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HEADER    TRANSFERASE                             08-AUG-98   1BO4              
COMPND   1 CHAIN: A;
REMARK Output of the program extract_from_pdb (Version 1.95)
REMARK Legal PDB format not Guaranteed
REMARK This format is not meant to be used in place of the PDB format
REMARK The header refers to the original entry
REMARK The sequence from the original file has been taken in the field: ATOM
REMARK extract_from_pdb, 2001, 2002, 2003, 2004, 2005 (c) CNRS and Cedric Notredame
REMARK Contains Coordinates of: 
SEQRES   1 A  137  GLY ILE ILE ARG THR CYS ARG LEU GLY PRO ASP GLN VAL 
SEQRES   2 A  137  LYS SER MET ARG ALA ALA LEU ASP LEU PHE GLY ARG GLU 
SEQRES   3 A  137  PHE GLY ASP VAL ALA THR TYR SER GLN HIS GLN PRO ASP 
SEQRES   4 A  137  SER ASP TYR LEU GLY ASN LEU LEU ARG SER LYS THR PHE 
SEQRES   5 A  137  ILE ALA LEU ALA ALA PHE ASP GLN GLU ALA VAL VAL GLY 
SEQRES   6 A  137  ALA LEU ALA ALA TYR VAL LEU PRO LYS PHE GLU GLN PRO 
SEQRES   7 A  137  ARG SER GLU ILE TYR ILE TYR ASP LEU ALA VAL SER GLY 
SEQRES   8 A  137  GLU HIS ARG ARG GLN GLY ILE ALA THR ALA LEU ILE ASN 
SEQRES   9 A  137  LEU LEU LYS HIS GLU ALA ASN ALA LEU GLY ALA TYR VAL 
SEQRES  10 A  137  ILE TYR VAL GLN ALA ASP TYR GLY ASP ASP PRO ALA VAL 
SEQRES  11 A  137  ALA LEU TYR THR LYS LEU GLY 
ATOM      1  N   GLY A   1      11.666  98.870  36.705  1.00 37.49
ATOM      2  CA  GLY A   1      10.752  97.767  37.110  1.00 37.74
ATOM      3  C   GLY A   1      11.197  97.101  38.398  1.00 37.34
ATOM      4  O   GLY A   1      10.395  96.904  39.313  1.00 39.53
ATOM      5  N   ILE A   2      12.481  96.762  38.468  1.00 35.84
ATOM      6  CA  ILE A   2      13.065  96.109  39.636  1.00 33.97
ATOM      7  C   ILE A   2      12.475  94.734  39.904  1.00 32.54
ATOM      8  O   ILE A   2      11.368  94.603  40.425  1.00 32.91
ATOM      9  CB  ILE A   2      12.903  96.952  40.918  1.00 34.45
ATOM     10  CG1 ILE A   2      13.692  98.257  40.794  1.00 34.75
ATOM     11  CG2 ILE A   2      13.401  96.164  42.121  1.00 34.70
ATOM     12  CD1 ILE A   2      13.639  99.119  42.041  1.00 33.97
ATOM     13  N   ILE A   3      13.232  93.709  39.545  1.00 30.26
ATOM     14  CA  ILE A   3      12.807  92.339  39.757  1.00 29.30
ATOM     15  C   ILE A   3      13.740  91.712  40.778  1.00 27.87
ATOM     16  O   ILE A   3      14.951  91.688  40.585  1.00 27.17
ATOM     17  CB  ILE A   3      12.872  91.532  38.452  1.00 28.93
ATOM     18  CG1 ILE A   3      11.943  92.163  37.418  1.00 28.66
ATOM     19  CG2 ILE A   3      12.478  90.083  38.718  1.00 28.29
ATOM     20  CD1 ILE A   3      11.960  91.466  36.082  1.00 32.42
ATOM     21  N   ARG A   4      13.181  91.212  41.871  1.00 26.71
ATOM     22  CA  ARG A   4      14.005  90.598  42.899  1.00 27.20
ATOM     23  C   ARG A   4      13.881  89.081  42.914  1.00 25.81
ATOM     24  O   ARG A   4      12.821  88.530  42.646  1.00 25.55
ATOM     25  CB  ARG A   4      13.643  91.182  44.263  1.00 28.50
ATOM     26  CG  ARG A   4      13.844  92.687  44.306  1.00 31.34
ATOM     27  CD  ARG A   4      13.728  93.251  45.701  1.00 32.79
ATOM     28  NE  ARG A   4      14.050  94.672  45.710  1.00 32.77
ATOM     29  CZ  ARG A   4      14.238  95.389  46.811  1.00 34.31
ATOM     30  NH1 ARG A   4      14.140  94.815  48.006  1.00 34.27
ATOM     31  NH2 ARG A   4      14.524  96.682  46.715  1.00 35.26
ATOM     32  N   THR A   5      14.983  88.413  43.226  1.00 25.19
ATOM     33  CA  THR A   5      15.005  86.961  43.263  1.00 25.65
ATOM     34  C   THR A   5      15.507  86.455  44.597  1.00 25.13
ATOM     35  O   THR A   5      16.242  87.146  45.295  1.00 26.75
ATOM     36  CB  THR A   5      15.938  86.400  42.191  1.00 25.95
ATOM     37  OG1 THR A   5      17.248  86.940  42.390  1.00 27.42
ATOM     38  CG2 THR A   5      15.448  86.765  40.802  1.00 24.52
ATOM     39  N   CYS A   6      15.114  85.239  44.947  1.00 23.62
ATOM     40  CA  CYS A   6      15.563  84.642  46.191  1.00 22.83
ATOM     41  C   CYS A   6      15.173  83.173  46.238  1.00 21.02
ATOM     42  O   CYS A   6      14.311  82.718  45.484  1.00 19.26
ATOM     43  CB  CYS A   6      14.937  85.351  47.390  1.00 23.33
ATOM     44  SG  CYS A   6      13.219  84.890  47.686  1.00 27.12
ATOM     45  N   ARG A   7      15.838  82.435  47.114  1.00 19.90
ATOM     46  CA  ARG A   7      15.538  81.033  47.313  1.00 20.35
ATOM     47  C   ARG A   7      14.453  80.977  48.379  1.00 19.83
ATOM     48  O   ARG A   7      14.588  81.574  49.450  1.00 19.58
ATOM     49  CB  ARG A   7      16.763  80.265  47.808  1.00 21.25
ATOM     50  CG  ARG A   7      16.369  79.131  48.735  1.00 24.07
ATOM     51  CD  ARG A   7      16.708  77.733  48.253  1.00 22.98
ATOM     52  NE  ARG A   7      18.114  77.415  48.426  1.00 23.01
ATOM     53  CZ  ARG A   7      18.574  76.190  48.667  1.00 21.87
ATOM     54  NH1 ARG A   7      17.738  75.167  48.769  1.00 19.98
ATOM     55  NH2 ARG A   7      19.876  75.991  48.800  1.00 21.10
ATOM     56  N   LEU A   8      13.381  80.255  48.083  1.00 18.65
ATOM     57  CA  LEU A   8      12.276  80.115  49.017  1.00 18.50
ATOM     58  C   LEU A   8      12.605  79.124  50.131  1.00 17.47
ATOM     59  O   LEU A   8      13.167  78.061  49.886  1.00 17.21
ATOM     60  CB  LEU A   8      11.031  79.652  48.264  1.00 18.94
ATOM     61  CG  LEU A   8      10.548  80.596  47.157  1.00 20.26
ATOM     62  CD1 LEU A   8       9.380  79.977  46.398  1.00 20.42
ATOM     63  CD2 LEU A   8      10.144  81.923  47.782  1.00 19.54
ATOM     64  N   GLY A   9      12.264  79.490  51.360  1.00 17.89
ATOM     65  CA  GLY A   9      12.503  78.609  52.491  1.00 16.36
ATOM     66  C   GLY A   9      11.170  78.132  53.045  1.00 16.13
ATOM     67  O   GLY A   9      10.121  78.551  52.551  1.00 14.72
