP B 142      987   1162   1512    -77     20    224       O  
ATOM   4899  CB  ASP B 142     -38.352  -4.287 122.704  1.00  8.31           C  
ANISOU 4899  CB  ASP B 142      821    996   1342    -55     34    239       C  
ATOM   4900  CG  ASP B 142     -39.369  -3.312 122.128  1.00 14.97           C  
ANISOU 4900  CG  ASP B 142     1668   1834   2188    -48     43    251       C  
ATOM   4901  OD1 ASP B 142     -38.946  -2.276 121.562  1.00 17.25           O  
ANISOU 4901  OD1 ASP B 142     1958   2121   2476    -52     50    261       O  
ATOM   4902  OD2 ASP B 142     -40.583  -3.560 122.286  1.00 14.02           O  
ANISOU 4902  OD2 ASP B 142     1547   1708   2073    -40     44    253       O  
ATOM   4903  N   LYS B 143     -35.357  -5.996 122.313  1.00  6.29           N  
ANISOU 4903  N   LYS B 143      575    755   1061    -39      5    217       N  
ATOM   4904  CA  LYS B 143     -34.361  -6.851 122.962  1.00  6.19           C  
ANISOU 4904  CA  LYS B 143      562    741   1049    -41     -5    208       C  
ATOM   4905  C   LYS B 143     -32.926  -6.389 122.660  1.00 10.15           C  
ANISOU 4905  C   LYS B 143     1010   1267   1581    -73      7    214       C  
ATOM   4906  O   LYS B 143     -32.123  -6.243 123.582  1.00 10.04           O  
ANISOU 4906  O   LYS B 143      996   1244   1575    -84     -2    211       O  
ATOM   4907  CB  LYS B 143     -34.548  -8.325 122.542  1.00  7.71           C  
ANISOU 4907  CB  LYS B 143      707    959   1263    -53     -6    201       C  
ATOM   4908  CG  LYS B 143     -35.736  -9.011 123.211  1.00  9.67           C  
ANISOU 4908  CG  LYS B 143      964   1196   1513    -50    -13    199       C  
ATOM   4909  CD  LYS B 143     -35.842 -10.486 122.780  1.00 17.93           C  
ANISOU 4909  CD  LYS B 143     2004   2249   2561    -39    -26    189       C  
ATOM   4910  CE  LYS B 143     -36.977 -11.221 123.472  1.00 17.69           C  
ANISOU 4910  CE  LYS B 143     1979   2205   2537    -38    -33    190       C  
ATOM   4911  NZ  LYS B 143     -38.306 -10.646 123.126  1.00 26.16           N  
ANISOU 4911  NZ  LYS B 143     3054   3273   3610    -36    -25    199       N  
ATOM   4912  N   PHE B 144     -32.593  -6.200 121.363  1.00  7.09           N  
ANISOU 4912  N   PHE B 144      611    896   1189    -67     18    220       N  
ATOM   4913  CA  PHE B 144     -31.215  -5.874 120.946  1.00  7.84           C  
ANISOU 4913  CA  PHE B 144      688   1001   1291    -73     25    225       C  
ATOM   4914  C   PHE B 144     -31.008  -4.372 120.738  1.00 11.57           C  
ANISOU 4914  C   PHE B 144     1162   1466   1769    -86     38    242       C  
ATOM   4915  O   PHE B 144     -29.901  -3.860 120.957  1.00  9.84           O  
ANISOU 4915  O   PHE B 144      929   1245   1565   -100     39    247       O  
ATOM   4916  CB  PHE B 144     -30.838  -6.647 119.659  1.00  9.88           C  
ANISOU 4916  CB  PHE B 144      932   1282   1539    -57     34    223       C  
ATOM   4917  CG  PHE B 144     -30.925  -8.152 119.790  1.00 11.50           C  
ANISOU 4917  CG  PHE B 144     1137   1493   1742    -43     19    205       C  
ATOM   4918  CD1 PHE B 144     -29.865  -8.884 120.317  1.00 15.13           C  
ANISOU 4918  CD1 PHE B 144     1581   1953   2213    -43     10    196       C  
ATOM   4919  CD2 PHE B 144     -32.044  -8.843 119.339  1.00 13.57           C  
ANISOU 4919  CD2 PHE B 144     1410   1756   1992    -30     13    198       C  
ATOM   4920  CE1 PHE B 144     -29.946 -10.277 120.436  1.00 16.43           C  
ANISOU 4920  CE1 PHE B 144     1746   2119   2377    -30     -5    181       C  
ATOM   4921  CE2 PHE B 144     -32.121 -10.236 119.452  1.00 16.82           C  
ANISOU 4921  CE2 PHE B 144     1820   2167   2404    -18     -2    182       C  
ATOM   4922  CZ  PHE B 144     -31.070 -10.944 119.997  1.00 15.25           C  
ANISOU 4922  CZ  PHE B 144     1609   1969   2216    -18    -10    174       C  
ATOM   4923  N   GLY B 145     -32.050  -3.692 120.258  1.00  8.33           N  
ANISOU 4923  N   GLY B 145      764   1051   1350    -83     47    251       N  
ATOM   4924  CA  GLY B 145     -31.971  -2.275 119.928  1.00  8.18           C  
ANISOU 4924  CA  GLY B 145      747   1023   1336    -93     59    269       C  
ATOM   4925  C   GLY B 145     -31.819  -2.041 118.438  1.00 12.25           C  
ANISOU 4925  C   GLY B 145     1256   1559   1841    -85     77    284       C  
ATOM   4926  O   GLY B 145     -32.409  -2.763 117.629  1.00 12.55           O  
ANISOU 4926  O   GLY B 145     1297   1611   1860    -67     78    280       O  
ATOM   4927  N   PRO B 146     -30.995  -1.040 118.026  1.00  8.23           N  
ANISOU 4927  N   PRO B 146      738   1049   1341    -97     90    302       N  
ATOM   4928  CA  PRO B 146     -30.813  -0.796 116.583  1.00  7.89           C  
ANISOU 4928  CA  PRO B 146      688   1025   1283    -88    111    320       C  
ATOM   4929  C   PRO B 146     -30.366  -2.049 115.841  1.00 11.01           C  
ANISOU 4929  C   PRO B 146     1073   1448   1663    -70    115    309       C  
ATOM   4930  O   PRO B 146     -29.429  -2.718 116.265  1.00 11.06           O  
ANISOU 4930  O   PRO B 146     1062   1460   1680    -73    112    299       O  
ATOM   4931  CB  PRO B 146     -29.751   0.314 116.537  1.00  9.81           C  
ANISOU 4931  CB  PRO B 146      918   1261   1547   -108    124    340       C  
ATOM   4932  CG  PRO B 146     -29.148   0.338 117.911  1.00 14.19           C  
ANISOU 4932  CG  PRO B 146     1467   1798   2127   -125    106    327       C  
ATOM   4933  CD  PRO B 146     -30.209  -0.098 118.839  1.00  9.55           C  
ANISOU 4933  CD  PRO B 146      899   1196   1532   -119     87    308       C  
HETATM 4934  N   MSE B 147     -31.102  -2.423 114.799  1.00  6.02           N  
ANISOU 4934  N   MSE B 147      466    824    998    -42    110    306       N  
HETATM 4935  CA  MSE B 147     -30.854  -3.665 114.079  1.00  5.31           C  
ANISOU 4935  CA  MSE B 147      441    720    857     10     71    281       C  
HETATM 4936  C   MSE B 147     -31.469  -3.592 112.686  1.00 12.20           C  
ANISOU 4936  C   MSE B 147     1244   1653   1738    -12    129    304       C  
HETATM 4937  O   MSE B 147     -32.189  -2.638 112.383  1.00 11.79           O  
ANISOU 4937  O   MSE B 147     1206   1593   1682    -16    132    321       O  
HETATM 4938  CB  MSE B 147     -31.448  -4.866 114.867  1.00  5.70           C  
ANISOU 4938  CB  MSE B 147      458    782    926     -7     75    265       C  
HETATM 4939  CG  MSE B 147     -32.976  -4.787 115.046  1.00  9.79           C  
ANISOU 4939  CG  MSE B 147      948   1310   1461    -21     80    266       C  
HETATM 4940 SE   MSE B 147     -33.699  -6.289 116.037  0.75 14.55          SE  
ANISOU 4940 SE   MSE B 147     1555   1903   2072    -15     53    239      SE  
HETATM 4941  CE  MSE B 147     -33.224  -7.752 114.780  1.00 11.59           C  
ANISOU 4941  CE  MSE B 147     1176   1554   1675     11     51    222       C  
ATOM   4942  N   PRO B 148     -31.268  -4.624 111.828  1.00 10.18           N  
ANISOU 4942  N   PRO B 148      990   1420   1459      9    132    292       N  
ATOM   4943  CA  PRO B 148     -31.916  -4.601 110.515  1.00 10.06           C  
ANISOU 4943  CA  PRO B 148      993   1419   1410     28    136    297       C  
ATOM   4944  C   PRO B 148     -33.430  -4.732 110.625  1.00 14.03           C  
ANISOU 4944  C   PRO B 148     1514   1908   1908     33    109    289       C  
ATOM   4945  O   PRO B 148     -33.936  -5.394 111.540  1.00 13.53           O  
ANISOU 4945  O   PRO B 148     1449   1831   1862     29     88    271       O  
ATOM   4946  CB  PRO B 148     -31.298  -5.816 109.786  1.00 11.97           C  
ANISOU 4946  CB  PRO B 148     1233   1685   1631     51    141    279       C  
ATOM   4947  CG  PRO B 148     -30.128  -6.228 110.621  1.00 16.62           C  
ANISOU 4947  CG  PRO B 148     1796   2272   2247     42    147    271       C  
ATOM   4948  CD  PRO B 148     -30.455  -5.838 112.008  1.00 11.82           C  
ANISOU 4948  CD  PRO B 148     1183   1638   1670     18    130    271       C  
ATOM   4949  N   PHE B 149     -34.153  -4.056 109.737  1.00 10.56           N  
ANISOU 4949  N   PHE B 149     1091   1472   1448     41    111    306       N  
ATOM   4950  CA  PHE B 149     -35.595  -4.217 109.598  1.00 10.35           C  
ANISOU 4950  CA  PHE B 149     1080   1436   1416     49     85    299       C  
ATOM   4951  C   PHE B 149     -35.890  -4.480 108.115  1.00 14.93           C  
ANISOU 4951  C   PHE B 149     1679   2036   1956     72     82    300       C  
ATOM   4952  O   PHE B 149     -36.093  -3.536 107.348  1.00 14.90           O  
ANISOU 4952  O   PHE B 149     1688   2038   1937     75     92    324       O  
ATOM   4953  CB  PHE B 149     -36.339  -2.951 110.096  1.00 12.13           C  
ANISOU 4953  CB  PHE B 149     1309   1640   1661     34     84    320       C  
ATOM   4954  CG  PHE B 149     -37.832  -3.133 110.349  1.00 13.89           C  
ANISOU 4954  CG  PHE B 149     1539   1847   1891     39     57    312       C  
ATOM   4955  CD1 PHE B 149     -38.467  -4.337 110.054  1.00 16.79           C  
ANISOU 4955  CD1 PHE B 149     1911   2221   2250     53     33    291       C  
ATOM   4956  CD2 PHE B 149     -38.591  -2.105 110.898  1.00 16.19           C  
ANISOU 4956  CD2 PHE B 149     1832   2118   2202     30     55    327       C  
ATOM   4957  CE1 PHE B 149     -39.835  -4.505 110.296  1.00 17.72           C  
ANISOU 4957  CE1 PHE B 149     2030   2324   2380     56      9    286       C  
ATOM   4958  CE2 PHE B 149     -39.962  -2.272 111.131  1.00 18.79           C  
ANISOU 4958  CE2 PHE B 149     2164   2434   2542     35     34    322       C  
ATOM   4959  CZ  PHE B 149     -40.573  -3.472 110.837  1.00 16.76           C  
ANISOU 4959  CZ  PHE B 149     1907   2183   2278     47     11    303       C  
ATOM   4960  N   PRO B 150     -35.658  -5.738 107.648  1.00 12.24           N  
ANISOU 4960  N   PRO B 150     1343   1711   1598     90     74    276       N  
ATOM   4961  CA  PRO B 150     -35.735  -6.005 106.202  1.00 12.72           C  
ANISOU 4961  CA  PRO B 150     1424   1794   1615    114     74    275       C  
ATOM   4962  C   PRO B 150     -37.000  -5.463 105.544  1.00 17.17           C  
ANISOU 4962  C   PRO B 150     2009   2353   2164    121     53    286       C  
ATOM   4963  O   PRO B 150     -38.114  -5.704 106.029  1.00 16.00           O  
ANISOU 4963  O   PRO B 150     1859   2186   2034    117     24    277       O  
ATOM   4964  CB  PRO B 150     -35.650  -7.530 106.121  1.00 14.63           C  
ANISOU 4964  CB  PRO B 150     1668   2040   1850    130     56    240       C  
ATOM   4965  CG  PRO B 150     -34.909  -7.928 107.333  1.00 18.58           C  
ANISOU 4965  CG  PRO B 150     2144   2531   2385    115     63    230       C  
ATOM   4966  CD  PRO B 150     -35.305  -6.955 108.408  1.00 13.56           C  
ANISOU 4966  CD  PRO B 150     1497   1873   1782     89     63    248       C  
ATOM   4967  N   ALA B 151     -36.828  -4.685 104.460  1.00 14.99           N  
ANISOU 4967  N   ALA B 151     1748   2092   1855    131     70    309       N  
ATOM   4968  CA  ALA B 151     -37.948  -4.103 103.727  1.00 15.21           C  
ANISOU 4968  CA  ALA B 151     1798   2117   1866    139     50    324       C  
ATOM   4969  C   ALA B 151     -38.619  -5.151 102.849  1.00 20.18           C  
ANISOU 4969  C   ALA B 151     2449   2756   2464    163     18    299       C  
ATOM   4970  O   ALA B 151     -37.954  -6.071 102.367  1.00 19.42           O  
ANISOU 4970  O   ALA B 151     2358   2677   2342    179     23    278       O  
ATOM   4971  CB  ALA B 151     -37.462  -2.939 102.873  1.00 16.43           C  
ANISOU 4971  CB  ALA B 151     1964   2284   1994    141     79    359       C  
ATOM   4972  N   TYR B 152     -39.932  -5.026 102.640  1.00 17.93           N  
ANISOU 4972  N   TYR B 152     2173   2458   2181    167    -18    300       N  
ATOM   4973  CA  TYR B 152     -40.658  -5.972 101.796  1.00 19.36           C  
ANISOU 4973  CA  TYR B 152     2375   2645   2335    189    -55    276       C  
ATOM   4974  C   TYR B 152     -40.689  -5.532 100.330  1.00 25.98           C  
ANISOU 4974  C   TYR B 152     3247   3505   3120    211    -55    291       C  
ATOM   4975  O   TYR B 152     -40.829  -6.371  99.450  1.00 25.98           O  
ANISOU 4975  O   TYR B 152     3270   3518   3083    233    -76    269       O  
ATOM   4976  CB  TYR B 152     -42.091  -6.220 102.332  1.00 21.08           C  
ANISOU 4976  CB  TYR B 152     2583   2839   2589    181    -98    267       C  
ATOM   4977  CG  TYR B 152     -42.868  -4.952 102.620  1.00 24.12           C  
ANISOU 4977  CG  TYR B 152     2961   3209   2996    170    -99    298       C  
ATOM   4978  CD1 TYR B 152     -43.508  -4.253 101.597  1.00 26.32           C  
ANISOU 4978  CD1 TYR B 152     3261   3492   3248    183   -115    317       C  
ATOM   4979  CD2 TYR B 152     -43.048  -4.503 103.924  1.00 25.14           C  
ANISOU 4979  CD2 TYR B 152     3064   3317   3173    148    -88    306       C  
ATOM   4980  CE1 TYR B 152     -44.231  -3.092 101.856  1.00 27.14           C  
ANISOU 4980  CE1 TYR B 152     3357   3579   3374    175   -116    345       C  
ATOM   4981  CE2 TYR B 152     -43.787  -3.353 104.199  1.00 26.29           C  
ANISOU 4981  CE2 TYR B 152     3203   3446   3339    141    -89    331       C  
ATOM   4982  CZ  TYR B 152     -44.376  -2.649 103.160  1.00 35.03           C  
ANISOU 4982  CZ  TYR B 152     4330   4558   4422    154   -103    351       C  
ATOM   4983  OH  TYR B 152     -45.104  -1.513 103.423  1.00 36.95           O  
ANISOU 4983  OH  TYR B 152     4567   4783   4689    148   -104    376       O  
ATOM   4984  N   GLU B 153     -40.548  -4.204 100.066  1.00 25.00           N  
ANISOU 4984  N   GLU B 153     3127   3384   2989    205    -31    329       N  
ATOM   4985  CA  GLU B 153     -40.606  -3.658  98.689  1.00 26.19           C  
ANISOU 4985  CA  GLU B 153     3311   3553   3086    225    -29    349       C  
ATOM   4986  C   GLU B 153     -39.543  -4.288  97.776  1.00 31.79           C  
ANISOU 4986  C   GLU B 153     4041   4294   3744    247     -4    338       C  
ATOM   4987  O   GLU B 153     -39.846  -4.640  96.633  1.00 31.49           O  
ANISOU 4987  O   GLU B 153     4037   4272   3656    272    -23    330       O  
ATOM   4988  CB  GLU B 153     -40.468  -2.118  98.695  1.00 27.77           C  
ANISOU 4988  CB  GLU B 153     3509   3749   3294    212     -2    394       C  
ATOM   4989  CG  GLU B 153     -41.653  -1.390  99.326  1.00 37.92           C  
ANISOU 4989  CG  GLU B 153     4783   5006   4621    199    -29    407       C  
ATOM   4990  CD  GLU B 153     -41.401  -0.839 100.720  1.00 53.12           C  
ANISOU 4990  CD  GLU B 153     6674   6908   6600    171     -8    415       C  
ATOM   4991  OE1 GLU B 153     -40.303  -1.083 101.270  1.00 55.10           O  
ANISOU 4991  OE1 GLU B 153     6910   7165   6862    160     23    408       O  
ATOM   4992  OE2 GLU B 153     -42.292  -0.134 101.247  1.00 36.56           O  
ANISOU 4992  OE2 GLU B 153     4568   4787   4537    162    -24    427       O  
ATOM   4993  N   ILE B 154     -38.285  -4.412  98.278  1.00 29.39           N  
ANISOU 4993  N   ILE B 154     3716   3998   3451    238     38    337       N  
ATOM   4994  CA  ILE B 154     -37.176  -5.009  97.505  1.00 29.80           C  
ANISOU 4994  CA  ILE B 154     3782   4080   3461    259     69    327       C  
ATOM   4995  C   ILE B 154     -36.478  -6.123  98.301  1.00 32.60           C  
ANISOU 4995  C   ILE B 154     4113   4432   3842    256     75    293       C  
ATOM   4996  O   ILE B 154     -36.568  -6.153  99.529  1.00 31.26           O  
ANISOU 4996  O   ILE B 154     3913   4240   3725    232     68    289       O  
ATOM   4997  CB  ILE B 154     -36.160  -3.917  97.029  1.00 33.61           C  
ANISOU 4997  CB  ILE B 154     4265   4580   3924    256    123    369       C  
ATOM   4998  CG1 ILE B 154     -35.605  -3.096  98.234  1.00 34.12           C  
ANISOU 4998  CG1 ILE B 154     4291   4628   4047    222    149    391       C  
ATOM   4999  CG2 ILE B 154     -36.791  -3.003  95.959  1.00 34.44           C  
ANISOU 4999  CG2 ILE B 154     4405   4693   3989    267    116    400       C  
ATOM   5000  CD1 ILE B 154     -34.432  -2.122  97.869  1.00 45.13           C  
ANISOU 5000  CD1 ILE B 154     5678   6038   5432    215    204    431       C  
ATOM   5001  N   VAL B 155     -35.778  -7.036  97.599  1.00 29.66           N  
ANISOU 5001  N   VAL B 155     3756   4082   3432    281     87    270       N  
ATOM   5002  CA  VAL B 155     -35.033  -8.117  98.254  1.00 29.38           C  
ANISOU 5002  CA  VAL B 155     3699   4045   3419    282     94    239       C  
ATOM   5003  C   VAL B 155     -33.605  -7.646  98.573  1.00 32.93           C  
ANISOU 5003  C   VAL B 155     4121   4508   3882    272    150    260       C  
ATOM   5004  O   VAL B 155     -32.742  -7.642  97.690  1.00 33.25           O  
ANISOU 5004  O   VAL B 155     4173   4577   3883    293    187    268       O  
ATOM   5005  CB  VAL B 155     -35.033  -9.422  97.400  1.00 33.92           C  
ANISOU 5005  CB  VAL B 155     4303   4633   3952    316     76    199       C  
ATOM   5006  CG1 VAL B 155     -34.413 -10.584  98.176  1.00 33.67           C  
ANISOU 5006  CG1 VAL B 155     4248   4593   3950    316     75    166       C  
ATOM   5007  CG2 VAL B 155     -36.448  -9.774  96.938  1.00 33.77           C  
ANISOU 5007  CG2 VAL B 155     4312   4601   3917    326     18    182       C  
ATOM   5008  N   GLU B 156     -33.381  -7.175  99.815  1.00 28.24           N  
ANISOU 5008  N   GLU B 156     3492   3895   3344    241    157    273       N  
ATOM   5009  CA  GLU B 156     -32.079  -6.643 100.231  1.00 27.95           C  
ANISOU 5009  CA  GLU B 156     3425   3867   3329    227    204    295       C  
ATOM   5010  C   GLU B 156     -31.053  -7.762 100.387  1.00 31.97           C  
ANISOU 5010  C   GLU B 156     3918   4388   3842    241    219    267       C  
ATOM   5011  O   GLU B 156     -31.315  -8.744 101.089  1.00 31.01           O  
ANISOU 5011  O   GLU B 156     3789   4250   3743    240    190    235       O  
ATOM   5012  CB  GLU B 156     -32.213  -5.855 101.545  1.00 28.82           C  
ANISOU 5012  CB  GLU B 156     3506   3950   3496    190    199    311       C  
ATOM   5013  CG  GLU B 156     -33.084  -4.612 101.426  1.00 37.58           C  
ANISOU 5013  CG  GLU B 156     4626   5045   4605    177    190    342       C  
ATOM   5014  CD  GLU B 156     -33.501  -4.011 102.755  1.00 50.16           C  
ANISOU 5014  CD  GLU B 156     6199   6609   6253    146    174    348       C  
ATOM   5015  OE1 GLU B 156     -33.991  -4.771 103.621  1.00 42.32           O  
ANISOU 5015  OE1 GLU B 156     5198   5598   5284    142    145    321       O  
ATOM   5016  OE2 GLU B 156     -33.433  -2.769 102.893  1.00 43.86           O  
ANISOU 5016  OE2 GLU B 156     5395   5801   5469    128    190    381       O  
ATOM   5017  N   ALA B 157     -29.879  -7.625  99.718  1.00 28.50           N  
ANISOU 5017  N   ALA B 157     3473   3975   3380    254    267    281       N  
ATOM   5018  CA  ALA B 157     -28.802  -8.617  99.825  1.00 28.35           C  
ANISOU 5018  CA  ALA B 157     3435   3969   3366    270    287    257       C  
ATOM   5019  C   ALA B 157     -28.264  -8.659 101.250  1.00 31.88           C  
ANISOU 5019  C   ALA B 157     3839   4395   3877    242    284    256       C  
ATOM   5020  O   ALA B 157     -28.082  -9.741 101.811  1.00 32.02           O  
ANISOU 5020  O   ALA B 157     3847   4405   3913    248    266    224       O  
ATOM   5021  CB  ALA B 157     -27.684  -8.283  98.854  1.00 29.56           C  
ANISOU 5021  CB  ALA B 157     3587   4156   3488    288    343    279       C  
ATOM   5022  N   ASN B 158     -28.074  -7.479 101.862  1.00 27.14           N  
ANISOU 5022  N   ASN B 158     3218   3784   3309    210    297    290       N  
ATOM   5023  CA  ASN B 158     -27.654  -7.374 103.252  1.00 26.12           C  
ANISOU 5023  CA  ASN B 158     3052   3633   3237    181    289    290       C  
ATOM   5024  C   ASN B 158     -28.416  -6.233 103.931  1.00 28.21           C  
ANISOU 5024  C   ASN B 158     3318   3874   3528    150    273    313       C  
ATOM   5025  O   ASN B 158     -28.051  -5.064 103.769  1.00 28.44           O  
ANISOU 5025  O   ASN B 158     3339   3905   3563    134    298    348       O  
ATOM   5026  CB  ASN B 158     -26.136  -7.144 103.346  1.00 28.99           C  
ANISOU 5026  CB  ASN B 158     3379   4012   3622    176    333    307       C  
ATOM   5027  CG  ASN B 158     -25.589  -7.252 104.757  1.00 51.29           C  
ANISOU 5027  CG  ASN B 158     6168   6816   6505    151    320    301       C  
ATOM   5028  OD1 ASN B 158     -26.118  -7.986 105.607  1.00 44.31           O  
ANISOU 5028  OD1 ASN B 158     5285   5912   5638    147    283    274       O  
ATOM   5029  ND2 ASN B 158     -24.464  -6.598 105.004  1.00 41.43           N  
ANISOU 5029  ND2 ASN B 158     4885   5572   5285    134    351    326       N  
ATOM   5030  N   PRO B 159     -29.586  -6.534 104.570  1.00 22.62           N  
ANISOU 5030  N   PRO B 159     2621   3141   2830    143    230    294       N  
ATOM   5031  CA  PRO B 159     -30.393  -5.450 105.163  1.00 21.26           C  
ANISOU 5031  CA  PRO B 159     2452   2947   2680    118    215    315       C  
ATOM   5032  C   PRO B 159     -29.595  -4.615 106.159  1.00 23.48           C  
ANISOU 5032  C   PRO B 159     2703   3214   3004     88    231    334       C  
ATOM   5033  O   PRO B 159     -28.902  -5.162 107.022  1.00 22.56           O  
ANISOU 5033  O   PRO B 159     2563   3092   2917     80    229    320       O  
ATOM   5034  CB  PRO B 159     -31.548  -6.195 105.841  1.00 22.69           C  
ANISOU 5034  CB  PRO B 159     2643   3107   2872    118    171    287       C  
ATOM   5035  CG  PRO B 159     -31.605  -7.516 105.161  1.00 27.70           C  
ANISOU 5035  CG  PRO B 159     3291   3755   3478    146    160    256       C  
ATOM   5036  CD  PRO B 159     -30.202  -7.856 104.796  1.00 23.86           C  
ANISOU 5036  CD  PRO B 159     2790   3292   2985    158    195    256       C  
ATOM   5037  N   PRO B 160     -29.583  -3.274 105.991  1.00 18.66           N  
ANISOU 5037  N   PRO B 160     2094   2598   2400     72    247    369       N  
ATOM   5038  CA  PRO B 160     -28.756  -2.445 106.873  1.00 17.38           C  
ANISOU 5038  CA  PRO B 160     1903   2421   2280     43    261    387       C  
ATOM   5039  C   PRO B 160     -29.351  -2.297 108.264  1.00 18.68           C  
ANISOU 5039  C   PRO B 160     2063   2554   2479     22    230    375       C  
ATOM   5040  O   PRO B 160     -30.569  -2.394 108.431  1.00 17.20           O  
ANISOU 5040  O   PRO B 160     1896   2353   2285     26    204    365       O  
ATOM   5041  CB  PRO B 160     -28.697  -1.107 106.142  1.00 19.53           C  
ANISOU 5041  CB  PRO B 160     2183   2695   2543     34    285    428       C  
ATOM   5042  CG  PRO B 160     -29.970  -1.041 105.380  1.00 24.43           C  
ANISOU 5042  CG  PRO B 160     2837   3317   3126     52    268    428       C  
ATOM   5043  CD  PRO B 160     -30.305  -2.459 104.985  1.00 20.06           C  
ANISOU 5043  CD  PRO B 160     2297   2780   2544     79    252    393       C  
ATOM   5044  N   TYR B 161     -28.491  -2.056 109.272  1.00 14.26           N  
ANISOU 5044  N   TYR B 161     1479   1982   1959      0    232    377       N  
ATOM   5045  CA  TYR B 161     -28.942  -1.776 110.629  1.00 13.21           C  
ANISOU 5045  CA  TYR B 161     1344   1818   1857    -21    206    368       C  
ATOM   5046  C   TYR B 161     -29.638  -0.426 110.657  1.00 16.81           C  
ANISOU 5046  C   TYR B 161     1814   2255   2319    -35    205    391       C  
ATOM   5047  O   TYR B 161     -29.139   0.536 110.066  1.00 16.59           O  
ANISOU 5047  O   TYR B 161     1782   2230   2292    -43    228    420       O  
ATOM   5048  CB  TYR B 161     -27.750  -1.772 111.608  1.00 13.73           C  
ANISOU 5048  CB  TYR B 161     1380   1876   1960    -40    208    365       C  
ATOM   5049  CG  TYR B 161     -27.341  -3.146 112.103  1.00 14.80           C  
ANISOU 5049  CG  TYR B 161     1504   2020   2100    -29    195    336       C  
ATOM   5050  CD1 TYR B 161     -26.945  -4.141 111.210  1.00 16.71           C  
ANISOU 5050  CD1 TYR B 161     1742   2288   2318     -4    208    325       C  
ATOM   5051  CD2 TYR B 161     -27.169  -3.393 113.463  1.00 15.19           C  
ANISOU 5051  CD2 TYR B 161     1545   2050   2178    -44    172    321       C  
ATOM   5052  CE1 TYR B 161     -26.482  -5.377 111.660  1.00 16.61           C  
ANISOU 5052  CE1 TYR B 161     1718   2281   2314      6    196    300       C  
ATOM   5053  CE2 TYR B 161     -26.683  -4.617 113.923  1.00 15.95           C  
ANISOU 5053  CE2 TYR B 161     1628   2152   2281    -35    160    297       C  
ATOM   5054  CZ  TYR B 161     -26.348  -5.609 113.018  1.00 20.93           C  
ANISOU 5054  CZ  TYR B 161     2255   2807   2891    -10    172    287       C  
ATOM   5055  OH  TYR B 161     -25.878  -6.817 113.468  1.00 19.65           O  
ANISOU 5055  OH  TYR B 161     2081   2648   2738      1    159    264       O  
ATOM   5056  N   LYS B 162     -30.812  -0.358 111.280  1.00 12.33           N  
ANISOU 5056  N   LYS B 162     1263   1667   1754    -36    180    380       N  
ATOM   5057  CA  LYS B 162     -31.553   0.892 111.366  1.00 11.81           C  
ANISOU 5057  CA  LYS B 162     1211   1579   1695    -46    178    399       C  
ATOM   5058  C   LYS B 162     -31.649   1.361 112.801  1.00 14.63           C  
ANISOU 5058  C   LYS B 162     1565   1907   2086    -67    163    391       C  
ATOM   5059  O   LYS B 162     -31.709   0.541 113.716  1.00 12.58           O  
ANISOU 5059  O   LYS B 162     1302   1642   1835    -67    146    366       O  
ATOM   5060  CB  LYS B 162     -32.958   0.739 110.752  1.00 14.28           C  
ANISOU 5060  CB  LYS B 162     1548   1894   1983    -27    164    396       C  
ATOM   5061  CG  LYS B 162     -32.943   0.501 109.241  1.00 26.92           C  
ANISOU 5061  CG  LYS B 162     3159   3522   3546     -6    177    407       C  
ATOM   5062  CD  LYS B 162     -34.349   0.417 108.675  1.00 36.04           C  
ANISOU 5062  CD  LYS B 162     4337   4676   4679     11    157    405       C  
ATOM   5063  CE  LYS B 162     -34.342   0.214 107.182  1.00 50.66           C  
ANISOU 5063  CE  LYS B 162     6205   6555   6489     32    166    415       C  
ATOM   5064  NZ  LYS B 162     -35.718   0.185 106.625  1.00 61.43           N  
ANISOU 5064  NZ  LYS B 162     7591   7916   7834     48    142    414       N  
ATOM   5065  N   SER B 163     -31.638   2.685 113.010  1.00 11.76           N  
ANISOU 5065  N   SER B 163     1206   1521   1741    -83    168    412       N  
ATOM   5066  CA  SER B 163     -31.784   3.267 114.344  1.00 11.06           C  
ANISOU 5066  CA  SER B 163     1120   1402   1681   -101    153    404       C  
ATOM   5067  C   SER B 163     -33.165   2.972 114.898  1.00 13.24           C  
ANISOU 5067  C   SER B 163     1414   1666   1951    -90    134    386       C  
ATOM   5068  O   SER B 163     -34.104   2.762 114.128  1.00 12.55           O  
ANISOU 5068  O   SER B 163     1337   1587   1843    -72    132    389       O  
ATOM   5069  CB  SER B 163     -31.559   4.774 114.293  1.00 14.67           C  
ANISOU 5069  CB  SER B 163     1580   1836   2157   -119    162    430       C  
ATOM   5070  OG  SER B 163     -32.503   5.401 113.441  1.00 21.46           O  
ANISOU 5070  OG  SER B 163     2459   2695   3002   -107    166    449       O  
ATOM   5071  N   LEU B 164     -33.306   2.974 116.232  1.00  9.89           N  
ANISOU 5071  N   LEU B 164      992   1220   1544    -99    120    369       N  
ATOM   5072  CA  LEU B 164     -34.604   2.741 116.868  1.00  9.12           C  
ANISOU 5072  CA  LEU B 164      910   1111   1445    -89    106    354       C  
ATOM   5073  C   LEU B 164     -35.590   3.842 116.539  1.00 13.36           C  
ANISOU 5073  C   LEU B 164     1462   1631   1984    -85    109    370       C  
ATOM   5074  O   LEU B 164     -36.790   3.590 116.486  1.00 13.54           O  
ANISOU 5074  O   LEU B 164     1493   1652   1999    -70    102    365       O  
ATOM   5075  CB  LEU B 164     -34.454   2.584 118.389  1.00  8.74           C  
ANISOU 5075  CB  LEU B 164      864   1044   1412   -100     94    334       C  
ATOM   5076  CG  LEU B 164     -33.864   1.245 118.858  1.00 12.59           C  
ANISOU 5076  CG  LEU B 164     1340   1546   1896    -99     85    315       C  
ATOM   5077  CD1 LEU B 164     -33.707   1.220 120.353  1.00 12.59           C  
ANISOU 5077  CD1 LEU B 164     1347   1527   1909   -109     72    299       C  
ATOM   5078  CD2 LEU B 164     -34.733   0.065 118.394  1.00 12.81           C  
ANISOU 5078  CD2 LEU B 164     1369   1592   1907    -79     80    305       C  
ATOM   5079  N   LYS B 165     -35.081   5.058 116.232  1.00 10.10           N  
ANISOU 5079  N   LYS B 165     1051   1205   1582    -97    119    392       N  
ATOM   5080  CA  LYS B 165     -35.929   6.161 115.787  1.00  9.75           C  
ANISOU 5080  CA  LYS B 165     1021   1143   1540    -92    122    411       C  
ATOM   5081  C   LYS B 165     -36.583   5.811 114.443  1.00 13.10           C  
ANISOU 5081  C   LYS B 165     1448   1590   1939    -72    125    424       C  
ATOM   5082  O   LYS B 165     -37.800   5.885 114.318  1.00 11.62           O  
ANISOU 5082  O   LYS B 165     1270   1397   1748    -57    116    423       O  
ATOM   5083  CB  LYS B 165     -35.115   7.458 115.665  1.00 12.34           C  
ANISOU 5083  CB  LYS B 165     1349   1452   1887   -111    131    434       C  
ATOM   5084  CG  LYS B 165     -35.945   8.652 115.191  1.00 19.15           C  
ANISOU 5084  CG  LYS B 165     2228   2294   2754   -105    134    456       C  
ATOM   5085  CD  LYS B 165     -35.066   9.807 114.747  1.00 27.99           C  
ANISOU 5085  CD  LYS B 165     3346   3399   3890   -124    145    484       C  
ATOM   5086  CE  LYS B 165     -35.879  11.005 114.298  1.00 39.73           C  
ANISOU 5086  CE  LYS B 165     4850   4863   5383   -118    146    507       C  
ATOM   5087  NZ  LYS B 165     -36.726  10.693 113.109  1.00 46.99           N  
ANISOU 5087  NZ  LYS B 165     5775   5804   6275    -95    148    521       N  
ATOM   5088  N   ASP B 166     -35.765   5.378 113.448  1.00 10.01           N  
ANISOU 5088  N   ASP B 166     1048   1226   1531    -71    136    434       N  
ATOM   5089  CA  ASP B 166     -36.277   4.980 112.127  1.00  9.90           C  
ANISOU 5089  CA  ASP B 166     1040   1235   1486    -50    137    444       C  
ATOM   5090  C   ASP B 166     -37.147   3.733 112.220  1.00 13.23           C  
ANISOU 5090  C   ASP B 166     1462   1669   1894    -33    119    419       C  
ATOM   5091  O   ASP B 166     -38.166   3.646 111.539  1.00 12.56           O  
ANISOU 5091  O   ASP B 166     1387   1589   1795    -17    109    423       O  
ATOM   5092  CB  ASP B 166     -35.121   4.757 111.137  1.00 11.71           C  
ANISOU 5092  CB  ASP B 166     1261   1491   1697    -51    157    458       C  
ATOM   5093  CG  ASP B 166     -34.421   6.039 110.706  1.00 18.52           C  
ANISOU 5093  CG  ASP B 166     2123   2344   2570    -66    176    492       C  
ATOM   5094  OD1 ASP B 166     -34.898   7.132 111.085  1.00 18.44           O  
ANISOU 5094  OD1 ASP B 166     2122   2305   2579    -74    172    504       O  
ATOM   5095  OD2 ASP B 166     -33.435   5.947 109.947  1.00 21.05           O  
ANISOU 5095  OD2 ASP B 166     2435   2686   2879    -68    197    507       O  
ATOM   5096  N   ILE B 167     -36.759   2.772 113.086  1.00 10.19           N  
ANISOU 5096  N   ILE B 167     1067   1288   1517    -38    113    394       N  
ATOM   5097  CA  ILE B 167     -37.546   1.551 113.311  1.00  9.40           C  
ANISOU 5097  CA  ILE B 167      966   1196   1411    -25     96    370       C  
ATOM   5098  C   ILE B 167     -38.937   1.884 113.916  1.00 12.77           C  
ANISOU 5098  C   ILE B 167     1400   1601   1851    -20     83    367       C  
ATOM   5099  O   ILE B 167     -39.957   1.403 113.414  1.00 12.40           O  
ANISOU 5099  O   ILE B 167     1356   1560   1796     -5     70    364       O  
ATOM   5100  CB  ILE B 167     -36.747   0.519 114.185  1.00 12.27           C  
ANISOU 5100  CB  ILE B 167     1317   1564   1781    -32     93    347       C  
ATOM   5101  CG1 ILE B 167     -35.545  -0.076 113.385  1.00 12.97           C  
ANISOU 5101  CG1 ILE B 167     1396   1679   1854    -29    105    347       C  
ATOM   5102  CG2 ILE B 167     -37.662  -0.587 114.703  1.00 11.71           C  
ANISOU 5102  CG2 ILE B 167     1245   1492   1711    -23     75    325       C  
ATOM   5103  CD1 ILE B 167     -34.640  -1.066 114.201  1.00 16.55           C  
ANISOU 5103  CD1 ILE B 167     1835   2137   2317    -36    102    327       C  
ATOM   5104  N   TYR B 168     -38.974   2.751 114.951  1.00  9.77           N  
ANISOU 5104  N   TYR B 168     1022   1195   1494    -32     88    369       N  
ATOM   5105  CA  TYR B 168     -40.247   3.148 115.584  1.00  9.53           C  
ANISOU 5105  CA  TYR B 168      998   1145   1478    -26     81    367       C  
ATOM   5106  C   TYR B 168     -41.089   4.059 114.693  1.00 13.68           C  
ANISOU 5106  C   TYR B 168     1531   1663   2002    -14     80    388       C  
ATOM   5107  O   TYR B 168     -42.309   3.920 114.666  1.00 12.78           O  
ANISOU 5107  O   TYR B 168     1417   1545   1893     -1     69    387       O  
ATOM   5108  CB  TYR B 168     -40.011   3.780 116.967  1.00 10.67           C  
ANISOU 5108  CB  TYR B 168     1148   1264   1644    -39     86    359       C  
ATOM   5109  CG  TYR B 168     -40.097   2.776 118.100  1.00 12.11           C  
ANISOU 5109  CG  TYR B 168     1326   1446   1830    -41     81    336       C  
ATOM   5110  CD1 TYR B 168     -39.072   1.858 118.325  1.00 13.93           C  
ANISOU 5110  CD1 TYR B 168     1547   1691   2053    -49     78    323       C  
ATOM   5111  CD2 TYR B 168     -41.216   2.720 118.926  1.00 12.48           C  
ANISOU 5111  CD2 TYR B 168     1376   1479   1886    -33     79    328       C  
ATOM   5112  CE1 TYR B 168     -39.159   0.909 119.346  1.00 13.82           C  
ANISOU 5112  CE1 TYR B 168     1532   1677   2042    -50     72    304       C  
ATOM   5113  CE2 TYR B 168     -41.311   1.783 119.958  1.00 12.91           C  
ANISOU 5113  CE2 TYR B 168     1429   1535   1943    -34     76    310       C  
ATOM   5114  CZ  TYR B 168     -40.284   0.873 120.160  1.00 18.64           C  
ANISOU 5114  CZ  TYR B 168     2148   2273   2661    -43     71    299       C  
ATOM   5115  OH  TYR B 168     -40.381  -0.065 121.163  1.00 15.09           O  
ANISOU 5115  OH  TYR B 168     1698   1823   2212    -44     66    283       O  
ATOM   5116  N   ASP B 169     -40.436   4.950 113.905  1.00 10.85           N  
ANISOU 5116  N   ASP B 169     1179   1305   1637    -20     90    411       N  
ATOM   5117  CA  ASP B 169     -41.156   5.802 112.940  1.00 10.89           C  
ANISOU 5117  CA  ASP B 169     1194   1306   1638     -8     87    435       C  
ATOM   5118  C   ASP B 169     -41.808   4.949 111.862  1.00 15.08           C  
ANISOU 5118  C   ASP B 169     1724   1860   2144     10     73    434       C  
ATOM   5119  O   ASP B 169     -42.872   5.303 111.353  1.00 14.86           O  
ANISOU 5119  O   ASP B 169     1702   1828   2117     25     61    445       O  
ATOM   5120  CB  ASP B 169     -40.209   6.842 112.305  1.00 12.84           C  
ANISOU 5120  CB  ASP B 169     1447   1550   1881    -19    103    461       C  
ATOM   5121  CG  ASP B 169     -39.777   7.949 113.259  1.00 22.50           C  
ANISOU 5121  CG  ASP B 169     2674   2742   3133    -37    111    465       C  
ATOM   5122  OD1 ASP B 169     -40.259   7.959 114.422  1.00 23.54           O  
ANISOU 5122  OD1 ASP B 169     2806   2855   3283    -38    106    446       O  
ATOM   5123  OD2 ASP B 169     -38.963   8.807 112.844  1.00 26.34           O  
ANISOU 5123  OD2 ASP B 169     3163   3222   3623    -49    123    487       O  
ATOM   5124  N   GLU B 170     -41.188   3.799 111.535  1.00 11.90           N  
ANISOU 5124  N   GLU B 170     1317   1484   1723     11     72    420       N  
ATOM   5125  CA  GLU B 170     -41.749   2.864 110.571  1.00 11.91           C  
ANISOU 5125  CA  GLU B 170     1320   1506   1700     29     55    414       C  
ATOM   5126  C   GLU B 170     -42.937   2.112 111.178  1.00 16.44           C  
ANISOU 5126  C   GLU B 170     1885   2072   2289     36     34    395       C  
ATOM   5127  O   GLU B 170     -43.920   1.864 110.485  1.00 16.42           O  
ANISOU 5127  O   GLU B 170     1885   2074   2281     51     14    397       O  
ATOM   5128  CB  GLU B 170     -40.680   1.879 110.085  1.00 13.04           C  
ANISOU 5128  CB  GLU B 170     1461   1676   1819     29     61    402       C  
ATOM   5129  CG  GLU B 170     -41.161   0.969 108.968  1.00 18.75           C  
ANISOU 5129  CG  GLU B 170     2192   2420   2513     49     42    395       C  
ATOM   5130  CD  GLU B 170     -40.110   0.029 108.417  1.00 30.51           C  
ANISOU 5130  CD  GLU B 170     3682   3936   3976     53     51    382       C  
ATOM   5131  OE1 GLU B 170     -38.905   0.284 108.643  1.00 28.97           O  
ANISOU 5131  OE1 GLU B 170     3480   3745   3783     42     75    388       O  
ATOM   5132  OE2 GLU B 170     -40.488  -0.920 107.694  1.00 15.00           O  
ANISOU 5132  OE2 GLU B 170     1724   1986   1990     70     32    368       O  
ATOM   5133  N   TYR B 171     -42.861   1.778 112.498  1.00 12.35           N  
ANISOU 5133  N   TYR B 171     1357   1542   1794     26     38    378       N  
ATOM   5134  CA  TYR B 171     -43.954   1.078 113.187  1.00 11.64           C  
ANISOU 5134  CA  TYR B 171     1257   1443   1722     31     24    363       C  
ATOM   5135  C   TYR B 171     -45.286   1.818 113.003  1.00 15.35           C  
ANISOU 5135  C   TYR B 171     1726   1898   2207     42     15    377       C  
ATOM   5136  O   TYR B 171     -46.220   1.262 112.429  1.00 14.72           O  
ANISOU 5136  O   TYR B 171     1641   1824   2127     54     -6    375       O  
ATOM   5137  CB  TYR B 171     -43.645   0.908 114.691  1.00 12.19           C  
ANISOU 5137  CB  TYR B 171     1321   1499   1811     18     35    349       C  
ATOM   5138  CG  TYR B 171     -42.518  -0.063 114.998  1.00 13.14           C  
ANISOU 5138  CG  TYR B 171     1438   1633   1921      8     38    332       C  
ATOM   5139  CD1 TYR B 171     -42.183  -1.079 114.105  1.00 14.85           C  
ANISOU 5139  CD1 TYR B 171     1653   1872   2118     15     28    324       C  
ATOM   5140  CD2 TYR B 171     -41.897  -0.067 116.244  1.00 13.50           C  
ANISOU 5140  CD2 TYR B 171     1482   1668   1978     -5     48    323       C  
ATOM   5141  CE1 TYR B 171     -41.195  -2.014 114.409  1.00 14.75           C  
ANISOU 5141  CE1 TYR B 171     1635   1870   2100     10     30    308       C  
ATOM   5142  CE2 TYR B 171     -40.904  -0.993 116.556  1.00 14.17           C  
ANISOU 5142  CE2 TYR B 171     1562   1764   2057    -12     48    308       C  
ATOM   5143  CZ  TYR B 171     -40.571  -1.979 115.643  1.00 20.16           C  
ANISOU 5143  CZ  TYR B 171     2317   2544   2798     -4     39    301       C  
ATOM   5144  OH  TYR B 171     -39.590  -2.891 115.946  1.00 19.85           O  
ANISOU 5144  OH  TYR B 171     2271   2514   2755     -9     39    287       O  
ATOM   5145  N   PHE B 172     -45.347   3.107 113.438  1.00 12.09           N  
ANISOU 5145  N   PHE B 172     1320   1465   1810     39     29    391       N  
ATOM   5146  CA  PHE B 172     -46.572   3.922 113.347  1.00 12.03           C  
ANISOU 5146  CA  PHE B 172     1310   1440   1820     51     23    405       C  
ATOM   5147  C   PHE B 172     -47.034   4.091 111.900  1.00 16.97           C  
ANISOU 5147  C   PHE B 172     1942   2077   2428     65      4    422       C  
ATOM   5148  O   PHE B 172     -48.223   3.970 111.621  1.00 16.57           O  
ANISOU 5148  O   PHE B 172     1883   2023   2390     79    -14    425       O  
ATOM   5149  CB  PHE B 172     -46.362   5.302 114.004  1.00 13.53           C  
ANISOU 5149  CB  PHE B 172     1510   1604   2026     45     41    416       C  
ATOM   5150  CG  PHE B 172     -45.818   5.251 115.417  1.00 14.14           C  
ANISOU 5150  CG  PHE B 172     1587   1670   2115     32     57    399       C  
ATOM   5151  CD1 PHE B 172     -46.619   4.832 116.475  1.00 16.22           C  
ANISOU 5151  CD1 PHE B 172     1842   1924   2397     36     60    384       C  
ATOM   5152  CD2 PHE B 172     -44.547   5.724 115.705  1.00 15.52           C  
ANISOU 5152  CD2 PHE B 172     1772   1841   2285     15     70    399       C  
ATOM   5153  CE1 PHE B 172     -46.122   4.804 117.781  1.00 16.45           C  
ANISOU 5153  CE1 PHE B 172     1876   1943   2432     25     74    369       C  
ATOM   5154  CE2 PHE B 172     -44.053   5.697 117.012  1.00 17.64           C  
ANISOU 5154  CE2 PHE B 172     2043   2097   2562      4     80    382       C  
ATOM   5155  CZ  PHE B 172     -44.845   5.238 118.040  1.00 15.16           C  
ANISOU 5155  CZ  PHE B 172     1724   1775   2260      9     82    367       C  
ATOM   5156  N   ARG B 173     -46.082   4.361 110.970  1.00 14.64           N  
ANISOU 5156  N   ARG B 173     1661   1795   2105     62     10    434       N  
ATOM   5157  CA  ARG B 173     -46.395   4.535 109.538  1.00 15.08           C  
ANISOU 5157  CA  ARG B 173     1728   1865   2138     77     -7    452       C  
ATOM   5158  C   ARG B 173     -47.012   3.258 108.947  1.00 18.69           C  
ANISOU 5158  C   ARG B 173     2179   2340   2581     88    -34    436       C  
ATOM   5159  O   ARG B 173     -47.990   3.334 108.201  1.00 18.59           O  
ANISOU 5159  O   ARG B 173     2169   2328   2568    103    -59    445       O  
ATOM   5160  CB  ARG B 173     -45.127   4.941 108.752  1.00 15.05           C  
ANISOU 5160  CB  ARG B 173     1740   1875   2104     70     11    467       C  
ATOM   5161  CG  ARG B 173     -45.348   5.065 107.237  1.00 26.04           C  
ANISOU 5161  CG  ARG B 173     3148   3283   3462     86     -4    487       C  
ATOM   5162  CD  ARG B 173     -44.139   5.674 106.520  1.00 35.69           C  
ANISOU 5162  CD  ARG B 173     4386   4517   4659     80     20    508       C  
ATOM   5163  NE  ARG B 173     -42.953   4.812 106.594  1.00 34.87           N  
ANISOU 5163  NE  ARG B 173     4277   4433   4537     71     37    492       N  
ATOM   5164  CZ  ARG B 173     -41.925   5.033 107.410  1.00 40.87           C  
ANISOU 5164  CZ  ARG B 173     5027   5187   5313     52     61    489       C  
ATOM   5165  NH1 ARG B 173     -41.919   6.095 108.207  1.00 20.10           N  
ANISOU 5165  NH1 ARG B 173     2394   2529   2713     39     71    500       N  
ATOM   5166  NH2 ARG B 173     -40.887   4.208 107.417  1.00 25.30           N  
ANISOU 5166  NH2 ARG B 173     3050   3235   3327     47     73    475       N  
ATOM   5167  N   GLU B 174     -46.447   2.082 109.297  1.00 13.79           N  
ANISOU 5167  N   GLU B 174     1552   1732   1953     81    -33    412       N  
ATOM   5168  CA  GLU B 174     -46.961   0.795 108.810  1.00 13.34           C  
ANISOU 5168  CA  GLU B 174     1491   1689   1887     91    -61    394       C  
ATOM   5169  C   GLU B 174     -48.305   0.458 109.440  1.00 17.25           C  
ANISOU 5169  C   GLU B 174     1967   2169   2418     94    -79    387       C  
ATOM   5170  O   GLU B 174     -49.201  -0.022 108.749  1.00 16.20           O  
ANISOU 5170  O   GLU B 174     1830   2040   2285    106   -110    385       O  
ATOM   5171  CB  GLU B 174     -45.948  -0.330 109.067  1.00 14.20           C  
ANISOU 5171  CB  GLU B 174     1598   1813   1982     83    -53    371       C  
ATOM   5172  CG  GLU B 174     -44.737  -0.276 108.154  1.00 16.50           C  
ANISOU 5172  CG  GLU B 174     1907   2127   2236     85    -39    376       C  
ATOM   5173  CD  GLU B 174     -45.037  -0.620 106.713  1.00 29.73           C  
ANISOU 5173  CD  GLU B 174     3599   3820   3876    104    -61    378       C  
ATOM   5174  OE1 GLU B 174     -45.469  -1.765 106.453  1.00 22.96           O  
ANISOU 5174  OE1 GLU B 174     2741   2970   3014    112    -87    357       O  
ATOM   5175  OE2 GLU B 174     -44.845   0.256 105.842  1.00 22.21           O  
ANISOU 5175  OE2 GLU B 174     2664   2874   2901    110    -54    402       O  
ATOM   5176  N   LEU B 175     -48.462   0.736 110.756  1.00 14.56           N  
ANISOU 5176  N   LEU B 175     1612   1810   2108     84    -61    384       N  
ATOM   5177  CA  LEU B 175     -49.720   0.465 111.461  1.00 14.83           C  
ANISOU 5177  CA  LEU B 175     1625   1829   2178     87    -71    380       C  
ATOM   5178  C   LEU B 175     -50.860   1.359 110.948  1.00 20.00           C  
ANISOU 5178  C   LEU B 175     2276   2473   2849    102    -85    401       C  
ATOM   5179  O   LEU B 175     -51.977   0.875 110.770  1.00 20.73           O  
ANISOU 5179  O   LEU B 175     2351   2562   2962    110   -110    399       O  
ATOM   5180  CB  LEU B 175     -49.547   0.621 112.989  1.00 14.62           C  
ANISOU 5180  CB  LEU B 175     1591   1788   2176     76    -44    374       C  
ATOM   5181  CG  LEU B 175     -48.650  -0.439 113.676  1.00 19.11           C  
ANISOU 5181  CG  LEU B 175     2159   2366   2737     62    -35    353       C  
ATOM   5182  CD1 LEU B 175     -48.431  -0.101 115.142  1.00 19.14           C  
ANISOU 5182  CD1 LEU B 175     2160   2353   2757     52     -9    349       C  
ATOM   5183  CD2 LEU B 175     -49.239  -1.841 113.534  1.00 21.43           C  
ANISOU 5183  CD2 LEU B 175     2438   2666   3038     64    -59    339       C  
ATOM   5184  N   ASP B 176     -50.562   2.663 110.667  1.00 16.29           N  
ANISOU 5184  N   ASP B 176     1822   1996   2373    105    -72    420       N  
ATOM   5185  CA AASP B 176     -51.566   3.601 110.134  0.50 16.47           C  
ANISOU 5185  CA AASP B 176     1842   2005   2409    120    -86    442       C  
ATOM   5186  CA BASP B 176     -51.573   3.592 110.148  0.50 16.12           C  
ANISOU 5186  CA BASP B 176     1798   1962   2366    120    -86    442       C  
ATOM   5187  C   ASP B 176     -52.036   3.179 108.746  1.00 20.47           C  
ANISOU 5187  C   ASP B 176     2354   2528   2896    133   -122    447       C  
ATOM   5188  O   ASP B 176     -53.235   3.158 108.481  1.00 20.74           O  
ANISOU 5188  O   ASP B 176     2373   2555   2952    145   -148    453       O  
ATOM   5189  CB AASP B 176     -51.007   5.040 110.095  0.50 18.62           C  
ANISOU 5189  CB AASP B 176     2133   2266   2677    119    -64    462       C  
ATOM   5190  CB BASP B 176     -51.038   5.043 110.140  0.50 17.84           C  
ANISOU 5190  CB BASP B 176     2033   2166   2580    119    -63    462       C  
ATOM   5191  CG AASP B 176     -51.179   5.798 111.396  0.50 31.30           C  
ANISOU 5191  CG AASP B 176     3731   3846   4315    115    -38    461       C  
ATOM   5192  CG BASP B 176     -52.079   6.090 109.745  0.50 26.43           C  
ANISOU 5192  CG BASP B 176     3119   3237   3688    135    -75    485       C  
ATOM   5193  OD1AASP B 176     -52.328   6.171 111.716  0.50 33.37           O  
ANISOU 5193  OD1AASP B 176     3979   4092   4609    127    -43    467       O  
ATOM   5194  OD1BASP B 176     -53.287   5.845 109.976  0.50 26.20           O  
ANISOU 5194  OD1BASP B 176     3067   3199   3688    146    -91    483       O  
ATOM   5195  OD2AASP B 176     -50.153   6.133 112.027  0.50 36.19           O  
ANISOU 5195  OD2AASP B 176     4362   4461   4928    100    -13    456       O  
ATOM   5196  OD2BASP B 176     -51.679   7.183 109.303  0.50 33.50           O  
ANISOU 5196  OD2BASP B 176     4032   4123   4573    137    -67    506       O  
ATOM   5197  N   ALA B 177     -51.083   2.835 107.851  1.00 16.46           N  
ANISOU 5197  N   ALA B 177     1868   2042   2345    131   -125    445       N  
ATOM   5198  CA  ALA B 177     -51.408   2.423 106.478  1.00 16.15           C  
ANISOU 5198  CA  ALA B 177     1842   2018   2277    145   -160    448       C  
ATOM   5199  C   ALA B 177     -52.142   1.078 106.451  1.00 18.57           C  
ANISOU 5199  C   ALA B 177     2132   2330   2595    148   -193    426       C  
ATOM   5200  O   ALA B 177     -52.984   0.861 105.585  1.00 18.89           O  
ANISOU 5200  O   ALA B 177     2173   2373   2633    161   -231    429       O  
ATOM   5201  CB  ALA B 177     -50.140   2.342 105.641  1.00 16.88           C  
ANISOU 5201  CB  ALA B 177     1962   2133   2320    144   -148    450       C  
ATOM   5202  N   ALA B 178     -51.812   0.169 107.396  1.00 13.01           N  
ANISOU 5202  N   ALA B 178     1414   1626   1905    135   -180    404       N  
ATOM   5203  CA  ALA B 178     -52.430  -1.156 107.456  1.00 12.56           C  
ANISOU 5203  CA  ALA B 178     1340   1571   1863    134   -209    383       C  
ATOM   5204  C   ALA B 178     -53.873  -1.080 107.927  1.00 16.64           C  
ANISOU 5204  C   ALA B 178     1826   2069   2429    137   -226    389       C  
ATOM   5205  O   ALA B 178     -54.713  -1.825 107.431  1.00 16.68           O  
ANISOU 5205  O   ALA B 178     1819   2073   2445    142   -264    382       O  
ATOM   5206  CB  ALA B 178     -51.630  -2.065 108.366  1.00 12.87           C  
ANISOU 5206  CB  ALA B 178     1373   1612   1903    119   -188    361       C  
ATOM   5207  N   ILE B 179     -54.174  -0.164 108.881  1.00 12.79           N  
ANISOU 5207  N   ILE B 179     1324   1563   1970    135   -197    403       N  
ATOM   5208  CA  ILE B 179     -55.556   0.047 109.350  1.00 13.10           C  
ANISOU 5208  CA  ILE B 179     1333   1585   2059    141   -207    412       C  
ATOM   5209  C   ILE B 179     -56.426   0.681 108.228  1.00 16.48           C  
ANISOU 5209  C   ILE B 179     1762   2012   2489    158   -242    431       C  
ATOM   5210  O   ILE B 179     -57.601   0.347 108.100  1.00 15.50           O  
ANISOU 5210  O   ILE B 179     1611   1880   2398    165   -272    433       O  
ATOM   5211  CB  ILE B 179     -55.583   0.882 110.669  1.00 16.19           C  
ANISOU 5211  CB  ILE B 179     1714   1960   2478    137   -164    419       C  
ATOM   5212  CG1 ILE B 179     -54.990   0.063 111.846  1.00 16.87           C  
ANISOU 5212  CG1 ILE B 179     1796   2048   2569    120   -138    400       C  
ATOM   5213  CG2 ILE B 179     -57.015   1.367 110.993  1.00 17.74           C  
ANISOU 5213  CG2 ILE B 179     1880   2138   2722    149   -170    434       C  
ATOM   5214  CD1 ILE B 179     -54.782   0.865 113.154  1.00 24.72           C  
ANISOU 5214  CD1 ILE B 179     2788   3026   3577    116    -95    403       C  
ATOM   5215  N   ASN B 180     -55.809   1.515 107.369  1.00 14.13           N  
ANISOU 5215  N   ASN B 180     1494   1721   2153    166   -241    444       N  
ATOM   5216  CA  ASN B 180     -56.504   2.112 106.218  1.00 14.94           C  
ANISOU 5216  CA  ASN B 180     1604   1822   2248    184   -276    464       C  
ATOM   5217  C   ASN B 180     -56.475   1.163 104.998  1.00 18.87           C  
ANISOU 5217  C   ASN B 180     2119   2340   2712    189   -319    452       C  
ATOM   5218  O   ASN B 180     -57.222   1.362 104.039  1.00 18.80           O  
ANISOU 5218  O   ASN B 180     2113   2330   2699    204   -359    463       O  
ATOM   5219  CB  ASN B 180     -55.875   3.467 105.849  1.00 18.24           C  
ANISOU 5219  CB  ASN B 180     2050   2239   2643    189   -254    487       C  
ATOM   5220  CG  ASN B 180     -55.908   4.488 106.966  1.00 50.83           C  
ANISOU 5220  CG  ASN B 180     6166   6344   6802    186   -215    497       C  
ATOM   5221  OD1 ASN B 180     -56.739   4.424 107.882  1.00 43.83           O  
ANISOU 5221  OD1 ASN B 180     5250   5443   5961    186   -209    493       O  
ATOM   5222  ND2 ASN B 180     -55.029   5.478 106.887  1.00 46.82           N  
ANISOU 5222  ND2 ASN B 180     5683   5833   6273    183   -188    511       N  
ATOM   5223  N   GLY B 181     -55.614   0.147 105.060  1.00 15.54           N  
ANISOU 5223  N   GLY B 181     1707   1932   2264    179   -312    428       N  
ATOM   5224  CA  GLY B 181     -55.428  -0.806 103.971  1.00 15.37           C  
ANISOU 5224  CA  GLY B 181     1706   1928   2205    185   -349    412       C  
ATOM   5225  C   GLY B 181     -56.574  -1.781 103.802  1.00 19.65           C  
ANISOU 5225  C   GLY B 181     2225   2464   2778    187   -398    399       C  
ATOM   5226  O   GLY B 181     -56.897  -2.165 102.676  1.00 19.78           O  
ANISOU 5226  O   GLY B 181     2257   2488   2770    198   -443    394       O  
ATOM   5227  N   PHE B 182     -57.195  -2.217 104.933  1.00 15.62           N  
ANISOU 5227  N   PHE B 182     1676   1937   2321    175   -390    393       N  
ATOM   5228  CA  PHE B 182     -58.315  -3.171 104.893  1.00 15.45           C  
ANISOU 5228  CA  PHE B 182     1626   1907   2340    173   -434    382       C  
ATOM   5229  C   PHE B 182     -59.451  -2.675 103.988  1.00 21.61           C  
ANISOU 5229  C   PHE B 182     2397   2680   3132    189   -481    399       C  
ATOM   5230  O   PHE B 182     -59.772  -1.482 103.992  1.00 21.19           O  
ANISOU 5230  O   PHE B 182     2342   2621   3089    199   -469    424       O  
ATOM   5231  CB  PHE B 182     -58.849  -3.458 106.311  1.00 16.57           C  
ANISOU 5231  CB  PHE B 182     1725   2031   2539    159   -408    382       C  
ATOM   5232  CG  PHE B 182     -57.911  -4.256 107.188  1.00 16.78           C  
ANISOU 5232  CG  PHE B 182     1756   2062   2558    142   -375    363       C  
ATOM   5233  CD1 PHE B 182     -57.768  -5.629 107.012  1.00 18.92           C  
ANISOU 5233  CD1 PHE B 182     2027   2336   2826    134   -401    339       C  
ATOM   5234  CD2 PHE B 182     -57.274  -3.663 108.272  1.00 18.35           C  
ANISOU 5234  CD2 PHE B 182     1954   2258   2759    135   -321    369       C  
ATOM   5235  CE1 PHE B 182     -56.939  -6.377 107.857  1.00 19.34           C  
ANISOU 5235  CE1 PHE B 182     2082   2391   2875    120   -372    323       C  
ATOM   5236  CE2 PHE B 182     -56.444  -4.412 109.115  1.00 20.63           C  
ANISOU 5236  CE2 PHE B 182     2246   2550   3043    120   -294    352       C  
ATOM   5237  CZ  PHE B 182     -56.273  -5.761 108.894  1.00 18.51           C  
ANISOU 5237  CZ  PHE B 182     1978   2285   2769    113   -319    331       C  
ATOM   5238  N   ASN B 183     -60.048  -3.592 103.199  1.00 19.93           N  
ANISOU 5238  N   ASN B 183     2184   2469   2922    192   -538    385       N  
ATOM   5239  CA  ASN B 183     -61.145  -3.256 102.290  1.00 21.36           C  
ANISOU 5239  CA  ASN B 183     2357   2643   3115    207   -592    398       C  
ATOM   5240  C   ASN B 183     -62.136  -4.421 102.200  1.00 27.63           C  
ANISOU 5240  C   ASN B 183     3120   3426   3952    200   -646    382       C  
ATOM   5241  O   ASN B 183     -61.730  -5.559 101.952  1.00 27.37           O  
ANISOU 5241  O   ASN B 183     3101   3397   3900    193   -665    355       O  
ATOM   5242  CB  ASN B 183     -60.597  -2.895 100.885  1.00 22.93           C  
ANISOU 5242  CB  ASN B 183     2607   2860   3244    225   -617    400       C  
ATOM   5243  CG  ASN B 183     -61.642  -2.345  99.928  1.00 52.35           C  
ANISOU 5243  CG  ASN B 183     6332   6581   6977    243   -671    418       C  
ATOM   5244  OD1 ASN B 183     -62.815  -2.157 100.277  1.00 48.27           O  
ANISOU 5244  OD1 ASN B 183     5773   6046   6521    243   -692    431       O  
ATOM   5245  ND2 ASN B 183     -61.224  -2.043  98.713  1.00 46.90           N  
ANISOU 5245  ND2 ASN B 183     5689   5906   6225    259   -693    422       N  
ATOM   5246  N   ASP B 184     -63.442  -4.134 102.401  1.00 26.72           N  
ANISOU 5246  N   ASP B 184     2961   3293   3898    203   -670    400       N  
ATOM   5247  CA  ASP B 184     -64.500  -5.163 102.375  1.00 27.73           C  
ANISOU 5247  CA  ASP B 184     3051   3407   4079    194   -721    389       C  
ATOM   5248  C   ASP B 184     -64.650  -5.815 100.985  1.00 31.46           C  
ANISOU 5248  C   ASP B 184     3552   3884   4516    203   -795    372       C  
ATOM   5249  O   ASP B 184     -65.164  -6.930 100.882  1.00 31.80           O  
ANISOU 5249  O   ASP B 184     3577   3917   4588    192   -839    353       O  
ATOM   5250  CB  ASP B 184     -65.847  -4.572 102.842  1.00 30.46           C  
ANISOU 5250  CB  ASP B 184     3341   3734   4497    197   -728    416       C  
ATOM   5251  CG  ASP B 184     -65.837  -4.089 104.284  1.00 45.12           C  
ANISOU 5251  CG  ASP B 184     5167   5584   6394    189   -659    430       C  
ATOM   5252  OD1 ASP B 184     -64.914  -3.325 104.648  1.00 45.95           O  
ANISOU 5252  OD1 ASP B 184     5300   5697   6461    193   -606    435       O  
ATOM   5253  OD2 ASP B 184     -66.799  -4.400 105.020  1.00 54.65           O  
ANISOU 5253  OD2 ASP B 184     6321   6775   7669    181   -658    438       O  
ATOM   5254  N   SER B 185     -64.200  -5.120  99.924  1.00 27.58           N  
ANISOU 5254  N   SER B 185     3108   3408   3962    222   -808    377       N  
ATOM   5255  CA  SER B 185     -64.275  -5.644  98.555  1.00 27.48           C  
ANISOU 5255  CA  SER B 185     3133   3404   3906    235   -875    360       C  
ATOM   5256  C   SER B 185     -63.188  -6.695  98.302  1.00 30.32           C  
ANISOU 5256  C   SER B 185     3531   3775   4212    230   -870    326       C  
ATOM   5257  O   SER B 185     -63.366  -7.577  97.459  1.00 30.45           O  
ANISOU 5257  O   SER B 185     3568   3792   4210    234   -929    301       O  
ATOM   5258  CB  SER B 185     -64.153  -4.508  97.543  1.00 30.79           C  
ANISOU 5258  CB  SER B 185     3590   3835   4274    259   -886    381       C  
ATOM   5259  N   ALA B 186     -62.060  -6.600  99.033  1.00 25.53           N  
ANISOU 5259  N   ALA B 186     2937   3180   3584    222   -802    323       N  
ATOM   5260  CA  ALA B 186     -60.947  -7.532  98.875  1.00 24.96           C  
ANISOU 5260  CA  ALA B 186     2900   3120   3464    219   -790    292       C  
ATOM   5261  C   ALA B 186     -61.265  -8.905  99.495  1.00 28.60           C  
ANISOU 5261  C   ALA B 186     3332   3565   3972    199   -809    266       C  
ATOM   5262  O   ALA B 186     -62.229  -9.035 100.260  1.00 28.66           O  
ANISOU 5262  O   ALA B 186     3287   3551   4050    185   -816    277       O  
ATOM   5263  CB  ALA B 186     -59.688  -6.952  99.505  1.00 25.15           C  
ANISOU 5263  CB  ALA B 186     2940   3159   3457    215   -714    299       C  
ATOM   5264  N   GLN B 187     -60.443  -9.925  99.173  1.00 24.38           N  
ANISOU 5264  N   GLN B 187     2828   3036   3397    199   -815    234       N  
ATOM   5265  CA  GLN B 187     -60.600 -11.277  99.725  1.00 23.74           C  
ANISOU 5265  CA  GLN B 187     2726   2939   3357    181   -833    209       C  
ATOM   5266  C   GLN B 187     -60.356 -11.265 101.251  1.00 26.42           C  
ANISOU 5266  C   GLN B 187     3028   3270   3741    160   -770    221       C  
ATOM   5267  O   GLN B 187     -59.617 -10.412 101.749  1.00 25.76           O  
ANISOU 5267  O   GLN B 187     2952   3200   3637    162   -711    237       O  
ATOM   5268  CB  GLN B 187     -59.615 -12.259  99.036  1.00 25.03           C  
ANISOU 5268  CB  GLN B 187     2937   3112   3460    190   -846    171       C  
ATOM   5269  CG  GLN B 187     -59.781 -12.347  97.507  1.00 40.55           C  
ANISOU 5269  CG  GLN B 187     4948   5087   5372    214   -907    155       C  
ATOM   5270  CD  GLN B 187     -61.078 -13.011  97.099  1.00 58.72           C  
ANISOU 5270  CD  GLN B 187     7228   7364   7719    209   -987    145       C  
ATOM   5271  OE1 GLN B 187     -61.620 -13.870  97.810  1.00 55.12           O  
ANISOU 5271  OE1 GLN B 187     6733   6885   7327    188  -1003    137       O  
ATOM   5272  NE2 GLN B 187     -61.548 -12.701  95.899  1.00 48.84           N  
ANISOU 5272  NE2 GLN B 187     6005   6119   6434    228  -1042    144       N  
ATOM   5273  N   PRO B 188     -60.941 -12.231 102.018  1.00 22.07           N  
ANISOU 5273  N   PRO B 188     2438   2697   3252    140   -784    213       N  
ATOM   5274  CA  PRO B 188     -60.664 -12.271 103.474  1.00 20.99           C  
ANISOU 5274  CA  PRO B 188     2270   2553   3150    122   -724    224       C  
ATOM   5275  C   PRO B 188     -59.178 -12.506 103.764  1.00 22.35           C  
ANISOU 5275  C   PRO B 188     2477   2741   3273    122   -677    208       C  
ATOM   5276  O   PRO B 188     -58.443 -12.958 102.878  1.00 21.49           O  
ANISOU 5276  O   PRO B 188     2410   2644   3111    135   -695    184       O  
ATOM   5277  CB  PRO B 188     -61.530 -13.444 103.971  1.00 23.07           C  
ANISOU 5277  CB  PRO B 188     2495   2791   3481    102   -757    217       C  
ATOM   5278  CG  PRO B 188     -62.532 -13.684 102.872  1.00 28.33           C  
ANISOU 5278  CG  PRO B 188     3157   3447   4160    109   -834    210       C  
ATOM   5279  CD  PRO B 188     -61.846 -13.321 101.606  1.00 24.15           C  
ANISOU 5279  CD  PRO B 188     2685   2939   3552    133   -853    196       C  
ATOM   5280  N   ILE B 189     -58.721 -12.176 105.004  1.00 16.87           N  
ANISOU 5280  N   ILE B 189     1767   2048   2596    111   -616    222       N  
ATOM   5281  CA  ILE B 189     -57.303 -12.352 105.393  1.00 15.52           C  
ANISOU 5281  CA  ILE B 189     1622   1890   2383    110   -570    210       C  
ATOM   5282  C   ILE B 189     -56.790 -13.741 104.989  1.00 18.78           C  
ANISOU 5282  C   ILE B 189     2056   2301   2780    109   -600    176       C  
ATOM   5283  O   ILE B 189     -55.808 -13.842 104.258  1.00 18.52           O  
ANISOU 5283  O   ILE B 189     2063   2285   2690    124   -597    158       O  
ATOM   5284  CB  ILE B 189     -57.089 -12.068 106.910  1.00 17.54           C  
ANISOU 5284  CB  ILE B 189     1852   2142   2671     94   -513    226       C  
ATOM   5285  CG1 ILE B 189     -57.580 -10.643 107.285  1.00 17.34           C  
ANISOU 5285  CG1 ILE B 189     1810   2118   2660     98   -483    257       C  
ATOM   5286  CG2 ILE B 189     -55.616 -12.277 107.300  1.00 16.35           C  
ANISOU 5286  CG2 ILE B 189     1728   2004   2481     93   -472    213       C  
ATOM   5287  CD1 ILE B 189     -57.508 -10.322 108.780  1.00 18.72           C  
ANISOU 5287  CD1 ILE B 189     1961   2286   2867     84   -430    273       C  
ATOM   5288  N   PHE B 190     -57.504 -14.799 105.397  1.00 15.14           N  
ANISOU 5288  N   PHE B 190     1567   1815   2369     94   -630    167       N  
ATOM   5289  CA  PHE B 190     -57.191 -16.168 104.978  1.00 15.59           C  
ANISOU 5289  CA  PHE B 190     1642   1863   2418     93   -667    134       C  
ATOM   5290  C   PHE B 190     -58.405 -16.807 104.289  1.00 20.86           C  
ANISOU 5290  C   PHE B 190     2295   2510   3121     91   -738    125       C  
ATOM   5291  O   PHE B 190     -59.534 -16.358 104.494  1.00 20.31           O  
ANISOU 5291  O   PHE B 190     2189   2430   3099     83   -752    148       O  
ATOM   5292  CB  PHE B 190     -56.744 -17.025 106.186  1.00 16.86           C  
ANISOU 5292  CB  PHE B 190     1786   2010   2609     75   -637    130       C  
ATOM   5293  CG  PHE B 190     -55.502 -16.518 106.877  1.00 17.88           C  
ANISOU 5293  CG  PHE B 190     1930   2158   2705     77   -573    136       C  
ATOM   5294  CD1 PHE B 190     -54.241 -16.754 106.340  1.00 20.01           C  
ANISOU 5294  CD1 PHE B 190     2240   2446   2919     91   -563    113       C  
ATOM   5295  CD2 PHE B 190     -55.587 -15.843 108.088  1.00 19.46           C  
ANISOU 5295  CD2 PHE B 190     2104   2358   2933     64   -525    162       C  
ATOM   5296  CE1 PHE B 190     -53.094 -16.286 106.981  1.00 20.21           C  
ANISOU 5296  CE1 PHE B 190     2274   2486   2919     92   -507    119       C  
ATOM   5297  CE2 PHE B 190     -54.437 -15.391 108.736  1.00 21.27           C  
ANISOU 5297  CE2 PHE B 190     2347   2602   3133     65   -471    166       C  
ATOM   5298  CZ  PHE B 190     -53.198 -15.610 108.175  1.00 19.05           C  
ANISOU 5298  CZ  PHE B 190     2102   2338   2800     78   -464    145       C  
ATOM   5299  N   SER B 191     -58.172 -17.856 103.463  1.00 19.35           N  
ANISOU 5299  N   SER B 191     2132   2311   2908     98   -786     91       N  
ATOM   5300  CA  SER B 191     -59.261 -18.564 102.769  1.00 20.83           C  
ANISOU 5300  CA  SER B 191     2309   2476   3128     95   -861     78       C  
ATOM   5301  C   SER B 191     -60.162 -19.291 103.777  1.00 26.93           C  
ANISOU 5301  C   SER B 191     3030   3218   3985     66   -871     90       C  
ATOM   5302  O   SER B 191     -61.370 -19.410 103.556  1.00 27.65           O  
ANISOU 5302  O   SER B 191     3090   3291   4126     57   -918     98       O  
ATOM   5303  CB  SER B 191     -58.693 -19.558 101.760  1.00 24.80           C  
ANISOU 5303  CB  SER B 191     2860   2977   3587    110   -905     35       C  
ATOM   5304  OG  SER B 191     -57.917 -20.557 102.402  1.00 33.39           O  
ANISOU 5304  OG  SER B 191     3951   4054   4680    101   -884     17       O  
ATOM   5305  N   ASP B 192     -59.571 -19.764 104.888  1.00 23.92           N  
ANISOU 5305  N   ASP B 192     2637   2831   3621     52   -825     93       N  
ATOM   5306  CA  ASP B 192     -60.312 -20.397 105.973  1.00 23.87           C  
ANISOU 5306  CA  ASP B 192     2582   2798   3690     25   -822    110       C  
ATOM   5307  C   ASP B 192     -60.148 -19.577 107.256  1.00 26.93           C  
ANISOU 5307  C   ASP B 192     2945   3197   4092     16   -748    143       C  
ATOM   5308  O   ASP B 192     -59.027 -19.191 107.602  1.00 26.06           O  
ANISOU 5308  O   ASP B 192     2859   3105   3936     25   -699    141       O  
ATOM   5309  CB  ASP B 192     -59.822 -21.846 106.190  1.00 26.05           C  
ANISOU 5309  CB  ASP B 192     2869   3052   3976     15   -839     83       C  
ATOM   5310  CG  ASP B 192     -60.506 -22.569 107.347  1.00 39.46           C  
ANISOU 5310  CG  ASP B 192     4520   4722   5752    -14   -832    103       C  
ATOM   5311  OD1 ASP B 192     -61.725 -22.345 107.553  1.00 40.15           O  
ANISOU 5311  OD1 ASP B 192     4563   4797   5897    -28   -848    128       O  
ATOM   5312  OD2 ASP B 192     -59.850 -23.423 107.982  1.00 46.76           O  
ANISOU 5312  OD2 ASP B 192     5451   5635   6679    -23   -814     94       O  
ATOM   5313  N   ALA B 193     -61.268 -19.289 107.951  1.00 22.66           N  
ANISOU 5313  N   ALA B 193     2353   2642   3614      1   -741    174       N  
ATOM   5314  CA  ALA B 193     -61.248 -18.494 109.182  1.00 21.55           C  
ANISOU 5314  CA  ALA B 193     2188   2510   3489     -5   -673    205       C  
ATOM   5315  C   ALA B 193     -60.393 -19.157 110.277  1.00 23.51           C  
ANISOU 5315  C   ALA B 193     2443   2755   3736    -17   -630    203       C  
ATOM   5316  O   ALA B 193     -59.702 -18.464 111.023  1.00 21.55           O  
ANISOU 5316  O   ALA B 193     2203   2523   3462    -14   -573    214       O  
ATOM   5317  CB  ALA B 193     -62.666 -18.275 109.685  1.00 22.70           C  
ANISOU 5317  CB  ALA B 193     2277   2640   3707    -19   -678    236       C  
ATOM   5318  N   GLY B 194     -60.404 -20.495 110.314  1.00 20.36           N  
ANISOU 5318  N   GLY B 194     2042   2333   3362    -31   -662    187       N  
ATOM   5319  CA  GLY B 194     -59.648 -21.273 111.299  1.00 19.60           C  
ANISOU 5319  CA  GLY B 194     1951   2229   3268    -42   -630    184       C  
ATOM   5320  C   GLY B 194     -58.142 -21.073 111.231  1.00 22.12           C  
ANISOU 5320  C   GLY B 194     2316   2571   3518    -27   -599    165       C  
ATOM   5321  O   GLY B 194     -57.436 -21.348 112.206  1.00 21.44           O  
ANISOU 5321  O   GLY B 194     2234   2485   3429    -34   -560    170       O  
ATOM   5322  N   ILE B 195     -57.630 -20.597 110.066  1.00 17.84           N  
ANISOU 5322  N   ILE B 195     1809   2048   2922     -5   -617    144       N  
ATOM   5323  CA  ILE B 195     -56.189 -20.343 109.886  1.00 17.18           C  
ANISOU 5323  CA  ILE B 195     1767   1988   2774     11   -587    127       C  
ATOM   5324  C   ILE B 195     -55.717 -19.173 110.778  1.00 19.59           C  
ANISOU 5324  C   ILE B 195     2068   2313   3063     12   -522    152       C  
ATOM   5325  O   ILE B 195     -54.656 -19.261 111.400  1.00 19.15           O  
ANISOU 5325  O   ILE B 195     2026   2264   2984     12   -486    148       O  
ATOM   5326  CB  ILE B 195     -55.842 -20.112 108.383  1.00 20.50           C  
ANISOU 5326  CB  ILE B 195     2224   2424   3141     35   -621    102       C  
ATOM   5327  CG1 ILE B 195     -56.285 -21.325 107.517  1.00 21.71           C  
ANISOU 5327  CG1 ILE B 195     2386   2555   3308     36   -689     73       C  
ATOM   5328  CG2 ILE B 195     -54.355 -19.818 108.206  1.00 20.25           C  
ANISOU 5328  CG2 ILE B 195     2231   2418   3047     52   -585     88       C  
ATOM   5329  CD1 ILE B 195     -56.118 -21.117 105.987  1.00 28.72           C  
ANISOU 5329  CD1 ILE B 195     3313   3458   4142     60   -728     48       C  
ATOM   5330  N   ASP B 196     -56.516 -18.086 110.848  1.00 15.58           N  
ANISOU 5330  N   ASP B 196     1539   1811   2570     13   -510    176       N  
ATOM   5331  CA  ASP B 196     -56.203 -16.952 111.720  1.00 14.42           C  
ANISOU 5331  CA  ASP B 196     1387   1678   2412     13   -452    199       C  
ATOM   5332  C   ASP B 196     -56.414 -17.355 113.188  1.00 17.24           C  
ANISOU 5332  C   ASP B 196     1719   2021   2811     -6   -420    217       C  
ATOM   5333  O   ASP B 196     -57.537 -17.310 113.691  1.00 16.82           O  
ANISOU 5333  O   ASP B 196     1630   1954   2807    -16   -419    238       O  
ATOM   5334  CB  ASP B 196     -57.068 -15.725 111.350  1.00 15.85           C  
ANISOU 5334  CB  ASP B 196     1554   1866   2601     21   -452    220       C  
ATOM   5335  CG  ASP B 196     -56.815 -14.492 112.209  1.00 19.11           C  
ANISOU 5335  CG  ASP B 196     1964   2290   3005     23   -395    242       C  
ATOM   5336  OD1 ASP B 196     -55.803 -14.480 112.953  1.00 19.27           O  
ANISOU 5336  OD1 ASP B 196     2001   2318   3004     20   -357    239       O  
ATOM   5337  OD2 ASP B 196     -57.612 -13.541 112.124  1.00 20.19           O  
ANISOU 5337  OD2 ASP B 196     2084   2428   3158     28   -391    261       O  
ATOM   5338  N   LEU B 197     -55.335 -17.790 113.853  1.00 14.02           N  
ANISOU 5338  N   LEU B 197     1329   1617   2382     -9   -393    208       N  
ATOM   5339  CA  LEU B 197     -55.395 -18.310 115.224  1.00 13.50           C  
ANISOU 5339  CA  LEU B 197     1245   1537   2347    -26   -364    223       C  
ATOM   5340  C   LEU B 197     -55.778 -17.224 116.253  1.00 16.87           C  
ANISOU 5340  C   LEU B 197     1656   1970   2785    -28   -315    252       C  
ATOM   5341  O   LEU B 197     -56.200 -17.554 117.366  1.00 16.61           O  
ANISOU 5341  O   LEU B 197     1602   1925   2784    -41   -292    270       O  
ATOM   5342  CB  LEU B 197     -54.046 -18.954 115.609  1.00 13.16           C  
ANISOU 5342  CB  LEU B 197     1229   1497   2273    -26   -351    206       C  
ATOM   5343  CG  LEU B 197     -53.563 -20.089 114.694  1.00 17.89           C  
ANISOU 5343  CG  LEU B 197     1848   2089   2861    -20   -395    176       C  
ATOM   5344  CD1 LEU B 197     -52.079 -20.329 114.865  1.00 18.15           C  
ANISOU 5344  CD1 LEU B 197     1909   2133   2853    -13   -376    158       C  
ATOM   5345  CD2 LEU B 197     -54.342 -21.365 114.946  1.00 20.30           C  
ANISOU 5345  CD2 LEU B 197     2132   2365   3217    -36   -427    177       C  
ATOM   5346  N   ILE B 198     -55.623 -15.936 115.888  1.00 13.03           N  
ANISOU 5346  N   ILE B 198     1180   1501   2270    -15   -298    256       N  
ATOM   5347  CA  ILE B 198     -55.875 -14.834 116.827  1.00 12.18           C  
ANISOU 5347  CA  ILE B 198     1063   1399   2168    -14   -252    278       C  
ATOM   5348  C   ILE B 198     -57.313 -14.323 116.761  1.00 14.80           C  
ANISOU 5348  C   ILE B 198     1359   1722   2542    -13   -257    300       C  
ATOM   5349  O   ILE B 198     -57.983 -14.261 117.792  1.00 14.80           O  
ANISOU 5349  O   ILE B 198     1335   1713   2576    -20   -228    320       O  
ATOM   5350  CB  ILE B 198     -54.836 -13.685 116.650  1.00 14.94           C  