ATOM     68  N   PRO A  10      11.167  77.264  54.063  1.00 16.51
ATOM     69  CA  PRO A  10       9.939  76.737  54.674  1.00 16.84
ATOM     70  C   PRO A  10       9.028  77.835  55.231  1.00 18.02
ATOM     71  O   PRO A  10       7.866  77.598  55.566  1.00 17.41
ATOM     72  CB  PRO A  10      10.477  75.810  55.759  1.00 17.45
ATOM     73  CG  PRO A  10      11.822  76.470  56.105  1.00 18.41
ATOM     74  CD  PRO A  10      12.347  76.683  54.732  1.00 16.34
ATOM     75  N   ASP A  11       9.572  79.039  55.320  1.00 17.68
ATOM     76  CA  ASP A  11       8.843  80.186  55.826  1.00 19.55
ATOM     77  C   ASP A  11       8.119  80.913  54.691  1.00 19.51
ATOM     78  O   ASP A  11       7.348  81.846  54.923  1.00 20.22
ATOM     79  CB  ASP A  11       9.829  81.137  56.500  1.00 20.45
ATOM     80  CG  ASP A  11      10.982  81.519  55.581  1.00 22.33
ATOM     81  OD1 ASP A  11      11.638  80.603  55.034  1.00 22.37
ATOM     82  OD2 ASP A  11      11.238  82.729  55.412  1.00 23.24
ATOM     83  N   GLN A  12       8.361  80.473  53.464  1.00 18.14
ATOM     84  CA  GLN A  12       7.758  81.109  52.305  1.00 17.60
ATOM     85  C   GLN A  12       6.878  80.164  51.500  1.00 17.32
ATOM     86  O   GLN A  12       6.885  80.174  50.266  1.00 15.88
ATOM     87  CB  GLN A  12       8.864  81.689  51.429  1.00 16.47
ATOM     88  CG  GLN A  12       9.693  82.721  52.165  1.00 18.73
ATOM     89  CD  GLN A  12      10.933  83.125  51.405  1.00 19.93
ATOM     90  OE1 GLN A  12      11.814  82.299  51.153  1.00 20.28
ATOM     91  NE2 GLN A  12      11.014  84.399  51.031  1.00 21.15
ATOM     92  N   VAL A  13       6.117  79.343  52.211  1.00 17.24
ATOM     93  CA  VAL A  13       5.213  78.407  51.563  1.00 18.31
ATOM     94  C   VAL A  13       4.250  79.146  50.625  1.00 18.18
ATOM     95  O   VAL A  13       3.942  78.661  49.535  1.00 18.70
ATOM     96  CB  VAL A  13       4.406  77.609  52.618  1.00 18.15
ATOM     97  CG1 VAL A  13       3.250  76.896  51.964  1.00 16.24
ATOM     98  CG2 VAL A  13       5.314  76.588  53.294  1.00 16.16
ATOM     99  N   LYS A  14       3.789  80.320  51.049  1.00 18.13
ATOM    100  CA  LYS A  14       2.863  81.120  50.255  1.00 19.41
ATOM    101  C   LYS A  14       3.410  81.497  48.881  1.00 18.26
ATOM    102  O   LYS A  14       2.697  81.423  47.878  1.00 18.20
ATOM    103  CB  LYS A  14       2.472  82.388  51.018  1.00 23.14
ATOM    104  CG  LYS A  14       1.741  82.111  52.323  1.00 28.54
ATOM    105  CD  LYS A  14       1.261  83.402  52.978  1.00 30.97
ATOM    106  CE  LYS A  14       0.440  83.107  54.220  1.00 33.10
ATOM    107  NZ  LYS A  14      -0.154  84.350  54.792  1.00 34.43
ATOM    108  N   SER A  15       4.665  81.924  48.825  1.00 16.88
ATOM    109  CA  SER A  15       5.250  82.265  47.537  1.00 15.52
ATOM    110  C   SER A  15       5.444  80.982  46.738  1.00 13.98
ATOM    111  O   SER A  15       5.282  80.968  45.520  1.00 14.04
ATOM    112  CB  SER A  15       6.585  82.981  47.720  1.00 15.22
ATOM    113  OG  SER A  15       6.373  84.309  48.151  1.00 17.66
ATOM    114  N   MET A  16       5.783  79.903  47.430  1.00 12.86
ATOM    115  CA  MET A  16       5.978  78.629  46.762  1.00 12.93
ATOM    116  C   MET A  16       4.682  78.302  46.027  1.00 13.17
ATOM    117  O   MET A  16       4.700  77.929  44.854  1.00 12.34
ATOM    118  CB  MET A  16       6.301  77.533  47.782  1.00 13.01
ATOM    119  CG  MET A  16       6.505  76.160  47.165  1.00 13.86
ATOM    120  SD  MET A  16       7.858  76.089  45.976  1.00 14.78
ATOM    121  CE  MET A  16       7.712  74.384  45.439  1.00 18.83
ATOM    122  N   ARG A  17       3.554  78.459  46.715  1.00 12.81
ATOM    123  CA  ARG A  17       2.270  78.186  46.087  1.00 13.14
ATOM    124  C   ARG A  17       2.018  79.134  44.930  1.00 12.40
ATOM    125  O   ARG A  17       1.448  78.739  43.919  1.00 13.32
ATOM    126  CB  ARG A  17       1.122  78.281  47.100  1.00 12.07
ATOM    127  CG  ARG A  17       1.043  77.103  48.043  1.00 11.74
ATOM    128  CD  ARG A  17      -0.325  77.038  48.730  1.00 11.86
ATOM    129  NE  ARG A  17      -0.540  75.728  49.351  1.00 15.92
ATOM    130  CZ  ARG A  17       0.007  75.348  50.495  1.00 16.80
ATOM    131  NH1 ARG A  17       0.795  76.187  51.140  1.00 21.59
ATOM    132  NH2 ARG A  17      -0.214  74.136  50.986  1.00 14.21
ATOM    133  N   ALA A  18       2.447  80.385  45.075  1.00 12.40
ATOM    134  CA  ALA A  18       2.264  81.366  44.012  1.00 12.27
ATOM    135  C   ALA A  18       3.127  80.955  42.823  1.00 12.07
ATOM    136  O   ALA A  18       2.748  81.156  41.669  1.00 12.16
ATOM    137  CB  ALA A  18       2.660  82.760  44.495  1.00 11.62
ATOM    138  N   ALA A  19       4.290  80.378  43.108  1.00 10.46
ATOM    139  CA  ALA A  19       5.175  79.934  42.043  1.00 11.43
ATOM    140  C   ALA A  19       4.525  78.756  41.323  1.00 11.10
ATOM    141  O   ALA A  19       4.661  78.611  40.107  1.00 11.47
ATOM    142  CB  ALA A  19       6.537  79.526  42.610  1.00 12.44
ATOM    143  N   LEU A  20       3.815  77.919  42.073  1.00 10.15
ATOM    144  CA  LEU A  20       3.145  76.774  41.466  1.00 11.18
ATOM    145  C   LEU A  20       2.051  77.250  40.506  1.00 11.94
ATOM    146  O   LEU A  20       1.898  76.691  39.415  1.00  9.95
ATOM    147  CB  LEU A  20       2.551  75.843  42.535  1.00  7.75
ATOM    148  CG  LEU A  20       3.540  75.055  43.409  1.00  8.39
ATOM    149  CD1 LEU A  20       2.775  74.208  44.436  1.00  6.35
ATOM    150  CD2 LEU A  20       4.394  74.154  42.520  1.00  6.71
ATOM    151  N   ASP A  21       1.307  78.284  40.901  1.00 11.98
ATOM    152  CA  ASP A  21       0.251  78.821  40.043  1.00 13.26
ATOM    153  C   ASP A  21       0.847  79.385  38.750  1.00 13.80
ATOM    154  O   ASP A  21       0.249  79.253  37.676  1.00 14.38