ANISOU 5350  CB  ILE B 198     1443   1768   2467     -2   -226    273       C  
ATOM   5351  CG1 ILE B 198     -53.394 -14.236 116.713  1.00 15.71           C  
ANISOU 5351  CG1 ILE B 198     1570   1873   2527     -3   -221    253       C  
ATOM   5352  CG2 ILE B 198     -55.061 -12.561 117.705  1.00 14.90           C  
ANISOU 5352  CG2 ILE B 198     1430   1763   2467     -1   -179    294       C  
ATOM   5353  CD1 ILE B 198     -52.369 -13.246 116.465  1.00 25.50           C  
ANISOU 5353  CD1 ILE B 198     2835   3131   3724      7   -200    249       C  
ATOM   5354  N   TYR B 199     -57.776 -13.902 115.565  1.00 11.07           N  
ANISOU 5354  N   TYR B 199      885   1253   2067     -2   -291    296       N  
ATOM   5355  CA  TYR B 199     -59.095 -13.269 115.447  1.00 11.76           C  
ANISOU 5355  CA  TYR B 199      940   1335   2195      1   -297    316       C  
ATOM   5356  C   TYR B 199     -60.028 -13.949 114.436  1.00 17.56           C  
ANISOU 5356  C   TYR B 199     1654   2058   2962     -1   -356    312       C  
ATOM   5357  O   TYR B 199     -61.157 -13.490 114.246  1.00 18.35           O  
ANISOU 5357  O   TYR B 199     1722   2152   3099      3   -368    329       O  
ATOM   5358  CB  TYR B 199     -58.956 -11.769 115.144  1.00 12.60           C  
ANISOU 5358  CB  TYR B 199     1059   1454   2273     18   -277    324       C  
ATOM   5359  CG  TYR B 199     -58.320 -10.983 116.271  1.00 13.70           C  
ANISOU 5359  CG  TYR B 199     1212   1600   2394     20   -219    332       C  
ATOM   5360  CD1 TYR B 199     -58.831 -11.047 117.567  1.00 15.60           C  
ANISOU 5360  CD1 TYR B 199     1429   1831   2666     12   -183    349       C  
ATOM   5361  CD2 TYR B 199     -57.294 -10.076 116.022  1.00 13.93           C  
ANISOU 5361  CD2 TYR B 199     1275   1643   2375     29   -202    325       C  
ATOM   5362  CE1 TYR B 199     -58.286 -10.286 118.599  1.00 15.10           C  
ANISOU 5362  CE1 TYR B 199     1382   1772   2584     15   -133    354       C  
ATOM   5363  CE2 TYR B 199     -56.750  -9.300 117.045  1.00 14.31           C  
ANISOU 5363  CE2 TYR B 199     1334   1693   2408     30   -154    331       C  
ATOM   5364  CZ  TYR B 199     -57.256  -9.402 118.332  1.00 19.54           C  
ANISOU 5364  CZ  TYR B 199     1979   2347   3100     24   -121    344       C  
ATOM   5365  OH  TYR B 199     -56.741  -8.628 119.341  1.00 17.82           O  
ANISOU 5365  OH  TYR B 199     1777   2131   2865     26    -77    348       O  
ATOM   5366  N   LYS B 200     -59.592 -15.088 113.849  1.00 14.67           N  
ANISOU 5366  N   LYS B 200     1302   1686   2584     -7   -395    289       N  
ATOM   5367  CA  LYS B 200     -60.418 -15.867 112.898  1.00 14.35           C  
ANISOU 5367  CA  LYS B 200     1246   1631   2574    -10   -457    280       C  
ATOM   5368  C   LYS B 200     -60.999 -14.991 111.764  1.00 16.47           C  
ANISOU 5368  C   LYS B 200     1516   1908   2835      6   -489    282       C  
ATOM   5369  O   LYS B 200     -62.206 -15.027 111.507  1.00 15.36           O  
ANISOU 5369  O   LYS B 200     1340   1755   2742      3   -520    295       O  
ATOM   5370  CB  LYS B 200     -61.535 -16.646 113.641  1.00 17.45           C  
ANISOU 5370  CB  LYS B 200     1591   2000   3039    -30   -463    298       C  
ATOM   5371  CG  LYS B 200     -60.993 -17.711 114.589  1.00 27.46           C  
ANISOU 5371  CG  LYS B 200     2862   3257   4315    -46   -443    295       C  
ATOM   5372  CD  LYS B 200     -62.110 -18.468 115.290  1.00 35.13           C  
ANISOU 5372  CD  LYS B 200     3785   4204   5358    -67   -447    318       C  
ATOM   5373  CE  LYS B 200     -61.573 -19.506 116.250  1.00 44.34           C  
ANISOU 5373  CE  LYS B 200     4956   5359   6531    -83   -427    318       C  
ATOM   5374  NZ  LYS B 200     -60.797 -20.567 115.545  1.00 53.04           N  
ANISOU 5374  NZ  LYS B 200     6090   6454   7611    -84   -471    286       N  
ATOM   5375  N   ASN B 201     -60.121 -14.193 111.094  1.00 13.20           N  
ANISOU 5375  N   ASN B 201     1141   1515   2360     23   -481    272       N  
ATOM   5376  CA  ASN B 201     -60.490 -13.319 109.947  1.00 12.89           C  
ANISOU 5376  CA  ASN B 201     1112   1485   2301     41   -510    274       C  
ATOM   5377  C   ASN B 201     -61.277 -12.055 110.337  1.00 16.90           C  
ANISOU 5377  C   ASN B 201     1593   1994   2835     48   -484    303       C  
ATOM   5378  O   ASN B 201     -61.640 -11.274 109.456  1.00 18.57           O  
ANISOU 5378  O   ASN B 201     1811   2212   3035     63   -507    309       O  
ATOM   5379  CB  ASN B 201     -61.217 -14.109 108.840  1.00 12.00           C  
ANISOU 5379  CB  ASN B 201      994   1361   2205     42   -583    259       C  
ATOM   5380  CG  ASN B 201     -60.287 -14.856 107.917  1.00 25.38           C  
ANISOU 5380  CG  ASN B 201     2734   3063   3848     49   -613    226       C  
ATOM   5381  OD1 ASN B 201     -59.075 -14.616 107.885  1.00 15.89           O  
ANISOU 5381  OD1 ASN B 201     1567   1878   2592     57   -582    216       O  
ATOM   5382  ND2 ASN B 201     -60.850 -15.703 107.074  1.00 18.42           N  
ANISOU 5382  ND2 ASN B 201     1851   2167   2980     48   -677    209       N  
ATOM   5383  N   ASP B 202     -61.462 -11.802 111.649  1.00 12.07           N  
ANISOU 5383  N   ASP B 202      957   1376   2253     39   -434    322       N  
ATOM   5384  CA  ASP B 202     -62.165 -10.596 112.092  1.00 12.12           C  
ANISOU 5384  CA  ASP B 202      940   1382   2283     48   -404    348       C  
ATOM   5385  C   ASP B 202     -61.290  -9.353 111.875  1.00 16.40           C  
ANISOU 5385  C   ASP B 202     1519   1941   2771     64   -375    348       C  
ATOM   5386  O   ASP B 202     -60.332  -9.128 112.624  1.00 16.37           O  
ANISOU 5386  O   ASP B 202     1536   1945   2740     61   -330    345       O  
ATOM   5387  CB  ASP B 202     -62.601 -10.717 113.571  1.00 13.76           C  
ANISOU 5387  CB  ASP B 202     1114   1580   2534     37   -356    365       C  
ATOM   5388  CG  ASP B 202     -63.630  -9.673 114.002  1.00 22.65           C  
ANISOU 5388  CG  ASP B 202     2207   2702   3700     47   -332    392       C  
ATOM   5389  OD1 ASP B 202     -63.571  -8.531 113.487  1.00 23.13           O  
ANISOU 5389  OD1 ASP B 202     2281   2769   3738     65   -330    397       O  
ATOM   5390  OD2 ASP B 202     -64.443  -9.977 114.898  1.00 26.81           O  
ANISOU 5390  OD2 ASP B 202     2693   3216   4277     39   -311    409       O  
ATOM   5391  N   VAL B 203     -61.587  -8.580 110.805  1.00 12.18           N  
ANISOU 5391  N   VAL B 203      993   1412   2222     80   -403    353       N  
ATOM   5392  CA  VAL B 203     -60.818  -7.388 110.429  1.00 11.37           C  
ANISOU 5392  CA  VAL B 203      926   1323   2071     94   -381    357       C  
ATOM   5393  C   VAL B 203     -60.882  -6.299 111.519  1.00 14.99           C  
ANISOU 5393  C   VAL B 203     1374   1778   2545     98   -325    375       C  
ATOM   5394  O   VAL B 203     -59.855  -5.699 111.851  1.00 13.68           O  
ANISOU 5394  O   VAL B 203     1237   1621   2341     99   -289    373       O  
ATOM   5395  CB  VAL B 203     -61.276  -6.845 109.034  1.00 15.42           C  
ANISOU 5395  CB  VAL B 203     1448   1840   2570    111   -428    361       C  
ATOM   5396  CG1 VAL B 203     -60.874  -5.384 108.844  1.00 14.84           C  
ANISOU 5396  CG1 VAL B 203     1398   1774   2466    126   -401    376       C  
ATOM   5397  CG2 VAL B 203     -60.731  -7.715 107.903  1.00 15.37           C  
ANISOU 5397  CG2 VAL B 203     1473   1843   2522    112   -473    337       C  
ATOM   5398  N   SER B 204     -62.088  -6.061 112.089  1.00 11.96           N  
ANISOU 5398  N   SER B 204      947   1381   2217     99   -319    394       N  
ATOM   5399  CA  SER B 204     -62.284  -5.024 113.113  1.00 11.76           C  
ANISOU 5399  CA  SER B 204      912   1350   2208    106   -267    411       C  
ATOM   5400  C   SER B 204     -61.428  -5.286 114.360  1.00 14.58           C  
ANISOU 5400  C   SER B 204     1283   1709   2550     94   -217    403       C  
ATOM   5401  O   SER B 204     -60.918  -4.345 114.961  1.00 13.53           O  
ANISOU 5401  O   SER B 204     1167   1577   2397    100   -176    406       O  
ATOM   5402  CB  SER B 204     -63.754  -4.922 113.498  1.00 15.26           C  
ANISOU 5402  CB  SER B 204     1302   1778   2716    111   -268    431       C  
ATOM   5403  OG  SER B 204     -64.209  -6.122 114.101  1.00 25.94           O  
ANISOU 5403  OG  SER B 204     2625   3124   4106     94   -270    429       O  
ATOM   5404  N   LYS B 205     -61.268  -6.568 114.741  1.00 11.25           N  
ANISOU 5404  N   LYS B 205      854   1286   2136     78   -223    392       N  
ATOM   5405  CA  LYS B 205     -60.433  -6.935 115.891  1.00 10.90           C  
ANISOU 5405  CA  LYS B 205      823   1243   2075     66   -181    385       C  
ATOM   5406  C   LYS B 205     -58.945  -6.767 115.575  1.00 15.43           C  
ANISOU 5406  C   LYS B 205     1443   1830   2590     65   -176    367       C  
ATOM   5407  O   LYS B 205     -58.161  -6.437 116.466  1.00 13.79           O  
ANISOU 5407  O   LYS B 205     1254   1625   2362     62   -136    364       O  
ATOM   5408  CB  LYS B 205     -60.737  -8.366 116.356  1.00 11.89           C  
ANISOU 5408  CB  LYS B 205      927   1361   2230     49   -192    381       C  
ATOM   5409  CG  LYS B 205     -62.082  -8.500 117.058  1.00 21.28           C  
ANISOU 5409  CG  LYS B 205     2068   2537   3481     47   -179    402       C  
ATOM   5410  CD  LYS B 205     -62.327  -9.921 117.537  1.00 26.63           C  
ANISOU 5410  CD  LYS B 205     2724   3205   4187     27   -188    402       C  
ATOM   5411  CE  LYS B 205     -63.647 -10.053 118.247  1.00 25.13           C  
ANISOU 5411  CE  LYS B 205     2484   3003   4061     25   -171    427       C  
ATOM   5412  NZ  LYS B 205     -63.878 -11.441 118.717  1.00 32.60           N  
ANISOU 5412  NZ  LYS B 205     3409   3939   5038      4   -179    429       N  
ATOM   5413  N   TRP B 206     -58.563  -6.934 114.286  1.00 14.14           N  
ANISOU 5413  N   TRP B 206     1299   1676   2398     69   -215    356       N  
ATOM   5414  CA  TRP B 206     -57.188  -6.688 113.851  1.00 14.04           C  
ANISOU 5414  CA  TRP B 206     1327   1677   2330     71   -209    342       C  
ATOM   5415  C   TRP B 206     -56.868  -5.203 113.845  1.00 16.76           C  
ANISOU 5415  C   TRP B 206     1688   2025   2655     82   -182    354       C  
ATOM   5416  O   TRP B 206     -55.730  -4.815 114.139  1.00 16.08           O  
ANISOU 5416  O   TRP B 206     1629   1946   2536     78   -156    348       O  
ATOM   5417  CB  TRP B 206     -56.925  -7.306 112.470  1.00 13.28           C  
ANISOU 5417  CB  TRP B 206     1247   1590   2207     74   -255    328       C  
ATOM   5418  CG  TRP B 206     -56.526  -8.747 112.534  1.00 14.63           C  
ANISOU 5418  CG  TRP B 206     1420   1761   2376     63   -273    308       C  
ATOM   5419  CD1 TRP B 206     -57.281  -9.821 112.169  1.00 17.77           C  
ANISOU 5419  CD1 TRP B 206     1799   2150   2803     58   -313    301       C  
ATOM   5420  CD2 TRP B 206     -55.342  -9.278 113.151  1.00 14.35           C  
ANISOU 5420  CD2 TRP B 206     1403   1731   2317     54   -248    294       C  
ATOM   5421  NE1 TRP B 206     -56.605 -10.989 112.444  1.00 17.21           N  
ANISOU 5421  NE1 TRP B 206     1737   2078   2724     47   -317    282       N  
ATOM   5422  CE2 TRP B 206     -55.421 -10.684 113.069  1.00 18.34           C  
ANISOU 5422  CE2 TRP B 206     1902   2230   2835     45   -277    278       C  
ATOM   5423  CE3 TRP B 206     -54.216  -8.698 113.766  1.00 15.60           C  
ANISOU 5423  CE3 TRP B 206     1583   1898   2447     52   -208    293       C  
ATOM   5424  CZ2 TRP B 206     -54.421 -11.521 113.575  1.00 17.58           C  
ANISOU 5424  CZ2 TRP B 206     1819   2136   2723     37   -265    263       C  
ATOM   5425  CZ3 TRP B 206     -53.219  -9.528 114.251  1.00 17.08           C  
ANISOU 5425  CZ3 TRP B 206     1782   2089   2619     43   -198    278       C  
ATOM   5426  CH2 TRP B 206     -53.323 -10.920 114.149  1.00 17.78           C  
ANISOU 5426  CH2 TRP B 206     1865   2172   2720     36   -226    263       C  
ATOM   5427  N   LYS B 207     -57.880  -4.353 113.550  1.00 12.07           N  
ANISOU 5427  N   LYS B 207     1077   1423   2086     94   -189    372       N  
ATOM   5428  CA  LYS B 207     -57.715  -2.900 113.606  1.00 10.89           C  
ANISOU 5428  CA  LYS B 207      941   1270   1925    105   -165    385       C  
ATOM   5429  C   LYS B 207     -57.539  -2.437 115.050  1.00 13.54           C  
ANISOU 5429  C   LYS B 207     1274   1597   2272    102   -115    388       C  
ATOM   5430  O   LYS B 207     -56.696  -1.585 115.320  1.00 12.97           O  
ANISOU 5430  O   LYS B 207     1227   1525   2174    102    -89    387       O  
ATOM   5431  CB  LYS B 207     -58.912  -2.187 112.958  1.00 13.48           C  
ANISOU 5431  CB  LYS B 207     1249   1590   2281    121   -187    403       C  
ATOM   5432  CG  LYS B 207     -58.947  -2.300 111.441  1.00 16.63           C  
ANISOU 5432  CG  LYS B 207     1661   1999   2658    129   -235    402       C  
ATOM   5433  CD  LYS B 207     -60.137  -1.556 110.864  1.00 25.09           C  
ANISOU 5433  CD  LYS B 207     2712   3061   3759    146   -259    422       C  
ATOM   5434  CE  LYS B 207     -60.172  -1.623 109.365  1.00 35.47           C  
ANISOU 5434  CE  LYS B 207     4046   4386   5047    155   -309    422       C  
ATOM   5435  NZ  LYS B 207     -61.365  -0.936 108.817  1.00 48.52           N  
ANISOU 5435  NZ  LYS B 207     5676   6028   6730    171   -337    442       N  
ATOM   5436  N   ARG B 208     -58.319  -3.031 115.993  1.00  9.89           N  
ANISOU 5436  N   ARG B 208      784   1127   1849     97   -102    390       N  
ATOM   5437  CA  ARG B 208     -58.201  -2.723 117.427  1.00  9.41           C  
ANISOU 5437  CA  ARG B 208      723   1059   1796     95    -55    392       C  
ATOM   5438  C   ARG B 208     -56.817  -3.106 117.957  1.00 12.38           C  
ANISOU 5438  C   ARG B 208     1129   1442   2133     81    -38    375       C  
ATOM   5439  O   ARG B 208     -56.200  -2.324 118.675  1.00 11.77           O  
ANISOU 5439  O   ARG B 208     1072   1361   2039     82     -7    374       O  
ATOM   5440  CB  ARG B 208     -59.303  -3.446 118.235  1.00  9.85           C  
ANISOU 5440  CB  ARG B 208      740   1106   1897     92    -45    400       C  
ATOM   5441  CG  ARG B 208     -60.714  -2.937 117.944  1.00 14.02           C  
ANISOU 5441  CG  ARG B 208     1233   1625   2470    107    -54    419       C  
ATOM   5442  CD  ARG B 208     -61.752  -3.663 118.782  1.00 22.14           C  
ANISOU 5442  CD  ARG B 208     2221   2646   3547    103    -40    429       C  
ATOM   5443  NE  ARG B 208     -63.114  -3.193 118.502  1.00 23.01           N  
ANISOU 5443  NE  ARG B 208     2290   2746   3705    117    -48    448       N  
ATOM   5444  CZ  ARG B 208     -63.691  -2.175 119.134  1.00 33.29           C  
ANISOU 5444  CZ  ARG B 208     3581   4039   5026    135    -12    461       C  
ATOM   5445  NH1 ARG B 208     -63.032  -1.510 120.075  1.00 25.26           N  
ANISOU 5445  NH1 ARG B 208     2594   3021   3982    139     33    455       N  
ATOM   5446  NH2 ARG B 208     -64.930  -1.811 118.825  1.00 12.30           N  
ANISOU 5446  NH2 ARG B 208      884   1374   2417    149    -22    478       N  
ATOM   5447  N   PHE B 209     -56.313  -4.309 117.571  1.00  9.64           N  
ANISOU 5447  N   PHE B 209      785   1104   1773     69    -62    363       N  
ATOM   5448  CA  PHE B 209     -54.986  -4.780 117.979  1.00  9.76           C  
ANISOU 5448  CA  PHE B 209      826   1127   1754     57    -51    347       C  
ATOM   5449  C   PHE B 209     -53.879  -3.871 117.421  1.00 14.72           C  
ANISOU 5449  C   PHE B 209     1486   1764   2345     60    -47    343       C  
ATOM   5450  O   PHE B 209     -52.971  -3.485 118.161  1.00 13.79           O  
ANISOU 5450  O   PHE B 209     1386   1645   2207     55    -21    338       O  
ATOM   5451  CB  PHE B 209     -54.765  -6.245 117.534  1.00 11.62           C  
ANISOU 5451  CB  PHE B 209     1058   1369   1988     47    -81    334       C  
ATOM   5452  CG  PHE B 209     -53.361  -6.758 117.762  1.00 13.19           C  
ANISOU 5452  CG  PHE B 209     1281   1577   2153     38    -75    318       C  
ATOM   5453  CD1 PHE B 209     -52.949  -7.170 119.026  1.00 16.01           C  
ANISOU 5453  CD1 PHE B 209     1642   1930   2511     28    -49    314       C  
ATOM   5454  CD2 PHE B 209     -52.461  -6.863 116.708  1.00 15.67           C  
ANISOU 5454  CD2 PHE B 209     1616   1905   2435     40    -94    306       C  
ATOM   5455  CE1 PHE B 209     -51.651  -7.648 119.235  1.00 16.82           C  
ANISOU 5455  CE1 PHE B 209     1765   2040   2586     20    -47    300       C  
ATOM   5456  CE2 PHE B 209     -51.161  -7.332 116.922  1.00 18.54           C  
ANISOU 5456  CE2 PHE B 209     1998   2276   2770     32    -87    292       C  
ATOM   5457  CZ  PHE B 209     -50.766  -7.724 118.182  1.00 16.31           C  
ANISOU 5457  CZ  PHE B 209     1717   1988   2493     22    -65    289       C  
ATOM   5458  N   ALA B 210     -53.954  -3.532 116.106  1.00 12.27           N  
ANISOU 5458  N   ALA B 210     1180   1460   2022     69    -74    347       N  
ATOM   5459  CA  ALA B 210     -52.968  -2.648 115.469  1.00 12.59           C  
ANISOU 5459  CA  ALA B 210     1248   1508   2028     71    -69    348       C  
ATOM   5460  C   ALA B 210     -53.008  -1.247 116.094  1.00 17.13           C  
ANISOU 5460  C   ALA B 210     1829   2070   2608     77    -39    360       C  
ATOM   5461  O   ALA B 210     -51.965  -0.608 116.248  1.00 16.54           O  
ANISOU 5461  O   ALA B 210     1777   1997   2511     72    -22    358       O  
ATOM   5462  CB  ALA B 210     -53.231  -2.561 113.973  1.00 13.29           C  
ANISOU 5462  CB  ALA B 210     1341   1606   2104     82   -103    353       C  
ATOM   5463  N   ASN B 211     -54.205  -0.797 116.502  1.00 13.97           N  
ANISOU 5463  N   ASN B 211     1409   1656   2242     86    -33    371       N  
ATOM   5464  CA  ASN B 211     -54.373   0.496 117.139  1.00 14.01           C  
ANISOU 5464  CA  ASN B 211     1420   1646   2256     94     -5    380       C  
ATOM   5465  C   ASN B 211     -53.860   0.457 118.577  1.00 16.77           C  
ANISOU 5465  C   ASN B 211     1780   1990   2604     86     28    370       C  
ATOM   5466  O   ASN B 211     -53.334   1.455 119.069  1.00 16.57           O  
ANISOU 5466  O   ASN B 211     1774   1954   2569     87     50    370       O  
ATOM   5467  CB  ASN B 211     -55.835   0.913 117.108  1.00 17.18           C  
ANISOU 5467  CB  ASN B 211     1796   2036   2697    110     -9    395       C  
ATOM   5468  CG  ASN B 211     -56.040   2.393 117.187  1.00 36.23           C  
ANISOU 5468  CG  ASN B 211     4217   4432   5115    124      8    407       C  
ATOM   5469  OD1 ASN B 211     -55.301   3.179 116.585  1.00 26.68           O  
ANISOU 5469  OD1 ASN B 211     3032   3223   3882    124      5    411       O  
ATOM   5470  ND2 ASN B 211     -57.134   2.801 117.805  1.00 30.78           N  
ANISOU 5470  ND2 ASN B 211     3506   3729   4460    137     23    416       N  
ATOM   5471  N   SER B 212     -54.023  -0.699 119.261  1.00 12.64           N  
ANISOU 5471  N   SER B 212     1243   1470   2089     77     31    362       N  
ATOM   5472  CA  SER B 212     -53.533  -0.877 120.633  1.00 11.70           C  
ANISOU 5472  CA  SER B 212     1134   1346   1963     70     60    353       C  
ATOM   5473  C   SER B 212     -52.023  -0.976 120.644  1.00 15.43           C  
ANISOU 5473  C   SER B 212     1634   1827   2402     56     59    340       C  
ATOM   5474  O   SER B 212     -51.384  -0.529 121.595  1.00 15.48           O  
ANISOU 5474  O   SER B 212     1659   1826   2396     52     81    334       O  
ATOM   5475  CB  SER B 212     -54.143  -2.124 121.262  1.00 13.38           C  
ANISOU 5475  CB  SER B 212     1327   1562   2197     64     62    352       C  
ATOM   5476  OG  SER B 212     -55.556  -2.046 121.286  1.00 17.96           O  
ANISOU 5476  OG  SER B 212     1877   2134   2814     75     64    366       O  
ATOM   5477  N   LEU B 213     -51.438  -1.555 119.577  1.00 11.99           N  
ANISOU 5477  N   LEU B 213     1201   1406   1950     51     34    336       N  
ATOM   5478  CA  LEU B 213     -49.990  -1.621 119.430  1.00 11.70           C  
ANISOU 5478  CA  LEU B 213     1185   1378   1882     40     33    326       C  
ATOM   5479  C   LEU B 213     -49.431  -0.213 119.213  1.00 13.91           C  
ANISOU 5479  C   LEU B 213     1482   1651   2150     42     44    332       C  
ATOM   5480  O   LEU B 213     -48.405   0.138 119.793  1.00 12.73           O  
ANISOU 5480  O   LEU B 213     1350   1499   1987     33     57    326       O  
ATOM   5481  CB  LEU B 213     -49.612  -2.532 118.252  1.00 11.96           C  
ANISOU 5481  CB  LEU B 213     1215   1428   1901     38      5    320       C  
ATOM   5482  CG  LEU B 213     -48.188  -3.108 118.289  1.00 17.09           C  
ANISOU 5482  CG  LEU B 213     1878   2089   2525     27      5    306       C  
ATOM   5483  CD1 LEU B 213     -48.025  -4.110 119.456  1.00 17.25           C  
ANISOU 5483  CD1 LEU B 213     1895   2107   2553     18     12    295       C  
ATOM   5484  CD2 LEU B 213     -47.842  -3.784 116.971  1.00 18.74           C  
ANISOU 5484  CD2 LEU B 213     2089   2316   2717     30    -19    301       C  
ATOM   5485  N   ARG B 214     -50.170   0.628 118.448  1.00  9.75           N  
ANISOU 5485  N   ARG B 214      952   1119   1633     54     38    347       N  
ATOM   5486  CA  ARG B 214     -49.800   2.027 118.226  1.00  9.13           C  
ANISOU 5486  CA  ARG B 214      890   1030   1549     57     48    357       C  
ATOM   5487  C   ARG B 214     -49.738   2.769 119.561  1.00 12.41           C  
ANISOU 5487  C   ARG B 214     1315   1425   1973     56     74    352       C  
ATOM   5488  O   ARG B 214     -48.795   3.517 119.804  1.00 11.25           O  
ANISOU 5488  O   ARG B 214     1188   1271   1815     48     84    350       O  
ATOM   5489  CB  ARG B 214     -50.809   2.703 117.285  1.00  8.35           C  
ANISOU 5489  CB  ARG B 214      783    926   1464     73     35    374       C  
ATOM   5490  CG  ARG B 214     -50.431   4.126 116.899  1.00 22.94           C  
ANISOU 5490  CG  ARG B 214     2649   2762   3307     76     42    388       C  
ATOM   5491  CD  ARG B 214     -51.592   4.858 116.240  1.00 33.19           C  
ANISOU 5491  CD  ARG B 214     3938   4050   4624     94     31    406       C  
ATOM   5492  NE  ARG B 214     -52.023   4.207 115.000  1.00 40.24           N  
ANISOU 5492  NE  ARG B 214     4821   4960   5509    100      2    412       N  
ATOM   5493  CZ  ARG B 214     -53.034   4.640 114.253  1.00 57.28           C  
ANISOU 5493  CZ  ARG B 214     6969   7113   7682    116    -16    428       C  
ATOM   5494  NH1 ARG B 214     -53.717   5.721 114.611  1.00 49.67           N  
ANISOU 5494  NH1 ARG B 214     6001   6127   6742    129     -5    440       N  
ATOM   5495  NH2 ARG B 214     -53.359   4.007 113.136  1.00 42.58           N  
ANISOU 5495  NH2 ARG B 214     5102   5267   5810    121    -47    431       N  
ATOM   5496  N   LEU B 215     -50.718   2.510 120.455  1.00  9.36           N  
ANISOU 5496  N   LEU B 215      917   1031   1608     64     86    350       N  
ATOM   5497  CA  LEU B 215     -50.735   3.107 121.791  1.00  8.91           C  
ANISOU 5497  CA  LEU B 215      873    957   1555     66    113    343       C  
ATOM   5498  C   LEU B 215     -49.576   2.569 122.652  1.00 12.56           C  
ANISOU 5498  C   LEU B 215     1352   1423   1996     50    119    327       C  
ATOM   5499  O   LEU B 215     -48.948   3.335 123.386  1.00 11.93           O  
ANISOU 5499  O   LEU B 215     1294   1330   1908     46    131    320       O  
ATOM   5500  CB  LEU B 215     -52.091   2.839 122.484  1.00  8.89           C  
ANISOU 5500  CB  LEU B 215      851    948   1578     80    127    346       C  
ATOM   5501  CG  LEU B 215     -52.278   3.494 123.863  1.00 13.86           C  
ANISOU 5501  CG  LEU B 215     1496   1560   2211     88    158    339       C  
ATOM   5502  CD1 LEU B 215     -52.176   5.018 123.769  1.00 13.92           C  
ANISOU 5502  CD1 LEU B 215     1522   1547   2220     97    165    342       C  
ATOM   5503  CD2 LEU B 215     -53.607   3.091 124.482  1.00 17.42           C  
ANISOU 5503  CD2 LEU B 215     1923   2008   2686    102    176    345       C  
ATOM   5504  N   ARG B 216     -49.275   1.256 122.534  1.00  9.44           N  
ANISOU 5504  N   ARG B 216      947   1046   1594     40    106    321       N  
ATOM   5505  CA  ARG B 216     -48.174   0.625 123.279  1.00  9.09           C  
ANISOU 5505  CA  ARG B 216      916   1007   1532     26    108    307       C  
ATOM   5506  C   ARG B 216     -46.815   1.224 122.869  1.00 12.53           C  
ANISOU 5506  C   ARG B 216     1368   1444   1949     14    102    304       C  
ATOM   5507  O   ARG B 216     -46.020   1.602 123.734  1.00 11.95           O  
ANISOU 5507  O   ARG B 216     1312   1361   1866      6    109    294       O  
ATOM   5508  CB  ARG B 216     -48.184  -0.911 123.062  1.00  9.17           C  
ANISOU 5508  CB  ARG B 216      910   1033   1540     20     93    303       C  
ATOM   5509  CG  ARG B 216     -46.973  -1.633 123.653  1.00 13.21           C  
ANISOU 5509  CG  ARG B 216     1433   1551   2033      6     90    290       C  
ATOM   5510  CD  ARG B 216     -46.915  -3.087 123.208  1.00 13.78           C  
ANISOU 5510  CD  ARG B 216     1490   1638   2106      2     72    286       C  
ATOM   5511  NE  ARG B 216     -47.797  -3.943 124.005  1.00  9.78           N  
ANISOU 5511  NE  ARG B 216      974   1128   1614      3     78    287       N  
ATOM   5512  CZ  ARG B 216     -48.008  -5.231 123.749  1.00 25.36           C  
ANISOU 5512  CZ  ARG B 216     2932   3109   3595      0     63    286       C  
ATOM   5513  NH1 ARG B 216     -47.455  -5.803 122.683  1.00 13.35           N  
ANISOU 5513  NH1 ARG B 216     1407   1599   2066     -2     40    279       N  
ATOM   5514  NH2 ARG B 216     -48.807  -5.947 124.529  1.00 14.69           N  
ANISOU 5514  NH2 ARG B 216     1570   1752   2259      0     71    291       N  
ATOM   5515  N   LEU B 217     -46.563   1.330 121.549  1.00  8.71           N  
ANISOU 5515  N   LEU B 217      877    970   1460     14     87    312       N  
ATOM   5516  CA  LEU B 217     -45.287   1.842 121.031  1.00  8.16           C  
ANISOU 5516  CA  LEU B 217      820    905   1377      3     84    313       C  
ATOM   5517  C   LEU B 217     -45.168   3.365 121.202  1.00 13.58           C  
ANISOU 5517  C   LEU B 217     1521   1570   2069      3     94    321       C  
ATOM   5518  O   LEU B 217     -44.055   3.899 121.197  1.00 13.38           O  
ANISOU 5518  O   LEU B 217     1507   1541   2037     -9     95    320       O  
ATOM   5519  CB  LEU B 217     -45.107   1.449 119.556  1.00  7.57           C  
ANISOU 5519  CB  LEU B 217      735    849   1291      5     68    321       C  
ATOM   5520  CG  LEU B 217     -45.151  -0.063 119.263  1.00 11.18           C  
ANISOU 5520  CG  LEU B 217     1179   1325   1743      6     54    311       C  
ATOM   5521  CD1 LEU B 217     -45.262  -0.322 117.794  1.00 10.42           C  
ANISOU 5521  CD1 LEU B 217     1078   1245   1636     13     39    319       C  
ATOM   5522  CD2 LEU B 217     -43.932  -0.780 119.851  1.00 13.73           C  
ANISOU 5522  CD2 LEU B 217     1507   1656   2055     -7     55    298       C  
ATOM   5523  N   ALA B 218     -46.318   4.066 121.370  1.00 10.04           N  
ANISOU 5523  N   ALA B 218     1073   1106   1637     18    102    328       N  
ATOM   5524  CA  ALA B 218     -46.320   5.507 121.611  1.00  9.55           C  
ANISOU 5524  CA  ALA B 218     1026   1019   1583     21    112    333       C  
ATOM   5525  C   ALA B 218     -45.874   5.810 123.039  1.00 13.05           C  
ANISOU 5525  C   ALA B 218     1488   1445   2024     15    124    317       C  
ATOM   5526  O   ALA B 218     -45.021   6.672 123.246  1.00 12.51           O  
ANISOU 5526  O   ALA B 218     1437   1363   1955      4    124    315       O  
ATOM   5527  CB  ALA B 218     -47.706   6.079 121.364  1.00 10.39           C  
ANISOU 5527  CB  ALA B 218     1125   1115   1709     41    116    345       C  
ATOM   5528  N   VAL B 219     -46.419   5.056 124.034  1.00  8.96           N  
ANISOU 5528  N   VAL B 219      968    930   1506     20    133    305       N  
ATOM   5529  CA  VAL B 219     -46.054   5.235 125.449  1.00  7.88           C  
ANISOU 5529  CA  VAL B 219      853    779   1361     17    143    288       C  
ATOM   5530  C   VAL B 219     -44.578   4.846 125.691  1.00 12.33           C  
ANISOU 5530  C   VAL B 219     1426   1350   1909     -4    130    278       C  
ATOM   5531  O   VAL B 219     -43.946   5.369 126.607  1.00 12.04           O  
ANISOU 5531  O   VAL B 219     1411   1297   1866    -11    131    266       O  
ATOM   5532  CB  VAL B 219     -47.030   4.468 126.398  1.00 10.38           C  
ANISOU 5532  CB  VAL B 219     1166   1099   1680     29    158    283       C  
ATOM   5533  CG1 VAL B 219     -46.599   4.598 127.859  1.00  9.88           C  
ANISOU 5533  CG1 VAL B 219     1130   1024   1602     27    169    265       C  
ATOM   5534  CG2 VAL B 219     -48.460   4.960 126.214  1.00  9.58           C  
ANISOU 5534  CG2 VAL B 219     1053    990   1599     50    173    293       C  
ATOM   5535  N   ARG B 220     -44.006   4.019 124.788  1.00  8.62           N  
ANISOU 5535  N   ARG B 220      939    902   1434    -14    117    283       N  
ATOM   5536  CA  ARG B 220     -42.590   3.648 124.839  1.00  8.12           C  
ANISOU 5536  CA  ARG B 220      878    848   1361    -32    105    276       C  
ATOM   5537  C   ARG B 220     -41.684   4.904 124.689  1.00 11.68           C  
ANISOU 5537  C   ARG B 220     1341   1282   1816    -44    102    280       C  
ATOM   5538  O   ARG B 220     -40.536   4.897 125.143  1.00 10.95           O  
ANISOU 5538  O   ARG B 220     1256   1187   1720    -60     94    271       O  
ATOM   5539  CB  ARG B 220     -42.269   2.626 123.725  1.00  8.01           C  
ANISOU 5539  CB  ARG B 220      842    860   1341    -35     94    282       C  
ATOM   5540  CG  ARG B 220     -40.864   2.021 123.821  1.00  7.66           C  
ANISOU 5540  CG  ARG B 220      796    827   1287    -51     84    274       C  
ATOM   5541  CD  ARG B 220     -40.847   0.737 124.626  1.00  6.09           C  
ANISOU 5541  CD  ARG B 220      594    637   1082    -51     79    262       C  
ATOM   5542  NE  ARG B 220     -41.437  -0.381 123.882  1.00 13.03           N  
ANISOU 5542  NE  ARG B 220     1456   1535   1960    -43     74    265       N  
ATOM   5543  CZ  ARG B 220     -42.636  -0.895 124.143  1.00 26.43           C  
ANISOU 5543  CZ  ARG B 220     3149   3231   3664    -32     79    266       C  
ATOM   5544  NH1 ARG B 220     -43.357  -0.434 125.157  1.00 21.91           N  
ANISOU 5544  NH1 ARG B 220     2588   2643   3096    -26     92    264       N  
ATOM   5545  NH2 ARG B 220     -43.100  -1.907 123.423  1.00  7.96           N  
ANISOU 5545  NH2 ARG B 220      793    906   1326    -26     69    267       N  
ATOM   5546  N   LEU B 221     -42.217   5.977 124.061  1.00  8.54           N  
ANISOU 5546  N   LEU B 221      946    870   1429    -37    108    293       N  
ATOM   5547  CA  LEU B 221     -41.431   7.171 123.738  1.00  8.42           C  
ANISOU 5547  CA  LEU B 221      940    837   1421    -49    105    301       C  
ATOM   5548  C   LEU B 221     -41.681   8.347 124.724  1.00 12.23           C  
ANISOU 5548  C   LEU B 221     1448   1285   1914    -45    110    292       C  
ATOM   5549  O   LEU B 221     -41.339   9.491 124.406  1.00 10.82           O  
ANISOU 5549  O   LEU B 221     1278   1086   1748    -52    108    301       O  
ATOM   5550  CB  LEU B 221     -41.722   7.628 122.280  1.00  8.35           C  
ANISOU 5550  CB  LEU B 221      920    835   1418    -44    106    325       C  
ATOM   5551  CG  LEU B 221     -41.660   6.530 121.197  1.00 12.22           C  
ANISOU 5551  CG  LEU B 221     1389   1358   1896    -42    101    333       C  
ATOM   5552  CD1 LEU B 221     -42.002   7.097 119.828  1.00 12.50           C  
ANISOU 5552  CD1 LEU B 221     1420   1397   1932    -34    100    356       C  
ATOM   5553  CD2 LEU B 221     -40.303   5.864 121.169  1.00 12.84           C  
ANISOU 5553  CD2 LEU B 221     1460   1452   1965    -59     95    327       C  
ATOM   5554  N   THR B 222     -42.233   8.059 125.936  1.00  8.37           N  
ANISOU 5554  N   THR B 222      973    789   1418    -35    117    274       N  
ATOM   5555  CA  THR B 222     -42.514   9.129 126.929  1.00  8.25           C  
ANISOU 5555  CA  THR B 222      986    742   1408    -28    123    261       C  
ATOM   5556  C   THR B 222     -41.243   9.904 127.342  1.00 11.25           C  
ANISOU 5556  C   THR B 222     1383   1100   1791    -49    107    253       C  
ATOM   5557  O   THR B 222     -41.335  11.070 127.717  1.00 11.89           O  
ANISOU 5557  O   THR B 222     1487   1150   1882    -47    108    248       O  
ATOM   5558  CB  THR B 222     -43.230   8.559 128.162  1.00 14.22           C  
ANISOU 5558  CB  THR B 222     1754   1498   2151    -14    135    244       C  
ATOM   5559  OG1 THR B 222     -42.432   7.520 128.728  1.00 15.46           O  
ANISOU 5559  OG1 THR B 222     1911   1672   2291    -27    125    233       O  
ATOM   5560  CG2 THR B 222     -44.617   8.047 127.845  1.00 10.82           C  
ANISOU 5560  CG2 THR B 222     1306   1081   1726      8    152    254       C  
ATOM   5561  N   GLU B 223     -40.072   9.239 127.318  1.00  6.84           N  
ANISOU 5561  N   GLU B 223      816    557   1227    -70     93    250       N  
ATOM   5562  CA  GLU B 223     -38.823   9.841 127.795  1.00  6.32           C  
ANISOU 5562  CA  GLU B 223      754    490   1159    -83     72    232       C  
ATOM   5563  C   GLU B 223     -37.983  10.433 126.653  1.00 10.02           C  
ANISOU 5563  C   GLU B 223     1214    940   1654   -110     69    263       C  
ATOM   5564  O   GLU B 223     -37.372  11.490 126.827  1.00  9.65           O  
ANISOU 5564  O   GLU B 223     1179    864   1623   -124     59    263       O  
ATOM   5565  CB  GLU B 223     -37.990   8.810 128.598  1.00  7.28           C  
ANISOU 5565  CB  GLU B 223      884    609   1274   -103     61    225       C  
ATOM   5566  CG  GLU B 223     -38.795   8.055 129.655  1.00 12.17           C  
ANISOU 5566  CG  GLU B 223     1518   1234   1871    -85     70    209       C  
ATOM   5567  CD  GLU B 223     -39.545   8.942 130.631  1.00 15.66           C  
ANISOU 5567  CD  GLU B 223     1994   1647   2308    -70     79    194       C  
ATOM   5568  OE1 GLU B 223     -38.882   9.659 131.412  1.00  7.83           O  
ANISOU 5568  OE1 GLU B 223     1028    630   1316    -79     64    178       O  
ATOM   5569  OE2 GLU B 223     -40.796   8.937 130.598  1.00  3.60           O  
ANISOU 5569  OE2 GLU B 223      393    396    579     12     45     50       O  
ATOM   5570  N   VAL B 224     -37.916   9.735 125.501  1.00  6.92           N  
ANISOU 5570  N   VAL B 224      793    576   1258   -110     74    281       N  
ATOM   5571  CA  VAL B 224     -37.064  10.167 124.381  1.00  7.10           C  
ANISOU 5571  CA  VAL B 224      799    603   1294   -126     73    304       C  
ATOM   5572  C   VAL B 224     -37.742  11.247 123.495  1.00 11.67           C  
ANISOU 5572  C   VAL B 224     1381   1167   1886   -118     82    326       C  
ATOM   5573  O   VAL B 224     -37.053  12.116 122.954  1.00 11.30           O  
ANISOU 5573  O   VAL B 224     1332   1106   1855   -134     80    343       O  
ATOM   5574  CB  VAL B 224     -36.547   8.957 123.540  1.00 10.67           C  
ANISOU 5574  CB  VAL B 224     1224   1096   1736   -129     75    313       C  
ATOM   5575  CG1 VAL B 224     -37.687   8.295 122.758  1.00 10.44           C  
ANISOU 5575  CG1 VAL B 224     1185   1088   1693   -107     86    321       C  
ATOM   5576  CG2 VAL B 224     -35.420   9.381 122.607  1.00 10.53           C  
ANISOU 5576  CG2 VAL B 224     1189   1082   1731   -148     75    334       C  
ATOM   5577  N   ASP B 225     -39.083  11.183 123.344  1.00  8.68           N  
ANISOU 5577  N   ASP B 225     1007    791   1501    -94     93    327       N  
ATOM   5578  CA  ASP B 225     -39.803  12.134 122.487  1.00  8.41           C  
ANISOU 5578  CA  ASP B 225      975    742   1478    -83     99    349       C  
ATOM   5579  C   ASP B 225     -41.268  12.261 122.911  1.00 12.00           C  
ANISOU 5579  C   ASP B 225     1440   1186   1932    -56    108    341       C  
ATOM   5580  O   ASP B 225     -42.120  11.516 122.418  1.00 10.91           O  
ANISOU 5580  O   ASP B 225     1288   1072   1786    -40    113    346       O  
ATOM   5581  CB  ASP B 225     -39.699  11.705 120.999  1.00  9.95           C  
ANISOU 5581  CB  ASP B 225     1149    967   1665    -83    103    375       C  
ATOM   5582  CG  ASP B 225     -40.121  12.779 120.009  1.00 15.84           C  
ANISOU 5582  CG  ASP B 225     1899   1698   2422    -77    107    402       C  
ATOM   5583  OD1 ASP B 225     -40.818  13.726 120.422  1.00 16.41           O  
ANISOU 5583  OD1 ASP B 225     1988   1739   2509    -67    108    401       O  
ATOM   5584  OD2 ASP B 225     -39.779  12.650 118.817  1.00 19.20           O  
ANISOU 5584  OD2 ASP B 225     2312   2143   2840    -80    110    425       O  
ATOM   5585  N   GLN B 226     -41.572  13.240 123.802  1.00  9.17           N  
ANISOU 5585  N   GLN B 226     1106    792   1586    -51    109    328       N  
ATOM   5586  CA  GLN B 226     -42.947  13.461 124.288  1.00  8.81           C  
ANISOU 5586  CA  GLN B 226     1070    735   1543    -23    121    320       C  
ATOM   5587  C   GLN B 226     -43.863  13.887 123.164  1.00 12.29           C  
ANISOU 5587  C   GLN B 226     1499   1176   1995     -7    125    345       C  
ATOM   5588  O   GLN B 226     -45.014  13.461 123.123  1.00 10.87           O  
ANISOU 5588  O   GLN B 226     1309   1006   1814     15    134    345       O  
ATOM   5589  CB  GLN B 226     -42.979  14.510 125.425  1.00 10.43           C  
ANISOU 5589  CB  GLN B 226     1307    899   1758    -19    121    301       C  
ATOM   5590  CG  GLN B 226     -42.299  14.048 126.728  1.00 21.08           C  
ANISOU 5590  CG  GLN B 226     2672   2247   3091    -30    115    272       C  
ATOM   5591  CD  GLN B 226     -40.793  14.240 126.699  1.00 35.05           C  
ANISOU 5591  CD  GLN B 226     4443   4010   4865    -61     96    272       C  
ATOM   5592  OE1 GLN B 226     -40.258  15.060 125.945  1.00 27.33           O  
ANISOU 5592  OE1 GLN B 226     3462   3017   3906    -75     88    290       O  
ATOM   5593  NE2 GLN B 226     -40.092  13.551 127.585  1.00 30.32           N  
ANISOU 5593  NE2 GLN B 226     3850   3420   4252    -72     86    251       N  
ATOM   5594  N   GLU B 227     -43.352  14.747 122.227  1.00  9.85           N  
ANISOU 5594  N   GLU B 227     1190    855   1698    -18    119    369       N  
ATOM   5595  CA  GLU B 227     -44.162  15.252 121.109  1.00  9.85           C  
ANISOU 5595  CA  GLU B 227     1183    853   1707     -2    120    395       C  
ATOM   5596  C   GLU B 227     -44.693  14.111 120.244  1.00 14.81           C  
ANISOU 5596  C   GLU B 227     1787   1521   2319      7    119    405       C  
ATOM   5597  O   GLU B 227     -45.884  14.081 119.931  1.00 14.36           O  
ANISOU 5597  O   GLU B 227     1722   1467   2268     30    121    412       O  
ATOM   5598  CB  GLU B 227     -43.366  16.254 120.256  1.00 11.19           C  
ANISOU 5598  CB  GLU B 227     1358   1006   1888    -19    114    421       C  
ATOM   5599  CG  GLU B 227     -44.208  16.926 119.177  1.00 17.58           C  
ANISOU 5599  CG  GLU B 227     2165   1808   2706     -2    114    450       C  
ATOM   5600  CD  GLU B 227     -43.493  17.989 118.361  1.00 28.98           C  
ANISOU 5600  CD  GLU B 227     3617   3232   4163    -17    110    480       C  
ATOM   5601  OE1 GLU B 227     -42.314  18.283 118.662  1.00 15.79           O  
ANISOU 5601  OE1 GLU B 227     1951   1550   2498    -44    108    478       O  
ATOM   5602  OE2 GLU B 227     -44.116  18.532 117.423  1.00 24.66           O  
ANISOU 5602  OE2 GLU B 227     3070   2679   3621     -4    108    506       O  
ATOM   5603  N   LYS B 228     -43.818  13.152 119.883  1.00 12.47           N  
ANISOU 5603  N   LYS B 228     1477   1255   2004    -10    115    405       N  
ATOM   5604  CA  LYS B 228     -44.225  11.996 119.078  1.00 11.93           C  
ANISOU 5604  CA  LYS B 228     1389   1223   1919     -1    112    411       C  
ATOM   5605  C   LYS B 228     -45.076  11.018 119.910  1.00 15.28           C  
ANISOU 5605  C   LYS B 228     1805   1658   2341     12    115    389       C  
ATOM   5606  O   LYS B 228     -46.080  10.512 119.419  1.00 15.75           O  
ANISOU 5606  O   LYS B 228     1852   1733   2402     28    112    395       O  
ATOM   5607  CB  LYS B 228     -42.994  11.288 118.480  1.00 14.22           C  
ANISOU 5607  CB  LYS B 228     1670   1540   2191    -21    109    415       C  
ATOM   5608  CG  LYS B 228     -43.343  10.247 117.411  1.00 29.49           C  
ANISOU 5608  CG  LYS B 228     3588   3510   4107    -12    103    423       C  
ATOM   5609  CD  LYS B 228     -42.142   9.929 116.506  1.00 43.96           C  
ANISOU 5609  CD  LYS B 228     5415   5365   5922    -26    103    436       C  
ATOM   5610  CE  LYS B 228     -41.788  11.091 115.594  1.00 61.01           C  
ANISOU 5610  CE  LYS B 228     7583   7513   8085    -30    107    466       C  
ATOM   5611  NZ  LYS B 228     -40.631  10.773 114.713  1.00 71.75           N  
ANISOU 5611  NZ  LYS B 228     8936   8897   9428    -44    113    480       N  
ATOM   5612  N   CYS B 229     -44.701  10.800 121.186  1.00 10.49           N  
ANISOU 5612  N   CYS B 229     1208   1044   1733      5    121    366       N  
ATOM   5613  CA  CYS B 229     -45.490   9.953 122.087  1.00 10.03           C  
ANISOU 5613  CA  CYS B 229     1145    993   1672     17    127    348       C  
ATOM   5614  C   CYS B 229     -46.940  10.418 122.128  1.00 13.49           C  
ANISOU 5614  C   CYS B 229     1580   1419   2128     42    136    353       C  
ATOM   5615  O   CYS B 229     -47.849   9.642 121.832  1.00 12.94           O  
ANISOU 5615  O   CYS B 229     1491   1366   2060     55    135    357       O  
ATOM   5616  CB  CYS B 229     -44.874   9.928 123.485  1.00 10.04           C  
ANISOU 5616  CB  CYS B 229     1164    982   1668      7    132    324       C  
ATOM   5617  SG  CYS B 229     -46.041   9.483 124.802  1.00 13.59           S  
ANISOU 5617  SG  CYS B 229     1619   1427   2118     28    149    306       S  
ATOM   5618  N   ILE B 230     -47.155  11.688 122.503  1.00 10.44           N  
ANISOU 5618  N   ILE B 230     1212   1000   1756     50    142    354       N  
ATOM   5619  CA  ILE B 230     -48.490  12.259 122.655  1.00 10.04           C  
ANISOU 5619  CA  ILE B 230     1158    932   1725     77    153    357       C  
ATOM   5620  C   ILE B 230     -49.255  12.302 121.319  1.00 14.33           C  
ANISOU 5620  C   ILE B 230     1682   1486   2278     89    142    383       C  
ATOM   5621  O   ILE B 230     -50.432  11.956 121.281  1.00 14.34           O  
ANISOU 5621  O   ILE B 230     1665   1493   2292    108    146    386       O  
ATOM   5622  CB  ILE B 230     -48.411  13.652 123.345  1.00 12.87           C  
ANISOU 5622  CB  ILE B 230     1544   1250   2096     83    160    350       C  
ATOM   5623  CG1 ILE B 230     -47.817  13.517 124.778  1.00 12.75           C  
ANISOU 5623  CG1 ILE B 230     1551   1225   2067     75    169    321       C  
ATOM   5624  CG2 ILE B 230     -49.787  14.337 123.374  1.00 14.34           C  
ANISOU 5624  CG2 ILE B 230     1726   1416   2305    113    171    356       C  
ATOM   5625  CD1 ILE B 230     -47.364  14.843 125.416  1.00 14.07           C  
ANISOU 5625  CD1 ILE B 230     1752   1352   2244     73    169    310       C  
ATOM   5626  N   ALA B 231     -48.567  12.667 120.218  1.00 11.19           N  
ANISOU 5626  N   ALA B 231     1286   1090   1874     77    129    402       N  
ATOM   5627  CA  ALA B 231     -49.198  12.730 118.889  1.00 11.04           C  
ANISOU 5627  CA  ALA B 231     1253   1082   1859     88    115    427       C  
ATOM   5628  C   ALA B 231     -49.662  11.337 118.419  1.00 13.60           C  
ANISOU 5628  C   ALA B 231     1554   1442   2173     91    106    426       C  
ATOM   5629  O   ALA B 231     -50.771  11.201 117.907  1.00 12.29           O  
ANISOU 5629  O   ALA B 231     1370   1279   2018    109     98    436       O  
ATOM   5630  CB  ALA B 231     -48.231  13.330 117.877  1.00 11.88           C  
ANISOU 5630  CB  ALA B 231     1371   1188   1956     72    106    448       C  
ATOM   5631  N   GLU B 232     -48.821  10.304 118.620  1.00 10.23           N  
ANISOU 5631  N   GLU B 232     1124   1038   1726     73    105    412       N  
ATOM   5632  CA  GLU B 232     -49.166   8.934 118.219  1.00  9.74           C  
ANISOU 5632  CA  GLU B 232     1041   1005   1653     74     94    408       C  
ATOM   5633  C   GLU B 232     -50.226   8.320 119.149  1.00 13.00           C  
ANISOU 5633  C   GLU B 232     1440   1418   2083     87    103    395       C  
ATOM   5634  O   GLU B 232     -51.106   7.599 118.681  1.00 12.07           O  
ANISOU 5634  O   GLU B 232     1301   1313   1973     96     92    400       O  
ATOM   5635  CB  GLU B 232     -47.909   8.043 118.155  1.00 10.71           C  
ANISOU 5635  CB  GLU B 232     1167   1150   1752     53     91    398       C  
ATOM   5636  CG  GLU B 232     -46.931   8.440 117.046  1.00 18.76           C  
ANISOU 5636  CG  GLU B 232     2196   2178   2755     43     84    414       C  
ATOM   5637  CD  GLU B 232     -47.461   8.297 115.628  1.00 29.21           C  
ANISOU 5637  CD  GLU B 232     3512   3517   4070     54     68    433       C  
ATOM   5638  OE1 GLU B 232     -48.438   7.540 115.429  1.00 15.62           O  
ANISOU 5638  OE1 GLU B 232     1775   1807   2353     67     56    430       O  
ATOM   5639  OE2 GLU B 232     -46.842   8.875 114.705  1.00 30.24           O  
ANISOU 5639  OE2 GLU B 232     3653   3650   4188     50     66    452       O  
ATOM   5640  N   ALA B 233     -50.170   8.649 120.458  1.00  9.33           N  
ANISOU 5640  N   ALA B 233      987    935   1624     87    123    380       N  
ATOM   5641  CA  ALA B 233     -51.161   8.160 121.422  1.00  9.62           C  
ANISOU 5641  CA  ALA B 233     1011    970   1675    100    137    370       C  
ATOM   5642  C   ALA B 233     -52.529   8.801 121.180  1.00 13.30           C  
ANISOU 5642  C   ALA B 233     1462   1422   2169    125    141    384       C  
ATOM   5643  O   ALA B 233     -53.546   8.122 121.285  1.00 12.45           O  
ANISOU 5643  O   ALA B 233     1330   1323   2078    135    142    386       O  
ATOM   5644  CB  ALA B 233     -50.698   8.438 122.840  1.00 10.65           C  
ANISOU 5644  CB  ALA B 233     1163   1085   1799     96    158    351       C  
ATOM   5645  N   ASN B 234     -52.552  10.122 120.824  1.00 10.45           N  
ANISOU 5645  N   ASN B 234     1115   1038   1817    133    140    394       N  
ATOM   5646  CA  ASN B 234     -53.803  10.822 120.494  1.00 10.32           C  
ANISOU 5646  CA  ASN B 234     1085   1007   1831    159    141    409       C  
ATOM   5647  C   ASN B 234     -54.442  10.226 119.252  1.00 14.88           C  
ANISOU 5647  C   ASN B 234     1637   1604   2414    163    115    427       C  
ATOM   5648  O   ASN B 234     -55.659  10.067 119.205  1.00 14.13           O  
ANISOU 5648  O   ASN B 234     1515   1508   2344    181    114    434       O  
ATOM   5649  CB  ASN B 234     -53.555  12.334 120.294  1.00  8.99           C  
ANISOU 5649  CB  ASN B 234      939    808   1669    165    142    418       C  
ATOM   5650  CG  ASN B 234     -53.549  13.129 121.575  1.00 22.05           C  
ANISOU 5650  CG  ASN B 234     2614   2433   3330    173    167    400       C  
ATOM   5651  OD1 ASN B 234     -54.339  12.884 122.489  1.00 18.67           O  
ANISOU 5651  OD1 ASN B 234     2178   2003   2914    189    187    389       O  
ATOM   5652  ND2 ASN B 234     -52.770  14.191 121.603  1.00 13.60           N  
ANISOU 5652  ND2 ASN B 234     1572   1339   2256    166    166    400       N  
ATOM   5653  N   ALA B 235     -53.617   9.878 118.240  1.00 12.59           N  
ANISOU 5653  N   ALA B 235     1353   1332   2100    147     94    433       N  
ATOM   5654  CA  ALA B 235     -54.106   9.253 117.014  1.00 12.79           C  
ANISOU 5654  CA  ALA B 235     1360   1378   2124    151     66    447       C  
ATOM   5655  C   ALA B 235     -54.676   7.862 117.306  1.00 18.12           C  
ANISOU 5655  C   ALA B 235     2009   2072   2804    149     61    436       C  
ATOM   5656  O   ALA B 235     -55.672   7.471 116.707  1.00 17.88           O  
ANISOU 5656  O   ALA B 235     1954   2048   2791    161     42    446       O  
ATOM   5657  CB  ALA B 235     -52.981   9.154 115.993  1.00 13.27           C  
ANISOU 5657  CB  ALA B 235     1437   1453   2151    135     50    454       C  
ATOM   5658  N   ALA B 236     -54.062   7.130 118.271  1.00 15.09           N  
ANISOU 5658  N   ALA B 236     1629   1695   2409    135     78    417       N  
ATOM   5659  CA  ALA B 236     -54.523   5.794 118.657  1.00 14.96           C  
ANISOU 5659  CA  ALA B 236     1590   1694   2399    131     76    408       C  
ATOM   5660  C   ALA B 236     -55.840   5.862 119.441  1.00 18.69           C  
ANISOU 5660  C   ALA B 236     2039   2154   2907    148     93    411       C  
ATOM   5661  O   ALA B 236     -56.738   5.065 119.195  1.00 18.62           O  
ANISOU 5661  O   ALA B 236     2000   2155   2919    153     80    416       O  
ATOM   5662  CB  ALA B 236     -53.455   5.088 119.485  1.00 15.24           C  
ANISOU 5662  CB  ALA B 236     1641   1739   2412    112     88    389       C  
ATOM   5663  N   ILE B 237     -55.951   6.817 120.384  1.00 15.11           N  
ANISOU 5663  N   ILE B 237     1598   1680   2462    159    121    407       N  
ATOM   5664  CA  ILE B 237     -57.161   6.966 121.209  1.00 15.07           C  
ANISOU 5664  CA  ILE B 237     1572   1664   2490    178    145    410       C  
ATOM   5665  C   ILE B 237     -58.342   7.564 120.391  1.00 19.07           C  
ANISOU 5665  C   ILE B 237     2054   2162   3030    200    130    429       C  
ATOM   5666  O   ILE B 237     -59.497   7.204 120.628  1.00 19.07           O  
ANISOU 5666  O   ILE B 237     2021   2163   3064    213    136    436       O  
ATOM   5667  CB  ILE B 237     -56.858   7.793 122.508  1.00 18.15           C  
ANISOU 5667  CB  ILE B 237     1989   2034   2874    185    181    396       C  
ATOM   5668  CG1 ILE B 237     -55.716   7.134 123.336  1.00 18.09           C  
ANISOU 5668  CG1 ILE B 237     2005   2035   2833    164    190    377       C  
ATOM   5669  CG2 ILE B 237     -58.139   7.976 123.367  1.00 18.91           C  
ANISOU 5669  CG2 ILE B 237     2064   2119   3002    209    210    399       C  
ATOM   5670  CD1 ILE B 237     -55.173   8.005 124.469  1.00 24.04           C  
ANISOU 5670  CD1 ILE B 237     2792   2768   3572    167    216    361       C  
ATOM   5671  N   SER B 238     -58.037   8.432 119.407  1.00 15.53           N  
ANISOU 5671  N   SER B 238     1620   1706   2575    203    110    440       N  
ATOM   5672  CA  SER B 238     -59.072   9.096 118.600  1.00 15.71           C  
ANISOU 5672  CA  SER B 238     1624   1718   2627    225     93    460       C  
ATOM   5673  C   SER B 238     -59.489   8.257 117.376  1.00 19.52           C  
ANISOU 5673  C   SER B 238     2083   2221   3112    221     52    472       C  
ATOM   5674  O   SER B 238     -60.491   8.576 116.728  1.00 20.02           O  
ANISOU 5674  O   SER B 238     2124   2278   3204    238     33    488       O  
ATOM   5675  CB  SER B 238     -58.596  10.475 118.149  1.00 19.59           C  
ANISOU 5675  CB  SER B 238     2143   2189   3110    231     90    469       C  
ATOM   5676  OG  SER B 238     -58.225  11.278 119.257  1.00 30.13           O  
ANISOU 5676  OG  SER B 238     3502   3502   4443    235    123    456       O  
ATOM   5677  N   SER B 239     -58.708   7.203 117.046  1.00 15.49           N  
ANISOU 5677  N   SER B 239     1579   1732   2572    199     37    462       N  
ATOM   5678  CA  SER B 239     -58.971   6.368 115.863  1.00 15.20           C  
ANISOU 5678  CA  SER B 239     1528   1714   2532    195     -4    469       C  
ATOM   5679  C   SER B 239     -60.384   5.763 115.877  1.00 18.99           C  
ANISOU 5679  C   SER B 239     1964   2195   3056    206    -17    476       C  
ATOM   5680  O   SER B 239     -60.808   5.186 116.883  1.00 18.45           O  
ANISOU 5680  O   SER B 239     1876   2126   3010    204      7    469       O  
ATOM   5681  CB  SER B 239     -57.928   5.262 115.741  1.00 18.60           C  
ANISOU 5681  CB  SER B 239     1973   2166   2928    172    -11    453       C  
ATOM   5682  OG  SER B 239     -58.172   4.445 114.607  1.00 27.83           O  
ANISOU 5682  OG  SER B 239     3132   3352   4091    169    -51    456       O  
ATOM   5683  N   PRO B 240     -61.109   5.824 114.727  1.00 16.04           N  
ANISOU 5683  N   PRO B 240     1575   1823   2696    217    -56    491       N  
ATOM   5684  CA  PRO B 240     -62.452   5.216 114.675  1.00 16.10           C  
ANISOU 5684  CA  PRO B 240     1537   1831   2750    225    -74    498       C  
ATOM   5685  C   PRO B 240     -62.405   3.681 114.710  1.00 19.47           C  
ANISOU 5685  C   PRO B 240     1948   2274   3175    206    -90    486       C  
ATOM   5686  O   PRO B 240     -63.425   3.037 114.961  1.00 19.08           O  
ANISOU 5686  O   PRO B 240     1859   2224   3168    208    -96    490       O  
ATOM   5687  CB  PRO B 240     -63.021   5.734 113.352  1.00 18.11           C  
ANISOU 5687  CB  PRO B 240     1787   2082   3011    240   -118    517       C  
ATOM   5688  CG  PRO B 240     -61.838   6.004 112.511  1.00 22.75           C  
ANISOU 5688  CG  PRO B 240     2419   2680   3545    231   -131    515       C  
ATOM   5689  CD  PRO B 240     -60.747   6.458 113.440  1.00 17.85           C  
ANISOU 5689  CD  PRO B 240     1829   2055   2900    221    -87    503       C  
ATOM   5690  N   ALA B 241     -61.206   3.097 114.485  1.00 15.74           N  
ANISOU 5690  N   ALA B 241     1507   1817   2658    187    -94    471       N  
ATOM   5691  CA  ALA B 241     -61.014   1.645 114.513  1.00 15.60           C  
ANISOU 5691  CA  ALA B 241     1480   1812   2634    169   -109    457       C  
ATOM   5692  C   ALA B 241     -61.176   1.084 115.940  1.00 19.74           C  
ANISOU 5692  C   ALA B 241     1988   2333   3181    161    -71    450       C  
ATOM   5693  O   ALA B 241     -61.534  -0.081 116.111  1.00 19.22           O  
ANISOU 5693  O   ALA B 241     1898   2271   3132    150    -82    445       O  
ATOM   5694  CB  ALA B 241     -59.642   1.293 113.968  1.00 15.99           C  
ANISOU 5694  CB  ALA B 241     1568   1877   2630    156   -118    442       C  
ATOM   5695  N   GLY B 242     -60.906   1.922 116.940  1.00 16.24           N  
ANISOU 5695  N   GLY B 242     1557   1879   2733    167    -27    449       N  
ATOM   5696  CA  GLY B 242     -61.031   1.538 118.339  1.00 15.64           C  
ANISOU 5696  CA  GLY B 242     1471   1799   2672    162     14    444       C  
ATOM   5697  C   GLY B 242     -59.825   0.782 118.863  1.00 17.90           C  
ANISOU 5697  C   GLY B 242     1785   2096   2921    142     25    426       C  
ATOM   5698  O   GLY B 242     -58.888   0.503 118.113  1.00 16.67           O  
ANISOU 5698  O   GLY B 242     1651   1951   2731    131      2    417       O  
ATOM   5699  N   LEU B 243     -59.839   0.450 120.162  1.00 14.01           N  
ANISOU 5699  N   LEU B 243     1289   1601   2434    138     61    422       N  
ATOM   5700  CA  LEU B 243     -58.752  -0.297 120.802  1.00 13.64           C  
ANISOU 5700  CA  LEU B 243     1266   1562   2355    119     72    406       C  
ATOM   5701  C   LEU B 243     -59.296  -1.606 121.376  1.00 16.58           C  
ANISOU 5701  C   LEU B 243     1611   1938   2751    109     75    408       C  
ATOM   5702  O   LEU B 243     -60.508  -1.851 121.314  1.00 16.02           O  
ANISOU 5702  O   LEU B 243     1502   1862   2722    116     71    422       O  
ATOM   5703  CB  LEU B 243     -58.128   0.551 121.942  1.00 13.90           C  
ANISOU 5703  CB  LEU B 243     1328   1585   2366    123    113    398       C  
ATOM   5704  CG  LEU B 243     -57.558   1.915 121.536  1.00 18.88           C  
ANISOU 5704  CG  LEU B 243     1986   2208   2978    132    114    397       C  
ATOM   5705  CD1 LEU B 243     -57.577   2.878 122.701  1.00 19.01           C  
ANISOU 5705  CD1 LEU B 243     2021   2209   2994    144    154    393       C  
ATOM   5706  CD2 LEU B 243     -56.160   1.780 120.986  1.00 21.84           C  
ANISOU 5706  CD2 LEU B 243     2391   2593   3314    116     96    386       C  
ATOM   5707  N   ILE B 244     -58.415  -2.437 121.969  1.00 11.67           N  
ANISOU 5707  N   ILE B 244     1007   1323   2105     93     82    396       N  
ATOM   5708  CA  ILE B 244     -58.861  -3.590 122.745  1.00 11.13           C  
ANISOU 5708  CA  ILE B 244      917   1254   2056     83     93    400       C  
ATOM   5709  C   ILE B 244     -59.515  -3.052 124.042  1.00 15.59           C  
ANISOU 5709  C   ILE B 244     1476   1810   2637     95    142    410       C  
ATOM   5710  O   ILE B 244     -58.809  -2.710 124.999  1.00 13.71           O  
ANISOU 5710  O   ILE B 244     1268   1570   2370     95    171    401       O  
ATOM   5711  CB  ILE B 244     -57.677  -4.579 123.019  1.00 13.11           C  
ANISOU 5711  CB  ILE B 244     1192   1513   2275     64     85    385       C  
ATOM   5712  CG1 ILE B 244     -57.119  -5.143 121.685  1.00 12.94           C  
ANISOU 5712  CG1 ILE B 244     1176   1500   2239     56     39    374       C  
ATOM   5713  CG2 ILE B 244     -58.110  -5.717 123.965  1.00 13.44           C  
ANISOU 5713  CG2 ILE B 244     1216   1552   2337     54    100    392       C  
ATOM   5714  CD1 ILE B 244     -55.835  -5.937 121.819  1.00 19.06           C  
ANISOU 5714  CD1 ILE B 244     1977   2284   2981     41     32    358       C  
ATOM   5715  N   SER B 245     -60.858  -2.842 124.002  1.00 14.42           N  
ANISOU 5715  N   SER B 245     1289   1655   2534    108    149    427       N  
ATOM   5716  CA ASER B 245     -61.576  -2.200 125.105  0.50 14.94           C  
ANISOU 5716  CA ASER B 245     1346   1713   2616    125    198    437       C  
ATOM   5717  CA BSER B 245     -61.590  -2.194 125.093  0.50 14.92           C  
ANISOU 5717  CA BSER B 245     1344   1711   2615    125    198    437       C  
ATOM   5718  C   SER B 245     -62.326  -3.200 125.986  1.00 19.59           C  
ANISOU 5718  C   SER B 245     1907   2303   3235    119    222    452       C  
ATOM   5719  O   SER B 245     -62.801  -2.831 127.064  1.00 19.70           O  
ANISOU 5719  O   SER B 245     1918   2312   3255    132    270    459       O  
ATOM   5720  CB ASER B 245     -62.528  -1.133 124.576  0.50 19.15           C  
ANISOU 5720  CB ASER B 245     1857   2237   3181    148    198    449       C  
ATOM   5721  CB BSER B 245     -62.567  -1.158 124.540  0.50 19.07           C  
ANISOU 5721  CB BSER B 245     1846   2228   3173    147    196    449       C  
ATOM   5722  OG ASER B 245     -61.814  -0.072 123.963  0.50 28.10           O  
ANISOU 5722  OG ASER B 245     3023   3368   4286    155    184    438       O  
ATOM   5723  OG BSER B 245     -63.449  -1.735 123.591  0.50 28.08           O  
ANISOU 5723  OG BSER B 245     2944   3370   4356    144    160    462       O  
ATOM   5724  N   ASP B 246     -62.420  -4.471 125.548  1.00 17.16           N  
ANISOU 5724  N   ASP B 246     1577   1999   2944     99    192    456       N  
ATOM   5725  CA  ASP B 246     -63.052  -5.519 126.366  1.00 17.60           C  
ANISOU 5725  CA  ASP B 246     1606   2054   3029     90    213    472       C  
ATOM   5726  C   ASP B 246     -62.396  -6.886 126.133  1.00 20.90           C  
ANISOU 5726  C   ASP B 246     2029   2475   3435     64    181    465       C  
ATOM   5727  O   ASP B 246     -61.625  -7.045 125.184  1.00 19.64           O  
ANISOU 5727  O   ASP B 246     1888   2320   3254     56    140    448       O  
ATOM   5728  CB  ASP B 246     -64.587  -5.580 126.131  1.00 20.42           C  
ANISOU 5728  CB  ASP B 246     1904   2405   3451     97    214    496       C  
ATOM   5729  CG  ASP B 246     -65.003  -6.273 124.842  1.00 34.70           C  
ANISOU 5729  CG  ASP B 246     3681   4212   5293     85    155    498       C  
ATOM   5730  OD1 ASP B 246     -64.306  -6.097 123.824  1.00 35.46           O  
ANISOU 5730  OD1 ASP B 246     3800   4312   5361     82    114    481       O  
ATOM   5731  OD2 ASP B 246     -66.077  -6.909 124.833  1.00 42.98           O  
ANISOU 5731  OD2 ASP B 246     4681   5255   6395     79    151    518       O  
ATOM   5732  N   LYS B 247     -62.702  -7.875 127.008  1.00 18.17           N  
ANISOU 5732  N   LYS B 247     1669   2128   3107     52    202    478       N  
ATOM   5733  CA  LYS B 247     -62.097  -9.224 126.952  1.00 17.28           C  
ANISOU 5733  CA  LYS B 247     1564   2015   2987     29    176    473       C  
ATOM   5734  C   LYS B 247     -62.327  -9.934 125.606  1.00 20.12           C  
ANISOU 5734  C   LYS B 247     1900   2372   3374     17    116    469       C  
ATOM   5735  O   LYS B 247     -61.537 -10.795 125.226  1.00 20.01           O  
ANISOU 5735  O   LYS B 247     1903   2358   3341      2     85    454       O  
ATOM   5736  CB  LYS B 247     -62.596 -10.096 128.125  1.00 20.03           C  
ANISOU 5736  CB  LYS B 247     1896   2360   3357     20    211    495       C  
ATOM   5737  CG  LYS B 247     -64.122 -10.187 128.222  1.00 32.10           C  
ANISOU 5737  CG  LYS B 247     3366   3880   4948     24    228    524       C  
ATOM   5738  CD  LYS B 247     -64.558 -10.898 129.489  1.00 41.87           C  
ANISOU 5738  CD  LYS B 247     4592   5115   6201     17    274    548       C  
ATOM   5739  CE  LYS B 247     -66.057 -10.912 129.639  1.00 52.44           C  
ANISOU 5739  CE  LYS B 247     5871   6448   7605     22    297    579       C  
ATOM   5740  NZ  LYS B 247     -66.474 -11.528 130.924  1.00 63.99           N  
ANISOU 5740  NZ  LYS B 247     7324   7911   9080     17    349    606       N  
ATOM   5741  N   ALA B 248     -63.396  -9.563 124.885  1.00 16.59           N  
ANISOU 5741  N   ALA B 248     1414   1920   2969     25    100    480       N  
ATOM   5742  CA  ALA B 248     -63.709 -10.170 123.586  1.00 16.04           C  
ANISOU 5742  CA  ALA B 248     1323   1846   2925     15     40    475       C  
ATOM   5743  C   ALA B 248     -62.684  -9.754 122.503  1.00 18.30           C  
ANISOU 5743  C   ALA B 248     1647   2141   3164     20      3    449       C  
ATOM   5744  O   ALA B 248     -62.540 -10.446 121.493  1.00 18.17           O  
ANISOU 5744  O   ALA B 248     1630   2124   3150     11    -48    437       O  
ATOM   5745  CB  ALA B 248     -65.115  -9.780 123.154  1.00 16.98           C  
ANISOU 5745  CB  ALA B 248     1391   1959   3101     25     31    494       C  
ATOM   5746  N   ASP B 249     -61.969  -8.638 122.729  1.00 13.59           N  
ANISOU 5746  N   ASP B 249     1085   1552   2525     33     28    440       N  
ATOM   5747  CA  ASP B 249     -60.992  -8.117 121.763  1.00 12.64           C  
ANISOU 5747  CA  ASP B 249     1001   1440   2361     38      1    419       C  
ATOM   5748  C   ASP B 249     -59.565  -8.613 122.062  1.00 16.39           C  
ANISOU 5748  C   ASP B 249     1517   1923   2789     27      3    400       C  
ATOM   5749  O   ASP B 249     -58.662  -8.414 121.241  1.00 16.37           O  
ANISOU 5749  O   ASP B 249     1541   1928   2751     28    -20    383       O  
ATOM   5750  CB  ASP B 249     -61.023  -6.574 121.745  1.00 13.92           C  
ANISOU 5750  CB  ASP B 249     1175   1604   2509     58     23    422       C  
ATOM   5751  CG  ASP B 249     -62.382  -5.988 121.421  1.00 21.69           C  
ANISOU 5751  CG  ASP B 249     2119   2580   3540     73     20    440       C  
ATOM   5752  OD1 ASP B 249     -63.151  -6.644 120.684  1.00 23.06           O  
ANISOU 5752  OD1 ASP B 249     2260   2751   3750     67    -17    447       O  
ATOM   5753  OD2 ASP B 249     -62.645  -4.839 121.837  1.00 24.73           O  
ANISOU 5753  OD2 ASP B 249     2507   2963   3926     90     52    447       O  
ATOM   5754  N   ASN B 250     -59.354  -9.229 123.252  1.00 12.43           N  
ANISOU 5754  N   ASN B 250     1019   1418   2286     18     33    404       N  
ATOM   5755  CA  ASN B 250     -58.018  -9.684 123.691  1.00 11.62           C  
ANISOU 5755  CA  ASN B 250      953   1321   2141      8     37    388       C  
ATOM   5756  C   ASN B 250     -57.310 -10.534 122.634  1.00 15.02           C  
ANISOU 5756  C   ASN B 250     1394   1756   2557     -1    -10    370       C  
ATOM   5757  O   ASN B 250     -57.930 -11.407 122.021  1.00 14.60           O  
ANISOU 5757  O   ASN B 250     1316   1696   2534     -8    -43    372       O  
ATOM   5758  CB  ASN B 250     -58.110 -10.450 125.013  1.00 10.77           C  
ANISOU 5758  CB  ASN B 250      843   1208   2042     -1     67    399       C  
ATOM   5759  CG  ASN B 250     -58.445  -9.588 126.202  1.00 20.07           C  
ANISOU 5759  CG  ASN B 250     2026   2385   3216     10    119    411       C  
ATOM   5760  OD1 ASN B 250     -58.535  -8.360 126.109  1.00 14.12           O  
ANISOU 5760  OD1 ASN B 250     1279   1633   2452     26    134    409       O  
ATOM   5761  ND2 ASN B 250     -58.576 -10.211 127.363  1.00  7.48           N  
ANISOU 5761  ND2 ASN B 250      431    787   1625      4    148    423       N  
ATOM   5762  N   ALA B 251     -55.998 -10.295 122.439  1.00 10.13           N  
ANISOU 5762  N   ALA B 251      810   1146   1893      0    -13    352       N  
ATOM   5763  CA  ALA B 251     -55.211 -11.047 121.476  1.00  8.95           C  
ANISOU 5763  CA  ALA B 251      674   1002   1725     -6    -51    333       C  
ATOM   5764  C   ALA B 251     -54.524 -12.237 122.149  1.00 11.05           C  
ANISOU 5764  C   ALA B 251      950   1265   1985    -19    -51    326       C  
ATOM   5765  O   ALA B 251     -53.778 -12.057 123.120  1.00  8.80           O  
ANISOU 5765  O   ALA B 251      685    982   1677    -21    -23    325       O  
ATOM   5766  CB  ALA B 251     -54.179 -10.142 120.821  1.00  9.19           C  
ANISOU 5766  CB  ALA B 251      733   1045   1713      3    -53    320       C  
ATOM   5767  N   TYR B 252     -54.825 -13.457 121.678  1.00  7.81           N  
ANISOU 5767  N   TYR B 252      525    846   1597    -27    -84    322       N  
ATOM   5768  CA  TYR B 252     -54.216 -14.671 122.206  1.00  7.72           C  
ANISOU 5768  CA  TYR B 252      521    828   1583    -39    -89    316       C  
ATOM   5769  C   TYR B 252     -53.537 -15.455 121.088  1.00 11.27           C  
ANISOU 5769  C   TYR B 252      983   1280   2019    -38   -131    293       C  
ATOM   5770  O   TYR B 252     -53.976 -15.393 119.933  1.00 11.60           O  
ANISOU 5770  O   TYR B 252     1017   1323   2067    -33   -162    286       O  
ATOM   5771  CB  TYR B 252     -55.277 -15.568 122.883  1.00  8.84           C  
ANISOU 5771  CB  TYR B 252      633    953   1771    -51    -87    336       C  
ATOM   5772  CG  TYR B 252     -56.098 -14.878 123.947  1.00 10.74           C  
ANISOU 5772  CG  TYR B 252      859   1192   2029    -49    -43    361       C  
ATOM   5773  CD1 TYR B 252     -55.596 -14.697 125.233  1.00 12.69           C  
ANISOU 5773  CD1 TYR B 252     1125   1441   2256    -50     -3    368       C  
ATOM   5774  CD2 TYR B 252     -57.433 -14.560 123.723  1.00 11.88           C  
ANISOU 5774  CD2 TYR B 252      968   1331   2215    -47    -42    378       C  
ATOM   5775  CE1 TYR B 252     -56.376 -14.137 126.243  1.00 12.88           C  
ANISOU 5775  CE1 TYR B 252     1137   1463   2293    -46     39    389       C  
ATOM   5776  CE2 TYR B 252     -58.227 -14.015 124.730  1.00 13.06           C  
ANISOU 5776  CE2 TYR B 252     1101   1478   2383    -43      2    401       C  
ATOM   5777  CZ  TYR B 252     -57.692 -13.801 125.988  1.00 19.72           C  
ANISOU 5777  CZ  TYR B 252     1967   2324   3200    -42     44    406       C  
ATOM   5778  OH  TYR B 252     -58.469 -13.249 126.978  1.00 21.78           O  
ANISOU 5778  OH  TYR B 252     2217   2585   3475    -35     89    428       O  
HETATM 5779  N   MSE B 253     -52.537 -16.269 121.440  1.00  7.09           N  
ANISOU 5779  N   MSE B 253      472    750   1473    -44   -134    281       N  
HETATM 5780  CA  MSE B 253     -51.950 -17.214 120.500  1.00  6.77           C  
ANISOU 5780  CA  MSE B 253      475    690   1408    -43   -164    258       C  
HETATM 5781  C   MSE B 253     -52.084 -18.640 121.049  1.00 13.67           C  
ANISOU 5781  C   MSE B 253     1306   1562   2325    -55   -186    260       C  
HETATM 5782  O   MSE B 253     -51.385 -19.011 122.000  1.00 12.73           O  
ANISOU 5782  O   MSE B 253     1199   1440   2196    -60   -168    263       O  
HETATM 5783  CB  MSE B 253     -50.483 -16.875 120.215  1.00  7.57           C  
ANISOU 5783  CB  MSE B 253      572    826   1479    -33   -167    240       C  
HETATM 5784  CG  MSE B 253     -49.843 -17.791 119.149  1.00 13.46           C  
ANISOU 5784  CG  MSE B 253     1330   1573   2213    -27   -203    214       C  
HETATM 5785 SE   MSE B 253     -50.657 -17.596 117.384  0.75 20.04          SE  
ANISOU 5785 SE   MSE B 253     2158   2410   3047    -16   -244    203      SE  
HETATM 5786  CE  MSE B 253     -49.994 -15.877 116.950  1.00 16.56           C  
ANISOU 5786  CE  MSE B 253     1735   1996   2563     -2   -215    206       C  
ATOM   5787  N   PRO B 254     -53.071 -19.420 120.552  1.00 12.66           N  
ANISOU 5787  N   PRO B 254     1156   1417   2235    -62   -218    263       N  
ATOM   5788  CA  PRO B 254     -53.254 -20.773 121.087  1.00 13.29           C  
ANISOU 5788  CA  PRO B 254     1227   1476   2347    -76   -232    267       C  
ATOM   5789  C   PRO B 254     -52.153 -21.728 120.624  1.00 18.07           C  
ANISOU 5789  C   PRO B 254     1856   2077   2932    -72   -259    241       C  
ATOM   5790  O   PRO B 254     -51.741 -21.694 119.459  1.00 17.74           O  
ANISOU 5790  O   PRO B 254     1828   2044   2869    -60   -286    216       O  
ATOM   5791  CB  PRO B 254     -54.628 -21.183 120.550  1.00 15.23           C  
ANISOU 5791  CB  PRO B 254     1440   1704   2641    -84   -262    276       C  
ATOM   5792  CG  PRO B 254     -54.778 -20.425 119.282  1.00 19.28           C  
ANISOU 5792  CG  PRO B 254     1958   2231   3138    -70   -284    261       C  
ATOM   5793  CD  PRO B 254     -54.029 -19.124 119.458  1.00 14.64           C  
ANISOU 5793  CD  PRO B 254     1391   1668   2505    -57   -247    261       C  
ATOM   5794  N   PRO B 255     -51.622 -22.571 121.533  1.00 15.08           N  
ANISOU 5794  N   PRO B 255     1485   1687   2559    -80   -251    245       N  
ATOM   5795  CA  PRO B 255     -50.634 -23.561 121.099  1.00 15.24           C  
ANISOU 5795  CA  PRO B 255     1525   1700   2565    -74   -279    220       C  
ATOM   5796  C   PRO B 255     -51.304 -24.731 120.379  1.00 20.20           C  
ANISOU 5796  C   PRO B 255     2141   2303   3231    -81   -325    209       C  
ATOM   5797  O   PRO B 255     -52.527 -24.892 120.475  1.00 20.31           O  
ANISOU 5797  O   PRO B 255     2128   2302   3286    -94   -334    228       O  
ATOM   5798  CB  PRO B 255     -49.985 -23.999 122.404  1.00 16.83           C  
ANISOU 5798  CB  PRO B 255     1735   1895   2763    -81   -255    233       C  
ATOM   5799  CG  PRO B 255     -51.059 -23.861 123.426  1.00 21.14           C  
ANISOU 5799  CG  PRO B 255     2260   2432   3340    -96   -229    267       C  
ATOM   5800  CD  PRO B 255     -51.999 -22.759 122.951  1.00 16.67           C  
ANISOU 5800  CD  PRO B 255     1676   1878   2780    -93   -220    274       C  
ATOM   5801  N   LYS B 256     -50.516 -25.546 119.644  1.00 17.15           N  
ANISOU 5801  N   LYS B 256     1775   1912   2831    -71   -357    180       N  
ATOM   5802  CA  LYS B 256     -51.060 -26.720 118.947  1.00 17.46           C  
ANISOU 5802  CA  LYS B 256     1807   1923   2903    -75   -406    165       C  
ATOM   5803  C   LYS B 256     -51.723 -27.678 119.927  1.00 21.55           C  
ANISOU 5803  C   LYS B 256     2306   2410   3472    -98   -408    190       C  
ATOM   5804  O   LYS B 256     -52.851 -28.120 119.687  1.00 22.25           O  
ANISOU 5804  O   LYS B 256     2370   2477   3605   -111   -434    199       O  
ATOM   5805  CB  LYS B 256     -49.962 -27.450 118.162  1.00 20.14           C  
ANISOU 5805  CB  LYS B 256     2175   2261   3216    -58   -433    128       C  
ATOM   5806  CG  LYS B 256     -49.620 -26.806 116.835  1.00 29.72           C  
ANISOU 5806  CG  LYS B 256     3405   3498   4389    -37   -445    101       C  
ATOM   5807  CD  LYS B 256     -48.635 -27.660 116.056  1.00 36.06           C  
ANISOU 5807  CD  LYS B 256     4235   4296   5170    -18   -471     65       C  
ATOM   5808  CE  LYS B 256     -48.352 -27.102 114.692  1.00 41.21           C  
ANISOU 5808  CE  LYS B 256     4906   4971   5780      4   -483     39       C  
ATOM   5809  NZ  LYS B 256     -47.374 -27.940 113.952  1.00 44.77           N  
ANISOU 5809  NZ  LYS B 256     5384   5420   6207     25   -504      2       N  
ATOM   5810  N   ALA B 257     -51.018 -28.000 121.062  1.00 16.72           N  
ANISOU 5810  N   ALA B 257     1703   1796   2854   -102   -381    203       N  
ATOM   5811  CA  ALA B 257     -51.506 -28.961 122.072  1.00 16.04           C  
ANISOU 5811  CA  ALA B 257     1603   1680   2811   -122   -380    230       C  
ATOM   5812  C   ALA B 257     -52.011 -30.258 121.405  1.00 20.11           C  
ANISOU 5812  C   ALA B 257     2111   2160   3370   -130   -433    216       C  
ATOM   5813  O   ALA B 257     -53.076 -30.775 121.767  1.00 20.12           O  
ANISOU 5813  O   ALA B 257     2086   2137   3423   -151   -441    241       O  
ATOM   5814  CB  ALA B 257     -52.612 -28.327 122.918  1.00 16.57           C  
ANISOU 5814  CB  ALA B 257     1643   1750   2904   -137   -346    269       C  
ATOM   5815  N   ASP B 258     -51.245 -30.771 120.411  1.00 16.63           N  
ANISOU 5815  N   ASP B 258     1694   1717   2910   -114   -468    177       N  
ATOM   5816  CA  ASP B 258     -51.641 -31.954 119.635  1.00 16.63           C  
ANISOU 5816  CA  ASP B 258     1693   1683   2945   -118   -524    157       C  
ATOM   5817  C   ASP B 258     -50.705 -33.159 119.900  1.00 19.24           C  
ANISOU 5817  C   ASP B 258     2043   1989   3277   -113   -540    142       C  
ATOM   5818  O   ASP B 258     -50.773 -34.165 119.188  1.00 18.76           O  
ANISOU 5818  O   ASP B 258     1991   1900   3238   -111   -587    117       O  
ATOM   5819  CB  ASP B 258     -51.683 -31.619 118.120  1.00 18.57           C  
ANISOU 5819  CB  ASP B 258     1950   1940   3167   -100   -557    120       C  
ATOM   5820  CG  ASP B 258     -50.333 -31.214 117.534  1.00 27.08           C  
ANISOU 5820  CG  ASP B 258     3060   3046   4182    -71   -547     88       C  
ATOM   5821  OD1 ASP B 258     -49.431 -30.831 118.320  1.00 27.91           O  
ANISOU 5821  OD1 ASP B 258     3174   3170   4261    -66   -507     98       O  
ATOM   5822  OD2 ASP B 258     -50.203 -31.214 116.293  1.00 31.21           O  
ANISOU 5822  OD2 ASP B 258     3599   3575   4683    -53   -577     55       O  
ATOM   5823  N   GLY B 259     -49.855 -33.039 120.918  1.00 15.00           N  
ANISOU 5823  N   GLY B 259     1517   1463   2719   -110   -503    157       N  
ATOM   5824  CA  GLY B 259     -48.913 -34.091 121.279  1.00 14.54           C  
ANISOU 5824  CA  GLY B 259     1478   1384   2662   -104   -515    147       C  
ATOM   5825  C   GLY B 259     -47.514 -33.860 120.735  1.00 17.17           C  
ANISOU 5825  C   GLY B 259     1839   1741   2944    -75   -512    113       C  
ATOM   5826  O   GLY B 259     -46.566 -34.543 121.141  1.00 15.64           O  
ANISOU 5826  O   GLY B 259     1660   1536   2745    -66   -514    106       O  
ATOM   5827  N   SER B 260     -47.372 -32.901 119.786  1.00 13.38           N  
ANISOU 5827  N   SER B 260     1364   1292   2427    -59   -507     92       N  
ATOM   5828  CA  SER B 260     -46.068 -32.563 119.208  1.00 13.17           C  
ANISOU 5828  CA  SER B 260     1361   1291   2352    -31   -498     62       C  
ATOM   5829  C   SER B 260     -45.158 -31.946 120.263  1.00 16.31           C  
ANISOU 5829  C   SER B 260     1761   1711   2724    -30   -455     81       C  
ATOM   5830  O   SER B 260     -45.630 -31.201 121.127  1.00 14.74           O  
ANISOU 5830  O   SER B 260     1550   1524   2528    -46   -424    113       O  
ATOM   5831  CB  SER B 260     -46.235 -31.602 118.035  1.00 17.83           C  
ANISOU 5831  CB  SER B 260     1955   1910   2909    -18   -499     43       C  
ATOM   5832  OG  SER B 260     -47.015 -32.182 117.004  1.00 31.13           O  
ANISOU 5832  OG  SER B 260     3640   3574   4613    -17   -544     22       O  
ATOM   5833  N   TRP B 261     -43.857 -32.278 120.217  1.00 13.45           N  
ANISOU 5833  N   TRP B 261     1416   1354   2339    -10   -453     61       N  
ATOM   5834  CA  TRP B 261     -42.885 -31.772 121.183  1.00 12.98           C  
ANISOU 5834  CA  TRP B 261     1361   1315   2258     -8   -419     76       C  
ATOM   5835  C   TRP B 261     -42.780 -30.247 121.117  1.00 16.02           C  
ANISOU 5835  C   TRP B 261     1741   1737   2607     -7   -384     84       C  
ATOM   5836  O   TRP B 261     -42.619 -29.675 120.028  1.00 15.54           O  
ANISOU 5836  O   TRP B 261     1685   1697   2521      8   -385     62       O  
ATOM   5837  CB  TRP B 261     -41.503 -32.415 120.945  1.00 12.07           C  
ANISOU 5837  CB  TRP B 261     1259   1198   2127     16   -429     50       C  
ATOM   5838  CG  TRP B 261     -40.505 -32.129 122.034  1.00 12.73           C  
ANISOU 5838  CG  TRP B 261     1346   1294   2198     16   -403     66       C  
ATOM   5839  CD1 TRP B 261     -40.190 -32.933 123.087  1.00 15.62           C  
ANISOU 5839  CD1 TRP B 261     1715   1637   2584     10   -408     82       C  
ATOM   5840  CD2 TRP B 261     -39.734 -30.925 122.201  1.00 12.21           C  
ANISOU 5840  CD2 TRP B 261     1279   1264   2096     22   -370     69       C  
ATOM   5841  NE1 TRP B 261     -39.251 -32.319 123.888  1.00 14.70           N  
ANISOU 5841  NE1 TRP B 261     1601   1541   2444     13   -383     94       N  
ATOM   5842  CE2 TRP B 261     -38.958 -31.083 123.368  1.00 15.87           C  
ANISOU 5842  CE2 TRP B 261     1746   1725   2560     19   -360     86       C  
ATOM   5843  CE3 TRP B 261     -39.617 -29.729 121.467  1.00 13.12           C  
ANISOU 5843  CE3 TRP B 261     1393   1412   2180     29   -350     61       C  
ATOM   5844  CZ2 TRP B 261     -38.077 -30.094 123.821  1.00 14.87           C  
ANISOU 5844  CZ2 TRP B 261     1620   1626   2405     23   -333     92       C  
ATOM   5845  CZ3 TRP B 261     -38.786 -28.729 121.950  1.00 14.16           C  
ANISOU 5845  CZ3 TRP B 261     1524   1570   2286     31   -320     70       C  
ATOM   5846  CH2 TRP B 261     -38.012 -28.925 123.100  1.00 14.66           C  
ANISOU 5846  CH2 TRP B 261     1590   1629   2352     27   -313     84       C  
ATOM   5847  N   GLY B 262     -42.861 -29.604 122.283  1.00 11.64           N  
ANISOU 5847  N   GLY B 262     1182   1192   2050    -21   -353    114       N  
ATOM   5848  CA  GLY B 262     -42.700 -28.157 122.406  1.00 10.88           C  
ANISOU 5848  CA  GLY B 262     1084   1127   1923    -20   -319    123       C  
ATOM   5849  C   GLY B 262     -43.771 -27.342 121.704  1.00 14.54           C  
ANISOU 5849  C   GLY B 262     1537   1601   2386    -25   -316    126       C  
ATOM   5850  O   GLY B 262     -43.543 -26.179 121.374  1.00 13.54           O  
ANISOU 5850  O   GLY B 262     1412   1501   2232    -19   -295    124       O  
ATOM   5851  N   GLN B 263     -44.968 -27.931 121.503  1.00 11.39           N  
ANISOU 5851  N   GLN B 263     1127   1180   2022    -37   -338    132       N  
ATOM   5852  CA  GLN B 263     -46.077 -27.215 120.856  1.00 10.92           C  
ANISOU 5852  CA  GLN B 263     1054   1128   1968    -41   -339    137       C  
ATOM   5853  C   GLN B 263     -47.260 -27.004 121.814  1.00 14.75           C  
ANISOU 5853  C   GLN B 263     1518   1601   2484    -63   -322    172       C  
ATOM   5854  O   GLN B 263     -48.383 -26.762 121.369  1.00 14.59           O  
ANISOU 5854  O   GLN B 263     1481   1577   2484    -70   -331    179       O  
ATOM   5855  CB  GLN B 263     -46.524 -27.935 119.567  1.00 11.79           C  
ANISOU 5855  CB  GLN B 263     1166   1224   2092    -34   -383    111       C  
ATOM   5856  CG  GLN B 263     -45.481 -27.867 118.437  1.00 17.05           C  
ANISOU 5856  CG  GLN B 263     1852   1908   2719     -9   -393     76       C  
ATOM   5857  CD  GLN B 263     -45.213 -26.438 117.978  1.00 22.64           C  
ANISOU 5857  CD  GLN B 263     2563   2650   3388      0   -365     77       C  
ATOM   5858  OE1 GLN B 263     -46.128 -25.629 117.807  1.00 17.26           O  
ANISOU 5858  OE1 GLN B 263     1870   1976   2710     -7   -359     91       O  
ATOM   5859  NE2 GLN B 263     -43.959 -26.137 117.685  1.00 10.44           N  
ANISOU 5859  NE2 GLN B 263     1033   1127   1808     18   -350     61       N  
ATOM   5860  N   ASP B 264     -46.987 -27.020 123.128  1.00 11.03           N  
ANISOU 5860  N   ASP B 264     1050   1128   2014    -72   -296    195       N  
ATOM   5861  CA  ASP B 264     -48.000 -26.742 124.153  1.00 10.84           C  
ANISOU 5861  CA  ASP B 264     1010   1098   2012    -89   -271    230       C  
ATOM   5862  C   ASP B 264     -47.754 -25.355 124.739  1.00 14.62           C  
ANISOU 5862  C   ASP B 264     1494   1602   2457    -85   -229    242       C  
ATOM   5863  O   ASP B 264     -46.886 -24.627 124.247  1.00 14.71           O  
ANISOU 5863  O   ASP B 264     1519   1636   2435    -72   -224    223       O  
ATOM   5864  CB  ASP B 264     -47.921 -27.800 125.283  1.00 12.58           C  
ANISOU 5864  CB  ASP B 264     1233   1294   2254   -101   -270    251       C  
ATOM   5865  CG  ASP B 264     -48.065 -29.231 124.810  1.00 17.34           C  
ANISOU 5865  CG  ASP B 264     1832   1865   2891   -105   -312    240       C  
ATOM   5866  OD1 ASP B 264     -48.848 -29.467 123.880  1.00 18.85           O  
ANISOU 5866  OD1 ASP B 264     2010   2046   3107   -108   -339    229       O  
ATOM   5867  OD2 ASP B 264     -47.475 -30.123 125.446  1.00 20.56           O  
ANISOU 5867  OD2 ASP B 264     2251   2256   3305   -107   -318    244       O  
ATOM   5868  N   TYR B 265     -48.482 -24.994 125.825  1.00 10.96           N  
ANISOU 5868  N   TYR B 265     1021   1137   2005    -97   -199    273       N  
ATOM   5869  CA  TYR B 265     -48.111 -23.843 126.624  1.00  9.96           C  
ANISOU 5869  CA  TYR B 265      907   1030   1846    -93   -160    282       C  
ATOM   5870  C   TYR B 265     -46.870 -24.241 127.393  1.00 14.00           C  
ANISOU 5870  C   TYR B 265     1443   1543   2335    -90   -158    279       C  
ATOM   5871  O   TYR B 265     -46.963 -24.980 128.378  1.00 14.34           O  
ANISOU 5871  O   TYR B 265     1489   1570   2390    -99   -153    298       O  
ATOM   5872  CB  TYR B 265     -49.249 -23.438 127.572  1.00 10.89           C  
ANISOU 5872  CB  TYR B 265     1011   1145   1981   -103   -128    315       C  
ATOM   5873  CG  TYR B 265     -48.971 -22.149 128.316  1.00 11.76           C  
ANISOU 5873  CG  TYR B 265     1136   1276   2058    -97    -89    322       C  
ATOM   5874  CD1 TYR B 265     -49.009 -20.920 127.661  1.00 13.20           C  
ANISOU 5874  CD1 TYR B 265     1317   1476   2223    -88    -81    310       C  
ATOM   5875  CD2 TYR B 265     -48.667 -22.156 129.673  1.00 12.02           C  
ANISOU 5875  CD2 TYR B 265     1185   1306   2074   -100    -63    339       C  
ATOM   5876  CE1 TYR B 265     -48.715 -19.734 128.332  1.00 13.00           C  
ANISOU 5876  CE1 TYR B 265     1306   1465   2167    -82    -49    314       C  
ATOM   5877  CE2 TYR B 265     -48.403 -20.973 130.362  1.00 12.45           C  
ANISOU 5877  CE2 TYR B 265     1257   1377   2096    -94    -32    342       C  
ATOM   5878  CZ  TYR B 265     -48.420 -19.764 129.686  1.00 16.22           C  
ANISOU 5878  CZ  TYR B 265     1733   1871   2560    -85    -25    329       C  
ATOM   5879  OH  TYR B 265     -48.145 -18.600 130.358  1.00 15.00           O  
ANISOU 5879  OH  TYR B 265     1596   1729   2376    -79      4    330       O  
ATOM   5880  N   ASN B 266     -45.700 -23.969 126.796  1.00  9.65           N  
ANISOU 5880  N   ASN B 266      905   1006   1756    -77   -169    253       N  
ATOM   5881  CA  ASN B 266     -44.450 -24.650 127.102  1.00  9.21           C  
ANISOU 5881  CA  ASN B 266      865    946   1687    -72   -182    242       C  
ATOM   5882  C   ASN B 266     -43.924 -24.550 128.529  1.00 12.47           C  
ANISOU 5882  C   ASN B 266     1294   1359   2084    -76   -162    260       C  
ATOM   5883  O   ASN B 266     -43.110 -25.388 128.922  1.00 11.40           O  
ANISOU 5883  O   ASN B 266     1170   1214   1948    -74   -177    257       O  
ATOM   5884  CB  ASN B 266     -43.383 -24.337 126.067  1.00  8.11           C  
ANISOU 5884  CB  ASN B 266      732    824   1525    -56   -194    212       C  
ATOM   5885  CG  ASN B 266     -43.687 -24.965 124.727  1.00 23.71           C  
ANISOU 5885  CG  ASN B 266     2699   2793   3516    -50   -224    191       C  
ATOM   5886  OD1 ASN B 266     -44.017 -26.154 124.633  1.00 15.85           O  
ANISOU 5886  OD1 ASN B 266     1700   1775   2548    -53   -249    190       O  
ATOM   5887  ND2 ASN B 266     -43.695 -24.161 123.680  1.00 16.16           N  
ANISOU 5887  ND2 ASN B 266     1741   1856   2544    -41   -223    177       N  
ATOM   5888  N   TYR B 267     -44.471 -23.621 129.356  1.00  9.68           N  
ANISOU 5888  N   TYR B 267      943   1014   1719    -81   -129    280       N  
ATOM   5889  CA  TYR B 267     -44.119 -23.589 130.789  1.00  9.53           C  
ANISOU 5889  CA  TYR B 267      945    994   1684    -85   -111    298       C  
ATOM   5890  C   TYR B 267     -44.443 -24.941 131.445  1.00 12.78           C  
ANISOU 5890  C   TYR B 267     1356   1381   2119    -94   -122    318       C  
ATOM   5891  O   TYR B 267     -43.769 -25.342 132.398  1.00 13.00           O  
ANISOU 5891  O   TYR B 267     1403   1404   2134    -94   -122    327       O  
ATOM   5892  CB  TYR B 267     -44.861 -22.455 131.524  1.00 10.65           C  
ANISOU 5892  CB  TYR B 267     1090   1145   1811    -88    -74    316       C  
ATOM   5893  CG  TYR B 267     -44.291 -21.076 131.273  1.00 11.85           C  
ANISOU 5893  CG  TYR B 267     1250   1319   1934    -80    -62    300       C  
ATOM   5894  CD1 TYR B 267     -43.014 -20.737 131.718  1.00 13.65           C  
ANISOU 5894  CD1 TYR B 267     1499   1555   2133    -75    -66    289       C  
ATOM   5895  CD2 TYR B 267     -45.085 -20.060 130.753  1.00 13.00           C  
ANISOU 5895  CD2 TYR B 267     1383   1473   2081    -78    -45    300       C  
ATOM   5896  CE1 TYR B 267     -42.507 -19.450 131.551  1.00 13.81           C  
ANISOU 5896  CE1 TYR B 267     1526   1591   2129    -70    -55    277       C  
ATOM   5897  CE2 TYR B 267     -44.591 -18.767 130.588  1.00 14.09           C  
ANISOU 5897  CE2 TYR B 267     1532   1628   2195    -71    -33    288       C  
ATOM   5898  CZ  TYR B 267     -43.302 -18.465 130.993  1.00 20.99           C  
ANISOU 5898  CZ  TYR B 267     2425   2508   3042    -68    -38    277       C  
ATOM   5899  OH  TYR B 267     -42.814 -17.190 130.837  1.00 20.91           O  
ANISOU 5899  OH  TYR B 267     2423   2511   3011    -64    -28    266       O  
ATOM   5900  N   THR B 268     -45.476 -25.660 130.911  1.00  8.08           N  
ANISOU 5900  N   THR B 268      740    769   1562   -102   -132    325       N  
ATOM   5901  CA  THR B 268     -45.865 -26.985 131.420  1.00  7.72           C  
ANISOU 5901  CA  THR B 268      690    696   1546   -113   -144    345       C  
ATOM   5902  C   THR B 268     -44.738 -28.004 131.230  1.00 10.49           C  
ANISOU 5902  C   THR B 268     1053   1034   1897   -106   -178    328       C  
ATOM   5903  O   THR B 268     -44.508 -28.831 132.105  1.00 10.30           O  
ANISOU 5903  O   THR B 268     1041    994   1879   -111   -182    346       O  
ATOM   5904  CB  THR B 268     -47.186 -27.462 130.763  1.00 13.31           C  
ANISOU 5904  CB  THR B 268     1370   1388   2299   -124   -153    354       C  
ATOM   5905  OG1 THR B 268     -47.010 -27.534 129.347  1.00 11.80           O  
ANISOU 5905  OG1 THR B 268     1169   1198   2116   -116   -184    322       O  
ATOM   5906  CG2 THR B 268     -48.369 -26.556 131.099  1.00 12.76           C  
ANISOU 5906  CG2 THR B 268     1285   1328   2235   -130   -117    376       C  
HETATM 5907  N   MSE B 269     -44.010 -27.922 130.097  1.00  6.65           N  
ANISOU 5907  N   MSE B 269      565    559   1404    -92   -201    294       N  
HETATM 5908  CA  MSE B 269     -42.898 -28.842 129.834  1.00  5.81           C  
ANISOU 5908  CA  MSE B 269      467    483   1257    -66   -224    252       C  
HETATM 5909  C   MSE B 269     -41.684 -28.522 130.722  1.00 10.95           C  
ANISOU 5909  C   MSE B 269     1140   1104   1918    -76   -224    277       C  
HETATM 5910  O   MSE B 269     -41.111 -29.429 131.331  1.00 11.55           O  
ANISOU 5910  O   MSE B 269     1227   1163   1999    -75   -239    283       O  
HETATM 5911  CB  MSE B 269     -42.504 -28.819 128.345  1.00  6.48           C  
ANISOU 5911  CB  MSE B 269      554    546   1361    -65   -245    230       C  
HETATM 5912  CG  MSE B 269     -41.413 -29.837 127.995  1.00 11.45           C  
ANISOU 5912  CG  MSE B 269     1183   1151   2018    -56   -284    218       C  
HETATM 5913 SE   MSE B 269     -41.003 -29.900 126.100  0.75 16.44          SE  
ANISOU 5913 SE   MSE B 269     1808   1791   2645    -36   -308    172      SE  
HETATM 5914  CE  MSE B 269     -40.342 -28.060 125.863  1.00 13.03           C  
ANISOU 5914  CE  MSE B 269     1378   1405   2168    -28   -274    165       C  
ATOM   5915  N   PHE B 270     -41.312 -27.225 130.819  1.00  7.00           N  
ANISOU 5915  N   PHE B 270      645    630   1386    -72   -202    271       N  
ATOM   5916  CA  PHE B 270     -40.138 -26.801 131.594  1.00  5.94           C  
ANISOU 5916  CA  PHE B 270      515    530   1213    -66   -198    258       C  
ATOM   5917  C   PHE B 270     -40.294 -27.110 133.099  1.00 10.56           C  
ANISOU 5917  C   PHE B 270     1132   1081   1800    -74   -187    300       C  
ATOM   5918  O   PHE B 270     -39.372 -27.659 133.714  1.00 10.24           O  
ANISOU 5918  O   PHE B 270     1106   1034   1753    -70   -203    302       O  
ATOM   5919  CB  PHE B 270     -39.849 -25.295 131.384  1.00  6.84           C  
ANISOU 5919  CB  PHE B 270      643    648   1307    -62   -177    259       C  
ATOM   5920  CG  PHE B 270     -39.906 -24.820 129.945  1.00  7.65           C  
ANISOU 5920  CG  PHE B 270      729    764   1413    -55   -180    235       C  
ATOM   5921  CD1 PHE B 270     -39.193 -25.478 128.949  1.00  9.87           C  
ANISOU 5921  CD1 PHE B 270     1004   1044   1703    -44   -205    212       C  
ATOM   5922  CD2 PHE B 270     -40.549 -23.631 129.615  1.00  8.85           C  
ANISOU 5922  CD2 PHE B 270      876    931   1555    -58   -158    237       C  
ATOM   5923  CE1 PHE B 270     -39.225 -25.024 127.629  1.00 10.44           C  
ANISOU 5923  CE1 PHE B 270     1065   1130   1772    -35   -206    191       C  
ATOM   5924  CE2 PHE B 270     -40.558 -23.165 128.298  1.00 11.40           C  
ANISOU 5924  CE2 PHE B 270     1188   1267   1878    -51   -162    217       C  
ATOM   5925  CZ  PHE B 270     -39.903 -23.866 127.314  1.00  9.47           C  
ANISOU 5925  CZ  PHE B 270      937   1021   1639    -40   -186    195       C  
ATOM   5926  N   GLN B 271     -41.455 -26.743 133.695  1.00  7.80           N  
ANISOU 5926  N   GLN B 271      783    730   1451    -85   -160    325       N  
ATOM   5927  CA  GLN B 271     -41.665 -26.932 135.136  1.00  8.25           C  
ANISOU 5927  CA  GLN B 271      860    779   1495    -92   -144    355       C  
ATOM   5928  C   GLN B 271     -42.174 -28.331 135.496  1.00 13.36           C  
ANISOU 5928  C   GLN B 271     1505   1398   2173   -100   -155    379       C  
ATOM   5929  O   GLN B 271     -41.639 -28.953 136.413  1.00 13.06           O  
ANISOU 5929  O   GLN B 271     1487   1349   2126   -100   -164    394       O  
ATOM   5930  CB  GLN B 271     -42.596 -25.847 135.716  1.00  9.27           C  
ANISOU 5930  CB  GLN B 271      994    922   1607    -97   -103    372       C  
ATOM   5931  CG  GLN B 271     -42.803 -25.981 137.231  1.00 12.05           C  
ANISOU 5931  CG  GLN B 271     1371   1268   1938   -100    -82    403       C  
ATOM   5932  CD  GLN B 271     -43.626 -24.860 137.797  1.00 19.93           C  
ANISOU 5932  CD  GLN B 271     2375   2279   2916   -101    -41    415       C  
ATOM   5933  OE1 GLN B 271     -43.154 -23.737 137.959  1.00  7.92           O  
ANISOU 5933  OE1 GLN B 271      869    776   1363    -94    -32    400       O  
ATOM   5934  NE2 GLN B 271     -44.825 -25.182 138.254  1.00 11.47           N  
ANISOU 5934  NE2 GLN B 271     1297   1200   1862   -109    -15    445       N  
ATOM   5935  N   ILE B 272     -43.266 -28.781 134.856  1.00 10.56           N  
ANISOU 5935  N   ILE B 272     1127   1030   1854   -109   -155    385       N  
ATOM   5936  CA  ILE B 272     -43.893 -30.050 135.230  1.00 10.59           C  
ANISOU 5936  CA  ILE B 272     1126   1005   1893   -121   -164    411       C  
ATOM   5937  C   ILE B 272     -43.156 -31.258 134.633  1.00 14.90           C  
ANISOU 5937  C   ILE B 272     1671   1529   2462   -116   -207    394       C  
ATOM   5938  O   ILE B 272     -42.652 -32.098 135.381  1.00 15.90           O  
ANISOU 5938  O   ILE B 272     1813   1638   2590   -116   -220    409       O  
ATOM   5939  CB  ILE B 272     -45.421 -30.062 134.900  1.00 13.75           C  
ANISOU 5939  CB  ILE B 272     1500   1397   2328   -135   -147    429       C  
ATOM   5940  CG1 ILE B 272     -46.132 -28.812 135.495  1.00 14.52           C  
ANISOU 5940  CG1 ILE B 272     1597   1516   2402   -136   -101    445       C  
ATOM   5941  CG2 ILE B 272     -46.077 -31.374 135.391  1.00 14.43           C  
ANISOU 5941  CG2 ILE B 272     1580   1450   2453   -150   -153    462       C  
ATOM   5942  CD1 ILE B 272     -47.619 -28.631 135.039  1.00 18.51           C  
ANISOU 5942  CD1 ILE B 272     2071   2018   2944   -147    -83    459       C  
ATOM   5943  N   THR B 273     -43.117 -31.362 133.284  1.00 11.08           N  
ANISOU 5943  N   THR B 273     1169   1044   1997   -110   -230    363       N  
ATOM   5944  CA  THR B 273     -42.509 -32.517 132.603  1.00 10.13           C  
ANISOU 5944  CA  THR B 273     1047    902   1901   -103   -270    342       C  
ATOM   5945  C   THR B 273     -41.028 -32.680 132.975  1.00 14.06           C  
ANISOU 5945  C   THR B 273     1564   1404   2374    -87   -285    330       C  
ATOM   5946  O   THR B 273     -40.583 -33.800 133.239  1.00 14.14           O  
ANISOU 5946  O   THR B 273     1581   1389   2401    -84   -310    334       O  
ATOM   5947  CB  THR B 273     -42.708 -32.413 131.066  1.00 17.45           C  
ANISOU 5947  CB  THR B 273     1955   1832   2842    -96   -288    308       C  
ATOM   5948  OG1 THR B 273     -44.044 -31.989 130.784  1.00 15.26           O  
ANISOU 5948  OG1 THR B 273     1659   1556   2582   -110   -273    320       O  
ATOM   5949  CG2 THR B 273     -42.415 -33.729 130.349  1.00 13.57           C  
ANISOU 5949  CG2 THR B 273     1463   1313   2382    -90   -330    289       C  
ATOM   5950  N   TRP B 274     -40.267 -31.564 133.009  1.00 10.01           N  
ANISOU 5950  N   TRP B 274     1058    923   1824    -77   -271    315       N  
ATOM   5951  CA  TRP B 274     -38.827 -31.618 133.305  1.00  9.43           C  
ANISOU 5951  CA  TRP B 274      998    856   1730    -63   -286    302       C  
ATOM   5952  C   TRP B 274     -38.511 -31.390 134.803  1.00 13.35           C  
ANISOU 5952  C   TRP B 274     1518   1355   2201    -67   -273    330       C  
ATOM   5953  O   TRP B 274     -37.338 -31.397 135.187  1.00 13.92           O  
ANISOU 5953  O   TRP B 274     1601   1431   2256    -56   -288    323       O  
ATOM   5954  CB  TRP B 274     -38.048 -30.618 132.426  1.00  7.94           C  
ANISOU 5954  CB  TRP B 274      801    696   1520    -50   -282    270       C  
ATOM   5955  CG  TRP B 274     -38.128 -30.904 130.949  1.00  8.78           C  
ANISOU 5955  CG  TRP B 274      891    802   1645    -40   -298    240       C  
ATOM   5956  CD1 TRP B 274     -38.508 -32.076 130.359  1.00 11.80           C  
ANISOU 5956  CD1 TRP B 274     1267   1157   2060    -39   -323    233       C  
ATOM   5957  CD2 TRP B 274     -37.664 -30.055 129.892  1.00  8.38           C  
ANISOU 5957  CD2 TRP B 274      829    776   1578    -29   -292    212       C  
ATOM   5958  NE1 TRP B 274     -38.390 -31.977 128.993  1.00 11.25           N  
ANISOU 5958  NE1 TRP B 274     1186   1096   1993    -27   -332    201       N  
ATOM   5959  CE2 TRP B 274     -37.871 -30.746 128.677  1.00 12.30           C  
ANISOU 5959  CE2 TRP B 274     1316   1262   2095    -20   -313    189       C  
ATOM   5960  CE3 TRP B 274     -37.108 -28.762 129.850  1.00  9.53           C  
ANISOU 5960  CE3 TRP B 274      976    952   1694    -26   -272    205       C  
ATOM   5961  CZ2 TRP B 274     -37.549 -30.188 127.433  1.00 11.49           C  
ANISOU 5961  CZ2 TRP B 274     1205   1180   1980     -7   -311    160       C  
ATOM   5962  CZ3 TRP B 274     -36.796 -28.209 128.617  1.00 10.98           C  
ANISOU 5962  CZ3 TRP B 274     1147   1154   1869    -15   -270    179       C  
ATOM   5963  CH2 TRP B 274     -37.011 -28.920 127.427  1.00 11.69           C  
ANISOU 5963  CH2 TRP B 274     1229   1235   1976     -5   -288    157       C  
ATOM   5964  N   SER B 275     -39.564 -31.211 135.652  1.00  8.52           N  
ANISOU 5964  N   SER B 275      913    739   1585    -82   -247    362       N  
ATOM   5965  CA  SER B 275     -39.396 -31.020 137.113  1.00  8.31           C  
ANISOU 5965  CA  SER B 275      914    715   1530    -85   -232    391       C  
ATOM   5966  C   SER B 275     -38.397 -29.880 137.456  1.00 13.38           C  
ANISOU 5966  C   SER B 275     1570   1384   2130    -76   -228    375       C  
ATOM   5967  O   SER B 275     -37.560 -30.025 138.362  1.00 13.20           O  
ANISOU 5967  O   SER B 275     1570   1360   2087    -71   -240    383       O  
ATOM   5968  CB  SER B 275     -38.983 -32.326 137.789  1.00 10.91           C  
ANISOU 5968  CB  SER B 275     1256   1016   1872    -85   -257    410       C  
ATOM   5969  OG  SER B 275     -40.007 -33.299 137.671  1.00 18.85           O  
ANISOU 5969  OG  SER B 275     2252   1995   2916    -97   -258    431       O  
ATOM   5970  N   GLY B 276     -38.522 -28.762 136.748  1.00  8.83           N  
ANISOU 5970  N   GLY B 276      982    830   1544    -74   -212    354       N  
ATOM   5971  CA  GLY B 276     -37.706 -27.589 136.987  1.00  8.45           C  
ANISOU 5971  CA  GLY B 276      944    805   1461    -68   -206    340       C  
ATOM   5972  C   GLY B 276     -38.526 -26.411 137.454  1.00 12.56           C  
ANISOU 5972  C   GLY B 276     1473   1341   1958    -75   -170    350       C  
ATOM   5973  O   GLY B 276     -39.196 -25.759 136.651  1.00 12.90           O  
ANISOU 5973  O   GLY B 276     1498   1393   2009    -77   -153    340       O  
ATOM   5974  N   PRO B 277     -38.539 -26.132 138.780  1.00  9.44           N  
ANISOU 5974  N   PRO B 277     1108    947   1533    -77   -157    370       N  
ATOM   5975  CA  PRO B 277     -39.396 -25.041 139.287  1.00  9.58           C  
ANISOU 5975  CA  PRO B 277     1136    977   1527    -80   -118    380       C  
ATOM   5976  C   PRO B 277     -39.112 -23.686 138.643  1.00 13.25           C  
ANISOU 5976  C   PRO B 277     1594   1462   1980    -76   -111    354       C  
ATOM   5977  O   PRO B 277     -37.963 -23.255 138.584  1.00 13.15           O  
ANISOU 5977  O   PRO B 277     1587   1458   1953    -71   -130    334       O  
ATOM   5978  CB  PRO B 277     -39.095 -25.023 140.792  1.00 11.43           C  
ANISOU 5978  CB  PRO B 277     1410   1209   1725    -78   -114    400       C  
ATOM   5979  CG  PRO B 277     -38.575 -26.377 141.094  1.00 15.77           C  
ANISOU 5979  CG  PRO B 277     1964   1740   2288    -78   -144    413       C  
ATOM   5980  CD  PRO B 277     -37.837 -26.828 139.877  1.00 11.03           C  
ANISOU 5980  CD  PRO B 277     1336   1137   1719    -74   -176    386       C  
ATOM   5981  N   ILE B 278     -40.165 -23.025 138.144  1.00 10.55           N  
ANISOU 5981  N   ILE B 278     1237   1127   1646    -79    -83    354       N  
ATOM   5982  CA  ILE B 278     -40.082 -21.653 137.652  1.00 10.09           C  
ANISOU 5982  CA  ILE B 278     1174   1085   1574    -76    -70    335       C  
ATOM   5983  C   ILE B 278     -40.763 -20.751 138.668  1.00 15.56           C  
ANISOU 5983  C   ILE B 278     1890   1782   2238    -76    -36    349       C  
ATOM   5984  O   ILE B 278     -41.986 -20.804 138.824  1.00 15.27           O  
ANISOU 5984  O   ILE B 278     1847   1743   2212    -78     -7    368       O  
ATOM   5985  CB  ILE B 278     -40.691 -21.526 136.229  1.00 12.99           C  
ANISOU 5985  CB  ILE B 278     1507   1456   1971    -77    -68    323       C  
ATOM   5986  CG1 ILE B 278     -39.919 -22.433 135.216  1.00 13.59           C  
ANISOU 5986  CG1 ILE B 278     1565   1528   2070    -74   -102    306       C  
ATOM   5987  CG2 ILE B 278     -40.698 -20.066 135.769  1.00 13.34           C  
ANISOU 5987  CG2 ILE B 278     1550   1517   2002    -74    -52    307       C  
ATOM   5988  CD1 ILE B 278     -40.544 -22.491 133.794  1.00 21.40           C  
ANISOU 5988  CD1 ILE B 278     2525   2519   3086    -74   -104    294       C  
ATOM   5989  N   CYS B 279     -39.960 -20.062 139.479  1.00 13.35           N  
ANISOU 5989  N   CYS B 279     1640   1509   1924    -72    -40    341       N  
ATOM   5990  CA  CYS B 279     -40.406 -19.479 140.728  1.00 13.46           C  
ANISOU 5990  CA  CYS B 279     1687   1524   1903    -68    -13    355       C  
ATOM   5991  C   CYS B 279     -40.908 -18.082 140.633  1.00 13.84           C  
ANISOU 5991  C   CYS B 279     1739   1581   1938    -64     14    345       C  
ATOM   5992  O   CYS B 279     -40.509 -17.326 139.743  1.00 13.59           O  
ANISOU 5992  O   CYS B 279     1691   1557   1916    -65      5    323       O  
ATOM   5993  CB  CYS B 279     -39.324 -19.607 141.794  1.00 14.50           C  
ANISOU 5993  CB  CYS B 279     1854   1653   2001    -66    -37    354       C  
ATOM   5994  SG  CYS B 279     -38.867 -21.305 142.179  1.00 18.59           S  
ANISOU 5994  SG  CYS B 279     2375   2156   2531    -68    -65    373       S  
HETATM 5995  N   MSE B 280     -41.690 -17.678 141.639  1.00  7.24           N  
ANISOU 5995  N   MSE B 280      928    746   1078    -59     48    360       N  
HETATM 5996  CA  MSE B 280     -42.018 -16.285 141.865  1.00  5.87           C  
ANISOU 5996  CA  MSE B 280      746    606    880    -40     64    313       C  
HETATM 5997  C   MSE B 280     -40.779 -15.607 142.438  1.00  9.47           C  
ANISOU 5997  C   MSE B 280     1258   1036   1304    -50     47    328       C  
HETATM 5998  O   MSE B 280     -40.072 -16.215 143.240  1.00  8.56           O  
ANISOU 5998  O   MSE B 280     1167    916   1169    -50     26    333       O  
HETATM 5999  CB  MSE B 280     -43.199 -16.168 142.861  1.00  6.57           C  
ANISOU 5999  CB  MSE B 280      877    666    953    -44    118    372       C  
HETATM 6000  CG  MSE B 280     -43.571 -14.717 143.209  1.00 10.65           C  
ANISOU 6000  CG  MSE B 280     1413   1187   1444    -33    146    359       C  
HETATM 6001 SE   MSE B 280     -45.001 -14.593 144.546  0.75 15.54          SE  
ANISOU 6001 SE   MSE B 280     2060   1808   2037    -19    208    388      SE  
HETATM 6002  CE  MSE B 280     -44.118 -15.455 146.026  1.00 12.38           C  
ANISOU 6002  CE  MSE B 280     1713   1404   1588    -18    189    401       C  
ATOM   6003  N   SER B 281     -40.453 -14.399 141.957  1.00  6.95           N  
ANISOU 6003  N   SER B 281      936    721    983    -49     44    305       N  
ATOM   6004  CA  SER B 281     -39.279 -13.676 142.449  1.00  6.44           C  
ANISOU 6004  CA  SER B 281      899    655    892    -49     17    285       C  
ATOM   6005  C   SER B 281     -39.577 -13.012 143.780  1.00  9.94           C  
ANISOU 6005  C   SER B 281     1390   1094   1291    -39     37    286       C  
ATOM   6006  O   SER B 281     -40.744 -12.753 144.092  1.00  9.37           O  
ANISOU 6006  O   SER B 281     1325   1023   1212    -30     78    298       O  
ATOM   6007  CB  SER B 281     -38.834 -12.631 141.436  1.00  8.36           C  
ANISOU 6007  CB  SER B 281     1122    901   1153    -53      8    263       C  
ATOM   6008  OG  SER B 281     -39.827 -11.633 141.263  1.00 12.26           O  
ANISOU 6008  OG  SER B 281     1617   1396   1647    -46     42    261       O  
ATOM   6009  N   LYS B 282     -38.525 -12.704 144.563  1.00  7.32           N  
ANISOU 6009  N   LYS B 282     1093    759    929    -39      7    272       N  
ATOM   6010  CA  LYS B 282     -38.690 -11.998 145.837  1.00  8.10           C  
ANISOU 6010  CA  LYS B 282     1243    853    979    -28     20    268       C  
ATOM   6011  C   LYS B 282     -39.261 -10.601 145.594  1.00 10.95           C  
ANISOU 6011  C   LYS B 282     1609   1214   1339    -21     46    253       C  
ATOM   6012  O   LYS B 282     -40.107 -10.136 146.361  1.00 10.07           O  
ANISOU 6012  O   LYS B 282     1527   1101   1199     -8     81    257       O  
ATOM   6013  CB  LYS B 282     -37.340 -11.911 146.591  1.00 11.15           C  
ANISOU 6013  CB  LYS B 282     1663   1235   1339    -31    -27    254       C  
ATOM   6014  CG  LYS B 282     -37.450 -11.288 147.992  1.00 27.96           C  
ANISOU 6014  CG  LYS B 282     3854   3359   3412    -18    -20    248       C  
ATOM   6015  CD  LYS B 282     -38.249 -12.176 148.952  1.00 39.65           C  
ANISOU 6015  CD  LYS B 282     5360   4842   4862     -7      9    277       C  
ATOM   6016  CE  LYS B 282     -38.362 -11.567 150.324  1.00 54.04           C  
ANISOU 6016  CE  LYS B 282     7247   6661   6624      8     19    271       C  
ATOM   6017  NZ  LYS B 282     -39.114 -12.448 151.254  1.00 66.42           N  
ANISOU 6017  NZ  LYS B 282     8841   8233   8162     19     51    302       N  
ATOM   6018  N   SER B 283     -38.853  -9.962 144.474  1.00  8.10           N  
ANISOU 6018  N   SER B 283     1216    853   1010    -30     32    236       N  
ATOM   6019  CA  SER B 283     -39.367  -8.648 144.078  1.00  7.75           C  
ANISOU 6019  CA  SER B 283     1170    805    971    -25     54    223       C  
ATOM   6020  C   SER B 283     -40.886  -8.676 143.911  1.00 12.32           C  
ANISOU 6020  C   SER B 283     1735   1388   1559    -14    104    240       C  
ATOM   6021  O   SER B 283     -41.575  -7.814 144.446  1.00 12.46           O  
ANISOU 6021  O   SER B 283     1777   1400   1556      0    134    235       O  
ATOM   6022  CB  SER B 283     -38.710  -8.189 142.783  1.00  8.82           C  
ANISOU 6022  CB  SER B 283     1267    940   1142    -37     31    209       C  
ATOM   6023  OG  SER B 283     -37.306  -8.087 142.931  1.00 13.62           O  
ANISOU 6023  OG  SER B 283     1884   1545   1747    -48    -13    194       O  
ATOM   6024  N   VAL B 284     -41.415  -9.699 143.192  1.00 10.08           N  
ANISOU 6024  N   VAL B 284     1411   1111   1307    -19    112    260       N  
ATOM   6025  CA  VAL B 284     -42.860  -9.839 142.974  1.00 10.00           C  
ANISOU 6025  CA  VAL B 284     1381   1104   1314    -11    156    279       C  
ATOM   6026  C   VAL B 284     -43.600 -10.122 144.294  1.00 14.47           C  
ANISOU 6026  C   VAL B 284     1982   1670   1847      2    190    296       C  
ATOM   6027  O   VAL B 284     -44.661  -9.543 144.535  1.00 15.66           O  
ANISOU 6027  O   VAL B 284     2135   1821   1994     16    232    302       O  
ATOM   6028  CB  VAL B 284     -43.186 -10.898 141.873  1.00 13.35           C  
ANISOU 6028  CB  VAL B 284     1756   1534   1782    -21    150    294       C  
ATOM   6029  CG1 VAL B 284     -44.683 -11.207 141.829  1.00 13.15           C  
ANISOU 6029  CG1 VAL B 284     1711   1511   1776    -15    191    317       C  
ATOM   6030  CG2 VAL B 284     -42.693 -10.430 140.508  1.00 12.43           C  
ANISOU 6030  CG2 VAL B 284     1608   1420   1696    -29    127    277       C  
ATOM   6031  N   GLU B 285     -42.998 -10.945 145.187  1.00  9.80           N  
ANISOU 6031  N   GLU B 285     1418   1078   1228      0    173    304       N  
ATOM   6032  CA  GLU B 285     -43.583 -11.201 146.506  1.00  9.33           C  
ANISOU 6032  CA  GLU B 285     1397   1018   1129     13    205    322       C  
ATOM   6033  C   GLU B 285     -43.762  -9.884 147.269  1.00 14.05           C  
ANISOU 6033  C   GLU B 285     2038   1613   1688     30    226    303       C  
ATOM   6034  O   GLU B 285     -44.821  -9.647 147.841  1.00 13.79           O  
ANISOU 6034  O   GLU B 285     2017   1582   1641     46    274    315       O  
ATOM   6035  CB  GLU B 285     -42.715 -12.176 147.318  1.00 10.46           C  
ANISOU 6035  CB  GLU B 285     1568   1160   1245      8    174    330       C  
ATOM   6036  CG  GLU B 285     -43.374 -12.620 148.622  1.00 18.62           C  
ANISOU 6036  CG  GLU B 285     2640   2195   2238     21    209    355       C  
ATOM   6037  CD  GLU B 285     -42.481 -13.393 149.575  1.00 29.94           C  
ANISOU 6037  CD  GLU B 285     4112   3627   3636     19    178    362       C  
ATOM   6038  OE1 GLU B 285     -41.311 -13.653 149.218  1.00 15.17           O  
ANISOU 6038  OE1 GLU B 285     2235   1752   1775      7    126    348       O  
ATOM   6039  OE2 GLU B 285     -42.942 -13.705 150.696  1.00 24.84           O  
ANISOU 6039  OE2 GLU B 285     3504   2982   2951     30    206    383       O  
ATOM   6040  N   LYS B 286     -42.748  -8.987 147.197  1.00 11.38           N  
ANISOU 6040  N   LYS B 286     1718   1268   1337     27    190    272       N  
ATOM   6041  CA  LYS B 286     -42.815  -7.669 147.835  1.00 11.49           C  
ANISOU 6041  CA  LYS B 286     1774   1274   1317     42    203    249       C  
ATOM   6042  C   LYS B 286     -43.934  -6.812 147.222  1.00 14.87           C  
ANISOU 6042  C   LYS B 286     2178   1702   1771     53    244    248       C  
ATOM   6043  O   LYS B 286     -44.559  -6.023 147.928  1.00 13.50           O  
ANISOU 6043  O   LYS B 286     2036   1523   1569     73    278    242       O  
ATOM   6044  CB  LYS B 286     -41.461  -6.939 147.719  1.00 13.38           C  
ANISOU 6044  CB  LYS B 286     2029   1504   1550     32    150    218       C  
ATOM   6045  CG  LYS B 286     -40.346  -7.581 148.532  1.00 19.40           C  
ANISOU 6045  CG  LYS B 286     2825   2265   2282     26    108    216       C  
ATOM   6046  CD  LYS B 286     -39.046  -6.802 148.397  1.00 22.23           C  
ANISOU 6046  CD  LYS B 286     3194   2613   2641     14     56    186       C  
ATOM   6047  CE  LYS B 286     -37.937  -7.397 149.224  1.00 19.71           C  
ANISOU 6047  CE  LYS B 286     2906   2292   2293      9     11    184       C  
ATOM   6048  NZ  LYS B 286     -36.679  -6.619 149.091  1.00 19.97           N  
ANISOU 6048  NZ  LYS B 286     2944   2313   2331     -3    -41    156       N  
ATOM   6049  N   LEU B 287     -44.199  -6.989 145.901  1.00 11.79           N  
ANISOU 6049  N   LEU B 287     1732   1315   1433     42    241    255       N  
ATOM   6050  CA  LEU B 287     -45.224  -6.219 145.190  1.00 11.51           C  
ANISOU 6050  CA  LEU B 287     1668   1278   1426     51    274    255       C  
ATOM   6051  C   LEU B 287     -46.651  -6.729 145.477  1.00 15.95           C  
ANISOU 6051  C   LEU B 287     2216   1849   1997     64    327    284       C  
ATOM   6052  O   LEU B 287     -47.598  -5.947 145.410  1.00 16.51           O  
ANISOU 6052  O   LEU B 287     2280   1917   2076     80    364    283       O  
ATOM   6053  CB  LEU B 287     -44.959  -6.239 143.668  1.00 11.15           C  
ANISOU 6053  CB  LEU B 287     1572   1235   1430     34    249    253       C  
ATOM   6054  CG  LEU B 287     -43.663  -5.565 143.193  1.00 15.53           C  
ANISOU 6054  CG  LEU B 287     2133   1783   1986     22    204    227       C  
ATOM   6055  CD1 LEU B 287     -43.403  -5.866 141.732  1.00 15.51           C  
ANISOU 6055  CD1 LEU B 287     2079   1785   2027      6    182    230       C  
ATOM   6056  CD2 LEU B 287     -43.707  -4.067 143.422  1.00 16.16           C  
ANISOU 6056  CD2 LEU B 287     2238   1849   2051     33    212    205       C  
ATOM   6057  N   VAL B 288     -46.813  -8.059 145.704  1.00 12.22           N  
ANISOU 6057  N   VAL B 288     1731   1384   1529     56    330    310       N  
ATOM   6058  CA  VAL B 288     -48.158  -8.666 145.865  1.00 12.12           C  
ANISOU 6058  CA  VAL B 288     1694   1377   1534     63    378    342       C  
ATOM   6059  C   VAL B 288     -48.575  -8.836 147.347  1.00 15.50           C  
ANISOU 6059  C   VAL B 288     2167   1807   1914     81    416    356       C  
ATOM   6060  O   VAL B 288     -49.757  -9.062 147.631  1.00 15.02           O  
ANISOU 6060  O   VAL B 288     2091   1751   1863     92    466    381       O  
ATOM   6061  CB  VAL B 288     -48.301 -10.002 145.068  1.00 15.31           C  
ANISOU 6061  CB  VAL B 288     2050   1785   1982     44    362    365       C  
ATOM   6062  CG1 VAL B 288     -48.104  -9.771 143.571  1.00 14.32           C  
ANISOU 6062  CG1 VAL B 288     1880   1658   1901     31    332    352       C  
ATOM   6063  CG2 VAL B 288     -47.334 -11.065 145.590  1.00 14.88           C  
ANISOU 6063  CG2 VAL B 288     2017   1730   1906     31    329    371       C  
ATOM   6064  N   THR B 289     -47.604  -8.739 148.281  1.00 11.28           N  
ANISOU 6064  N   THR B 289     1688   1270   1328     83    394    341       N  
ATOM   6065  CA  THR B 289     -47.872  -8.902 149.715  1.00 11.24           C  
ANISOU 6065  CA  THR B 289     1734   1269   1269    101    426    353       C  
ATOM   6066  C   THR B 289     -48.677  -7.730 150.280  1.00 14.64           C  
ANISOU 6066  C   THR B 289     2190   1697   1674    129    474    342       C  
ATOM   6067  O   THR B 289     -48.412  -6.578 149.941  1.00 13.10           O  
ANISOU 6067  O   THR B 289     2004   1494   1480    135    462    311       O  
ATOM   6068  CB  THR B 289     -46.543  -9.109 150.488  1.00 18.16           C  
ANISOU 6068  CB  THR B 289     2662   2141   2097     96    380    338       C  
ATOM   6069  OG1 THR B 289     -45.948 -10.329 150.060  1.00 19.12           O  
ANISOU 6069  OG1 THR B 289     2757   2264   2243     73    343    354       O  
ATOM   6070  CG2 THR B 289     -46.742  -9.134 152.010  1.00 16.61           C  
ANISOU 6070  CG2 THR B 289     2529   1948   1836    116    409    347       C  
ATOM   6071  N   ASN B 290     -49.678  -8.039 151.149  1.00 11.63           N  
ANISOU 6071  N   ASN B 290     1823   1324   1273    147    532    369       N  
ATOM   6072  CA  ASN B 290     -50.452  -7.046 151.919  1.00 11.41           C  
ANISOU 6072  CA  ASN B 290     1828   1296   1211    179    585    360       C  
ATOM   6073  C   ASN B 290     -51.407  -6.194 151.062  1.00 15.43           C  
ANISOU 6073  C   ASN B 290     2292   1802   1767    189    614    355       C  
ATOM   6074  O   ASN B 290     -52.544  -5.951 151.476  1.00 16.34           O  
ANISOU 6074  O   ASN B 290     2403   1923   1883    211    675    370       O  
ATOM   6075  CB  ASN B 290     -49.525  -6.153 152.764  1.00  9.46           C  
ANISOU 6075  CB  ASN B 290     1654   1040    901    192    560    323       C  
ATOM   6076  CG  ASN B 290     -50.244  -5.419 153.869  1.00 30.53           C  
ANISOU 6076  CG  ASN B 290     4371   3709   3518    228    616    317       C  
ATOM   6077  OD1 ASN B 290     -50.956  -6.016 154.680  1.00 25.97           O  
ANISOU 6077  OD1 ASN B 290     3807   3143   2916    242    665    347       O  
ATOM   6078  ND2 ASN B 290     -49.989  -4.132 153.988  1.00 23.46           N  
ANISOU 6078  ND2 ASN B 290     3509   2801   2602    244    607    278       N  
ATOM   6079  N   ILE B 291     -50.928  -5.693 149.909  1.00 10.95           N  
ANISOU 6079  N   ILE B 291     1695   1227   1240    173    572    333       N  
ATOM   6080  CA  ILE B 291     -51.719  -4.802 149.036  1.00 10.22           C  
ANISOU 6080  CA  ILE B 291     1563   1130   1191    183    592    326       C  
ATOM   6081  C   ILE B 291     -53.127  -5.371 148.746  1.00 15.43           C  
ANISOU 6081  C   ILE B 291     2169   1799   1896    188    642    363       C  
ATOM   6082  O   ILE B 291     -53.262  -6.540 148.390  1.00 15.82           O  
ANISOU 6082  O   ILE B 291     2182   1856   1974    168    634    391       O  
ATOM   6083  CB  ILE B 291     -50.933  -4.450 147.721  1.00 11.81           C  
ANISOU 6083  CB  ILE B 291     1734   1323   1431    160    535    306       C  
ATOM   6084  CG1 ILE B 291     -51.689  -3.373 146.882  1.00 11.46           C  
ANISOU 6084  CG1 ILE B 291     1658   1272   1425    173    552    296       C  
ATOM   6085  CG2 ILE B 291     -50.623  -5.729 146.886  1.00 10.45           C  
ANISOU 6085  CG2 ILE B 291     1515   1158   1296    131    502    326       C  
ATOM   6086  CD1 ILE B 291     -50.909  -2.851 145.648  1.00 15.67           C  
ANISOU 6086  CD1 ILE B 291     2169   1796   1989    154    501    276       C  
ATOM   6087  N   GLY B 292     -54.153  -4.551 148.969  1.00 12.54           N  
ANISOU 6087  N   GLY B 292     1799   1433   1534    215    693    363       N  
ATOM   6088  CA  GLY B 292     -55.537  -4.945 148.726  1.00 12.71           C  
ANISOU 6088  CA  GLY B 292     1766   1461   1601    222    743    398       C  
ATOM   6089  C   GLY B 292     -56.299  -5.321 149.982  1.00 17.74           C  
ANISOU 6089  C   GLY B 292     2426   2109   2205    244    807    424       C  
ATOM   6090  O   GLY B 292     -57.531  -5.345 149.978  1.00 18.33           O  
ANISOU 6090  O   GLY B 292     2463   2189   2311    258    861    449       O  
ATOM   6091  N   GLY B 293     -55.565  -5.672 151.037  1.00 14.76           N  
ANISOU 6091  N   GLY B 293     2108   1734   1765    245    802    420       N  
ATOM   6092  CA  GLY B 293     -56.149  -5.990 152.342  1.00 15.03           C  
ANISOU 6092  CA  GLY B 293     2178   1779   1755    267    862    443       C  
ATOM   6093  C   GLY B 293     -56.881  -7.323 152.411  1.00 18.39           C  
ANISOU 6093  C   GLY B 293     2559   2215   2211    253    892    495       C  
ATOM   6094  O   GLY B 293     -57.406  -7.686 153.468  1.00 17.88           O  
ANISOU 6094  O   GLY B 293     2520   2161   2113    270    946    521       O  
ATOM   6095  N   VAL B 294     -56.932  -8.066 151.285  1.00 14.78           N  
ANISOU 6095  N   VAL B 294     2040   1757   1820    223    858    510       N  
ATOM   6096  CA  VAL B 294     -57.630  -9.363 151.252  1.00 15.14           C  
ANISOU 6096  CA  VAL B 294     2040   1809   1905    206    880    558       C  
ATOM   6097  C   VAL B 294     -56.779 -10.449 151.923  1.00 19.56           C  
ANISOU 6097  C   VAL B 294     2638   2370   2425    188    855    573       C  
ATOM   6098  O   VAL B 294     -55.637 -10.677 151.519  1.00 18.90           O  
ANISOU 6098  O   VAL B 294     2568   2280   2334    169    790    551       O  
ATOM   6099  CB  VAL B 294     -58.053  -9.767 149.804  1.00 18.85           C  
ANISOU 6099  CB  VAL B 294     2430   2273   2458    181    850    568       C  
ATOM   6100  CG1 VAL B 294     -58.836 -11.082 149.809  1.00 18.82           C  
ANISOU 6100  CG1 VAL B 294     2379   2272   2498    163    873    618       C  
ATOM   6101  CG2 VAL B 294     -58.870  -8.656 149.143  1.00 18.98           C  
ANISOU 6101  CG2 VAL B 294     2412   2287   2512    199    871    554       C  
ATOM   6102  N   ALA B 295     -57.331 -11.105 152.966  1.00 17.06           N  
ANISOU 6102  N   ALA B 295     2336   2061   2083    197    907    611       N  
ATOM   6103  CA  ALA B 295     -56.615 -12.144 153.720  1.00 17.03           C  
ANISOU 6103  CA  ALA B 295     2373   2059   2040    184    889    630       C  
ATOM   6104  C   ALA B 295     -56.212 -13.332 152.826  1.00 20.90           C  
ANISOU 6104  C   ALA B 295     2818   2541   2584    146    834    645       C  
ATOM   6105  O   ALA B 295     -56.850 -13.578 151.796  1.00 21.03           O  
ANISOU 6105  O   ALA B 295     2766   2553   2671    131    830    656       O  
ATOM   6106  CB  ALA B 295     -57.467 -12.629 154.879  1.00 18.50           C  
ANISOU 6106  CB  ALA B 295     2575   2256   2199    200    961    674       C  
ATOM   6107  N   TRP B 296     -55.146 -14.069 153.226  1.00 16.26           N  
ANISOU 6107  N   TRP B 296     2268   1949   1961    132    791    645       N  
ATOM   6108  CA  TRP B 296     -54.664 -15.243 152.481  1.00 14.85           C  
ANISOU 6108  CA  TRP B 296     2055   1761   1827     99    739    658       C  
ATOM   6109  C   TRP B 296     -55.808 -16.268 152.272  1.00 19.87           C  
ANISOU 6109  C   TRP B 296     2632   2394   2522     85    774    709       C  
ATOM   6110  O   TRP B 296     -56.522 -16.598 153.220  1.00 19.95           O  
ANISOU 6110  O   TRP B 296     2655   2411   2515     95    832    746       O  
ATOM   6111  CB  TRP B 296     -53.471 -15.895 153.219  1.00 12.74           C  
ANISOU 6111  CB  TRP B 296     1844   1490   1506     93    699    658       C  
ATOM   6112  CG  TRP B 296     -52.940 -17.124 152.548  1.00 12.71           C  
ANISOU 6112  CG  TRP B 296     1810   1476   1545     62    647    670       C  
ATOM   6113  CD1 TRP B 296     -53.276 -18.418 152.818  1.00 15.70           C  
ANISOU 6113  CD1 TRP B 296     2172   1848   1944     47    657    715       C  
ATOM   6114  CD2 TRP B 296     -51.984 -17.171 151.484  1.00 11.47           C  
ANISOU 6114  CD2 TRP B 296     1633   1310   1415     45    578    638       C  
ATOM   6115  NE1 TRP B 296     -52.599 -19.268 151.978  1.00 14.48           N  
ANISOU 6115  NE1 TRP B 296     1992   1681   1830     22    596    710       N  
ATOM   6116  CE2 TRP B 296     -51.783 -18.530 151.160  1.00 15.05           C  
ANISOU 6116  CE2 TRP B 296     2061   1752   1904     21    549    663       C  
ATOM   6117  CE3 TRP B 296     -51.251 -16.196 150.790  1.00 11.94           C  
ANISOU 6117  CE3 TRP B 296     1695   1370   1472     47    540    591       C  
ATOM   6118  CZ2 TRP B 296     -50.894 -18.936 150.163  1.00 13.75           C  
ANISOU 6118  CZ2 TRP B 296     1875   1579   1771      3    484    640       C  
ATOM   6119  CZ3 TRP B 296     -50.384 -16.600 149.792  1.00 12.63           C  
ANISOU 6119  CZ3 TRP B 296     1759   1449   1591     28    478    571       C  
ATOM   6120  CH2 TRP B 296     -50.217 -17.955 149.482  1.00 13.20           C  
ANISOU 6120  CH2 TRP B 296     1807   1512   1697      7    452    595       C  
ATOM   6121  N   PRO B 297     -56.041 -16.725 151.010  1.00 16.77           N  
ANISOU 6121  N   PRO B 297     2175   1992   2204     61    742    710       N  
ATOM   6122  CA  PRO B 297     -57.181 -17.632 150.763  1.00 17.04           C  
ANISOU 6122  CA  PRO B 297     2151   2022   2302     46    772    756       C  
ATOM   6123  C   PRO B 297     -56.954 -19.044 151.306  1.00 23.19           C  
ANISOU 6123  C   PRO B 297     2939   2792   3079     27    764    795       C  
ATOM   6124  O   PRO B 297     -55.814 -19.490 151.414  1.00 23.55           O  
ANISOU 6124  O   PRO B 297     3020   2832   3095     18    715    781       O  
ATOM   6125  CB  PRO B 297     -57.312 -17.624 149.241  1.00 17.88           C  
ANISOU 6125  CB  PRO B 297     2195   2119   2478     28    729    737       C  
ATOM   6126  CG  PRO B 297     -55.954 -17.308 148.748  1.00 21.30           C  
ANISOU 6126  CG  PRO B 297     2659   2551   2884     24    664    692       C  
ATOM   6127  CD  PRO B 297     -55.330 -16.388 149.758  1.00 17.21           C  
ANISOU 6127  CD  PRO B 297     2209   2041   2287     49    679    670       C  
ATOM   6128  N   GLN B 298     -58.047 -19.757 151.624  1.00 20.51           N  
ANISOU 6128  N   GLN B 298     2565   2451   2777     20    813    845       N  
ATOM   6129  CA  GLN B 298     -57.963 -21.118 152.154  1.00 20.65           C  
ANISOU 6129  CA  GLN B 298     2589   2458   2799      1    811    888       C  
ATOM   6130  C   GLN B 298     -57.792 -22.153 151.026  1.00 24.77           C  
ANISOU 6130  C   GLN B 298     3060   2959   3392    -32    751    891       C  
ATOM   6131  O   GLN B 298     -58.169 -21.896 149.882  1.00 24.68           O  
ANISOU 6131  O   GLN B 298     2997   2943   3437    -40    730    873       O  
ATOM   6132  CB  GLN B 298     -59.206 -21.445 153.000  1.00 22.76           C  
ANISOU 6132  CB  GLN B 298     2840   2731   3077      7    890    945       C  
ATOM   6133  N   GLY B 299     -57.210 -23.300 151.365  1.00 21.25           N  
ANISOU 6133  N   GLY B 299     2634   2500   2941    -48    723    913       N  
ATOM   6134  CA  GLY B 299     -57.053 -24.415 150.436  1.00 20.76           C  
ANISOU 6134  CA  GLY B 299     2531   2416   2944    -78    669    918       C  
ATOM   6135  C   GLY B 299     -56.010 -24.195 149.358  1.00 24.45           C  
ANISOU 6135  C   GLY B 299     2996   2877   3416    -83    597    865       C  
ATOM   6136  O   GLY B 299     -56.126 -24.754 148.262  1.00 24.18           O  
ANISOU 6136  O   GLY B 299     2915   2828   3443   -103    557    859       O  
ATOM   6137  N   VAL B 300     -54.958 -23.405 149.661  1.00 20.28           N  
ANISOU 6137  N   VAL B 300     2521   2361   2823    -66    577    827       N  
ATOM   6138  CA  VAL B 300     -53.871 -23.190 148.701  1.00 18.85           C  
ANISOU 6138  CA  VAL B 300     2341   2177   2644    -70    511    779       C  
ATOM   6139  C   VAL B 300     -52.875 -24.344 148.780  1.00 22.26           C  
ANISOU 6139  C   VAL B 300     2793   2593   3073    -84    460    783       C  
ATOM   6140  O   VAL B 300     -52.295 -24.586 149.839  1.00 22.26           O  
ANISOU 6140  O   VAL B 300     2843   2594   3019    -77    463    796       O  
ATOM   6141  CB  VAL B 300     -53.180 -21.807 148.890  1.00 22.33           C  
ANISOU 6141  CB  VAL B 300     2823   2635   3026    -47    508    735       C  
ATOM   6142  CG1 VAL B 300     -52.020 -21.635 147.903  1.00 21.60           C  
ANISOU 6142  CG1 VAL B 300     2729   2540   2938    -53    441    690       C  
ATOM   6143  CG2 VAL B 300     -54.187 -20.669 148.742  1.00 22.28           C  
ANISOU 6143  CG2 VAL B 300     2796   2643   3028    -32    557    729       C  
ATOM   6144  N   VAL B 301     -52.772 -25.134 147.701  1.00 17.81           N  
ANISOU 6144  N   VAL B 301     2188   2012   2568   -104    415    777       N  
ATOM   6145  CA  VAL B 301     -51.901 -26.313 147.680  1.00 17.24           C  
ANISOU 6145  CA  VAL B 301     2128   1921   2501   -117    366    782       C  
ATOM   6146  C   VAL B 301     -51.105 -26.369 146.383  1.00 19.59           C  
ANISOU 6146  C   VAL B 301     2405   2212   2826   -123    304    738       C  
ATOM   6147  O   VAL B 301     -51.554 -25.841 145.359  1.00 19.01           O  
ANISOU 6147  O   VAL B 301     2294   2143   2787   -125    300    717       O  
ATOM   6148  CB  VAL B 301     -52.715 -27.642 147.899  1.00 21.30           C  
ANISOU 6148  CB  VAL B 301     2615   2412   3064   -137    379    834       C  
ATOM   6149  CG1 VAL B 301     -53.538 -27.584 149.182  1.00 21.43           C  
ANISOU 6149  CG1 VAL B 301     2652   2438   3054   -130    447    881       C  
ATOM   6150  CG2 VAL B 301     -53.608 -27.947 146.695  1.00 21.17           C  
ANISOU 6150  CG2 VAL B 301     2534   2384   3127   -154    370    834       C  
ATOM   6151  N   ASN B 302     -49.947 -27.047 146.400  1.00 15.01           N  
ANISOU 6151  N   ASN B 302     1849   1622   2234   -126    256    727       N  
ATOM   6152  CA  ASN B 302     -49.224 -27.332 145.168  1.00 14.23           C  
ANISOU 6152  CA  ASN B 302     1727   1514   2166   -132    199    691       C  
ATOM   6153  C   ASN B 302     -49.922 -28.492 144.469  1.00 17.15           C  
ANISOU 6153  C   ASN B 302     2053   1859   2604   -151    185    711       C  
ATOM   6154  O   ASN B 302     -50.078 -29.552 145.060  1.00 17.19           O  
ANISOU 6154  O   ASN B 302     2064   1845   2622   -162    186    747       O  
ATOM   6155  CB  ASN B 302     -47.753 -27.678 145.462  1.00 14.73           C  
ANISOU 6155  CB  ASN B 302     1829   1574   2195   -126    155    673       C  
ATOM   6156  CG  ASN B 302     -46.935 -27.933 144.219  1.00 25.96           C  
ANISOU 6156  CG  ASN B 302     3229   2990   3646   -129    101    635       C  
ATOM   6157  OD1 ASN B 302     -47.046 -28.980 143.577  1.00 14.87           O  
ANISOU 6157  OD1 ASN B 302     1799   1563   2288   -140     74    640       O  
ATOM   6158  ND2 ASN B 302     -46.084 -26.986 143.865  1.00 18.69           N  
ANISOU 6158  ND2 ASN B 302     2320   2086   2697   -117     84    596       N  
ATOM   6159  N   GLN B 303     -50.449 -28.253 143.261  1.00 13.40           N  
ANISOU 6159  N   GLN B 303     1535   1384   2174   -157    174    691       N  
ATOM   6160  CA  GLN B 303     -51.276 -29.251 142.562  1.00 13.46           C  
ANISOU 6160  CA  GLN B 303     1498   1366   2249   -176    161    709       C  
ATOM   6161  C   GLN B 303     -50.444 -30.346 141.845  1.00 18.85           C  
ANISOU 6161  C   GLN B 303     2178   2026   2959   -184    100    691       C  
ATOM   6162  O   GLN B 303     -51.022 -31.276 141.269  1.00 19.31           O  
ANISOU 6162  O   GLN B 303     2205   2060   3074   -200     82    702       O  
ATOM   6163  CB  GLN B 303     -52.244 -28.566 141.583  1.00 14.20           C  
ANISOU 6163  CB  GLN B 303     1548   1469   2381   -178    172    696       C  
ATOM   6164  CG  GLN B 303     -53.227 -27.609 142.269  1.00 25.57           C  
ANISOU 6164  CG  GLN B 303     2983   2927   3805   -171    234    718       C  
ATOM   6165  CD  GLN B 303     -54.190 -26.993 141.284  1.00 41.53           C  
ANISOU 6165  CD  GLN B 303     4958   4954   5868   -173    240    707       C  
ATOM   6166  OE1 GLN B 303     -55.059 -27.667 140.722  1.00 36.92           O  
ANISOU 6166  OE1 GLN B 303     4331   4352   5345   -189    232    724       O  
ATOM   6167  NE2 GLN B 303     -54.109 -25.685 141.119  1.00 33.53           N  
ANISOU 6167  NE2 GLN B 303     3952   3964   4824   -156    256    681       N  
ATOM   6168  N   THR B 304     -49.096 -30.256 141.911  1.00 15.17           N  
ANISOU 6168  N   THR B 304     1745   1566   2453   -172     70    663       N  
ATOM   6169  CA  THR B 304     -48.222 -31.277 141.307  1.00 14.59           C  
ANISOU 6169  CA  THR B 304     1672   1471   2400   -175     15    645       C  
ATOM   6170  C   THR B 304     -47.832 -32.343 142.349  1.00 19.60           C  
ANISOU 6170  C   THR B 304     2334   2085   3027   -179      9    679       C  
ATOM   6171  O   THR B 304     -47.915 -33.544 142.068  1.00 19.73           O  
ANISOU 6171  O   THR B 304     2338   2072   3087   -191    -19    691       O  
ATOM   6172  CB  THR B 304     -46.983 -30.617 140.661  1.00 19.21           C  
ANISOU 6172  CB  THR B 304     2270   2074   2956   -159    -16    596       C  
ATOM   6173  OG1 THR B 304     -47.415 -29.619 139.744  1.00 15.15           O  
ANISOU 6173  OG1 THR B 304     1731   1577   2447   -155     -7    570       O  
ATOM   6174  CG2 THR B 304     -46.087 -31.630 139.941  1.00 17.76           C  
ANISOU 6174  CG2 THR B 304     2084   1870   2796   -158    -70    574       C  
ATOM   6175  N   SER B 305     -47.435 -31.904 143.554  1.00 16.22           N  
ANISOU 6175  N   SER B 305     1947   1672   2545   -169     33    694       N  
ATOM   6176  CA  SER B 305     -47.020 -32.819 144.624  1.00 16.52           C  
ANISOU 6176  CA  SER B 305     2017   1693   2566   -171     27    728       C  
ATOM   6177  C   SER B 305     -48.161 -33.098 145.609  1.00 21.06           C  
ANISOU 6177  C   SER B 305     2594   2263   3146   -181     78    783       C  
ATOM   6178  O   SER B 305     -48.103 -34.074 146.363  1.00 21.50           O  
ANISOU 6178  O   SER B 305     2668   2298   3204   -188     75    820       O  
ATOM   6179  CB  SER B 305     -45.815 -32.255 145.369  1.00 19.92           C  
ANISOU 6179  CB  SER B 305     2494   2142   2933   -153     17    712       C  
ATOM   6180  OG  SER B 305     -46.094 -30.968 145.898  1.00 29.27           O  
ANISOU 6180  OG  SER B 305     3695   3355   4071   -143     58    708       O  
ATOM   6181  N   GLY B 306     -49.170 -32.222 145.616  1.00 16.81           N  
ANISOU 6181  N   GLY B 306     2038   1743   2607   -181    125    789       N  
ATOM   6182  CA  GLY B 306     -50.293 -32.328 146.541  1.00 16.25           C  
ANISOU 6182  CA  GLY B 306     1966   1672   2538   -188    181    841       C  
ATOM   6183  C   GLY B 306     -49.991 -31.731 147.903  1.00 18.87           C  
ANISOU 6183  C   GLY B 306     2350   2024   2796   -172    217    857       C  
ATOM   6184  O   GLY B 306     -50.827 -31.786 148.808  1.00 18.21           O  
ANISOU 6184  O   GLY B 306     2274   1944   2703   -174    268    901       O  
ATOM   6185  N   VAL B 307     -48.783 -31.140 148.058  1.00 15.34           N  
ANISOU 6185  N   VAL B 307     1940   1592   2296   -155    190    821       N  
ATOM   6186  CA  VAL B 307     -48.355 -30.546 149.328  1.00 15.61           C  
ANISOU 6186  CA  VAL B 307     2030   1645   2256   -138    214    830       C  
ATOM   6187  C   VAL B 307     -49.081 -29.218 149.580  1.00 19.97           C  
ANISOU 6187  C   VAL B 307     2584   2224   2779   -126    267    823       C  
ATOM   6188  O   VAL B 307     -49.022 -28.307 148.742  1.00 19.41           O  
ANISOU 6188  O   VAL B 307     2493   2166   2715   -121    260    783       O  
ATOM   6189  CB  VAL B 307     -46.802 -30.379 149.394  1.00 19.42           C  
ANISOU 6189  CB  VAL B 307     2549   2132   2698   -126    161    794       C  
ATOM   6190  CG1 VAL B 307     -46.377 -29.701 150.698  1.00 19.45           C  
ANISOU 6190  CG1 VAL B 307     2613   2154   2623   -108    181    800       C  
ATOM   6191  CG2 VAL B 307     -46.099 -31.728 149.230  1.00 19.30           C  
ANISOU 6191  CG2 VAL B 307     2533   2088   2711   -135    111    803       C  
ATOM   6192  N   ALA B 308     -49.789 -29.119 150.724  1.00 16.67           N  
ANISOU 6192  N   ALA B 308     2190   1814   2328   -120    323    863       N  
ATOM   6193  CA  ALA B 308     -50.517 -27.904 151.096  1.00 16.49           C  
ANISOU 6193  CA  ALA B 308     2173   1815   2275   -105    379    860       C  
ATOM   6194  C   ALA B 308     -49.551 -26.787 151.500  1.00 19.79           C  
ANISOU 6194  C   ALA B 308     2641   2255   2625    -84    366    819       C  
ATOM   6195  O   ALA B 308     -48.405 -27.066 151.869  1.00 19.08           O  
ANISOU 6195  O   ALA B 308     2588   2160   2500    -80    324    808       O  
ATOM   6196  CB  ALA B 308     -51.478 -28.202 152.236  1.00 17.94           C  
ANISOU 6196  CB  ALA B 308     2372   2001   2442   -103    443    915       C  
ATOM   6197  N   VAL B 309     -50.004 -25.516 151.415  1.00 15.67           N  
ANISOU 6197  N   VAL B 309     2117   1752   2085    -70    400    797       N  
ATOM   6198  CA  VAL B 309     -49.168 -24.373 151.793  1.00 14.93           C  
ANISOU 6198  CA  VAL B 309     2069   1675   1929    -50    389    758       C  
ATOM   6199  C   VAL B 309     -48.742 -24.467 153.269  1.00 18.82           C  
ANISOU 6199  C   VAL B 309     2630   2173   2348    -36    401    778       C  
ATOM   6200  O   VAL B 309     -49.559 -24.803 154.131  1.00 18.87           O  
ANISOU 6200  O   VAL B 309     2649   2181   2339    -32    453    821       O  
ATOM   6201  CB  VAL B 309     -49.853 -22.995 151.462  1.00 18.21           C  
ANISOU 6201  CB  VAL B 309     2470   2107   2342    -37    426    734       C  
ATOM   6202  CG1 VAL B 309     -51.076 -22.752 152.351  1.00 18.49           C  
ANISOU 6202  CG1 VAL B 309     2512   2152   2360    -25    502    770       C  
ATOM   6203  CG2 VAL B 309     -48.853 -21.842 151.582  1.00 17.71           C  
ANISOU 6203  CG2 VAL B 309     2447   2056   2228    -21    401    687       C  
ATOM   6204  N   SER B 310     -47.449 -24.256 153.539  1.00 14.86           N  
ANISOU 6204  N   SER B 310     2170   1673   1805    -29    353    749       N  
ATOM   6205  CA  SER B 310     -46.926 -24.261 154.897  1.00 14.81           C  
ANISOU 6205  CA  SER B 310     2232   1671   1724    -15    355    762       C  
ATOM   6206  C   SER B 310     -47.331 -22.960 155.613  1.00 19.39           C  
ANISOU 6206  C   SER B 310     2850   2270   2246      8    401    748       C  
ATOM   6207  O   SER B 310     -48.107 -22.173 155.062  1.00 18.77           O  
ANISOU 6207  O   SER B 310     2740   2200   2192     12    435    734       O  
ATOM   6208  CB  SER B 310     -45.406 -24.389 154.873  1.00 16.74           C  
ANISOU 6208  CB  SER B 310     2503   1909   1948    -15    283    733       C  
ATOM   6209  OG  SER B 310     -44.809 -23.244 154.287  1.00 21.86           O  
ANISOU 6209  OG  SER B 310     3148   2567   2592     -9    258    681       O  
ATOM   6210  N   SER B 311     -46.787 -22.718 156.833  1.00 16.69           N  
ANISOU 6210  N   SER B 311     2578   1935   1828     26    399    749       N  
ATOM   6211  CA ASER B 311     -47.068 -21.482 157.564  0.50 16.63           C  
ANISOU 6211  CA ASER B 311     2615   1944   1760     50    438    731       C  
ATOM   6212  CA BSER B 311     -47.057 -21.481 157.568  0.50 16.71           C  
ANISOU 6212  CA BSER B 311     2625   1954   1769     50    437    730       C  
ATOM   6213  C   SER B 311     -46.331 -20.301 156.921  1.00 20.64           C  
ANISOU 6213  C   SER B 311     3122   2456   2267     54    399    672       C  
ATOM   6214  O   SER B 311     -46.638 -19.137 157.223  1.00 20.74           O  
ANISOU 6214  O   SER B 311     3158   2478   2245     73    429    649       O  
ATOM   6215  CB ASER B 311     -46.675 -21.622 159.032  0.50 19.64           C  
ANISOU 6215  CB ASER B 311     3074   2329   2057     68    442    748       C  
ATOM   6216  CB BSER B 311     -46.637 -21.625 159.024  0.50 19.95           C  
ANISOU 6216  CB BSER B 311     3114   2368   2097     67    440    747       C  
ATOM   6217  OG ASER B 311     -45.285 -21.853 159.177  0.50 26.24           O  
ANISOU 6217  OG ASER B 311     3942   3158   2871     64    369    727       O  
ATOM   6218  OG BSER B 311     -47.371 -22.656 159.657  0.50 28.10           O  
ANISOU 6218  OG BSER B 311     4150   3398   3128     64    482    806       O  
ATOM   6219  N   VAL B 312     -45.384 -20.597 155.995  1.00 16.76           N  
ANISOU 6219  N   VAL B 312     2599   1953   1815     37    335    648       N  
ATOM   6220  CA  VAL B 312     -44.633 -19.572 155.279  1.00 16.16           C  
ANISOU 6220  CA  VAL B 312     2515   1880   1747     37    297    596       C  
ATOM   6221  C   VAL B 312     -45.501 -18.949 154.165  1.00 20.87           C  
ANISOU 6221  C   VAL B 312     3054   2479   2397     33    326    583       C  
ATOM   6222  O   VAL B 312     -45.521 -19.450 153.031  1.00 20.00           O  
ANISOU 6222  O   VAL B 312     2887   2362   2349     16    306    582       O  
ATOM   6223  CB  VAL B 312     -43.278 -20.123 154.724  1.00 19.14           C  
ANISOU 6223  CB  VAL B 312     2881   2247   2147     23    221    577       C  
ATOM   6224  CG1 VAL B 312     -42.477 -19.014 154.033  1.00 18.40           C  
ANISOU 6224  CG1 VAL B 312     2778   2155   2059     22    184    527       C  
ATOM   6225  CG2 VAL B 312     -42.455 -20.772 155.835  1.00 19.33           C  
ANISOU 6225  CG2 VAL B 312     2959   2265   2119     28    189    593       C  
ATOM   6226  N   HIS B 313     -46.283 -17.916 154.522  1.00 18.07           N  
ANISOU 6226  N   HIS B 313     2714   2134   2017     51    376    576       N  
ATOM   6227  CA  HIS B 313     -47.113 -17.155 153.575  1.00 17.84           C  
ANISOU 6227  CA  HIS B 313     2638   2109   2033     51    405    562       C  
ATOM   6228  C   HIS B 313     -47.587 -15.843 154.238  1.00 21.80           C  
ANISOU 6228  C   HIS B 313     3177   2620   2488     77    448    544       C  
ATOM   6229  O   HIS B 313     -47.692 -15.780 155.465  1.00 22.20           O  
ANISOU 6229  O   HIS B 313     3283   2675   2477     94    475    556       O  
ATOM   6230  CB  HIS B 313     -48.331 -17.996 153.096  1.00 18.48           C  
ANISOU 6230  CB  HIS B 313     2663   2188   2171     40    445    602       C  
ATOM   6231  CG  HIS B 313     -49.329 -18.290 154.172  1.00 22.34           C  
ANISOU 6231  CG  HIS B 313     3174   2684   2632     53    510    643       C  
ATOM   6232  ND1 HIS B 313     -50.324 -17.382 154.502  1.00 24.32           N  
ANISOU 6232  ND1 HIS B 313     3428   2945   2869     73    571    644       N  
ATOM   6233  CD2 HIS B 313     -49.505 -19.414 154.904  1.00 24.56           C  
ANISOU 6233  CD2 HIS B 313     3469   2962   2902     48    523    687       C  
ATOM   6234  CE1 HIS B 313     -51.045 -17.966 155.444  1.00 24.34           C  
ANISOU 6234  CE1 HIS B 313     3448   2952   2849     81    622    688       C  
ATOM   6235  NE2 HIS B 313     -50.588 -19.188 155.725  1.00 24.77           N  
ANISOU 6235  NE2 HIS B 313     3509   2997   2903     65    596    716       N  
ATOM   6236  N   PRO B 314     -47.855 -14.769 153.451  1.00 18.25           N  
ANISOU 6236  N   PRO B 314     2701   2171   2063     81    454    514       N  
ATOM   6237  CA  PRO B 314     -48.309 -13.511 154.074  1.00 18.36           C  
ANISOU 6237  CA  PRO B 314     2751   2190   2034    107    494    495       C  
ATOM   6238  C   PRO B 314     -49.730 -13.616 154.621  1.00 22.46           C  
ANISOU 6238  C   PRO B 314     3265   2718   2551    123    572    530       C  
ATOM   6239  O   PRO B 314     -50.521 -14.423 154.129  1.00 22.22           O  
ANISOU 6239  O   PRO B 314     3182   2688   2572    110    595    564       O  
ATOM   6240  CB  PRO B 314     -48.221 -12.500 152.930  1.00 19.45           C  
ANISOU 6240  CB  PRO B 314     2854   2324   2212    103    476    460       C  
ATOM   6241  CG  PRO B 314     -48.390 -13.311 151.697  1.00 23.63           C  
ANISOU 6241  CG  PRO B 314     3314   2851   2812     79    457    474       C  
ATOM   6242  CD  PRO B 314     -47.760 -14.649 151.978  1.00 19.20           C  
ANISOU 6242  CD  PRO B 314     2759   2286   2248     64    426    497       C  
ATOM   6243  N   GLU B 315     -50.059 -12.794 155.646  1.00 19.36           N  
ANISOU 6243  N   GLU B 315     2925   2331   2099    152    613    522       N  
ATOM   6244  CA  GLU B 315     -51.418 -12.745 156.213  1.00 19.45           C  
ANISOU 6244  CA  GLU B 315     2932   2353   2104    172    694    554       C  
ATOM   6245  C   GLU B 315     -52.398 -12.198 155.164  1.00 21.80           C  
ANISOU 6245  C   GLU B 315     3164   2651   2469    172    722    550       C  
ATOM   6246  O   GLU B 315     -53.483 -12.757 154.976  1.00 21.48           O  
ANISOU 6246  O   GLU B 315     3077   2614   2470    169    768    588       O  
ATOM   6247  CB  GLU B 315     -51.438 -11.868 157.486  1.00 21.50           C  
ANISOU 6247  CB  GLU B 315     3270   2619   2282    206    727    537       C  
ATOM   6248  CG  GLU B 315     -52.817 -11.736 158.121  1.00 35.12           C  
ANISOU 6248  CG  GLU B 315     4993   4355   3997    231    816    568       C  
ATOM   6249  CD  GLU B 315     -52.855 -10.864 159.362  1.00 62.70           C  
ANISOU 6249  CD  GLU B 315     8565   7854   7404    269    852    549       C  
ATOM   6250  OE1 GLU B 315     -52.141 -11.188 160.339  1.00 63.20           O  
ANISOU 6250  OE1 GLU B 315     8694   7919   7401    274    833    551       O  
ATOM   6251  OE2 GLU B 315     -53.661  -9.906 159.388  1.00 59.33           O  
ANISOU 6251  OE2 GLU B 315     8135   7430   6979    294    900    535       O  
ATOM   6252  N   LYS B 316     -51.992 -11.117 154.465  1.00 16.77           N  
ANISOU 6252  N   LYS B 316     2521   2006   1843    174    692    507       N  
ATOM   6253  CA ALYS B 316     -52.797 -10.498 153.408  0.50 15.95           C  
ANISOU 6253  CA ALYS B 316     2358   1901   1799    175    710    500       C  