ATOM    155  CB  ASP A  21      -0.549  79.915  40.762  1.00 14.41
ATOM    156  CG  ASP A  21      -1.258  79.405  42.011  1.00 16.72
ATOM    157  OD1 ASP A  21      -1.910  78.338  41.954  1.00 19.98
ATOM    158  OD2 ASP A  21      -1.184  80.088  43.048  1.00 19.18
ATOM    159  N   LEU A  22       2.023  80.004  38.852  1.00 13.28
ATOM    160  CA  LEU A  22       2.696  80.560  37.679  1.00 13.31
ATOM    161  C   LEU A  22       3.050  79.414  36.728  1.00 11.94
ATOM    162  O   LEU A  22       2.910  79.533  35.513  1.00 11.65
ATOM    163  CB  LEU A  22       3.976  81.301  38.087  1.00 14.51
ATOM    164  CG  LEU A  22       4.820  81.887  36.945  1.00 15.99
ATOM    165  CD1 LEU A  22       4.038  82.992  36.239  1.00 17.00
ATOM    166  CD2 LEU A  22       6.109  82.457  37.503  1.00 17.45
ATOM    167  N   PHE A  23       3.533  78.312  37.286  1.00 11.20
ATOM    168  CA  PHE A  23       3.868  77.145  36.479  1.00 11.97
ATOM    169  C   PHE A  23       2.602  76.693  35.744  1.00 12.62
ATOM    170  O   PHE A  23       2.625  76.454  34.538  1.00 11.67
ATOM    171  CB  PHE A  23       4.389  76.011  37.373  1.00 11.03
ATOM    172  CG  PHE A  23       5.828  76.175  37.802  1.00  9.73
ATOM    173  CD1 PHE A  23       6.768  76.757  36.952  1.00  9.94
ATOM    174  CD2 PHE A  23       6.247  75.716  39.046  1.00  8.08
ATOM    175  CE1 PHE A  23       8.108  76.875  37.342  1.00  9.00
ATOM    176  CE2 PHE A  23       7.578  75.832  39.447  1.00  7.80
ATOM    177  CZ  PHE A  23       8.509  76.413  38.594  1.00  7.12
ATOM    178  N   GLY A  24       1.500  76.595  36.481  1.00 12.49
ATOM    179  CA  GLY A  24       0.246  76.187  35.878  1.00 15.79
ATOM    180  C   GLY A  24      -0.172  77.044  34.693  1.00 16.47
ATOM    181  O   GLY A  24      -0.587  76.523  33.655  1.00 16.97
ATOM    182  N   ARG A  25      -0.059  78.359  34.843  1.00 16.55
ATOM    183  CA  ARG A  25      -0.431  79.277  33.776  1.00 18.79
ATOM    184  C   ARG A  25       0.515  79.252  32.578  1.00 19.99
ATOM    185  O   ARG A  25       0.070  79.239  31.430  1.00 20.60
ATOM    186  CB  ARG A  25      -0.545  80.713  34.320  1.00 18.76
ATOM    187  CG  ARG A  25      -1.746  80.920  35.236  1.00 18.94
ATOM    188  CD  ARG A  25      -1.966  82.382  35.667  1.00 21.10
ATOM    189  NE  ARG A  25      -1.169  82.808  36.820  1.00 24.27
ATOM    190  CZ  ARG A  25       0.126  83.097  36.797  1.00 25.13
ATOM    191  NH1 ARG A  25       0.813  83.015  35.665  1.00 28.03
ATOM    192  NH2 ARG A  25       0.732  83.477  37.914  1.00 25.39
ATOM    193  N   GLU A  26       1.817  79.235  32.835  1.00 19.63
ATOM    194  CA  GLU A  26       2.779  79.240  31.743  1.00 20.51
ATOM    195  C   GLU A  26       2.865  77.915  30.982  1.00 20.48
ATOM    196  O   GLU A  26       3.252  77.892  29.814  1.00 20.40
ATOM    197  CB  GLU A  26       4.160  79.645  32.264  1.00 20.53
ATOM    198  CG  GLU A  26       4.202  81.028  32.906  1.00 24.33
ATOM    199  CD  GLU A  26       3.633  82.125  32.007  1.00 27.62
ATOM    200  OE1 GLU A  26       4.056  82.227  30.833  1.00 28.37
ATOM    201  OE2 GLU A  26       2.765  82.895  32.477  1.00 28.90
ATOM    202  N   PHE A  27       2.497  76.819  31.638  1.00 19.34
ATOM    203  CA  PHE A  27       2.533  75.500  31.013  1.00 19.35
ATOM    204  C   PHE A  27       1.173  75.111  30.417  1.00 20.44
ATOM    205  O   PHE A  27       1.035  74.044  29.819  1.00 21.30
ATOM    206  CB  PHE A  27       2.954  74.448  32.049  1.00 18.57
ATOM    207  CG  PHE A  27       4.348  74.636  32.579  1.00 17.09
ATOM    208  CD1 PHE A  27       5.339  75.214  31.795  1.00 16.64
ATOM    209  CD2 PHE A  27       4.671  74.229  33.872  1.00 16.54
ATOM    210  CE1 PHE A  27       6.626  75.387  32.293  1.00 15.40
ATOM    211  CE2 PHE A  27       5.956  74.399  34.376  1.00 14.45
ATOM    212  CZ  PHE A  27       6.932  74.980  33.583  1.00 14.43
ATOM    213  N   GLY A  28       0.174  75.973  30.574  1.00 20.88
ATOM    214  CA  GLY A  28      -1.143  75.653  30.052  1.00 21.68
ATOM    215  C   GLY A  28      -1.690  74.397  30.712  1.00 22.86
ATOM    216  O   GLY A  28      -2.242  73.514  30.048  1.00 23.19
ATOM    217  N   ASP A  29      -1.536  74.317  32.029  1.00 22.12
ATOM    218  CA  ASP A  29      -2.003  73.162  32.776  1.00 21.16
ATOM    219  C   ASP A  29      -2.264  73.616  34.207  1.00 21.23
ATOM    220  O   ASP A  29      -1.638  73.137  35.161  1.00 19.61
ATOM    221  CB  ASP A  29      -0.933  72.072  32.763  1.00 23.09
ATOM    222  CG  ASP A  29      -1.488  70.707  33.104  1.00 25.12
ATOM    223  OD1 ASP A  29      -2.655  70.622  33.548  1.00 26.39
ATOM    224  OD2 ASP A  29      -0.748  69.718  32.935  1.00 26.84
ATOM    225  N   VAL A  30      -3.198  74.552  34.344  1.00 20.51
ATOM    226  CA  VAL A  30      -3.549  75.110  35.634  1.00 19.40
ATOM    227  C   VAL A  30      -3.995  74.061  36.645  1.00 19.01
ATOM    228  O   VAL A  30      -3.614  74.120  37.816  1.00 18.33
ATOM    229  CB  VAL A  30      -4.650  76.184  35.475  1.00 20.46
ATOM    230  CG1 VAL A  30      -4.991  76.790  36.830  1.00 18.47
ATOM    231  CG2 VAL A  30      -4.174  77.272  34.506  1.00 19.86
ATOM    232  N   ALA A  31      -4.790  73.095  36.200  1.00 18.20
ATOM    233  CA  ALA A  31      -5.284  72.053  37.096  1.00 17.14
ATOM    234  C   ALA A  31      -4.145  71.307  37.777  1.00 16.68
ATOM    235  O   ALA A  31      -4.129  71.156  38.996  1.00 16.13
ATOM    236  CB  ALA A  31      -6.161  71.069  36.323  1.00 17.85
ATOM    237  N   THR A  32      -3.188  70.853  36.975  1.00 16.89
ATOM    238  CA  THR A  32      -2.035  70.106  37.469  1.00 15.76
ATOM    239  C   THR A  32      -1.185  70.808  38.536  1.00 15.25
ATOM    240  O   THR A  32      -0.702  70.162  39.471  1.00 15.82
ATOM    241  CB  THR A  32      -1.113  69.716  36.292  1.00 16.08
ATOM    242  OG1 THR A  32      -1.815  68.824  35.416  1.00 18.05