ATOM   6254  CA BLYS B 316     -52.796 -10.528 153.400  0.50 15.80           C  
ANISOU 6254  CA BLYS B 316     2339   1883   1782    174    710    501       C  
ATOM   6255  C   LYS B 316     -52.032 -10.565 152.083  1.00 18.19           C  
ANISOU 6255  C   LYS B 316     2602   2177   2133    148    644    479       C  
ATOM   6256  O   LYS B 316     -50.811 -10.389 152.072  1.00 16.13           O  
ANISOU 6256  O   LYS B 316     2372   1910   1846    140    589    451       O  
ATOM   6257  CB ALYS B 316     -53.115  -9.021 153.761  0.50 18.61           C  
ANISOU 6257  CB ALYS B 316     2728   2238   2107    206    741    468       C  
ATOM   6258  CB BLYS B 316     -53.198  -9.088 153.759  0.50 18.19           C  
ANISOU 6258  CB BLYS B 316     2672   2185   2056    206    744    472       C  
ATOM   6259  CG ALYS B 316     -53.714  -8.818 155.172  0.50 31.92           C  
ANISOU 6259  CG ALYS B 316     4467   3931   3729    238    805    482       C  
ATOM   6260  CG BLYS B 316     -54.252  -9.011 154.879  0.50 27.58           C  
ANISOU 6260  CG BLYS B 316     3886   3385   3209    236    824    497       C  
ATOM   6261  CD ALYS B 316     -55.154  -9.297 155.259  0.50 40.06           C  
ANISOU 6261  CD ALYS B 316     5452   4973   4794    247    878    527       C  
ATOM   6262  CD BLYS B 316     -54.347  -7.606 155.491  0.50 33.48           C  
ANISOU 6262  CD BLYS B 316     4684   4129   3907    271    849    461       C  
ATOM   6263  CE ALYS B 316     -55.757  -9.038 156.617  0.50 49.09           C  
ANISOU 6263  CE ALYS B 316     6649   6127   5876    281    947    540       C  
ATOM   6264  CE BLYS B 316     -53.241  -7.345 156.493  0.50 41.92           C  
ANISOU 6264  CE BLYS B 316     5838   5194   4895    280    817    434       C  
ATOM   6265  NZ ALYS B 316     -57.177  -9.474 156.679  0.50 55.95           N  
ANISOU 6265  NZ ALYS B 316     7467   7006   6784    289   1021    586       N  
ATOM   6266  NZ BLYS B 316     -53.289  -5.956 157.019  0.50 49.23           N  
ANISOU 6266  NZ BLYS B 316     6815   6114   5776    313    835    394       N  
ATOM   6267  N   VAL B 317     -52.734 -10.844 150.969  1.00 14.71           N  
ANISOU 6267  N   VAL B 317     2092   1735   1761    134    648    493       N  
ATOM   6268  CA  VAL B 317     -52.077 -10.959 149.659  1.00 13.71           C  
ANISOU 6268  CA  VAL B 317     1926   1601   1680    111    589    474       C  
ATOM   6269  C   VAL B 317     -53.026 -10.566 148.513  1.00 16.78           C  
ANISOU 6269  C   VAL B 317     2253   1990   2133    109    604    476       C  
ATOM   6270  O   VAL B 317     -54.246 -10.702 148.645  1.00 15.90           O  
ANISOU 6270  O   VAL B 317     2112   1882   2046    118    655    504       O  
ATOM   6271  CB  VAL B 317     -51.483 -12.398 149.449  1.00 17.31           C  
ANISOU 6271  CB  VAL B 317     2368   2056   2154     84    550    494       C  
ATOM   6272  CG1 VAL B 317     -52.593 -13.420 149.199  1.00 17.37           C  
ANISOU 6272  CG1 VAL B 317     2325   2065   2211     74    581    537       C  
ATOM   6273  CG2 VAL B 317     -50.461 -12.415 148.310  1.00 16.50           C  
ANISOU 6273  CG2 VAL B 317     2244   1947   2077     64    485    467       C  
ATOM   6274  N   ASP B 318     -52.456 -10.090 147.380  1.00 13.07           N  
ANISOU 6274  N   ASP B 318     1761   1515   1690     98    558    449       N  
ATOM   6275  CA  ASP B 318     -53.223  -9.826 146.162  1.00 12.40           C  
ANISOU 6275  CA  ASP B 318     1616   1428   1666     94    560    451       C  
ATOM   6276  C   ASP B 318     -53.920 -11.134 145.725  1.00 16.92           C  
ANISOU 6276  C   ASP B 318     2138   2003   2289     76    565    487       C  
ATOM   6277  O   ASP B 318     -53.274 -12.181 145.663  1.00 17.38           O  
ANISOU 6277  O   ASP B 318     2197   2059   2349     57    531    495       O  
ATOM   6278  CB  ASP B 318     -52.281  -9.316 145.044  1.00 13.06           C  
ANISOU 6278  CB  ASP B 318     1691   1507   1763     82    505    418       C  
ATOM   6279  CG  ASP B 318     -52.995  -8.838 143.790  1.00 19.26           C  
ANISOU 6279  CG  ASP B 318     2424   2290   2602     81    504    416       C  
ATOM   6280  OD1 ASP B 318     -53.763  -9.632 143.208  1.00 20.15           O  
ANISOU 6280  OD1 ASP B 318     2489   2405   2762     71    509    441       O  
ATOM   6281  OD2 ASP B 318     -52.660  -7.743 143.305  1.00 21.80           O  
ANISOU 6281  OD2 ASP B 318     2754   2608   2922     87    489    390       O  
ATOM   6282  N   PRO B 319     -55.267 -11.117 145.521  1.00 13.79           N  
ANISOU 6282  N   PRO B 319     1698   1608   1934     83    607    511       N  
ATOM   6283  CA  PRO B 319     -55.982 -12.387 145.238  1.00 13.86           C  
ANISOU 6283  CA  PRO B 319     1660   1616   1992     65    612    548       C  
ATOM   6284  C   PRO B 319     -55.461 -13.134 144.004  1.00 16.76           C  
ANISOU 6284  C   PRO B 319     1993   1976   2399     39    552    540       C  
ATOM   6285  O   PRO B 319     -55.611 -14.355 143.916  1.00 16.43           O  
ANISOU 6285  O   PRO B 319     1929   1930   2384     21    542    565       O  
ATOM   6286  CB  PRO B 319     -57.438 -11.940 145.063  1.00 16.00           C  
ANISOU 6286  CB  PRO B 319     1886   1889   2304     79    661    567       C  
ATOM   6287  CG  PRO B 319     -57.531 -10.653 145.815  1.00 20.20           C  
ANISOU 6287  CG  PRO B 319     2459   2426   2792    109    700    549       C  
ATOM   6288  CD  PRO B 319     -56.205  -9.982 145.642  1.00 15.41           C  
ANISOU 6288  CD  PRO B 319     1896   1815   2144    109    653    507       C  
ATOM   6289  N   ARG B 320     -54.825 -12.410 143.065  1.00 12.83           N  
ANISOU 6289  N   ARG B 320     1494   1478   1904     38    513    507       N  
ATOM   6290  CA  ARG B 320     -54.281 -13.011 141.843  1.00 12.14           C  
ANISOU 6290  CA  ARG B 320     1377   1385   1848     16    458    496       C  
ATOM   6291  C   ARG B 320     -53.016 -13.844 142.133  1.00 16.65           C  
ANISOU 6291  C   ARG B 320     1981   1955   2392      3    420    489       C  
ATOM   6292  O   ARG B 320     -52.797 -14.868 141.486  1.00 16.14           O  
ANISOU 6292  O   ARG B 320     1892   1885   2357    -15    386    495       O  
ATOM   6293  CB  ARG B 320     -53.971 -11.922 140.798  1.00 10.62           C  
ANISOU 6293  CB  ARG B 320     1177   1194   1664     21    433    465       C  
ATOM   6294  CG  ARG B 320     -55.199 -11.137 140.350  1.00 14.73           C  
ANISOU 6294  CG  ARG B 320     1662   1714   2218     35    463    472       C  
ATOM   6295  CD  ARG B 320     -54.818  -9.905 139.548  1.00 19.25           C  
ANISOU 6295  CD  ARG B 320     2240   2287   2788     43    444    442       C  
ATOM   6296  NE  ARG B 320     -54.168  -8.889 140.382  1.00 18.56           N  
ANISOU 6296  NE  ARG B 320     2203   2199   2648     58    457    421       N  
ATOM   6297  CZ  ARG B 320     -53.873  -7.665 139.960  1.00 26.19           C  
ANISOU 6297  CZ  ARG B 320     3182   3163   3607     68    448    397       C  
ATOM   6298  NH1 ARG B 320     -54.160  -7.298 138.720  1.00 12.82           N  
ANISOU 6298  NH1 ARG B 320     1454   1469   1950     66    429    392       N  
ATOM   6299  NH2 ARG B 320     -53.291  -6.797 140.777  1.00 11.07           N  
ANISOU 6299  NH2 ARG B 320     1316   1245   1646     81    458    377       N  
ATOM   6300  N   ALA B 321     -52.176 -13.387 143.105  1.00 13.92           N  
ANISOU 6300  N   ALA B 321     1688   1611   1988     12    422    475       N  
ATOM   6301  CA  ALA B 321     -50.877 -14.023 143.415  1.00 13.43           C  
ANISOU 6301  CA  ALA B 321     1658   1547   1897      2    383    466       C  
ATOM   6302  C   ALA B 321     -50.968 -15.565 143.669  1.00 16.33           C  
ANISOU 6302  C   ALA B 321     2015   1909   2282    -13    375    496       C  
ATOM   6303  O   ALA B 321     -50.251 -16.324 143.020  1.00 15.51           O  
ANISOU 6303  O   ALA B 321     1899   1799   2195    -28    331    489       O  
ATOM   6304  CB  ALA B 321     -50.211 -13.324 144.596  1.00 14.35           C  
ANISOU 6304  CB  ALA B 321     1835   1666   1951     16    392    452       C  
ATOM   6305  N   PRO B 322     -51.873 -16.057 144.589  1.00 12.89           N  
ANISOU 6305  N   PRO B 322     1581   1472   1844     -9    420    531       N  
ATOM   6306  CA  PRO B 322     -51.946 -17.516 144.824  1.00 12.00           C  
ANISOU 6306  CA  PRO B 322     1458   1352   1751    -26    412    562       C  
ATOM   6307  C   PRO B 322     -52.556 -18.280 143.640  1.00 15.33           C  
ANISOU 6307  C   PRO B 322     1820   1763   2240    -43    393    572       C  
ATOM   6308  O   PRO B 322     -52.498 -19.510 143.607  1.00 15.67           O  
ANISOU 6308  O   PRO B 322     1852   1796   2307    -59    375    592       O  
ATOM   6309  CB  PRO B 322     -52.820 -17.633 146.094  1.00 14.30           C  
ANISOU 6309  CB  PRO B 322     1767   1646   2021    -15    472    597       C  
ATOM   6310  CG  PRO B 322     -52.910 -16.229 146.647  1.00 19.11           C  
ANISOU 6310  CG  PRO B 322     2408   2266   2586     10    504    578       C  
ATOM   6311  CD  PRO B 322     -52.789 -15.324 145.480  1.00 14.74           C  
ANISOU 6311  CD  PRO B 322     1829   1713   2056     11    480    545       C  
ATOM   6312  N   LYS B 323     -53.143 -17.554 142.668  1.00 11.40           N  
ANISOU 6312  N   LYS B 323     1288   1270   1775    -40    394    558       N  
ATOM   6313  CA  LYS B 323     -53.684 -18.179 141.459  1.00 11.16           C  
ANISOU 6313  CA  LYS B 323     1203   1230   1806    -56    370    563       C  
ATOM   6314  C   LYS B 323     -52.642 -18.204 140.334  1.00 14.68           C  
ANISOU 6314  C   LYS B 323     1647   1675   2256    -63    312    528       C  
ATOM   6315  O   LYS B 323     -52.656 -19.113 139.502  1.00 14.19           O  
ANISOU 6315  O   LYS B 323     1557   1603   2233    -77    279    529       O  
ATOM   6316  CB  LYS B 323     -54.971 -17.486 141.007  1.00 13.63           C  
ANISOU 6316  CB  LYS B 323     1476   1547   2156    -48    401    571       C  
ATOM   6317  CG  LYS B 323     -56.150 -17.766 141.931  1.00 24.15           C  
ANISOU 6317  CG  LYS B 323     2795   2878   3502    -45    457    612       C  
ATOM   6318  CD  LYS B 323     -57.463 -17.354 141.312  1.00 35.14           C  
ANISOU 6318  CD  LYS B 323     4134   4270   4946    -42    480    623       C  
ATOM   6319  CE  LYS B 323     -58.644 -17.741 142.176  1.00 48.58           C  
ANISOU 6319  CE  LYS B 323     5815   5972   6670    -40    537    667       C  
ATOM   6320  NZ  LYS B 323     -58.758 -19.218 142.336  1.00 61.61           N  
ANISOU 6320  NZ  LYS B 323     7450   7608   8351    -64    524    698       N  
ATOM   6321  N   ILE B 324     -51.680 -17.264 140.366  1.00 10.47           N  
ANISOU 6321  N   ILE B 324     1146   1150   1681    -52    300    498       N  
ATOM   6322  CA  ILE B 324     -50.557 -17.287 139.430  1.00  9.79           C  
ANISOU 6322  CA  ILE B 324     1062   1064   1593    -58    250    467       C  
ATOM   6323  C   ILE B 324     -49.489 -18.276 139.927  1.00 14.55           C  
ANISOU 6323  C   ILE B 324     1691   1661   2176    -66    222    468       C  
ATOM   6324  O   ILE B 324     -49.045 -19.135 139.168  1.00 14.83           O  
ANISOU 6324  O   ILE B 324     1710   1690   2236    -76    184    461       O  
ATOM   6325  CB  ILE B 324     -49.959 -15.859 139.217  1.00 12.29           C  
ANISOU 6325  CB  ILE B 324     1399   1391   1879    -46    248    437       C  
ATOM   6326  CG1 ILE B 324     -51.053 -14.850 138.774  1.00 12.18           C  
ANISOU 6326  CG1 ILE B 324     1361   1382   1886    -36    277    438       C  
ATOM   6327  CG2 ILE B 324     -48.786 -15.902 138.208  1.00 13.69           C  
ANISOU 6327  CG2 ILE B 324     1575   1570   2058    -52    200    408       C  
ATOM   6328  CD1 ILE B 324     -50.576 -13.366 138.711  1.00 17.86           C  
ANISOU 6328  CD1 ILE B 324     2103   2107   2575    -22    281    411       C  
ATOM   6329  N   PHE B 325     -49.090 -18.158 141.222  1.00 10.48           N  
ANISOU 6329  N   PHE B 325     1217   1148   1616    -59    239    475       N  
ATOM   6330  CA  PHE B 325     -48.037 -19.001 141.790  1.00  9.42           C  
ANISOU 6330  CA  PHE B 325     1111   1008   1459    -64    211    477       C  
ATOM   6331  C   PHE B 325     -48.563 -19.903 142.899  1.00 12.86           C  
ANISOU 6331  C   PHE B 325     1560   1436   1889    -67    236    514       C  
ATOM   6332  O   PHE B 325     -49.123 -19.414 143.887  1.00 12.50           O  
ANISOU 6332  O   PHE B 325     1537   1397   1816    -56    279    530       O  
ATOM   6333  CB  PHE B 325     -46.865 -18.144 142.314  1.00 10.60           C  
ANISOU 6333  CB  PHE B 325     1304   1166   1559    -55    197    451       C  
ATOM   6334  CG  PHE B 325     -46.339 -17.137 141.323  1.00 10.99           C  
ANISOU 6334  CG  PHE B 325     1342   1222   1611    -52    178    417       C  
ATOM   6335  CD1 PHE B 325     -45.468 -17.523 140.311  1.00 12.86           C  
ANISOU 6335  CD1 PHE B 325     1562   1458   1868    -60    135    398       C  
ATOM   6336  CD2 PHE B 325     -46.677 -15.792 141.427  1.00 12.77           C  
ANISOU 6336  CD2 PHE B 325     1577   1454   1820    -41    203    405       C  
ATOM   6337  CE1 PHE B 325     -44.981 -16.591 139.392  1.00 13.53           C  
ANISOU 6337  CE1 PHE B 325     1637   1550   1955    -58    120    371       C  
ATOM   6338  CE2 PHE B 325     -46.171 -14.854 140.520  1.00 15.21           C  
ANISOU 6338  CE2 PHE B 325     1878   1768   2133    -40    185    377       C  
ATOM   6339  CZ  PHE B 325     -45.332 -15.258 139.506  1.00 12.87           C  
ANISOU 6339  CZ  PHE B 325     1562   1472   1855    -49    144    362       C  
ATOM   6340  N   GLN B 326     -48.315 -21.213 142.778  1.00  8.92           N  
ANISOU 6340  N   GLN B 326     1052    925   1414    -80    210    528       N  
ATOM   6341  CA  GLN B 326     -48.663 -22.179 143.816  1.00  9.48           C  
ANISOU 6341  CA  GLN B 326     1137    985   1478    -84    228    566       C  
ATOM   6342  C   GLN B 326     -47.474 -22.344 144.806  1.00 15.70           C  
ANISOU 6342  C   GLN B 326     1977   1774   2215    -78    209    563       C  
ATOM   6343  O   GLN B 326     -46.359 -21.898 144.510  1.00 15.19           O  
ANISOU 6343  O   GLN B 326     1927   1714   2131    -74    175    530       O  
ATOM   6344  CB  GLN B 326     -49.044 -23.535 143.186  1.00 10.38           C  
ANISOU 6344  CB  GLN B 326     1215   1080   1648   -101    207    585       C  
ATOM   6345  CG  GLN B 326     -47.920 -24.175 142.369  1.00 19.48           C  
ANISOU 6345  CG  GLN B 326     2364   2224   2814   -107    149    559       C  
ATOM   6346  CD  GLN B 326     -48.342 -25.499 141.775  1.00 28.60           C  
ANISOU 6346  CD  GLN B 326     3486   3357   4023   -123    128    575       C  
ATOM   6347  OE1 GLN B 326     -49.483 -25.956 141.946  1.00 20.96           O  
ANISOU 6347  OE1 GLN B 326     2496   2381   3088   -132    155    607       O  
ATOM   6348  NE2 GLN B 326     -47.421 -26.158 141.086  1.00 16.50           N  
ANISOU 6348  NE2 GLN B 326     1950   1815   2504   -126     80    554       N  
ATOM   6349  N   PRO B 327     -47.687 -22.994 145.988  1.00 13.60           N  
ANISOU 6349  N   PRO B 327     1738   1503   1927    -78    231    597       N  
ATOM   6350  CA  PRO B 327     -46.580 -23.115 146.962  1.00 13.58           C  
ANISOU 6350  CA  PRO B 327     1787   1500   1872    -71    210    595       C  
ATOM   6351  C   PRO B 327     -45.435 -23.997 146.459  1.00 17.50           C  
ANISOU 6351  C   PRO B 327     2279   1985   2385    -79    151    581       C  
ATOM   6352  O   PRO B 327     -45.582 -24.697 145.448  1.00 16.10           O  
ANISOU 6352  O   PRO B 327     2062   1796   2259    -90    130    579       O  
ATOM   6353  CB  PRO B 327     -47.260 -23.728 148.201  1.00 15.72           C  
ANISOU 6353  CB  PRO B 327     2082   1768   2123    -69    249    641       C  
ATOM   6354  CG  PRO B 327     -48.728 -23.519 147.983  1.00 20.13           C  
ANISOU 6354  CG  PRO B 327     2605   2329   2714    -72    300    662       C  
ATOM   6355  CD  PRO B 327     -48.941 -23.555 146.522  1.00 15.06           C  
ANISOU 6355  CD  PRO B 327     1910   1682   2131    -83    276    641       C  
ATOM   6356  N   GLY B 328     -44.312 -23.977 147.190  1.00 14.64           N  
ANISOU 6356  N   GLY B 328     1960   1625   1980    -72    124    573       N  
ATOM   6357  CA  GLY B 328     -43.155 -24.814 146.890  1.00 14.28           C  
ANISOU 6357  CA  GLY B 328     1914   1568   1946    -76     70    562       C  
ATOM   6358  C   GLY B 328     -43.510 -26.281 146.761  1.00 18.54           C  
ANISOU 6358  C   GLY B 328     2433   2085   2525    -88     61    593       C  
ATOM   6359  O   GLY B 328     -44.279 -26.812 147.569  1.00 19.35           O  
ANISOU 6359  O   GLY B 328     2548   2182   2624    -91     92    632       O  
ATOM   6360  N   ILE B 329     -42.987 -26.937 145.725  1.00 13.66           N  
ANISOU 6360  N   ILE B 329     1785   1456   1949    -94     20    575       N  
ATOM   6361  CA  ILE B 329     -43.327 -28.329 145.430  1.00 13.11           C  
ANISOU 6361  CA  ILE B 329     1694   1363   1926   -106      7    599       C  
ATOM   6362  C   ILE B 329     -42.850 -29.310 146.538  1.00 18.68           C  
ANISOU 6362  C   ILE B 329     2434   2053   2611   -105     -8    630       C  
ATOM   6363  O   ILE B 329     -43.458 -30.368 146.722  1.00 18.60           O  
ANISOU 6363  O   ILE B 329     2416   2022   2630   -115     -2    664       O  
ATOM   6364  CB  ILE B 329     -42.809 -28.735 144.007  1.00 15.02           C  
ANISOU 6364  CB  ILE B 329     1899   1597   2213   -109    -35    566       C  
ATOM   6365  CG1 ILE B 329     -43.467 -30.055 143.521  1.00 14.89           C  
ANISOU 6365  CG1 ILE B 329     1854   1553   2251   -122    -45    588       C  
ATOM   6366  CG2 ILE B 329     -41.260 -28.805 143.967  1.00 15.44           C  
ANISOU 6366  CG2 ILE B 329     1969   1651   2248    -99    -81    540       C  
ATOM   6367  CD1 ILE B 329     -43.236 -30.376 142.025  1.00 16.08           C  
ANISOU 6367  CD1 ILE B 329     1967   1696   2446   -124    -79    555       C  
ATOM   6368  N   GLU B 330     -41.797 -28.931 147.300  1.00 15.68           N  
ANISOU 6368  N   GLU B 330     2094   1681   2181    -93    -27    619       N  
ATOM   6369  CA  GLU B 330     -41.207 -29.828 148.299  1.00 15.85           C  
ANISOU 6369  CA  GLU B 330     2151   1689   2182    -91    -48    646       C  
ATOM   6370  C   GLU B 330     -41.815 -29.650 149.712  1.00 19.27           C  
ANISOU 6370  C   GLU B 330     2627   2128   2566    -87     -7    684       C  
ATOM   6371  O   GLU B 330     -42.222 -30.636 150.323  1.00 19.01           O  
ANISOU 6371  O   GLU B 330     2606   2079   2540    -93      3    725       O  
ATOM   6372  CB  GLU B 330     -39.674 -29.672 148.338  1.00 17.18           C  
ANISOU 6372  CB  GLU B 330     2337   1861   2329    -80    -99    616       C  
ATOM   6373  CG  GLU B 330     -38.979 -30.712 149.206  1.00 28.24           C  
ANISOU 6373  CG  GLU B 330     3769   3244   3717    -77   -131    641       C  
ATOM   6374  CD  GLU B 330     -37.470 -30.572 149.272  1.00 46.85           C  
ANISOU 6374  CD  GLU B 330     6140   5604   6058    -66   -183    613       C  
ATOM   6375  OE1 GLU B 330     -36.985 -29.435 149.476  1.00 37.78           O  
ANISOU 6375  OE1 GLU B 330     5008   4475   4872    -58   -185    588       O  
ATOM   6376  OE2 GLU B 330     -36.774 -31.609 149.184  1.00 39.71           O  
ANISOU 6376  OE2 GLU B 330     5230   4679   5177    -64   -223    618       O  
ATOM   6377  N   ASN B 331     -41.804 -28.402 150.259  1.00 15.16           N  
ANISOU 6377  N   ASN B 331     2136   1631   1994    -76     17    669       N  
ATOM   6378  CA  ASN B 331     -42.250 -28.170 151.653  1.00 14.85           C  
ANISOU 6378  CA  ASN B 331     2145   1599   1898    -67     55    700       C  
ATOM   6379  C   ASN B 331     -43.504 -27.254 151.771  1.00 18.41           C  
ANISOU 6379  C   ASN B 331     2590   2066   2338    -65    119    707       C  
ATOM   6380  O   ASN B 331     -43.990 -27.015 152.879  1.00 17.88           O  
ANISOU 6380  O   ASN B 331     2561   2006   2224    -56    158    733       O  
ATOM   6381  CB  ASN B 331     -41.090 -27.632 152.517  1.00 14.60           C  
ANISOU 6381  CB  ASN B 331     2167   1577   1805    -53     24    683       C  
ATOM   6382  CG  ASN B 331     -40.590 -26.255 152.109  1.00 21.59           C  
ANISOU 6382  CG  ASN B 331     3052   2480   2672    -46     15    635       C  
ATOM   6383  OD1 ASN B 331     -41.018 -25.677 151.107  1.00 15.72           O  
ANISOU 6383  OD1 ASN B 331     2268   1743   1962    -50     29    613       O  
ATOM   6384  ND2 ASN B 331     -39.675 -25.708 152.889  1.00 12.39           N  
ANISOU 6384  ND2 ASN B 331     1932   1322   1454    -34    -11    619       N  
ATOM   6385  N   GLY B 332     -43.992 -26.755 150.638  1.00 14.58           N  
ANISOU 6385  N   GLY B 332     2058   1586   1896    -71    128    684       N  
ATOM   6386  CA  GLY B 332     -45.200 -25.933 150.602  1.00 14.15           C  
ANISOU 6386  CA  GLY B 332     1990   1545   1843    -68    185    689       C  
ATOM   6387  C   GLY B 332     -44.987 -24.477 150.996  1.00 17.55           C  
ANISOU 6387  C   GLY B 332     2451   1995   2221    -51    201    660       C  
ATOM   6388  O   GLY B 332     -45.958 -23.748 151.219  1.00 16.57           O  
ANISOU 6388  O   GLY B 332     2326   1883   2087    -44    253    666       O  
ATOM   6389  N   ASP B 333     -43.713 -24.034 151.084  1.00 13.55           N  
ANISOU 6389  N   ASP B 333     1971   1493   1683    -44    156    626       N  
ATOM   6390  CA  ASP B 333     -43.419 -22.627 151.384  1.00 12.56           C  
ANISOU 6390  CA  ASP B 333     1875   1383   1513    -30    163    594       C  
ATOM   6391  C   ASP B 333     -43.856 -21.738 150.233  1.00 14.54           C  
ANISOU 6391  C   ASP B 333     2082   1641   1800    -33    175    566       C  
ATOM   6392  O   ASP B 333     -43.560 -22.037 149.072  1.00 12.56           O  
ANISOU 6392  O   ASP B 333     1790   1385   1598    -44    145    550       O  
ATOM   6393  CB  ASP B 333     -41.918 -22.423 151.667  1.00 14.36           C  
ANISOU 6393  CB  ASP B 333     2136   1611   1709    -26    106    566       C  
ATOM   6394  CG  ASP B 333     -41.442 -22.974 152.998  1.00 22.62           C  
ANISOU 6394  CG  ASP B 333     3238   2653   2704    -19     94    590       C  
ATOM   6395  OD1 ASP B 333     -42.285 -23.486 153.766  1.00 23.44           O  
ANISOU 6395  OD1 ASP B 333     3360   2756   2791    -16    135    629       O  
ATOM   6396  OD2 ASP B 333     -40.232 -22.863 153.284  1.00 29.13           O  
ANISOU 6396  OD2 ASP B 333     4089   3476   3504    -15     44    570       O  
ATOM   6397  N   TRP B 334     -44.599 -20.672 150.537  1.00 11.31           N  
ANISOU 6397  N   TRP B 334     1685   1243   1368    -21    219    561       N  
ATOM   6398  CA  TRP B 334     -45.003 -19.719 149.524  1.00 10.76           C  
ANISOU 6398  CA  TRP B 334     1579   1180   1328    -21    230    535       C  
ATOM   6399  C   TRP B 334     -44.223 -18.440 149.694  1.00 15.01           C  
ANISOU 6399  C   TRP B 334     2149   1726   1828    -11    213    496       C  
ATOM   6400  O   TRP B 334     -44.618 -17.570 150.475  1.00 14.67           O  
ANISOU 6400  O   TRP B 334     2141   1690   1744      5    247    493       O  
ATOM   6401  CB  TRP B 334     -46.515 -19.454 149.583  1.00  9.76           C  
ANISOU 6401  CB  TRP B 334     1433   1058   1216    -16    293    557       C  
ATOM   6402  CG  TRP B 334     -47.065 -18.842 148.327  1.00 10.59           C  
ANISOU 6402  CG  TRP B 334     1488   1167   1370    -20    299    539       C  
ATOM   6403  CD1 TRP B 334     -47.537 -19.502 147.233  1.00 13.35           C  
ANISOU 6403  CD1 TRP B 334     1783   1509   1780    -35    290    547       C  
ATOM   6404  CD2 TRP B 334     -47.176 -17.441 148.032  1.00 10.51           C  
ANISOU 6404  CD2 TRP B 334     1480   1165   1348     -9    312    509       C  
ATOM   6405  NE1 TRP B 334     -47.958 -18.601 146.280  1.00 12.76           N  
ANISOU 6405  NE1 TRP B 334     1676   1440   1731    -33    297    525       N  
ATOM   6406  CE2 TRP B 334     -47.763 -17.328 146.751  1.00 14.05           C  
ANISOU 6406  CE2 TRP B 334     1873   1612   1853    -17    312    503       C  
ATOM   6407  CE3 TRP B 334     -46.899 -16.266 148.754  1.00 12.17           C  
ANISOU 6407  CE3 TRP B 334     1734   1381   1507      8    324    488       C  
ATOM   6408  CZ2 TRP B 334     -48.034 -16.089 146.157  1.00 12.92           C  
ANISOU 6408  CZ2 TRP B 334     1718   1476   1717     -9    323    478       C  
ATOM   6409  CZ3 TRP B 334     -47.171 -15.041 148.164  1.00 13.58           C  
ANISOU 6409  CZ3 TRP B 334     1901   1564   1695     16    335    462       C  
ATOM   6410  CH2 TRP B 334     -47.732 -14.962 146.881  1.00 13.69           C  
ANISOU 6410  CH2 TRP B 334     1859   1578   1765      8    335    459       C  
ATOM   6411  N   LYS B 335     -43.032 -18.391 149.100  1.00 11.97           N  
ANISOU 6411  N   LYS B 335     1758   1338   1453    -18    160    468       N  
ATOM   6412  CA  LYS B 335     -42.171 -17.223 149.164  1.00 11.66           C  
ANISOU 6412  CA  LYS B 335     1743   1303   1386    -12    136    431       C  
ATOM   6413  C   LYS B 335     -41.443 -17.030 147.837  1.00 15.92           C  
ANISOU 6413  C   LYS B 335     2240   1842   1968    -23     98    404       C  
ATOM   6414  O   LYS B 335     -41.318 -17.978 147.048  1.00 14.38           O  
ANISOU 6414  O   LYS B 335     2008   1642   1813    -34     79    412       O  
ATOM   6415  CB  LYS B 335     -41.159 -17.342 150.332  1.00 13.25           C  
ANISOU 6415  CB  LYS B 335     1999   1501   1534     -6    105    429       C  
ATOM   6416  CG  LYS B 335     -40.144 -18.474 150.164  1.00 17.24           C  
ANISOU 6416  CG  LYS B 335     2495   2000   2057    -16     54    434       C  
ATOM   6417  CD  LYS B 335     -39.047 -18.406 151.230  1.00 19.98           C  
ANISOU 6417  CD  LYS B 335     2894   2343   2353    -10     15    426       C  
ATOM   6418  CE  LYS B 335     -38.011 -19.506 151.064  1.00 21.97           C  
ANISOU 6418  CE  LYS B 335     3134   2586   2625    -18    -37    432       C  
ATOM   6419  NZ  LYS B 335     -38.575 -20.855 151.359  1.00 19.01           N  
ANISOU 6419  NZ  LYS B 335     2757   2205   2262    -21    -22    472       N  
ATOM   6420  N   GLY B 336     -41.013 -15.801 147.578  1.00 13.26           N  
ANISOU 6420  N   GLY B 336     1910   1508   1621    -20     89    373       N  
ATOM   6421  CA  GLY B 336     -40.300 -15.470 146.361  1.00 12.91           C  
ANISOU 6421  CA  GLY B 336     1829   1464   1612    -29     58    348       C  
ATOM   6422  C   GLY B 336     -38.847 -15.883 146.401  1.00 18.10           C  
ANISOU 6422  C   GLY B 336     2493   2119   2267    -36      4    336       C  
ATOM   6423  O   GLY B 336     -38.194 -15.776 147.445  1.00 18.46           O  
ANISOU 6423  O   GLY B 336     2581   2161   2273    -31    -16    333       O  
ATOM   6424  N   LEU B 337     -38.327 -16.369 145.267  1.00 14.18           N  
ANISOU 6424  N   LEU B 337     1954   1622   1813    -45    -22    329       N  
ATOM   6425  CA  LEU B 337     -36.927 -16.751 145.149  1.00 13.57           C  
ANISOU 6425  CA  LEU B 337     1873   1542   1741    -50    -72    316       C  
ATOM   6426  C   LEU B 337     -36.051 -15.502 144.991  1.00 16.86           C  
ANISOU 6426  C   LEU B 337     2296   1961   2149    -52    -93    287       C  
ATOM   6427  O   LEU B 337     -36.268 -14.711 144.067  1.00 16.12           O  
ANISOU 6427  O   LEU B 337     2176   1872   2076    -55    -80    273       O  
ATOM   6428  CB  LEU B 337     -36.734 -17.708 143.934  1.00 13.22           C  
ANISOU 6428  CB  LEU B 337     1781   1497   1745    -57    -87    318       C  
ATOM   6429  CG  LEU B 337     -35.278 -18.137 143.619  1.00 16.95           C  
ANISOU 6429  CG  LEU B 337     2240   1967   2231    -60   -136    304       C  
ATOM   6430  CD1 LEU B 337     -34.666 -18.883 144.782  1.00 16.95           C  
ANISOU 6430  CD1 LEU B 337     2274   1960   2207    -57   -163    317       C  
ATOM   6431  CD2 LEU B 337     -35.224 -18.996 142.367  1.00 16.69           C  
ANISOU 6431  CD2 LEU B 337     2163   1935   2244    -63   -144    303       C  
ATOM   6432  N   VAL B 338     -35.091 -15.295 145.925  1.00 13.77           N  
ANISOU 6432  N   VAL B 338     1939   1566   1727    -51   -125    278       N  
ATOM   6433  CA  VAL B 338     -34.151 -14.163 145.836  1.00 13.70           C  
ANISOU 6433  CA  VAL B 338     1935   1556   1715    -55   -151    251       C  
ATOM   6434  C   VAL B 338     -33.399 -14.234 144.505  1.00 16.08           C  
ANISOU 6434  C   VAL B 338     2185   1862   2063    -64   -172    239       C  
ATOM   6435  O   VAL B 338     -32.946 -15.310 144.113  1.00 15.69           O  
ANISOU 6435  O   VAL B 338     2112   1813   2037    -66   -191    247       O  
ATOM   6436  CB  VAL B 338     -33.183 -14.110 147.053  1.00 18.08           C  
ANISOU 6436  CB  VAL B 338     2533   2103   2232    -53   -191    245       C  
ATOM   6437  CG1 VAL B 338     -32.189 -12.959 146.910  1.00 18.20           C  
ANISOU 6437  CG1 VAL B 338     2549   2115   2251    -60   -222    217       C  
ATOM   6438  CG2 VAL B 338     -33.960 -13.991 148.362  1.00 18.11           C  
ANISOU 6438  CG2 VAL B 338     2593   2105   2184    -41   -167    256       C  
ATOM   6439  N   TYR B 339     -33.391 -13.131 143.756  1.00 11.59           N  
ANISOU 6439  N   TYR B 339     1599   1295   1508    -69   -162    222       N  
ATOM   6440  CA  TYR B 339     -32.947 -13.131 142.370  1.00 11.26           C  
ANISOU 6440  CA  TYR B 339     1509   1260   1508    -76   -169    214       C  
ATOM   6441  C   TYR B 339     -31.446 -12.877 142.188  1.00 16.64           C  
ANISOU 6441  C   TYR B 339     2177   1941   2205    -84   -211    199       C  
ATOM   6442  O   TYR B 339     -30.893 -11.936 142.761  1.00 16.51           O  
ANISOU 6442  O   TYR B 339     2183   1918   2173    -88   -228    186       O  
ATOM   6443  CB  TYR B 339     -33.778 -12.119 141.535  1.00 11.40           C  
ANISOU 6443  CB  TYR B 339     1512   1281   1537    -76   -135    209       C  
ATOM   6444  CG  TYR B 339     -33.329 -12.003 140.096  1.00 10.52           C  
ANISOU 6444  CG  TYR B 339     1354   1177   1463    -83   -139    201       C  
ATOM   6445  CD1 TYR B 339     -33.750 -12.917 139.138  1.00 12.24           C  
ANISOU 6445  CD1 TYR B 339     1541   1403   1708    -80   -129    210       C  
ATOM   6446  CD2 TYR B 339     -32.530 -10.943 139.678  1.00 10.22           C  
ANISOU 6446  CD2 TYR B 339     1308   1140   1436    -91   -152    186       C  
ATOM   6447  CE1 TYR B 339     -33.341 -12.814 137.810  1.00 12.71           C  
ANISOU 6447  CE1 TYR B 339     1562   1470   1795    -84   -131    203       C  
ATOM   6448  CE2 TYR B 339     -32.112 -10.830 138.355  1.00 10.33           C  
ANISOU 6448  CE2 TYR B 339     1282   1163   1482    -95   -153    182       C  
ATOM   6449  CZ  TYR B 339     -32.508 -11.776 137.426  1.00 15.09           C  
ANISOU 6449  CZ  TYR B 339     1855   1774   2104    -91   -142    189       C  
ATOM   6450  OH  TYR B 339     -32.098 -11.670 136.121  1.00 11.99           O  
ANISOU 6450  OH  TYR B 339     1427   1391   1737    -93   -141    185       O  
ATOM   6451  N   GLY B 340     -30.827 -13.684 141.322  1.00 13.67           N  
ANISOU 6451  N   GLY B 340     1762   1570   1861    -86   -226    200       N  
ATOM   6452  CA  GLY B 340     -29.506 -13.420 140.769  1.00 13.63           C  
ANISOU 6452  CA  GLY B 340     1729   1569   1882    -93   -256    188       C  
ATOM   6453  C   GLY B 340     -28.309 -13.679 141.668  1.00 16.92           C  
ANISOU 6453  C   GLY B 340     2158   1978   2291    -95   -301    184       C  
ATOM   6454  O   GLY B 340     -27.301 -12.986 141.549  1.00 16.38           O  
ANISOU 6454  O   GLY B 340     2078   1908   2236   -103   -326    172       O  
ATOM   6455  N   PRO B 341     -28.287 -14.791 142.447  1.00 13.72           N  
ANISOU 6455  N   PRO B 341     1771   1568   1872    -87   -317    196       N  
ATOM   6456  CA  PRO B 341     -27.038 -15.161 143.123  1.00 13.56           C  
ANISOU 6456  CA  PRO B 341     1755   1542   1853    -88   -366    194       C  
ATOM   6457  C   PRO B 341     -26.068 -15.815 142.123  1.00 17.71           C  
ANISOU 6457  C   PRO B 341     2231   2074   2424    -87   -383    191       C  
ATOM   6458  O   PRO B 341     -26.455 -16.081 140.979  1.00 17.47           O  
ANISOU 6458  O   PRO B 341     2168   2052   2417    -85   -357    191       O  
ATOM   6459  CB  PRO B 341     -27.500 -16.153 144.178  1.00 15.15           C  
ANISOU 6459  CB  PRO B 341     1993   1737   2025    -79   -370    211       C  
ATOM   6460  CG  PRO B 341     -28.666 -16.837 143.556  1.00 19.32           C  
ANISOU 6460  CG  PRO B 341     2510   2269   2562    -74   -330    225       C  
ATOM   6461  CD  PRO B 341     -29.339 -15.817 142.647  1.00 15.00           C  
ANISOU 6461  CD  PRO B 341     1945   1729   2024    -79   -294    215       C  
ATOM   6462  N   LYS B 342     -24.825 -16.086 142.545  1.00 13.96           N  
ANISOU 6462  N   LYS B 342     1749   1596   1961    -88   -428    187       N  
ATOM   6463  CA  LYS B 342     -23.863 -16.783 141.683  1.00 13.42           C  
ANISOU 6463  CA  LYS B 342     1632   1533   1935    -84   -444    185       C  
ATOM   6464  C   LYS B 342     -24.387 -18.193 141.329  1.00 17.03           C  
ANISOU 6464  C   LYS B 342     2080   1989   2400    -71   -431    197       C  
ATOM   6465  O   LYS B 342     -25.068 -18.819 142.145  1.00 16.91           O  
ANISOU 6465  O   LYS B 342     2100   1966   2359    -66   -430    211       O  
ATOM   6466  CB  LYS B 342     -22.482 -16.861 142.356  1.00 15.82           C  
ANISOU 6466  CB  LYS B 342     1931   1830   2250    -86   -497    182       C  
ATOM   6467  CG  LYS B 342     -21.804 -15.498 142.509  1.00 23.97           C  
ANISOU 6467  CG  LYS B 342     2961   2861   3287   -101   -514    168       C  
ATOM   6468  CD  LYS B 342     -20.433 -15.614 143.151  1.00 29.98           C  
ANISOU 6468  CD  LYS B 342     3713   3615   4064   -104   -570    165       C  
ATOM   6469  CE  LYS B 342     -19.791 -14.260 143.342  1.00 33.21           C  
ANISOU 6469  CE  LYS B 342     4120   4019   4480   -121   -591    152       C  
ATOM   6470  NZ  LYS B 342     -18.465 -14.366 144.001  1.00 36.48           N  
ANISOU 6470  NZ  LYS B 342     4523   4425   4912   -125   -650    149       N  
ATOM   6471  N   ALA B 343     -24.136 -18.649 140.077  1.00 12.94           N  
ANISOU 6471  N   ALA B 343     1519   1480   1917    -65   -419    193       N  
ATOM   6472  CA  ALA B 343     -24.680 -19.919 139.550  1.00 12.29           C  
ANISOU 6472  CA  ALA B 343     1426   1395   1847    -53   -407    200       C  
ATOM   6473  C   ALA B 343     -24.489 -21.112 140.507  1.00 16.19           C  
ANISOU 6473  C   ALA B 343     1941   1875   2335    -44   -436    214       C  
ATOM   6474  O   ALA B 343     -25.377 -21.955 140.611  1.00 15.56           O  
ANISOU 6474  O   ALA B 343     1876   1788   2248    -39   -423    227       O  
ATOM   6475  CB  ALA B 343     -24.064 -20.232 138.195  1.00 12.90           C  
ANISOU 6475  CB  ALA B 343     1456   1484   1963    -45   -401    189       C  
ATOM   6476  N   GLU B 344     -23.327 -21.182 141.205  1.00 13.01           N  
ANISOU 6476  N   GLU B 344     1538   1467   1936    -43   -479    213       N  
ATOM   6477  CA  GLU B 344     -23.038 -22.294 142.127  1.00 12.72           C  
ANISOU 6477  CA  GLU B 344     1522   1417   1894    -33   -512    227       C  
ATOM   6478  C   GLU B 344     -23.920 -22.253 143.399  1.00 17.59           C  
ANISOU 6478  C   GLU B 344     2195   2024   2464    -37   -508    244       C  
ATOM   6479  O   GLU B 344     -24.019 -23.255 144.111  1.00 17.42           O  
ANISOU 6479  O   GLU B 344     2196   1990   2433    -30   -525    261       O  
ATOM   6480  CB  GLU B 344     -21.535 -22.333 142.501  1.00 14.08           C  
ANISOU 6480  CB  GLU B 344     1677   1586   2086    -30   -561    222       C  
ATOM   6481  CG  GLU B 344     -21.052 -21.112 143.284  1.00 22.98           C  
ANISOU 6481  CG  GLU B 344     2823   2715   3193    -44   -582    215       C  
ATOM   6482  CD  GLU B 344     -20.581 -19.936 142.443  1.00 36.67           C  
ANISOU 6482  CD  GLU B 344     4523   4462   4950    -55   -570    198       C  
ATOM   6483  OE1 GLU B 344     -20.788 -19.960 141.208  1.00 27.29           O  
ANISOU 6483  OE1 GLU B 344     3300   3284   3785    -52   -537    192       O  
ATOM   6484  OE2 GLU B 344     -19.990 -18.996 143.022  1.00 29.16           O  
ANISOU 6484  OE2 GLU B 344     3580   3509   3992    -66   -595    191       O  
ATOM   6485  N   GLU B 345     -24.554 -21.100 143.676  1.00 14.71           N  
ANISOU 6485  N   GLU B 345     1854   1665   2069    -48   -485    240       N  
ATOM   6486  CA  GLU B 345     -25.409 -20.951 144.859  1.00 14.71           C  
ANISOU 6486  CA  GLU B 345     1908   1659   2022    -49   -476    254       C  
ATOM   6487  C   GLU B 345     -26.873 -21.308 144.549  1.00 19.01           C  
ANISOU 6487  C   GLU B 345     2460   2204   2559    -49   -428    267       C  
ATOM   6488  O   GLU B 345     -27.704 -21.344 145.461  1.00 18.66           O  
ANISOU 6488  O   GLU B 345     2457   2155   2478    -48   -413    283       O  
ATOM   6489  CB  GLU B 345     -25.307 -19.527 145.431  1.00 15.96           C  
ANISOU 6489  CB  GLU B 345     2093   1821   2152    -59   -479    241       C  
ATOM   6490  CG  GLU B 345     -23.925 -19.184 145.961  1.00 25.75           C  
ANISOU 6490  CG  GLU B 345     3332   3057   3396    -61   -532    230       C  
ATOM   6491  CD  GLU B 345     -23.831 -17.837 146.649  1.00 48.44           C  
ANISOU 6491  CD  GLU B 345     6237   5929   6239    -71   -541    216       C  
ATOM   6492  OE1 GLU B 345     -24.698 -17.545 147.503  1.00 42.40           O  
ANISOU 6492  OE1 GLU B 345     5522   5161   5428    -69   -523    223       O  
ATOM   6493  OE2 GLU B 345     -22.833 -17.120 146.411  1.00 50.40           O  
ANISOU 6493  OE2 GLU B 345     6462   6177   6509    -79   -568    200       O  
ATOM   6494  N   ALA B 346     -27.185 -21.595 143.264  1.00 15.43           N  
ANISOU 6494  N   ALA B 346     1966   1755   2140    -48   -405    261       N  
ATOM   6495  CA  ALA B 346     -28.545 -21.965 142.857  1.00 14.95           C  
ANISOU 6495  CA  ALA B 346     1907   1694   2081    -48   -365    273       C  
ATOM   6496  C   ALA B 346     -28.982 -23.273 143.516  1.00 18.82           C  
ANISOU 6496  C   ALA B 346     2416   2169   2565    -43   -370    298       C  
ATOM   6497  O   ALA B 346     -28.186 -24.211 143.617  1.00 18.70           O  
ANISOU 6497  O   ALA B 346     2393   2144   2567    -35   -403    302       O  
ATOM   6498  CB  ALA B 346     -28.625 -22.093 141.343  1.00 15.41           C  
ANISOU 6498  CB  ALA B 346     1919   1759   2176    -47   -349    260       C  
ATOM   6499  N   ASN B 347     -30.251 -23.325 144.000  1.00 14.65           N  
ANISOU 6499  N   ASN B 347     1914   1638   2016    -46   -337    317       N  
ATOM   6500  CA  ASN B 347     -30.825 -24.519 144.649  1.00 14.73           C  
ANISOU 6500  CA  ASN B 347     1944   1633   2021    -43   -335    346       C  
ATOM   6501  C   ASN B 347     -30.080 -24.912 145.940  1.00 18.70           C  
ANISOU 6501  C   ASN B 347     2483   2127   2496    -37   -370    359       C  
ATOM   6502  O   ASN B 347     -30.065 -26.090 146.316  1.00 16.86           O  
ANISOU 6502  O   ASN B 347     2258   1879   2270    -33   -385    381       O  
ATOM   6503  CB  ASN B 347     -30.914 -25.700 143.660  1.00 14.37           C  
ANISOU 6503  CB  ASN B 347     1863   1578   2021    -40   -340    347       C  
ATOM   6504  CG  ASN B 347     -31.834 -25.427 142.493  1.00 25.93           C  
ANISOU 6504  CG  ASN B 347     3297   3048   3508    -45   -305    338       C  
ATOM   6505  OD1 ASN B 347     -32.836 -24.713 142.613  1.00 18.15           O  
ANISOU 6505  OD1 ASN B 347     2321   2069   2505    -51   -270    343       O  
ATOM   6506  ND2 ASN B 347     -31.536 -26.019 141.353  1.00 19.50           N  
ANISOU 6506  ND2 ASN B 347     2447   2231   2731    -40   -316    324       N  
ATOM   6507  N   THR B 348     -29.491 -23.906 146.639  1.00 15.89           N  
ANISOU 6507  N   THR B 348     2152   1778   2106    -38   -385    348       N  
ATOM   6508  CA  THR B 348     -28.846 -24.104 147.944  1.00 16.06           C  
ANISOU 6508  CA  THR B 348     2216   1793   2094    -33   -421    359       C  
ATOM   6509  C   THR B 348     -29.312 -23.020 148.912  1.00 19.86           C  
ANISOU 6509  C   THR B 348     2743   2281   2521    -34   -403    359       C  
ATOM   6510  O   THR B 348     -29.530 -21.876 148.500  1.00 19.02           O  
ANISOU 6510  O   THR B 348     2629   2185   2412    -39   -383    338       O  
ATOM   6511  CB  THR B 348     -27.303 -24.089 147.802  1.00 25.39           C  
ANISOU 6511  CB  THR B 348     3377   2973   3295    -30   -474    341       C  
ATOM   6512  OG1 THR B 348     -26.884 -22.786 147.398  1.00 25.64           O  
ANISOU 6512  OG1 THR B 348     3395   3018   3329    -36   -474    313       O  
ATOM   6513  CG2 THR B 348     -26.788 -25.144 146.815  1.00 24.17           C  
ANISOU 6513  CG2 THR B 348     3176   2813   3195    -24   -490    338       C  
ATOM   6514  N   GLY B 349     -29.450 -23.379 150.188  1.00 16.47           N  
ANISOU 6514  N   GLY B 349     2363   1844   2048    -29   -410    381       N  
ATOM   6515  CA  GLY B 349     -29.879 -22.448 151.227  1.00 16.40           C  
ANISOU 6515  CA  GLY B 349     2407   1842   1982    -26   -394    381       C  
ATOM   6516  C   GLY B 349     -31.234 -21.823 150.951  1.00 21.39           C  
ANISOU 6516  C   GLY B 349     3039   2482   2606    -29   -333    383       C  
ATOM   6517  O   GLY B 349     -32.226 -22.536 150.762  1.00 21.38           O  
ANISOU 6517  O   GLY B 349     3029   2478   2617    -30   -297    407       O  
ATOM   6518  N   ILE B 350     -31.284 -20.474 150.890  1.00 17.61           N  
ANISOU 6518  N   ILE B 350     2568   2012   2111    -31   -321    358       N  
ATOM   6519  CA  ILE B 350     -32.533 -19.745 150.625  1.00 17.19           C  
ANISOU 6519  CA  ILE B 350     2514   1966   2050    -31   -264    357       C  
ATOM   6520  C   ILE B 350     -32.905 -19.804 149.131  1.00 19.87           C  
ANISOU 6520  C   ILE B 350     2793   2310   2446    -39   -244    349       C  
ATOM   6521  O   ILE B 350     -34.017 -19.425 148.757  1.00 18.72           O  
ANISOU 6521  O   ILE B 350     2638   2169   2305    -40   -197    353       O  
ATOM   6522  CB  ILE B 350     -32.448 -18.266 151.138  1.00 20.41           C  
ANISOU 6522  CB  ILE B 350     2957   2379   2420    -28   -261    332       C  
ATOM   6523  CG1 ILE B 350     -31.428 -17.437 150.304  1.00 20.39           C  
ANISOU 6523  CG1 ILE B 350     2921   2378   2449    -37   -295    299       C  
ATOM   6524  CG2 ILE B 350     -32.123 -18.220 152.652  1.00 21.66           C  
ANISOU 6524  CG2 ILE B 350     3181   2533   2516    -18   -283    338       C  
ATOM   6525  CD1 ILE B 350     -31.503 -15.901 150.537  1.00 27.47           C  
ANISOU 6525  CD1 ILE B 350     3841   3276   3320    -37   -286    273       C  
ATOM   6526  N   TYR B 351     -31.965 -20.264 148.281  1.00 16.00           N  
ANISOU 6526  N   TYR B 351     2263   1817   1998    -44   -279    338       N  
ATOM   6527  CA  TYR B 351     -32.173 -20.293 146.835  1.00 14.50           C  
ANISOU 6527  CA  TYR B 351     2019   1632   1857    -49   -264    327       C  
ATOM   6528  C   TYR B 351     -32.741 -21.640 146.344  1.00 17.51           C  
ANISOU 6528  C   TYR B 351     2376   2006   2270    -49   -253    349       C  
ATOM   6529  O   TYR B 351     -32.781 -21.886 145.138  1.00 16.73           O  
ANISOU 6529  O   TYR B 351     2235   1910   2213    -53   -250    339       O  
ATOM   6530  CB  TYR B 351     -30.866 -19.937 146.087  1.00 14.92           C  
ANISOU 6530  CB  TYR B 351     2041   1690   1939    -53   -302    301       C  
ATOM   6531  CG  TYR B 351     -30.241 -18.637 146.555  1.00 16.03           C  
ANISOU 6531  CG  TYR B 351     2202   1833   2055    -56   -318    280       C  
ATOM   6532  CD1 TYR B 351     -30.825 -17.410 146.252  1.00 17.66           C  
ANISOU 6532  CD1 TYR B 351     2410   2046   2254    -59   -288    266       C  
ATOM   6533  CD2 TYR B 351     -29.053 -18.633 147.279  1.00 17.06           C  
ANISOU 6533  CD2 TYR B 351     2351   1959   2173    -55   -367    273       C  
ATOM   6534  CE1 TYR B 351     -30.260 -16.212 146.687  1.00 17.64           C  
ANISOU 6534  CE1 TYR B 351     2429   2043   2231    -62   -305    246       C  
ATOM   6535  CE2 TYR B 351     -28.471 -17.440 147.709  1.00 17.96           C  
ANISOU 6535  CE2 TYR B 351     2485   2073   2268    -59   -386    253       C  
ATOM   6536  CZ  TYR B 351     -29.080 -16.230 147.412  1.00 24.05           C  
ANISOU 6536  CZ  TYR B 351     3258   2848   3031    -63   -355    239       C  
ATOM   6537  OH  TYR B 351     -28.510 -15.053 147.828  1.00 23.61           O  
ANISOU 6537  OH  TYR B 351     3222   2789   2958    -68   -376    218       O  
ATOM   6538  N   GLN B 352     -33.243 -22.482 147.276  1.00 14.54           N  
ANISOU 6538  N   GLN B 352     2030   1621   1873    -46   -246    378       N  
ATOM   6539  CA  GLN B 352     -33.860 -23.765 146.910  1.00 14.42           C  
ANISOU 6539  CA  GLN B 352     1995   1596   1890    -48   -236    401       C  
ATOM   6540  C   GLN B 352     -35.204 -23.540 146.193  1.00 19.32           C  
ANISOU 6540  C   GLN B 352     2592   2220   2529    -53   -189    406       C  
ATOM   6541  O   GLN B 352     -36.187 -23.136 146.827  1.00 20.10           O  
ANISOU 6541  O   GLN B 352     2714   2323   2602    -53   -150    422       O  
ATOM   6542  CB  GLN B 352     -34.040 -24.660 148.148  1.00 16.01           C  
ANISOU 6542  CB  GLN B 352     2235   1784   2062    -44   -240    435       C  
ATOM   6543  CG  GLN B 352     -32.721 -25.118 148.760  1.00 24.15           C  
ANISOU 6543  CG  GLN B 352     3286   2809   3083    -38   -294    434       C  
ATOM   6544  CD  GLN B 352     -32.936 -25.912 150.019  1.00 30.64           C  
ANISOU 6544  CD  GLN B 352     4151   3619   3871    -33   -296    469       C  
ATOM   6545  OE1 GLN B 352     -33.313 -27.088 149.985  1.00 27.25           O  
ANISOU 6545  OE1 GLN B 352     3715   3176   3464    -35   -294    496       O  
ATOM   6546  NE2 GLN B 352     -32.659 -25.298 151.160  1.00 11.04           N  
ANISOU 6546  NE2 GLN B 352     1719   1143   1335    -27   -304    470       N  
ATOM   6547  N   SER B 353     -35.223 -23.742 144.848  1.00 15.06           N  
ANISOU 6547  N   SER B 353     2006   1681   2035    -57   -191    391       N  
ATOM   6548  CA  SER B 353     -36.407 -23.485 144.011  1.00 14.44           C  
ANISOU 6548  CA  SER B 353     1901   1607   1979    -62   -154    392       C  
ATOM   6549  C   SER B 353     -37.593 -24.404 144.353  1.00 17.62           C  
ANISOU 6549  C   SER B 353     2305   1997   2392    -66   -127    426       C  
ATOM   6550  O   SER B 353     -38.744 -24.040 144.098  1.00 17.61           O  
ANISOU 6550  O   SER B 353     2293   2001   2399    -70    -89    433       O  
ATOM   6551  CB  SER B 353     -36.054 -23.607 142.532  1.00 17.94           C  
ANISOU 6551  CB  SER B 353     2300   2052   2464    -63   -169    369       C  
ATOM   6552  OG  SER B 353     -35.547 -24.894 142.226  1.00 28.98           O  
ANISOU 6552  OG  SER B 353     3684   3436   3891    -62   -199    373       O  
ATOM   6553  N   LYS B 354     -37.318 -25.589 144.924  1.00 13.05           N  
ANISOU 6553  N   LYS B 354     1739   1402   1816    -66   -147    448       N  
ATOM   6554  CA  LYS B 354     -38.387 -26.513 145.335  1.00 12.43           C  
ANISOU 6554  CA  LYS B 354     1664   1311   1749    -72   -123    484       C  
ATOM   6555  C   LYS B 354     -39.048 -26.042 146.653  1.00 15.19           C  
ANISOU 6555  C   LYS B 354     2054   1666   2051    -69    -87    510       C  
ATOM   6556  O   LYS B 354     -40.092 -26.572 147.045  1.00 14.85           O  
ANISOU 6556  O   LYS B 354     2013   1615   2015    -74    -55    543       O  
ATOM   6557  CB  LYS B 354     -37.844 -27.952 145.475  1.00 14.26           C  
ANISOU 6557  CB  LYS B 354     1896   1521   2002    -72   -158    500       C  
ATOM   6558  CG  LYS B 354     -37.412 -28.575 144.139  1.00 23.16           C  
ANISOU 6558  CG  LYS B 354     2982   2639   3180    -73   -187    478       C  
ATOM   6559  CD  LYS B 354     -36.627 -29.891 144.334  1.00 31.35           C  
ANISOU 6559  CD  LYS B 354     4023   3654   4233    -69   -228    487       C  
ATOM   6560  CE  LYS B 354     -37.382 -30.932 145.120  1.00 44.70           C  
ANISOU 6560  CE  LYS B 354     5729   5324   5933    -75   -218    529       C  
ATOM   6561  NZ  LYS B 354     -36.552 -32.142 145.366  1.00 55.37           N  
ANISOU 6561  NZ  LYS B 354     7088   6652   7296    -70   -261    538       N  
ATOM   6562  N   GLN B 355     -38.449 -25.018 147.315  1.00 10.21           N  
ANISOU 6562  N   GLN B 355     1456   1048   1374    -61    -91    494       N  
ATOM   6563  CA  GLN B 355     -38.988 -24.456 148.558  1.00  9.37           C  
ANISOU 6563  CA  GLN B 355     1394    949   1216    -54    -57    512       C  
ATOM   6564  C   GLN B 355     -39.480 -23.011 148.351  1.00 13.85           C  
ANISOU 6564  C   GLN B 355     1961   1533   1768    -50    -25    490       C  
ATOM   6565  O   GLN B 355     -39.778 -22.313 149.324  1.00 12.71           O  
ANISOU 6565  O   GLN B 355     1856   1397   1577    -42      0    495       O  
ATOM   6566  CB  GLN B 355     -37.946 -24.523 149.684  1.00 10.18           C  
ANISOU 6566  CB  GLN B 355     1545   1050   1272    -46    -90    513       C  
ATOM   6567  CG  GLN B 355     -37.590 -25.957 150.088  1.00 18.86           C  
ANISOU 6567  CG  GLN B 355     2652   2132   2382    -48   -117    542       C  
ATOM   6568  CD  GLN B 355     -36.630 -26.007 151.254  1.00 31.94           C  
ANISOU 6568  CD  GLN B 355     4359   3787   3990    -39   -151    546       C  
ATOM   6569  OE1 GLN B 355     -36.150 -24.978 151.750  1.00 26.11           O  
ANISOU 6569  OE1 GLN B 355     3650   3061   3211    -31   -158    525       O  
ATOM   6570  NE2 GLN B 355     -36.324 -27.208 151.711  1.00 24.77           N  
ANISOU 6570  NE2 GLN B 355     3463   2863   3087    -38   -174    574       N  
ATOM   6571  N   CYS B 356     -39.576 -22.571 147.078  1.00 10.91           N  
ANISOU 6571  N   CYS B 356     1546   1166   1434    -55    -26    466       N  
ATOM   6572  CA  CYS B 356     -40.119 -21.256 146.736  1.00 11.27           C  
ANISOU 6572  CA  CYS B 356     1585   1224   1473    -52      4    447       C  
ATOM   6573  C   CYS B 356     -41.395 -21.415 145.920  1.00 15.30           C  
ANISOU 6573  C   CYS B 356     2055   1734   2024    -58     39    459       C  
ATOM   6574  O   CYS B 356     -41.571 -22.434 145.247  1.00 15.46           O  
ANISOU 6574  O   CYS B 356     2044   1744   2085    -66     27    469       O  
ATOM   6575  CB  CYS B 356     -39.083 -20.413 145.992  1.00 11.53           C  
ANISOU 6575  CB  CYS B 356     1606   1264   1511    -52    -28    409       C  
ATOM   6576  SG  CYS B 356     -37.653 -19.934 146.996  1.00 15.58           S  
ANISOU 6576  SG  CYS B 356     2165   1777   1976    -46    -68    392       S  
ATOM   6577  N   ALA B 357     -42.287 -20.409 145.968  1.00 11.76           N  
ANISOU 6577  N   ALA B 357     1607   1295   1566    -53     80    457       N  
ATOM   6578  CA  ALA B 357     -43.529 -20.435 145.192  1.00 11.46           C  
ANISOU 6578  CA  ALA B 357     1530   1257   1568    -57    112    467       C  
ATOM   6579  C   ALA B 357     -43.232 -20.591 143.694  1.00 15.75           C  
ANISOU 6579  C   ALA B 357     2028   1799   2158    -65     82    446       C  
ATOM   6580  O   ALA B 357     -42.317 -19.952 143.185  1.00 15.60           O  
ANISOU 6580  O   ALA B 357     2008   1786   2133    -63     57    416       O  
ATOM   6581  CB  ALA B 357     -44.323 -19.163 145.436  1.00 11.93           C  
ANISOU 6581  CB  ALA B 357     1598   1328   1609    -47    154    462       C  
ATOM   6582  N   GLU B 358     -43.948 -21.516 143.011  1.00 12.18           N  
ANISOU 6582  N   GLU B 358     1540   1337   1750    -74     84    462       N  
ATOM   6583  CA  GLU B 358     -43.729 -21.777 141.576  1.00 11.39           C  
ANISOU 6583  CA  GLU B 358     1401   1235   1692    -80     56    442       C  
ATOM   6584  C   GLU B 358     -45.016 -21.566 140.779  1.00 14.49           C  
ANISOU 6584  C   GLU B 358     1757   1629   2121    -84     81    448       C  
ATOM   6585  O   GLU B 358     -46.059 -21.337 141.368  1.00 13.78           O  
ANISOU 6585  O   GLU B 358     1668   1540   2028    -83    120    470       O  
ATOM   6586  CB  GLU B 358     -43.182 -23.204 141.356  1.00 12.59           C  
ANISOU 6586  CB  GLU B 358     1544   1372   1868    -87     20    448       C  
ATOM   6587  CG  GLU B 358     -44.154 -24.302 141.766  1.00 18.57           C  
ANISOU 6587  CG  GLU B 358     2294   2113   2650    -96     36    485       C  
ATOM   6588  CD  GLU B 358     -43.693 -25.711 141.449  1.00 29.75           C  
ANISOU 6588  CD  GLU B 358     3700   3510   4096   -102     -1    490       C  
ATOM   6589  OE1 GLU B 358     -42.471 -25.910 141.246  1.00 14.40           O  
ANISOU 6589  OE1 GLU B 358     1764   1565   2143    -98    -38    469       O  
ATOM   6590  OE2 GLU B 358     -44.548 -26.625 141.440  1.00 25.13           O  
ANISOU 6590  OE2 GLU B 358     3098   2908   3544   -112      7    516       O  
ATOM   6591  N   LEU B 359     -44.944 -21.675 139.424  1.00 11.60           N  
ANISOU 6591  N   LEU B 359     1357   1262   1788    -88     58    428       N  
ATOM   6592  CA  LEU B 359     -46.122 -21.467 138.558  1.00 11.37           C  
ANISOU 6592  CA  LEU B 359     1292   1233   1795    -91     74    432       C  
ATOM   6593  C   LEU B 359     -47.266 -22.423 138.926  1.00 15.11           C  
ANISOU 6593  C   LEU B 359     1750   1693   2300   -100     92    467       C  
ATOM   6594  O   LEU B 359     -47.048 -23.631 139.061  1.00 14.98           O  
ANISOU 6594  O   LEU B 359     1733   1661   2300   -108     72    479       O  
ATOM   6595  CB  LEU B 359     -45.747 -21.627 137.069  1.00 11.01           C  
ANISOU 6595  CB  LEU B 359     1219   1188   1776    -93     39    406       C  
ATOM   6596  CG  LEU B 359     -44.621 -20.708 136.548  1.00 15.08           C  
ANISOU 6596  CG  LEU B 359     1744   1717   2267    -85     22    374       C  
ATOM   6597  CD1 LEU B 359     -44.308 -21.010 135.102  1.00 15.20           C  
ANISOU 6597  CD1 LEU B 359     1734   1733   2307    -86     -8    352       C  
ATOM   6598  CD2 LEU B 359     -44.986 -19.241 136.710  1.00 14.95           C  
ANISOU 6598  CD2 LEU B 359     1736   1714   2231    -78     51    368       C  
ATOM   6599  N   GLY B 360     -48.463 -21.862 139.127  1.00 11.22           N  
ANISOU 6599  N   GLY B 360     1243   1204   1816    -99    131    484       N  
ATOM   6600  CA  GLY B 360     -49.641 -22.631 139.531  1.00 10.72           C  
ANISOU 6600  CA  GLY B 360     1160   1128   1785   -108    156    520       C  
ATOM   6601  C   GLY B 360     -50.782 -22.582 138.534  1.00 13.65           C  
ANISOU 6601  C   GLY B 360     1485   1497   2207   -114    160    524       C  
ATOM   6602  O   GLY B 360     -51.593 -23.507 138.474  1.00 13.03           O  
ANISOU 6602  O   GLY B 360     1380   1402   2170   -127    161    549       O  
ATOM   6603  N   PHE B 361     -50.859 -21.495 137.738  1.00 10.63           N  
ANISOU 6603  N   PHE B 361     1091   1127   1822   -106    159    499       N  
ATOM   6604  CA  PHE B 361     -51.927 -21.331 136.734  1.00 10.83           C  
ANISOU 6604  CA  PHE B 361     1073   1150   1893   -109    159    500       C  
ATOM   6605  C   PHE B 361     -51.732 -22.305 135.545  1.00 15.46           C  
ANISOU 6605  C   PHE B 361     1635   1722   2515   -121    109    487       C  
ATOM   6606  O   PHE B 361     -52.663 -22.518 134.761  1.00 14.83           O  
ANISOU 6606  O   PHE B 361     1520   1636   2480   -127    101    492       O  
ATOM   6607  CB  PHE B 361     -51.983 -19.874 136.234  1.00 12.21           C  
ANISOU 6607  CB  PHE B 361     1247   1341   2050    -96    170    479       C  
ATOM   6608  CG  PHE B 361     -50.847 -19.494 135.312  1.00 13.59           C  
ANISOU 6608  CG  PHE B 361     1433   1523   2206    -92    132    442       C  
ATOM   6609  CD1 PHE B 361     -49.610 -19.113 135.824  1.00 16.48           C  
ANISOU 6609  CD1 PHE B 361     1837   1898   2527    -85    127    426       C  
ATOM   6610  CD2 PHE B 361     -51.015 -19.507 133.929  1.00 14.97           C  
ANISOU 6610  CD2 PHE B 361     1581   1698   2409    -94    103    426       C  
ATOM   6611  CE1 PHE B 361     -48.555 -18.784 134.970  1.00 17.05           C  
ANISOU 6611  CE1 PHE B 361     1916   1977   2587    -82     95    395       C  
ATOM   6612  CE2 PHE B 361     -49.960 -19.171 133.079  1.00 17.60           C  
ANISOU 6612  CE2 PHE B 361     1925   2039   2723    -89     73    395       C  
ATOM   6613  CZ  PHE B 361     -48.736 -18.821 133.603  1.00 15.70           C  
ANISOU 6613  CZ  PHE B 361     1718   1806   2441    -84     71    381       C  
ATOM   6614  N   ILE B 362     -50.517 -22.888 135.416  1.00 11.69           N  
ANISOU 6614  N   ILE B 362     1181   1242   2020   -121     75    469       N  
ATOM   6615  CA  ILE B 362     -50.221 -23.847 134.349  1.00 11.43           C  
ANISOU 6615  CA  ILE B 362     1131   1195   2016   -128     29    453       C  
ATOM   6616  C   ILE B 362     -50.851 -25.225 134.644  1.00 15.53           C  
ANISOU 6616  C   ILE B 362     1635   1689   2577   -144     21    480       C  
ATOM   6617  O   ILE B 362     -50.623 -26.181 133.902  1.00 14.08           O  
ANISOU 6617  O   ILE B 362     1441   1489   2419   -150    -19    469       O  
ATOM   6618  CB  ILE B 362     -48.684 -23.945 134.074  1.00 14.20           C  
ANISOU 6618  CB  ILE B 362     1508   1551   2335   -121     -2    423       C  
ATOM   6619  CG1 ILE B 362     -47.918 -24.466 135.320  1.00 14.36           C  
ANISOU 6619  CG1 ILE B 362     1560   1566   2329   -121      3    436       C  
ATOM   6620  CG2 ILE B 362     -48.128 -22.596 133.593  1.00 14.85           C  
ANISOU 6620  CG2 ILE B 362     1600   1656   2385   -108      2    396       C  
ATOM   6621  CD1 ILE B 362     -46.405 -24.837 135.045  1.00 17.47           C  
ANISOU 6621  CD1 ILE B 362     1974   1961   2702   -114    -34    410       C  
ATOM   6622  N   ILE B 363     -51.647 -25.315 135.734  1.00 13.24           N  
ANISOU 6622  N   ILE B 363     1342   1395   2292   -150     60    517       N  
ATOM   6623  CA  ILE B 363     -52.383 -26.530 136.086  1.00 14.07           C  
ANISOU 6623  CA  ILE B 363     1429   1476   2441   -167     60    550       C  
ATOM   6624  C   ILE B 363     -53.887 -26.222 136.120  1.00 19.66           C  
ANISOU 6624  C   ILE B 363     2099   2182   3187   -173     93    577       C  
ATOM   6625  O   ILE B 363     -54.314 -25.326 136.854  1.00 20.28           O  
ANISOU 6625  O   ILE B 363     2183   2277   3243   -164    139    592       O  
ATOM   6626  CB  ILE B 363     -51.882 -27.116 137.451  1.00 17.85           C  
ANISOU 6626  CB  ILE B 363     1941   1948   2892   -168     77    576       C  
ATOM   6627  CG1 ILE B 363     -50.349 -27.330 137.441  1.00 18.02           C  
ANISOU 6627  CG1 ILE B 363     1999   1972   2877   -160     43    549       C  
ATOM   6628  CG2 ILE B 363     -52.632 -28.423 137.801  1.00 18.77           C  
ANISOU 6628  CG2 ILE B 363     2039   2037   3058   -188     76    614       C  
ATOM   6629  CD1 ILE B 363     -49.725 -27.478 138.831  1.00 22.45           C  
ANISOU 6629  CD1 ILE B 363     2599   2534   3395   -155     61    568       C  
ATOM   6630  N   LYS B 364     -54.680 -26.920 135.282  1.00 16.03           N  
ANISOU 6630  N   LYS B 364     1601   1704   2786   -188     67    582       N  
ATOM   6631  CA  LYS B 364     -56.125 -26.696 135.213  1.00 15.75           C  
ANISOU 6631  CA  LYS B 364     1523   1666   2796   -195     92    608       C  
ATOM   6632  C   LYS B 364     -56.892 -28.018 135.355  1.00 19.52           C  
ANISOU 6632  C   LYS B 364     1971   2113   3333   -219     82    641       C  
ATOM   6633  O   LYS B 364     -56.573 -28.996 134.671  1.00 16.79           O  
ANISOU 6633  O   LYS B 364     1621   1745   3013   -229     33    628       O  
ATOM   6634  CB  LYS B 364     -56.501 -25.987 133.900  1.00 17.74           C  
ANISOU 6634  CB  LYS B 364     1749   1926   3065   -190     68    580       C  
ATOM   6635  CG  LYS B 364     -57.967 -25.563 133.829  1.00 27.79           C  
ANISOU 6635  CG  LYS B 364     2977   3200   4384   -194     95    605       C  
ATOM   6636  CD  LYS B 364     -58.283 -24.882 132.510  1.00 38.64           C  
ANISOU 6636  CD  LYS B 364     4329   4581   5772   -187     66    577       C  
ATOM   6637  CE  LYS B 364     -59.715 -24.412 132.443  1.00 49.76           C  
ANISOU 6637  CE  LYS B 364     5690   5990   7227   -190     91    601       C  
ATOM   6638  NZ  LYS B 364     -59.999 -23.699 131.170  1.00 56.36           N  
ANISOU 6638  NZ  LYS B 364     6507   6833   8073   -181     60    575       N  
ATOM   6639  N   ASP B 365     -57.900 -28.047 136.263  1.00 18.77           N  
ANISOU 6639  N   ASP B 365     1856   2016   3261   -226    130    686       N  
ATOM   6640  CA  ASP B 365     -58.729 -29.243 136.523  1.00 19.72           C  
ANISOU 6640  CA  ASP B 365     1944   2106   3442   -251    129    726       C  
ATOM   6641  C   ASP B 365     -57.874 -30.471 136.942  1.00 23.09           C  
ANISOU 6641  C   ASP B 365     2402   2511   3862   -261    103    732       C  
ATOM   6642  O   ASP B 365     -58.202 -31.603 136.595  1.00 22.79           O  
ANISOU 6642  O   ASP B 365     2342   2441   3878   -281     70    744       O  
ATOM   6643  CB  ASP B 365     -59.624 -29.574 135.301  1.00 21.94           C  
ANISOU 6643  CB  ASP B 365     2175   2370   3793   -265     89    718       C  
ATOM   6644  CG  ASP B 365     -60.566 -28.443 134.905  1.00 33.07           C  
ANISOU 6644  CG  ASP B 365     3550   3799   5217   -256    113    718       C  
ATOM   6645  OD1 ASP B 365     -60.870 -27.590 135.773  1.00 33.19           O  
ANISOU 6645  OD1 ASP B 365     3570   3835   5205   -243    171    737       O  
ATOM   6646  OD2 ASP B 365     -61.038 -28.443 133.748  1.00 41.36           O  
ANISOU 6646  OD2 ASP B 365     4569   4841   6307   -261     72    699       O  
ATOM   6647  N   GLY B 366     -56.795 -30.215 137.687  1.00 20.43           N  
ANISOU 6647  N   GLY B 366     2114   2189   3461   -246    116    724       N  
ATOM   6648  CA  GLY B 366     -55.923 -31.266 138.210  1.00 20.93           C  
ANISOU 6648  CA  GLY B 366     2209   2233   3511   -251     95    731       C  
ATOM   6649  C   GLY B 366     -54.922 -31.814 137.205  1.00 25.55           C  
ANISOU 6649  C   GLY B 366     2807   2805   4097   -249     30    688       C  
ATOM   6650  O   GLY B 366     -54.231 -32.800 137.491  1.00 25.42           O  
ANISOU 6650  O   GLY B 366     2811   2768   4079   -254      6    692       O  
ATOM   6651  N   TYR B 367     -54.824 -31.179 136.018  1.00 21.98           N  
ANISOU 6651  N   TYR B 367     2341   2364   3644   -240      4    647       N  
ATOM   6652  CA  TYR B 367     -53.898 -31.631 134.968  1.00 21.91           C  
ANISOU 6652  CA  TYR B 367     2344   2347   3635   -235    -54    604       C  
ATOM   6653  C   TYR B 367     -53.131 -30.448 134.339  1.00 23.78           C  
ANISOU 6653  C   TYR B 367     2597   2614   3822   -213    -58    561       C  
ATOM   6654  O   TYR B 367     -53.606 -29.314 134.381  1.00 23.36           O  
ANISOU 6654  O   TYR B 367     2536   2585   3754   -206    -26    562       O  
ATOM   6655  CB  TYR B 367     -54.653 -32.430 133.885  1.00 24.31           C  
ANISOU 6655  CB  TYR B 367     2610   2622   4004   -251    -97    598       C  
ATOM   6656  CG  TYR B 367     -55.169 -33.767 134.378  1.00 27.69           C  
ANISOU 6656  CG  TYR B 367     3025   3013   4484   -274   -105    635       C  
ATOM   6657  CD1 TYR B 367     -54.349 -34.892 134.389  1.00 30.10           C  
ANISOU 6657  CD1 TYR B 367     3352   3291   4793   -277   -142    627       C  
ATOM   6658  CD2 TYR B 367     -56.471 -33.904 134.848  1.00 29.08           C  
ANISOU 6658  CD2 TYR B 367     3164   3178   4706   -293    -74    679       C  
ATOM   6659  CE1 TYR B 367     -54.809 -36.119 134.867  1.00 32.30           C  
ANISOU 6659  CE1 TYR B 367     3620   3533   5121   -299   -151    663       C  
ATOM   6660  CE2 TYR B 367     -56.942 -35.125 135.334  1.00 30.63           C  
ANISOU 6660  CE2 TYR B 367     3347   3338   4951   -316    -80    717       C  
ATOM   6661  CZ  TYR B 367     -56.108 -36.232 135.337  1.00 40.51           C  
ANISOU 6661  CZ  TYR B 367     4624   4562   6207   -319   -119    709       C  
ATOM   6662  OH  TYR B 367     -56.570 -37.442 135.804  1.00 43.64           O  
ANISOU 6662  OH  TYR B 367     5008   4919   6654   -343   -126    748       O  
ATOM   6663  N   PRO B 368     -51.920 -30.693 133.748  1.00 18.78           N  
ANISOU 6663  N   PRO B 368     1988   1982   3166   -202    -97    524       N  
ATOM   6664  CA  PRO B 368     -51.174 -29.579 133.128  1.00 17.46           C  
ANISOU 6664  CA  PRO B 368     1834   1844   2955   -183    -99    486       C  
ATOM   6665  C   PRO B 368     -52.003 -28.838 132.078  1.00 19.89           C  
ANISOU 6665  C   PRO B 368     2114   2162   3282   -182   -103    472       C  
ATOM   6666  O   PRO B 368     -52.615 -29.468 131.215  1.00 20.48           O  
ANISOU 6666  O   PRO B 368     2163   2218   3401   -191   -134    466       O  
ATOM   6667  CB  PRO B 368     -49.955 -30.270 132.503  1.00 19.06           C  
ANISOU 6667  CB  PRO B 368     2057   2038   3148   -175   -144    453       C  
ATOM   6668  CG  PRO B 368     -49.810 -31.544 133.255  1.00 24.05           C  
ANISOU 6668  CG  PRO B 368     2697   2641   3800   -186   -154    477       C  
ATOM   6669  CD  PRO B 368     -51.191 -31.973 133.622  1.00 20.06           C  
ANISOU 6669  CD  PRO B 368     2164   2117   3342   -206   -137    516       C  
ATOM   6670  N   TYR B 369     -52.058 -27.502 132.181  1.00 15.10           N  
ANISOU 6670  N   TYR B 369     1511   1584   2644   -170    -71    467       N  
ATOM   6671  CA  TYR B 369     -52.826 -26.658 131.255  1.00 13.92           C  
ANISOU 6671  CA  TYR B 369     1335   1445   2507   -167    -72    456       C  
ATOM   6672  C   TYR B 369     -52.032 -26.471 129.940  1.00 17.80           C  
ANISOU 6672  C   TYR B 369     1836   1946   2982   -155   -111    413       C  
ATOM   6673  O   TYR B 369     -51.586 -25.358 129.629  1.00 16.57           O  
ANISOU 6673  O   TYR B 369     1692   1814   2791   -141   -101    395       O  
ATOM   6674  CB  TYR B 369     -53.129 -25.287 131.918  1.00 14.49           C  
ANISOU 6674  CB  TYR B 369     1412   1542   2550   -157    -22    467       C  
ATOM   6675  CG  TYR B 369     -54.240 -24.490 131.257  1.00 14.86           C  
ANISOU 6675  CG  TYR B 369     1427   1597   2622   -155    -14    469       C  
ATOM   6676  CD1 TYR B 369     -54.910 -24.981 130.138  1.00 16.80           C  
ANISOU 6676  CD1 TYR B 369     1642   1829   2913   -163    -51    462       C  
ATOM   6677  CD2 TYR B 369     -54.658 -23.270 131.783  1.00 15.11           C  
ANISOU 6677  CD2 TYR B 369     1458   1647   2635   -145     30    480       C  
ATOM   6678  CE1 TYR B 369     -55.939 -24.258 129.533  1.00 18.32           C  
ANISOU 6678  CE1 TYR B 369     1804   2028   3130   -161    -47    465       C  
ATOM   6679  CE2 TYR B 369     -55.687 -22.538 131.188  1.00 15.93           C  
ANISOU 6679  CE2 TYR B 369     1531   1756   2764   -142     38    483       C  
ATOM   6680  CZ  TYR B 369     -56.319 -23.031 130.058  1.00 23.52           C  
ANISOU 6680  CZ  TYR B 369     2462   2706   3771   -150     -2    476       C  
ATOM   6681  OH  TYR B 369     -57.333 -22.314 129.471  1.00 24.24           O  
ANISOU 6681  OH  TYR B 369     2520   2801   3887   -147      2    480       O  
ATOM   6682  N   LYS B 370     -51.839 -27.577 129.185  1.00 15.01           N  
ANISOU 6682  N   LYS B 370     1478   1571   2654   -160   -156    397       N  
ATOM   6683  CA  LYS B 370     -51.024 -27.585 127.961  1.00 14.65           C  
ANISOU 6683  CA  LYS B 370     1444   1532   2591   -147   -193    356       C  
ATOM   6684  C   LYS B 370     -51.647 -26.759 126.824  1.00 18.68           C  
ANISOU 6684  C   LYS B 370     1936   2055   3105   -141   -203    341       C  
ATOM   6685  O   LYS B 370     -50.923 -26.259 125.965  1.00 18.59           O  
ANISOU 6685  O   LYS B 370     1940   2061   3064   -126   -216    311       O  
ATOM   6686  CB  LYS B 370     -50.768 -29.030 127.490  1.00 16.40           C  
ANISOU 6686  CB  LYS B 370     1667   1724   2841   -152   -238    344       C  
ATOM   6687  CG  LYS B 370     -49.900 -29.843 128.447  1.00 19.16           C  
ANISOU 6687  CG  LYS B 370     2039   2061   3181   -154   -236    353       C  
ATOM   6688  CD  LYS B 370     -49.608 -31.228 127.891  1.00 23.01           C  
ANISOU 6688  CD  LYS B 370     2529   2518   3697   -156   -283    337       C  
ATOM   6689  CE  LYS B 370     -48.686 -32.014 128.791  1.00 25.64           C  
ANISOU 6689  CE  LYS B 370     2885   2839   4020   -155   -283    346       C  
ATOM   6690  NZ  LYS B 370     -48.327 -33.325 128.200  1.00 25.30           N  
ANISOU 6690  NZ  LYS B 370     2846   2764   4004   -154   -329    327       N  
ATOM   6691  N   SER B 371     -52.988 -26.649 126.798  1.00 14.68           N  
ANISOU 6691  N   SER B 371     1398   1540   2638   -152   -197    363       N  
ATOM   6692  CA  SER B 371     -53.696 -25.959 125.713  1.00 13.67           C  
ANISOU 6692  CA  SER B 371     1251   1422   2521   -147   -211    351       C  
ATOM   6693  C   SER B 371     -53.883 -24.442 125.981  1.00 16.31           C  
ANISOU 6693  C   SER B 371     1586   1783   2828   -137   -170    359       C  
ATOM   6694  O   SER B 371     -54.518 -23.751 125.173  1.00 15.81           O  
ANISOU 6694  O   SER B 371     1506   1728   2773   -132   -178    353       O  
ATOM   6695  CB  SER B 371     -55.048 -26.616 125.458  1.00 17.41           C  
ANISOU 6695  CB  SER B 371     1688   1871   3057   -164   -232    369       C  
ATOM   6696  OG  SER B 371     -55.879 -26.538 126.606  1.00 26.99           O  
ANISOU 6696  OG  SER B 371     2879   3079   4295   -177   -191    409       O  
ATOM   6697  N   ARG B 372     -53.321 -23.923 127.102  1.00 11.27           N  
ANISOU 6697  N   ARG B 372      967   1157   2157   -133   -129    370       N  
ATOM   6698  CA  ARG B 372     -53.486 -22.506 127.457  1.00 10.57           C  
ANISOU 6698  CA  ARG B 372      881   1091   2043   -123    -90    377       C  
ATOM   6699  C   ARG B 372     -52.921 -21.579 126.369  1.00 14.13           C  
ANISOU 6699  C   ARG B 372     1344   1561   2463   -107   -105    348       C  
ATOM   6700  O   ARG B 372     -51.735 -21.665 126.031  1.00 12.65           O  
ANISOU 6700  O   ARG B 372     1181   1381   2243   -100   -120    324       O  
ATOM   6701  CB  ARG B 372     -52.832 -22.194 128.817  1.00  9.01           C  
ANISOU 6701  CB  ARG B 372      710    902   1812   -120    -51    389       C  
ATOM   6702  CG  ARG B 372     -53.145 -20.775 129.325  1.00 16.02           C  
ANISOU 6702  CG  ARG B 372     1601   1808   2678   -110     -9    398       C  
ATOM   6703  CD  ARG B 372     -52.261 -20.377 130.491  1.00 19.22           C  
ANISOU 6703  CD  ARG B 372     2041   2222   3040   -104     21    400       C  
ATOM   6704  NE  ARG B 372     -52.613 -19.051 131.020  1.00 18.64           N  
ANISOU 6704  NE  ARG B 372     1972   2162   2947    -94     60    407       N  
ATOM   6705  CZ  ARG B 372     -52.099 -17.909 130.565  1.00 25.61           C  
ANISOU 6705  CZ  ARG B 372     2869   3060   3802    -82     62    387       C  