ATOM    243  CG2 THR A  32       0.156  69.043  36.790  1.00 16.66
ATOM    244  N   TYR A  33      -1.012  72.118  38.405  1.00 12.92
ATOM    245  CA  TYR A  33      -0.176  72.868  39.341  1.00 12.52
ATOM    246  C   TYR A  33      -0.889  73.684  40.393  1.00 12.63
ATOM    247  O   TYR A  33      -0.262  74.183  41.321  1.00 12.74
ATOM    248  CB  TYR A  33       0.749  73.824  38.591  1.00 11.00
ATOM    249  CG  TYR A  33       1.822  73.153  37.788  1.00 11.46
ATOM    250  CD1 TYR A  33       1.557  72.617  36.524  1.00 11.27
ATOM    251  CD2 TYR A  33       3.105  73.015  38.312  1.00 10.54
ATOM    252  CE1 TYR A  33       2.553  71.960  35.804  1.00 12.25
ATOM    253  CE2 TYR A  33       4.103  72.361  37.608  1.00 11.59
ATOM    254  CZ  TYR A  33       3.825  71.837  36.358  1.00 12.23
ATOM    255  OH  TYR A  33       4.833  71.203  35.675  1.00 12.78
ATOM    256  N   SER A  34      -2.196  73.824  40.267  1.00 13.20
ATOM    257  CA  SER A  34      -2.908  74.642  41.218  1.00 14.59
ATOM    258  C   SER A  34      -4.056  73.969  41.932  1.00 13.80
ATOM    259  O   SER A  34      -4.452  74.416  43.000  1.00 12.58
ATOM    260  CB  SER A  34      -3.417  75.908  40.514  1.00 16.95
ATOM    261  OG  SER A  34      -4.237  76.656  41.394  1.00 25.85
ATOM    262  N   GLN A  35      -4.581  72.892  41.354  1.00 13.81
ATOM    263  CA  GLN A  35      -5.720  72.209  41.947  1.00 15.11
ATOM    264  C   GLN A  35      -5.427  71.032  42.850  1.00 14.73
ATOM    265  O   GLN A  35      -6.329  70.527  43.510  1.00 14.40
ATOM    266  CB  GLN A  35      -6.688  71.772  40.848  1.00 16.79
ATOM    267  CG  GLN A  35      -7.331  72.948  40.160  1.00 18.72
ATOM    268  CD  GLN A  35      -8.036  73.838  41.157  1.00 20.70
ATOM    269  OE1 GLN A  35      -9.010  73.429  41.787  1.00 24.70
ATOM    270  NE2 GLN A  35      -7.532  75.052  41.326  1.00 21.86
ATOM    271  N   HIS A  36      -4.174  70.606  42.903  1.00 13.98
ATOM    272  CA  HIS A  36      -3.822  69.468  43.734  1.00 14.73
ATOM    273  C   HIS A  36      -2.513  69.699  44.471  1.00 14.56
ATOM    274  O   HIS A  36      -1.711  68.784  44.618  1.00 14.77
ATOM    275  CB  HIS A  36      -3.721  68.223  42.854  1.00 15.80
ATOM    276  CG  HIS A  36      -5.003  67.868  42.169  1.00 17.12
ATOM    277  ND1 HIS A  36      -6.113  67.427  42.858  1.00 15.96
ATOM    278  CD2 HIS A  36      -5.367  67.922  40.867  1.00 18.17
ATOM    279  CE1 HIS A  36      -7.104  67.222  42.006  1.00 16.36
ATOM    280  NE2 HIS A  36      -6.675  67.514  40.794  1.00 17.05
ATOM    281  N   GLN A  37      -2.299  70.922  44.943  1.00 14.41
ATOM    282  CA  GLN A  37      -1.059  71.236  45.642  1.00 12.64
ATOM    283  C   GLN A  37      -1.009  70.492  46.965  1.00 13.34
ATOM    284  O   GLN A  37      -2.038  70.262  47.598  1.00 14.78
ATOM    285  CB  GLN A  37      -0.944  72.741  45.886  1.00 10.25
ATOM    286  CG  GLN A  37      -1.105  73.586  44.627  1.00 10.29
ATOM    287  CD  GLN A  37      -0.783  75.060  44.850  1.00 11.55
ATOM    288  OE1 GLN A  37      -0.954  75.591  45.950  1.00 11.11
ATOM    289  NE2 GLN A  37      -0.344  75.738  43.787  1.00 12.86
ATOM    290  N   PRO A  38       0.188  70.061  47.382  1.00 12.75
ATOM    291  CA  PRO A  38       0.314  69.343  48.651  1.00 12.41
ATOM    292  C   PRO A  38       0.056  70.296  49.815  1.00 12.43
ATOM    293  O   PRO A  38       0.091  71.510  49.628  1.00 10.46
ATOM    294  CB  PRO A  38       1.754  68.833  48.601  1.00 14.23
ATOM    295  CG  PRO A  38       2.442  69.919  47.862  1.00 13.04
ATOM    296  CD  PRO A  38       1.496  70.129  46.704  1.00 12.65
ATOM    297  N   ASP A  39      -0.212  69.756  51.006  1.00 11.94
ATOM    298  CA  ASP A  39      -0.467  70.610  52.160  1.00 11.90
ATOM    299  C   ASP A  39       0.805  71.349  52.595  1.00  9.87
ATOM    300  O   ASP A  39       1.890  71.096  52.079  1.00  8.66
ATOM    301  CB  ASP A  39      -1.063  69.813  53.332  1.00 12.80
ATOM    302  CG  ASP A  39      -0.191  68.648  53.770  1.00 14.90
ATOM    303  OD1 ASP A  39       1.048  68.821  53.856  1.00 15.61
ATOM    304  OD2 ASP A  39      -0.760  67.564  54.056  1.00 15.16
ATOM    305  N   SER A  40       0.670  72.256  53.552  1.00  9.74
ATOM    306  CA  SER A  40       1.804  73.056  53.997  1.00 10.70
ATOM    307  C   SER A  40       2.888  72.314  54.746  1.00 11.94
ATOM    308  O   SER A  40       4.060  72.697  54.683  1.00 12.74
ATOM    309  CB  SER A  40       1.316  74.242  54.822  1.00  8.99
ATOM    310  OG  SER A  40       0.567  75.100  53.995  1.00  8.04
ATOM    311  N   ASP A  41       2.514  71.261  55.461  1.00 12.80
ATOM    312  CA  ASP A  41       3.521  70.491  56.164  1.00 14.12
ATOM    313  C   ASP A  41       4.443  69.882  55.123  1.00 13.02
ATOM    314  O   ASP A  41       5.664  69.932  55.250  1.00 13.00
ATOM    315  CB  ASP A  41       2.892  69.387  57.004  1.00 17.04
ATOM    316  CG  ASP A  41       3.922  68.399  57.518  1.00 21.14
ATOM    317  OD1 ASP A  41       4.233  67.426  56.792  1.00 24.22
ATOM    318  OD2 ASP A  41       4.446  68.615  58.631  1.00 23.42
ATOM    319  N   TYR A  42       3.843  69.323  54.077  1.00 11.62
ATOM    320  CA  TYR A  42       4.603  68.689  53.008  1.00 10.40
ATOM    321  C   TYR A  42       5.487  69.693  52.285  1.00 10.99
ATOM    322  O   TYR A  42       6.672  69.447  52.060  1.00  9.53
ATOM    323  CB  TYR A  42       3.632  68.030  52.031  1.00  9.74
ATOM    324  CG  TYR A  42       4.249  67.400  50.809  1.00  8.09
ATOM    325  CD1 TYR A  42       4.833  68.180  49.815  1.00  6.92
ATOM    326  CD2 TYR A  42       4.189  66.020  50.619  1.00  9.09
ATOM    327  CE1 TYR A  42       5.333  67.602  48.661  1.00  8.85
ATOM    328  CE2 TYR A  42       4.685  65.433  49.474  1.00  8.45
ATOM    329  CZ  TYR A  42       5.253  66.228  48.495  1.00  8.97
ATOM    330  OH  TYR A  42       5.722  65.649  47.340  1.00 11.27
ATOM    331  N   LEU A  43       4.905  70.827  51.918  1.00 10.77
ATOM    332  CA  LEU A  43       5.650  71.858  51.209  1.00 11.61
ATOM    333  C   LEU A  43       6.753  72.416  52.108  1.00 11.36
ATOM    334  O   LEU A  43       7.852  72.713  51.644  1.00 11.78
ATOM    335  CB  LEU A  43       4.677  72.953  50.763  1.00 11.67
ATOM    336  CG  LEU A  43       4.600  73.345  49.287  1.00 12.30
ATOM    337  CD1 LEU A  43       4.847  72.162  48.370  1.00  9.67
ATOM    338  CD2 LEU A  43       3.222  73.956  49.028  1.00 11.48
ATOM    339  N   GLY A  44       6.463  72.540  53.399  1.00 12.56
ATOM    340  CA  GLY A  44       7.459  73.048  54.329  1.00 11.66
ATOM    341  C   GLY A  44       8.633  72.088  54.463  1.00 11.80
ATOM    342  O   GLY A  44       9.782  72.517  54.550  1.00 10.80
ATOM    343  N   ASN A  45       8.353  70.787  54.486  1.00 12.46
ATOM    344  CA  ASN A  45       9.416  69.793  54.600  1.00 13.84
ATOM    345  C   ASN A  45      10.258  69.802  53.339  1.00 13.71
ATOM    346  O   ASN A  45      11.488  69.749  53.399  1.00 14.04
ATOM    347  CB  ASN A  45       8.845  68.389  54.818  1.00 16.02
ATOM    348  CG  ASN A  45       8.039  68.283  56.087  1.00 18.85
ATOM    349  OD1 ASN A  45       8.438  68.805  57.124  1.00 21.88
ATOM    350  ND2 ASN A  45       6.906  67.585  56.022  1.00 21.44
ATOM    351  N   LEU A  46       9.591  69.877  52.194  1.00 13.49
ATOM    352  CA  LEU A  46      10.289  69.903  50.920  1.00 15.79
ATOM    353  C   LEU A  46      11.247  71.099  50.858  1.00 16.34
ATOM    354  O   LEU A  46      12.419  70.948  50.516  1.00 17.13
ATOM    355  CB  LEU A  46       9.276  69.984  49.779  1.00 16.10
ATOM    356  CG  LEU A  46       9.794  69.935  48.343  1.00 17.42
ATOM    357  CD1 LEU A  46      10.624  68.663  48.131  1.00 17.65
ATOM    358  CD2 LEU A  46       8.604  69.968  47.393  1.00 15.96
ATOM    359  N   LEU A  47      10.742  72.282  51.196  1.00 16.59
ATOM    360  CA  LEU A  47      11.547  73.502  51.174  1.00 17.19
ATOM    361  C   LEU A  47      12.614  73.502  52.260  1.00 18.26
ATOM    362  O   LEU A  47      13.529  74.313  52.238  1.00 19.38
ATOM    363  CB  LEU A  47      10.654  74.724  51.345  1.00 14.53
ATOM    364  CG  LEU A  47       9.659  74.976  50.211  1.00 15.93
ATOM    365  CD1 LEU A  47       8.654  76.056  50.619  1.00 12.94
ATOM    366  CD2 LEU A  47      10.424  75.375  48.954  1.00 14.45
ATOM    367  N   ARG A  48      12.495  72.582  53.205  1.00 19.57
ATOM    368  CA  ARG A  48      13.454  72.492  54.294  1.00 20.68
ATOM    369  C   ARG A  48      14.615  71.551  53.935  1.00 20.65
ATOM    370  O   ARG A  48      15.680  71.604  54.553  1.00 19.43
ATOM    371  CB  ARG A  48      12.733  72.012  55.557  1.00 22.65
ATOM    372  CG  ARG A  48      13.561  72.050  56.831  1.00 26.17
ATOM    373  CD  ARG A  48      12.715  71.643  58.037  1.00 27.87
ATOM    374  NE  ARG A  48      11.670  72.614  58.358  1.00 29.29
ATOM    375  CZ  ARG A  48      11.903  73.846  58.810  1.00 31.23
ATOM    376  NH1 ARG A  48      13.148  74.268  58.997  1.00 31.88
ATOM    377  NH2 ARG A  48      10.892  74.656  59.096  1.00 31.22
ATOM    378  N   SER A  49      14.415  70.710  52.922  1.00 19.58
ATOM    379  CA  SER A  49      15.449  69.769  52.509  1.00 21.08
ATOM    380  C   SER A  49      16.543  70.457  51.710  1.00 21.42
ATOM    381  O   SER A  49      16.344  71.541  51.161  1.00 21.69
ATOM    382  CB  SER A  49      14.858  68.642  51.663  1.00 21.34
ATOM    383  OG  SER A  49      14.461  69.129  50.401  1.00 24.55
ATOM    384  N   LYS A  50      17.701  69.813  51.639  1.00 20.94
ATOM    385  CA  LYS A  50      18.826  70.376  50.912  1.00 22.04
ATOM    386  C   LYS A  50      18.910  69.825  49.492  1.00 21.26
ATOM    387  O   LYS A  50      19.728  70.286  48.693  1.00 22.36
ATOM    388  CB  LYS A  50      20.126  70.084  51.667  1.00 24.50
ATOM    389  CG  LYS A  50      20.128  70.623  53.089  1.00 27.24
ATOM    390  CD  LYS A  50      21.434  70.327  53.793  1.00 31.77
ATOM    391  CE  LYS A  50      21.427  70.869  55.216  1.00 33.97
ATOM    392  NZ  LYS A  50      22.715  70.584  55.916  1.00 36.41
ATOM    393  N   THR A  51      18.067  68.844  49.180  1.00 18.50
ATOM    394  CA  THR A  51      18.068  68.255  47.853  1.00 17.95
ATOM    395  C   THR A  51      16.983  68.802  46.935  1.00 16.00
ATOM    396  O   THR A  51      16.774  68.285  45.838  1.00 16.39
ATOM    397  CB  THR A  51      17.950  66.723  47.918  1.00 18.26
ATOM    398  OG1 THR A  51      16.751  66.362  48.610  1.00 20.45
ATOM    399  CG2 THR A  51      19.159  66.140  48.631  1.00 18.80
ATOM    400  N   PHE A  52      16.288  69.838  47.389  1.00 14.67
ATOM    401  CA  PHE A  52      15.259  70.487  46.576  1.00 14.06
ATOM    402  C   PHE A  52      15.491  71.987  46.641  1.00 13.99
ATOM    403  O   PHE A  52      15.759  72.536  47.714  1.00 13.86
ATOM    404  CB  PHE A  52      13.850  70.201  47.081  1.00 13.05
ATOM    405  CG  PHE A  52      12.783  70.914  46.298  1.00 12.52
ATOM    406  CD1 PHE A  52      12.500  70.547  44.988  1.00 13.01
ATOM    407  CD2 PHE A  52      12.107  71.999  46.847  1.00 12.62
ATOM    408  CE1 PHE A  52      11.557  71.251  44.231  1.00 13.01
ATOM    409  CE2 PHE A  52      11.161  72.710  46.098  1.00 14.47
ATOM    410  CZ  PHE A  52      10.888  72.333  44.788  1.00 14.14
ATOM    411  N   ILE A  53      15.374  72.652  45.499  1.00 14.17
ATOM    412  CA  ILE A  53      15.604  74.085  45.449  1.00 13.59
ATOM    413  C   ILE A  53      14.510  74.838  44.701  1.00 13.87
ATOM    414  O   ILE A  53      14.255  74.587  43.526  1.00 14.55
ATOM    415  CB  ILE A  53      16.959  74.379  44.777  1.00 14.81
ATOM    416  CG1 ILE A  53      18.081  73.675  45.547  1.00 13.68