ATOM   6706  NH1 ARG B 372     -51.240 -17.916 129.552  1.00  9.60           N  
ANISOU 6706  NH1 ARG B 372      849   1038   1762    -80     28    361       N  
ATOM   6707  NH2 ARG B 372     -52.458 -16.751 131.105  1.00  9.68           N  
ANISOU 6707  NH2 ARG B 372      857   1051   1770    -72     97    394       N  
ATOM   6708  N   PRO B 373     -53.744 -20.630 125.849  1.00 11.56           N  
ANISOU 6708  N   PRO B 373     1001   1245   2148   -102    -98    351       N  
ATOM   6709  CA  PRO B 373     -53.225 -19.696 124.846  1.00 11.22           C  
ANISOU 6709  CA  PRO B 373      970   1220   2074    -88   -109    328       C  
ATOM   6710  C   PRO B 373     -52.257 -18.687 125.455  1.00 14.15           C  
ANISOU 6710  C   PRO B 373     1369   1608   2398    -78    -77    323       C  
ATOM   6711  O   PRO B 373     -52.397 -18.318 126.626  1.00 13.69           O  
ANISOU 6711  O   PRO B 373     1316   1551   2336    -79    -41    341       O  
ATOM   6712  CB  PRO B 373     -54.497 -19.007 124.306  1.00 13.24           C  
ANISOU 6712  CB  PRO B 373     1196   1476   2358    -85   -109    339       C  
ATOM   6713  CG  PRO B 373     -55.654 -19.819 124.854  1.00 17.88           C  
ANISOU 6713  CG  PRO B 373     1752   2044   2998   -100   -106    365       C  
ATOM   6714  CD  PRO B 373     -55.169 -20.392 126.123  1.00 13.39           C  
ANISOU 6714  CD  PRO B 373     1199   1470   2421   -107    -81    378       C  
ATOM   6715  N   TYR B 374     -51.255 -18.271 124.684  1.00  9.45           N  
ANISOU 6715  N   TYR B 374      794   1026   1770    -68    -91    299       N  
ATOM   6716  CA  TYR B 374     -50.326 -17.243 125.125  1.00  8.78           C  
ANISOU 6716  CA  TYR B 374      733    957   1646    -61    -66    294       C  
ATOM   6717  C   TYR B 374     -51.006 -15.868 125.077  1.00 12.93           C  
ANISOU 6717  C   TYR B 374     1252   1491   2171    -53    -42    303       C  
ATOM   6718  O   TYR B 374     -51.727 -15.571 124.122  1.00 12.48           O  
ANISOU 6718  O   TYR B 374     1178   1435   2129    -49    -58    303       O  
ATOM   6719  CB  TYR B 374     -49.064 -17.246 124.244  1.00  9.45           C  
ANISOU 6719  CB  TYR B 374      836   1053   1701    -54    -87    268       C  
ATOM   6720  CG  TYR B 374     -48.157 -18.436 124.482  1.00 10.40           C  
ANISOU 6720  CG  TYR B 374      968   1166   1817    -57   -104    258       C  
ATOM   6721  CD1 TYR B 374     -48.330 -19.622 123.774  1.00 12.08           C  
ANISOU 6721  CD1 TYR B 374     1172   1368   2051    -59   -138    247       C  
ATOM   6722  CD2 TYR B 374     -47.069 -18.346 125.346  1.00 10.76           C  
ANISOU 6722  CD2 TYR B 374     1034   1217   1839    -57    -90    255       C  
ATOM   6723  CE1 TYR B 374     -47.484 -20.713 123.972  1.00 12.79           C  
ANISOU 6723  CE1 TYR B 374     1272   1448   2138    -60   -155    237       C  
ATOM   6724  CE2 TYR B 374     -46.200 -19.421 125.531  1.00 11.78           C  
ANISOU 6724  CE2 TYR B 374     1172   1339   1965    -59   -107    246       C  
ATOM   6725  CZ  TYR B 374     -46.411 -20.604 124.843  1.00 19.38           C  
ANISOU 6725  CZ  TYR B 374     2125   2289   2949    -60   -138    237       C  
ATOM   6726  OH  TYR B 374     -45.557 -21.664 125.022  1.00 19.06           O  
ANISOU 6726  OH  TYR B 374     2094   2240   2908    -59   -156    227       O  
ATOM   6727  N   ASP B 375     -50.817 -15.052 126.118  1.00  9.86           N  
ANISOU 6727  N   ASP B 375      877   1106   1764    -51     -7    312       N  
ATOM   6728  CA  ASP B 375     -51.384 -13.701 126.145  1.00  9.96           C  
ANISOU 6728  CA  ASP B 375      887   1124   1774    -42     17    319       C  
ATOM   6729  C   ASP B 375     -50.534 -12.747 125.317  1.00 15.11           C  
ANISOU 6729  C   ASP B 375     1555   1788   2398    -34      9    302       C  
ATOM   6730  O   ASP B 375     -49.333 -12.622 125.563  1.00 14.39           O  
ANISOU 6730  O   ASP B 375     1487   1703   2277    -35     10    290       O  
ATOM   6731  CB  ASP B 375     -51.515 -13.192 127.588  1.00 11.44           C  
ANISOU 6731  CB  ASP B 375     1087   1309   1952    -41     57    332       C  
ATOM   6732  CG  ASP B 375     -52.444 -14.028 128.446  1.00 16.81           C  
ANISOU 6732  CG  ASP B 375     1749   1978   2660    -47     72    354       C  
ATOM   6733  OD1 ASP B 375     -53.530 -14.413 127.946  1.00 16.03           O  
ANISOU 6733  OD1 ASP B 375     1619   1873   2600    -50     63    366       O  
ATOM   6734  OD2 ASP B 375     -52.125 -14.236 129.632  1.00 20.89           O  
ANISOU 6734  OD2 ASP B 375     2285   2493   3161    -50     95    362       O  
ATOM   6735  N   LEU B 376     -51.143 -12.118 124.287  1.00 13.07           N  
ANISOU 6735  N   LEU B 376     1284   1534   2149    -27     -2    302       N  
ATOM   6736  CA  LEU B 376     -50.432 -11.184 123.401  1.00 13.04           C  
ANISOU 6736  CA  LEU B 376     1294   1541   2120    -19     -9    291       C  
ATOM   6737  C   LEU B 376     -50.742  -9.738 123.773  1.00 15.78           C  
ANISOU 6737  C   LEU B 376     1646   1887   2461    -11     19    300       C  
ATOM   6738  O   LEU B 376     -49.829  -8.955 124.015  1.00 15.83           O  
ANISOU 6738  O   LEU B 376     1675   1898   2442    -10     31    293       O  
ATOM   6739  CB  LEU B 376     -50.802 -11.452 121.921  1.00 13.62           C  
ANISOU 6739  CB  LEU B 376     1356   1619   2202    -14    -43    285       C  
ATOM   6740  CG  LEU B 376     -49.934 -12.496 121.175  1.00 19.07           C  
ANISOU 6740  CG  LEU B 376     2053   2313   2878    -17    -72    266       C  
ATOM   6741  CD1 LEU B 376     -49.872 -13.807 121.930  1.00 19.86           C  
ANISOU 6741  CD1 LEU B 376     2150   2404   2993    -27    -78    265       C  
ATOM   6742  CD2 LEU B 376     -50.452 -12.726 119.774  1.00 21.21           C  
ANISOU 6742  CD2 LEU B 376     2315   2587   3156    -10   -106    260       C  
ATOM   6743  N   PHE B 377     -52.031  -9.385 123.827  1.00 11.89           N  
ANISOU 6743  N   PHE B 377     1132   1388   1996     -5     28    314       N  
ATOM   6744  CA  PHE B 377     -52.458  -8.046 124.224  1.00 10.54           C  
ANISOU 6744  CA  PHE B 377      965   1214   1825      5     56    323       C  
ATOM   6745  C   PHE B 377     -53.828  -8.116 124.895  1.00 12.50           C  
ANISOU 6745  C   PHE B 377     1189   1453   2108      9     77    341       C  
ATOM   6746  O   PHE B 377     -54.816  -8.488 124.251  1.00 11.11           O  
ANISOU 6746  O   PHE B 377      984   1275   1964     10     60    350       O  
ATOM   6747  CB  PHE B 377     -52.505  -7.100 123.002  1.00 11.87           C  
ANISOU 6747  CB  PHE B 377     1134   1388   1990     14     41    321       C  
ATOM   6748  CG  PHE B 377     -52.110  -5.667 123.306  1.00 12.57           C  
ANISOU 6748  CG  PHE B 377     1243   1474   2060     22     64    321       C  
ATOM   6749  CD1 PHE B 377     -52.646  -4.996 124.403  1.00 15.76           C  
ANISOU 6749  CD1 PHE B 377     1649   1868   2472     29     97    329       C  
ATOM   6750  CD2 PHE B 377     -51.287  -4.957 122.440  1.00 13.49           C  
ANISOU 6750  CD2 PHE B 377     1375   1597   2154     23     52    315       C  
ATOM   6751  CE1 PHE B 377     -52.280  -3.676 124.683  1.00 16.31           C  
ANISOU 6751  CE1 PHE B 377     1739   1931   2526     36    115    327       C  
ATOM   6752  CE2 PHE B 377     -50.939  -3.628 122.709  1.00 15.87           C  
ANISOU 6752  CE2 PHE B 377     1694   1892   2443     29     71    316       C  
ATOM   6753  CZ  PHE B 377     -51.439  -2.997 123.827  1.00 14.24           C  
ANISOU 6753  CZ  PHE B 377     1492   1674   2245     35    100    320       C  
ATOM   6754  N   LEU B 378     -53.887  -7.782 126.200  1.00  8.68           N  
ANISOU 6754  N   LEU B 378      717    965   1618     12    113    347       N  
ATOM   6755  CA  LEU B 378     -55.136  -7.831 126.969  1.00  8.30           C  
ANISOU 6755  CA  LEU B 378      646    910   1600     17    141    366       C  
ATOM   6756  C   LEU B 378     -55.674  -6.429 127.217  1.00 12.75           C  
ANISOU 6756  C   LEU B 378     1212   1469   2165     35    169    370       C  
ATOM   6757  O   LEU B 378     -54.889  -5.484 127.341  1.00 12.38           O  
ANISOU 6757  O   LEU B 378     1194   1422   2089     40    175    359       O  
ATOM   6758  CB  LEU B 378     -54.915  -8.562 128.318  1.00  7.95           C  
ANISOU 6758  CB  LEU B 378      613    862   1545     10    165    371       C  
ATOM   6759  CG  LEU B 378     -54.234  -9.947 128.237  1.00 11.10           C  
ANISOU 6759  CG  LEU B 378     1016   1263   1940     -7    139    365       C  
ATOM   6760  CD1 LEU B 378     -53.998 -10.512 129.615  1.00 10.07           C  
ANISOU 6760  CD1 LEU B 378      902   1130   1796    -12    165    373       C  
ATOM   6761  CD2 LEU B 378     -55.057 -10.919 127.388  1.00 13.64           C  
ANISOU 6761  CD2 LEU B 378     1300   1580   2301    -14    111    374       C  
ATOM   6762  N   SER B 379     -57.026  -6.295 127.357  1.00  9.99           N  
ANISOU 6762  N   SER B 379      829   1113   1853     44    186    389       N  
ATOM   6763  CA  SER B 379     -57.676  -4.988 127.574  1.00  9.64           C  
ANISOU 6763  CA  SER B 379      783   1063   1817     65    214    394       C  
ATOM   6764  C   SER B 379     -57.150  -4.265 128.835  1.00 14.88           C  
ANISOU 6764  C   SER B 379     1484   1723   2447     73    252    386       C  
ATOM   6765  O   SER B 379     -57.201  -3.041 128.897  1.00 16.21           O  
ANISOU 6765  O   SER B 379     1666   1886   2609     88    267    382       O  
ATOM   6766  CB  SER B 379     -59.192  -5.142 127.640  1.00 12.88           C  
ANISOU 6766  CB  SER B 379     1150   1469   2277     73    228    416       C  
ATOM   6767  OG  SER B 379     -59.596  -5.837 128.809  1.00 23.11           O  
ANISOU 6767  OG  SER B 379     2437   2763   3580     70    262    429       O  
ATOM   6768  N   GLU B 380     -56.608  -5.029 129.823  1.00 11.35           N  
ANISOU 6768  N   GLU B 380     1055   1278   1978     63    265    384       N  
ATOM   6769  CA  GLU B 380     -55.990  -4.438 131.029  1.00 10.69           C  
ANISOU 6769  CA  GLU B 380     1013   1192   1857     70    295    374       C  
ATOM   6770  C   GLU B 380     -54.933  -3.437 130.638  1.00 13.88           C  
ANISOU 6770  C   GLU B 380     1448   1593   2232     71    279    354       C  
ATOM   6771  O   GLU B 380     -55.001  -2.278 131.044  1.00 13.56           O  
ANISOU 6771  O   GLU B 380     1426   1544   2181     86    299    348       O  
ATOM   6772  CB  GLU B 380     -55.349  -5.528 131.913  1.00 11.83           C  
ANISOU 6772  CB  GLU B 380     1175   1341   1980     56    298    374       C  
ATOM   6773  CG  GLU B 380     -56.322  -6.547 132.442  1.00 20.84           C  
ANISOU 6773  CG  GLU B 380     2288   2482   3147     53    318    396       C  
ATOM   6774  CD  GLU B 380     -56.550  -7.728 131.531  1.00 24.11           C  
ANISOU 6774  CD  GLU B 380     2669   2899   3594     36    283    405       C  
ATOM   6775  OE1 GLU B 380     -57.211  -7.552 130.485  1.00 14.60           O  
ANISOU 6775  OE1 GLU B 380     1432   1693   2421     38    264    409       O  
ATOM   6776  OE2 GLU B 380     -56.117  -8.844 131.891  1.00 16.50           O  
ANISOU 6776  OE2 GLU B 380     1710   1936   2623     21    274    408       O  
ATOM   6777  N   GLU B 381     -53.919  -3.895 129.858  1.00 10.60           N  
ANISOU 6777  N   GLU B 381     1039   1184   1803     54    242    343       N  
ATOM   6778  CA  GLU B 381     -52.796  -3.059 129.431  1.00  9.82           C  
ANISOU 6778  CA  GLU B 381      967   1084   1679     51    225    327       C  
ATOM   6779  C   GLU B 381     -53.278  -1.768 128.753  1.00 12.36           C  
ANISOU 6779  C   GLU B 381     1284   1399   2015     66    227    329       C  
ATOM   6780  O   GLU B 381     -52.779  -0.696 129.070  1.00 12.41           O  
ANISOU 6780  O   GLU B 381     1317   1395   2003     71    236    319       O  
ATOM   6781  CB  GLU B 381     -51.863  -3.848 128.496  1.00 10.74           C  
ANISOU 6781  CB  GLU B 381     1080   1212   1789     35    187    320       C  
ATOM   6782  CG  GLU B 381     -50.633  -3.064 128.061  1.00 17.44           C  
ANISOU 6782  CG  GLU B 381     1953   2060   2613     30    172    306       C  
ATOM   6783  CD  GLU B 381     -49.724  -3.793 127.087  1.00 32.22           C  
ANISOU 6783  CD  GLU B 381     3821   3945   4478     17    140    299       C  
ATOM   6784  OE1 GLU B 381     -49.693  -5.046 127.122  1.00 21.71           O  
ANISOU 6784  OE1 GLU B 381     2479   2620   3151      9    129    300       O  
ATOM   6785  OE2 GLU B 381     -49.001  -3.108 126.327  1.00 16.74           O  
ANISOU 6785  OE2 GLU B 381     1868   1986   2507     14    127    294       O  
ATOM   6786  N   VAL B 382     -54.286  -1.873 127.854  1.00  9.35           N  
ANISOU 6786  N   VAL B 382      868   1019   1666     72    218    342       N  
ATOM   6787  CA  VAL B 382     -54.842  -0.703 127.146  1.00  9.44           C  
ANISOU 6787  CA  VAL B 382      872   1023   1694     87    217    347       C  
ATOM   6788  C   VAL B 382     -55.303   0.377 128.137  1.00 15.18           C  
ANISOU 6788  C   VAL B 382     1613   1734   2419    106    254    347       C  
ATOM   6789  O   VAL B 382     -55.006   1.563 127.939  1.00 15.21           O  
ANISOU 6789  O   VAL B 382     1635   1727   2415    114    255    340       O  
ATOM   6790  CB  VAL B 382     -55.980  -1.106 126.163  1.00 12.93           C  
ANISOU 6790  CB  VAL B 382     1271   1468   2173     91    199    363       C  
ATOM   6791  CG1 VAL B 382     -56.662   0.130 125.571  1.00 12.81           C  
ANISOU 6791  CG1 VAL B 382     1248   1442   2176    110    201    371       C  
ATOM   6792  CG2 VAL B 382     -55.450  -2.009 125.061  1.00 12.41           C  
ANISOU 6792  CG2 VAL B 382     1198   1414   2102     75    159    360       C  
ATOM   6793  N   HIS B 383     -55.976  -0.040 129.240  1.00 11.85           N  
ANISOU 6793  N   HIS B 383     1186   1312   2004    113    286    352       N  
ATOM   6794  CA  HIS B 383     -56.413   0.893 130.281  1.00 11.58           C  
ANISOU 6794  CA  HIS B 383     1169   1265   1965    134    326    349       C  
ATOM   6795  C   HIS B 383     -55.218   1.522 131.006  1.00 14.40           C  
ANISOU 6795  C   HIS B 383     1575   1614   2280    130    329    328       C  
ATOM   6796  O   HIS B 383     -55.230   2.723 131.274  1.00 15.02           O  
ANISOU 6796  O   HIS B 383     1676   1677   2354    146    343    320       O  
ATOM   6797  CB  HIS B 383     -57.346   0.197 131.290  1.00 12.54           C  
ANISOU 6797  CB  HIS B 383     1275   1391   2100    142    362    362       C  
ATOM   6798  CG  HIS B 383     -58.678  -0.181 130.723  1.00 16.31           C  
ANISOU 6798  CG  HIS B 383     1700   1870   2626    149    364    384       C  
ATOM   6799  ND1 HIS B 383     -59.610   0.783 130.361  1.00 18.17           N  
ANISOU 6799  ND1 HIS B 383     1916   2097   2891    171    375    392       N  
ATOM   6800  CD2 HIS B 383     -59.243  -1.404 130.591  1.00 18.49           C  
ANISOU 6800  CD2 HIS B 383     1942   2157   2928    137    359    400       C  
ATOM   6801  CE1 HIS B 383     -60.673   0.115 129.942  1.00 18.01           C  
ANISOU 6801  CE1 HIS B 383     1847   2081   2914    171    372    412       C  
ATOM   6802  NE2 HIS B 383     -60.501  -1.205 130.058  1.00 18.47           N  
ANISOU 6802  NE2 HIS B 383     1895   2151   2972    150    362    418       N  
ATOM   6803  N   PHE B 384     -54.172   0.712 131.313  1.00  9.42           N  
ANISOU 6803  N   PHE B 384      964    993   1623    110    314    319       N  
ATOM   6804  CA  PHE B 384     -52.988   1.214 132.028  1.00  8.41           C  
ANISOU 6804  CA  PHE B 384      881    858   1458    105    312    300       C  
ATOM   6805  C   PHE B 384     -52.110   2.112 131.151  1.00 12.65           C  
ANISOU 6805  C   PHE B 384     1430   1388   1990     97    284    290       C  
ATOM   6806  O   PHE B 384     -51.410   2.984 131.672  1.00 11.94           O  
ANISOU 6806  O   PHE B 384     1374   1284   1879     98    286    275       O  
ATOM   6807  CB  PHE B 384     -52.173   0.062 132.629  1.00  9.21           C  
ANISOU 6807  CB  PHE B 384      994    970   1534     87    303    295       C  
ATOM   6808  CG  PHE B 384     -52.897  -0.687 133.723  1.00  9.63           C  
ANISOU 6808  CG  PHE B 384     1046   1027   1585     95    334    305       C  
ATOM   6809  CD1 PHE B 384     -53.273  -0.044 134.899  1.00 11.94           C  
ANISOU 6809  CD1 PHE B 384     1366   1311   1861    113    370    300       C  
ATOM   6810  CD2 PHE B 384     -53.118  -2.054 133.622  1.00 10.80           C  
ANISOU 6810  CD2 PHE B 384     1169   1188   1745     82    327    319       C  
ATOM   6811  CE1 PHE B 384     -53.942  -0.734 135.908  1.00 12.85           C  
ANISOU 6811  CE1 PHE B 384     1480   1431   1971    121    403    312       C  
ATOM   6812  CE2 PHE B 384     -53.762  -2.752 134.649  1.00 13.98           C  
ANISOU 6812  CE2 PHE B 384     1571   1594   2146     88    358    331       C  
ATOM   6813  CZ  PHE B 384     -54.173  -2.087 135.783  1.00 12.12           C  
ANISOU 6813  CZ  PHE B 384     1361   1352   1893    107    398    329       C  
ATOM   6814  N   LEU B 385     -52.158   1.917 129.818  1.00  9.36           N  
ANISOU 6814  N   LEU B 385      986    979   1592     90    259    300       N  
ATOM   6815  CA  LEU B 385     -51.448   2.796 128.883  1.00  9.20           C  
ANISOU 6815  CA  LEU B 385      973    952   1569     84    237    296       C  
ATOM   6816  C   LEU B 385     -52.088   4.190 128.888  1.00 13.99           C  
ANISOU 6816  C   LEU B 385     1587   1538   2189    104    253    298       C  
ATOM   6817  O   LEU B 385     -51.382   5.194 129.029  1.00 13.45           O  
ANISOU 6817  O   LEU B 385     1547   1455   2110    103    249    287       O  
ATOM   6818  CB  LEU B 385     -51.465   2.202 127.455  1.00  8.80           C  
ANISOU 6818  CB  LEU B 385      894    916   1532     75    209    307       C  
ATOM   6819  CG  LEU B 385     -50.578   0.964 127.231  1.00 12.83           C  
ANISOU 6819  CG  LEU B 385     1402   1444   2028     56    187    302       C  
ATOM   6820  CD1 LEU B 385     -50.943   0.260 125.936  1.00 12.65           C  
ANISOU 6820  CD1 LEU B 385     1350   1436   2021     53    164    313       C  
ATOM   6821  CD2 LEU B 385     -49.103   1.336 127.242  1.00 14.73           C  
ANISOU 6821  CD2 LEU B 385     1668   1683   2244     41    174    290       C  
ATOM   6822  N   LYS B 386     -53.444   4.248 128.819  1.00 11.02           N  
ANISOU 6822  N   LYS B 386     1185   1160   1840    124    270    311       N  
ATOM   6823  CA  LYS B 386     -54.176   5.515 128.891  1.00 11.36           C  
ANISOU 6823  CA  LYS B 386     1232   1183   1900    147    288    313       C  
ATOM   6824  C   LYS B 386     -54.061   6.129 130.278  1.00 14.96           C  
ANISOU 6824  C   LYS B 386     1724   1623   2337    159    317    296       C  
ATOM   6825  O   LYS B 386     -53.885   7.338 130.398  1.00 14.76           O  
ANISOU 6825  O   LYS B 386     1723   1577   2310    169    321    287       O  
ATOM   6826  CB  LYS B 386     -55.654   5.320 128.510  1.00 14.20           C  
ANISOU 6826  CB  LYS B 386     1552   1547   2297    165    299    331       C  
ATOM   6827  CG  LYS B 386     -55.871   5.068 127.016  1.00 23.31           C  
ANISOU 6827  CG  LYS B 386     2676   2710   3471    158    265    346       C  
ATOM   6828  CD  LYS B 386     -57.358   4.997 126.654  1.00 29.95           C  
ANISOU 6828  CD  LYS B 386     3475   3551   4353    177    272    365       C  
ATOM   6829  CE  LYS B 386     -58.009   3.722 127.135  1.00 38.92           C  
ANISOU 6829  CE  LYS B 386     4584   4702   5503    173    283    372       C  
ATOM   6830  NZ  LYS B 386     -59.461   3.702 126.830  1.00 50.19           N  
ANISOU 6830  NZ  LYS B 386     5967   6127   6975    190    289    391       N  
ATOM   6831  N   ALA B 387     -54.083   5.278 131.338  1.00 10.99           N  
ANISOU 6831  N   ALA B 387     1229   1130   1818    157    336    291       N  
ATOM   6832  CA  ALA B 387     -53.967   5.747 132.722  1.00 10.73           C  
ANISOU 6832  CA  ALA B 387     1233   1084   1759    170    364    274       C  
ATOM   6833  C   ALA B 387     -52.652   6.492 132.954  1.00 12.72           C  
ANISOU 6833  C   ALA B 387     1528   1322   1984    158    344    253       C  
ATOM   6834  O   ALA B 387     -52.648   7.537 133.605  1.00 11.92           O  
ANISOU 6834  O   ALA B 387     1458   1199   1874    173    358    238       O  
ATOM   6835  CB  ALA B 387     -54.084   4.576 133.687  1.00 11.59           C  
ANISOU 6835  CB  ALA B 387     1343   1209   1851    166    383    276       C  
ATOM   6836  N   GLU B 388     -51.526   5.960 132.408  1.00  8.98           N  
ANISOU 6836  N   GLU B 388     1054    859   1499    131    311    252       N  
ATOM   6837  CA  GLU B 388     -50.215   6.606 132.560  1.00  9.10           C  
ANISOU 6837  CA  GLU B 388     1104    861   1494    116    289    234       C  
ATOM   6838  C   GLU B 388     -50.187   7.960 131.856  1.00 13.90           C  
ANISOU 6838  C   GLU B 388     1716   1446   2119    121    281    235       C  
ATOM   6839  O   GLU B 388     -49.725   8.943 132.434  1.00 13.83           O  
ANISOU 6839  O   GLU B 388     1742   1413   2100    124    280    218       O  
ATOM   6840  CB  GLU B 388     -49.086   5.701 132.029  1.00 10.02           C  
ANISOU 6840  CB  GLU B 388     1212    996   1601     87    258    236       C  
ATOM   6841  CG  GLU B 388     -47.717   6.370 132.086  1.00 16.12           C  
ANISOU 6841  CG  GLU B 388     2012   1755   2359     70    234    221       C  
ATOM   6842  CD  GLU B 388     -46.569   5.580 131.489  1.00 26.80           C  
ANISOU 6842  CD  GLU B 388     3352   3124   3706     44    206    224       C  
ATOM   6843  OE1 GLU B 388     -46.730   4.358 131.272  1.00 15.62           O  
ANISOU 6843  OE1 GLU B 388     1914   1731   2289     39    204    232       O  
ATOM   6844  OE2 GLU B 388     -45.486   6.176 131.291  1.00 14.21           O  
ANISOU 6844  OE2 GLU B 388     1771   1520   2109     29    186    217       O  
ATOM   6845  N   LEU B 389     -50.681   8.013 130.602  1.00 10.68           N  
ANISOU 6845  N   LEU B 389     1275   1044   1737    122    272    254       N  
ATOM   6846  CA  LEU B 389     -50.718   9.260 129.825  1.00 10.18           C  
ANISOU 6846  CA  LEU B 389     1215    960   1693    128    263    259       C  
ATOM   6847  C   LEU B 389     -51.561  10.331 130.523  1.00 13.94           C  
ANISOU 6847  C   LEU B 389     1709   1410   2178    156    289    251       C  
ATOM   6848  O   LEU B 389     -51.204  11.512 130.497  1.00 13.03           O  
ANISOU 6848  O   LEU B 389     1617   1268   2067    159    283    244       O  
ATOM   6849  CB  LEU B 389     -51.263   8.994 128.409  1.00  9.83           C  
ANISOU 6849  CB  LEU B 389     1132    930   1671    128    249    283       C  
ATOM   6850  CG  LEU B 389     -50.385   8.109 127.514  1.00 13.76           C  
ANISOU 6850  CG  LEU B 389     1616   1451   2160    102    222    290       C  
ATOM   6851  CD1 LEU B 389     -51.175   7.553 126.372  1.00 13.29           C  
ANISOU 6851  CD1 LEU B 389     1520   1409   2120    107    213    310       C  
ATOM   6852  CD2 LEU B 389     -49.165   8.880 127.000  1.00 16.17           C  
ANISOU 6852  CD2 LEU B 389     1939   1746   2458     85    202    288       C  
ATOM   6853  N   TYR B 390     -52.676   9.919 131.159  1.00 11.40           N  
ANISOU 6853  N   TYR B 390     1374   1094   1862    178    319    254       N  
ATOM   6854  CA  TYR B 390     -53.574  10.861 131.837  1.00 11.62           C  
ANISOU 6854  CA  TYR B 390     1417   1100   1900    210    349    246       C  
ATOM   6855  C   TYR B 390     -53.002  11.322 133.180  1.00 17.65           C  
ANISOU 6855  C   TYR B 390     2229   1845   2631    215    361    219       C  
ATOM   6856  O   TYR B 390     -53.146  12.492 133.538  1.00 18.92           O  
ANISOU 6856  O   TYR B 390     2417   1977   2796    233    370    205       O  
ATOM   6857  CB  TYR B 390     -54.992  10.247 132.026  1.00 11.65           C  
ANISOU 6857  CB  TYR B 390     1385   1118   1923    232    380    261       C  
ATOM   6858  CG  TYR B 390     -55.674   9.841 130.728  1.00 11.39           C  
ANISOU 6858  CG  TYR B 390     1303   1099   1924    230    365    287       C  
ATOM   6859  CD1 TYR B 390     -55.388  10.495 129.531  1.00 12.78           C  
ANISOU 6859  CD1 TYR B 390     1474   1267   2116    223    335    296       C  
ATOM   6860  CD2 TYR B 390     -56.679   8.877 130.717  1.00 12.04           C  
ANISOU 6860  CD2 TYR B 390     1347   1202   2027    237    380    303       C  
ATOM   6861  CE1 TYR B 390     -56.004  10.122 128.336  1.00 12.40           C  
ANISOU 6861  CE1 TYR B 390     1384   1232   2094    222    318    319       C  
ATOM   6862  CE2 TYR B 390     -57.322   8.512 129.532  1.00 12.63           C  
ANISOU 6862  CE2 TYR B 390     1378   1288   2133    235    361    325       C  
ATOM   6863  CZ  TYR B 390     -56.982   9.140 128.342  1.00 18.82           C  
ANISOU 6863  CZ  TYR B 390     2160   2065   2926    229    329    332       C  
ATOM   6864  OH  TYR B 390     -57.608   8.785 127.170  1.00 17.80           O  
ANISOU 6864  OH  TYR B 390     1993   1948   2824    228    307    353       O  
ATOM   6865  N   ALA B 391     -52.352  10.400 133.931  1.00 13.84           N  
ANISOU 6865  N   ALA B 391     1762   1380   2119    199    360    209       N  
ATOM   6866  CA  ALA B 391     -51.777  10.727 135.246  1.00 13.08           C  
ANISOU 6866  CA  ALA B 391     1714   1268   1986    203    367    182       C  
ATOM   6867  C   ALA B 391     -50.560  11.650 135.120  1.00 13.94           C  
ANISOU 6867  C   ALA B 391     1856   1352   2088    186    334    166       C  
ATOM   6868  O   ALA B 391     -50.310  12.465 136.010  1.00 13.15           O  
ANISOU 6868  O   ALA B 391     1798   1226   1970    196    338    142       O  
ATOM   6869  CB  ALA B 391     -51.392   9.455 135.979  1.00 13.64           C  
ANISOU 6869  CB  ALA B 391     1790   1363   2028    190    370    180       C  
ATOM   6870  N   ARG B 392     -49.815  11.535 134.009  1.00  8.61           N  
ANISOU 6870  N   ARG B 392     1160    684   1427    159    302    178       N  
ATOM   6871  CA  ARG B 392     -48.606  12.332 133.791  1.00  8.38           C  
ANISOU 6871  CA  ARG B 392     1154    634   1397    138    270    168       C  
ATOM   6872  C   ARG B 392     -48.908  13.677 133.101  1.00 14.42           C  
ANISOU 6872  C   ARG B 392     1920   1368   2190    148    267    173       C  
ATOM   6873  O   ARG B 392     -47.990  14.471 132.859  1.00 14.84           O  
ANISOU 6873  O   ARG B 392     1990   1399   2248    131    242    167       O  
ATOM   6874  CB  ARG B 392     -47.569  11.534 132.997  1.00  7.41           C  
ANISOU 6874  CB  ARG B 392     1009    534   1273    105    241    179       C  
ATOM   6875  CG  ARG B 392     -47.054  10.300 133.747  1.00  9.15           C  
ANISOU 6875  CG  ARG B 392     1234    777   1465     93    237    172       C  
ATOM   6876  CD  ARG B 392     -46.016   9.556 132.951  1.00 10.40           C  
ANISOU 6876  CD  ARG B 392     1370    956   1625     63    209    182       C  
ATOM   6877  NE  ARG B 392     -44.777  10.321 132.820  1.00 12.86           N  
ANISOU 6877  NE  ARG B 392     1699   1249   1939     42    181    173       N  
ATOM   6878  CZ  ARG B 392     -43.727   9.905 132.124  1.00 17.64           C  
ANISOU 6878  CZ  ARG B 392     2287   1867   2548     16    157    181       C  
ATOM   6879  NH1 ARG B 392     -43.767   8.747 131.482  1.00  5.71           N  
ANISOU 6879  NH1 ARG B 392      716    437   1015     16    154    173       N  
ATOM   6880  NH2 ARG B 392     -42.636  10.653 132.050  1.00  9.02           N  
ANISOU 6880  NH2 ARG B 392     1209    757   1463     -4    134    175       N  
ATOM   6881  N   GLY B 393     -50.191  13.930 132.823  1.00 10.57           N  
ANISOU 6881  N   GLY B 393     1414    880   1724    176    292    185       N  
ATOM   6882  CA  GLY B 393     -50.631  15.178 132.206  1.00 10.25           C  
ANISOU 6882  CA  GLY B 393     1373    809   1712    190    290    192       C  
ATOM   6883  C   GLY B 393     -50.241  15.305 130.747  1.00 13.96           C  
ANISOU 6883  C   GLY B 393     1817   1284   2203    170    264    217       C  
ATOM   6884  O   GLY B 393     -50.296  16.397 130.182  1.00 14.12           O  
ANISOU 6884  O   GLY B 393     1842   1278   2246    175    256    224       O  
ATOM   6885  N   PHE B 394     -49.843  14.187 130.123  1.00 10.86           N  
ANISOU 6885  N   PHE B 394     1397    926   1804    149    251    231       N  
ATOM   6886  CA  PHE B 394     -49.468  14.164 128.706  1.00 10.36           C  
ANISOU 6886  CA  PHE B 394     1308    873   1755    131    229    255       C  
ATOM   6887  C   PHE B 394     -50.700  14.367 127.830  1.00 13.78           C  
ANISOU 6887  C   PHE B 394     1712   1308   2214    153    237    278       C  
ATOM   6888  O   PHE B 394     -50.649  15.122 126.859  1.00 13.25           O  
ANISOU 6888  O   PHE B 394     1641   1229   2165    152    223    295       O  
ATOM   6889  CB  PHE B 394     -48.763  12.837 128.356  1.00 12.03           C  
ANISOU 6889  CB  PHE B 394     1501   1122   1950    106    215    261       C  
ATOM   6890  CG  PHE B 394     -47.281  12.796 128.694  1.00 14.03           C  
ANISOU 6890  CG  PHE B 394     1775   1372   2185     78    196    248       C  
ATOM   6891  CD1 PHE B 394     -46.804  13.351 129.876  1.00 17.63           C  
ANISOU 6891  CD1 PHE B 394     2267   1804   2629     77    197    223       C  
ATOM   6892  CD2 PHE B 394     -46.387  12.100 127.888  1.00 16.04           C  
ANISOU 6892  CD2 PHE B 394     2010   1649   2434     53    177    259       C  
ATOM   6893  CE1 PHE B 394     -45.443  13.302 130.192  1.00 18.86           C  
ANISOU 6893  CE1 PHE B 394     2438   1956   2772     51    175    211       C  
ATOM   6894  CE2 PHE B 394     -45.029  12.029 128.220  1.00 19.14           C  
ANISOU 6894  CE2 PHE B 394     2417   2040   2815     28    160    248       C  
ATOM   6895  CZ  PHE B 394     -44.568  12.624 129.372  1.00 17.43           C  
ANISOU 6895  CZ  PHE B 394     2234   1799   2590     26    157    225       C  
ATOM   6896  N   ILE B 395     -51.823  13.706 128.192  1.00 10.43           N  
ANISOU 6896  N   ILE B 395     1268    900   1795    174    259    279       N  
ATOM   6897  CA  ILE B 395     -53.114  13.879 127.516  1.00 10.95           C  
ANISOU 6897  CA  ILE B 395     1305    967   1891    198    266    298       C  
ATOM   6898  C   ILE B 395     -54.213  14.073 128.569  1.00 15.91           C  
ANISOU 6898  C   ILE B 395     1934   1584   2527    230    301    287       C  
ATOM   6899  O   ILE B 395     -54.165  13.445 129.627  1.00 15.06           O  
ANISOU 6899  O   ILE B 395     1837   1486   2399    231    320    271       O  
ATOM   6900  CB  ILE B 395     -53.429  12.661 126.581  1.00 14.13           C  
ANISOU 6900  CB  ILE B 395     1667   1406   2297    188    254    318       C  
ATOM   6901  CG1 ILE B 395     -52.299  12.436 125.552  1.00 14.63           C  
ANISOU 6901  CG1 ILE B 395     1731   1482   2348    159    223    327       C  
ATOM   6902  CG2 ILE B 395     -54.805  12.837 125.881  1.00 15.15           C  
ANISOU 6902  CG2 ILE B 395     1762   1534   2459    213    257    338       C  
ATOM   6903  CD1 ILE B 395     -52.431  11.128 124.746  1.00 21.99           C  
ANISOU 6903  CD1 ILE B 395     2630   2449   3276    148    209    340       C  
ATOM   6904  N   ALA B 396     -55.192  14.956 128.292  1.00 13.70           N  
ANISOU 6904  N   ALA B 396     1646   1284   2277    258    311    296       N  
ATOM   6905  CA  ALA B 396     -56.308  15.183 129.214  1.00 13.32           C  
ANISOU 6905  CA  ALA B 396     1595   1226   2240    292    348    288       C  
ATOM   6906  C   ALA B 396     -57.228  13.960 129.255  1.00 15.60           C  
ANISOU 6906  C   ALA B 396     1843   1547   2539    298    364    301       C  
ATOM   6907  O   ALA B 396     -57.613  13.436 128.207  1.00 15.12           O  
ANISOU 6907  O   ALA B 396     1744   1504   2496    291    345    323       O  
ATOM   6908  CB  ALA B 396     -57.093  16.417 128.793  1.00 14.38           C  
ANISOU 6908  CB  ALA B 396     1726   1329   2408    321    351    297       C  
ATOM   6909  N   GLY B 397     -57.515  13.480 130.458  1.00 11.31           N  
ANISOU 6909  N   GLY B 397     1307   1010   1980    309    397    287       N  
ATOM   6910  CA  GLY B 397     -58.364  12.312 130.649  1.00 11.27           C  
ANISOU 6910  CA  GLY B 397     1264   1033   1985    313    416    300       C  
ATOM   6911  C   GLY B 397     -58.496  11.900 132.097  1.00 15.21           C  
ANISOU 6911  C   GLY B 397     1783   1537   2460    323    454    284       C  
ATOM   6912  O   GLY B 397     -57.824  12.458 132.971  1.00 15.06           O  
ANISOU 6912  O   GLY B 397     1810   1501   2410    326    462    260       O  
ATOM   6913  N   ASP B 398     -59.385  10.927 132.371  1.00 12.03           N  
ANISOU 6913  N   ASP B 398     1344   1156   2070    330    478    298       N  
ATOM   6914  CA  ASP B 398     -59.616  10.440 133.729  1.00 12.17           C  
ANISOU 6914  CA  ASP B 398     1377   1181   2065    341    520    289       C  
ATOM   6915  C   ASP B 398     -58.669   9.277 134.050  1.00 16.54           C  
ANISOU 6915  C   ASP B 398     1944   1757   2584    309    505    285       C  
ATOM   6916  O   ASP B 398     -58.931   8.132 133.657  1.00 15.79           O  
ANISOU 6916  O   ASP B 398     1813   1685   2502    293    497    303       O  
ATOM   6917  CB  ASP B 398     -61.090  10.015 133.909  1.00 14.37           C  
ANISOU 6917  CB  ASP B 398     1608   1471   2380    365    557    310       C  
ATOM   6918  CG  ASP B 398     -61.496   9.758 135.357  1.00 24.14           C  
ANISOU 6918  CG  ASP B 398     2864   2714   3596    385    610    302       C  
ATOM   6919  OD1 ASP B 398     -60.592   9.612 136.214  1.00 24.51           O  
ANISOU 6919  OD1 ASP B 398     2958   2760   3594    375    613    282       O  
ATOM   6920  OD2 ASP B 398     -62.709   9.645 135.618  1.00 31.17           O  
ANISOU 6920  OD2 ASP B 398     3718   3608   4516    410    649    318       O  
ATOM   6921  N   ALA B 399     -57.560   9.573 134.757  1.00 13.69           N  
ANISOU 6921  N   ALA B 399     1636   1387   2181    299    498    260       N  
ATOM   6922  CA  ALA B 399     -56.548   8.567 135.088  1.00 13.33           C  
ANISOU 6922  CA  ALA B 399     1606   1358   2102    270    480    255       C  
ATOM   6923  C   ALA B 399     -57.091   7.513 136.059  1.00 16.87           C  
ANISOU 6923  C   ALA B 399     2047   1826   2537    275    515    262       C  
ATOM   6924  O   ALA B 399     -56.858   6.322 135.863  1.00 16.46           O  
ANISOU 6924  O   ALA B 399     1976   1796   2484    253    501    274       O  
ATOM   6925  CB  ALA B 399     -55.314   9.240 135.675  1.00 14.16           C  
ANISOU 6925  CB  ALA B 399     1767   1445   2168    261    464    227       C  
ATOM   6926  N   LYS B 400     -57.841   7.954 137.095  1.00 13.83           N  
ANISOU 6926  N   LYS B 400     1678   1433   2145    307    561    256       N  
ATOM   6927  CA  LYS B 400     -58.410   7.050 138.105  1.00 13.50           C  
ANISOU 6927  CA  LYS B 400     1632   1408   2089    316    602    266       C  
ATOM   6928  C   LYS B 400     -59.330   5.999 137.465  1.00 17.07           C  
ANISOU 6928  C   LYS B 400     2021   1882   2584    308    607    299       C  
ATOM   6929  O   LYS B 400     -59.177   4.805 137.733  1.00 16.57           O  
ANISOU 6929  O   LYS B 400     1949   1837   2511    289    607    310       O  
ATOM   6930  CB  LYS B 400     -59.174   7.854 139.177  1.00 16.81           C  
ANISOU 6930  CB  LYS B 400     2075   1814   2497    356    655    255       C  
ATOM   6931  CG  LYS B 400     -59.767   6.989 140.289  1.00 25.69           C  
ANISOU 6931  CG  LYS B 400     3201   2957   3604    367    703    267       C  
ATOM   6932  CD  LYS B 400     -60.553   7.824 141.290  1.00 31.90           C  
ANISOU 6932  CD  LYS B 400     4011   3731   4378    411    759    256       C  
ATOM   6933  CE  LYS B 400     -61.232   6.968 142.327  1.00 39.05           C  
ANISOU 6933  CE  LYS B 400     4912   4656   5268    424    813    273       C  
ATOM   6934  NZ  LYS B 400     -61.953   7.792 143.337  1.00 43.79           N  
ANISOU 6934  NZ  LYS B 400     5540   5246   5852    470    871    261       N  
ATOM   6935  N   SER B 401     -60.280   6.445 136.611  1.00 13.45           N  
ANISOU 6935  N   SER B 401     1518   1417   2173    322    609    313       N  
ATOM   6936  CA  SER B 401     -61.228   5.538 135.951  1.00 13.32           C  
ANISOU 6936  CA  SER B 401     1439   1418   2204    315    609    344       C  
ATOM   6937  C   SER B 401     -60.526   4.518 135.049  1.00 16.17           C  
ANISOU 6937  C   SER B 401     1784   1794   2567    278    560    351       C  
ATOM   6938  O   SER B 401     -60.919   3.354 135.026  1.00 15.50           O  
ANISOU 6938  O   SER B 401     1667   1725   2497    264    562    370       O  
ATOM   6939  CB  SER B 401     -62.267   6.323 135.162  1.00 16.89           C  
ANISOU 6939  CB  SER B 401     1852   1860   2706    337    612    355       C  
ATOM   6940  OG  SER B 401     -63.272   6.848 136.018  1.00 23.59           O  
ANISOU 6940  OG  SER B 401     2701   2698   3562    375    665    355       O  
ATOM   6941  N   GLU B 402     -59.458   4.945 134.330  1.00 12.12           N  
ANISOU 6941  N   GLU B 402     1293   1274   2037    261    516    336       N  
ATOM   6942  CA  GLU B 402     -58.677   4.026 133.491  1.00 11.27           C  
ANISOU 6942  CA  GLU B 402     1175   1180   1926    228    471    339       C  
ATOM   6943  C   GLU B 402     -57.890   3.036 134.349  1.00 14.64           C  
ANISOU 6943  C   GLU B 402     1627   1618   2316    209    473    333       C  
ATOM   6944  O   GLU B 402     -57.858   1.845 134.040  1.00 13.13           O  
ANISOU 6944  O   GLU B 402     1413   1443   2134    190    458    346       O  
ATOM   6945  CB  GLU B 402     -57.732   4.801 132.552  1.00 12.04           C  
ANISOU 6945  CB  GLU B 402     1292   1267   2015    216    431    327       C  
ATOM   6946  CG  GLU B 402     -58.446   5.476 131.384  1.00 20.36           C  
ANISOU 6946  CG  GLU B 402     2314   2313   3108    228    416    339       C  
ATOM   6947  CD  GLU B 402     -59.134   4.525 130.413  1.00 33.31           C  
ANISOU 6947  CD  GLU B 402     3903   3970   4784    218    395    361       C  
ATOM   6948  OE1 GLU B 402     -58.789   3.321 130.411  1.00 20.50           O  
ANISOU 6948  OE1 GLU B 402     2272   2363   3153    196    383    364       O  
ATOM   6949  OE2 GLU B 402     -59.981   4.997 129.623  1.00 21.17           O  
ANISOU 6949  OE2 GLU B 402     2334   2426   3282    231    388    374       O  
ATOM   6950  N   TYR B 403     -57.303   3.524 135.465  1.00 12.12           N  
ANISOU 6950  N   TYR B 403     1358   1291   1956    217    492    314       N  
ATOM   6951  CA  TYR B 403     -56.560   2.683 136.406  1.00 11.88           C  
ANISOU 6951  CA  TYR B 403     1357   1270   1887    203    495    307       C  
ATOM   6952  C   TYR B 403     -57.455   1.568 136.973  1.00 16.19           C  
ANISOU 6952  C   TYR B 403     1876   1831   2445    206    527    331       C  
ATOM   6953  O   TYR B 403     -57.070   0.398 136.949  1.00 15.17           O  
ANISOU 6953  O   TYR B 403     1738   1715   2312    184    510    339       O  
ATOM   6954  CB  TYR B 403     -55.972   3.547 137.551  1.00 12.69           C  
ANISOU 6954  CB  TYR B 403     1518   1358   1944    217    512    282       C  
ATOM   6955  CG  TYR B 403     -55.468   2.742 138.731  1.00 13.32           C  
ANISOU 6955  CG  TYR B 403     1630   1447   1982    211    523    278       C  
ATOM   6956  CD1 TYR B 403     -54.172   2.237 138.753  1.00 14.74           C  
ANISOU 6956  CD1 TYR B 403     1834   1631   2135    185    486    267       C  
ATOM   6957  CD2 TYR B 403     -56.259   2.555 139.862  1.00 14.23           C  
ANISOU 6957  CD2 TYR B 403     1756   1566   2084    233    573    286       C  
ATOM   6958  CE1 TYR B 403     -53.690   1.527 139.851  1.00 15.09           C  
ANISOU 6958  CE1 TYR B 403     1910   1683   2141    180    493    264       C  
ATOM   6959  CE2 TYR B 403     -55.794   1.835 140.960  1.00 15.21           C  
ANISOU 6959  CE2 TYR B 403     1914   1699   2167    228    583    284       C  
ATOM   6960  CZ  TYR B 403     -54.505   1.326 140.953  1.00 23.44           C  
ANISOU 6960  CZ  TYR B 403     2980   2745   3183    202    541    273       C  
ATOM   6961  OH  TYR B 403     -54.033   0.629 142.041  1.00 24.76           O  
ANISOU 6961  OH  TYR B 403     3182   2919   3308    198    548    272       O  
ATOM   6962  N   GLU B 404     -58.661   1.934 137.454  1.00 12.93           N  
ANISOU 6962  N   GLU B 404     1447   1415   2051    233    573    342       N  
ATOM   6963  CA  GLU B 404     -59.588   0.972 138.050  1.00 12.80           C  
ANISOU 6963  CA  GLU B 404     1402   1411   2050    237    610    367       C  
ATOM   6964  C   GLU B 404     -60.175   0.023 137.010  1.00 17.03           C  
ANISOU 6964  C   GLU B 404     1877   1957   2635    219    587    392       C  
ATOM   6965  O   GLU B 404     -60.418  -1.140 137.317  1.00 16.37           O  
ANISOU 6965  O   GLU B 404     1775   1884   2559    206    595    411       O  
ATOM   6966  CB  GLU B 404     -60.697   1.691 138.815  1.00 14.56           C  
ANISOU 6966  CB  GLU B 404     1622   1628   2281    273    668    373       C  
ATOM   6967  CG  GLU B 404     -60.198   2.412 140.053  1.00 22.54           C  
ANISOU 6967  CG  GLU B 404     2697   2631   3237    293    696    349       C  
ATOM   6968  CD  GLU B 404     -61.285   3.043 140.894  1.00 35.82           C  
ANISOU 6968  CD  GLU B 404     4379   4308   4922    332    759    353       C  
ATOM   6969  OE1 GLU B 404     -62.144   3.752 140.322  1.00 38.42           O  
ANISOU 6969  OE1 GLU B 404     4674   4629   5294    352    769    359       O  
ATOM   6970  OE2 GLU B 404     -61.218   2.915 142.136  1.00 21.91           O  
ANISOU 6970  OE2 GLU B 404     2657   2550   3117    346    796    348       O  
ATOM   6971  N   ALA B 405     -60.366   0.505 135.761  1.00 14.42           N  
ANISOU 6971  N   ALA B 405     1519   1622   2340    217    556    392       N  
ATOM   6972  CA  ALA B 405     -60.882  -0.340 134.672  1.00 14.24           C  
ANISOU 6972  CA  ALA B 405     1442   1606   2362    200    526    411       C  
ATOM   6973  C   ALA B 405     -59.867  -1.434 134.297  1.00 18.49           C  
ANISOU 6973  C   ALA B 405     1988   2153   2882    168    485    407       C  
ATOM   6974  O   ALA B 405     -60.255  -2.565 134.005  1.00 18.40           O  
ANISOU 6974  O   ALA B 405     1943   2150   2897    152    474    425       O  
ATOM   6975  CB  ALA B 405     -61.209   0.511 133.457  1.00 14.67           C  
ANISOU 6975  CB  ALA B 405     1474   1653   2448    208    499    410       C  
ATOM   6976  N   GLY B 406     -58.579  -1.091 134.343  1.00 14.92           N  
ANISOU 6976  N   GLY B 406     1582   1699   2388    159    462    384       N  
ATOM   6977  CA  GLY B 406     -57.507  -2.043 134.080  1.00 14.27           C  
ANISOU 6977  CA  GLY B 406     1511   1625   2286    132    425    378       C  
ATOM   6978  C   GLY B 406     -57.382  -3.095 135.162  1.00 17.62           C  
ANISOU 6978  C   GLY B 406     1947   2056   2691    124    445    386       C  
ATOM   6979  O   GLY B 406     -57.215  -4.283 134.862  1.00 17.05           O  
ANISOU 6979  O   GLY B 406     1857   1991   2630    104    423    396       O  
ATOM   6980  N   VAL B 407     -57.488  -2.669 136.447  1.00 13.76           N  
ANISOU 6980  N   VAL B 407     1491   1564   2174    141    487    383       N  
ATOM   6981  CA  VAL B 407     -57.409  -3.588 137.596  1.00 13.46           C  
ANISOU 6981  CA  VAL B 407     1469   1532   2112    136    511    394       C  
ATOM   6982  C   VAL B 407     -58.610  -4.550 137.600  1.00 17.97           C  
ANISOU 6982  C   VAL B 407     1991   2110   2727    134    533    426       C  
ATOM   6983  O   VAL B 407     -58.429  -5.757 137.774  1.00 17.07           O  
ANISOU 6983  O   VAL B 407     1870   2001   2615    115    524    439       O  
ATOM   6984  CB  VAL B 407     -57.284  -2.814 138.946  1.00 17.29           C  
ANISOU 6984  CB  VAL B 407     2004   2013   2552    159    551    382       C  
ATOM   6985  CG1 VAL B 407     -57.213  -3.781 140.130  1.00 17.19           C  
ANISOU 6985  CG1 VAL B 407     2011   2008   2511    155    576    395       C  
ATOM   6986  CG2 VAL B 407     -56.072  -1.887 138.935  1.00 16.73           C  
ANISOU 6986  CG2 VAL B 407     1981   1934   2444    158    524    350       C  
ATOM   6987  N   ARG B 408     -59.837  -4.015 137.330  1.00 15.54           N  
ANISOU 6987  N   ARG B 408     1646   1799   2459    152    559    439       N  
ATOM   6988  CA  ARG B 408     -61.064  -4.828 137.280  1.00 15.47           C  
ANISOU 6988  CA  ARG B 408     1583   1794   2500    150    581    472       C  
ATOM   6989  C   ARG B 408     -61.026  -5.851 136.141  1.00 19.00           C  
ANISOU 6989  C   ARG B 408     1991   2242   2984    122    531    480       C  
ATOM   6990  O   ARG B 408     -61.514  -6.967 136.304  1.00 19.79           O  
ANISOU 6990  O   ARG B 408     2063   2345   3111    109    536    504       O  
ATOM   6991  CB  ARG B 408     -62.309  -3.933 137.164  1.00 16.10           C  
ANISOU 6991  CB  ARG B 408     1630   1870   2617    177    615    482       C  
ATOM   6992  CG  ARG B 408     -62.622  -3.171 138.443  1.00 27.55           C  
ANISOU 6992  CG  ARG B 408     3111   3319   4037    206    675    479       C  
ATOM   6993  CD  ARG B 408     -63.873  -2.325 138.307  1.00 37.93           C  
ANISOU 6993  CD  ARG B 408     4390   4629   5393    235    710    490       C  
ATOM   6994  NE  ARG B 408     -64.189  -1.626 139.555  1.00 48.41           N  
ANISOU 6994  NE  ARG B 408     5749   5955   6690    267    772    486       N  
ATOM   6995  CZ  ARG B 408     -64.938  -2.145 140.525  1.00 67.68           C  
ANISOU 6995  CZ  ARG B 408     8178   8404   9133    277    827    511       C  
ATOM   6996  NH1 ARG B 408     -65.450  -3.363 140.398  1.00 60.27           N  
ANISOU 6996  NH1 ARG B 408     7194   7473   8232    256    828    543       N  
ATOM   6997  NH2 ARG B 408     -65.170  -1.456 141.631  1.00 54.26           N  
ANISOU 6997  NH2 ARG B 408     6513   6703   7399    309    883    504       N  
ATOM   6998  N   ALA B 409     -60.436  -5.476 134.992  1.00 15.04           N  
ANISOU 6998  N   ALA B 409     1491   1739   2484    115    483    461       N  
ATOM   6999  CA  ALA B 409     -60.289  -6.394 133.854  1.00 14.21           C  
ANISOU 6999  CA  ALA B 409     1357   1635   2406     91    432    464       C  
ATOM   7000  C   ALA B 409     -59.278  -7.507 134.174  1.00 16.83           C  
ANISOU 7000  C   ALA B 409     1714   1971   2710     69    412    459       C  
ATOM   7001  O   ALA B 409     -59.414  -8.626 133.674  1.00 15.58           O  
ANISOU 7001  O   ALA B 409     1528   1812   2578     50    385    470       O  
ATOM   7002  CB  ALA B 409     -59.848  -5.627 132.618  1.00 14.55           C  
ANISOU 7002  CB  ALA B 409     1402   1677   2449     92    391    445       C  
ATOM   7003  N   SER B 410     -58.268  -7.200 135.032  1.00 12.95           N  
ANISOU 7003  N   SER B 410     1274   1481   2165     72    422    443       N  
ATOM   7004  CA  SER B 410     -57.247  -8.174 135.426  1.00 11.67           C  
ANISOU 7004  CA  SER B 410     1138   1322   1974     54    403    438       C  
ATOM   7005  C   SER B 410     -57.803  -9.175 136.426  1.00 15.67           C  
ANISOU 7005  C   SER B 410     1637   1829   2488     49    434    465       C  
ATOM   7006  O   SER B 410     -57.537 -10.368 136.309  1.00 15.03           O  
ANISOU 7006  O   SER B 410     1547   1747   2416     30    412    473       O  
ATOM   7007  CB  SER B 410     -56.028  -7.468 136.005  1.00 13.79           C  
ANISOU 7007  CB  SER B 410     1461   1590   2188     59    401    414       C  
ATOM   7008  OG  SER B 410     -54.981  -8.386 136.268  1.00 13.87           O  
ANISOU 7008  OG  SER B 410     1494   1603   2173     41    376    408       O  
ATOM   7009  N   PHE B 411     -58.610  -8.698 137.397  1.00 12.30           N  
ANISOU 7009  N   PHE B 411     1213   1403   2058     68    488    479       N  
ATOM   7010  CA  PHE B 411     -59.270  -9.582 138.363  1.00 12.13           C  
ANISOU 7010  CA  PHE B 411     1181   1382   2045     66    526    510       C  
ATOM   7011  C   PHE B 411     -60.295 -10.474 137.666  1.00 16.76           C  
ANISOU 7011  C   PHE B 411     1705   1965   2697     52    517    536       C  
ATOM   7012  O   PHE B 411     -60.470 -11.628 138.055  1.00 16.54           O  
ANISOU 7012  O   PHE B 411     1665   1935   2683     36    521    559       O  
ATOM   7013  CB  PHE B 411     -59.926  -8.767 139.493  1.00 13.95           C  
ANISOU 7013  CB  PHE B 411     1429   1616   2257     93    589    518       C  
ATOM   7014  CG  PHE B 411     -58.979  -8.409 140.622  1.00 15.26           C  
ANISOU 7014  CG  PHE B 411     1660   1785   2355    103    604    501       C  
ATOM   7015  CD1 PHE B 411     -57.878  -7.586 140.397  1.00 17.19           C  
ANISOU 7015  CD1 PHE B 411     1945   2026   2562    105    573    466       C  
ATOM   7016  CD2 PHE B 411     -59.223  -8.841 141.920  1.00 17.41           C  
ANISOU 7016  CD2 PHE B 411     1954   2060   2600    110    649    521       C  
ATOM   7017  CE1 PHE B 411     -57.004  -7.264 141.435  1.00 17.63           C  
ANISOU 7017  CE1 PHE B 411     2061   2082   2557    113    581    450       C  
ATOM   7018  CE2 PHE B 411     -58.351  -8.509 142.959  1.00 19.47           C  
ANISOU 7018  CE2 PHE B 411     2279   2324   2796    120    658    504       C  
ATOM   7019  CZ  PHE B 411     -57.246  -7.727 142.709  1.00 17.07           C  
ANISOU 7019  CZ  PHE B 411     2014   2016   2457    121    622    468       C  
ATOM   7020  N   ALA B 412     -60.917  -9.964 136.572  1.00 13.59           N  
ANISOU 7020  N   ALA B 412     1265   1561   2336     56    498    533       N  
ATOM   7021  CA  ALA B 412     -61.829 -10.762 135.753  1.00 13.84           C  
ANISOU 7021  CA  ALA B 412     1238   1588   2433     41    478    553       C  
ATOM   7022  C   ALA B 412     -61.047 -11.838 134.999  1.00 17.72           C  
ANISOU 7022  C   ALA B 412     1731   2075   2927     15    421    544       C  
ATOM   7023  O   ALA B 412     -61.461 -13.000 134.971  1.00 17.83           O  
ANISOU 7023  O   ALA B 412     1716   2082   2975     -3    412    565       O  
ATOM   7024  CB  ALA B 412     -62.571  -9.866 134.771  1.00 14.58           C  
ANISOU 7024  CB  ALA B 412     1298   1681   2563     54    467    549       C  
ATOM   7025  N   THR B 413     -59.856 -11.469 134.479  1.00 13.40           N  
ANISOU 7025  N   THR B 413     1220   1531   2341     13    385    512       N  
ATOM   7026  CA  THR B 413     -58.961 -12.398 133.789  1.00 12.85           C  
ANISOU 7026  CA  THR B 413     1157   1459   2266     -7    333    499       C  
ATOM   7027  C   THR B 413     -58.521 -13.551 134.729  1.00 17.48           C  
ANISOU 7027  C   THR B 413     1762   2042   2838    -21    341    512       C  
ATOM   7028  O   THR B 413     -58.441 -14.702 134.295  1.00 17.57           O  
ANISOU 7028  O   THR B 413     1757   2046   2873    -40    308    517       O  
ATOM   7029  CB  THR B 413     -57.743 -11.622 133.215  1.00 20.22           C  
ANISOU 7029  CB  THR B 413     2128   2398   3158     -2    304    465       C  
ATOM   7030  OG1 THR B 413     -58.194 -10.749 132.175  1.00 18.54           O  
ANISOU 7030  OG1 THR B 413     1893   2186   2964      7    290    457       O  
ATOM   7031  CG2 THR B 413     -56.656 -12.546 132.680  1.00 19.60           C  
ANISOU 7031  CG2 THR B 413     2062   2318   3065    -20    258    450       C  
ATOM   7032  N   TRP B 414     -58.273 -13.236 136.017  1.00 14.04           N  
ANISOU 7032  N   TRP B 414     1361   1611   2362    -11    382    517       N  
ATOM   7033  CA  TRP B 414     -57.793 -14.223 136.984  1.00 14.29           C  
ANISOU 7033  CA  TRP B 414     1417   1640   2373    -21    390    531       C  
ATOM   7034  C   TRP B 414     -58.913 -14.825 137.850  1.00 19.25           C  
ANISOU 7034  C   TRP B 414     2020   2264   3029    -23    436    570       C  
ATOM   7035  O   TRP B 414     -58.632 -15.592 138.774  1.00 19.63           O  
ANISOU 7035  O   TRP B 414     2090   2310   3058    -30    450    586       O  
ATOM   7036  CB  TRP B 414     -56.682 -13.629 137.856  1.00 13.06           C  
ANISOU 7036  CB  TRP B 414     1320   1491   2152    -11    400    512       C  
ATOM   7037  CG  TRP B 414     -55.396 -13.435 137.119  1.00 13.68           C  
ANISOU 7037  CG  TRP B 414     1421   1571   2206    -16    352    479       C  
ATOM   7038  CD1 TRP B 414     -54.921 -12.270 136.592  1.00 16.22           C  
ANISOU 7038  CD1 TRP B 414     1757   1897   2509     -6    342    452       C  
ATOM   7039  CD2 TRP B 414     -54.504 -14.465 136.683  1.00 13.37           C  
ANISOU 7039  CD2 TRP B 414     1387   1528   2166    -33    308    470       C  
ATOM   7040  NE1 TRP B 414     -53.747 -12.501 135.918  1.00 15.37           N  
ANISOU 7040  NE1 TRP B 414     1663   1791   2387    -16    297    430       N  
ATOM   7041  CE2 TRP B 414     -53.473 -13.844 135.948  1.00 16.90           C  
ANISOU 7041  CE2 TRP B 414     1851   1980   2591    -32    275    439       C  
ATOM   7042  CE3 TRP B 414     -54.462 -15.858 136.863  1.00 14.47           C  
ANISOU 7042  CE3 TRP B 414     1517   1658   2322    -50    294    487       C  
ATOM   7043  CZ2 TRP B 414     -52.415 -14.567 135.389  1.00 16.15           C  
ANISOU 7043  CZ2 TRP B 414     1763   1883   2490    -44    232    424       C  
ATOM   7044  CZ3 TRP B 414     -53.410 -16.570 136.314  1.00 15.44           C  
ANISOU 7044  CZ3 TRP B 414     1650   1779   2440    -61    248    470       C  
ATOM   7045  CH2 TRP B 414     -52.408 -15.930 135.580  1.00 15.84           C  
ANISOU 7045  CH2 TRP B 414     1716   1836   2467    -57    218    438       C  
ATOM   7046  N   GLY B 415     -60.165 -14.533 137.494  1.00 15.89           N  
ANISOU 7046  N   GLY B 415     1548   1837   2651    -18    455    587       N  
ATOM   7047  CA  GLY B 415     -61.331 -15.093 138.176  1.00 16.17           C  
ANISOU 7047  CA  GLY B 415     1550   1869   2724    -20    499    627       C  
ATOM   7048  C   GLY B 415     -61.451 -14.695 139.639  1.00 19.66           C  
ANISOU 7048  C   GLY B 415     2025   2320   3125     -2    563    643       C  
ATOM   7049  O   GLY B 415     -61.896 -15.494 140.469  1.00 18.42           O  
ANISOU 7049  O   GLY B 415     1861   2160   2977     -9    595    676       O  
ATOM   7050  N   VAL B 416     -61.087 -13.443 139.964  1.00 16.24           N  
ANISOU 7050  N   VAL B 416     1628   1896   2647     22    582    619       N  
ATOM   7051  CA  VAL B 416     -61.198 -12.929 141.336  1.00 15.98           C  
ANISOU 7051  CA  VAL B 416     1632   1870   2568     44    642    628       C  
ATOM   7052  C   VAL B 416     -61.976 -11.596 141.378  1.00 19.33           C  
ANISOU 7052  C   VAL B 416     2046   2300   2997     73    682    621       C  
ATOM   7053  O   VAL B 416     -61.690 -10.736 142.214  1.00 19.16           O  
ANISOU 7053  O   VAL B 416     2070   2284   2925     96    714    607       O  
ATOM   7054  CB  VAL B 416     -59.811 -12.823 142.045  1.00 19.62           C  
ANISOU 7054  CB  VAL B 416     2164   2336   2957     46    629    604       C  
ATOM   7055  CG1 VAL B 416     -59.368 -14.176 142.581  1.00 19.53           C  
ANISOU 7055  CG1 VAL B 416     2165   2320   2936     26    618    625       C  
ATOM   7056  CG2 VAL B 416     -58.753 -12.231 141.111  1.00 18.77           C  
ANISOU 7056  CG2 VAL B 416     2074   2226   2832     43    573    563       C  
ATOM   7057  N   THR B 417     -63.016 -11.471 140.520  1.00 15.46           N  
ANISOU 7057  N   THR B 417     1495   1806   2571     72    680    633       N  
ATOM   7058  CA  THR B 417     -63.855 -10.265 140.437  1.00 15.42           C  
ANISOU 7058  CA  THR B 417     1472   1804   2583    100    714    630       C  
ATOM   7059  C   THR B 417     -64.547  -9.946 141.779  1.00 21.04           C  
ANISOU 7059  C   THR B 417     2196   2523   3275    125    792    652       C  
ATOM   7060  O   THR B 417     -64.684  -8.775 142.135  1.00 21.08           O  
ANISOU 7060  O   THR B 417     2222   2531   3256    155    824    635       O  
ATOM   7061  CB  THR B 417     -64.871 -10.408 139.281  1.00 22.66           C  
ANISOU 7061  CB  THR B 417     2317   2715   3577     92    693    644       C  
ATOM   7062  OG1 THR B 417     -64.158 -10.527 138.053  1.00 21.36           O  
ANISOU 7062  OG1 THR B 417     2152   2545   3418     74    623    619       O  
ATOM   7063  CG2 THR B 417     -65.846  -9.233 139.204  1.00 21.51           C  
ANISOU 7063  CG2 THR B 417     2146   2572   3456    122    729    645       C  
ATOM   7064  N   SER B 418     -64.960 -10.990 142.529  1.00 18.54           N  
ANISOU 7064  N   SER B 418     1867   2209   2969    114    824    688       N  
ATOM   7065  CA  SER B 418     -65.653 -10.805 143.815  1.00 19.24           C  
ANISOU 7065  CA  SER B 418     1966   2306   3038    138    903    713       C  
ATOM   7066  C   SER B 418     -64.749 -10.126 144.871  1.00 23.36           C  
ANISOU 7066  C   SER B 418     2569   2834   3472    160    924    688       C  
ATOM   7067  O   SER B 418     -65.239  -9.704 145.919  1.00 23.74           O  
ANISOU 7067  O   SER B 418     2637   2890   3493    187    990    700       O  
ATOM   7068  CB  SER B 418     -66.163 -12.142 144.344  1.00 23.00           C  
ANISOU 7068  CB  SER B 418     2415   2781   3542    117    927    760       C  
ATOM   7069  OG  SER B 418     -65.096 -13.048 144.568  1.00 31.21           O  
ANISOU 7069  OG  SER B 418     3494   3818   4545     94    890    756       O  
ATOM   7070  N   GLU B 419     -63.439  -9.994 144.573  1.00 19.06           N  
ANISOU 7070  N   GLU B 419     2071   2286   2884    149    869    652       N  
ATOM   7071  CA  GLU B 419     -62.479  -9.410 145.517  1.00 18.45           C  
ANISOU 7071  CA  GLU B 419     2072   2212   2726    166    878    626       C  
ATOM   7072  C   GLU B 419     -62.010  -8.002 145.079  1.00 19.69           C  
ANISOU 7072  C   GLU B 419     2255   2365   2862    185    858    582       C  
ATOM   7073  O   GLU B 419     -61.393  -7.290 145.874  1.00 18.43           O  
ANISOU 7073  O   GLU B 419     2156   2206   2640    204    870    558       O  
ATOM   7074  CB  GLU B 419     -61.257 -10.343 145.692  1.00 19.51           C  
ANISOU 7074  CB  GLU B 419     2244   2345   2825    140    832    620       C  
ATOM   7075  CG  GLU B 419     -61.619 -11.771 146.093  1.00 32.21           C  
ANISOU 7075  CG  GLU B 419     3830   3954   4455    120    845    663       C  
ATOM   7076  CD  GLU B 419     -62.225 -11.922 147.476  1.00 60.84           C  
ANISOU 7076  CD  GLU B 419     7477   7589   8051    138    917    695       C  
ATOM   7077  OE1 GLU B 419     -61.939 -11.071 148.349  1.00 63.83           O  
ANISOU 7077  OE1 GLU B 419     7912   7974   8368    166    948    676       O  
ATOM   7078  OE2 GLU B 419     -62.914 -12.941 147.710  1.00 59.43           O  
ANISOU 7078  OE2 GLU B 419     7263   7410   7908    124    942    738       O  
ATOM   7079  N   VAL B 420     -62.303  -7.607 143.813  1.00 15.53           N  
ANISOU 7079  N   VAL B 420     1683   1833   2387    179    824    572       N  
ATOM   7080  CA  VAL B 420     -61.765  -6.362 143.233  1.00 15.39           C  
ANISOU 7080  CA  VAL B 420     1686   1808   2353    192    796    533       C  
ATOM   7081  C   VAL B 420     -62.310  -5.060 143.904  1.00 20.39           C  
ANISOU 7081  C   VAL B 420     2342   2440   2966    231    849    522       C  
ATOM   7082  O   VAL B 420     -61.603  -4.053 143.939  1.00 19.40           O  
ANISOU 7082  O   VAL B 420     2261   2307   2803    243    833    487       O  
ATOM   7083  CB  VAL B 420     -61.888  -6.328 141.673  1.00 18.95           C  
ANISOU 7083  CB  VAL B 420     2087   2253   2860    175    744    528       C  
ATOM   7084  CG1 VAL B 420     -63.311  -5.967 141.233  1.00 19.05           C  
ANISOU 7084  CG1 VAL B 420     2039   2265   2935    190    774    548       C  
ATOM   7085  CG2 VAL B 420     -60.865  -5.362 141.063  1.00 18.13           C  
ANISOU 7085  CG2 VAL B 420     2017   2143   2730    176    700    488       C  
ATOM   7086  N   ASP B 421     -63.554  -5.102 144.451  1.00 19.32           N  
ANISOU 7086  N   ASP B 421     2176   2310   2856    251    912    551       N  
ATOM   7087  CA  ASP B 421     -64.144  -3.935 145.125  1.00 20.33           C  
ANISOU 7087  CA  ASP B 421     2323   2437   2966    292    968    541       C  
ATOM   7088  C   ASP B 421     -63.395  -3.593 146.419  1.00 24.79           C  
ANISOU 7088  C   ASP B 421     2969   3003   3447    309    991    521       C  
ATOM   7089  O   ASP B 421     -63.016  -2.440 146.622  1.00 25.32           O  
ANISOU 7089  O   ASP B 421     3079   3062   3480    332    991    486       O  
ATOM   7090  CB  ASP B 421     -65.645  -4.160 145.408  1.00 23.39           C  
ANISOU 7090  CB  ASP B 421     2655   2832   3403    309   1032    580       C  
ATOM   7091  CG  ASP B 421     -66.533  -4.055 144.175  1.00 33.77           C  
ANISOU 7091  CG  ASP B 421     3892   4140   4799    303   1013    593       C  
ATOM   7092  OD1 ASP B 421     -66.018  -3.655 143.102  1.00 33.43           O  
ANISOU 7092  OD1 ASP B 421     3844   4088   4768    292    954    569       O  
ATOM   7093  OD2 ASP B 421     -67.748  -4.321 144.295  1.00 38.90           O  
ANISOU 7093  OD2 ASP B 421     4486   4795   5498    313   1059    627       O  
ATOM   7094  N   ASP B 422     -63.161  -4.602 147.282  1.00 21.41           N  
ANISOU 7094  N   ASP B 422     2563   2585   2988    298   1008    542       N  
ATOM   7095  CA  ASP B 422     -62.430  -4.407 148.542  1.00 21.49           C  
ANISOU 7095  CA  ASP B 422     2652   2597   2915    313   1026    525       C  
ATOM   7096  C   ASP B 422     -60.951  -4.112 148.279  1.00 23.55           C  
ANISOU 7096  C   ASP B 422     2964   2850   3136    297    958    485       C  
ATOM   7097  O   ASP B 422     -60.331  -3.354 149.029  1.00 23.70           O  
ANISOU 7097  O   ASP B 422     3048   2864   3094    316    961    455       O  
ATOM   7098  CB  ASP B 422     -62.577  -5.642 149.452  1.00 24.02           C  
ANISOU 7098  CB  ASP B 422     2980   2931   3217    303   1058    563       C  
ATOM   7099  CG  ASP B 422     -64.006  -5.891 149.930  1.00 36.66           C  
ANISOU 7099  CG  ASP B 422     4537   4541   4849    322   1135    604       C  
ATOM   7100  OD1 ASP B 422     -64.753  -4.898 150.118  1.00 36.91           O  
ANISOU 7100  OD1 ASP B 422     4566   4573   4886    357   1182    596       O  
ATOM   7101  OD2 ASP B 422     -64.344  -7.065 150.207  1.00 44.00           O  
ANISOU 7101  OD2 ASP B 422     5442   5479   5798    303   1152    645       O  
ATOM   7102  N   TYR B 423     -60.387  -4.703 147.197  1.00 17.28           N  
ANISOU 7102  N   TYR B 423     2137   2052   2376    262    895    485       N  
ATOM   7103  CA  TYR B 423     -58.993  -4.485 146.807  1.00 15.52           C  
ANISOU 7103  CA  TYR B 423     1951   1821   2124    244    830    451       C  
ATOM   7104  C   TYR B 423     -58.747  -3.001 146.468  1.00 17.89           C  
ANISOU 7104  C   TYR B 423     2272   2108   2416    263    817    413       C  
ATOM   7105  O   TYR B 423     -57.849  -2.380 147.035  1.00 17.16           O  
ANISOU 7105  O   TYR B 423     2241   2009   2271    270    802    382       O  
ATOM   7106  CB  TYR B 423     -58.632  -5.382 145.598  1.00 15.75           C  
ANISOU 7106  CB  TYR B 423     1934   1851   2201    207    773    460       C  
ATOM   7107  CG  TYR B 423     -57.174  -5.311 145.181  1.00 16.26           C  
ANISOU 7107  CG  TYR B 423     2031   1910   2239    187    708    430       C  
ATOM   7108  CD1 TYR B 423     -56.239  -6.207 145.692  1.00 17.73           C  
ANISOU 7108  CD1 TYR B 423     2247   2099   2390    169    683    432       C  
ATOM   7109  CD2 TYR B 423     -56.760  -4.446 144.169  1.00 16.56           C  
ANISOU 7109  CD2 TYR B 423     2060   1938   2294    184    670    403       C  
ATOM   7110  CE1 TYR B 423     -54.906  -6.181 145.274  1.00 17.31           C  
ANISOU 7110  CE1 TYR B 423     2217   2041   2319    151    624    406       C  
ATOM   7111  CE2 TYR B 423     -55.436  -4.424 143.731  1.00 16.93           C  
ANISOU 7111  CE2 TYR B 423     2129   1980   2322    165    613    379       C  
ATOM   7112  CZ  TYR B 423     -54.507  -5.284 144.296  1.00 22.11           C  
ANISOU 7112  CZ  TYR B 423     2815   2641   2944    148    591    380       C  
ATOM   7113  OH  TYR B 423     -53.195  -5.257 143.873  1.00 15.82           O  
ANISOU 7113  OH  TYR B 423     2038   1840   2133    130    536    357       O  
ATOM   7114  N   LEU B 424     -59.594  -2.424 145.592  1.00 14.33           N  
ANISOU 7114  N   LEU B 424     1773   1654   2020    272    825    416       N  
ATOM   7115  CA  LEU B 424     -59.422  -1.044 145.114  1.00 13.99           C  
ANISOU 7115  CA  LEU B 424     1743   1595   1978    288    811    385       C  
ATOM   7116  C   LEU B 424     -59.695   0.026 146.193  1.00 18.65           C  
ANISOU 7116  C   LEU B 424     2383   2178   2525    327    859    365       C  
ATOM   7117  O   LEU B 424     -59.242   1.156 146.050  1.00 18.81           O  
ANISOU 7117  O   LEU B 424     2433   2182   2531    339    841    333       O  
ATOM   7118  CB  LEU B 424     -60.289  -0.790 143.864  1.00 13.91           C  
ANISOU 7118  CB  LEU B 424     1665   1582   2038    287    804    397       C  
ATOM   7119  CG  LEU B 424     -59.800  -1.466 142.567  1.00 17.92           C  
ANISOU 7119  CG  LEU B 424     2135   2092   2583    251    743    402       C  
ATOM   7120  CD1 LEU B 424     -60.848  -1.365 141.468  1.00 18.33           C  
ANISOU 7120  CD1 LEU B 424     2120   2143   2703    253    741    420       C  
ATOM   7121  CD2 LEU B 424     -58.480  -0.867 142.100  1.00 18.83           C  
ANISOU 7121  CD2 LEU B 424     2288   2197   2671    238    688    368       C  
ATOM   7122  N   THR B 425     -60.428  -0.332 147.267  1.00 15.43           N  
ANISOU 7122  N   THR B 425     1985   1782   2098    348    920    385       N  
ATOM   7123  CA  THR B 425     -60.745   0.628 148.342  1.00 15.65           C  
ANISOU 7123  CA  THR B 425     2062   1803   2080    389    971    367       C  
ATOM   7124  C   THR B 425     -59.769   0.501 149.534  1.00 19.21           C  
ANISOU 7124  C   THR B 425     2593   2255   2451    391    966    348       C  
ATOM   7125  O   THR B 425     -59.890   1.245 150.515  1.00 19.38           O  
ANISOU 7125  O   THR B 425     2667   2271   2424    425   1003    329       O  
ATOM   7126  CB  THR B 425     -62.218   0.473 148.790  1.00 23.38           C  
ANISOU 7126  CB  THR B 425     3004   2794   3087    417   1048    400       C  
ATOM   7127  OG1 THR B 425     -62.431  -0.864 149.241  1.00 21.69           O  
ANISOU 7127  OG1 THR B 425     2773   2597   2871    400   1068    437       O  
ATOM   7128  CG2 THR B 425     -63.206   0.815 147.676  1.00 23.17           C  
ANISOU 7128  CG2 THR B 425     2902   2763   3139    421   1051    414       C  
ATOM   7129  N   SER B 426     -58.798  -0.428 149.441  1.00 14.66           N  
ANISOU 7129  N   SER B 426     2027   1685   1859    357    918    352       N  
ATOM   7130  CA  SER B 426     -57.863  -0.694 150.541  1.00 14.21           C  
ANISOU 7130  CA  SER B 426     2041   1630   1729    356    908    339       C  
ATOM   7131  C   SER B 426     -56.636   0.238 150.513  1.00 17.72           C  
ANISOU 7131  C   SER B 426     2539   2056   2138    353    854    292       C  
ATOM   7132  O   SER B 426     -56.044   0.453 149.454  1.00 16.64           O  
ANISOU 7132  O   SER B 426     2378   1910   2036    329    800    280       O  
ATOM   7133  CB  SER B 426     -57.417  -2.147 150.519  1.00 16.93           C  
ANISOU 7133  CB  SER B 426     2370   1987   2075    323    884    367       C  
ATOM   7134  OG  SER B 426     -56.457  -2.409 151.528  1.00 25.83           O  
ANISOU 7134  OG  SER B 426     3566   3116   3133    321    867    355       O  
ATOM   7135  N   THR B 427     -56.202   0.704 151.703  1.00 14.94           N  
ANISOU 7135  N   THR B 427     2263   1699   1716    374    865    268       N  
ATOM   7136  CA  THR B 427     -55.016   1.565 151.837  1.00 14.90           C  
ANISOU 7136  CA  THR B 427     2313   1674   1674    371    812    224       C  
ATOM   7137  C   THR B 427     -53.779   0.742 152.279  1.00 18.53           C  
ANISOU 7137  C   THR B 427     2809   2138   2093    344    762    221       C  
ATOM   7138  O   THR B 427     -52.713   1.317 152.546  1.00 17.22           O  
ANISOU 7138  O   THR B 427     2693   1958   1892    340    716    187       O  
ATOM   7139  CB  THR B 427     -55.303   2.720 152.809  1.00 24.47           C  
ANISOU 7139  CB  THR B 427     3587   2873   2838    413    848    193       C  
ATOM   7140  OG1 THR B 427     -55.645   2.177 154.087  1.00 27.62           O  
ANISOU 7140  OG1 THR B 427     4028   3287   3180    435    896    207       O  
ATOM   7141  CG2 THR B 427     -56.418   3.634 152.315  1.00 23.13           C  
ANISOU 7141  CG2 THR B 427     3382   2695   2713    441    890    192       C  
ATOM   7142  N   GLU B 428     -53.926  -0.605 152.357  1.00 15.11           N  
ANISOU 7142  N   GLU B 428     2349   1725   1666    327    770    259       N  
ATOM   7143  CA  GLU B 428     -52.819  -1.492 152.730  1.00 14.46           C  
ANISOU 7143  CA  GLU B 428     2295   1647   1551    302    724    261       C  
ATOM   7144  C   GLU B 428     -51.709  -1.407 151.698  1.00 17.36           C  
ANISOU 7144  C   GLU B 428     2642   2005   1950    269    651    242       C  
ATOM   7145  O   GLU B 428     -51.970  -1.526 150.496  1.00 16.54           O  
ANISOU 7145  O   GLU B 428     2476   1901   1907    252    639    253       O  
ATOM   7146  CB  GLU B 428     -53.308  -2.951 152.877  1.00 15.68           C  
ANISOU 7146  CB  GLU B 428     2418   1822   1719    289    749    308       C  
ATOM   7147  CG  GLU B 428     -54.306  -3.158 154.014  1.00 24.56           C  
ANISOU 7147  CG  GLU B 428     3566   2958   2807    320    824    331       C  
ATOM   7148  CD  GLU B 428     -53.738  -2.988 155.414  1.00 50.20           C  
ANISOU 7148  CD  GLU B 428     6900   6206   5967    339    828    314       C  
ATOM   7149  OE1 GLU B 428     -52.526  -3.246 155.603  1.00 40.79           O  
ANISOU 7149  OE1 GLU B 428     5744   5009   4745    321    768    298       O  
ATOM   7150  OE2 GLU B 428     -54.527  -2.688 156.339  1.00 53.53           O  
ANISOU 7150  OE2 GLU B 428     7353   6633   6351    374    891    320       O  
ATOM   7151  N   LYS B 429     -50.490  -1.106 152.146  1.00 13.03           N  
ANISOU 7151  N   LYS B 429     2146   1446   1360    262    602    213       N  
ATOM   7152  CA  LYS B 429     -49.353  -0.926 151.246  1.00 11.97           C  
ANISOU 7152  CA  LYS B 429     1995   1301   1252    232    534    194       C  
ATOM   7153  C   LYS B 429     -48.591  -2.215 151.077  1.00 16.64           C  
ANISOU 7153  C   LYS B 429     2570   1904   1848    203    496    213       C  
ATOM   7154  O   LYS B 429     -48.388  -2.940 152.052  1.00 16.39           O  
ANISOU 7154  O   LYS B 429     2574   1880   1773    206    500    224       O  
ATOM   7155  CB  LYS B 429     -48.412   0.175 151.781  1.00 13.72           C  
ANISOU 7155  CB  LYS B 429     2279   1502   1433    238    497    150       C  
ATOM   7156  CG  LYS B 429     -49.070   1.547 151.890  1.00 17.74           C  
ANISOU 7156  CG  LYS B 429     2806   1994   1939    268    528    126       C  
ATOM   7157  CD  LYS B 429     -48.131   2.569 152.509  1.00 24.45           C  