ATOM    417  CG2 ILE A  53      17.209  75.881  44.731  1.00 14.59
ATOM    418  CD1 ILE A  53      19.435  73.787  44.885  1.00 14.52
ATOM    419  N   ALA A  54      13.864  75.766  45.388  1.00 14.02
ATOM    420  CA  ALA A  54      12.819  76.566  44.769  1.00 14.41
ATOM    421  C   ALA A  54      13.283  78.011  44.716  1.00 14.66
ATOM    422  O   ALA A  54      13.627  78.600  45.735  1.00 15.09
ATOM    423  CB  ALA A  54      11.526  76.459  45.560  1.00 13.66
ATOM    424  N   LEU A  55      13.314  78.562  43.511  1.00 15.58
ATOM    425  CA  LEU A  55      13.719  79.942  43.285  1.00 16.24
ATOM    426  C   LEU A  55      12.554  80.705  42.687  1.00 16.50
ATOM    427  O   LEU A  55      11.846  80.189  41.826  1.00 17.58
ATOM    428  CB  LEU A  55      14.913  79.995  42.327  1.00 16.27
ATOM    429  CG  LEU A  55      16.326  79.837  42.908  1.00 16.94
ATOM    430  CD1 LEU A  55      16.358  78.793  43.997  1.00 16.06
ATOM    431  CD2 LEU A  55      17.291  79.500  41.779  1.00 14.60
ATOM    432  N   ALA A  56      12.364  81.938  43.144  1.00 16.65
ATOM    433  CA  ALA A  56      11.280  82.778  42.655  1.00 15.72
ATOM    434  C   ALA A  56      11.762  84.192  42.377  1.00 15.96
ATOM    435  O   ALA A  56      12.641  84.710  43.062  1.00 16.95
ATOM    436  CB  ALA A  56      10.149  82.808  43.676  1.00 15.87
ATOM    437  N   ALA A  57      11.179  84.810  41.359  1.00 16.22
ATOM    438  CA  ALA A  57      11.508  86.173  40.977  1.00 15.34
ATOM    439  C   ALA A  57      10.256  86.991  41.228  1.00 16.21
ATOM    440  O   ALA A  57       9.154  86.577  40.854  1.00 15.96
ATOM    441  CB  ALA A  57      11.885  86.230  39.513  1.00 15.37
ATOM    442  N   PHE A  58      10.420  88.145  41.870  1.00 16.64
ATOM    443  CA  PHE A  58       9.283  89.001  42.196  1.00 16.94
ATOM    444  C   PHE A  58       9.282  90.349  41.498  1.00 17.82
ATOM    445  O   PHE A  58      10.320  90.984  41.330  1.00 17.54
ATOM    446  CB  PHE A  58       9.208  89.273  43.707  1.00 13.98
ATOM    447  CG  PHE A  58       9.080  88.038  44.553  1.00 14.13
ATOM    448  CD1 PHE A  58      10.170  87.191  44.753  1.00 12.56
ATOM    449  CD2 PHE A  58       7.860  87.727  45.170  1.00 12.43
ATOM    450  CE1 PHE A  58      10.052  86.058  45.557  1.00 13.63
ATOM    451  CE2 PHE A  58       7.730  86.599  45.973  1.00 10.03
ATOM    452  CZ  PHE A  58       8.826  85.761  46.170  1.00 11.68
ATOM    453  N   ASP A  59       8.089  90.778  41.108  1.00 19.57
ATOM    454  CA  ASP A  59       7.882  92.075  40.479  1.00 20.95
ATOM    455  C   ASP A  59       6.728  92.698  41.259  1.00 20.55
ATOM    456  O   ASP A  59       5.606  92.198  41.218  1.00 21.23
ATOM    457  CB  ASP A  59       7.530  91.911  38.996  1.00 22.06
ATOM    458  CG  ASP A  59       7.162  93.229  38.335  1.00 24.12
ATOM    459  OD1 ASP A  59       7.851  94.238  38.595  1.00 26.60
ATOM    460  OD2 ASP A  59       6.198  93.257  37.543  1.00 24.70
ATOM    461  N   GLN A  60       7.011  93.764  42.000  1.00 21.56
ATOM    462  CA  GLN A  60       5.980  94.428  42.805  1.00 23.99
ATOM    463  C   GLN A  60       5.464  93.439  43.839  1.00 23.09
ATOM    464  O   GLN A  60       4.287  93.446  44.190  1.00 22.19
ATOM    465  CB  GLN A  60       4.809  94.897  41.933  1.00 26.95
ATOM    466  CG  GLN A  60       5.145  95.994  40.933  1.00 33.17
ATOM    467  CD  GLN A  60       5.387  97.335  41.595  1.00 37.23
ATOM    468  OE1 GLN A  60       6.246  97.464  42.470  1.00 40.70
ATOM    469  NE2 GLN A  60       4.631  98.343  41.180  1.00 38.29
ATOM    470  N   GLU A  61       6.356  92.568  44.294  1.00 22.60
ATOM    471  CA  GLU A  61       6.025  91.574  45.299  1.00 22.76
ATOM    472  C   GLU A  61       5.026  90.509  44.845  1.00 22.05
ATOM    473  O   GLU A  61       4.267  89.966  45.643  1.00 22.26
ATOM    474  CB  GLU A  61       5.551  92.286  46.577  1.00 24.29
ATOM    475  CG  GLU A  61       6.663  93.145  47.186  1.00 27.48
ATOM    476  CD  GLU A  61       6.291  93.801  48.504  1.00 29.45
ATOM    477  OE1 GLU A  61       5.486  94.760  48.512  1.00 28.02
ATOM    478  OE2 GLU A  61       6.817  93.340  49.538  1.00 30.55
ATOM    479  N   ALA A  62       5.047  90.212  43.550  1.00 21.34
ATOM    480  CA  ALA A  62       4.191  89.188  42.955  1.00 18.99
ATOM    481  C   ALA A  62       5.136  88.255  42.211  1.00 17.68
ATOM    482  O   ALA A  62       6.055  88.720  41.537  1.00 17.91
ATOM    483  CB  ALA A  62       3.207  89.817  41.986  1.00 17.93
ATOM    484  N   VAL A  63       4.926  86.947  42.335  1.00 16.40
ATOM    485  CA  VAL A  63       5.789  85.986  41.659  1.00 15.74
ATOM    486  C   VAL A  63       5.654  86.127  40.148  1.00 15.96
ATOM    487  O   VAL A  63       4.558  86.018  39.604  1.00 16.30
ATOM    488  CB  VAL A  63       5.449  84.536  42.069  1.00 16.44
ATOM    489  CG1 VAL A  63       6.332  83.560  41.306  1.00 15.87
ATOM    490  CG2 VAL A  63       5.641  84.364  43.570  1.00 14.97
ATOM    491  N   VAL A  64       6.780  86.365  39.480  1.00 15.34
ATOM    492  CA  VAL A  64       6.812  86.543  38.034  1.00 15.38
ATOM    493  C   VAL A  64       7.761  85.552  37.349  1.00 15.52
ATOM    494  O   VAL A  64       7.880  85.528  36.123  1.00 13.81
ATOM    495  CB  VAL A  64       7.242  87.990  37.679  1.00 16.17
ATOM    496  CG1 VAL A  64       8.598  88.300  38.273  1.00 14.38
ATOM    497  CG2 VAL A  64       7.285  88.161  36.180  1.00 19.00
ATOM    498  N   GLY A  65       8.430  84.733  38.152  1.00 16.34
ATOM    499  CA  GLY A  65       9.348  83.741  37.621  1.00 15.46
ATOM    500  C   GLY A  65       9.615  82.714  38.702  1.00 15.27
ATOM    501  O   GLY A  65       9.737  83.063  39.880  1.00 14.15
ATOM    502  N   ALA A  66       9.696  81.448  38.319  1.00 14.51
ATOM    503  CA  ALA A  66       9.945  80.391  39.293  1.00 13.11
ATOM    504  C   ALA A  66      10.854  79.335  38.716  1.00 12.92
ATOM    505  O   ALA A  66      10.825  79.052  37.519  1.00 12.24
ATOM    506  CB  ALA A  66       8.636  79.765  39.739  1.00 12.25
ATOM    507  N   LEU A  67      11.647  78.737  39.595  1.00 14.31
ATOM    508  CA  LEU A  67      12.609  77.718  39.213  1.00 13.14
ATOM    509  C   LEU A  67      12.570  76.609  40.259  1.00 12.83
ATOM    510  O   LEU A  67      12.764  76.869  41.451  1.00 11.44
ATOM    511  CB  LEU A  67      14.003  78.351  39.186  1.00 13.71
ATOM    512  CG  LEU A  67      15.270  77.644  38.708  1.00 15.36
ATOM    513  CD1 LEU A  67      15.485  76.342  39.467  1.00 15.75
ATOM    514  CD2 LEU A  67      15.162  77.400  37.229  1.00 17.92
ATOM    515  N   ALA A  68      12.321  75.382  39.814  1.00 10.27
ATOM    516  CA  ALA A  68      12.289  74.237  40.717  1.00 11.33
ATOM    517  C   ALA A  68      13.368  73.249  40.276  1.00 11.02
ATOM    518  O   ALA A  68      13.376  72.796  39.128  1.00 11.80
ATOM    519  CB  ALA A  68      10.924  73.567  40.682  1.00 10.08
ATOM    520  N   ALA A  69      14.281  72.925  41.182  1.00 10.07
ATOM    521  CA  ALA A  69      15.357  72.005  40.854  1.00  9.78
ATOM    522  C   ALA A  69      15.595  70.989  41.952  1.00 10.22
ATOM    523  O   ALA A  69      15.233  71.206  43.110  1.00 10.64
ATOM    524  CB  ALA A  69      16.629  72.777  40.584  1.00  9.07
ATOM    525  N   TYR A  70      16.187  69.864  41.559  1.00 11.74
ATOM    526  CA  TYR A  70      16.517  68.789  42.485  1.00 13.20
ATOM    527  C   TYR A  70      18.013  68.559  42.492  1.00 13.86
ATOM    528  O   TYR A  70      18.666  68.623  41.452  1.00 13.99
ATOM    529  CB  TYR A  70      15.835  67.474  42.106  1.00 11.25
ATOM    530  CG  TYR A  70      14.338  67.472  42.289  1.00 11.75
ATOM    531  CD1 TYR A  70      13.774  67.165  43.528  1.00  9.79
ATOM    532  CD2 TYR A  70      13.486  67.791  41.230  1.00 10.72
ATOM    533  CE1 TYR A  70      12.395  67.175  43.711  1.00 10.36
ATOM    534  CE2 TYR A  70      12.105  67.801  41.397  1.00 11.74
ATOM    535  CZ  TYR A  70      11.567  67.494  42.639  1.00 12.42
ATOM    536  OH  TYR A  70      10.200  67.513  42.808  1.00 15.14
ATOM    537  N   VAL A  71      18.541  68.296  43.680  1.00 14.93
ATOM    538  CA  VAL A  71      19.957  68.030  43.861  1.00 14.94
ATOM    539  C   VAL A  71      20.092  66.524  44.018  1.00 15.82
ATOM    540  O   VAL A  71      19.515  65.932  44.935  1.00 15.58
ATOM    541  CB  VAL A  71      20.497  68.698  45.132  1.00 15.56
ATOM    542  CG1 VAL A  71      22.006  68.493  45.232  1.00 15.67
ATOM    543  CG2 VAL A  71      20.138  70.174  45.131  1.00 14.72
ATOM    544  N   LEU A  72      20.833  65.889  43.122  1.00 16.23
ATOM    545  CA  LEU A  72      20.997  64.453  43.245  1.00 16.96
ATOM    546  C   LEU A  72      22.294  64.101  43.906  1.00 16.34
ATOM    547  O   LEU A  72      23.369  64.349  43.363  1.00 15.22
ATOM    548  CB  LEU A  72      20.943  63.756  41.885  1.00 18.05
ATOM    549  CG  LEU A  72      19.673  63.932  41.052  1.00 21.26
ATOM    550  CD1 LEU A  72      19.741  63.029  39.822  1.00 20.61
ATOM    551  CD2 LEU A  72      18.454  63.583  41.892  1.00 20.41
ATOM    552  N   PRO A  73      22.223  63.576  45.125  1.00 16.41
ATOM    553  CA  PRO A  73      23.444  63.191  45.819  1.00 15.88
ATOM    554  C   PRO A  73      23.818  61.872  45.124  1.00 14.99
ATOM    555  O   PRO A  73      23.068  60.907  45.170  1.00 13.74
ATOM    556  CB  PRO A  73      22.965  63.008  47.268  1.00 16.81
ATOM    557  CG  PRO A  73      21.609  63.815  47.305  1.00 19.76
ATOM    558  CD  PRO A  73      21.047  63.359  45.993  1.00 16.82
ATOM    559  N   LYS A  74      24.969  61.863  44.454  1.00 15.23
ATOM    560  CA  LYS A  74      25.419  60.694  43.702  1.00 14.95
ATOM    561  C   LYS A  74      25.942  59.474  44.500  1.00 15.22
ATOM    562  O   LYS A  74      26.448  59.608  45.608  1.00 15.09
ATOM    563  CB  LYS A  74      26.445  61.110  42.598  1.00 15.50
ATOM    564  CG  LYS A  74      25.934  62.128  41.549  1.00 14.29
ATOM    565  CD  LYS A  74      24.660  61.683  40.786  1.00 14.18
ATOM    566  CE  LYS A  74      24.855  60.549  39.761  1.00 14.52
ATOM    567  NZ  LYS A  74      26.033  60.818  38.918  1.00 15.10
ATOM    568  N   PHE A  75      25.815  58.283  43.904  1.00 14.39
ATOM    569  CA  PHE A  75      26.267  57.030  44.529  1.00 13.84
ATOM    570  C   PHE A  75      27.671  56.635  44.086  1.00 13.79
ATOM    571  O   PHE A  75      28.421  56.033  44.860  1.00 13.41
ATOM    572  CB  PHE A  75      25.316  55.889  44.187  1.00 13.63
ATOM    573  CG  PHE A  75      24.929  55.854  42.751  1.00 14.50
ATOM    574  CD1 PHE A  75      24.002  56.767  42.280  1.00 15.26
ATOM    575  CD2 PHE A  75      25.561  55.010  41.843  1.00 13.46
ATOM    576  CE1 PHE A  75      23.711  56.875  40.939  1.00 12.51
ATOM    577  CE2 PHE A  75      25.281  55.105  40.489  1.00 13.29
ATOM    578  CZ  PHE A  75      24.352  56.045  40.033  1.00 14.10
ATOM    579  N   GLU A  76      28.026  56.949  42.840  1.00 11.88
ATOM    580  CA  GLU A  76      29.338  56.562  42.349  1.00 13.70
ATOM    581  C   GLU A  76      30.473  57.335  43.009  1.00 14.36
ATOM    582  O   GLU A  76      31.552  56.787  43.221  1.00 13.83
ATOM    583  CB  GLU A  76      29.456  56.715  40.821  1.00 14.01
ATOM    584  CG  GLU A  76      29.521  58.141  40.295  1.00 14.34
ATOM    585  CD  GLU A  76      28.175  58.837  40.272  1.00 16.43
ATOM    586  OE1 GLU A  76      27.142  58.173  40.535  1.00 14.44
ATOM    587  OE2 GLU A  76      28.159  60.052  39.973  1.00 16.29
ATOM    588  N   GLN A  77      30.228  58.604  43.328  1.00 15.16
ATOM    589  CA  GLN A  77      31.228  59.461  43.966  1.00 15.41
ATOM    590  C   GLN A  77      30.548  60.447  44.917  1.00 15.98