ANISOU 7157  CD  LYS B 429     3722   2821   2748    273    489     83       C  
ATOM   7158  N   ASN B 430     -48.096  -2.487 149.854  1.00 13.90           N  
ANISOU 7158  N   ASN B 430     2172   1556   1552    175    456    215       N  
ATOM   7159  CA  ASN B 430     -47.201  -3.619 149.644  1.00 13.68           C  
ANISOU 7159  CA  ASN B 430     2131   1536   1529    148    412    227       C  
ATOM   7160  C   ASN B 430     -45.806  -3.292 150.222  1.00 17.77           C  
ANISOU 7160  C   ASN B 430     2700   2043   2007    140    359    198       C  
ATOM   7161  O   ASN B 430     -45.634  -2.237 150.842  1.00 17.89           O  
ANISOU 7161  O   ASN B 430     2762   2045   1989    156    358    170       O  
ATOM   7162  CB  ASN B 430     -47.120  -4.007 148.137  1.00 11.14           C  
ANISOU 7162  CB  ASN B 430     1741   1218   1273    124    389    237       C  
ATOM   7163  CG  ASN B 430     -46.576  -2.919 147.227  1.00 19.69           C  
ANISOU 7163  CG  ASN B 430     2813   2288   2381    116    358    211       C  
ATOM   7164  OD1 ASN B 430     -46.020  -1.912 147.673  1.00 13.77           O  
ANISOU 7164  OD1 ASN B 430     2104   1524   1605    123    342    182       O  
ATOM   7165  ND2 ASN B 430     -46.678  -3.138 145.924  1.00  5.59           N  
ANISOU 7165  ND2 ASN B 430      941    517    665    120    324    168       N  
ATOM   7166  N   GLU B 431     -44.833  -4.191 150.054  1.00 14.07           N  
ANISOU 7166  N   GLU B 431     2223   1580   1544    117    313    205       N  
ATOM   7167  CA  GLU B 431     -43.504  -3.974 150.632  1.00 13.83           C  
ANISOU 7167  CA  GLU B 431     2236   1539   1479    109    260    180       C  
ATOM   7168  C   GLU B 431     -42.674  -2.945 149.847  1.00 17.32           C  
ANISOU 7168  C   GLU B 431     2667   1967   1948     96    218    150       C  
ATOM   7169  O   GLU B 431     -41.589  -2.564 150.288  1.00 17.20           O  
ANISOU 7169  O   GLU B 431     2686   1940   1910     89    173    127       O  
ATOM   7170  CB  GLU B 431     -42.758  -5.301 150.819  1.00 14.99           C  
ANISOU 7170  CB  GLU B 431     2378   1695   1621     92    227    199       C  
ATOM   7171  CG  GLU B 431     -43.405  -6.187 151.878  1.00 25.81           C  
ANISOU 7171  CG  GLU B 431     3777   3076   2952    106    263    226       C  
ATOM   7172  CD  GLU B 431     -42.636  -7.441 152.246  1.00 47.58           C  
ANISOU 7172  CD  GLU B 431     6540   5839   5698     92    228    243       C  
ATOM   7173  OE1 GLU B 431     -41.825  -7.909 151.416  1.00 44.27           O  
ANISOU 7173  OE1 GLU B 431     6084   5420   5317     70    185    242       O  
ATOM   7174  OE2 GLU B 431     -42.909  -8.001 153.331  1.00 44.15           O  
ANISOU 7174  OE2 GLU B 431     6146   5411   5218    105    248    261       O  
ATOM   7175  N   ALA B 432     -43.252  -2.395 148.762  1.00 14.32           N  
ANISOU 7175  N   ALA B 432     2243   1585   1614     94    236    151       N  
ATOM   7176  CA  ALA B 432     -42.651  -1.280 148.028  1.00 13.83           C  
ANISOU 7176  CA  ALA B 432     2171   1506   1576     84    207    126       C  
ATOM   7177  C   ALA B 432     -43.246   0.057 148.522  1.00 18.10           C  
ANISOU 7177  C   ALA B 432     2750   2031   2097    108    234    104       C  
ATOM   7178  O   ALA B 432     -42.740   1.130 148.178  1.00 17.87           O  
ANISOU 7178  O   ALA B 432     2727   1982   2080    103    209     80       O  
ATOM   7179  CB  ALA B 432     -42.898  -1.443 146.534  1.00 14.13           C  
ANISOU 7179  CB  ALA B 432     2144   1552   1675     70    208    140       C  
ATOM   7180  N   GLY B 433     -44.299  -0.034 149.351  1.00 14.20           N  
ANISOU 7180  N   GLY B 433     2281   1543   1573    135    285    113       N  
ATOM   7181  CA  GLY B 433     -44.980   1.133 149.903  1.00 14.29           C  
ANISOU 7181  CA  GLY B 433     2330   1539   1562    163    318     93       C  
ATOM   7182  C   GLY B 433     -46.186   1.562 149.092  1.00 18.59           C  
ANISOU 7182  C   GLY B 433     2830   2084   2148    176    363    106       C  
ATOM   7183  O   GLY B 433     -46.805   2.589 149.388  1.00 18.93           O  
ANISOU 7183  O   GLY B 433     2897   2114   2183    201    391     90       O  
ATOM   7184  N   THR B 434     -46.547   0.765 148.069  1.00 14.76           N  
ANISOU 7184  N   THR B 434     2283   1615   1711    160    368    134       N  
ATOM   7185  CA  THR B 434     -47.652   1.101 147.170  1.00 14.44           C  
ANISOU 7185  CA  THR B 434     2194   1576   1716    169    403    148       C  
ATOM   7186  C   THR B 434     -48.960   0.478 147.637  1.00 19.30           C  
ANISOU 7186  C   THR B 434     2798   2207   2328    190    463    175       C  
ATOM   7187  O   THR B 434     -49.020  -0.733 147.872  1.00 19.77           O  
ANISOU 7187  O   THR B 434     2845   2283   2383    181    468    199       O  
ATOM   7188  CB  THR B 434     -47.318   0.665 145.735  1.00 17.87           C  
ANISOU 7188  CB  THR B 434     2569   2018   2204    142    373    161       C  
ATOM   7189  OG1 THR B 434     -45.959   0.979 145.453  1.00 16.00           O  
ANISOU 7189  OG1 THR B 434     2344   1771   1965    120    318    140       O  
ATOM   7190  CG2 THR B 434     -48.235   1.306 144.700  1.00 16.43           C  
ANISOU 7190  CG2 THR B 434     2344   1832   2068    150    395    168       C  
ATOM   7191  N   SER B 435     -50.037   1.287 147.690  1.00 16.04           N  
ANISOU 7191  N   SER B 435     2382   1788   1925    217    508    173       N  
ATOM   7192  CA  SER B 435     -51.379   0.787 147.998  1.00 16.04           C  
ANISOU 7192  CA  SER B 435     2360   1803   1933    237    569    202       C  
ATOM   7193  C   SER B 435     -52.225   0.716 146.715  1.00 20.13           C  
ANISOU 7193  C   SER B 435     2806   2324   2516    231    580    222       C  
ATOM   7194  O   SER B 435     -51.891   1.363 145.723  1.00 19.85           O  
ANISOU 7194  O   SER B 435     2751   2279   2513    221    549    210       O  
ATOM   7195  CB  SER B 435     -52.061   1.678 149.035  1.00 18.95           C  
ANISOU 7195  CB  SER B 435     2775   2163   2265    275    618    187       C  
ATOM   7196  OG  SER B 435     -52.198   3.008 148.562  1.00 23.72           O  
ANISOU 7196  OG  SER B 435     3379   2745   2887    289    615    162       O  
ATOM   7197  N   ALA B 436     -53.300  -0.089 146.728  1.00 17.42           N  
ANISOU 7197  N   ALA B 436     2425   1997   2196    237    621    255       N  
ATOM   7198  CA  ALA B 436     -54.161  -0.251 145.550  1.00 17.20           C  
ANISOU 7198  CA  ALA B 436     2329   1974   2232    231    629    277       C  
ATOM   7199  C   ALA B 436     -55.099   0.954 145.352  1.00 19.93           C  
ANISOU 7199  C   ALA B 436     2665   2308   2599    260    663    269       C  
ATOM   7200  O   ALA B 436     -55.428   1.290 144.215  1.00 19.53           O  
ANISOU 7200  O   ALA B 436     2570   2253   2597    255    648    273       O  
ATOM   7201  CB  ALA B 436     -54.969  -1.527 145.664  1.00 18.06           C  
ANISOU 7201  CB  ALA B 436     2400   2100   2361    226    658    315       C  
ATOM   7202  N   ARG B 437     -55.540   1.596 146.467  1.00 16.29           N  
ANISOU 7202  N   ARG B 437     2247   1841   2101    293    707    258       N  
ATOM   7203  CA  ARG B 437     -56.446   2.760 146.406  1.00 15.67           C  
ANISOU 7203  CA  ARG B 437     2163   1750   2040    326    744    249       C  
ATOM   7204  C   ARG B 437     -55.778   3.926 145.661  1.00 18.37           C  
ANISOU 7204  C   ARG B 437     2516   2070   2393    321    700    219       C  
ATOM   7205  O   ARG B 437     -54.761   4.449 146.120  1.00 18.08           O  
ANISOU 7205  O   ARG B 437     2534   2020   2317    318    671    189       O  
ATOM   7206  CB  ARG B 437     -56.869   3.191 147.822  1.00 16.28           C  
ANISOU 7206  CB  ARG B 437     2294   1826   2067    363    797    238       C  
ATOM   7207  CG  ARG B 437     -58.016   4.191 147.838  1.00 27.02           C  
ANISOU 7207  CG  ARG B 437     3641   3176   3449    401    847    235       C  
ATOM   7208  CD  ARG B 437     -58.329   4.656 149.243  1.00 34.90           C  
ANISOU 7208  CD  ARG B 437     4699   4171   4390    440    899    220       C  
ATOM   7209  NE  ARG B 437     -59.461   5.582 149.267  1.00 41.94           N  
ANISOU 7209  NE  ARG B 437     5576   5054   5306    479    950    218       N  
ATOM   7210  CZ  ARG B 437     -60.717   5.207 149.496  1.00 58.73           C  
ANISOU 7210  CZ  ARG B 437     7662   7195   7456    501   1013    249       C  
ATOM   7211  NH1 ARG B 437     -61.002   3.936 149.754  1.00 44.51           N  
ANISOU 7211  NH1 ARG B 437     5836   5419   5658    485   1033    285       N  
ATOM   7212  NH2 ARG B 437     -61.694   6.105 149.490  1.00 47.25           N  
ANISOU 7212  NH2 ARG B 437     6194   5731   6027    539   1057    245       N  
ATOM   7213  N   TYR B 438     -56.340   4.313 144.487  1.00 14.19           N  
ANISOU 7213  N   TYR B 438     1936   1536   1921    320    694    228       N  
ATOM   7214  CA  TYR B 438     -55.725   5.319 143.611  1.00 13.40           C  
ANISOU 7214  CA  TYR B 438     1838   1416   1838    312    651    207       C  
ATOM   7215  C   TYR B 438     -55.583   6.694 144.274  1.00 17.88           C  
ANISOU 7215  C   TYR B 438     2460   1957   2378    339    661    173       C  
ATOM   7216  O   TYR B 438     -54.597   7.384 144.031  1.00 16.75           O  
ANISOU 7216  O   TYR B 438     2345   1795   2225    326    619    149       O  
ATOM   7217  CB  TYR B 438     -56.489   5.436 142.284  1.00 14.10           C  
ANISOU 7217  CB  TYR B 438     1862   1505   1990    309    646    227       C  
ATOM   7218  CG  TYR B 438     -55.729   6.215 141.228  1.00 15.00           C  
ANISOU 7218  CG  TYR B 438     1975   1603   2123    293    597    212       C  
ATOM   7219  CD1 TYR B 438     -54.696   5.623 140.504  1.00 16.64           C  
ANISOU 7219  CD1 TYR B 438     2173   1818   2331    257    547    214       C  
ATOM   7220  CD2 TYR B 438     -56.017   7.552 140.978  1.00 15.20           C  
ANISOU 7220  CD2 TYR B 438     2009   1603   2162    314    601    198       C  
ATOM   7221  CE1 TYR B 438     -53.979   6.340 139.548  1.00 16.91           C  
ANISOU 7221  CE1 TYR B 438     2205   1838   2381    242    505    204       C  
ATOM   7222  CE2 TYR B 438     -55.308   8.278 140.021  1.00 15.62           C  
ANISOU 7222  CE2 TYR B 438     2062   1641   2232    298    557    188       C  
ATOM   7223  CZ  TYR B 438     -54.287   7.667 139.309  1.00 22.14           C  
ANISOU 7223  CZ  TYR B 438     2878   2477   3059    262    510    192       C  
ATOM   7224  OH  TYR B 438     -53.582   8.374 138.368  1.00 22.12           O  
ANISOU 7224  OH  TYR B 438     2874   2459   3072    246    471    185       O  
ATOM   7225  N   ASP B 439     -56.588   7.109 145.079  1.00 16.31           N  
ANISOU 7225  N   ASP B 439     2274   1755   2169    378    718    172       N  
ATOM   7226  CA  ASP B 439     -56.574   8.432 145.732  1.00 16.86           C  
ANISOU 7226  CA  ASP B 439     2396   1797   2212    409    732    139       C  
ATOM   7227  C   ASP B 439     -55.565   8.507 146.889  1.00 19.96           C  
ANISOU 7227  C   ASP B 439     2863   2182   2537    408    717    109       C  
ATOM   7228  O   ASP B 439     -55.133   9.601 147.254  1.00 19.48           O  
ANISOU 7228  O   ASP B 439     2853   2096   2455    422    704     75       O  
ATOM   7229  CB  ASP B 439     -57.981   8.821 146.208  1.00 19.50           C  
ANISOU 7229  CB  ASP B 439     2719   2132   2558    453    800    147       C  
ATOM   7230  CG  ASP B 439     -58.951   9.104 145.072  1.00 32.06           C  
ANISOU 7230  CG  ASP B 439     4243   3721   4218    460    808    169       C  
ATOM   7231  OD1 ASP B 439     -58.481   9.456 143.960  1.00 32.31           O  
ANISOU 7231  OD1 ASP B 439     4253   3741   4281    438    760    167       O  
ATOM   7232  OD2 ASP B 439     -60.181   9.052 145.314  1.00 39.61           O  
ANISOU 7232  OD2 ASP B 439     5169   4685   5195    489    864    187       O  
ATOM   7233  N   ASP B 440     -55.178   7.348 147.451  1.00 16.73           N  
ANISOU 7233  N   ASP B 440     2464   1797   2097    391    715    122       N  
ATOM   7234  CA  ASP B 440     -54.177   7.297 148.521  1.00 16.80           C  
ANISOU 7234  CA  ASP B 440     2542   1801   2040    388    695     97       C  
ATOM   7235  C   ASP B 440     -52.754   7.373 147.927  1.00 19.87           C  
ANISOU 7235  C   ASP B 440     2938   2178   2432    349    621     81       C  
ATOM   7236  O   ASP B 440     -52.106   6.347 147.740  1.00 18.26           O  
ANISOU 7236  O   ASP B 440     2720   1992   2227    319    592     96       O  
ATOM   7237  CB  ASP B 440     -54.352   6.014 149.370  1.00 18.68           C  
ANISOU 7237  CB  ASP B 440     2786   2066   2243    386    722    121       C  
ATOM   7238  CG  ASP B 440     -53.291   5.836 150.448  1.00 30.22           C  
ANISOU 7238  CG  ASP B 440     4319   3526   3638    381    696     98       C  
ATOM   7239  OD1 ASP B 440     -52.892   6.853 151.064  1.00 31.23           O  
ANISOU 7239  OD1 ASP B 440     4505   3630   3729    399    687     62       O  
ATOM   7240  OD2 ASP B 440     -52.858   4.684 150.670  1.00 36.80           O  
ANISOU 7240  OD2 ASP B 440     5149   4379   4456    360    683    118       O  
ATOM   7241  N   GLN B 441     -52.289   8.590 147.615  1.00 17.89           N  
ANISOU 7241  N   GLN B 441     2710   1899   2191    351    592     53       N  
ATOM   7242  CA  GLN B 441     -50.975   8.785 146.984  1.00 17.66           C  
ANISOU 7242  CA  GLN B 441     2682   1857   2171    315    525     40       C  
ATOM   7243  C   GLN B 441     -49.926   9.333 147.979  1.00 23.36           C  
ANISOU 7243  C   GLN B 441     3477   2557   2841    315    492      2       C  
ATOM   7244  O   GLN B 441     -48.944   9.961 147.562  1.00 23.02           O  
ANISOU 7244  O   GLN B 441     3444   2493   2810    293    442    -16       O  
ATOM   7245  CB  GLN B 441     -51.098   9.703 145.754  1.00 18.31           C  
ANISOU 7245  CB  GLN B 441     2729   1920   2308    310    509     40       C  
ATOM   7246  CG  GLN B 441     -51.895   9.076 144.615  1.00 19.48           C  
ANISOU 7246  CG  GLN B 441     2804   2089   2508    302    524     76       C  
ATOM   7247  CD  GLN B 441     -52.259  10.079 143.546  1.00 32.22           C  
ANISOU 7247  CD  GLN B 441     4389   3683   4170    307    518     77       C  
ATOM   7248  OE1 GLN B 441     -51.661  11.155 143.433  1.00 24.18           O  
ANISOU 7248  OE1 GLN B 441     3399   2635   3152    305    490     54       O  
ATOM   7249  NE2 GLN B 441     -53.238   9.731 142.716  1.00 25.09           N  
ANISOU 7249  NE2 GLN B 441     3429   2795   3310    311    540    106       N  
ATOM   7250  N   GLN B 442     -50.098   9.033 149.279  1.00 20.76           N  
ANISOU 7250  N   GLN B 442     3198   2236   2456    337    519     -7       N  
ATOM   7251  CA  GLN B 442     -49.168   9.495 150.311  1.00 21.15           C  
ANISOU 7251  CA  GLN B 442     3320   2265   2450    339    487    -44       C  
ATOM   7252  C   GLN B 442     -48.202   8.387 150.727  1.00 25.50           C  
ANISOU 7252  C   GLN B 442     3883   2835   2971    311    451    -36       C  
ATOM   7253  O   GLN B 442     -48.608   7.227 150.869  1.00 25.25           O  
ANISOU 7253  O   GLN B 442     3828   2833   2932    309    477     -6       O  
ATOM   7254  CB  GLN B 442     -49.935  10.026 151.531  1.00 23.25           C  
ANISOU 7254  CB  GLN B 442     3644   2522   2666    385    536    -64       C  
ATOM   7255  N   GLY B 443     -46.931   8.752 150.919  1.00 21.86           N  
ANISOU 7255  N   GLY B 443     3456   2354   2493    290    390    -62       N  
ATOM   7256  CA  GLY B 443     -45.900   7.815 151.350  1.00 21.47           C  
ANISOU 7256  CA  GLY B 443     3421   2319   2416    265    349    -59       C  
ATOM   7257  C   GLY B 443     -44.906   7.465 150.261  1.00 24.67           C  
ANISOU 7257  C   GLY B 443     3779   2728   2869    223    296    -48       C  
ATOM   7258  O   GLY B 443     -45.198   7.624 149.071  1.00 23.99           O  
ANISOU 7258  O   GLY B 443     3636   2642   2836    211    301    -32       O  
ATOM   7259  N   ALA B 444     -43.718   6.957 150.663  1.00 20.89           N  
ANISOU 7259  N   ALA B 444     3320   2251   2367    199    245    -55       N  
ATOM   7260  CA  ALA B 444     -42.662   6.569 149.722  1.00 20.08           C  
ANISOU 7260  CA  ALA B 444     3173   2152   2305    160    194    -45       C  
ATOM   7261  C   ALA B 444     -43.079   5.349 148.887  1.00 22.70           C  
ANISOU 7261  C   ALA B 444     3441   2516   2669    148    215     -6       C  
ATOM   7262  O   ALA B 444     -43.485   4.318 149.443  1.00 22.92           O  
ANISOU 7262  O   ALA B 444     3472   2565   2670    156    240     13       O  
ATOM   7263  CB  ALA B 444     -41.372   6.272 150.477  1.00 20.94           C  
ANISOU 7263  CB  ALA B 444     3320   2256   2381    143    138    -62       C  
ATOM   7264  N   GLY B 445     -43.000   5.488 147.568  1.00 16.41           N  
ANISOU 7264  N   GLY B 445     2588   1719   1927    129    206      7       N  
ATOM   7265  CA  GLY B 445     -43.364   4.423 146.640  1.00 14.91           C  
ANISOU 7265  CA  GLY B 445     2337   1557   1772    116    220     41       C  
ATOM   7266  C   GLY B 445     -44.849   4.374 146.324  1.00 15.72           C  
ANISOU 7266  C   GLY B 445     2413   1669   1891    139    278     60       C  
ATOM   7267  O   GLY B 445     -45.312   3.444 145.665  1.00 13.72           O  
ANISOU 7267  O   GLY B 445     2112   1438   1664    132    293     88       O  
ATOM   7268  N   ASN B 446     -45.602   5.420 146.737  1.00 11.90           N  
ANISOU 7268  N   ASN B 446     1957   1168   1397    167    309     45       N  
ATOM   7269  CA  ASN B 446     -47.060   5.423 146.612  1.00 11.38           C  
ANISOU 7269  CA  ASN B 446     1868   1111   1346    193    368     63       C  
ATOM   7270  C   ASN B 446     -47.589   6.511 145.621  1.00 14.75           C  
ANISOU 7270  C   ASN B 446     2266   1520   1817    200    376     60       C  
ATOM   7271  O   ASN B 446     -48.747   6.902 145.715  1.00 15.19           O  
ANISOU 7271  O   ASN B 446     2317   1575   1881    228    422     65       O  
ATOM   7272  CB  ASN B 446     -47.716   5.588 148.011  1.00 10.15           C  
ANISOU 7272  CB  ASN B 446     1765    952   1137    228    410     52       C  
ATOM   7273  CG  ASN B 446     -49.099   4.982 148.123  1.00 18.89           C  
ANISOU 7273  CG  ASN B 446     2845   2081   2252    249    472     81       C  
ATOM   7274  OD1 ASN B 446     -49.523   4.176 147.289  1.00 12.77           O  
ANISOU 7274  OD1 ASN B 446     2013   1324   1517    236    480    110       O  
ATOM   7275  ND2 ASN B 446     -49.797   5.295 149.206  1.00  9.35           N  
ANISOU 7275  ND2 ASN B 446     1678    869   1004    283    517     72       N  
ATOM   7276  N   THR B 447     -46.763   6.917 144.619  1.00 10.82           N  
ANISOU 7276  N   THR B 447     1746   1012   1352    174    333     56       N  
ATOM   7277  CA  THR B 447     -47.212   7.908 143.608  1.00 10.30           C  
ANISOU 7277  CA  THR B 447     1654    931   1330    179    338     57       C  
ATOM   7278  C   THR B 447     -48.242   7.292 142.662  1.00 13.94           C  
ANISOU 7278  C   THR B 447     2055   1413   1829    182    366     90       C  
ATOM   7279  O   THR B 447     -48.307   6.066 142.537  1.00 14.53           O  
ANISOU 7279  O   THR B 447     2103   1514   1905    170    369    110       O  
ATOM   7280  CB  THR B 447     -46.012   8.484 142.816  1.00 14.62           C  
ANISOU 7280  CB  THR B 447     2195   1462   1900    149    285     48       C  
ATOM   7281  OG1 THR B 447     -45.418   7.442 142.048  1.00 13.50           O  
ANISOU 7281  OG1 THR B 447     2011   1343   1774    121    262     68       O  
ATOM   7282  CG2 THR B 447     -44.972   9.143 143.717  1.00 13.71           C  
ANISOU 7282  CG2 THR B 447     2136   1321   1752    144    251     16       C  
ATOM   7283  N   ALA B 448     -49.006   8.143 141.945  1.00  9.50           N  
ANISOU 7283  N   ALA B 448     1470    838   1301    196    383     94       N  
ATOM   7284  CA  ALA B 448     -50.016   7.679 140.987  1.00  8.61           C  
ANISOU 7284  CA  ALA B 448     1300    742   1228    200    405    123       C  
ATOM   7285  C   ALA B 448     -49.397   6.810 139.880  1.00 12.02           C  
ANISOU 7285  C   ALA B 448     1690   1194   1684    167    371    142       C  
ATOM   7286  O   ALA B 448     -49.972   5.781 139.513  1.00 11.23           O  
ANISOU 7286  O   ALA B 448     1551   1116   1598    164    383    165       O  
ATOM   7287  CB  ALA B 448     -50.741   8.863 140.377  1.00  9.46           C  
ANISOU 7287  CB  ALA B 448     1397    829   1368    219    418    122       C  
ATOM   7288  N   LEU B 449     -48.216   7.219 139.352  1.00  8.78           N  
ANISOU 7288  N   LEU B 449     1287    773   1278    143    328    131       N  
ATOM   7289  CA  LEU B 449     -47.527   6.462 138.293  1.00  8.12           C  
ANISOU 7289  CA  LEU B 449     1165    706   1213    114    296    146       C  
ATOM   7290  C   LEU B 449     -47.047   5.097 138.805  1.00 12.79           C  
ANISOU 7290  C   LEU B 449     1756   1320   1782    100    288    151       C  
ATOM   7291  O   LEU B 449     -47.138   4.101 138.083  1.00 12.16           O  
ANISOU 7291  O   LEU B 449     1639   1261   1720     88    283    170       O  
ATOM   7292  CB  LEU B 449     -46.336   7.275 137.730  1.00  7.85           C  
ANISOU 7292  CB  LEU B 449     1141    656   1188     93    257    135       C  
ATOM   7293  CG  LEU B 449     -45.570   6.623 136.560  1.00 11.44           C  
ANISOU 7293  CG  LEU B 449     1557   1127   1662     66    227    150       C  
ATOM   7294  CD1 LEU B 449     -46.501   6.317 135.399  1.00 10.71           C  
ANISOU 7294  CD1 LEU B 449     1420   1050   1601     71    241    173       C  
ATOM   7295  CD2 LEU B 449     -44.429   7.504 136.100  1.00 12.35           C  
ANISOU 7295  CD2 LEU B 449     1682   1224   1786     46    195    140       C  
ATOM   7296  N   GLU B 450     -46.564   5.044 140.066  1.00 10.23           N  
ANISOU 7296  N   GLU B 450     1477    990   1419    104    286    134       N  
ATOM   7297  CA  GLU B 450     -46.105   3.796 140.672  1.00  9.82           C  
ANISOU 7297  CA  GLU B 450     1431    957   1343     93    278    139       C  
ATOM   7298  C   GLU B 450     -47.246   2.797 140.831  1.00 14.46           C  
ANISOU 7298  C   GLU B 450     1995   1564   1934    105    315    162       C  
ATOM   7299  O   GLU B 450     -47.049   1.607 140.591  1.00 13.35           O  
ANISOU 7299  O   GLU B 450     1831   1443   1800     91    305    178       O  
ATOM   7300  CB  GLU B 450     -45.416   4.058 142.014  1.00 11.17           C  
ANISOU 7300  CB  GLU B 450     1659   1116   1469     97    267    116       C  
ATOM   7301  CG  GLU B 450     -43.999   4.587 141.862  1.00 18.34           C  
ANISOU 7301  CG  GLU B 450     2583   2009   2376     74    218     97       C  
ATOM   7302  CD  GLU B 450     -43.354   5.031 143.156  1.00 27.81           C  
ANISOU 7302  CD  GLU B 450     3842   3192   3533     79    202     70       C  
ATOM   7303  OE1 GLU B 450     -43.845   6.013 143.757  1.00 11.78           O  
ANISOU 7303  OE1 GLU B 450     1847   1141   1487    101    220     53       O  
ATOM   7304  OE2 GLU B 450     -42.310   4.451 143.527  1.00 17.52           O  
ANISOU 7304  OE2 GLU B 450     2549   1893   2213     61    167     65       O  
ATOM   7305  N   LYS B 451     -48.472   3.292 141.169  1.00 11.01           N  
ANISOU 7305  N   LYS B 451     1560   1122   1500    133    358    166       N  
ATOM   7306  CA  LYS B 451     -49.667   2.436 141.270  1.00 10.56           C  
ANISOU 7306  CA  LYS B 451     1475   1083   1455    145    397    191       C  
ATOM   7307  C   LYS B 451     -50.002   1.832 139.911  1.00 15.19           C  
ANISOU 7307  C   LYS B 451     2002   1682   2087    130    385    213       C  
ATOM   7308  O   LYS B 451     -50.293   0.638 139.820  1.00 15.30           O  
ANISOU 7308  O   LYS B 451     1990   1713   2109    122    389    232       O  
ATOM   7309  CB  LYS B 451     -50.873   3.245 141.779  1.00 12.86           C  
ANISOU 7309  CB  LYS B 451     1775   1364   1747    178    445    190       C  
ATOM   7310  CG  LYS B 451     -50.719   3.784 143.178  1.00 15.75           C  
ANISOU 7310  CG  LYS B 451     2202   1719   2064    198    463    168       C  
ATOM   7311  CD  LYS B 451     -51.884   4.717 143.527  1.00 14.37           C  
ANISOU 7311  CD  LYS B 451     2034   1532   1894    233    511    165       C  
ATOM   7312  CE  LYS B 451     -51.755   5.299 144.905  1.00 14.10           C  
ANISOU 7312  CE  LYS B 451     2065   1485   1808    257    530    140       C  
ATOM   7313  NZ  LYS B 451     -51.961   4.273 145.958  1.00 17.07           N  
ANISOU 7313  NZ  LYS B 451     2459   1881   2147    262    557    153       N  
ATOM   7314  N   ILE B 452     -50.027   2.678 138.853  1.00 11.84           N  
ANISOU 7314  N   ILE B 452     1558   1248   1692    129    371    210       N  
ATOM   7315  CA  ILE B 452     -50.368   2.242 137.495  1.00 10.69           C  
ANISOU 7315  CA  ILE B 452     1361   1113   1586    118    358    228       C  
ATOM   7316  C   ILE B 452     -49.414   1.155 137.011  1.00 14.02           C  
ANISOU 7316  C   ILE B 452     1769   1550   2007     90    323    233       C  
ATOM   7317  O   ILE B 452     -49.863   0.117 136.527  1.00 14.12           O  
ANISOU 7317  O   ILE B 452     1748   1578   2039     84    323    251       O  
ATOM   7318  CB  ILE B 452     -50.408   3.461 136.512  1.00 13.33           C  
ANISOU 7318  CB  ILE B 452     1687   1433   1946    121    347    224       C  
ATOM   7319  CG1 ILE B 452     -51.487   4.484 136.941  1.00 13.43           C  
ANISOU 7319  CG1 ILE B 452     1707   1430   1965    152    384    221       C  
ATOM   7320  CG2 ILE B 452     -50.622   2.991 135.046  1.00 13.30           C  
ANISOU 7320  CG2 ILE B 452     1635   1442   1977    109    327    242       C  
ATOM   7321  CD1 ILE B 452     -51.361   5.817 136.283  1.00 18.56           C  
ANISOU 7321  CD1 ILE B 452     2362   2058   2630    157    372    212       C  
ATOM   7322  N   ILE B 453     -48.091   1.385 137.147  1.00  9.59           N  
ANISOU 7322  N   ILE B 453     1235    984   1425     75    292    215       N  
ATOM   7323  CA  ILE B 453     -47.091   0.424 136.675  1.00  9.23           C  
ANISOU 7323  CA  ILE B 453     1176    951   1379     51    258    217       C  
ATOM   7324  C   ILE B 453     -47.087  -0.864 137.517  1.00 12.07           C  
ANISOU 7324  C   ILE B 453     1542   1324   1721     48    264    225       C  
ATOM   7325  O   ILE B 453     -46.952  -1.950 136.962  1.00 10.35           O  
ANISOU 7325  O   ILE B 453     1296   1119   1516     36    249    237       O  
ATOM   7326  CB  ILE B 453     -45.674   1.069 136.556  1.00 12.18           C  
ANISOU 7326  CB  ILE B 453     1571   1315   1741     36    224    199       C  
ATOM   7327  CG1 ILE B 453     -45.704   2.334 135.641  1.00 12.35           C  
ANISOU 7327  CG1 ILE B 453     1586   1323   1785     37    219    196       C  
ATOM   7328  CG2 ILE B 453     -44.645   0.044 136.054  1.00 12.96           C  
ANISOU 7328  CG2 ILE B 453     1653   1428   1842     14    192    202       C  
ATOM   7329  CD1 ILE B 453     -46.197   2.068 134.146  1.00 16.57           C  
ANISOU 7329  CD1 ILE B 453     2075   1870   2353     34    216    214       C  
ATOM   7330  N   THR B 454     -47.311  -0.746 138.848  1.00  9.58           N  
ANISOU 7330  N   THR B 454     1262   1002   1374     62    286    220       N  
ATOM   7331  CA  THR B 454     -47.425  -1.928 139.719  1.00  9.81           C  
ANISOU 7331  CA  THR B 454     1300   1042   1385     61    296    231       C  
ATOM   7332  C   THR B 454     -48.595  -2.810 139.262  1.00 13.89           C  
ANISOU 7332  C   THR B 454     1774   1571   1932     64    319    257       C  
ATOM   7333  O   THR B 454     -48.434  -4.025 139.119  1.00 14.11           O  
ANISOU 7333  O   THR B 454     1785   1609   1967     51    307    270       O  
ATOM   7334  CB  THR B 454     -47.585  -1.501 141.195  1.00 16.06           C  
ANISOU 7334  CB  THR B 454     2141   1826   2135     79    322    222       C  
ATOM   7335  OG1 THR B 454     -46.455  -0.723 141.578  1.00 18.20           O  
ANISOU 7335  OG1 THR B 454     2451   2084   2381     74    293    196       O  
ATOM   7336  CG2 THR B 454     -47.735  -2.696 142.137  1.00 14.33           C  
ANISOU 7336  CG2 THR B 454     1934   1618   1893     79    335    237       C  
ATOM   7337  N   GLN B 455     -49.755  -2.187 138.978  1.00  8.30           N  
ANISOU 7337  N   GLN B 455     1048    859   1247     80    350    265       N  
ATOM   7338  CA  GLN B 455     -50.937  -2.912 138.540  1.00  7.42           C  
ANISOU 7338  CA  GLN B 455      893    757   1170     83    370    290       C  
ATOM   7339  C   GLN B 455     -50.809  -3.393 137.097  1.00 11.25           C  
ANISOU 7339  C   GLN B 455     1336   1249   1691     67    338    296       C  
ATOM   7340  O   GLN B 455     -51.315  -4.462 136.764  1.00 12.87           O  
ANISOU 7340  O   GLN B 455     1509   1462   1919     59    337    314       O  
ATOM   7341  CB  GLN B 455     -52.196  -2.063 138.725  1.00  8.74           C  
ANISOU 7341  CB  GLN B 455     1052    918   1352    108    412    296       C  
ATOM   7342  CG  GLN B 455     -52.557  -1.823 140.198  1.00 18.60           C  
ANISOU 7342  CG  GLN B 455     2339   2163   2566    128    453    294       C  
ATOM   7343  CD  GLN B 455     -52.830  -3.112 140.935  1.00 26.51           C  
ANISOU 7343  CD  GLN B 455     3338   3177   3559    123    471    316       C  
ATOM   7344  OE1 GLN B 455     -53.446  -4.049 140.403  1.00 21.97           O  
ANISOU 7344  OE1 GLN B 455     2719   2610   3018    114    472    339       O  
ATOM   7345  NE2 GLN B 455     -52.412  -3.175 142.189  1.00 14.87           N  
ANISOU 7345  NE2 GLN B 455     1911   1702   2037    130    484    309       N  
ATOM   7346  N   LYS B 456     -50.095  -2.625 136.246  1.00  6.07           N  
ANISOU 7346  N   LYS B 456      672    598   1034     84    292    254       N  
ATOM   7347  CA  LYS B 456     -49.842  -3.017 134.859  1.00  5.66           C  
ANISOU 7347  CA  LYS B 456      588    578    984     96    224    212       C  
ATOM   7348  C   LYS B 456     -48.904  -4.227 134.814  1.00  8.99           C  
ANISOU 7348  C   LYS B 456     1017    974   1424     27    251    283       C  
ATOM   7349  O   LYS B 456     -49.104  -5.132 134.010  1.00  7.10           O  
ANISOU 7349  O   LYS B 456      747    743   1207     19    235    293       O  
ATOM   7350  CB  LYS B 456     -49.236  -1.844 134.077  1.00  7.28           C  
ANISOU 7350  CB  LYS B 456      808    741   1218     45    261    271       C  
ATOM   7351  CG  LYS B 456     -49.091  -2.103 132.588  1.00 12.75           C  
ANISOU 7351  CG  LYS B 456     1468   1442   1934     35    233    276       C  
ATOM   7352  CD  LYS B 456     -48.359  -0.977 131.914  1.00 16.31           C  
ANISOU 7352  CD  LYS B 456     1930   1886   2383     32    217    265       C  
ATOM   7353  CE  LYS B 456     -48.225  -1.197 130.439  1.00 19.00           C  
ANISOU 7353  CE  LYS B 456     2242   2235   2740     24    193    271       C  
ATOM   7354  NZ  LYS B 456     -47.316  -0.202 129.825  1.00 18.55           N  
ANISOU 7354  NZ  LYS B 456     2197   2172   2677     19    178    263       N  
ATOM   7355  N   TYR B 457     -47.884  -4.242 135.706  1.00  7.14           N  
ANISOU 7355  N   TYR B 457      819    738   1157     22    242    271       N  
ATOM   7356  CA  TYR B 457     -46.915  -5.328 135.803  1.00  7.41           C  
ANISOU 7356  CA  TYR B 457      856    779   1181      7    215    269       C  
ATOM   7357  C   TYR B 457     -47.606  -6.637 136.218  1.00 13.80           C  
ANISOU 7357  C   TYR B 457     1651   1593   1998      6    227    288       C  
ATOM   7358  O   TYR B 457     -47.495  -7.639 135.508  1.00 14.56           O  
ANISOU 7358  O   TYR B 457     1723   1696   2114     -5    207    295       O  
ATOM   7359  CB  TYR B 457     -45.798  -4.954 136.811  1.00  8.39           C  
ANISOU 7359  CB  TYR B 457     1023    897   1269      4    205    253       C  
ATOM   7360  CG  TYR B 457     -44.725  -6.007 136.970  1.00  9.60           C  
ANISOU 7360  CG  TYR B 457     1180   1056   1412    -10    175    250       C  
ATOM   7361  CD1 TYR B 457     -44.872  -7.046 137.887  1.00 11.41           C  
ANISOU 7361  CD1 TYR B 457     1420   1287   1627    -10    182    262       C  
ATOM   7362  CD2 TYR B 457     -43.502  -5.889 136.313  1.00 10.13           C  
ANISOU 7362  CD2 TYR B 457     1242   1125   1481    -23    142    238       C  
ATOM   7363  CE1 TYR B 457     -43.866  -7.986 138.083  1.00 12.15           C  
ANISOU 7363  CE1 TYR B 457     1520   1385   1713    -22    153    260       C  
ATOM   7364  CE2 TYR B 457     -42.478  -6.809 136.521  1.00 10.53           C  
ANISOU 7364  CE2 TYR B 457     1297   1181   1524    -34    115    235       C  
ATOM   7365  CZ  TYR B 457     -42.664  -7.857 137.410  1.00 16.88           C  
ANISOU 7365  CZ  TYR B 457     2112   1986   2316    -33    119    245       C  
ATOM   7366  OH  TYR B 457     -41.665  -8.778 137.612  1.00 14.36           O  
ANISOU 7366  OH  TYR B 457     1796   1669   1991    -42     90    243       O  
ATOM   7367  N   ILE B 458     -48.359  -6.615 137.360  1.00 10.74           N  
ANISOU 7367  N   ILE B 458     1281   1203   1598     18    262    298       N  
ATOM   7368  CA  ILE B 458     -49.078  -7.806 137.867  1.00 11.02           C  
ANISOU 7368  CA  ILE B 458     1304   1242   1642     16    279    321       C  
ATOM   7369  C   ILE B 458     -50.068  -8.345 136.821  1.00 15.62           C  
ANISOU 7369  C   ILE B 458     1837   1828   2271     13    279    337       C  
ATOM   7370  O   ILE B 458     -50.154  -9.566 136.622  1.00 15.89           O  
ANISOU 7370  O   ILE B 458     1852   1864   2322      1    267    350       O  
ATOM   7371  CB  ILE B 458     -49.782  -7.505 139.237  1.00 14.51           C  
ANISOU 7371  CB  ILE B 458     1773   1681   2060     33    323    331       C  
ATOM   7372  CG1 ILE B 458     -48.767  -6.985 140.287  1.00 14.45           C  
ANISOU 7372  CG1 ILE B 458     1819   1669   2003     36    317    312       C  
ATOM   7373  CG2 ILE B 458     -50.537  -8.754 139.761  1.00 16.05           C  
ANISOU 7373  CG2 ILE B 458     1953   1880   2266     30    344    359       C  
ATOM   7374  CD1 ILE B 458     -49.428  -6.354 141.572  1.00 17.22           C  
ANISOU 7374  CD1 ILE B 458     2204   2016   2322     58    362    314       C  
ATOM   7375  N   ALA B 459     -50.763  -7.431 136.100  1.00 11.26           N  
ANISOU 7375  N   ALA B 459     1265   1274   1740     22    289    336       N  
ATOM   7376  CA  ALA B 459     -51.721  -7.818 135.060  1.00 11.26           C  
ANISOU 7376  CA  ALA B 459     1219   1276   1784     20    284    349       C  
ATOM   7377  C   ALA B 459     -51.027  -8.461 133.836  1.00 15.38           C  
ANISOU 7377  C   ALA B 459     1723   1801   2318      4    240    341       C  
ATOM   7378  O   ALA B 459     -51.694  -9.085 133.008  1.00 15.38           O  
ANISOU 7378  O   ALA B 459     1689   1803   2352      0    228    351       O  
ATOM   7379  CB  ALA B 459     -52.536  -6.606 134.623  1.00 12.16           C  
ANISOU 7379  CB  ALA B 459     1320   1386   1914     35    302    349       C  
ATOM   7380  N   GLY B 460     -49.700  -8.310 133.748  1.00 12.33           N  
ANISOU 7380  N   GLY B 460     1361   1418   1906     -2    215    323       N  
ATOM   7381  CA  GLY B 460     -48.921  -8.837 132.627  1.00 11.30           C  
ANISOU 7381  CA  GLY B 460     1218   1293   1783    -14    177    313       C  
ATOM   7382  C   GLY B 460     -48.134 -10.098 132.944  1.00 14.46           C  
ANISOU 7382  C   GLY B 460     1624   1694   2175    -26    157    312       C  
ATOM   7383  O   GLY B 460     -47.453 -10.638 132.069  1.00 13.82           O  
ANISOU 7383  O   GLY B 460     1534   1618   2099    -33    127    303       O  
ATOM   7384  N   ILE B 461     -48.217 -10.583 134.197  1.00 10.78           N  
ANISOU 7384  N   ILE B 461     1176   1224   1694    -26    174    322       N  
ATOM   7385  CA  ILE B 461     -47.474 -11.789 134.608  1.00 10.18           C  
ANISOU 7385  CA  ILE B 461     1109   1147   1610    -36    155    323       C  
ATOM   7386  C   ILE B 461     -48.130 -13.074 134.051  1.00 13.76           C  
ANISOU 7386  C   ILE B 461     1532   1599   2099    -43    144    337       C  
ATOM   7387  O   ILE B 461     -49.293 -13.346 134.346  1.00 13.19           O  
ANISOU 7387  O   ILE B 461     1443   1522   2047    -42    166    357       O  
ATOM   7388  CB  ILE B 461     -47.323 -11.861 136.171  1.00 12.72           C  
ANISOU 7388  CB  ILE B 461     1465   1466   1901    -32    176    331       C  
ATOM   7389  CG1 ILE B 461     -46.607 -10.607 136.728  1.00 12.43           C  
ANISOU 7389  CG1 ILE B 461     1463   1429   1830    -25    181    313       C  
ATOM   7390  CG2 ILE B 461     -46.596 -13.160 136.595  1.00 13.15           C  
ANISOU 7390  CG2 ILE B 461     1528   1518   1950    -42    154    336       C  
ATOM   7391  CD1 ILE B 461     -46.528 -10.555 138.268  1.00 13.77           C  
ANISOU 7391  CD1 ILE B 461     1672   1596   1964    -19    201    318       C  
ATOM   7392  N   PRO B 462     -47.375 -13.924 133.301  1.00 10.56           N  
ANISOU 7392  N   PRO B 462     1117   1194   1701    -52    109    328       N  
ATOM   7393  CA  PRO B 462     -45.959 -13.794 132.941  1.00 10.50           C  
ANISOU 7393  CA  PRO B 462     1125   1192   1674    -54     82    306       C  
ATOM   7394  C   PRO B 462     -45.737 -13.497 131.434  1.00 14.30           C  
ANISOU 7394  C   PRO B 462     1586   1680   2168    -53     62    292       C  
ATOM   7395  O   PRO B 462     -44.618 -13.194 131.035  1.00 14.47           O  
ANISOU 7395  O   PRO B 462     1615   1708   2174    -53     45    276       O  
ATOM   7396  CB  PRO B 462     -45.409 -15.174 133.302  1.00 12.40           C  
ANISOU 7396  CB  PRO B 462     1368   1426   1916    -61     62    310       C  
ATOM   7397  CG  PRO B 462     -46.626 -16.153 133.012  1.00 16.57           C  
ANISOU 7397  CG  PRO B 462     1870   1947   2481    -65     65    328       C  
ATOM   7398  CD  PRO B 462     -47.881 -15.260 132.946  1.00 12.08           C  
ANISOU 7398  CD  PRO B 462     1287   1380   1925    -59     94    339       C  
ATOM   7399  N   ASP B 463     -46.806 -13.665 130.590  1.00 10.20           N  
ANISOU 7399  N   ASP B 463     1040   1160   1677    -51     61    299       N  
ATOM   7400  CA  ASP B 463     -46.693 -13.600 129.115  1.00  8.79           C  
ANISOU 7400  CA  ASP B 463      844    988   1509    -50     38    287       C  
ATOM   7401  C   ASP B 463     -46.301 -12.222 128.580  1.00 12.54           C  
ANISOU 7401  C   ASP B 463     1326   1471   1967    -44     43    277       C  
ATOM   7402  O   ASP B 463     -45.837 -12.123 127.441  1.00 12.32           O  
ANISOU 7402  O   ASP B 463     1291   1450   1938    -42     25    266       O  
ATOM   7403  CB  ASP B 463     -47.989 -14.092 128.441  1.00 10.26           C  
ANISOU 7403  CB  ASP B 463     1001   1168   1729    -50     33    297       C  
ATOM   7404  CG  ASP B 463     -48.288 -15.564 128.675  1.00 12.17           C  
ANISOU 7404  CG  ASP B 463     1232   1399   1992    -58     19    306       C  
ATOM   7405  OD1 ASP B 463     -47.351 -16.310 129.057  1.00 10.64           O  
ANISOU 7405  OD1 ASP B 463     1052   1203   1786    -62      7    299       O  
ATOM   7406  OD2 ASP B 463     -49.436 -15.987 128.406  1.00 14.92           O  
ANISOU 7406  OD2 ASP B 463     1557   1740   2373    -61     17    318       O  
ATOM   7407  N   LEU B 464     -46.522 -11.148 129.372  1.00  8.39           N  
ANISOU 7407  N   LEU B 464      814    943   1430    -39     69    282       N  
ATOM   7408  CA  LEU B 464     -46.143  -9.794 128.943  1.00  8.06           C  
ANISOU 7408  CA  LEU B 464      782    906   1376    -35     74    274       C  
ATOM   7409  C   LEU B 464     -44.790  -9.366 129.546  1.00 13.10           C  
ANISOU 7409  C   LEU B 464     1445   1545   1987    -39     71    262       C  
ATOM   7410  O   LEU B 464     -44.549  -8.170 129.733  1.00 13.79           O  
ANISOU 7410  O   LEU B 464     1547   1630   2063    -36     82    258       O  
ATOM   7411  CB  LEU B 464     -47.249  -8.766 129.297  1.00  7.97           C  
ANISOU 7411  CB  LEU B 464      769    888   1371    -26    102    284       C  
ATOM   7412  CG  LEU B 464     -48.545  -8.794 128.412  1.00 11.99           C  
ANISOU 7412  CG  LEU B 464     1249   1397   1910    -20    102    295       C  
ATOM   7413  CD1 LEU B 464     -48.203  -8.722 126.913  1.00 11.67           C  
ANISOU 7413  CD1 LEU B 464     1197   1365   1873    -20     75    287       C  
ATOM   7414  CD2 LEU B 464     -49.411 -10.021 128.721  1.00 12.91           C  
ANISOU 7414  CD2 LEU B 464     1346   1510   2051    -24    102    308       C  
ATOM   7415  N   ALA B 465     -43.867 -10.344 129.755  1.00  9.47           N  
ANISOU 7415  N   ALA B 465      990   1087   1521    -45     53    255       N  
ATOM   7416  CA  ALA B 465     -42.546 -10.084 130.360  1.00  8.72           C  
ANISOU 7416  CA  ALA B 465      916    994   1405    -50     45    245       C  
ATOM   7417  C   ALA B 465     -41.695  -9.103 129.536  1.00 11.61           C  
ANISOU 7417  C   ALA B 465     1280   1365   1765    -52     38    235       C  
ATOM   7418  O   ALA B 465     -40.833  -8.425 130.095  1.00 11.14           O  
ANISOU 7418  O   ALA B 465     1238   1303   1692    -56     37    228       O  
ATOM   7419  CB  ALA B 465     -41.795 -11.390 130.561  1.00  9.41           C  
ANISOU 7419  CB  ALA B 465     1001   1081   1491    -55     24    241       C  
ATOM   7420  N   GLN B 466     -41.918  -9.045 128.206  1.00  8.12           N  
ANISOU 7420  N   GLN B 466      819    931   1334    -48     32    234       N  
ATOM   7421  CA  GLN B 466     -41.213  -8.084 127.359  1.00  8.25           C  
ANISOU 7421  CA  GLN B 466      835    954   1347    -49     30    229       C  
ATOM   7422  C   GLN B 466     -41.676  -6.664 127.681  1.00 13.67           C  
ANISOU 7422  C   GLN B 466     1532   1631   2030    -47     48    234       C  
ATOM   7423  O   GLN B 466     -40.855  -5.757 127.769  1.00 14.95           O  
ANISOU 7423  O   GLN B 466     1705   1791   2185    -52     48    229       O  
ATOM   7424  CB  GLN B 466     -41.429  -8.404 125.861  1.00  9.45           C  
ANISOU 7424  CB  GLN B 466      967   1117   1506    -44     20    229       C  
ATOM   7425  CG  GLN B 466     -40.594  -7.516 124.909  1.00 10.68           C  
ANISOU 7425  CG  GLN B 466     1121   1281   1655    -45     19    227       C  
ATOM   7426  CD  GLN B 466     -39.105  -7.645 125.165  1.00 18.29           C  
ANISOU 7426  CD  GLN B 466     2088   2250   2611    -52     11    219       C  
ATOM   7427  OE1 GLN B 466     -38.529  -8.730 125.092  1.00 10.51           O  
ANISOU 7427  OE1 GLN B 466     1097   1271   1627    -52     -2    212       O  
ATOM   7428  NE2 GLN B 466     -38.451  -6.528 125.446  1.00 10.63           N  
ANISOU 7428  NE2 GLN B 466     1127   1276   1638    -59     17    220       N  
ATOM   7429  N   GLU B 467     -42.983  -6.490 127.929  1.00 10.30           N  
ANISOU 7429  N   GLU B 467     1104   1198   1612    -40     64    243       N  
ATOM   7430  CA  GLU B 467     -43.536  -5.191 128.321  1.00 10.36           C  
ANISOU 7430  CA  GLU B 467     1124   1195   1619    -35     83    246       C  
ATOM   7431  C   GLU B 467     -43.155  -4.838 129.745  1.00 15.72           C  
ANISOU 7431  C   GLU B 467     1828   1862   2281    -37     92    240       C  
ATOM   7432  O   GLU B 467     -42.964  -3.657 130.061  1.00 16.65           O  
ANISOU 7432  O   GLU B 467     1964   1971   2393    -36     99    236       O  
ATOM   7433  CB  GLU B 467     -45.062  -5.166 128.135  1.00 11.13           C  
ANISOU 7433  CB  GLU B 467     1207   1290   1734    -24     97    258       C  
ATOM   7434  CG  GLU B 467     -45.476  -5.101 126.675  1.00 13.83           C  
ANISOU 7434  CG  GLU B 467     1527   1638   2088    -20     86    263       C  
ATOM   7435  CD  GLU B 467     -44.842  -3.953 125.908  1.00 20.43           C  
ANISOU 7435  CD  GLU B 467     2369   2475   2918    -20     83    262       C  
ATOM   7436  OE1 GLU B 467     -44.972  -2.793 126.358  1.00 16.99           O  
ANISOU 7436  OE1 GLU B 467     1948   2028   2481    -17     97    263       O  
ATOM   7437  OE2 GLU B 467     -44.187  -4.220 124.875  1.00 10.05           O  
ANISOU 7437  OE2 GLU B 467     1047   1173   1600    -24     67    259       O  
ATOM   7438  N   GLY B 468     -42.981  -5.867 130.584  1.00 11.66           N  
ANISOU 7438  N   GLY B 468     1321   1350   1759    -40     88    240       N  
ATOM   7439  CA  GLY B 468     -42.473  -5.698 131.938  1.00 11.18           C  
ANISOU 7439  CA  GLY B 468     1290   1281   1679    -42     91    233       C  
ATOM   7440  C   GLY B 468     -41.039  -5.211 131.950  1.00 14.18           C  
ANISOU 7440  C   GLY B 468     1680   1659   2048    -52     71    221       C  
ATOM   7441  O   GLY B 468     -40.697  -4.297 132.703  1.00 14.39           O  
ANISOU 7441  O   GLY B 468     1731   1674   2061    -53     74    213       O  
ATOM   7442  N   TRP B 469     -40.196  -5.773 131.046  1.00  9.37           N  
ANISOU 7442  N   TRP B 469     1052   1062   1448    -59     51    218       N  
ATOM   7443  CA  TRP B 469     -38.799  -5.349 130.903  1.00  8.23           C  
ANISOU 7443  CA  TRP B 469      910    918   1300    -70     33    209       C  
ATOM   7444  C   TRP B 469     -38.716  -3.960 130.227  1.00 11.05           C  
ANISOU 7444  C   TRP B 469     1265   1269   1663    -72     40    210       C  
ATOM   7445  O   TRP B 469     -37.873  -3.140 130.607  1.00 11.00           O  
ANISOU 7445  O   TRP B 469     1272   1254   1653    -80     32    203       O  
ATOM   7446  CB  TRP B 469     -37.991  -6.398 130.107  1.00  6.07           C  
ANISOU 7446  CB  TRP B 469      614    659   1035    -73     15    208       C  
ATOM   7447  CG  TRP B 469     -36.521  -6.084 129.975  1.00  6.67           C  
ANISOU 7447  CG  TRP B 469      686    737   1111    -84     -2    201       C  
ATOM   7448  CD1 TRP B 469     -35.731  -5.459 130.898  1.00  9.60           C  
ANISOU 7448  CD1 TRP B 469     1075   1097   1475    -92    -12    194       C  
ATOM   7449  CD2 TRP B 469     -35.636  -6.569 128.956  1.00  6.33           C  
ANISOU 7449  CD2 TRP B 469      620    708   1078    -86    -12    199       C  
ATOM   7450  NE1 TRP B 469     -34.423  -5.446 130.470  1.00  8.85           N  
ANISOU 7450  NE1 TRP B 469      966   1009   1390   -101    -28    190       N  
ATOM   7451  CE2 TRP B 469     -34.338  -6.116 129.277  1.00 10.15           C  
ANISOU 7451  CE2 TRP B 469     1103   1189   1563    -97    -26    194       C  
ATOM   7452  CE3 TRP B 469     -35.818  -7.331 127.787  1.00  7.49           C  
ANISOU 7452  CE3 TRP B 469      745    869   1231    -79    -12    201       C  
ATOM   7453  CZ2 TRP B 469     -33.232  -6.371 128.456  1.00  9.67           C  
ANISOU 7453  CZ2 TRP B 469     1020   1141   1514   -100    -35    193       C  
ATOM   7454  CZ3 TRP B 469     -34.719  -7.596 126.984  1.00  8.77           C  
ANISOU 7454  CZ3 TRP B 469      889   1044   1400    -80    -20    198       C  
ATOM   7455  CH2 TRP B 469     -33.446  -7.120 127.318  1.00  9.61           C  
ANISOU 7455  CH2 TRP B 469      992   1148   1509    -91    -29    195       C  
ATOM   7456  N   ASN B 470     -39.643  -3.676 129.274  1.00  5.99           N  
ANISOU 7456  N   ASN B 470      607    649   1018    -36     40    200       N  
ATOM   7457  CA  ASN B 470     -39.710  -2.372 128.604  1.00  5.56           C  
ANISOU 7457  CA  ASN B 470      549    609    955     -4     32    182       C  
ATOM   7458  C   ASN B 470     -40.004  -1.243 129.593  1.00 10.11           C  
ANISOU 7458  C   ASN B 470     1159   1127   1555    -62     70    218       C  
ATOM   7459  O   ASN B 470     -39.318  -0.221 129.574  1.00 10.63           O  
ANISOU 7459  O   ASN B 470     1234   1182   1623    -69     65    214       O  
ATOM   7460  CB  ASN B 470     -40.760  -2.385 127.487  1.00  4.76           C  
ANISOU 7460  CB  ASN B 470      435    499    874    -11     48    206       C  
ATOM   7461  CG  ASN B 470     -40.379  -3.239 126.300  1.00 21.18           C  
ANISOU 7461  CG  ASN B 470     2494   2575   2977    -55     57    236       C  
ATOM   7462  OD1 ASN B 470     -39.210  -3.602 126.108  1.00 14.87           O  
ANISOU 7462  OD1 ASN B 470     1690   1784   2174    -63     45    231       O  
ATOM   7463  ND2 ASN B 470     -41.364  -3.582 125.474  1.00  8.53           N  
ANISOU 7463  ND2 ASN B 470      879    981   1383    -45     59    243       N  
ATOM   7464  N   ASP B 471     -41.044  -1.419 130.456  1.00  6.55           N  
ANISOU 7464  N   ASP B 471      721    670   1099    -50     86    218       N  
ATOM   7465  CA  ASP B 471     -41.429  -0.385 131.437  1.00  6.36           C  
ANISOU 7465  CA  ASP B 471      724    626   1065    -44    100    212       C  
ATOM   7466  C   ASP B 471     -40.389  -0.243 132.555  1.00 10.67           C  
ANISOU 7466  C   ASP B 471     1297   1162   1593    -53     85    197       C  
ATOM   7467  O   ASP B 471     -40.269   0.831 133.144  1.00 10.14           O  
ANISOU 7467  O   ASP B 471     1256   1077   1521    -52     87    188       O  
ATOM   7468  CB  ASP B 471     -42.829  -0.671 132.026  1.00  7.54           C  
ANISOU 7468  CB  ASP B 471      876    774   1213    -27    125    218       C  
ATOM   7469  CG  ASP B 471     -43.977  -0.462 131.038  1.00 11.97           C  
ANISOU 7469  CG  ASP B 471     1414   1339   1796    -16    138    231       C  
ATOM   7470  OD1 ASP B 471     -43.809   0.340 130.095  1.00  9.73           O  
ANISOU 7470  OD1 ASP B 471     1122   1052   1523    -18    133    234       O  
ATOM   7471  OD2 ASP B 471     -45.066  -1.027 131.268  1.00 16.55           O  
ANISOU 7471  OD2 ASP B 471     1983   1922   2382     -6    155    240       O  
ATOM   7472  N   LYS B 472     -39.632  -1.332 132.848  1.00  8.76           N  
ANISOU 7472  N   LYS B 472     1051    931   1344    -61     68    195       N  
ATOM   7473  CA  LYS B 472     -38.555  -1.284 133.846  1.00  8.49           C  
ANISOU 7473  CA  LYS B 472     1042    890   1295    -71     48    182       C  
ATOM   7474  C   LYS B 472     -37.370  -0.465 133.316  1.00 11.97           C  
ANISOU 7474  C   LYS B 472     1476   1324   1748    -86     27    176       C  
ATOM   7475  O   LYS B 472     -36.711   0.243 134.082  1.00 11.36           O  
ANISOU 7475  O   LYS B 472     1422   1231   1664    -93     13    164       O  
ATOM   7476  CB  LYS B 472     -38.104  -2.710 134.236  1.00 11.05           C  
ANISOU 7476  CB  LYS B 472     1361   1227   1612    -74     34    183       C  
ATOM   7477  CG  LYS B 472     -37.016  -2.744 135.341  1.00 15.50           C  
ANISOU 7477  CG  LYS B 472     1949   1783   2158    -82      9    170       C  
ATOM   7478  CD  LYS B 472     -37.483  -2.039 136.626  1.00 17.58           C  
ANISOU 7478  CD  LYS B 472     2254   2029   2396    -74     18    161       C  
ATOM   7479  CE  LYS B 472     -36.445  -2.075 137.706  1.00  3.05           C  
ANISOU 7479  CE  LYS B 472      384    385    392     -1     -2      3       C  
ATOM   7480  NZ  LYS B 472     -36.870  -1.294 138.893  1.00 10.08           N  
ANISOU 7480  NZ  LYS B 472     1378   1053   1399    -71     -3    135       N  
ATOM   7481  N   ARG B 473     -37.146  -0.509 132.007  1.00  8.39           N  
ANISOU 7481  N   ARG B 473      992    882   1313    -91     27    186       N  
ATOM   7482  CA  ARG B 473     -36.084   0.269 131.382  1.00  8.16           C  
ANISOU 7482  CA  ARG B 473      952    848   1299   -106     14    186       C  
ATOM   7483  C   ARG B 473     -36.531   1.686 131.134  1.00 11.31           C  
ANISOU 7483  C   ARG B 473     1362   1229   1706   -104     25    189       C  
ATOM   7484  O   ARG B 473     -35.733   2.604 131.230  1.00 11.76           O  
ANISOU 7484  O   ARG B 473     1426   1271   1772   -117     12    184       O  
ATOM   7485  CB  ARG B 473     -35.630  -0.388 130.070  1.00  6.79           C  
ANISOU 7485  CB  ARG B 473      743    697   1138   -109     12    197       C  
ATOM   7486  CG  ARG B 473     -34.827  -1.674 130.281  1.00  8.96           C  
ANISOU 7486  CG  ARG B 473     1006    986   1411   -113     -5    193       C  
ATOM   7487  CD  ARG B 473     -34.440  -2.317 128.965  1.00  9.99           C  
ANISOU 7487  CD  ARG B 473     1106   1139   1553   -113     -4    201       C  
ATOM   7488  NE  ARG B 473     -35.585  -2.929 128.296  1.00  8.79           N  
ANISOU 7488  NE  ARG B 473      945    997   1397    -99     10    208       N  
ATOM   7489  CZ  ARG B 473     -35.532  -3.470 127.082  1.00 16.98           C  
ANISOU 7489  CZ  ARG B 473     1960   2052   2440    -94     13    214       C  
ATOM   7490  NH1 ARG B 473     -34.396  -3.458 126.392  1.00  3.02           N  
ANISOU 7490  NH1 ARG B 473      382    382    382      0      0      0       N  
ATOM   7491  NH2 ARG B 473     -36.615  -4.013 126.543  1.00  4.04           N  
ANISOU 7491  NH2 ARG B 473      472    493    571     -1     -3     45       N  
ATOM   7492  N   ARG B 474     -37.816   1.875 130.856  1.00  7.89           N  
ANISOU 7492  N   ARG B 474      930    796   1273    -88     47    195       N  
ATOM   7493  CA  ARG B 474     -38.354   3.183 130.509  1.00  7.55           C  
ANISOU 7493  CA  ARG B 474      894    734   1239    -84     59    200       C  
ATOM   7494  C   ARG B 474     -38.598   4.067 131.757  1.00 11.05           C  
ANISOU 7494  C   ARG B 474     1374   1151   1672    -78     61    184       C  
ATOM   7495  O   ARG B 474     -38.347   5.273 131.711  1.00 11.29           O  
ANISOU 7495  O   ARG B 474     1418   1160   1712    -83     57    181       O  
ATOM   7496  CB  ARG B 474     -39.648   3.027 129.685  1.00  7.10           C  
ANISOU 7496  CB  ARG B 474      822    688   1189    -68     80    213       C  
ATOM   7497  CG  ARG B 474     -40.217   4.345 129.164  1.00 12.32           C  
ANISOU 7497  CG  ARG B 474     1487   1330   1863    -61     90    221       C  
ATOM   7498  CD  ARG B 474     -41.410   4.112 128.249  1.00 12.68           C  
ANISOU 7498  CD  ARG B 474     1513   1388   1917    -46    105    236       C  
ATOM   7499  NE  ARG B 474     -42.462   3.324 128.903  1.00  9.10           N  
ANISOU 7499  NE  ARG B 474     1059    940   1457    -31    118    233       N  
ATOM   7500  CZ  ARG B 474     -43.475   3.859 129.573  1.00 18.65           C  
ANISOU 7500  CZ  ARG B 474     2283   2136   2667    -15    137    231       C  
ATOM   7501  NH1 ARG B 474     -43.603   5.176 129.655  1.00  9.18           N  
ANISOU 7501  NH1 ARG B 474     1100    913   1474    -10    143    228       N  
ATOM   7502  NH2 ARG B 474     -44.379   3.080 130.151  1.00 10.01           N  
ANISOU 7502  NH2 ARG B 474     1185   1048   1569     -3    152    231       N  
ATOM   7503  N   LEU B 475     -39.085   3.468 132.861  1.00  7.60           N  
ANISOU 7503  N   LEU B 475      957    715   1214    -68     68    175       N  
ATOM   7504  CA  LEU B 475     -39.470   4.240 134.052  1.00  7.66           C  
ANISOU 7504  CA  LEU B 475     1004    701   1207    -57     75    160       C  
ATOM   7505  C   LEU B 475     -38.781   3.735 135.338  1.00 11.95           C  
ANISOU 7505  C   LEU B 475     1574   1241   1725    -62     58    144       C  
ATOM   7506  O   LEU B 475     -38.989   4.312 136.410  1.00 12.23           O  
ANISOU 7506  O   LEU B 475     1647   1258   1741    -53     61    128       O  
ATOM   7507  CB  LEU B 475     -41.013   4.205 134.234  1.00  7.62           C  
ANISOU 7507  CB  LEU B 475     1002    696   1198    -33    108    165       C  
ATOM   7508  CG  LEU B 475     -41.858   4.703 133.036  1.00 11.93           C  
ANISOU 7508  CG  LEU B 475     1522   1243   1768    -25    124    181       C  
ATOM   7509  CD1 LEU B 475     -43.316   4.377 133.234  1.00 12.02           C  
ANISOU 7509  CD1 LEU B 475     1528   1260   1779     -2    154    189       C  
ATOM   7510  CD2 LEU B 475     -41.673   6.205 132.812  1.00 14.90           C  
ANISOU 7510  CD2 LEU B 475     1912   1592   2156    -26    120    177       C  
ATOM   7511  N   ASN B 476     -37.985   2.639 135.236  1.00  9.06           N  
ANISOU 7511  N   ASN B 476     1191    894   1358    -74     39    147       N  
ATOM   7512  CA  ASN B 476     -37.396   1.952 136.415  1.00  9.23           C  
ANISOU 7512  CA  ASN B 476     1236    917   1355    -77     22    136       C  
ATOM   7513  C   ASN B 476     -38.520   1.433 137.346  1.00 14.30           C  
ANISOU 7513  C   ASN B 476     1900   1562   1971    -57     47    136       C  
ATOM   7514  O   ASN B 476     -38.311   1.260 138.548  1.00 15.24           O  
ANISOU 7514  O   ASN B 476     2053   1675   2062    -53     40    125       O  
ATOM   7515  CB  ASN B 476     -36.408   2.879 137.181  1.00 10.41           C  
ANISOU 7515  CB  ASN B 476     1415   1042   1497    -88     -7    117       C  
ATOM   7516  CG  ASN B 476     -35.548   2.144 138.202  1.00 28.04           C  
ANISOU 7516  CG  ASN B 476     3666   3277   3709    -95    -35    107       C  
ATOM   7517  OD1 ASN B 476     -35.205   0.964 138.036  1.00 16.80           O  
ANISOU 7517  OD1 ASN B 476     2222   1874   2287    -99    -42    116       O  
ATOM   7518  ND2 ASN B 476     -35.158   2.837 139.255  1.00 20.46           N  
ANISOU 7518  ND2 ASN B 476     2747   2296   2731    -96    -54     87       N  
ATOM   7519  N   LEU B 477     -39.701   1.168 136.769  1.00 10.52           N  
ANISOU 7519  N   LEU B 477     1401   1093   1502    -44     78    151       N  
ATOM   7520  CA  LEU B 477     -40.851   0.715 137.519  1.00 10.38           C  
ANISOU 7520  CA  LEU B 477     1398   1080   1468    -25    107    156       C  
ATOM   7521  C   LEU B 477     -41.318  -0.670 137.038  1.00 15.27           C  
ANISOU 7521  C   LEU B 477     1984   1721   2096    -25    115    174       C  
ATOM   7522  O   LEU B 477     -41.202  -0.989 135.856  1.00 15.13           O  
ANISOU 7522  O   LEU B 477     1932   1715   2103    -33    108    183       O  
ATOM   7523  CB  LEU B 477     -42.001   1.736 137.409  1.00 10.08           C  
ANISOU 7523  CB  LEU B 477     1365   1029   1437     -7    138    156       C  
ATOM   7524  CG  LEU B 477     -41.782   3.073 138.108  1.00 14.21           C  
ANISOU 7524  CG  LEU B 477     1927   1526   1946     -1    135    136       C  
ATOM   7525  CD1 LEU B 477     -42.911   4.030 137.803  1.00 14.50           C  
ANISOU 7525  CD1 LEU B 477     1962   1550   1996     18    165    139       C  
ATOM   7526  CD2 LEU B 477     -41.647   2.889 139.600  1.00 16.22           C  
ANISOU 7526  CD2 LEU B 477     2227   1775   2162      7    136    122       C  
ATOM   7527  N   PRO B 478     -41.876  -1.504 137.942  1.00 12.45           N  
ANISOU 7527  N   PRO B 478     1640   1370   1720    -16    131    180       N  
ATOM   7528  CA  PRO B 478     -42.058  -1.273 139.380  1.00 12.71           C  
ANISOU 7528  CA  PRO B 478     1718   1394   1719     -4    143    171       C  
ATOM   7529  C   PRO B 478     -40.758  -1.461 140.159  1.00 16.35           C  
ANISOU 7529  C   PRO B 478     2207   1850   2156    -15    108    157       C  
ATOM   7530  O   PRO B 478     -39.715  -1.752 139.566  1.00 15.38           O  
ANISOU 7530  O   PRO B 478     2065   1732   2048    -33     76    155       O  
ATOM   7531  CB  PRO B 478     -43.109  -2.320 139.754  1.00 14.48           C  
ANISOU 7531  CB  PRO B 478     1934   1630   1939      7    172    190       C  
ATOM   7532  CG  PRO B 478     -42.806  -3.469 138.851  1.00 18.74           C  
ANISOU 7532  CG  PRO B 478     2434   2185   2502     -7    154    203       C  
ATOM   7533  CD  PRO B 478     -42.338  -2.850 137.549  1.00 13.94           C  
ANISOU 7533  CD  PRO B 478     1800   1577   1922    -17    137    198       C  
ATOM   7534  N   ARG B 479     -40.813  -1.287 141.488  1.00 13.23           N  
ANISOU 7534  N   ARG B 479     1858   1447   1724     -5    113    147       N  
ATOM   7535  CA  ARG B 479     -39.662  -1.524 142.341  1.00 12.85           C  
ANISOU 7535  CA  ARG B 479     1839   1394   1649    -14     78    135       C  
ATOM   7536  C   ARG B 479     -39.249  -2.994 142.265  1.00 16.70           C  
ANISOU 7536  C   ARG B 479     2306   1898   2140    -23     62    150       C  
ATOM   7537  O   ARG B 479     -40.077  -3.878 142.484  1.00 16.33           O  
ANISOU 7537  O   ARG B 479     2254   1863   2089    -15     88    168       O  
ATOM   7538  CB  ARG B 479     -39.982  -1.142 143.797  1.00 12.22           C  
ANISOU 7538  CB  ARG B 479     1816   1303   1523      4     90    123       C  
ATOM   7539  CG  ARG B 479     -38.790  -1.303 144.732  1.00 18.17           C  
ANISOU 7539  CG  ARG B 479     2605   2050   2247     -5     48    108       C  
ATOM   7540  CD  ARG B 479     -39.198  -1.884 146.072  1.00 21.43           C  
ANISOU 7540  CD  ARG B 479     3062   2467   2612     12     64    112       C  
ATOM   7541  NE  ARG B 479     -38.032  -2.224 146.892  1.00 23.84           N  
ANISOU 7541  NE  ARG B 479     3399   2769   2892      3     18    101       N  
ATOM   7542  CZ  ARG B 479     -37.359  -3.367 146.781  1.00 32.19           C  
ANISOU 7542  CZ  ARG B 479     4437   3838   3957    -10     -8    115       C  
ATOM   7543  NH1 ARG B 479     -37.721  -4.274 145.879  1.00 11.73           N  
ANISOU 7543  NH1 ARG B 479     1797   1262   1398    -16      7    137       N  
ATOM   7544  NH2 ARG B 479     -36.306  -3.602 147.555  1.00 16.33           N  
ANISOU 7544  NH2 ARG B 479     2456   1824   1924    -16    -51    105       N  
ATOM   7545  N   LEU B 480     -37.994  -3.254 141.900  1.00 13.63           N  
ANISOU 7545  N   LEU B 480     1904   1511   1765    -41     22    144       N  
ATOM   7546  CA  LEU B 480     -37.457  -4.614 141.872  1.00 13.00           C  
ANISOU 7546  CA  LEU B 480     1807   1444   1688    -49      3    156       C  
ATOM   7547  C   LEU B 480     -36.176  -4.675 142.680  1.00 16.22           C  
ANISOU 7547  C   LEU B 480     2241   1846   2078    -57    -40    143       C  
ATOM   7548  O   LEU B 480     -35.454  -3.679 142.762  1.00 15.52           O  
ANISOU 7548  O   LEU B 480     2165   1744   1990    -65    -63    125       O  
ATOM   7549  CB  LEU B 480     -37.183  -5.074 140.410  1.00 12.79           C  
ANISOU 7549  CB  LEU B 480     1727   1429   1702    -60     -4    165       C  
ATOM   7550  CG  LEU B 480     -38.403  -5.129 139.462  1.00 17.91           C  
ANISOU 7550  CG  LEU B 480     2346   2086   2374    -53     31    178       C  
ATOM   7551  CD1 LEU B 480     -37.982  -5.524 138.067  1.00 18.04           C  
ANISOU 7551  CD1 LEU B 480     2318   2113   2424    -63     18    183       C  
ATOM   7552  CD2 LEU B 480     -39.453  -6.094 139.972  1.00 20.83           C  
ANISOU 7552  CD2 LEU B 480     2719   2462   2734    -42     57    195       C  
ATOM   7553  N   ASP B 481     -35.886  -5.834 143.292  1.00 12.49           N  
ANISOU 7553  N   ASP B 481     1776   1379   1589    -57    -54    153       N  
ATOM   7554  CA  ASP B 481     -34.625  -6.027 143.998  1.00 12.12           C  
ANISOU 7554  CA  ASP B 481     1749   1327   1528    -65    -99    143       C  
ATOM   7555  C   ASP B 481     -33.490  -6.071 143.007  1.00 14.73           C  
ANISOU 7555  C   ASP B 481     2038   1661   1898    -82   -131    138       C  
ATOM   7556  O   ASP B 481     -33.644  -6.632 141.917  1.00 13.77           O  
ANISOU 7556  O   ASP B 481     1873   1551   1807    -85   -120    149       O  
ATOM   7557  CB  ASP B 481     -34.648  -7.336 144.817  1.00 13.91           C  
ANISOU 7557  CB  ASP B 481     1992   1561   1733    -59   -105    158       C  
ATOM   7558  CG  ASP B 481     -35.598  -7.322 145.994  1.00 21.46           C  
ANISOU 7558  CG  ASP B 481     2996   2514   2643    -42    -76    163       C  
ATOM   7559  OD1 ASP B 481     -36.049  -6.227 146.377  1.00 21.32           O  
ANISOU 7559  OD1 ASP B 481     3007   2487   2607    -34    -58    150       O  
ATOM   7560  OD2 ASP B 481     -35.808  -8.393 146.597  1.00 27.39           O  
ANISOU 7560  OD2 ASP B 481     3758   3271   3376    -37    -72    181       O  
ATOM   7561  N   VAL B 482     -32.349  -5.492 143.364  1.00 11.16           N  
ANISOU 7561  N   VAL B 482     1597   1198   1445    -93   -171    122       N  
ATOM   7562  CA  VAL B 482     -31.159  -5.587 142.532  1.00 10.17           C  
ANISOU 7562  CA  VAL B 482     1431   1077   1358   -109   -202    120       C  
ATOM   7563  C   VAL B 482     -30.588  -7.004 142.652  1.00 13.34           C  
ANISOU 7563  C   VAL B 482     1818   1489   1763   -109   -223    131       C  
ATOM   7564  O   VAL B 482     -30.629  -7.587 143.738  1.00 13.78           O  
ANISOU 7564  O   VAL B 482     1907   1541   1787   -101   -235    134       O  
ATOM   7565  CB  VAL B 482     -30.103  -4.498 142.915  1.00 13.90           C  
ANISOU 7565  CB  VAL B 482     1917   1531   1833   -122   -240    101       C  
ATOM   7566  CG1 VAL B 482     -28.793  -4.709 142.156  1.00 13.48           C  
ANISOU 7566  CG1 VAL B 482     1819   1483   1821   -139   -272    101       C  
ATOM   7567  CG2 VAL B 482     -30.651  -3.096 142.668  1.00 13.38           C  
ANISOU 7567  CG2 VAL B 482     1864   1452   1769   -123   -219     90       C  
ATOM   7568  N   ALA B 483     -30.158  -7.600 141.518  1.00  9.33           N  
ANISOU 7568  N   ALA B 483     1261    993   1292   -114   -225    139       N  
ATOM   7569  CA  ALA B 483     -29.608  -8.966 141.519  1.00  9.02           C  
ANISOU 7569  CA  ALA B 483     1204    963   1262   -112   -244    149       C  
ATOM   7570  C   ALA B 483     -28.424  -9.080 142.477  1.00 12.98           C  
ANISOU 7570  C   ALA B 483     1722   1455   1754   -118   -293    141       C  
ATOM   7571  O   ALA B 483     -27.618  -8.151 142.574  1.00 11.85           O  
ANISOU 7571  O   ALA B 483     1580   1303   1620   -129   -318    127       O  
ATOM   7572  CB  ALA B 483     -29.185  -9.363 140.114  1.00  9.20           C  
ANISOU 7572  CB  ALA B 483     1173    998   1326   -117   -240    153       C  
ATOM   7573  N   VAL B 484     -28.351 -10.200 143.236  1.00 11.00           N  
ANISOU 7573  N   VAL B 484     1488   1205   1486   -110   -308    150       N  
ATOM   7574  CA  VAL B 484     -27.269 -10.431 144.207  1.00 10.91           C  
ANISOU 7574  CA  VAL B 484     1496   1186   1464   -113   -358    145       C  
ATOM   7575  C   VAL B 484     -25.899 -10.349 143.521  1.00 14.88           C  
ANISOU 7575  C   VAL B 484     1954   1690   2009   -125   -392    139       C  
ATOM   7576  O   VAL B 484     -25.023  -9.615 143.979  1.00 14.52           O  
ANISOU 7576  O   VAL B 484     1916   1634   1966   -135   -427    126       O  
ATOM   7577  CB  VAL B 484     -27.456 -11.779 144.965  1.00 14.35           C  
ANISOU 7577  CB  VAL B 484     1952   1623   1878   -101   -366    162       C  
ATOM   7578  CG1 VAL B 484     -26.329 -12.003 145.971  1.00 14.11           C  
ANISOU 7578  CG1 VAL B 484     1942   1584   1835   -103   -421    157       C  
ATOM   7579  CG2 VAL B 484     -28.814 -11.828 145.657  1.00 14.22           C  
ANISOU 7579  CG2 VAL B 484     1978   1606   1820    -90   -328    171       C  
ATOM   7580  N   TYR B 485     -25.740 -11.051 142.393  1.00 12.01           N  
ANISOU 7580  N   TYR B 485     1542   1339   1681   -123   -379    146       N  
ATOM   7581  CA  TYR B 485     -24.514 -10.987 141.608  1.00 11.74           C  
ANISOU 7581  CA  TYR B 485     1460   1310   1690   -132   -401    142       C  
ATOM   7582  C   TYR B 485     -24.811 -10.656 140.153  1.00 14.76           C  
ANISOU 7582  C   TYR B 485     1803   1705   2101   -135   -364    143       C  
ATOM   7583  O   TYR B 485     -25.730 -11.229 139.561  1.00 14.39           O  
ANISOU 7583  O   TYR B 485     1750   1666   2051   -125   -331    151       O  
ATOM   7584  CB  TYR B 485     -23.717 -12.302 141.712  1.00 13.22           C  
ANISOU 7584  CB  TYR B 485     1629   1502   1894   -125   -430    149       C  
ATOM   7585  CG  TYR B 485     -22.515 -12.343 140.788  1.00 15.91           C  
ANISOU 7585  CG  TYR B 485     1914   1850   2282   -131   -445    146       C  
ATOM   7586  CD1 TYR B 485     -21.337 -11.672 141.113  1.00 18.73           C  
ANISOU 7586  CD1 TYR B 485     2259   2199   2658   -144   -484    138       C  
ATOM   7587  CD2 TYR B 485     -22.583 -12.980 139.551  1.00 16.55           C  
ANISOU 7587  CD2 TYR B 485     1954   1945   2390   -123   -419    151       C  
ATOM   7588  CE1 TYR B 485     -20.253 -11.645 140.234  1.00 20.19           C  
ANISOU 7588  CE1 TYR B 485     2389   2392   2890   -149   -492    138       C  
ATOM   7589  CE2 TYR B 485     -21.509 -12.952 138.662  1.00 17.77           C  
ANISOU 7589  CE2 TYR B 485     2058   2109   2587   -126   -426    149       C  
ATOM   7590  CZ  TYR B 485     -20.341 -12.288 139.010  1.00 25.61           C  
ANISOU 7590  CZ  TYR B 485     3037   3095   3600   -139   -461    144       C  
ATOM   7591  OH  TYR B 485     -19.269 -12.282 138.149  1.00 25.45           O  
ANISOU 7591  OH  TYR B 485     2963   3084   3623   -142   -465    145       O  
ATOM   7592  N   ARG B 486     -24.029  -9.738 139.571  1.00 10.42           N  
ANISOU 7592  N   ARG B 486     1226   1155   1580   -148   -372    137       N  
ATOM   7593  CA  ARG B 486     -24.143  -9.377 138.159  1.00  9.63           C  
ANISOU 7593  CA  ARG B 486     1087   1066   1506   -151   -339    140       C  
ATOM   7594  C   ARG B 486     -22.765  -9.403 137.504  1.00 14.20           C  
ANISOU 7594  C   ARG B 486     1618   1652   2127   -158   -359    140       C  
ATOM   7595  O   ARG B 486     -21.753  -9.212 138.190  1.00 14.13           O  
ANISOU 7595  O   ARG B 486     1608   1634   2129   -167   -398    135       O  
ATOM   7596  CB  ARG B 486     -24.780  -7.985 138.003  1.00  8.63           C  
ANISOU 7596  CB  ARG B 486      976    931   1370   -160   -318    135       C  
ATOM   7597  CG  ARG B 486     -26.234  -7.920 138.444  1.00 14.96           C  
ANISOU 7597  CG  ARG B 486     1819   1730   2136   -149   -289    137       C  
ATOM   7598  CD  ARG B 486     -26.638  -6.504 138.792  1.00 18.80           C  
ANISOU 7598  CD  ARG B 486     2332   2200   2609   -157   -282    128       C  
ATOM   7599  NE  ARG B 486     -25.936  -6.025 139.984  1.00 23.48           N  
ANISOU 7599  NE  ARG B 486     2955   2776   3189   -165   -322    116       N  
ATOM   7600  CZ  ARG B 486     -25.807  -4.743 140.302  1.00 31.36           C  
ANISOU 7600  CZ  ARG B 486     3973   3757   4186   -176   -331    105       C  
ATOM   7601  NH1 ARG B 486     -26.295  -3.803 139.503  1.00 16.56           N  
ANISOU 7601  NH1 ARG B 486     2089   1880   2324   -180   -303    106       N  
ATOM   7602  NH2 ARG B 486     -25.159  -4.388 141.403  1.00 15.49           N  
ANISOU 7602  NH2 ARG B 486     1992   1730   2163   -182   -372     92       N  
ATOM   7603  N   ASP B 487     -22.720  -9.641 136.172  1.00 11.80           N  
ANISOU 7603  N   ASP B 487     1274   1364   1846   -154   -331    145       N  
ATOM   7604  CA  ASP B 487     -21.463  -9.691 135.398  1.00 12.30           C  
ANISOU 7604  CA  ASP B 487     1287   1437   1949   -158   -339    148       C  
ATOM   7605  C   ASP B 487     -20.468  -8.609 135.886  1.00 16.56           C  
ANISOU 7605  C   ASP B 487     1820   1963   2508   -179   -369    144       C  
ATOM   7606  O   ASP B 487     -20.662  -7.423 135.610  1.00 16.43           O  
ANISOU 7606  O   ASP B 487     1807   1940   2495   -192   -356    144       O  
ATOM   7607  CB  ASP B 487     -21.765  -9.518 133.884  1.00 14.42           C  
ANISOU 7607  CB  ASP B 487     1526   1722   2231   -154   -297    154       C  
ATOM   7608  CG  ASP B 487     -20.571  -9.753 132.965  1.00 21.69           C  
ANISOU 7608  CG  ASP B 487     2394   2657   3190   -153   -296    158       C  
ATOM   7609  OD1 ASP B 487     -19.456  -9.988 133.485  1.00 21.93           O  
ANISOU 7609  OD1 ASP B 487     2406   2684   3243   -157   -329    157       O  
ATOM   7610  OD2 ASP B 487     -20.761  -9.729 131.729  1.00 22.84           O  
ANISOU 7610  OD2 ASP B 487     2517   2818   3342   -147   -262    163       O  
ATOM   7611  N   GLN B 488     -19.423  -9.026 136.653  1.00 12.89           N  
ANISOU 7611  N   GLN B 488     1347   1493   2059   -182   -413    142       N  
ATOM   7612  CA  GLN B 488     -18.458  -8.087 137.261  1.00 13.45           C  
ANISOU 7612  CA  GLN B 488     1413   1547   2149   -202   -451    137       C  
ATOM   7613  C   GLN B 488     -17.623  -7.317 136.215  1.00 17.95           C  
ANISOU 7613  C   GLN B 488     1932   2124   2765   -217   -439    144       C  
ATOM   7614  O   GLN B 488     -17.045  -6.270 136.536  1.00 17.54           O  
ANISOU 7614  O   GLN B 488     1877   2056   2732   -238   -462    142       O  
ATOM   7615  CB  GLN B 488     -17.546  -8.808 138.282  1.00 15.42           C  
ANISOU 7615  CB  GLN B 488     1664   1790   2406   -200   -504    134       C  
ATOM   7616  CG  GLN B 488     -16.757  -9.982 137.696  1.00 33.84           C  
ANISOU 7616  CG  GLN B 488     3950   4139   4770   -186   -507    141       C  
ATOM   7617  CD  GLN B 488     -15.870 -10.632 138.733  1.00 56.63           C  
ANISOU 7617  CD  GLN B 488     6838   7016   7664   -184   -562    138       C  
ATOM   7618  OE1 GLN B 488     -15.074  -9.971 139.410  1.00 52.58           O  
ANISOU 7618  OE1 GLN B 488     6323   6488   7166   -200   -604    134       O  
ATOM   7619  NE2 GLN B 488     -15.936 -11.950 138.826  1.00 50.20           N  
ANISOU 7619  NE2 GLN B 488     6024   6208   6842   -163   -565    142       N  
ATOM   7620  N   ALA B 489     -17.586  -7.816 134.963  1.00 14.46           N  
ANISOU 7620  N   ALA B 489     1451   1703   2339   -206   -402    153       N  
ATOM   7621  CA  ALA B 489     -16.903  -7.121 133.872  1.00 14.42           C  
ANISOU 7621  CA  ALA B 489     1399   1706   2372   -218   -380    164       C  
ATOM   7622  C   ALA B 489     -17.760  -5.958 133.364  1.00 17.63           C  
ANISOU 7622  C   ALA B 489     1824   2108   2765   -228   -348    167       C  
ATOM   7623  O   ALA B 489     -17.280  -5.122 132.598  1.00 17.63           O  
ANISOU 7623  O   ALA B 489     1794   2110   2794   -242   -332    177       O  
ATOM   7624  CB  ALA B 489     -16.615  -8.091 132.735  1.00 15.12           C  
ANISOU 7624  CB  ALA B 489     1446   1821   2477   -198   -351    171       C  
ATOM   7625  N   VAL B 490     -19.036  -5.910 133.789  1.00 13.44           N  
ANISOU 7625  N   VAL B 490     1343   1571   2193   -220   -337    160       N  
ATOM   7626  CA  VAL B 490     -19.981  -4.889 133.335  1.00 12.94           C  
ANISOU 7626  CA  VAL B 490     1300   1502   2114   -226   -306    163       C  
ATOM   7627  C   VAL B 490     -20.555  -4.090 134.532  1.00 15.69           C  
ANISOU 7627  C   VAL B 490     1700   1825   2437   -235   -327    151       C  
ATOM   7628  O   VAL B 490     -20.822  -2.895 134.402  1.00 14.88           O  
ANISOU 7628  O   VAL B 490     1609   1709   2337   -248   -319    151       O  
ATOM   7629  CB  VAL B 490     -21.125  -5.524 132.469  1.00 16.21           C  
ANISOU 7629  CB  VAL B 490     1721   1935   2504   -205   -263    166       C  
ATOM   7630  CG1 VAL B 490     -22.073  -4.451 131.938  1.00 15.51           C  
ANISOU 7630  CG1 VAL B 490     1650   1841   2403   -210   -233    171       C  
ATOM   7631  CG2 VAL B 490     -20.551  -6.353 131.320  1.00 15.95           C  
ANISOU 7631  CG2 VAL B 490     1642   1926   2491   -193   -244    175       C  
ATOM   7632  N   TYR B 491     -20.731  -4.755 135.693  1.00 12.14           N  
ANISOU 7632  N   TYR B 491     1283   1368   1961   -227   -355    140       N  
ATOM   7633  CA  TYR B 491     -21.412  -4.148 136.842  1.00 12.20           C  
ANISOU 7633  CA  TYR B 491     1346   1355   1936   -229   -370    128       C  
ATOM   7634  C   TYR B 491     -20.539  -4.062 138.084  1.00 17.43           C  
ANISOU 7634  C   TYR B 491     2024   1999   2599   -239   -424    117       C  
ATOM   7635  O   TYR B 491     -19.723  -4.949 138.335  1.00 17.63           O  
ANISOU 7635  O   TYR B 491     2029   2031   2637   -236   -451    118       O  
ATOM   7636  CB  TYR B 491     -22.713  -4.913 137.165  1.00 12.11           C  
ANISOU 7636  CB  TYR B 491     1369   1350   1881   -208   -346    127       C  
ATOM   7637  CG  TYR B 491     -23.745  -4.840 136.065  1.00 12.42           C  
ANISOU 7637  CG  TYR B 491     1401   1402   1917   -199   -297    135       C  
ATOM   7638  CD1 TYR B 491     -24.672  -3.804 136.018  1.00 13.69           C  
ANISOU 7638  CD1 TYR B 491     1587   1552   2062   -200   -275    133       C  
ATOM   7639  CD2 TYR B 491     -23.817  -5.825 135.085  1.00 13.05           C  
ANISOU 7639  CD2 TYR B 491     1449   1504   2006   -187   -275    144       C  
ATOM   7640  CE1 TYR B 491     -25.632  -3.737 135.010  1.00 12.11           C  
ANISOU 7640  CE1 TYR B 491     1378   1363   1859   -191   -233    142       C  
ATOM   7641  CE2 TYR B 491     -24.773  -5.769 134.071  1.00 13.48           C  
ANISOU 7641  CE2 TYR B 491     1497   1569   2054   -178   -235    151       C  
ATOM   7642  CZ  TYR B 491     -25.671  -4.715 134.030  1.00 16.53           C  
ANISOU 7642  CZ  TYR B 491     1908   1946   2429   -181   -215    151       C  
ATOM   7643  OH  TYR B 491     -26.609  -4.654 133.034  1.00 15.22           O  
ANISOU 7643  OH  TYR B 491     1735   1790   2258   -172   -179    159       O  
ATOM   7644  N   ASN B 492     -20.783  -3.033 138.915  1.00 14.61           N  
ANISOU 7644  N   ASN B 492     1708   1618   2225   -248   -442    104       N  
ATOM   7645  CA  ASN B 492     -20.176  -2.904 140.233  1.00 14.80           C  
ANISOU 7645  CA  ASN B 492     1762   1622   2238   -255   -495     90       C  
ATOM   7646  C   ASN B 492     -21.136  -3.503 141.269  1.00 17.42           C  
ANISOU 7646  C   ASN B 492     2150   1953   2513   -235   -493     82       C  
ATOM   7647  O   ASN B 492     -22.200  -2.935 141.523  1.00 17.16           O  
ANISOU 7647  O   ASN B 492     2158   1913   2449   -228   -468     76       O  
ATOM   7648  CB  ASN B 492     -19.889  -1.409 140.553  1.00 16.61           C  
ANISOU 7648  CB  ASN B 492     2008   1824   2480   -276   -517     78       C  
ATOM   7649  CG  ASN B 492     -19.284  -1.165 141.926  1.00 40.24           C  
ANISOU 7649  CG  ASN B 492     5036   4793   5458   -283   -577     60       C  
ATOM   7650  OD1 ASN B 492     -18.937  -2.099 142.666  1.00 37.00           O  
ANISOU 7650  OD1 ASN B 492     4637   4389   5032   -274   -607     58       O  
ATOM   7651  ND2 ASN B 492     -19.135   0.102 142.288  1.00 31.29           N  
ANISOU 7651  ND2 ASN B 492     3925   3632   4331   -300   -598     46       N  
ATOM   7652  N   ASN B 493     -20.792  -4.690 141.809  1.00 13.04           N  
ANISOU 7652  N   ASN B 493     1598   1409   1949   -224   -516     85       N  
ATOM   7653  CA  ASN B 493     -21.674  -5.437 142.711  1.00 13.19           C  
ANISOU 7653  CA  ASN B 493     1666   1430   1917   -205   -510     84       C  
ATOM   7654  C   ASN B 493     -21.959  -4.710 144.042  1.00 18.62           C  
ANISOU 7654  C   ASN B 493     2417   2095   2562   -205   -535     67       C  
ATOM   7655  O   ASN B 493     -22.956  -5.007 144.694  1.00 19.10           O  
ANISOU 7655  O   ASN B 493     2524   2157   2577   -189   -515     67       O  
ATOM   7656  CB  ASN B 493     -21.129  -6.850 142.960  1.00 13.95           C  
ANISOU 7656  CB  ASN B 493     1746   1537   2016   -195   -532     94       C  
ATOM   7657  CG  ASN B 493     -21.280  -7.764 141.765  1.00 35.06           C  
ANISOU 7657  CG  ASN B 493     4373   4233   4715   -186   -497    109       C  
ATOM   7658  OD1 ASN B 493     -22.389  -8.167 141.396  1.00 21.39           O  
ANISOU 7658  OD1 ASN B 493     2652   2511   2964   -173   -455    115       O  
ATOM   7659  ND2 ASN B 493     -20.168  -8.123 141.146  1.00 33.41           N  
ANISOU 7659  ND2 ASN B 493     4113   4032   4550   -192   -513    113       N  
ATOM   7660  N   ASN B 494     -21.107  -3.735 144.420  1.00 15.53           N  
ANISOU 7660  N   ASN B 494     2030   1684   2188   -223   -577     53       N  
ATOM   7661  CA  ASN B 494     -21.330  -2.944 145.640  1.00 15.73           C  
ANISOU 7661  CA  ASN B 494     2118   1685   2172   -223   -603     33       C  
ATOM   7662  C   ASN B 494     -22.480  -1.941 145.450  1.00 19.23           C  
ANISOU 7662  C   ASN B 494     2591   2120   2596   -218   -559     26       C  
ATOM   7663  O   ASN B 494     -23.077  -1.495 146.431  1.00 18.52           O  
ANISOU 7663  O   ASN B 494     2561   2015   2460   -208   -562     10       O  
ATOM   7664  CB  ASN B 494     -20.044  -2.217 146.060  1.00 17.62           C  
ANISOU 7664  CB  ASN B 494     2351   1903   2441   -245   -666     19       C  
ATOM   7665  CG  ASN B 494     -18.930  -3.151 146.499  1.00 42.25           C  
ANISOU 7665  CG  ASN B 494     5452   5028   5575   -247   -718     24       C  
ATOM   7666  OD1 ASN B 494     -19.151  -4.338 146.790  1.00 38.38           O  
ANISOU 7666  OD1 ASN B 494     4969   4553   5061   -229   -713     35       O  
ATOM   7667  ND2 ASN B 494     -17.722  -2.620 146.610  1.00 31.86           N  
ANISOU 7667  ND2 ASN B 494     4111   3695   4298   -268   -770     17       N  
ATOM   7668  N   ASP B 495     -22.813  -1.623 144.184  1.00 16.03           N  
ANISOU 7668  N   ASP B 495     2145   1724   2224   -223   -517     37       N  
ATOM   7669  CA  ASP B 495     -23.897  -0.695 143.862  1.00 15.66           C  
ANISOU 7669  CA  ASP B 495     2118   1669   2164   -218   -475     33       C  
ATOM   7670  C   ASP B 495     -25.238  -1.454 143.735  1.00 18.59           C  
ANISOU 7670  C   ASP B 495     2502   2060   2503   -194   -423     44       C  
ATOM   7671  O   ASP B 495     -25.504  -2.075 142.701  1.00 17.29           O  
ANISOU 7671  O   ASP B 495     2295   1915   2358   -191   -391     61       O  
ATOM   7672  CB  ASP B 495     -23.572   0.074 142.556  1.00 17.57           C  
ANISOU 7672  CB  ASP B 495     2309   1909   2457   -236   -458     41       C  
ATOM   7673  CG  ASP B 495     -24.555   1.188 142.209  1.00 28.64           C  
ANISOU 7673  CG  ASP B 495     3730   3298   3853   -233   -422     37       C  
ATOM   7674  OD1 ASP B 495     -25.511   1.410 142.996  1.00 29.93           O  
ANISOU 7674  OD1 ASP B 495     3946   3454   3973   -216   -408     25       O  
ATOM   7675  OD2 ASP B 495     -24.351   1.854 141.173  1.00 32.42           O  
ANISOU 7675  OD2 ASP B 495     4173   3775   4370   -246   -408     45       O  
ATOM   7676  N   LYS B 496     -26.056  -1.438 144.807  1.00 14.56           N  
ANISOU 7676  N   LYS B 496     2049   1541   1940   -178   -415     35       N  
ATOM   7677  CA  LYS B 496     -27.358  -2.119 144.800  1.00 13.60           C  
ANISOU 7677  CA  LYS B 496     1942   1437   1790   -156   -366     47       C  
ATOM   7678  C   LYS B 496     -28.512  -1.126 145.038  1.00 15.86           C  
ANISOU 7678  C   LYS B 496     2265   1710   2050   -144   -330     37       C  
ATOM   7679  O   LYS B 496     -29.571  -1.515 145.550  1.00 15.14           O  
ANISOU 7679  O   LYS B 496     2205   1626   1923   -124   -298     42       O  
ATOM   7680  CB  LYS B 496     -27.395  -3.260 145.845  1.00 16.67           C  
ANISOU 7680  CB  LYS B 496     2361   1834   2140   -143   -380     52       C  
ATOM   7681  CG  LYS B 496     -26.421  -4.400 145.553  1.00 30.48           C  
ANISOU 7681  CG  LYS B 496     4071   3596   3914   -150   -409     64       C  
ATOM   7682  CD  LYS B 496     -26.739  -5.638 146.407  1.00 41.59           C  
ANISOU 7682  CD  LYS B 496     5505   5013   5285   -134   -410     76       C  
ATOM   7683  CE  LYS B 496     -25.500  -6.278 147.025  1.00 52.24           C  
ANISOU 7683  CE  LYS B 496     6854   6360   6637   -140   -468     75       C  
ATOM   7684  NZ  LYS B 496     -24.545  -6.757 145.993  1.00 57.80           N  
ANISOU 7684  NZ  LYS B 496     7493   7074   7396   -152   -483     83       N  
ATOM   7685  N   ASP B 497     -28.325   0.150 144.624  1.00 11.33           N  
ANISOU 7685  N   ASP B 497     1688   1118   1500   -156   -334     25       N  
ATOM   7686  CA  ASP B 497     -29.361   1.174 144.760  1.00 10.48           C  
ANISOU 7686  CA  ASP B 497     1612    996   1374   -144   -302     15       C  
ATOM   7687  C   ASP B 497     -30.533   0.875 143.815  1.00 12.94           C  
ANISOU 7687  C   ASP B 497     1896   1325   1695   -131   -245     34       C  
ATOM   7688  O   ASP B 497     -30.359   0.867 142.594  1.00 12.30           O  
ANISOU 7688  O   ASP B 497     1766   1254   1654   -142   -234     48       O  
ATOM   7689  CB  ASP B 497     -28.776   2.580 144.479  1.00 12.31           C  
ANISOU 7689  CB  ASP B 497     1842   1200   1634   -161   -325      0       C  
ATOM   7690  CG  ASP B 497     -29.678   3.734 144.912  1.00 19.34           C  
ANISOU 7690  CG  ASP B 497     2778   2067   2502   -147   -304    -18       C  
ATOM   7691  OD1 ASP B 497     -30.905   3.513 145.052  1.00 18.66           O  
ANISOU 7691  OD1 ASP B 497     2710   1991   2389   -124   -258    -12       O  
ATOM   7692  OD2 ASP B 497     -29.162   4.855 145.084  1.00 26.24           O  
ANISOU 7692  OD2 ASP B 497     3668   2913   3390   -160   -332    -36       O  
ATOM   7693  N   ILE B 498     -31.722   0.606 144.385  1.00  9.24           N  
ANISOU 7693  N   ILE B 498     1459    862   1189   -109   -209     37       N  
ATOM   7694  CA  ILE B 498     -32.930   0.269 143.604  1.00  8.45           C  
ANISOU 7694  CA  ILE B 498     1335    779   1098    -96   -157     55       C  
ATOM   7695  C   ILE B 498     -33.416   1.458 142.762  1.00 13.04           C  
ANISOU 7695  C   ILE B 498     1902   1347   1704    -97   -135     52       C  
ATOM   7696  O   ILE B 498     -34.155   1.265 141.791  1.00 13.04           O  
ANISOU 7696  O   ILE B 498     1869   1361   1724    -92   -101     69       O  
ATOM   7697  CB  ILE B 498     -34.060  -0.276 144.532  1.00 10.93           C  
ANISOU 7697  CB  ILE B 498     1685   1099   1367    -72   -123     60       C  
ATOM   7698  CG1 ILE B 498     -34.446   0.773 145.617  1.00 11.52           C  
ANISOU 7698  CG1 ILE B 498     1820   1152   1404    -57   -120     37       C  
ATOM   7699  CG2 ILE B 498     -33.644  -1.617 145.167  1.00 10.46           C  
ANISOU 7699  CG2 ILE B 498     1631   1054   1287    -71   -142     70       C  
ATOM   7700  CD1 ILE B 498     -35.800   0.542 146.263  1.00 21.54           C  
ANISOU 7700  CD1 ILE B 498     3118   2428   2638    -30    -71     43       C  
ATOM   7701  N   LEU B 499     -33.003   2.682 143.131  1.00  9.90           N  
ANISOU 7701  N   LEU B 499     1531    923   1306   -103   -156     32       N  
ATOM   7702  CA  LEU B 499     -33.428   3.895 142.434  1.00  9.58           C  
ANISOU 7702  CA  LEU B 499     1484    866   1289   -103   -138     29       C  
ATOM   7703  C   LEU B 499     -32.556   4.175 141.198  1.00 14.28           C  
ANISOU 7703  C   LEU B 499     2029   1462   1933   -128   -155     40       C  
ATOM   7704  O   LEU B 499     -32.866   5.078 140.418  1.00 13.86           O  
ANISOU 7704  O   LEU B 499     1963   1398   1905   -130   -140     43       O  
ATOM   7705  CB  LEU B 499     -33.408   5.104 143.397  1.00 10.00           C  
ANISOU 7705  CB  LEU B 499     1592    887   1322    -98   -153      1       C  
ATOM   7706  CG  LEU B 499     -34.180   4.916 144.725  1.00 14.68           C  
ANISOU 7706  CG  LEU B 499     2241   1478   1860    -71   -137    -12       C  
ATOM   7707  CD1 LEU B 499     -34.078   6.148 145.587  1.00 15.37           C  
ANISOU 7707  CD1 LEU B 499     2382   1530   1926    -66   -156    -42       C  
ATOM   7708  CD2 LEU B 499     -35.640   4.571 144.470  1.00 17.42           C  
ANISOU 7708  CD2 LEU B 499     2581   1841   2198    -47    -79      4       C  
ATOM   7709  N   LYS B 500     -31.468   3.400 141.021  1.00 11.51           N  
ANISOU 7709  N   LYS B 500     1651   1124   1597   -145   -185     46       N  
ATOM   7710  CA  LYS B 500     -30.599   3.537 139.850  1.00 11.29           C  
ANISOU 7710  CA  LYS B 500     1574   1102   1615   -166   -197     59       C  
ATOM   7711  C   LYS B 500     -30.999   2.536 138.772  1.00 14.90           C  
ANISOU 7711  C   LYS B 500     1986   1589   2084   -161   -167     81       C  
ATOM   7712  O   LYS B 500     -30.840   1.329 138.960  1.00 14.27           O  
ANISOU 7712  O   LYS B 500     1898   1529   1995   -157   -172     87       O  
ATOM   7713  CB  LYS B 500     -29.116   3.355 140.239  1.00 14.21           C  
ANISOU 7713  CB  LYS B 500     1935   1466   1998   -187   -247     52       C  
ATOM   7714  CG  LYS B 500     -28.592   4.443 141.175  1.00 23.36           C  
ANISOU 7714  CG  LYS B 500     3133   2590   3151   -196   -284     28       C  
ATOM   7715  CD  LYS B 500     -27.093   4.281 141.473  1.00 35.86           C  
ANISOU 7715  CD  LYS B 500     4701   4168   4755   -219   -337     23       C  
ATOM   7716  CE  LYS B 500     -26.224   4.627 140.281  1.00 46.18           C  
ANISOU 7716  CE  LYS B 500     5952   5477   6117   -243   -342     39       C  
ATOM   7717  NZ  LYS B 500     -24.778   4.527 140.609  1.00 53.09           N  
ANISOU 7717  NZ  LYS B 500     6809   6344   7017   -265   -394     34       N  
ATOM   7718  N   SER B 501     -31.559   3.036 137.650  1.00 11.35           N  
ANISOU 7718  N   SER B 501     1513   1143   1656   -160   -139     94       N  
ATOM   7719  CA  SER B 501     -32.015   2.186 136.543  1.00 10.66           C  
ANISOU 7719  CA  SER B 501     1387   1082   1579   -154   -112    114       C  
ATOM   7720  C   SER B 501     -30.837   1.449 135.870  1.00 13.92           C  
ANISOU 7720  C   SER B 501     1760   1513   2016   -169   -131    123       C  
ATOM   7721  O   SER B 501     -31.040   0.401 135.248  1.00 12.89           O  
ANISOU 7721  O   SER B 501     1603   1406   1887   -162   -118    134       O  
ATOM   7722  CB  SER B 501     -32.774   3.019 135.511  1.00 13.35           C  
ANISOU 7722  CB  SER B 501     1716   1420   1937   -150    -83    125       C  
ATOM   7723  OG  SER B 501     -33.394   2.198 134.537  1.00 17.02           O  
ANISOU 7723  OG  SER B 501     2150   1909   2406   -141    -59    141       O  
ATOM   7724  N   ALA B 502     -29.596   1.967 136.051  1.00 10.47           N  
ANISOU 7724  N   ALA B 502     1317   1063   1599   -188   -164    117       N  
ATOM   7725  CA  ALA B 502     -28.386   1.354 135.482  1.00 10.07           C  
ANISOU 7725  CA  ALA B 502     1225   1027   1574   -202   -183    125       C  
ATOM   7726  C   ALA B 502     -27.989   0.050 136.223  1.00 12.41           C  
ANISOU 7726  C   ALA B 502     1524   1337   1854   -196   -203    121       C  
ATOM   7727  O   ALA B 502     -27.118  -0.684 135.751  1.00 12.65           O  
ANISOU 7727  O   ALA B 502     1519   1382   1904   -202   -214    128       O  
ATOM   7728  CB  ALA B 502     -27.231   2.348 135.509  1.00 11.09           C  
ANISOU 7728  CB  ALA B 502     1345   1136   1732   -226   -212    122       C  
ATOM   7729  N   ASN B 503     -28.657  -0.251 137.359  1.00  7.88           N  
ANISOU 7729  N   ASN B 503      992    757   1245   -183   -205    110       N  
ATOM   7730  CA  ASN B 503     -28.415  -1.501 138.094  1.00  7.87           C  
ANISOU 7730  CA  ASN B 503      998    767   1226   -176   -222    109       C  
ATOM   7731  C   ASN B 503     -29.214  -2.665 137.491  1.00 10.92           C  
ANISOU 7731  C   ASN B 503     1366   1176   1607   -161   -192    122       C  
ATOM   7732  O   ASN B 503     -29.007  -3.819 137.869  1.00 10.45           O  
ANISOU 7732  O   ASN B 503     1305   1127   1539   -155   -204    125       O  
ATOM   7733  CB  ASN B 503     -28.741  -1.333 139.582  1.00  8.56           C  
ANISOU 7733  CB  ASN B 503     1139    837   1275   -168   -237     94       C  
ATOM   7734  CG  ASN B 503     -27.665  -0.604 140.354  1.00 24.48           C  
ANISOU 7734  CG  ASN B 503     3174   2833   3296   -184   -282     78       C  
ATOM   7735  OD1 ASN B 503     -26.467  -0.806 140.137  1.00 19.38           O  
ANISOU 7735  OD1 ASN B 503     2497   2188   2677   -199   -313     80       O  
ATOM   7736  ND2 ASN B 503     -28.070   0.191 141.327  1.00 15.77           N  
ANISOU 7736  ND2 ASN B 503     2120   1709   2164   -179   -288     62       N  
ATOM   7737  N   PHE B 504     -30.066  -2.367 136.506  1.00  7.07           N  
ANISOU 7737  N   PHE B 504      864    695   1127   -155   -158    131       N  
ATOM   7738  CA  PHE B 504     -30.886  -3.371 135.843  1.00  5.70           C  
ANISOU 7738  CA  PHE B 504      672    541    951   -142   -132    143       C  
ATOM   7739  C   PHE B 504     -30.538  -3.453 134.359  1.00  9.21           C  
ANISOU 7739  C   PHE B 504     1074   1001   1425   -146   -122    153       C  
ATOM   7740  O   PHE B 504     -30.240  -2.428 133.738  1.00  8.54           O  
ANISOU 7740  O   PHE B 504      979    910   1357   -156   -118    155       O  
ATOM   7741  CB  PHE B 504     -32.379  -3.060 136.045  1.00  7.18           C  
ANISOU 7741  CB  PHE B 504      884    724   1120   -128   -100    146       C  
ATOM   7742  CG  PHE B 504     -32.794  -3.040 137.500  1.00  8.19           C  
ANISOU 7742  CG  PHE B 504     1057    840   1216   -120   -103    137       C  
ATOM   7743  CD1 PHE B 504     -33.172  -4.213 138.152  1.00 11.24           C  
ANISOU 7743  CD1 PHE B 504     1454   1234   1583   -110   -101    142       C  
ATOM   7744  CD2 PHE B 504     -32.728  -1.865 138.243  1.00  9.79           C  
ANISOU 7744  CD2 PHE B 504     1293   1022   1406   -123   -110    123       C  
ATOM   7745  CE1 PHE B 504     -33.502  -4.203 139.512  1.00 12.33           C  
ANISOU 7745  CE1 PHE B 504     1636   1362   1687   -102   -103    136       C  
ATOM   7746  CE2 PHE B 504     -33.057  -1.859 139.605  1.00 12.53           C  
ANISOU 7746  CE2 PHE B 504     1685   1357   1717   -113   -114    114       C  
ATOM   7747  CZ  PHE B 504     -33.440  -3.027 140.229  1.00 10.46           C  
ANISOU 7747  CZ  PHE B 504     1434   1107   1435   -103   -108    121       C  
ATOM   7748  N   ILE B 505     -30.481  -4.692 133.807  1.00  6.44           N  
ANISOU 7748  N   ILE B 505      699    668   1079   -139   -119    160       N  
ATOM   7749  CA  ILE B 505     -30.058  -4.928 132.416  1.00  6.35           C  
ANISOU 7749  CA  ILE B 505      648    673   1090   -140   -111    168       C  
ATOM   7750  C   ILE B 505     -30.799  -4.012 131.416  1.00 10.83           C  
ANISOU 7750  C   ILE B 505     1210   1241   1662   -139    -83    175       C  
ATOM   7751  O   ILE B 505     -32.008  -3.812 131.538  1.00 11.04           O  
ANISOU 7751  O   ILE B 505     1255   1264   1676   -130    -65    177       O  
ATOM   7752  CB  ILE B 505     -30.163  -6.440 132.042  1.00  8.89           C  
ANISOU 7752  CB  ILE B 505      954   1012   1412   -129   -110    170       C  
ATOM   7753  CG1 ILE B 505     -29.473  -6.737 130.682  1.00  8.65           C  
ANISOU 7753  CG1 ILE B 505      886   1000   1403   -128   -105    175       C  
ATOM   7754  CG2 ILE B 505     -31.609  -6.911 132.060  1.00 10.38           C  
ANISOU 7754  CG2 ILE B 505     1157   1202   1586   -116    -89    175       C  
ATOM   7755  CD1 ILE B 505     -29.294  -8.249 130.370  1.00 15.19           C  
ANISOU 7755  CD1 ILE B 505     1697   1840   2233   -116   -111    174       C  
ATOM   7756  N   LYS B 506     -30.049  -3.398 130.489  1.00  8.86           N  
ANISOU 7756  N   LYS B 506      936    997   1433   -148    -81    181       N  
ATOM   7757  CA  LYS B 506     -30.609  -2.431 129.533  1.00  8.74           C  
ANISOU 7757  CA  LYS B 506      917    981   1423   -148    -59    190       C  
ATOM   7758  C   LYS B 506     -30.959  -3.093 128.206  1.00 12.75           C  
ANISOU 7758  C   LYS B 506     1402   1511   1933   -137    -41    199       C  
ATOM   7759  O   LYS B 506     -31.881  -2.649 127.526  1.00 12.66           O  
ANISOU 7759  O   LYS B 506     1393   1501   1917   -130    -22    207       O  
ATOM   7760  CB  LYS B 506     -29.618  -1.263 129.297  1.00 10.87           C  
ANISOU 7760  CB  LYS B 506     1177   1241   1714   -166    -65    195       C  
ATOM   7761  CG  LYS B 506     -29.212  -0.501 130.577  1.00 18.12           C  
ANISOU 7761  CG  LYS B 506     2119   2133   2631   -179    -89    183       C  
ATOM   7762  CD  LYS B 506     -30.169   0.656 130.909  1.00 24.82           C  
ANISOU 7762  CD  LYS B 506     2999   2960   3471   -177    -77    181       C  
ATOM   7763  CE  LYS B 506     -31.279   0.244 131.849  1.00 30.93           C  
ANISOU 7763  CE  LYS B 506     3805   3730   4219   -162    -72    171       C  
ATOM   7764  NZ  LYS B 506     -32.191   1.378 132.145  1.00 36.00           N  
ANISOU 7764  NZ  LYS B 506     4474   4351   4853   -157    -58    169       N  
ATOM   7765  N   ARG B 507     -30.179  -4.109 127.798  1.00  8.86           N  
ANISOU 7765  N   ARG B 507      885   1034   1446   -134    -48    198       N  
ATOM   7766  CA  ARG B 507     -30.386  -4.768 126.504  1.00  8.66           C  
ANISOU 7766  CA  ARG B 507      840   1030   1420   -122    -33    204       C  
ATOM   7767  C   ARG B 507     -29.692  -6.123 126.446  1.00 11.58           C  
ANISOU 7767  C   ARG B 507     1193   1414   1794   -115    -45    197       C  
ATOM   7768  O   ARG B 507     -28.825  -6.417 127.275  1.00 12.12           O  
ANISOU 7768  O   ARG B 507     1258   1476   1869   -121    -65    191       O  
ATOM   7769  CB  ARG B 507     -29.874  -3.859 125.339  1.00  8.87           C  
ANISOU 7769  CB  ARG B 507      849   1065   1457   -128    -18    216       C  
ATOM   7770  CG  ARG B 507     -28.370  -3.526 125.437  1.00 15.20           C  
ANISOU 7770  CG  ARG B 507     1630   1867   2280   -143    -28    219       C  
ATOM   7771  CD  ARG B 507     -27.875  -2.696 124.252  1.00 17.87           C  
ANISOU 7771  CD  ARG B 507     1948   2213   2629   -148     -8    235       C  
ATOM   7772  NE  ARG B 507     -27.901  -3.454 122.994  1.00 19.04           N  
ANISOU 7772  NE  ARG B 507     2080   2387   2769   -132      9    239       N  
ATOM   7773  CZ  ARG B 507     -26.898  -4.219 122.569  1.00 25.33           C  
ANISOU 7773  CZ  ARG B 507     2851   3201   3574   -127     10    238       C  
ATOM   7774  NH1 ARG B 507     -25.797  -4.346 123.298  1.00 13.59           N  
ANISOU 7774  NH1 ARG B 507     1348   1708   2106   -138     -7    234       N  
ATOM   7775  NH2 ARG B 507     -26.991  -4.863 121.415  1.00 10.69           N  
ANISOU 7775  NH2 ARG B 507      986   1368   1707   -109     26    240       N  
HETATM 7776  N   MSE B 508     -30.027  -6.923 125.429  1.00  6.21           N  
ANISOU 7776  N   MSE B 508      511    747   1103    -94    -36    197       N  
HETATM 7777  CA  MSE B 508     -29.301  -8.146 125.116  1.00  4.95           C  
ANISOU 7777  CA  MSE B 508      474    549    860    -21    -46    178       C  
HETATM 7778  C   MSE B 508     -28.233  -7.836 124.062  1.00  8.69           C  
ANISOU 7778  C   MSE B 508      771   1094   1439    -91    -32    196       C  
HETATM 7779  O   MSE B 508     -28.450  -6.977 123.200  1.00  8.29           O  
ANISOU 7779  O   MSE B 508      717   1048   1384    -92    -13    206       O  
HETATM 7780  CB  MSE B 508     -30.262  -9.227 124.602  1.00  5.59           C  
ANISOU 7780  CB  MSE B 508      511    644    967    -34    -42    184       C  
HETATM 7781  CG  MSE B 508     -31.140  -9.826 125.699  1.00 10.13           C  
ANISOU 7781  CG  MSE B 508     1005   1252   1594    -73    -53    181       C  
HETATM 7782 SE   MSE B 508     -32.703 -10.802 125.007  0.75 15.18          SE  
ANISOU 7782 SE   MSE B 508     1650   1893   2225    -58    -48    179      SE  
HETATM 7783  CE  MSE B 508     -31.801 -11.989 123.744  1.00 11.61           C  
ANISOU 7783  CE  MSE B 508     1174   1459   1777    -42    -53    168       C  
ATOM   7784  N   ARG B 509     -27.064  -8.485 124.157  1.00  6.10           N  
ANISOU 7784  N   ARG B 509      484    744   1091    -65    -42    191       N  
ATOM   7785  CA  ARG B 509     -25.971  -8.230 123.213  1.00  6.47           C  
ANISOU 7785  CA  ARG B 509      446    832   1181    -86    -28    198       C  
ATOM   7786  C   ARG B 509     -26.300  -8.764 121.842  1.00 11.05           C  
ANISOU 7786  C   ARG B 509     1012   1435   1749    -68     -7    197       C  
ATOM   7787  O   ARG B 509     -27.026  -9.752 121.726  1.00 11.14           O  
ANISOU 7787  O   ARG B 509     1036   1448   1748    -53    -13    186       O  
ATOM   7788  CB  ARG B 509     -24.663  -8.858 123.705  1.00  7.31           C  
ANISOU 7788  CB  ARG B 509      521    944   1312    -89    -44    193       C  
ATOM   7789  CG  ARG B 509     -24.085  -8.209 124.949  1.00 19.28           C  
ANISOU 7789  CG  ARG B 509     2039   2441   2845   -110    -67    195       C  
ATOM   7790  CD  ARG B 509     -22.610  -8.581 125.144  1.00 32.81           C  
ANISOU 7790  CD  ARG B 509     3719   4160   4586   -112    -80    194       C  
ATOM   7791  NE  ARG B 509     -22.391 -10.035 125.114  1.00 46.94           N  
ANISOU 7791  NE  ARG B 509     5500   5958   6376    -91    -89    183       N  
ATOM   7792  CZ  ARG B 509     -21.946 -10.697 124.045  1.00 64.01           C  
ANISOU 7792  CZ  ARG B 509     7639   8140   8541    -73    -71    181       C  
ATOM   7793  NH1 ARG B 509     -21.662 -10.045 122.922  1.00 54.86           N  
ANISOU 7793  NH1 ARG B 509     6463   6997   7384    -72    -41    192       N  
ATOM   7794  NH2 ARG B 509     -21.779 -12.012 124.094  1.00 48.89           N  
ANISOU 7794  NH2 ARG B 509     5720   6229   6628    -53    -82    169       N  
ATOM   7795  N   TYR B 510     -25.708  -8.160 120.788  1.00  7.26           N  
ANISOU 7795  N   TYR B 510      515    971   1272    -68     16    209       N  
ATOM   7796  CA  TYR B 510     -25.818  -8.692 119.436  1.00  7.06           C  
ANISOU 7796  CA  TYR B 510      484    967   1230    -46     36    208       C  
ATOM   7797  C   TYR B 510     -25.102 -10.045 119.367  1.00 11.57           C  
ANISOU 7797  C   TYR B 510     1040   1548   1807    -28     29    192       C  
ATOM   7798  O   TYR B 510     -24.126 -10.257 120.089  1.00 10.55           O  
ANISOU 7798  O   TYR B 510      893   1415   1702    -35     17    190       O  
ATOM   7799  CB  TYR B 510     -25.161  -7.733 118.416  1.00  8.34           C  
ANISOU 7799  CB  TYR B 510      630   1144   1394    -50     65    227       C  
ATOM   7800  CG  TYR B 510     -25.787  -6.361 118.334  1.00  9.65           C  
ANISOU 7800  CG  TYR B 510      811   1300   1556    -66     74    244       C  
ATOM   7801  CD1 TYR B 510     -27.148  -6.210 118.072  1.00 11.25           C  
ANISOU 7801  CD1 TYR B 510     1040   1498   1736    -60     73    243       C  
ATOM   7802  CD2 TYR B 510     -24.994  -5.216 118.301  1.00 10.64           C  
ANISOU 7802  CD2 TYR B 510      920   1423   1701    -85     86    264       C  
ATOM   7803  CE1 TYR B 510     -27.716  -4.951 117.895  1.00 11.21           C  
ANISOU 7803  CE1 TYR B 510     1048   1483   1728    -72     82    260       C  
ATOM   7804  CE2 TYR B 510     -25.547  -3.956 118.089  1.00 11.76           C  
ANISOU 7804  CE2 TYR B 510     1075   1554   1839    -98     96    281       C  
ATOM   7805  CZ  TYR B 510     -26.911  -3.826 117.906  1.00 16.75           C  
ANISOU 7805  CZ  TYR B 510     1736   2180   2448    -90     93    279       C  
ATOM   7806  OH  TYR B 510     -27.458  -2.583 117.723  1.00 15.97           O  
ANISOU 7806  OH  TYR B 510     1650   2069   2348   -101    101    296       O  
ATOM   7807  N   PRO B 511     -25.472 -10.931 118.411  1.00  9.66           N  
ANISOU 7807  N   PRO B 511      804   1320   1547     -4     36    181       N  
ATOM   7808  CA  PRO B 511     -24.660 -12.140 118.198  1.00 10.28           C  
ANISOU 7808  CA  PRO B 511      866   1409   1633     16     33    166       C  
ATOM   7809  C   PRO B 511     -23.248 -11.758 117.745  1.00 15.63           C  
ANISOU 7809  C   PRO B 511     1510   2103   2327     16     55    177       C  
ATOM   7810  O   PRO B 511     -23.098 -10.852 116.924  1.00 14.70           O  
ANISOU 7810  O   PRO B 511     1386   1998   2201     13     82    193       O  
ATOM   7811  CB  PRO B 511     -25.424 -12.893 117.087  1.00 12.05           C  
ANISOU 7811  CB  PRO B 511     1106   1643   1828     40     40    153       C  
ATOM   7812  CG  PRO B 511     -26.765 -12.232 117.014  1.00 15.97           C  
ANISOU 7812  CG  PRO B 511     1630   2131   2308     31     37    160       C  
ATOM   7813  CD  PRO B 511     -26.561 -10.830 117.426  1.00 11.38           C  
ANISOU 7813  CD  PRO B 511     1043   1545   1737      7     47    181       C  
ATOM   7814  N   THR B 512     -22.208 -12.380 118.340  1.00 14.17           N  
ANISOU 7814  N   THR B 512     1300   1915   2167     19     43    171       N  
ATOM   7815  CA  THR B 512     -20.811 -12.034 117.999  1.00 14.80           C  
ANISOU 7815  CA  THR B 512     1342   2011   2271     18     63    182       C  
ATOM   7816  C   THR B 512     -20.491 -12.307 116.524  1.00 18.90           C  
ANISOU 7816  C   THR B 512     1851   2558   2773     44     99    182       C  
ATOM   7817  O   THR B 512     -19.669 -11.611 115.943  1.00 19.09           O  
ANISOU 7817  O   THR B 512     1850   2597   2807     41    128    200       O  
ATOM   7818  CB  THR B 512     -19.814 -12.734 118.949  1.00 23.94           C  
ANISOU 7818  CB  THR B 512     2474   3161   3462     18     39    175       C  
ATOM   7819  OG1 THR B 512     -20.004 -14.144 118.871  1.00 28.71           O  
ANISOU 7819  OG1 THR B 512     3087   3764   4059     44     27    153       O  
ATOM   7820  CG2 THR B 512     -19.953 -12.261 120.393  1.00 20.63           C  
ANISOU 7820  CG2 THR B 512     2064   2716   3058     -9      6    178       C  
ATOM   7821  N   LYS B 513     -21.189 -13.286 115.902  1.00 15.32           N  
ANISOU 7821  N   LYS B 513     1420   2109   2291     70     98    162       N  
ATOM   7822  CA  LYS B 513     -20.972 -13.610 114.485  1.00 14.94           C  
ANISOU 7822  CA  LYS B 513     1371   2086   2219     99    130    158       C  
ATOM   7823  C   LYS B 513     -21.281 -12.405 113.571  1.00 18.41           C  
ANISOU 7823  C   LYS B 513     1819   2540   2636     91    161    180       C  
ATOM   7824  O   LYS B 513     -20.729 -12.309 112.479  1.00 17.79           O  
ANISOU 7824  O   LYS B 513     1731   2486   2544    108    196    187       O  
ATOM   7825  CB  LYS B 513     -21.787 -14.864 114.064  1.00 16.91           C  
ANISOU 7825  CB  LYS B 513     1650   2333   2443    126    115    130       C  
ATOM   7826  CG  LYS B 513     -23.317 -14.661 114.038  1.00 29.95           C  
ANISOU 7826  CG  LYS B 513     3340   3972   4069    118     98    127       C  
ATOM   7827  CD  LYS B 513     -23.815 -14.269 112.633  1.00 38.25           C  
ANISOU 7827  CD  LYS B 513     4409   5042   5081    133    123    131       C  
ATOM   7828  CE  LYS B 513     -25.318 -14.332 112.513  1.00 49.35           C  
ANISOU 7828  CE  LYS B 513     5850   6436   6464    130    102    124       C  
ATOM   7829  NZ  LYS B 513     -25.990 -13.348 113.405  1.00 59.35           N  
ANISOU 7829  NZ  LYS B 513     7123   7685   7744     99     90    142       N  
ATOM   7830  N   GLU B 514     -22.123 -11.455 114.054  1.00 15.26           N  
ANISOU 7830  N   GLU B 514     1438   2125   2235     65    149    193       N  
ATOM   7831  CA  GLU B 514     -22.422 -10.227 113.311  1.00 15.13           C  
ANISOU 7831  CA  GLU B 514     1430   2118   2202     55    174    218       C  
ATOM   7832  C   GLU B 514     -21.175  -9.337 113.180  1.00 20.35           C  
ANISOU 7832  C   GLU B 514     2054   2789   2888     41    202    243       C  
ATOM   7833  O   GLU B 514     -21.048  -8.611 112.206  1.00 19.76           O  
ANISOU 7833  O   GLU B 514     1979   2731   2798     43    235    264       O  
ATOM   7834  CB  GLU B 514     -23.574  -9.446 113.977  1.00 15.67           C  
ANISOU 7834  CB  GLU B 514     1524   2164   2268     32    153    224       C  
ATOM   7835  CG  GLU B 514     -24.944 -10.062 113.747  1.00 20.58           C  
ANISOU 7835  CG  GLU B 514     2181   2780   2861     45    135    207       C  
ATOM   7836  CD  GLU B 514     -25.414 -10.022 112.306  1.00 30.42           C  
ANISOU 7836  CD  GLU B 514     3445   4045   4069     66    155    209       C  
ATOM   7837  OE1 GLU B 514     -25.695  -8.911 111.801  1.00 16.32           O  
ANISOU 7837  OE1 GLU B 514     1666   2263   2271     57    172    231       O  
ATOM   7838  OE2 GLU B 514     -25.525 -11.104 111.688  1.00 23.96           O  
ANISOU 7838  OE2 GLU B 514     2635   3236   3230     93    152    188       O  
ATOM   7839  N   SER B 515     -20.235  -9.426 114.157  1.00 18.39           N  
ANISOU 7839  N   SER B 515     1776   2531   2681     27    189    244       N  
ATOM   7840  CA  SER B 515     -18.997  -8.631 114.123  1.00 19.46           C  
ANISOU 7840  CA  SER B 515     1871   2673   2849     11    210    268       C  
ATOM   7841  C   SER B 515     -17.956  -9.255 113.185  1.00 26.15           C  
ANISOU 7841  C   SER B 515     2689   3550   3698     38    245    269       C  
ATOM   7842  O   SER B 515     -16.924  -8.636 112.913  1.00 26.77           O  
ANISOU 7842  O   SER B 515     2731   3639   3801     28    272    292       O  
ATOM   7843  CB  SER B 515     -18.412  -8.491 115.527  1.00 22.71           C  
ANISOU 7843  CB  SER B 515     2262   3062   3303    -14    178    267       C  
ATOM   7844  OG  SER B 515     -17.912  -9.729 116.005  1.00 31.81           O  
ANISOU 7844  OG  SER B 515     3401   4216   4470      3    159    245       O  
ATOM   7845  N   LEU B 516     -18.209 -10.496 112.719  1.00 23.52           N  
ANISOU 7845  N   LEU B 516     2370   3227   3339     71    245    243       N  
ATOM   7846  CA  LEU B 516     -17.251 -11.234 111.896  1.00 24.00           C  
ANISOU 7846  CA  LEU B 516     2406   3314   3400    102    276    237       C  
ATOM   7847  C   LEU B 516     -17.706 -11.351 110.433  1.00 26.96           C  
ANISOU 7847  C   LEU B 516     2807   3714   3724    131    311    236       C  
ATOM   7848  O   LEU B 516     -16.903 -11.128 109.522  1.00 26.81           O  
ANISOU 7848  O   LEU B 516     2766   3720   3700    145    355    252       O  
ATOM   7849  CB  LEU B 516     -17.003 -12.634 112.493  1.00 24.63           C  
ANISOU 7849  CB  LEU B 516     2480   3385   3493    122    248    207       C  
ATOM   7850  CG  LEU B 516     -16.404 -12.656 113.915  1.00 30.00           C  
ANISOU 7850  CG  LEU B 516     3133   4044   4222     99    213    207       C  
ATOM   7851  CD1 LEU B 516     -16.602 -14.009 114.570  1.00 30.04           C  
ANISOU 7851  CD1 LEU B 516     3149   4034   4231    117    177    177       C  
ATOM   7852  CD2 LEU B 516     -14.921 -12.270 113.898  1.00 33.38           C  
ANISOU 7852  CD2 LEU B 516     3505   4484   4693     93    236    228       C  
ATOM   7853  N   ILE B 517     -18.981 -11.735 110.203  1.00 22.49           N  
ANISOU 7853  N   ILE B 517     2286   3140   3119    141    290    217       N  
ATOM   7854  CA  ILE B 517     -19.490 -11.938 108.834  1.00 22.34           C  
ANISOU 7854  CA  ILE B 517     2298   3143   3048    170    315    212       C  
ATOM   7855  C   ILE B 517     -20.387 -10.773 108.354  1.00 24.68           C  
ANISOU 7855  C   ILE B 517     2621   3438   3317    153    322    235       C  
ATOM   7856  O   ILE B 517     -20.818 -10.764 107.197  1.00 24.40           O  
ANISOU 7856  O   ILE B 517     2612   3421   3236    175    342    235       O  
ATOM   7857  CB  ILE B 517     -20.186 -13.327 108.676  1.00 25.56           C  
ANISOU 7857  CB  ILE B 517     2736   3545   3431    200    288    172       C  
ATOM   7858  CG1 ILE B 517     -21.481 -13.414 109.529  1.00 25.54           C  
ANISOU 7858  CG1 ILE B 517     2763   3513   3430    181    240    161       C  
ATOM   7859  CG2 ILE B 517     -19.207 -14.471 109.006  1.00 27.41           C  
ANISOU 7859  CG2 ILE B 517     2943   3780   3692    221    286    151       C  
ATOM   7860  CD1 ILE B 517     -22.350 -14.666 109.242  1.00 34.24           C  
ANISOU 7860  CD1 ILE B 517     3898   4607   4506    206    213    126       C  
ATOM   7861  N   ASN B 518     -20.636  -9.783 109.233  1.00 19.86           N  
ANISOU 7861  N   ASN B 518     2005   2807   2734    117    305    254       N  
ATOM   7862  CA  ASN B 518     -21.442  -8.607 108.891  1.00 18.78           C  
ANISOU 7862  CA  ASN B 518     1892   2666   2578     99    310    278       C  
ATOM   7863  C   ASN B 518     -20.830  -7.347 109.567  1.00 21.78           C  
ANISOU 7863  C   ASN B 518     2242   3033   2999     62    317    309       C  
ATOM   7864  O   ASN B 518     -21.558  -6.517 110.118  1.00 20.67           O  
ANISOU 7864  O   ASN B 518     2117   2871   2865     38    297    319       O  
ATOM   7865  CB  ASN B 518     -22.910  -8.817 109.341  1.00 17.35           C  
ANISOU 7865  CB  ASN B 518     1748   2463   2382     95    269    260       C  
ATOM   7866  CG  ASN B 518     -23.907  -7.898 108.662  1.00 28.69           C  
ANISOU 7866  CG  ASN B 518     3214   3899   3787     90    274    277       C  
ATOM   7867  OD1 ASN B 518     -23.644  -7.325 107.602  1.00 20.46           O  
ANISOU 7867  OD1 ASN B 518     2175   2877   2722     99    308    299       O  
ATOM   7868  ND2 ASN B 518     -25.110  -7.818 109.218  1.00 19.26           N  
ANISOU 7868  ND2 ASN B 518     2044   2683   2591     80    241    269       N  
ATOM   7869  N   ALA B 519     -19.471  -7.242 109.541  1.00 18.66           N  
ANISOU 7869  N   ALA B 519     1805   2650   2634     59    343    324       N  
ATOM   7870  CA  ALA B 519     -18.707  -6.217 110.275  1.00 18.59           C  
ANISOU 7870  CA  ALA B 519     1763   2628   2673     24    344    350       C  
ATOM   7871  C   ALA B 519     -19.169  -4.778 109.997  1.00 22.73           C  
ANISOU 7871  C   ALA B 519     2301   3143   3193      0    355    382       C  
ATOM   7872  O   ALA B 519     -19.376  -4.013 110.940  1.00 22.15           O  
ANISOU 7872  O   ALA B 519     2226   3041   3147    -31    330    388       O  
ATOM   7873  CB  ALA B 519     -17.220  -6.358 109.978  1.00 19.65           C  
ANISOU 7873  CB  ALA B 519     1848   2782   2837     29    377    363       C  
ATOM   7874  N   THR B 520     -19.279  -4.391 108.703  1.00 19.76           N  
ANISOU 7874  N   THR B 520     1937   2789   2782     14    393    402       N  
ATOM   7875  CA  THR B 520     -19.668  -3.020 108.325  1.00 19.95           C  
ANISOU 7875  CA  THR B 520     1974   2805   2800     -7    407    437       C  
ATOM   7876  C   THR B 520     -20.988  -2.599 108.993  1.00 23.22           C  
ANISOU 7876  C   THR B 520     2424   3190   3208    -21    367    427       C  
ATOM   7877  O   THR B 520     -21.047  -1.545 109.633  1.00 23.17           O  
ANISOU 7877  O   THR B 520     2414   3159   3230    -52    355    444       O  
ATOM   7878  CB  THR B 520     -19.722  -2.878 106.791  1.00 30.37           C  
ANISOU 7878  CB  THR B 520     3310   4155   4073     18    451    456       C  
ATOM   7879  OG1 THR B 520     -18.429  -3.166 106.252  1.00 28.96           O  
ANISOU 7879  OG1 THR B 520     3094   4004   3906     30    493    469       O  
ATOM   7880  CG2 THR B 520     -20.175  -1.482 106.345  1.00 31.26           C  
ANISOU 7880  CG2 THR B 520     3439   4259   4179     -2    464    494       C  
ATOM   7881  N   GLU B 521     -22.027  -3.441 108.881  1.00 18.81           N  
ANISOU 7881  N   GLU B 521     1900   2633   2615      1    345    398       N  
ATOM   7882  CA  GLU B 521     -23.336  -3.138 109.453  1.00 17.54           C  
ANISOU 7882  CA  GLU B 521     1771   2447   2447     -8    310    388       C  
ATOM   7883  C   GLU B 521     -23.342  -3.267 110.986  1.00 19.57           C  
ANISOU 7883  C   GLU B 521     2018   2676   2742    -30    273    370       C  
ATOM   7884  O   GLU B 521     -24.065  -2.525 111.661  1.00 19.25           O  
ANISOU 7884  O   GLU B 521     1993   2611   2712    -49    253    374       O  
ATOM   7885  CB  GLU B 521     -24.425  -4.019 108.822  1.00 18.84           C  
ANISOU 7885  CB  GLU B 521     1971   2622   2566     21    297    364       C  
ATOM   7886  CG  GLU B 521     -24.651  -3.743 107.337  1.00 27.50           C  
ANISOU 7886  CG  GLU B 521     3088   3743   3618     41    327    382       C  
ATOM   7887  CD  GLU B 521     -25.155  -2.345 107.001  1.00 43.66           C  
ANISOU 7887  CD  GLU B 521     5149   5779   5660     25    335    416       C  
ATOM   7888  OE1 GLU B 521     -25.663  -1.655 107.916  1.00 27.92           O  
ANISOU 7888  OE1 GLU B 521     3158   3757   3694      0    311    419       O  
ATOM   7889  OE2 GLU B 521     -25.108  -1.974 105.807  1.00 38.79           O  
ANISOU 7889  OE2 GLU B 521     4545   5183   5011     38    364    438       O  
ATOM   7890  N   TYR B 522     -22.506  -4.176 111.539  1.00 14.88           N  
ANISOU 7890  N   TYR B 522     1399   2086   2169    -25    266    352       N  
ATOM   7891  CA  TYR B 522     -22.389  -4.348 112.994  1.00 13.83           C  
ANISOU 7891  CA  TYR B 522     1257   1929   2070    -44    231    337       C  
ATOM   7892  C   TYR B 522     -21.807  -3.096 113.650  1.00 18.35           C  
ANISOU 7892  C   TYR B 522     1811   2481   2681    -78    230    360       C  
ATOM   7893  O   TYR B 522     -22.286  -2.676 114.705  1.00 17.93           O  
ANISOU 7893  O   TYR B 522     1771   2401   2642    -97    201    353       O  
ATOM   7894  CB  TYR B 522     -21.533  -5.585 113.333  1.00 14.60           C  
ANISOU 7894  CB  TYR B 522     1330   2036   2182    -30    225    315       C  
ATOM   7895  CG  TYR B 522     -21.204  -5.712 114.808  1.00 15.61           C  
ANISOU 7895  CG  TYR B 522     1446   2140   2346    -49    190    304       C  
ATOM   7896  CD1 TYR B 522     -22.086  -6.331 115.689  1.00 16.79           C  
ANISOU 7896  CD1 TYR B 522     1620   2272   2487    -47    156    280       C  
ATOM   7897  CD2 TYR B 522     -19.998  -5.236 115.318  1.00 16.50           C  
ANISOU 7897  CD2 TYR B 522     1521   2247   2499    -70    191    317       C  
ATOM   7898  CE1 TYR B 522     -21.784  -6.459 117.045  1.00 16.99           C  
ANISOU 7898  CE1 TYR B 522     1639   2277   2541    -64    124    270       C  
ATOM   7899  CE2 TYR B 522     -19.698  -5.332 116.677  1.00 17.23           C  
ANISOU 7899  CE2 TYR B 522     1607   2318   2623    -87    155    306       C  
ATOM   7900  CZ  TYR B 522     -20.590  -5.955 117.536  1.00 22.30           C  
ANISOU 7900  CZ  TYR B 522     2279   2945   3252    -83    122    282       C  
ATOM   7901  OH  TYR B 522     -20.287  -6.081 118.873  1.00 19.17           O  
ANISOU 7901  OH  TYR B 522     1878   2527   2879    -98     87    272       O  
ATOM   7902  N   GLU B 523     -20.762  -2.497 113.028  1.00 15.70           N  
ANISOU 7902  N   GLU B 523     1445   2158   2362    -86    261    387       N  
ATOM   7903  CA  GLU B 523     -20.150  -1.265 113.541  1.00 15.74           C  
ANISOU 7903  CA  GLU B 523     1430   2143   2407   -120    260    411       C  
ATOM   7904  C   GLU B 523     -21.131  -0.094 113.473  1.00 18.37           C  
ANISOU 7904  C   GLU B 523     1795   2456   2730   -134    257    427       C  
ATOM   7905  O   GLU B 523     -21.124   0.766 114.356  1.00 18.18           O  
ANISOU 7905  O   GLU B 523     1771   2403   2734   -161    236    432       O  
ATOM   7906  CB  GLU B 523     -18.848  -0.931 112.773  1.00 17.77           C  
ANISOU 7906  CB  GLU B 523     1646   2420   2687   -124    299    440       C  
ATOM   7907  CG  GLU B 523     -17.724  -1.944 112.995  1.00 28.78           C  
ANISOU 7907  CG  GLU B 523     3001   3830   4104   -113    301    427       C  
ATOM   7908  CD  GLU B 523     -17.206  -2.036 114.424  1.00 51.35           C  
ANISOU 7908  CD  GLU B 523     5841   6664   7006   -135    260    413       C  
ATOM   7909  OE1 GLU B 523     -17.200  -0.998 115.125  1.00 53.91           O  
ANISOU 7909  OE1 GLU B 523     6165   6960   7357   -166    241    424       O  
ATOM   7910  OE2 GLU B 523     -16.734  -3.129 114.811  1.00 42.63           O  
ANISOU 7910  OE2 GLU B 523     4720   5567   5910   -120    247    391       O  
ATOM   7911  N   LYS B 524     -22.011  -0.080 112.440  1.00 14.61           N  
ANISOU 7911  N   LYS B 524     1346   1993   2211   -114    274    432       N  
ATOM   7912  CA  LYS B 524     -23.054   0.944 112.318  1.00 14.21           C  
ANISOU 7912  CA  LYS B 524     1327   1924   2147   -123    270    446       C  
ATOM   7913  C   LYS B 524     -24.054   0.836 113.476  1.00 18.46           C  
ANISOU 7913  C   LYS B 524     1890   2436   2688   -128    230    420       C  
ATOM   7914  O   LYS B 524     -24.429   1.849 114.064  1.00 18.73           O  
ANISOU 7914  O   LYS B 524     1936   2442   2739   -149    217    428       O  
ATOM   7915  CB  LYS B 524     -23.779   0.832 110.966  1.00 16.58           C  
ANISOU 7915  CB  LYS B 524     1652   2248   2401    -98    292    456       C  
ATOM   7916  CG  LYS B 524     -22.925   1.259 109.776  1.00 27.98           C  
ANISOU 7916  CG  LYS B 524     3078   3715   3838    -95    336    489       C  
ATOM   7917  N   GLY B 525     -24.425  -0.397 113.828  1.00 14.79           N  
ANISOU 7917  N   GLY B 525     1433   1979   2208   -110    212    390       N  
ATOM   7918  CA  GLY B 525     -25.318  -0.657 114.952  1.00 14.38           C  
ANISOU 7918  CA  GLY B 525     1403   1905   2158   -113    179    366       C  
ATOM   7919  C   GLY B 525     -24.679  -0.326 116.281  1.00 19.14           C  
ANISOU 7919  C   GLY B 525     1992   2483   2797   -137    156    360       C  
ATOM   7920  O   GLY B 525     -25.330   0.234 117.169  1.00 18.51           O  
ANISOU 7920  O   GLY B 525     1932   2377   2723   -149    136    354       O  
ATOM   7921  N   LYS B 526     -23.372  -0.612 116.403  1.00 16.76           N  
ANISOU 7921  N   LYS B 526     1657   2191   2521   -144    161    362       N  
ATOM   7922  CA  LYS B 526     -22.593  -0.295 117.596  1.00 16.51           C  
ANISOU 7922  CA  LYS B 526     1609   2138   2526   -168    137    358       C  
ATOM   7923  C   LYS B 526     -22.492   1.231 117.777  1.00 19.58           C  
ANISOU 7923  C   LYS B 526     2000   2502   2938   -196    137    380       C  
ATOM   7924  O   LYS B 526     -22.642   1.729 118.893  1.00 19.12           O  
ANISOU 7924  O   LYS B 526     1954   2415   2897   -213    109    370       O  
ATOM   7925  CB  LYS B 526     -21.193  -0.920 117.489  1.00 19.56           C  
ANISOU 7925  CB  LYS B 526     1954   2542   2938   -167    144    360       C  
ATOM   7926  CG  LYS B 526     -20.458  -1.020 118.812  1.00 35.32           C  
ANISOU 7926  CG  LYS B 526     3934   4518   4967   -185    110    347       C  
ATOM   7927  CD  LYS B 526     -19.115  -1.735 118.642  1.00 45.25           C  
ANISOU 7927  CD  LYS B 526     5148   5796   6251   -180    117    349       C  
ATOM   7928  CE  LYS B 526     -18.394  -1.929 119.955  1.00 60.78           C  
ANISOU 7928  CE  LYS B 526     7100   7744   8250   -196     78    335       C  
ATOM   7929  NZ  LYS B 526     -18.016  -0.629 120.581  1.00 72.22           N  
ANISOU 7929  NZ  LYS B 526     8543   9165   9732   -230     61    348       N  
ATOM   7930  N   SER B 527     -22.305   1.979 116.653  1.00 16.06           N  
ANISOU 7930  N   SER B 527     1545   2065   2491   -198    169    410       N  
ATOM   7931  CA  SER B 527     -22.236   3.450 116.678  1.00 15.33           C  
ANISOU 7931  CA  SER B 527     1456   1948   2422   -224    172    434       C  
ATOM   7932  C   SER B 527     -23.586   4.060 117.072  1.00 18.46           C  
ANISOU 7932  C   SER B 527     1894   2320   2801   -223    156    427       C  
ATOM   7933  O   SER B 527     -23.623   5.035 117.824  1.00 19.34           O  
ANISOU 7933  O   SER B 527     2014   2398   2935   -245    139    429       O  
ATOM   7934  CB  SER B 527     -21.795   3.989 115.320  1.00 17.47           C  
ANISOU 7934  CB  SER B 527     1710   2237   2691   -224    212    470       C  
ATOM   7935  OG  SER B 527     -20.508   3.512 114.970  1.00 22.59           O  
ANISOU 7935  OG  SER B 527     2316   2907   3359   -225    230    479       O  
HETATM 7936  N   MSE B 528     -24.703   3.477 116.565  1.00 12.71           N  
ANISOU 7936  N   MSE B 528     1190   1606   2033   -197    162    417       N  
HETATM 7937  CA  MSE B 528     -26.063   3.927 116.915  1.00 11.23           C  
ANISOU 7937  CA  MSE B 528     1040   1399   1830   -192    149    409       C  
HETATM 7938  C   MSE B 528     -26.337   3.749 118.407  1.00 15.26           C  
ANISOU 7938  C   MSE B 528     1563   1885   2350   -199    117    382       C  
HETATM 7939  O   MSE B 528     -26.944   4.624 119.028  1.00 14.31           O  
ANISOU 7939  O   MSE B 528     1465   1736   2237   -208    105    380       O  
HETATM 7940  CB  MSE B 528     -27.112   3.172 116.091  1.00 12.50           C  
ANISOU 7940  CB  MSE B 528     1218   1582   1951   -163    158    403       C  
HETATM 7941  CG  MSE B 528     -27.150   3.593 114.633  1.00 18.39           C  
ANISOU 7941  CG  MSE B 528     1963   2346   2678   -154    188    431       C  
HETATM 7942 SE   MSE B 528     -28.150   2.344 113.538  0.75 24.11          SE  
ANISOU 7942 SE   MSE B 528     2705   3103   3352   -117    194    418      SE  
HETATM 7943  CE  MSE B 528     -28.052   3.290 111.852  1.00 21.68           C  
ANISOU 7943  CE  MSE B 528     2402   2812   3024   -111    229    460       C  
ATOM   7944  N   LEU B 529     -25.874   2.614 118.994  1.00 11.70           N  
ANISOU 7944  N   LEU B 529     1100   1445   1900   -194    103    360       N  
ATOM   7945  CA  LEU B 529     -26.015   2.362 120.436  1.00 12.02           C  
ANISOU 7945  CA  LEU B 529     1153   1465   1947   -200     72    336       C  
ATOM   7946  C   LEU B 529     -25.292   3.427 121.249  1.00 17.46           C  
ANISOU 7946  C   LEU B 529     1839   2125   2669   -228     56    340       C  
ATOM   7947  O   LEU B 529     -25.820   3.904 122.257  1.00 16.75           O  
ANISOU 7947  O   LEU B 529     1775   2009   2580   -234     35    327       O  
ATOM   7948  CB  LEU B 529     -25.468   0.968 120.802  1.00 12.12           C  
ANISOU 7948  CB  LEU B 529     1151   1496   1957   -190     61    317       C  
ATOM   7949  CG  LEU B 529     -26.377  -0.217 120.491  1.00 16.52           C  
ANISOU 7949  CG  LEU B 529     1720   2072   2483   -164     64    303       C  
ATOM   7950  CD1 LEU B 529     -25.633  -1.517 120.657  1.00 16.42           C  
ANISOU 7950  CD1 LEU B 529     1688   2076   2473   -155     56    289       C  
ATOM   7951  CD2 LEU B 529     -27.616  -0.206 121.379  1.00 17.98           C  
ANISOU 7951  CD2 LEU B 529     1939   2239   2654   -160     49    288       C  
ATOM   7952  N   GLY B 530     -24.070   3.765 120.825  1.00 14.83           N  
ANISOU 7952  N   GLY B 530     1473   1797   2364   -244     64    358       N  
ATOM   7953  CA  GLY B 530     -23.236   4.734 121.525  1.00 15.29           C  
ANISOU 7953  CA  GLY B 530     1523   1827   2461   -273     45    363       C  
ATOM   7954  C   GLY B 530     -22.741   4.223 122.862  1.00 19.33           C  
ANISOU 7954  C   GLY B 530     2035   2328   2984   -280      8    338       C  
ATOM   7955  O   GLY B 530     -22.877   3.036 123.168  1.00 19.20           O  
ANISOU 7955  O   GLY B 530     2019   2328   2949   -263      1    320       O  
ATOM   7956  N   GLY B 531     -22.166   5.118 123.656  1.00 16.15           N  
ANISOU 7956  N   GLY B 531     1631   1893   2611   -306    -17    337       N  
ATOM   7957  CA  GLY B 531     -21.646   4.774 124.978  1.00 16.06           C  
ANISOU 7957  CA  GLY B 531     1623   1867   2610   -315    -56    314       C  
ATOM   7958  C   GLY B 531     -20.525   3.750 124.939  1.00 19.19           C  
ANISOU 7958  C   GLY B 531     1981   2287   3024   -313    -63    313       C  
ATOM   7959  O   GLY B 531     -19.571   3.894 124.168  1.00 18.70           O  
ANISOU 7959  O   GLY B 531     1878   2237   2991   -323    -46    335       O  
ATOM   7960  N   LYS B 532     -20.646   2.684 125.751  1.00 15.79           N  
ANISOU 7960  N   LYS B 532     1561   1863   2574   -299    -84    290       N  
ATOM   7961  CA  LYS B 532     -19.623   1.632 125.803  1.00 15.68           C  
ANISOU 7961  CA  LYS B 532     1512   1870   2577   -295    -93    287       C  
ATOM   7962  C   LYS B 532     -19.802   0.592 124.668  1.00 19.95           C  
ANISOU 7962  C   LYS B 532     2034   2446   3098   -269    -58    293       C  
ATOM   7963  O   LYS B 532     -18.916  -0.234 124.438  1.00 20.27           O  
ANISOU 7963  O   LYS B 532     2041   2506   3154   -262    -57    294       O  
ATOM   7964  CB  LYS B 532     -19.599   0.958 127.179  1.00 17.45           C  
ANISOU 7964  CB  LYS B 532     1756   2082   2791   -292   -134    261       C  
ATOM   7965  CG  LYS B 532     -19.123   1.885 128.299  1.00 23.28           C  
ANISOU 7965  CG  LYS B 532     2506   2786   3552   -318   -175    253       C  
ATOM   7966  CD  LYS B 532     -19.103   1.176 129.649  1.00 34.95           C  
ANISOU 7966  CD  LYS B 532     4008   4255   5015   -312   -216    229       C  
ATOM   7967  CE  LYS B 532     -18.633   2.081 130.769  1.00 43.79           C  
ANISOU 7967  CE  LYS B 532     5145   5340   6153   -336   -260    218       C  
ATOM   7968  NZ  LYS B 532     -17.199   2.453 130.616  1.00 53.87           N  
ANISOU 7968  NZ  LYS B 532     6373   6612   7483   -360   -279    231       N  
ATOM   7969  N   GLY B 533     -20.904   0.713 123.922  1.00 15.94           N  
ANISOU 7969  N   GLY B 533     1550   1947   2560   -254    -30    298       N  
ATOM   7970  CA  GLY B 533     -21.134  -0.083 122.723  1.00 14.93           C  
ANISOU 7970  CA  GLY B 533     1410   1852   2412   -231      4    304       C  
ATOM   7971  C   GLY B 533     -22.022  -1.288 122.929  1.00 16.80           C  
ANISOU 7971  C   GLY B 533     1670   2099   2614   -206     -1    284       C  
ATOM   7972  O   GLY B 533     -23.049  -1.206 123.615  1.00 15.68           O  
ANISOU 7972  O   GLY B 533     1563   1942   2452   -203    -14    271       O  
ATOM   7973  N   ASP B 534     -21.647  -2.424 122.301  1.00 11.82           N  
ANISOU 7973  N   ASP B 534     1018   1495   1978   -186     11    280       N  
ATOM   7974  CA  ASP B 534     -22.437  -3.651 122.329  1.00 10.48           C  
ANISOU 7974  CA  ASP B 534      866   1335   1779   -162      8    262       C  
ATOM   7975  C   ASP B 534     -22.257  -4.428 123.650  1.00 13.11           C  
ANISOU 7975  C   ASP B 534     1207   1656   2117   -162    -28    243       C  
ATOM   7976  O   ASP B 534     -21.637  -5.498 123.667  1.00 12.71           O  
ANISOU 7976  O   ASP B 534     1138   1618   2073   -150    -35    235       O  
ATOM   7977  CB  ASP B 534     -22.096  -4.540 121.111  1.00 11.67           C  
ANISOU 7977  CB  ASP B 534      995   1516   1922   -139     34    265       C  
ATOM   7978  CG  ASP B 534     -22.907  -5.827 121.026  1.00 13.91           C  
ANISOU 7978  CG  ASP B 534     1297   1809   2178   -114     29    246       C  
ATOM   7979  OD1 ASP B 534     -24.009  -5.876 121.617  1.00 13.90           O  
ANISOU 7979  OD1 ASP B 534     1328   1794   2160   -114     16    236       O  
ATOM   7980  OD2 ASP B 534     -22.470  -6.750 120.326  1.00 18.80           O  
ANISOU 7980  OD2 ASP B 534     1899   2448   2794    -94     41    241       O  
ATOM   7981  N   ILE B 535     -22.811  -3.890 124.750  1.00  8.76           N  
ANISOU 7981  N   ILE B 535      686   1081   1562   -175    -50    236       N  
ATOM   7982  CA  ILE B 535     -22.835  -4.575 126.055  1.00  8.28           C  
ANISOU 7982  CA  ILE B 535      642   1008   1497   -174    -83    219       C  
ATOM   7983  C   ILE B 535     -24.236  -4.442 126.693  1.00 11.84           C  
ANISOU 7983  C   ILE B 535     1136   1445   1918   -170    -85    210       C  
ATOM   7984  O   ILE B 535     -25.056  -3.655 126.213  1.00 10.49           O  
ANISOU 7984  O   ILE B 535      979   1270   1737   -170    -66    218       O  
ATOM   7985  CB  ILE B 535     -21.693  -4.072 127.011  1.00 11.22           C  
ANISOU 7985  CB  ILE B 535     1001   1363   1898   -195   -114    218       C  
ATOM   7986  CG1 ILE B 535     -21.763  -2.539 127.227  1.00 11.41           C  
ANISOU 7986  CG1 ILE B 535     1038   1366   1933   -218   -116    226       C  
ATOM   7987  CG2 ILE B 535     -20.293  -4.514 126.500  1.00 12.44           C  
ANISOU 7987  CG2 ILE B 535     1107   1534   2085   -195   -113    225       C  
ATOM   7988  CD1 ILE B 535     -20.879  -2.033 128.376  1.00 15.51           C  
ANISOU 7988  CD1 ILE B 535     1555   1863   2475   -239   -155    220       C  
ATOM   7989  N   VAL B 536     -24.512  -5.219 127.761  1.00  9.35           N  
ANISOU 7989  N   VAL B 536      840   1121   1590   -164   -108    197       N  
ATOM   7990  CA  VAL B 536     -25.857  -5.279 128.369  1.00  9.23           C  
ANISOU 7990  CA  VAL B 536      864   1096   1549   -157   -107    191       C  
ATOM   7991  C   VAL B 536     -26.262  -3.989 129.105  1.00 13.46           C  
ANISOU 7991  C   VAL B 536     1427   1608   2080   -171   -111    190       C  
ATOM   7992  O   VAL B 536     -27.439  -3.817 129.424  1.00 13.50           O  
ANISOU 7992  O   VAL B 536     1460   1605   2063   -164   -102    187       O  
ATOM   7993  CB  VAL B 536     -26.036  -6.525 129.275  1.00 12.78           C  
ANISOU 7993  CB  VAL B 536     1327   1544   1986   -147   -126    180       C  
ATOM   7994  CG1 VAL B 536     -25.907  -7.802 128.473  1.00 12.34           C  
ANISOU 7994  CG1 VAL B 536     1250   1508   1933   -130   -119    179       C  
ATOM   7995  CG2 VAL B 536     -25.046  -6.507 130.443  1.00 12.88           C  
ANISOU 7995  CG2 VAL B 536     1342   1544   2009   -158   -161    174       C  
ATOM   7996  N   SER B 537     -25.288  -3.122 129.432  1.00  9.86           N  
ANISOU 7996  N   SER B 537      962   1140   1645   -190   -128    191       N  
ATOM   7997  CA  SER B 537     -25.558  -1.927 130.236  1.00  9.88           C  
ANISOU 7997  CA  SER B 537      993   1116   1644   -203   -138    187       C  
ATOM   7998  C   SER B 537     -25.793  -0.659 129.386  1.00 14.80           C  
ANISOU 7998  C   SER B 537     1612   1732   2278   -212   -117    199       C  
ATOM   7999  O   SER B 537     -26.074   0.407 129.944  1.00 14.77           O  
ANISOU 7999  O   SER B 537     1633   1705   2274   -222   -123    196       O  
ATOM   8000  CB  SER B 537     -24.437  -1.693 131.242  1.00 13.88           C  
ANISOU 8000  CB  SER B 537     1500   1608   2168   -219   -176    179       C  
ATOM   8001  OG  SER B 537     -23.191  -1.529 130.589  1.00 25.11           O  
ANISOU 8001  OG  SER B 537     2879   3036   3624   -232   -180    189       O  
ATOM   8002  N   THR B 538     -25.713  -0.776 128.052  1.00 11.32           N  
ANISOU 8002  N   THR B 538     1143   1312   1845   -207    -91    214       N  
ATOM   8003  CA  THR B 538     -25.935   0.375 127.171  1.00 11.15           C  
ANISOU 8003  CA  THR B 538     1118   1285   1833   -214    -69    230       C  
ATOM   8004  C   THR B 538     -27.438   0.660 127.016  1.00 15.30           C  
ANISOU 8004  C   THR B 538     1672   1806   2334   -200    -51    229       C  
ATOM   8005  O   THR B 538     -28.179  -0.183 126.507  1.00 14.32           O  
ANISOU 8005  O   THR B 538     1548   1700   2192   -182    -36    229       O  
ATOM   8006  CB  THR B 538     -25.233   0.165 125.814  1.00 14.31           C  
ANISOU 8006  CB  THR B 538     1479   1709   2248   -213    -48    247       C  
ATOM   8007  OG1 THR B 538     -23.862  -0.140 126.046  1.00 15.15           O  
ANISOU 8007  OG1 THR B 538     1556   1820   2380   -225    -64    247       O  
ATOM   8008  CG2 THR B 538     -25.345   1.390 124.903  1.00  8.90           C  
ANISOU 8008  CG2 THR B 538      790   1018   1572   -223    -26    268       C  
ATOM   8009  N   PRO B 539     -27.922   1.845 127.493  1.00 13.02           N  
ANISOU 8009  N   PRO B 539     1409   1491   2046   -208    -53    228       N  
ATOM   8010  CA  PRO B 539     -29.361   2.140 127.380  1.00 12.68           C  
ANISOU 8010  CA  PRO B 539     1391   1443   1983   -193    -35    228       C  
ATOM   8011  C   PRO B 539     -29.786   2.350 125.936  1.00 17.11           C  
ANISOU 8011  C   PRO B 539     1937   2019   2545   -186     -8    247       C  
ATOM   8012  O   PRO B 539     -29.046   2.954 125.154  1.00 17.57           O  
ANISOU 8012  O   PRO B 539     1975   2079   2621   -198     -2    263       O  
ATOM   8013  CB  PRO B 539     -29.531   3.427 128.216  1.00 14.54           C  
ANISOU 8013  CB  PRO B 539     1655   1645   2224   -204    -45    222       C  
ATOM   8014  CG  PRO B 539     -28.227   3.594 128.962  1.00 19.27           C  
ANISOU 8014  CG  PRO B 539     2248   2232   2842   -224    -75    214       C  
ATOM   8015  CD  PRO B 539     -27.191   2.951 128.136  1.00 14.92           C  
ANISOU 8015  CD  PRO B 539     1656   1704   2308   -230    -73    226       C  
ATOM   8016  N   LEU B 540     -30.965   1.833 125.569  1.00 13.65           N  
ANISOU 8016  N   LEU B 540     1508   1593   2087   -167      6    247       N  
ATOM   8017  CA  LEU B 540     -31.483   1.969 124.214  1.00 12.96           C  
ANISOU 8017  CA  LEU B 540     1410   1520   1996   -157     27    264       C  
ATOM   8018  C   LEU B 540     -31.977   3.388 123.951  1.00 17.13           C  
ANISOU 8018  C   LEU B 540     1951   2027   2532   -161     36    276       C  
ATOM   8019  O   LEU B 540     -32.064   4.195 124.879  1.00 16.37           O  
ANISOU 8019  O   LEU B 540     1875   1904   2442   -169     27    269       O  
ATOM   8020  CB  LEU B 540     -32.612   0.947 123.955  1.00 12.83           C  
ANISOU 8020  CB  LEU B 540     1397   1518   1959   -136     34    258       C  
ATOM   8021  CG  LEU B 540     -32.200  -0.544 124.022  1.00 16.83           C  
ANISOU 8021  CG  LEU B 540     1889   2045   2459   -129     25    248       C  
ATOM   8022  CD1 LEU B 540     -33.373  -1.447 123.675  1.00 16.02           C  
ANISOU 8022  CD1 LEU B 540     1791   1954   2342   -111     31    244       C  
ATOM   8023  CD2 LEU B 540     -31.017  -0.833 123.096  1.00 18.15           C  
ANISOU 8023  CD2 LEU B 540     2030   2232   2634   -133     30    256       C  
ATOM   8024  N   TRP B 541     -32.280   3.704 122.670  1.00 14.78           N  
ANISOU 8024  N   TRP B 541     1644   1740   2231   -155     54    295       N  
ATOM   8025  CA  TRP B 541     -32.716   5.041 122.252  1.00 14.59           C  
ANISOU 8025  CA  TRP B 541     1632   1697   2216   -158     63    311       C  
ATOM   8026  C   TRP B 541     -33.859   5.595 123.132  1.00 17.52           C  
ANISOU 8026  C   TRP B 541     2031   2043   2584   -150     59    300       C  
ATOM   8027  O   TRP B 541     -33.746   6.707 123.649  1.00 17.46           O  
ANISOU 8027  O   TRP B 541     2037   2006   2590   -160     55    300       O  
ATOM   8028  CB  TRP B 541     -33.118   5.036 120.768  1.00 13.57           C  
ANISOU 8028  CB  TRP B 541     1493   1587   2076   -147     80    332       C  
ATOM   8029  CG  TRP B 541     -33.731   6.321 120.296  1.00 14.93           C  
ANISOU 8029  CG  TRP B 541     1677   1740   2255   -146     89    350       C  
ATOM   8030  CD1 TRP B 541     -33.089   7.508 120.087  1.00 18.22           C  
ANISOU 8030  CD1 TRP B 541     2094   2138   2692   -163     92    368       C  
ATOM   8031  CD2 TRP B 541     -35.078   6.509 119.852  1.00 14.73           C  
ANISOU 8031  CD2 TRP B 541     1665   1713   2219   -127     94    356       C  
ATOM   8032  NE1 TRP B 541     -33.971   8.441 119.593  1.00 17.91           N  
ANISOU 8032  NE1 TRP B 541     2069   2083   2653   -155     99    383       N  
ATOM   8033  CE2 TRP B 541     -35.200   7.854 119.435  1.00 18.94           C  
ANISOU 8033  CE2 TRP B 541     2206   2224   2764   -133    100    376       C  
ATOM   8034  CE3 TRP B 541     -36.208   5.676 119.786  1.00 15.72           C  
ANISOU 8034  CE3 TRP B 541     1793   1851   2328   -107     93    346       C  
ATOM   8035  CZ2 TRP B 541     -36.412   8.393 118.987  1.00 18.14           C  
ANISOU 8035  CZ2 TRP B 541     2118   2115   2660   -116    104    386       C  
ATOM   8036  CZ3 TRP B 541     -37.399   6.203 119.308  1.00 17.32           C  
ANISOU 8036  CZ3 TRP B 541     2005   2046   2528    -92     97    357       C  
ATOM   8037  CH2 TRP B 541     -37.496   7.548 118.928  1.00 18.11           C  
ANISOU 8037  CH2 TRP B 541     2115   2126   2641    -96    103    376       C  
ATOM   8038  N   TRP B 542     -34.926   4.797 123.346  1.00 12.38           N  
ANISOU 8038  N   TRP B 542     1385   1401   1916   -132     62    290       N  
ATOM   8039  CA  TRP B 542     -36.079   5.237 124.154  1.00 11.24           C  
ANISOU 8039  CA  TRP B 542     1264   1236   1769   -120     64    281       C  
ATOM   8040  C   TRP B 542     -35.799   5.186 125.671  1.00 14.99           C  
ANISOU 8040  C   TRP B 542     1758   1695   2242   -126     52    260       C  
ATOM   8041  O   TRP B 542     -36.631   5.631 126.465  1.00 14.92           O  
ANISOU 8041  O   TRP B 542     1772   1667   2231   -117     55    251       O  
ATOM   8042  CB  TRP B 542     -37.343   4.424 123.799  1.00  9.24           C  
ANISOU 8042  CB  TRP B 542     1007    999   1503    -99     72    282       C  
ATOM   8043  CG  TRP B 542     -37.120   2.936 123.744  1.00  9.74           C  
ANISOU 8043  CG  TRP B 542     1057   1088   1556    -96     67    273       C  
ATOM   8044  CD1 TRP B 542     -36.860   2.185 122.633  1.00 12.41           C  
ANISOU 8044  CD1 TRP B 542     1376   1451   1888    -93     68    281       C  
ATOM   8045  CD2 TRP B 542     -37.194   2.016 124.844  1.00  9.01           C  
ANISOU 8045  CD2 TRP B 542      970    996   1456    -94     60    257       C  
ATOM   8046  NE1 TRP B 542     -36.755   0.855 122.974  1.00 11.13           N  
ANISOU 8046  NE1 TRP B 542     1207   1304   1719    -89     60    268       N  
ATOM   8047  CE2 TRP B 542     -36.947   0.724 124.327  1.00 12.33           C  
ANISOU 8047  CE2 TRP B 542     1373   1442   1870    -91     55    255       C  
ATOM   8048  CE3 TRP B 542     -37.439   2.159 126.223  1.00  9.86           C  
ANISOU 8048  CE3 TRP B 542     1099   1087   1560    -94     57    243       C  
ATOM   8049  CZ2 TRP B 542     -36.924  -0.416 125.142  1.00 11.05           C  
ANISOU 8049  CZ2 TRP B 542     1213   1286   1702    -89     47    242       C  
ATOM   8050  CZ3 TRP B 542     -37.418   1.027 127.026  1.00 10.52           C  
ANISOU 8050  CZ3 TRP B 542     1184   1178   1633    -92     51    231       C  
ATOM   8051  CH2 TRP B 542     -37.166  -0.240 126.486  1.00 10.72           C  
ANISOU 8051  CH2 TRP B 542     1190   1226   1656    -90     45    232       C  
ATOM   8052  N   ASP B 543     -34.614   4.672 126.066  1.00 10.63           N  
ANISOU 8052  N   ASP B 543     1197   1149   1693   -141     37    252       N  
ATOM   8053  CA  ASP B 543     -34.244   4.544 127.478  1.00  9.75           C  
ANISOU 8053  CA  ASP B 543     1105   1024   1577   -147     21    232       C  
ATOM   8054  C   ASP B 543     -33.297   5.686 127.903  1.00 12.94           C  
ANISOU 8054  C   ASP B 543     1518   1401   1998   -166      6    230       C  
ATOM   8055  O   ASP B 543     -32.142   5.725 127.475  1.00 12.17           O  
ANISOU 8055  O   ASP B 543     1399   1309   1916   -184     -4    237       O  
ATOM   8056  CB  ASP B 543     -33.588   3.163 127.734  1.00 11.07           C  
ANISOU 8056  CB  ASP B 543     1257   1212   1735   -148     10    225       C  
ATOM   8057  CG  ASP B 543     -33.322   2.843 129.205  1.00 14.74           C  
ANISOU 8057  CG  ASP B 543     1744   1666   2190   -151     -8    205       C  
ATOM   8058  OD1 ASP B 543     -33.350   3.783 130.037  1.00 15.14           O  
ANISOU 8058  OD1 ASP B 543     1821   1692   2241   -155    -16    196       O  
ATOM   8059  OD2 ASP B 543     -33.035   1.672 129.510  1.00 13.43           O  
ANISOU 8059  OD2 ASP B 543     1571   1517   2016   -148    -17    200       O  
ATOM   8060  N   LYS B 544     -33.792   6.610 128.750  1.00  9.00           N  
ANISOU 8060  N   LYS B 544     1050    873   1498   -164      3    218       N  
ATOM   8061  CA  LYS B 544     -32.994   7.735 129.240  1.00  8.36           C  
ANISOU 8061  CA  LYS B 544      982    761   1434   -182    -16    213       C  
ATOM   8062  C   LYS B 544     -32.548   7.495 130.691  1.00 14.02           C  
ANISOU 8062  C   LYS B 544     1723   1465   2138   -187    -40    188       C  
ATOM   8063  O   LYS B 544     -32.120   8.436 131.371  1.00 14.78           O  
ANISOU 8063  O   LYS B 544     1841   1531   2244   -198    -59    176       O  
ATOM   8064  CB  LYS B 544     -33.801   9.057 129.138  1.00 10.05           C  
ANISOU 8064  CB  LYS B 544     1217    946   1655   -176     -5    216       C  
ATOM   8065  CG  LYS B 544     -34.144   9.476 127.695  1.00  9.16           C  
ANISOU 8065  CG  LYS B 544     1084    841   1556   -173     14    243       C  
ATOM   8066  CD  LYS B 544     -32.921   9.959 126.938  1.00  9.45           C  
ANISOU 8066  CD  LYS B 544     1097    875   1618   -198      7    261       C  
ATOM   8067  CE  LYS B 544     -33.276  10.473 125.572  1.00  7.12           C  
ANISOU 8067  CE  LYS B 544      787    586   1332   -195     26    289       C  
ATOM   8068  NZ  LYS B 544     -32.074  10.926 124.832  1.00 13.02           N  
ANISOU 8068  NZ  LYS B 544     1511   1333   2104   -219     23    310       N  
ATOM   8069  N   ASN B 545     -32.653   6.220 131.171  1.00 10.21           N  
ANISOU 8069  N   ASN B 545     1239   1005   1635   -177    -41    180       N  
ATOM   8070  CA  ASN B 545     -32.368   5.861 132.567  1.00  9.38           C  
ANISOU 8070  CA  ASN B 545     1161    892   1512   -177    -63    158       C  
ATOM   8071  C   ASN B 545     -33.223   6.677 133.539  1.00 12.69           C  
ANISOU 8071  C   ASN B 545     1624   1284   1914   -164    -58    141       C  
ATOM   8072  O   ASN B 545     -32.778   6.991 134.645  1.00 12.88           O  
ANISOU 8072  O   ASN B 545     1678   1289   1929   -169    -82    122       O  
ATOM   8073  CB  ASN B 545     -30.860   6.001 132.886  1.00  9.95           C  
ANISOU 8073  CB  ASN B 545     1224    956   1602   -202    -97    153       C  
ATOM   8074  CG  ASN B 545     -30.049   4.803 132.475  1.00 27.56           C  
ANISOU 8074  CG  ASN B 545     3419   3214   3837   -207   -105    161       C  
ATOM   8075  OD1 ASN B 545     -30.443   3.657 132.690  1.00 21.98           O  
ANISOU 8075  OD1 ASN B 545     2712   2529   3112   -193    -98    158       O  
ATOM   8076  ND2 ASN B 545     -28.846   5.043 131.991  1.00 24.76           N  
ANISOU 8076  ND2 ASN B 545     3036   2859   3512   -228   -120    169       N  
ATOM   8077  N   SER B 546     -34.470   7.012 133.124  1.00  8.78           N  
ANISOU 8077  N   SER B 546     1134    788   1415   -146    -29    148       N  
ATOM   8078  CA  SER B 546     -35.396   7.772 133.959  1.00  8.06           C  
ANISOU 8078  CA  SER B 546     1081    673   1310   -129    -18    134       C  
ATOM   8079  C   SER B 546     -35.838   6.943 135.143  1.00 10.79           C  
ANISOU 8079  C   SER B 546     1453   1027   1622   -113    -15    119       C  
ATOM   8080  O   SER B 546     -36.196   5.775 134.981  1.00 10.01           O  
ANISOU 8080  O   SER B 546     1336    955   1513   -106     -3    128       O  
ATOM   8081  CB  SER B 546     -36.618   8.206 133.147  1.00 10.36           C  
ANISOU 8081  CB  SER B 546     1364    964   1609   -111     13    148       C  
ATOM   8082  OG  SER B 546     -36.259   9.035 132.053  1.00 15.51           O  
ANISOU 8082  OG  SER B 546     1997   1608   2289   -124     11    164       O  
ATOM   8083  N   ASN B 547     -35.801   7.526 136.336  1.00  7.59           N  
ANISOU 8083  N   ASN B 547     1089    596   1198   -109    -26     97       N  
ATOM   8084  CA  ASN B 547     -36.258   6.849 137.532  1.00  7.61           C  
ANISOU 8084  CA  ASN B 547     1123    605   1165    -93    -20     84       C  
ATOM   8085  C   ASN B 547     -37.513   7.490 138.056  1.00 12.53           C  
ANISOU 8085  C   ASN B 547     1776   1213   1771    -66     10     75       C  
ATOM   8086  O   ASN B 547     -37.506   8.675 138.394  1.00 12.08           O  
ANISOU 8086  O   ASN B 547     1748   1125   1716    -64      4     60       O  
ATOM   8087  CB  ASN B 547     -35.170   6.850 138.614  1.00  6.29           C  
ANISOU 8087  CB  ASN B 547      985    425    981   -105    -59     63       C  
ATOM   8088  CG  ASN B 547     -35.660   6.344 139.957  1.00 21.04           C  
ANISOU 8088  CG  ASN B 547     2894   2295   2806    -86    -53     48       C  
ATOM   8089  OD1 ASN B 547     -36.212   5.249 140.071  1.00 14.18           O  
ANISOU 8089  OD1 ASN B 547     2016   1450   1920    -75    -33     60       O  
ATOM   8090  ND2 ASN B 547     -35.467   7.135 140.996  1.00 12.76           N  
ANISOU 8090  ND2 ASN B 547     1893   1219   1737    -82    -70     24       N  
ATOM   8091  N   TYR B 548     -38.591   6.712 138.161  1.00  9.57           N  
ANISOU 8091  N   TYR B 548     1396    858   1382    -46     42     85       N  
ATOM   8092  CA  TYR B 548     -39.829   7.190 138.758  1.00  9.86           C  
ANISOU 8092  CA  TYR B 548     1460    884   1402    -18     75     78       C  
ATOM   8093  C   TYR B 548     -40.181   6.393 140.011  1.00 13.54           C  
ANISOU 8093  C   TYR B 548     1956   1360   1828     -3     87     70       C  
ATOM   8094  O   TYR B 548     -41.263   6.573 140.578  1.00 13.24           O  
ANISOU 8094  O   TYR B 548     1938   1319   1774     22    120     67       O  
ATOM   8095  CB  TYR B 548     -40.972   7.173 137.740  1.00 10.99           C  
ANISOU 8095  CB  TYR B 548     1569   1039   1569     -5    108     99       C  
ATOM   8096  CG  TYR B 548     -40.945   8.357 136.797  1.00 12.92           C  
ANISOU 8096  CG  TYR B 548     1801   1263   1843    -10    105    103       C  
ATOM   8097  CD1 TYR B 548     -41.513   9.575 137.159  1.00 15.28           C  
ANISOU 8097  CD1 TYR B 548     2130   1533   2144      7    117     91       C  
ATOM   8098  CD2 TYR B 548     -40.341   8.265 135.547  1.00 13.46           C  
ANISOU 8098  CD2 TYR B 548     1833   1342   1940    -30     90    120       C  
ATOM   8099  CE1 TYR B 548     -41.500  10.666 136.293  1.00 16.04           C  
ANISOU 8099  CE1 TYR B 548     2216   1609   2271      2    112     97       C  
ATOM   8100  CE2 TYR B 548     -40.312   9.354 134.676  1.00 14.35           C  
ANISOU 8100  CE2 TYR B 548     1936   1436   2079    -35     87    128       C  
ATOM   8101  CZ  TYR B 548     -40.894  10.554 135.054  1.00 22.00           C  
ANISOU 8101  CZ  TYR B 548     2933   2374   3052    -19     98    117       C  
ATOM   8102  OH  TYR B 548     -40.881  11.629 134.202  1.00 23.47           O  
ANISOU 8102  OH  TYR B 548     3112   2540   3267    -24     94    126       O  
ATOM   8103  N   CYS B 549     -39.226   5.577 140.499  1.00 10.02           N  
ANISOU 8103  N   CYS B 549     1515    925   1366    -18     58     66       N  
ATOM   8104  CA  CYS B 549     -39.388   4.837 141.747  1.00  9.99           C  
ANISOU 8104  CA  CYS B 549     1545    929   1322     -6     63     59       C  
ATOM   8105  C   CYS B 549     -39.026   5.727 142.932  1.00 13.29           C  
ANISOU 8105  C   CYS B 549     2022   1320   1709      1     47     30       C  
ATOM   8106  O   CYS B 549     -37.956   6.346 142.936  1.00 12.26           O  
ANISOU 8106  O   CYS B 549     1899   1170   1587    -18      7     15       O  
ATOM   8107  CB  CYS B 549     -38.554   3.558 141.732  1.00 10.21           C  
ANISOU 8107  CB  CYS B 549     1554    978   1347    -23     39     69       C  
ATOM   8108  SG  CYS B 549     -38.669   2.572 143.252  1.00 14.56           S  
ANISOU 8108  SG  CYS B 549     2147   1539   1846    -10     41     65       S  
ATOM   8109  N   THR B 550     -39.949   5.859 143.900  1.00 10.05           N  
ANISOU 8109  N   THR B 550     1649    905   1263     28     78     22       N  
ATOM   8110  CA  THR B 550     -39.733   6.698 145.080  1.00  9.85           C  
ANISOU 8110  CA  THR B 550     1686    854   1203     40     66     -9       C  
ATOM   8111  C   THR B 550     -39.716   5.841 146.371  1.00 14.47           C  
ANISOU 8111  C   THR B 550     2311   1451   1735     52     67    -13       C  
ATOM   8112  O   THR B 550     -39.820   6.386 147.476  1.00 13.55           O  
ANISOU 8112  O   THR B 550     2252   1318   1578     70     68    -37       O  
ATOM   8113  CB  THR B 550     -40.795   7.827 145.147  1.00 15.55           C  
ANISOU 8113  CB  THR B 550     2427   1555   1925     67    102    -19       C  
ATOM   8114  OG1 THR B 550     -42.090   7.246 145.301  1.00 14.59           O  
ANISOU 8114  OG1 THR B 550     2297   1454   1792     92    155     -2       O  
ATOM   8115  CG2 THR B 550     -40.770   8.726 143.919  1.00 13.27           C  
ANISOU 8115  CG2 THR B 550     2104   1252   1687     55     97    -14       C  
ATOM   8116  N   SER B 551     -39.581   4.496 146.223  1.00 11.75           N  
ANISOU 8116  N   SER B 551     1939   1136   1391     42     67     10       N  
ATOM   8117  CA  SER B 551     -39.531   3.581 147.372  1.00 12.13           C  
ANISOU 8117  CA  SER B 551     2021   1196   1391     52     67     12       C  
ATOM   8118  C   SER B 551     -38.323   3.876 148.260  1.00 18.33           C  
ANISOU 8118  C   SER B 551     2853   1965   2148     42     14    -14       C  
ATOM   8119  O   SER B 551     -37.222   4.116 147.752  1.00 17.47           O  
ANISOU 8119  O   SER B 551     2725   1847   2068     16    -33    -21       O  
ATOM   8120  CB  SER B 551     -39.498   2.128 146.904  1.00 14.17           C  
ANISOU 8120  CB  SER B 551     2237   1484   1665     40     70     41       C  
ATOM   8121  OG  SER B 551     -40.714   1.759 146.278  1.00 21.35           O  
ANISOU 8121  OG  SER B 551     3109   2408   2594     51    119     65       O  
ATOM   8122  N   SER B 552     -38.534   3.893 149.583  1.00 17.12           N  
ANISOU 8122  N   SER B 552     2760   1806   1938     62     20    -29       N  
ATOM   8123  CA  SER B 552     -37.476   4.189 150.548  1.00 17.60           C  
ANISOU 8123  CA  SER B 552     2872   1849   1965     56    -33    -55       C  
ATOM   8124  C   SER B 552     -36.546   2.979 150.763  1.00 22.54           C  
ANISOU 8124  C   SER B 552     3487   2493   2584     38    -71    -42       C  
ATOM   8125  O   SER B 552     -35.374   3.159 151.111  1.00 22.99           O  
ANISOU 8125  O   SER B 552     3561   2536   2637     22   -129    -59       O  
ATOM   8126  CB  SER B 552     -38.078   4.629 151.875  1.00 20.70           C  
ANISOU 8126  CB  SER B 552     3339   2232   2295     88    -12    -76       C  
ATOM   8127  OG  SER B 552     -38.953   3.640 152.391  1.00 25.37           O  
ANISOU 8127  OG  SER B 552     3937   2849   2853    108     35    -53       O  
ATOM   8128  N   LYS B 553     -37.070   1.748 150.561  1.00 17.99           N  
ANISOU 8128  N   LYS B 553     2881   1944   2009     41    -41    -10       N  
ATOM   8129  CA  LYS B 553     -36.282   0.519 150.743  1.00 18.50           C  
ANISOU 8129  CA  LYS B 553     2934   2025   2069     27    -73      5       C  
ATOM   8130  C   LYS B 553     -36.490  -0.457 149.580  1.00 19.53           C  
ANISOU 8130  C   LYS B 553     2996   2178   2247     14    -56     36       C  
ATOM   8131  O   LYS B 553     -37.609  -0.492 149.018  1.00 19.99           O  
ANISOU 8131  O   LYS B 553     3028   2245   2321     25     -5     52       O  
ATOM   8132  CB  LYS B 553     -36.635  -0.157 152.079  1.00 20.87           C  
ANISOU 8132  CB  LYS B 553     3289   2334   2306     48    -60     10       C  
ATOM   8133  OXT LYS B 553     -35.544  -1.208 149.255  1.00 32.22           O  
ANISOU 8133  OXT LYS B 553     4576   3793   3875     -6    -93     45       O  
TER    8134      LYS B 553                                                      
HETATM 8135  S   SO4 B 554     -48.913   2.475 101.382  1.00 35.33           S  
HETATM 8136  O1  SO4 B 554     -49.804   1.325 101.466  1.00 39.60           O  
HETATM 8137  O2  SO4 B 554     -49.707   3.698 101.278  1.00 40.77           O  
HETATM 8138  O3  SO4 B 554     -48.054   2.343 100.190  1.00 40.98           O  
HETATM 8139  O4  SO4 B 554     -48.077   2.540 102.584  1.00 40.05           O  
HETATM 8140  O   HOH A 557     -62.137   9.579  69.733  1.00 13.75           O  
HETATM 8141  O   HOH A 560     -63.860  -2.461  64.687  1.00 15.56           O  
HETATM 8142  O   HOH A 562     -26.731  -1.934  77.752  1.00 31.82           O  
HETATM 8143  O   HOH A 565     -42.048 -10.664  85.526  1.00 10.31           O  
HETATM 8144  O   HOH A 567     -37.357  -6.414  92.865  1.00 25.21           O  
HETATM 8145  O   HOH A 569     -49.452 -11.108  82.803  1.00 16.34           O  
HETATM 8146  O   HOH A 570     -39.934   2.406 102.065  1.00 27.49           O  
HETATM 8147  O   HOH A 572     -63.436   0.079  63.992  1.00 30.48           O  
HETATM 8148  O   HOH A 577     -50.182  10.312  70.831  1.00 12.30           O  
HETATM 8149  O   HOH A 579     -57.883  21.949  71.603  1.00 27.96           O  
HETATM 8150  O   HOH A 580     -62.867  15.527  93.936  1.00 17.40           O  
HETATM 8151  O   HOH A 581     -62.867   9.740  93.017  1.00 16.86           O  
HETATM 8152  O   HOH A 582     -34.432  10.246 107.869  1.00 36.69           O  
HETATM 8153  O   HOH A 584     -57.094   0.911  90.781  1.00 20.25           O  
HETATM 8154  O   HOH A 585     -44.864   4.072 102.047  1.00 26.75           O  
HETATM 8155  O   HOH A 588     -57.508  -5.636  80.617  1.00 37.80           O  
HETATM 8156  O   HOH A 595     -63.088   7.936  98.744  1.00 19.69           O  
HETATM 8157  O   HOH A 597     -60.345  -4.106  88.223  1.00 23.17           O  
HETATM 8158  O   HOH A 598     -35.052  28.773  68.422  1.00 14.91           O  
HETATM 8159  O   HOH A 603     -58.253  14.489  73.433  1.00 13.36           O  
HETATM 8160  O   HOH A 604     -44.560  -3.180  90.194  1.00 16.71           O  
HETATM 8161  O   HOH A 605     -44.763   6.928  68.085  1.00 25.75           O  
HETATM 8162  O   HOH A 608     -23.107   0.176  75.429  1.00 28.24           O  
HETATM 8163  O   HOH A 609     -51.508  34.030  74.440  1.00 21.99           O  
HETATM 8164  O   HOH A 611     -66.537  -3.774  67.315  1.00  8.05           O  
HETATM 8165  O   HOH A 612     -52.024  -6.745  64.167  1.00 13.95           O  
HETATM 8166  O   HOH A 614     -42.650  30.554  88.330  1.00 19.80           O  
HETATM 8167  O   HOH A 616     -56.445  23.079  93.652  1.00 40.00           O  
HETATM 8168  O   HOH A 619     -21.675  -2.482  93.946  1.00 18.24           O  
HETATM 8169  O   HOH A 622     -19.780  19.560  75.109  1.00 10.75           O  
HETATM 8170  O   HOH A 623     -22.937   3.220  68.269  1.00 31.00           O  
HETATM 8171  O   HOH A 624     -55.395  21.131 101.855  1.00 18.47           O  
HETATM 8172  O   HOH A 630     -34.451  10.859 100.658  1.00 19.42           O  
HETATM 8173  O   HOH A 631     -52.956  28.945  90.764  1.00 26.68           O  
HETATM 8174  O   HOH A 632     -58.836  19.579  73.619  1.00 28.19           O  
HETATM 8175  O   HOH A 634     -41.148   1.339  52.546  1.00 16.74           O  
HETATM 8176  O   HOH A 635     -40.732  34.548  77.999  1.00 29.95           O  
HETATM 8177  O   HOH A 637     -52.011  29.222  63.599  1.00 24.14           O  
HETATM 8178  O   HOH A 638     -26.648  -1.642  70.155  1.00 27.38           O  
HETATM 8179  O   HOH A 639     -26.771   1.091  70.788  1.00 17.08           O  
HETATM 8180  O   HOH A 642     -38.970 -11.385  74.442  1.00 14.90           O  
HETATM 8181  O   HOH A 643     -63.219  12.320  95.640  1.00 30.75           O  
HETATM 8182  O   HOH A 645     -33.395  25.372  53.612  1.00 50.91           O  
HETATM 8183  O   HOH A 647     -55.289   1.242  92.864  1.00 29.59           O  
HETATM 8184  O   HOH A 648     -43.601  37.419  77.828  1.00 15.32           O  
HETATM 8185  O   HOH A 651     -57.277  -2.995  88.082  1.00 16.53           O  
HETATM 8186  O   HOH A 653     -43.428  16.316  50.815  1.00 13.03           O  
HETATM 8187  O   HOH A 654     -36.233  33.541  61.675  1.00 21.43           O  
HETATM 8188  O   HOH A 658     -45.692 -16.923  86.058  1.00 28.65           O  
HETATM 8189  O   HOH A 660     -41.393  10.139  80.989  1.00 13.46           O  
HETATM 8190  O   HOH A 661     -55.589  -8.761  70.509  1.00 15.83           O  
HETATM 8191  O   HOH A 663     -52.794  21.601  70.031  1.00 28.60           O  
HETATM 8192  O   HOH A 665     -31.802  35.754  68.810  1.00 20.80           O  
HETATM 8193  O   HOH A 671     -47.061  36.555  78.727  1.00 21.68           O  
HETATM 8194  O   HOH A 672     -29.740  -2.136  66.892  1.00 20.17           O  
HETATM 8195  O   HOH A 673     -38.060  40.114  69.782  1.00 13.26           O  
HETATM 8196  O   HOH A 675     -31.958  29.283  86.416  1.00 16.40           O  
HETATM 8197  O   HOH A 676     -22.496   1.100  81.801  1.00 16.03           O  
HETATM 8198  O   HOH A 677     -41.097  23.630  74.939  1.00 21.90           O  
HETATM 8199  O   HOH A 678     -45.875   0.240  51.904  1.00 20.09           O  
HETATM 8200  O   HOH A 679     -39.765  33.932  64.112  1.00 25.90           O  
HETATM 8201  O   HOH A 681     -31.226   2.884  55.495  1.00  9.29           O  
HETATM 8202  O   HOH A 686     -21.167   7.971  96.255  1.00 22.05           O  
HETATM 8203  O   HOH A 688     -58.803  16.821  49.386  1.00 18.23           O  
HETATM 8204  O   HOH A 689     -31.107  18.547  93.147  1.00 16.18           O  
HETATM 8205  O   HOH A 690     -30.639  31.388  59.291  1.00 10.40           O  
HETATM 8206  O   HOH A 691     -54.389  18.275  53.578  1.00 21.37           O  
HETATM 8207  O   HOH A 694     -17.607   7.951  61.905  1.00 23.29           O  
HETATM 8208  O   HOH A 696     -64.662  18.771  88.663  1.00 36.28           O  
HETATM 8209  O   HOH A 697     -18.621  20.265  57.176  1.00 24.40           O  
HETATM 8210  O   HOH A 698     -18.266  10.142  82.340  1.00 30.69           O  
HETATM 8211  O   HOH A 700     -17.305  16.226  66.374  1.00 18.97           O  
HETATM 8212  O   HOH A 703     -41.152   1.063  96.286  1.00 23.78           O  
HETATM 8213  O   HOH A 705     -62.023   8.139  88.632  1.00 24.25           O  
HETATM 8214  O   HOH A 706     -64.432  10.654  81.566  1.00 20.73           O  
HETATM 8215  O   HOH A 709     -36.522   8.125  52.233  1.00 18.33           O  
HETATM 8216  O   HOH A 710     -24.065  23.054  73.534  1.00 15.54           O  
HETATM 8217  O   HOH A 711     -33.095  12.232  53.894  1.00 17.37           O  
HETATM 8218  O   HOH A 713     -57.507   7.378 111.466  1.00 60.37           O  
HETATM 8219  O   HOH A 714     -59.080  18.525  81.390  1.00 26.98           O  
HETATM 8220  O   HOH A 715     -43.494 -15.634  86.102  1.00 18.72           O  
HETATM 8221  O   HOH A 719     -36.333  36.081  60.573  1.00 20.26           O  
HETATM 8222  O   HOH A 720     -29.899  -5.309  67.037  1.00 16.86           O  
HETATM 8223  O   HOH A 722     -20.342  -1.088  82.631  1.00 29.09           O  
HETATM 8224  O   HOH A 725     -62.858   4.652  98.648  1.00 19.14           O  
HETATM 8225  O   HOH A 727     -53.492  29.421  48.580  1.00 24.55           O  
HETATM 8226  O   HOH A 728     -65.151   9.543  54.230  1.00 35.39           O  
HETATM 8227  O   HOH A 731     -41.198  24.254  43.572  1.00 34.92           O  
HETATM 8228  O   HOH A 732     -18.354   5.797  81.911  1.00 55.85           O  
HETATM 8229  O   HOH A 733     -59.432   0.123  57.959  1.00 18.63           O  
HETATM 8230  O   HOH A 734     -41.967  26.285  90.272  1.00 29.75           O  
HETATM 8231  O   HOH A 738     -31.825  22.950  90.258  1.00 19.67           O  
HETATM 8232  O   HOH A 739     -40.497  37.215  78.378  1.00 31.33           O  
HETATM 8233  O   HOH A 741     -66.464  -6.296  66.583  1.00 20.13           O  
HETATM 8234  O   HOH A 742     -20.877  22.027  78.291  1.00 11.01           O  
HETATM 8235  O   HOH A 743     -54.655  -1.073  98.107  1.00 15.17           O  
HETATM 8236  O   HOH A 746     -21.782  -3.205  91.339  1.00 15.19           O  
HETATM 8237  O   HOH A 748     -43.159  16.316  47.901  1.00 18.09           O  
HETATM 8238  O   HOH A 749     -30.060  22.163  92.774  1.00 19.96           O  
HETATM 8239  O   HOH A 750     -21.252  22.716  73.435  1.00 17.85           O  
HETATM 8240  O   HOH A 751     -42.521  23.658  41.253  1.00 17.88           O  
HETATM 8241  O   HOH A 752     -46.524  25.553  89.660  1.00 21.26           O  
HETATM 8242  O   HOH A 753     -31.217  28.325  69.274  1.00 23.37           O  
HETATM 8243  O   HOH A 754     -25.694  21.222  72.206  1.00 14.58           O  
HETATM 8244  O   HOH A 755     -28.606  21.739  61.278  1.00 17.12           O  
HETATM 8245  O   HOH A 756     -39.296  18.178  81.729  1.00  9.59           O  
HETATM 8246  O   HOH A 757     -32.679   6.566  95.569  1.00  8.67           O  
HETATM 8247  O   HOH A 758     -37.705   5.737  96.314  1.00 19.29           O  
HETATM 8248  O   HOH A 759     -30.373  14.065 100.120  1.00 26.99           O  
HETATM 8249  O   HOH A 760     -32.270  12.170  99.952  1.00 19.61           O  
HETATM 8250  O   HOH A 761     -26.668   9.100  94.250  1.00 28.87           O  
HETATM 8251  O   HOH A 762     -33.060  -2.738  85.477  1.00 14.79           O  
HETATM 8252  O   HOH A 763     -38.183  -3.991  92.726  1.00 11.60           O  
HETATM 8253  O   HOH A 764     -45.311  29.242  83.355  1.00 10.28           O  
HETATM 8254  O   HOH A 765     -37.567  34.099  84.238  1.00  3.00           O  
HETATM 8255  O   HOH A 766     -44.977  35.177  81.162  1.00 15.38           O  
HETATM 8256  O   HOH A 767     -39.454   9.100  58.050  1.00 13.98           O  
HETATM 8257  O   HOH A 768     -53.648   6.903  53.831  1.00 10.60           O  
HETATM 8258  O   HOH A 769     -49.564  28.840  58.835  1.00 29.27           O  
HETATM 8259  O   HOH A 770     -42.030  32.604  63.506  1.00  9.38           O  
HETATM 8260  O   HOH A 771     -42.112  20.008  50.556  1.00 20.57           O  
HETATM 8261  O   HOH A 772     -23.047  27.721  59.540  1.00 14.91           O  
HETATM 8262  O   HOH A 773     -31.740  30.180  57.225  1.00 14.43           O  
HETATM 8263  O   HOH A 774     -33.126  25.875  51.000  1.00 23.48           O  
HETATM 8264  O   HOH A 775     -52.449  22.351  75.380  1.00 26.46           O  
HETATM 8265  O   HOH A 776     -43.565  -9.203  70.258  1.00 17.07           O  
HETATM 8266  O   HOH A 777     -45.281  -7.687  68.072  1.00 15.79           O  
HETATM 8267  O   HOH A 778     -56.234 -11.042  76.841  1.00 11.77           O  
HETATM 8268  O   HOH A 779     -64.833  13.747  58.901  1.00 18.14           O  
HETATM 8269  O   HOH A 780     -59.005   3.056  58.894  1.00  9.33           O  
HETATM 8270  O   HOH A 781     -57.127   8.386  48.862  1.00 23.12           O  
HETATM 8271  O   HOH A 782     -52.064   1.441  49.931  1.00 47.80           O  
HETATM 8272  O   HOH A 783     -44.002  -4.955  55.962  1.00 17.74           O  
HETATM 8273  O   HOH A 784     -42.692  14.983  76.445  1.00 19.46           O  
HETATM 8274  O   HOH A 785     -35.388  -0.177  69.431  1.00 10.70           O  
HETATM 8275  O   HOH A 786     -33.586   3.791  68.795  1.00 18.05           O  
HETATM 8276  O   HOH A 787     -20.690  11.090  81.775  1.00 16.50           O  
HETATM 8277  O   HOH A 788     -29.421  -2.580  85.228  1.00 21.28           O  
HETATM 8278  O   HOH A 789     -28.761  -0.806  80.118  1.00 13.82           O  
HETATM 8279  O   HOH A 836     -44.583   8.095  70.033  1.00 13.25           O  
HETATM 8280  O   HOH A 837     -51.971  18.822  70.804  1.00 15.60           O  
HETATM 8281  O   HOH A 843     -25.352  20.491  64.639  1.00 17.97           O  
HETATM 8282  O   HOH A 846     -33.272  14.110  57.886  1.00 10.50           O  
HETATM 8283  O   HOH A 848     -50.825 -12.184  76.221  1.00 15.22           O  
HETATM 8284  O   HOH A 850     -27.202   4.918  69.904  1.00  8.94           O  
HETATM 8285  O   HOH A 855     -33.195  20.595  54.636  1.00 12.73           O  
HETATM 8286  O   HOH A 856     -53.279  15.245  68.915  1.00 16.20           O  
HETATM 8287  O   HOH A 857     -26.474  17.060  76.143  1.00  7.04           O  
HETATM 8288  O   HOH A 859     -26.113  26.515  78.906  1.00 31.93           O  
HETATM 8289  O   HOH A 862     -35.817  -2.007  71.959  1.00  3.00           O  
HETATM 8290  O   HOH A 864     -42.909  11.050  78.969  1.00 14.95           O  
HETATM 8291  O   HOH A 865     -63.335  20.425  61.566  1.00 20.75           O  
HETATM 8292  O   HOH A 866     -44.201   9.941  81.640  1.00 19.66           O  
HETATM 8293  O   HOH A 868     -26.529  27.737  82.340  1.00  6.88           O  
HETATM 8294  O   HOH A 869     -30.798   0.455  82.203  1.00 15.91           O  
HETATM 8295  O   HOH A 874     -53.963  -9.143  66.697  1.00 42.81           O  
HETATM 8296  O   HOH A 875     -42.602  33.942  75.264  1.00 27.83           O  
HETATM 8297  O   HOH A 877     -50.058  21.493  44.327  1.00 28.87           O  
HETATM 8298  O   HOH A 878     -31.040  -0.543  85.001  1.00  3.18           O  
HETATM 8299  O   HOH A 880     -29.602  24.424  60.264  1.00 14.14           O  
HETATM 8300  O   HOH A 882     -23.129  19.365  72.196  1.00 14.68           O  
HETATM 8301  O   HOH A 883     -22.314  17.390  57.817  1.00 16.06           O  
HETATM 8302  O   HOH A 885     -52.341  26.382  58.033  1.00 24.27           O  
HETATM 8303  O   HOH A 888     -30.696  -3.398  77.202  1.00 23.11           O  
HETATM 8304  O   HOH A 889     -39.358  15.944  80.256  1.00 25.12           O  
HETATM 8305  O   HOH A 890     -44.534   8.309  94.503  1.00  7.93           O  
HETATM 8306  O   HOH A 892     -42.158 -13.551  77.649  1.00 21.64           O  
HETATM 8307  O   HOH A 893     -30.749  13.329  58.553  1.00 14.08           O  
HETATM 8308  O   HOH A 894     -33.491  31.105  69.547  1.00 14.97           O  
HETATM 8309  O   HOH A 896     -40.958  36.255  74.571  1.00 13.84           O  
HETATM 8310  O   HOH A 897     -62.269  13.670  64.514  1.00 24.67           O  
HETATM 8311  O   HOH A 899     -49.843  -9.475  66.103  1.00 10.44           O  
HETATM 8312  O   HOH A 901     -38.248  32.340  62.655  1.00 10.03           O  
HETATM 8313  O   HOH A 903     -33.737   6.727  69.629  1.00 20.59           O  
HETATM 8314  O   HOH A 909     -29.190  27.728  82.962  1.00 27.19           O  
HETATM 8315  O   HOH A 911     -56.552  18.211  72.983  1.00 18.22           O  
HETATM 8316  O   HOH A 916     -22.977  22.629  70.443  1.00 17.87           O  
HETATM 8317  O   HOH A 920     -46.303  13.449  79.581  1.00  7.54           O  
HETATM 8318  O   HOH A 922     -19.733  18.721  77.657  1.00 16.18           O  
HETATM 8319  O   HOH A 923     -32.121  -2.533  65.672  1.00 16.69           O  
HETATM 8320  O   HOH A 924     -31.101  30.004  71.430  1.00 21.23           O  
HETATM 8321  O   HOH A 928     -54.197  13.755  54.343  1.00 26.28           O  
HETATM 8322  O   HOH A 930     -29.577   9.004  63.877  1.00 13.69           O  
HETATM 8323  O   HOH A 931     -45.618   8.975  49.452  1.00 20.79           O  
HETATM 8324  O   HOH A 933     -54.533 -11.674  67.296  1.00 33.80           O  
HETATM 8325  O   HOH A 934     -32.228  24.662  48.832  1.00 23.43           O  
HETATM 8326  O   HOH A 935     -55.000  21.748  57.193  1.00 26.29           O  
HETATM 8327  O   HOH A 936     -39.496  -2.809  76.690  1.00  7.44           O  
HETATM 8328  O   HOH A 937     -32.578  -4.049  63.519  1.00 21.04           O  
HETATM 8329  O   HOH A 940     -23.398  14.846  80.665  1.00 13.44           O  
HETATM 8330  O   HOH A 941     -53.702  19.405  72.954  1.00 13.22           O  
HETATM 8331  O   HOH A 942     -55.073  22.708  82.801  1.00 12.55           O  
HETATM 8332  O   HOH A 945     -62.092  15.792  99.964  1.00 39.38           O  
HETATM 8333  O   HOH A 948     -53.859  22.017  46.556  1.00 34.99           O  
HETATM 8334  O   HOH A 950     -49.278  -2.300  48.665  1.00 29.36           O  
HETATM 8335  O   HOH A 956     -34.848  -0.879  54.493  1.00 20.33           O  
HETATM 8336  O   HOH A 957     -53.105   8.860 100.859  1.00 17.05           O  
HETATM 8337  O   HOH A 959     -63.613  13.697  55.677  1.00 16.03           O  
HETATM 8338  O   HOH A 961     -27.950  15.596  53.241  1.00 25.21           O  
HETATM 8339  O   HOH A 962     -42.957   3.393  75.286  1.00 22.63           O  
HETATM 8340  O   HOH A 964     -38.359   8.088 109.437  1.00 34.22           O  
HETATM 8341  O   HOH A 969     -39.518  -6.374  85.410  1.00 22.04           O  
HETATM 8342  O   HOH A 971     -24.241   9.788  60.570  1.00 14.26           O  
HETATM 8343  O   HOH A 972     -18.853   9.981  74.419  1.00 30.03           O  
HETATM 8344  O   HOH A 974     -53.083  10.129  65.078  1.00  6.17           O  
HETATM 8345  O   HOH A 978     -57.604  -6.038  58.098  1.00 28.17           O  
HETATM 8346  O   HOH A 979     -43.960  13.423  78.304  1.00 26.37           O  
HETATM 8347  O   HOH A 980     -34.559  26.527  71.082  1.00 25.77           O  
HETATM 8348  O   HOH A 981     -58.626   7.546  75.413  1.00  9.84           O  
HETATM 8349  O   HOH A 982     -49.929  -6.045  60.106  1.00 10.42           O  
HETATM 8350  O   HOH A 983     -40.088   4.036  52.636  1.00 20.73           O  
HETATM 8351  O   HOH A 985     -49.499  -0.458  95.837  1.00 32.16           O  
HETATM 8352  O   HOH A 986     -60.236  17.978  71.495  1.00 21.14           O  
HETATM 8353  O   HOH A 987     -59.506   1.815  83.488  1.00 14.08           O  
HETATM 8354  O   HOH A 988     -18.541  19.458  63.092  1.00 40.95           O  
HETATM 8355  O   HOH A 989     -43.944  16.050  79.661  1.00 11.50           O  
HETATM 8356  O   HOH A 990     -24.190  17.801  54.924  1.00 23.35           O  
HETATM 8357  O   HOH A 993     -63.210  12.067  68.817  1.00 31.79           O  
HETATM 8358  O   HOH A 997     -40.519  17.653  62.882  1.00 25.01           O  
HETATM 8359  O   HOH A 998     -48.726   2.546  71.675  1.00  8.21           O  
HETATM 8360  O   HOH A1002     -35.149  14.547  59.774  1.00 11.80           O  
HETATM 8361  O   HOH A1003     -33.138  33.372  62.051  1.00 33.82           O  
HETATM 8362  O   HOH A1005     -21.325  14.929  57.111  1.00 30.02           O  
HETATM 8363  O   HOH A1006     -42.481 -11.943  79.657  1.00  5.33           O  
HETATM 8364  O   HOH A1007     -20.904   3.523  70.738  1.00 10.14           O  
HETATM 8365  O   HOH A1008     -51.421   5.077  59.612  1.00 13.81           O  
HETATM 8366  O   HOH A1016     -45.874  10.270  70.998  1.00 14.79           O  
HETATM 8367  O   HOH A1018     -30.768  19.758  60.992  1.00 19.07           O  
HETATM 8368  O   HOH A1019     -26.042  21.519  62.207  1.00 11.72           O  
HETATM 8369  O   HOH A1021     -55.909  16.820 101.685  1.00 37.48           O  
HETATM 8370  O   HOH A1023     -35.734  22.069  68.241  1.00 14.97           O  
HETATM 8371  O   HOH A1024     -46.843   6.237  75.519  1.00 13.71           O  
HETATM 8372  O   HOH A1025     -47.957  -4.985  62.957  1.00 42.08           O  
HETATM 8373  O   HOH A1026     -36.670   4.742  82.008  1.00 28.85           O  
HETATM 8374  O   HOH A1028     -45.191  17.793  77.699  1.00 22.19           O  
HETATM 8375  O   HOH A1033     -33.165  -6.537  69.225  1.00 36.15           O  
HETATM 8376  O   HOH A1035     -49.266  30.547  48.551  1.00 25.18           O  
HETATM 8377  O   HOH A1037     -30.594  12.601  55.876  1.00 24.41           O  
HETATM 8378  O   HOH A1038     -54.003   3.293  99.841  1.00 32.56           O  
HETATM 8379  O   HOH A1039     -45.022  -5.900  63.623  1.00 12.22           O  
HETATM 8380  O   HOH A1041     -21.515   9.464  74.391  1.00 19.91           O  
HETATM 8381  O   HOH A1043     -41.905   7.444  68.501  1.00  8.13           O  
HETATM 8382  O   HOH A1044     -61.977  14.114  70.850  1.00 14.23           O  
HETATM 8383  O   HOH A1048     -62.958  20.175  64.456  1.00 23.47           O  
HETATM 8384  O   HOH A1051     -54.366 -11.931  74.032  1.00 14.12           O  
HETATM 8385  O   HOH A1052     -52.045  30.138  57.001  1.00 31.22           O  
HETATM 8386  O   HOH A1054     -52.210  21.525 100.752  1.00 38.02           O  
HETATM 8387  O   HOH A1055     -20.751  13.286  74.556  1.00 24.08           O  
HETATM 8388  O   HOH A1056     -20.884  19.106  64.555  1.00 22.65           O  
HETATM 8389  O   HOH A1058     -55.625  19.493  82.378  1.00 11.83           O  
HETATM 8390  O   HOH A1060     -38.892  31.526  83.838  1.00 19.67           O  
HETATM 8391  O   HOH A1063     -45.340  27.810  88.959  1.00 19.50           O  
HETATM 8392  O   HOH A1066     -38.334   3.833 100.430  1.00 32.47           O  
HETATM 8393  O   HOH A1068     -59.713  15.346  71.322  1.00 23.20           O  
HETATM 8394  O   HOH A1071     -35.502   4.683  61.143  1.00  8.41           O  
HETATM 8395  O   HOH A1073     -50.593  12.390  75.237  1.00 14.90           O  
HETATM 8396  O   HOH A1075     -16.022   6.893  63.870  1.00 28.46           O  
HETATM 8397  O   HOH A1080     -45.735   3.535  76.489  1.00 10.49           O  
HETATM 8398  O   HOH A1081     -33.062  28.393  65.487  1.00 15.99           O  
HETATM 8399  O   HOH A1082     -18.677  23.946  64.323  1.00 19.40           O  
HETATM 8400  O   HOH A1083     -52.503  19.894  45.678  1.00 26.15           O  
HETATM 8401  O   HOH A1084     -43.026  25.921  74.924  1.00 37.88           O  
HETATM 8402  O   HOH A1085     -32.723   9.556  68.161  1.00 25.20           O  
HETATM 8403  O   HOH A1086     -26.001  13.811  52.486  1.00 21.40           O  
HETATM 8404  O   HOH A1089     -32.118   3.221  75.508  1.00  7.43           O  
HETATM 8405  O   HOH A1090     -50.923  12.425  72.371  1.00 13.41           O  
HETATM 8406  O   HOH A1091     -43.025  21.371  74.706  1.00 22.93           O  
HETATM 8407  O   HOH A1092     -48.252  18.641  71.758  1.00 10.03           O  
HETATM 8408  O   HOH A1093     -21.393  17.475  85.401  1.00 18.73           O  
HETATM 8409  O   HOH A1094     -24.021  26.240  84.823  1.00  8.29           O  
HETATM 8410  O   HOH A1095     -34.065  -0.680  94.767  1.00 24.45           O  
HETATM 8411  O   HOH A1096     -59.515  17.535  95.958  1.00 13.96           O  
HETATM 8412  O   HOH A1097     -31.898  31.831  54.543  1.00 20.07           O  
HETATM 8413  O   HOH A1098     -58.143  -6.379  66.680  1.00 26.12           O  
HETATM 8414  O   HOH A1099     -44.944   5.769  58.765  1.00 11.52           O  
HETATM 8415  O   HOH A1100     -49.959  16.874  68.739  1.00 20.96           O  
HETATM 8416  O   HOH A1101     -22.059  11.664  72.922  1.00 22.94           O  
HETATM 8417  O   HOH A1102     -18.000   8.384  96.230  1.00 29.75           O  
HETATM 8418  O   HOH A1103     -44.329  -3.495  62.855  1.00 15.51           O  
HETATM 8419  O   HOH A1117     -16.913  10.709  95.226  1.00 20.60           O  
HETATM 8420  O   HOH A1120     -20.869  12.807  58.703  1.00 23.33           O  
HETATM 8421  O   HOH A1122     -32.725  11.728  66.204  1.00 11.04           O  
HETATM 8422  O   HOH A1123     -24.250  22.297  84.974  1.00 15.06           O  
HETATM 8423  O   HOH A1125     -40.932  -8.007  71.888  1.00 15.73           O  
HETATM 8424  O   HOH A1126     -43.011   4.344  60.441  1.00 22.40           O  
HETATM 8425  O   HOH A1127     -44.340   3.517  62.532  1.00 14.19           O  
HETATM 8426  O   HOH A1128     -38.171  23.901  86.834  1.00  9.33           O  
HETATM 8427  O   HOH A1131     -30.931  -4.984  84.211  1.00 11.56           O  
HETATM 8428  O   HOH A1133     -53.240  -7.945  85.555  1.00 26.86           O  
HETATM 8429  O   HOH A1135     -24.382  24.450  86.709  1.00 23.44           O  
HETATM 8430  O   HOH A1137     -51.565  23.490  45.564  1.00 17.76           O  
HETATM 8431  O   HOH A1138     -30.732  -4.079  81.482  1.00 17.82           O  
HETATM 8432  O   HOH A1139     -22.292   3.220  65.598  1.00 21.15           O  
HETATM 8433  O   HOH A1141     -21.623  21.735  84.695  1.00 16.63           O  
HETATM 8434  O   HOH A1143     -58.622  20.907  80.417  1.00 21.92           O  
HETATM 8435  O   HOH A1144     -32.213  -4.960  79.073  1.00 15.01           O  
HETATM 8436  O   HOH A1145     -51.059  30.428  87.172  1.00 19.06           O  
HETATM 8437  O   HOH A1146     -39.427  29.221  46.886  1.00 14.12           O  
HETATM 8438  O   HOH B 555     -40.821  -6.339  94.218  1.00 28.75           O  
HETATM 8439  O   HOH B 556     -52.500 -25.513 154.017  1.00 20.31           O  
HETATM 8440  O   HOH B 558     -39.703 -33.592 126.779  1.00  8.41           O  
HETATM 8441  O   HOH B 559     -55.057 -15.589 100.863  1.00 28.15           O  
HETATM 8442  O   HOH B 561     -28.347 -27.922 145.414  1.00 30.04           O  
HETATM 8443  O   HOH B 563     -59.276   4.044 119.149  1.00  8.32           O  
HETATM 8444  O   HOH B 564     -38.315 -29.796 152.439  1.00 16.02           O  
HETATM 8445  O   HOH B 566     -63.771  -6.988 129.341  1.00 23.52           O  
HETATM 8446  O   HOH B 568     -41.322 -24.862 143.744  1.00 17.72           O  
HETATM 8447  O   HOH B 571     -60.868  -9.428 131.521  1.00  8.02           O  
HETATM 8448  O   HOH B 573     -18.226  -6.244 141.196  1.00 15.32           O  
HETATM 8449  O   HOH B 574     -52.624  17.261 129.034  1.00 11.90           O  
HETATM 8450  O   HOH B 575     -57.367 -13.727 120.341  1.00 11.63           O  
HETATM 8451  O   HOH B 576     -58.577   4.467 109.742  1.00 23.83           O  
HETATM 8452  O   HOH B 578     -36.654 -29.773 140.972  1.00 12.06           O  
HETATM 8453  O   HOH B 583     -47.679 -28.859 154.003  1.00 17.92           O  
HETATM 8454  O   HOH B 586     -22.834   2.021 127.380  1.00 30.44           O  
HETATM 8455  O   HOH B 587     -53.353  -3.423 101.871  1.00 10.57           O  
HETATM 8456  O   HOH B 589     -43.874  -6.553 123.751  1.00 12.42           O  
HETATM 8457  O   HOH B 590     -48.698   5.610 106.734  1.00 16.23           O  
HETATM 8458  O   HOH B 591     -23.014  -9.168 130.573  1.00 14.50           O  
HETATM 8459  O   HOH B 592     -40.307 -32.429 145.573  1.00 25.35           O  
HETATM 8460  O   HOH B 593     -34.339 -11.476 107.449  1.00 44.44           O  
HETATM 8461  O   HOH B 594     -52.900 -31.987 130.244  1.00 21.54           O  
HETATM 8462  O   HOH B 596     -51.641  -2.156 103.711  1.00 17.85           O  
HETATM 8463  O   HOH B 599     -62.408  -2.050 114.679  1.00 15.24           O  
HETATM 8464  O   HOH B 600     -56.139 -16.302 155.862  1.00 19.39           O  
HETATM 8465  O   HOH B 601     -44.286 -31.916 128.032  1.00 13.78           O  
HETATM 8466  O   HOH B 602     -54.275 -24.469 145.342  1.00 23.70           O  
HETATM 8467  O   HOH B 606     -28.489 -12.707 149.687  1.00 15.66           O  
HETATM 8468  O   HOH B 607     -45.559  14.362 133.721  1.00 21.17           O  
HETATM 8469  O   HOH B 610     -54.708 -18.660 132.883  1.00 13.66           O  
HETATM 8470  O   HOH B 613     -26.197 -19.879 117.726  1.00 13.22           O  
HETATM 8471  O   HOH B 615     -55.682  -1.061 100.735  1.00 20.34           O  
HETATM 8472  O   HOH B 617     -45.490 -21.438 127.992  1.00 22.11           O  
HETATM 8473  O   HOH B 618     -58.674 -25.620 138.209  1.00 24.82           O  
HETATM 8474  O   HOH B 620     -59.802  -5.687 151.485  1.00 17.15           O  
HETATM 8475  O   HOH B 621     -51.421  -7.263 127.528  1.00 12.96           O  
HETATM 8476  O   HOH B 625     -57.012   4.860 111.941  1.00 43.67           O  
HETATM 8477  O   HOH B 626     -52.928   0.300 101.456  1.00 12.10           O  
HETATM 8478  O   HOH B 627     -40.267 -32.312 142.716  1.00 14.28           O  
HETATM 8479  O   HOH B 628     -24.973  -7.246 142.257  1.00 13.91           O  
HETATM 8480  O   HOH B 629     -42.658 -10.886  95.230  1.00 29.55           O  
HETATM 8481  O   HOH B 633     -35.642 -25.001 137.622  1.00 13.89           O  
HETATM 8482  O   HOH B 636     -43.862   2.533 105.267  1.00 25.18           O  
HETATM 8483  O   HOH B 640     -27.701  -7.379 107.841  1.00 29.75           O  
HETATM 8484  O   HOH B 641     -56.683 -27.592 138.722  1.00 29.66           O  
HETATM 8485  O   HOH B 644     -41.942   1.801 143.877  1.00 16.40           O  
HETATM 8486  O   HOH B 646     -17.644  -8.882 107.421  1.00 19.03           O  
HETATM 8487  O   HOH B 649     -57.001 -15.906 145.592  1.00 14.40           O  
HETATM 8488  O   HOH B 650     -54.349 -21.719 152.033  1.00 20.92           O  
HETATM 8489  O   HOH B 652     -40.706 -11.802 123.236  1.00 11.44           O  
HETATM 8490  O   HOH B 655     -38.680   9.867 140.763  1.00 21.24           O  
HETATM 8491  O   HOH B 656     -57.045   8.900 114.586  1.00 19.53           O  
HETATM 8492  O   HOH B 657     -49.889 -34.131 124.518  1.00 18.92           O  
HETATM 8493  O   HOH B 659     -45.019  -8.689 124.655  1.00 18.38           O  
HETATM 8494  O   HOH B 662     -48.749 -18.095 158.569  1.00 19.85           O  
HETATM 8495  O   HOH B 664     -54.471  14.234 132.093  1.00 21.27           O  
HETATM 8496  O   HOH B 666     -58.809  -3.135  97.821  1.00 24.63           O  
HETATM 8497  O   HOH B 667     -57.092  12.184 135.862  1.00 23.61           O  
HETATM 8498  O   HOH B 668     -29.547   8.958 130.207  1.00 21.38           O  
HETATM 8499  O   HOH B 669     -50.847 -20.321 158.972  1.00 29.68           O  
HETATM 8500  O   HOH B 670     -49.413   8.550 109.636  1.00 34.30           O  
HETATM 8501  O   HOH B 674     -53.722 -15.632 103.260  1.00 12.65           O  
HETATM 8502  O   HOH B 680     -49.069 -30.963 137.723  1.00 19.03           O  
HETATM 8503  O   HOH B 682     -51.355 -11.513 135.155  1.00 24.40           O  
HETATM 8504  O   HOH B 683     -17.954  -9.812 141.482  1.00 29.50           O  
HETATM 8505  O   HOH B 684     -49.163 -31.472 152.903  1.00 20.08           O  
HETATM 8506  O   HOH B 685     -39.346 -29.648 141.010  1.00 12.37           O  
HETATM 8507  O   HOH B 687     -58.562 -22.129 127.159  1.00 24.62           O  
HETATM 8508  O   HOH B 692     -21.840   1.760 140.092  1.00 19.76           O  
HETATM 8509  O   HOH B 693     -29.726 -24.145 126.996  1.00 21.42           O  
HETATM 8510  O   HOH B 695     -23.091 -23.485 147.191  1.00 29.88           O  
HETATM 8511  O   HOH B 699     -21.508  -5.840 106.768  1.00 17.29           O  
HETATM 8512  O   HOH B 701     -16.686  -5.317 139.061  1.00 26.06           O  
HETATM 8513  O   HOH B 702     -41.357   2.522 150.295  1.00 25.07           O  
HETATM 8514  O   HOH B 704     -33.523 -19.371 112.514  1.00 19.18           O  
HETATM 8515  O   HOH B 707     -42.387 -33.474 126.452  1.00 17.09           O  
HETATM 8516  O   HOH B 708     -55.359 -13.815 129.842  1.00 18.49           O  
HETATM 8517  O   HOH B 712     -60.841   9.873 129.997  1.00 28.42           O  
HETATM 8518  O   HOH B 716     -60.969  -7.683 153.007  1.00 26.58           O  
HETATM 8519  O   HOH B 717     -34.599 -28.022 141.035  1.00 28.42           O  
HETATM 8520  O   HOH B 718     -23.612 -19.638 118.193  1.00 13.28           O  
HETATM 8521  O   HOH B 721     -65.638 -11.535 135.875  1.00 27.74           O  
HETATM 8522  O   HOH B 723     -18.693  -2.945 123.041  1.00 31.25           O  
HETATM 8523  O   HOH B 724     -61.157 -13.162 126.530  1.00 30.86           O  
HETATM 8524  O   HOH B 726     -48.581   7.250 154.044  1.00 29.18           O  
HETATM 8525  O   HOH B 729     -50.659   6.465 152.654  1.00 25.61           O  
HETATM 8526  O   HOH B 730     -58.261 -20.108 114.484  1.00 37.06           O  
HETATM 8527  O   HOH B 735     -28.620 -26.040 140.035  1.00 20.25           O  
HETATM 8528  O   HOH B 736     -37.302 -12.003 102.285  1.00 25.26           O  
HETATM 8529  O   HOH B 737     -59.751   0.505 106.563  1.00 23.04           O  
HETATM 8530  O   HOH B 740     -39.541 -34.806 135.435  1.00 15.58           O  
HETATM 8531  O   HOH B 744     -35.197 -13.441 101.614  1.00 27.84           O  
HETATM 8532  O   HOH B 745     -51.351 -16.424 158.095  1.00  8.44           O  
HETATM 8533  O   HOH B 747     -44.502 -14.798 154.641  1.00 28.69           O  
HETATM 8534  O   HOH B 790     -42.269 -18.855 108.418  1.00 25.99           O  
HETATM 8535  O   HOH B 791     -40.901 -14.103 121.350  1.00 12.90           O  
HETATM 8536  O   HOH B 792     -41.683 -27.218 118.883  1.00 10.36           O  
HETATM 8537  O   HOH B 793     -35.803 -26.474 125.300  1.00  9.17           O  
HETATM 8538  O   HOH B 794     -46.605 -23.735 121.692  1.00 14.11           O  
HETATM 8539  O   HOH B 795     -31.862 -24.584 119.809  1.00 13.27           O  
HETATM 8540  O   HOH B 796     -33.873  -5.623 134.641  1.00 12.07           O  
HETATM 8541  O   HOH B 797     -27.268 -17.776 137.922  1.00  8.99           O  
HETATM 8542  O   HOH B 798     -24.994 -20.023 132.271  1.00 17.14           O  
HETATM 8543  O   HOH B 799     -23.289 -16.922 137.576  1.00 12.41           O  
HETATM 8544  O   HOH B 800     -22.510  -7.223 128.443  1.00 13.28           O  
HETATM 8545  O   HOH B 801     -19.049  -9.708 129.642  1.00 16.83           O  
HETATM 8546  O   HOH B 802     -22.208 -10.960 128.587  1.00 12.81           O  
HETATM 8547  O   HOH B 803     -32.698 -19.625 115.118  1.00  8.12           O  
HETATM 8548  O   HOH B 804     -57.089 -10.220 101.458  1.00 16.13           O  
HETATM 8549  O   HOH B 805     -45.043  -5.262 121.147  1.00 10.29           O  
HETATM 8550  O   HOH B 806     -36.434  -0.976 121.027  1.00 16.61           O  
HETATM 8551  O   HOH B 807     -40.792  -2.304 103.546  1.00 29.67           O  
HETATM 8552  O   HOH B 808     -32.902  -3.213 107.495  1.00 10.07           O  
HETATM 8553  O   HOH B 809     -31.874   7.898 112.930  1.00 17.72           O  
HETATM 8554  O   HOH B 810     -31.057   4.193 110.446  1.00 10.30           O  
HETATM 8555  O   HOH B 811     -56.700 -16.962 119.833  1.00 16.95           O  
HETATM 8556  O   HOH B 812     -54.431  -9.595 133.907  1.00  4.15           O  
HETATM 8557  O   HOH B 813     -58.121 -12.381 129.829  1.00 14.09           O  
HETATM 8558  O   HOH B 814     -65.057 -13.955 141.329  1.00 11.56           O  
HETATM 8559  O   HOH B 815     -64.342 -13.725 138.714  1.00  9.78           O  
HETATM 8560  O   HOH B 816     -46.505  -4.209 153.305  1.00 21.46           O  
HETATM 8561  O   HOH B 817     -51.539  -0.091 142.951  1.00 12.84           O  
HETATM 8562  O   HOH B 818     -59.155   5.856 144.696  1.00 13.73           O  
HETATM 8563  O   HOH B 819     -54.972  11.978 145.985  1.00 16.49           O  
HETATM 8564  O   HOH B 820     -45.414   4.309 151.380  1.00 14.38           O  
HETATM 8565  O   HOH B 821     -43.231   8.241 140.404  1.00 23.30           O  
HETATM 8566  O   HOH B 822     -47.164   9.940 139.475  1.00  5.09           O  
HETATM 8567  O   HOH B 823     -44.538  10.348 139.491  1.00  9.99           O  
HETATM 8568  O   HOH B 824     -46.864  -5.282 132.241  1.00 10.90           O  
HETATM 8569  O   HOH B 825     -34.187  -3.371 133.135  1.00  4.46           O  
HETATM 8570  O   HOH B 826     -32.497   0.115 127.367  1.00 10.98           O  
HETATM 8571  O   HOH B 827     -45.737   1.302 126.524  1.00 14.15           O  
HETATM 8572  O   HOH B 828     -43.271   1.055 127.556  1.00  7.37           O  
HETATM 8573  O   HOH B 829     -31.391  -9.197 146.882  1.00 16.69           O  
HETATM 8574  O   HOH B 830     -31.746 -10.047 144.336  1.00  4.28           O  
HETATM 8575  O   HOH B 831     -30.461   6.861 125.728  1.00 11.92           O  
HETATM 8576  O   HOH B 832     -34.367   4.027 148.626  1.00 17.27           O  
HETATM 8577  O   HOH B 833     -48.670  14.650 136.255  1.00 12.20           O  
HETATM 8578  O   HOH B 834     -52.850  14.401 136.458  1.00 20.95           O  
HETATM 8579  O   HOH B 835     -36.788  -9.771 103.755  1.00 15.17           O  
HETATM 8580  O   HOH B 838     -45.864 -29.565 127.501  1.00 13.50           O  
HETATM 8581  O   HOH B 839     -50.445 -31.557 124.076  1.00 17.36           O  
HETATM 8582  O   HOH B 840     -51.486 -12.069 132.615  1.00 14.71           O  
HETATM 8583  O   HOH B 841     -61.472 -11.954 131.464  1.00  8.99           O  
HETATM 8584  O   HOH B 842     -27.937 -14.188 126.424  1.00 10.22           O  
HETATM 8585  O   HOH B 844     -35.655   5.672 130.596  1.00  8.36           O  
HETATM 8586  O   HOH B 845     -27.629  -2.248 132.834  1.00  8.60           O  
HETATM 8587  O   HOH B 847     -45.023  -3.104 133.329  1.00 16.18           O  
HETATM 8588  O   HOH B 849     -30.702   3.795 118.002  1.00  3.00           O  
HETATM 8589  O   HOH B 851     -45.328 -11.674 122.741  1.00  8.79           O  
HETATM 8590  O   HOH B 852     -21.649 -16.855 125.515  1.00 19.12           O  
HETATM 8591  O   HOH B 853     -29.370   6.043 117.377  1.00 36.14           O  
HETATM 8592  O   HOH B 854     -42.481  -2.953 134.230  1.00 13.28           O  
HETATM 8593  O   HOH B 858     -36.074  12.831 120.485  1.00  7.80           O  
HETATM 8594  O   HOH B 860     -45.062  -3.815 108.233  1.00  4.52           O  
HETATM 8595  O   HOH B 861     -58.992  -1.750 127.615  1.00 11.58           O  
HETATM 8596  O   HOH B 863     -54.984  16.836 125.559  1.00 23.11           O  
HETATM 8597  O   HOH B 867     -41.281 -28.127 139.790  1.00  8.42           O  
HETATM 8598  O   HOH B 870     -40.426  -5.326 144.626  1.00 18.72           O  
HETATM 8599  O   HOH B 871     -47.025  -1.268 127.328  1.00  8.93           O  
HETATM 8600  O   HOH B 872     -40.473 -20.002 115.906  1.00  9.96           O  
HETATM 8601  O   HOH B 873     -47.351  -8.562 123.279  1.00 13.92           O  
HETATM 8602  O   HOH B 876     -26.838 -18.443 112.284  1.00 34.92           O  
HETATM 8603  O   HOH B 879     -31.821 -21.319 142.394  1.00 17.10           O  
HETATM 8604  O   HOH B 881     -52.271  15.961 124.914  1.00 17.88           O  
HETATM 8605  O   HOH B 884     -40.889  15.967 123.119  1.00 10.22           O  
HETATM 8606  O   HOH B 886     -62.655  -3.136 133.178  1.00 23.19           O  
HETATM 8607  O   HOH B 887     -30.479   2.379 120.920  1.00  8.86           O  
HETATM 8608  O   HOH B 891     -33.962  -0.689 134.132  1.00 26.86           O  
HETATM 8609  O   HOH B 895     -47.810 -24.362 119.424  1.00 11.96           O  
HETATM 8610  O   HOH B 898     -48.339   2.305 130.760  1.00  7.29           O  
HETATM 8611  O   HOH B 900     -44.973 -28.105 139.194  1.00 14.92           O  
HETATM 8612  O   HOH B 902     -51.013  12.011 138.982  1.00 23.20           O  
HETATM 8613  O   HOH B 904     -20.957  -1.184 132.024  1.00 16.88           O  
HETATM 8614  O   HOH B 905     -31.912 -24.906 128.232  1.00 14.17           O  
HETATM 8615  O   HOH B 906     -49.106  11.176 142.806  1.00 11.20           O  
HETATM 8616  O   HOH B 907     -44.453  -4.192  98.247  1.00 21.54           O  
HETATM 8617  O   HOH B 908     -51.820  -7.514 130.279  1.00 14.03           O  
HETATM 8618  O   HOH B 910     -35.156 -17.142 148.691  1.00 18.03           O  
HETATM 8619  O   HOH B 912     -23.025 -15.087 117.445  1.00 16.43           O  
HETATM 8620  O   HOH B 913     -32.398   6.169 117.293  1.00 14.91           O  
HETATM 8621  O   HOH B 914     -38.935   6.871 126.026  1.00 10.20           O  
HETATM 8622  O   HOH B 915     -47.709  16.122 120.406  1.00 16.84           O  
HETATM 8623  O   HOH B 917     -40.526  14.730 117.363  1.00 17.43           O  
HETATM 8624  O   HOH B 918     -30.585 -18.814 141.550  1.00 23.57           O  
HETATM 8625  O   HOH B 919     -31.550   8.304 123.700  1.00 17.43           O  
HETATM 8626  O   HOH B 921     -58.903   2.846 143.794  1.00 17.55           O  
HETATM 8627  O   HOH B 925     -26.459 -23.926 118.014  1.00 18.19           O  
HETATM 8628  O   HOH B 926     -37.714 -18.183 134.362  1.00  6.67           O  
HETATM 8629  O   HOH B 927     -44.071  12.294 134.684  1.00 19.51           O  
HETATM 8630  O   HOH B 929     -39.835  12.114 131.825  1.00 17.42           O  
HETATM 8631  O   HOH B 932     -55.325  -8.262 148.598  1.00 17.84           O  
HETATM 8632  O   HOH B 938     -34.643 -26.807 145.469  1.00 14.52           O  
HETATM 8633  O   HOH B 939     -44.981 -16.761 127.877  1.00 17.00           O  
HETATM 8634  O   HOH B 943     -43.976  21.255 116.612  1.00 17.98           O  
HETATM 8635  O   HOH B 944     -46.715 -12.805 124.854  1.00  8.99           O  
HETATM 8636  O   HOH B 946     -33.596 -26.745 131.006  1.00 19.52           O  
HETATM 8637  O   HOH B 947     -45.260  -1.124 143.854  1.00 25.48           O  
HETATM 8638  O   HOH B 949     -28.542   3.696 122.449  1.00 11.79           O  
HETATM 8639  O   HOH B 951     -48.542 -20.406 112.927  1.00 15.02           O  
HETATM 8640  O   HOH B 952     -53.895  -4.807 137.769  1.00 11.34           O  
HETATM 8641  O   HOH B 953     -63.125  -7.687 138.015  1.00  9.91           O  
HETATM 8642  O   HOH B 954     -43.121  -0.293 142.394  1.00 10.61           O  
HETATM 8643  O   HOH B 955     -52.364 -24.133 142.675  1.00 29.76           O  
HETATM 8644  O   HOH B 958     -31.686   7.271 139.256  1.00 15.44           O  
HETATM 8645  O   HOH B 960     -44.309 -17.618  99.083  1.00 21.37           O  
HETATM 8646  O   HOH B 963     -33.611  -8.409 136.690  1.00  8.09           O  
HETATM 8647  O   HOH B 965     -35.810  -1.149 141.676  1.00 10.91           O  
HETATM 8648  O   HOH B 966     -63.116   2.842 136.783  1.00 23.76           O  
HETATM 8649  O   HOH B 967     -55.644 -23.324 112.511  1.00 47.64           O  
HETATM 8650  O   HOH B 968     -29.869   8.286 118.897  1.00 19.41           O  
HETATM 8651  O   HOH B 970     -44.704 -29.358 115.087  1.00 30.60           O  
HETATM 8652  O   HOH B 973     -33.571   3.931 108.179  1.00 31.84           O  
HETATM 8653  O   HOH B 975     -28.247 -18.388 140.252  1.00 11.64           O  
HETATM 8654  O   HOH B 976     -30.095   7.437 121.665  1.00 15.51           O  
HETATM 8655  O   HOH B 977     -24.071 -14.815 145.211  1.00 22.80           O  
HETATM 8656  O   HOH B 984     -63.337  -2.488 110.088  1.00 16.78           O  
HETATM 8657  O   HOH B 991     -35.172   4.067 133.349  1.00 21.18           O  
HETATM 8658  O   HOH B 992     -36.451 -10.990 142.982  1.00 10.26           O  
HETATM 8659  O   HOH B 994     -61.029 -11.422 106.870  1.00 13.01           O  
HETATM 8660  O   HOH B 995     -41.219 -16.240 122.923  1.00 18.39           O  
HETATM 8661  O   HOH B 996     -26.239 -20.550 129.267  1.00 15.48           O  
HETATM 8662  O   HOH B 999     -22.469   1.222 129.941  1.00 30.96           O  
HETATM 8663  O   HOH B1000     -61.304  10.540 138.663  1.00 36.25           O  
HETATM 8664  O   HOH B1001     -54.480 -15.887 132.835  1.00 16.88           O  
HETATM 8665  O   HOH B1004     -25.677 -25.419 143.402  1.00 11.37           O  
HETATM 8666  O   HOH B1009     -65.109  -3.571 121.990  1.00 46.76           O  
HETATM 8667  O   HOH B1010     -34.748 -10.660 144.929  1.00  9.14           O  
HETATM 8668  O   HOH B1011     -21.996 -18.504 127.657  1.00 33.29           O  
HETATM 8669  O   HOH B1012     -34.417 -25.472 133.127  1.00 20.51           O  
HETATM 8670  O   HOH B1013     -30.291  -6.051 139.043  1.00  7.05           O  
HETATM 8671  O   HOH B1014     -41.869 -13.546 139.865  1.00  9.51           O  
HETATM 8672  O   HOH B1015     -25.010 -16.852 130.270  1.00  8.03           O  
HETATM 8673  O   HOH B1017     -35.615  -7.834 101.974  1.00 25.95           O  
HETATM 8674  O   HOH B1020     -35.408 -21.783 149.189  1.00 19.98           O  
HETATM 8675  O   HOH B1022     -41.736 -21.648 111.033  1.00 22.14           O  
HETATM 8676  O   HOH B1027     -38.775  10.378 117.197  1.00 23.10           O  
HETATM 8677  O   HOH B1029     -48.203 -23.119 113.478  1.00 14.80           O  
HETATM 8678  O   HOH B1030     -52.219  12.998 116.950  1.00 11.67           O  
HETATM 8679  O   HOH B1031     -44.717 -15.013  94.139  1.00 18.53           O  
HETATM 8680  O   HOH B1032     -46.319  13.714 137.210  1.00 22.94           O  
HETATM 8681  O   HOH B1034     -50.579  -5.135 131.742  1.00  9.79           O  
HETATM 8682  O   HOH B1036     -36.864 -27.449 133.047  1.00  8.39           O  
HETATM 8683  O   HOH B1040     -35.213 -28.846 134.682  1.00 22.73           O  
HETATM 8684  O   HOH B1042     -56.635 -24.060 154.203  1.00 24.15           O  
HETATM 8685  O   HOH B1045     -22.809 -19.902 124.485  1.00 26.87           O  
HETATM 8686  O   HOH B1046     -32.561 -16.463 141.803  1.00 10.62           O  
HETATM 8687  O   HOH B1047     -63.961  -8.968 108.734  1.00 28.44           O  
HETATM 8688  O   HOH B1049     -52.348   5.155 100.844  1.00 33.02           O  
HETATM 8689  O   HOH B1050     -37.888  -1.555 106.625  1.00 16.99           O  
HETATM 8690  O   HOH B1053     -53.711 -32.091 149.484  1.00 27.67           O  
HETATM 8691  O   HOH B1057     -45.879 -24.042 115.296  1.00 17.63           O  
HETATM 8692  O   HOH B1059     -32.312 -15.165 109.790  1.00 14.67           O  
HETATM 8693  O   HOH B1061     -46.061  -1.497  99.865  1.00 15.27           O  
HETATM 8694  O   HOH B1062     -58.047 -18.353 137.433  1.00 37.66           O  
HETATM 8695  O   HOH B1064     -27.588 -18.635 130.613  1.00 13.84           O  
HETATM 8696  O   HOH B1065     -54.571 -17.450 128.026  1.00 25.54           O  
HETATM 8697  O   HOH B1067     -28.656 -23.668 124.026  1.00  9.96           O  
HETATM 8698  O   HOH B1069     -43.813 -10.799 126.185  1.00 26.26           O  
HETATM 8699  O   HOH B1070     -24.705 -12.217 122.223  1.00 11.30           O  
HETATM 8700  O   HOH B1072     -60.322   1.083 126.610  1.00 16.49           O  
HETATM 8701  O   HOH B1074     -19.875 -18.221 139.027  1.00 29.11           O  
HETATM 8702  O   HOH B1076     -41.841  13.867 132.037  1.00 20.66           O  
HETATM 8703  O   HOH B1077     -37.885 -25.240 134.346  1.00 18.10           O  
HETATM 8704  O   HOH B1078     -55.087 -30.527 141.410  1.00 32.39           O  
HETATM 8705  O   HOH B1079     -52.840  -2.726  92.464  1.00 35.10           O  
HETATM 8706  O   HOH B1087     -44.475   0.996 139.894  1.00 30.83           O  
HETATM 8707  O   HOH B1088     -26.207 -22.103 116.249  1.00 15.63           O  
HETATM 8708  O   HOH B1104     -37.104 -22.788 131.725  1.00  7.70           O  
HETATM 8709  O   HOH B1105     -32.693   8.041 108.435  1.00 24.24           O  
HETATM 8710  O   HOH B1106     -48.263 -30.536 121.597  1.00 15.90           O  
HETATM 8711  O   HOH B1107     -54.155  -1.614 148.839  1.00 16.71           O  
HETATM 8712  O   HOH B1108     -56.343 -13.119 148.973  1.00 19.81           O  
HETATM 8713  O   HOH B1109     -55.061 -28.490 128.789  1.00 18.90           O  
HETATM 8714  O   HOH B1110     -55.812 -28.990 132.059  1.00 28.41           O  
HETATM 8715  O   HOH B1111     -49.897 -13.494 131.038  1.00 12.19           O  
HETATM 8716  O   HOH B1112     -53.542 -13.564 131.842  1.00 12.64           O  
HETATM 8717  O   HOH B1113     -40.261   0.093 150.437  1.00 10.72           O  
HETATM 8718  O   HOH B1114     -31.866   6.172 136.871  1.00 10.68           O  
HETATM 8719  O   HOH B1115     -32.819   2.335 151.269  1.00 20.67           O  
HETATM 8720  O   HOH B1116     -26.253   1.640 132.310  1.00 26.04           O  
HETATM 8721  O   HOH B1118     -25.891 -15.159 148.084  1.00 17.28           O  
HETATM 8722  O   HOH B1119     -59.308  -8.627 129.478  1.00  7.15           O  
HETATM 8723  O   HOH B1121     -41.374 -13.077  95.284  1.00 20.98           O  
HETATM 8724  O   HOH B1124     -61.884  -4.183 129.852  1.00 19.41           O  
HETATM 8725  O   HOH B1129     -55.063 -20.968 144.618  1.00 16.49           O  
HETATM 8726  O   HOH B1130     -56.397 -18.914 145.564  1.00 21.26           O  
HETATM 8727  O   HOH B1132     -63.594  -5.613 133.300  1.00 21.04           O  
HETATM 8728  O   HOH B1134     -48.491  -4.828 130.161  1.00 17.91           O  
HETATM 8729  O   HOH B1136     -32.072  10.380 133.183  1.00 25.62           O  
HETATM 8730  O   HOH B1140     -54.823 -23.865 138.969  1.00 18.76           O  
HETATM 8731  O   HOH B1142     -22.722 -12.684 146.232  1.00 20.73           O  
CONECT    3    6                                                                
CONECT    6    3    7                                                           
CONECT    7    6    8   10                                                      
CONECT    8    7    9   11                                                      
CONECT    9    8                                                                
CONECT   10    7                                                                
CONECT   11    8                                                                
CONECT  276  283                                                                
CONECT  283  276  284                                                           
CONECT  284  283  285  287                                                      
CONECT  285  284  286  291                                                      
CONECT  286  285                                                                
CONECT  287  284  288                                                           
CONECT  288  287  289                                                           
CONECT  289  288  290                                                           
CONECT  290  289                                                                
CONECT  291  285                                                                
CONECT  871  876                                                                
CONECT  876  871  877                                                           
CONECT  877  876  878  880                                                      
CONECT  878  877  879  884                                                      
CONECT  879  878                                                                
CONECT  880  877  881                                                           
CONECT  881  880  882                                                           
CONECT  882  881  883                                                           
CONECT  883  882                                                                
CONECT  884  878                                                                
CONECT 1695 1705                                                                
CONECT 1705 1695 1706                                                           
CONECT 1706 1705 1707 1709                                                      
CONECT 1707 1706 1708 1713                                                      
CONECT 1708 1707                                                                
CONECT 1709 1706 1710                                                           
CONECT 1710 1709 1711                                                           
CONECT 1711 1710 1712                                                           
CONECT 1712 1711                                                                
CONECT 1713 1707                                                                
CONECT 1828 1833                                                                
CONECT 1833 1828 1834                                                           
CONECT 1834 1833 1835 1837                                                      
CONECT 1835 1834 1836 1841                                                      
CONECT 1836 1835                                                                
CONECT 1837 1834 1838                                                           
CONECT 1838 1837 1839                                                           
CONECT 1839 1838 1840                                                           
CONECT 1840 1839                                                                
CONECT 1841 1835                                                                
CONECT 1917 1921                                                                
CONECT 1921 1917 1922                                                           
CONECT 1922 1921 1923 1925                                                      
CONECT 1923 1922 1924 1929                                                      
CONECT 1924 1923                                                                
CONECT 1925 1922 1926                                                           
CONECT 1926 1925 1927                                                           
CONECT 1927 1926 1928                                                           
CONECT 1928 1927                                                                
CONECT 1929 1923                                                                
CONECT 3686 3695                                                                
CONECT 3695 3686 3696                                                           
CONECT 3696 3695 3697 3699                                                      
CONECT 3697 3696 3698 3703                                                      
CONECT 3698 3697                                                                
CONECT 3699 3696 3700                                                           
CONECT 3700 3699 3701                                                           
CONECT 3701 3700 3702                                                           
CONECT 3702 3701                                                                
CONECT 3703 3697                                                                
CONECT 3858 3862                                                                
CONECT 3862 3858 3863                                                           
CONECT 3863 3862 3864 3866                                                      
CONECT 3864 3863 3865 3870                                                      
CONECT 3865 3864                                                                
CONECT 3866 3863 3867                                                           
CONECT 3867 3866 3868                                                           
CONECT 3868 3867 3869                                                           
CONECT 3869 3868                                                                
CONECT 3870 3864                                                                
CONECT 4071 4074                                                                
CONECT 4074 4071 4075                                                           
CONECT 4075 4074 4076 4078                                                      
CONECT 4076 4075 4077 4079                                                      
CONECT 4077 4076                                                                
CONECT 4078 4075                                                                
CONECT 4079 4076                                                                
CONECT 4336 4343                                                                
CONECT 4343 4336 4344                                                           
CONECT 4344 4343 4345 4347                                                      
CONECT 4345 4344 4346 4351                                                      
CONECT 4346 4345                                                                
CONECT 4347 4344 4348                                                           
CONECT 4348 4347 4349                                                           
CONECT 4349 4348 4350                                                           
CONECT 4350 4349                                                                
CONECT 4351 4345                                                                
CONECT 4929 4934                                                                
CONECT 4934 4929 4935                                                           
CONECT 4935 4934 4936 4938                                                      
CONECT 4936 4935 4937 4942                                                      
CONECT 4937 4936                                                                
CONECT 4938 4935 4939                                                           
CONECT 4939 4938 4940                                                           
CONECT 4940 4939 4941                                                           
CONECT 4941 4940                                                                
CONECT 4942 4936                                                                
CONECT 5769 5779                                                                
CONECT 5779 5769 5780                                                           
CONECT 5780 5779 5781 5783                                                      
CONECT 5781 5780 5782 5787                                                      
CONECT 5782 5781                                                                
CONECT 5783 5780 5784                                                           
CONECT 5784 5783 5785                                                           
CONECT 5785 5784 5786                                                           
CONECT 5786 5785                                                                
CONECT 5787 5781                                                                
CONECT 5902 5907                                                                
CONECT 5907 5902 5908                                                           
CONECT 5908 5907 5909 5911                                                      
CONECT 5909 5908 5910 5915                                                      
CONECT 5910 5909                                                                
CONECT 5911 5908 5912                                                           
CONECT 5912 5911 5913                                                           
CONECT 5913 5912 5914                                                           
CONECT 5914 5913                                                                
CONECT 5915 5909                                                                
CONECT 5991 5995                                                                
CONECT 5995 5991 5996                                                           
CONECT 5996 5995 5997 5999                                                      
CONECT 5997 5996 5998 6003                                                      
CONECT 5998 5997                                                                
CONECT 5999 5996 6000                                                           
CONECT 6000 5999 6001                                                           
CONECT 6001 6000 6002                                                           
CONECT 6002 6001                                                                
CONECT 6003 5997                                                                
CONECT 7767 7776                                                                
CONECT 7776 7767 7777                                                           
CONECT 7777 7776 7778 7780                                                      
CONECT 7778 7777 7779 7784                                                      
CONECT 7779 7778                                                                
CONECT 7780 7777 7781                                                           
CONECT 7781 7780 7782                                                           
CONECT 7782 7781 7783                                                           
CONECT 7783 7782                                                                
CONECT 7784 7778                                                                
CONECT 7932 7936                                                                
CONECT 7936 7932 7937                                                           
CONECT 7937 7936 7938 7940                                                      
CONECT 7938 7937 7939 7944                                                      
CONECT 7939 7938                                                                
CONECT 7940 7937 7941                                                           
CONECT 7941 7940 7942                                                           
CONECT 7942 7941 7943                                                           
CONECT 7943 7942                                                                
CONECT 7944 7938                                                                
CONECT 8135 8136 8137 8138 8139                                                 
CONECT 8136 8135                                                                
CONECT 8137 8135                                                                
CONECT 8138 8135                                                                
CONECT 8139 8135                                                                
MASTER      402    0   17   48   20    0    1    6 8670    2  159   82          
END