ATOM    591  O   GLN A  77      29.356  60.720  44.783  1.00 17.23
ATOM    592  CB  GLN A  77      31.987  60.256  42.918  1.00 15.75
ATOM    593  CG  GLN A  77      32.862  59.450  41.995  1.00 16.78
ATOM    594  CD  GLN A  77      33.498  60.330  40.951  1.00 18.43
ATOM    595  OE1 GLN A  77      33.966  61.430  41.264  1.00 18.50
ATOM    596  NE2 GLN A  77      33.534  59.858  39.710  1.00 17.04
ATOM    597  N   PRO A  78      31.290  60.989  45.898  1.00 14.47
ATOM    598  CA  PRO A  78      30.735  61.954  46.850  1.00 14.88
ATOM    599  C   PRO A  78      30.599  63.305  46.179  1.00 16.00
ATOM    600  O   PRO A  78      31.357  64.224  46.479  1.00 16.73
ATOM    601  CB  PRO A  78      31.794  62.002  47.938  1.00 15.37
ATOM    602  CG  PRO A  78      33.040  61.916  47.113  1.00 15.26
ATOM    603  CD  PRO A  78      32.698  60.710  46.241  1.00 14.05
ATOM    604  N   ARG A  79      29.650  63.416  45.260  1.00 16.44
ATOM    605  CA  ARG A  79      29.412  64.651  44.527  1.00 17.21
ATOM    606  C   ARG A  79      27.916  64.751  44.284  1.00 16.82
ATOM    607  O   ARG A  79      27.185  63.789  44.531  1.00 16.26
ATOM    608  CB  ARG A  79      30.134  64.613  43.185  1.00 16.66
ATOM    609  CG  ARG A  79      29.658  63.488  42.270  1.00 19.17
ATOM    610  CD  ARG A  79      30.532  63.417  41.031  1.00 19.02
ATOM    611  NE  ARG A  79      30.095  62.409  40.069  1.00 18.61
ATOM    612  CZ  ARG A  79      30.699  62.210  38.900  1.00 19.45
ATOM    613  NH1 ARG A  79      31.754  62.942  38.562  1.00 20.45
ATOM    614  NH2 ARG A  79      30.251  61.293  38.060  1.00 19.33
ATOM    615  N   SER A  80      27.455  65.902  43.795  1.00 16.68
ATOM    616  CA  SER A  80      26.028  66.081  43.534  1.00 17.47
ATOM    617  C   SER A  80      25.745  66.775  42.206  1.00 16.39
ATOM    618  O   SER A  80      26.554  67.558  41.709  1.00 17.26
ATOM    619  CB  SER A  80      25.384  66.871  44.670  1.00 16.15
ATOM    620  OG  SER A  80      26.008  68.133  44.792  1.00 21.61
ATOM    621  N   GLU A  81      24.584  66.480  41.637  1.00 16.56
ATOM    622  CA  GLU A  81      24.186  67.058  40.356  1.00 16.33
ATOM    623  C   GLU A  81      22.838  67.738  40.511  1.00 15.61
ATOM    624  O   GLU A  81      21.957  67.218  41.189  1.00 15.75
ATOM    625  CB  GLU A  81      24.081  65.954  39.301  1.00 17.25
ATOM    626  CG  GLU A  81      25.353  65.149  39.117  1.00 17.09
ATOM    627  CD  GLU A  81      25.148  63.920  38.239  1.00 19.03
ATOM    628  OE1 GLU A  81      24.008  63.683  37.781  1.00 19.75
ATOM    629  OE2 GLU A  81      26.130  63.187  38.010  1.00 18.93
ATOM    630  N   ILE A  82      22.683  68.899  39.883  1.00 16.31
ATOM    631  CA  ILE A  82      21.438  69.655  39.947  1.00 16.05
ATOM    632  C   ILE A  82      20.676  69.535  38.632  1.00 15.90
ATOM    633  O   ILE A  82      21.254  69.682  37.555  1.00 14.58
ATOM    634  CB  ILE A  82      21.689  71.160  40.168  1.00 18.58
ATOM    635  CG1 ILE A  82      22.530  71.391  41.426  1.00 19.18
ATOM    636  CG2 ILE A  82      20.356  71.899  40.254  1.00 18.26
ATOM    637  CD1 ILE A  82      21.922  70.840  42.663  1.00 23.63
ATOM    638  N   TYR A  83      19.379  69.272  38.729  1.00 14.80
ATOM    639  CA  TYR A  83      18.528  69.164  37.555  1.00 15.38
ATOM    640  C   TYR A  83      17.370  70.132  37.706  1.00 14.58
ATOM    641  O   TYR A  83      16.596  70.039  38.659  1.00 13.24
ATOM    642  CB  TYR A  83      17.964  67.743  37.384  1.00 16.16
ATOM    643  CG  TYR A  83      19.002  66.702  37.037  1.00 18.06
ATOM    644  CD1 TYR A  83      19.916  66.257  37.991  1.00 18.53
ATOM    645  CD2 TYR A  83      19.105  66.200  35.738  1.00 18.83
ATOM    646  CE1 TYR A  83      20.905  65.343  37.667  1.00 19.60
ATOM    647  CE2 TYR A  83      20.098  65.281  35.400  1.00 20.49
ATOM    648  CZ  TYR A  83      20.996  64.858  36.375  1.00 20.38
ATOM    649  OH  TYR A  83      21.986  63.953  36.067  1.00 20.96
ATOM    650  N   ILE A  84      17.271  71.080  36.780  1.00 14.46
ATOM    651  CA  ILE A  84      16.178  72.036  36.815  1.00 14.83
ATOM    652  C   ILE A  84      14.974  71.306  36.243  1.00 15.28
ATOM    653  O   ILE A  84      14.932  70.982  35.054  1.00 16.33
ATOM    654  CB  ILE A  84      16.480  73.277  35.963  1.00 14.89
ATOM    655  CG1 ILE A  84      17.702  73.994  36.530  1.00 13.75
ATOM    656  CG2 ILE A  84      15.257  74.210  35.940  1.00 14.85
ATOM    657  CD1 ILE A  84      18.111  75.205  35.744  1.00 14.59
ATOM    658  N   TYR A  85      14.006  71.022  37.101  1.00 15.57
ATOM    659  CA  TYR A  85      12.813  70.317  36.675  1.00 15.71
ATOM    660  C   TYR A  85      11.880  71.301  35.975  1.00 15.15
ATOM    661  O   TYR A  85      11.570  71.129  34.802  1.00 16.07
ATOM    662  CB  TYR A  85      12.140  69.669  37.888  1.00 15.99
ATOM    663  CG  TYR A  85      11.113  68.624  37.528  1.00 16.70
ATOM    664  CD1 TYR A  85       9.876  68.982  36.987  1.00 17.80
ATOM    665  CD2 TYR A  85      11.397  67.269  37.683  1.00 16.66
ATOM    666  CE1 TYR A  85       8.946  68.011  36.606  1.00 17.10
ATOM    667  CE2 TYR A  85      10.477  66.292  37.304  1.00 16.12
ATOM    668  CZ  TYR A  85       9.260  66.667  36.765  1.00 16.96
ATOM    669  OH  TYR A  85       8.367  65.700  36.355  1.00 17.37
ATOM    670  N   ASP A  86      11.438  72.335  36.690  1.00 16.21
ATOM    671  CA  ASP A  86      10.546  73.346  36.107  1.00 14.93
ATOM    672  C   ASP A  86      11.102  74.757  36.194  1.00 13.94
ATOM    673  O   ASP A  86      11.619  75.166  37.233  1.00 11.35
ATOM    674  CB  ASP A  86       9.156  73.333  36.768  1.00 15.21
ATOM    675  CG  ASP A  86       8.289  72.187  36.281  1.00 17.80
ATOM    676  OD1 ASP A  86       8.477  71.783  35.122  1.00 18.35
ATOM    677  OD2 ASP A  86       7.400  71.713  37.024  1.00 18.08
ATOM    678  N   LEU A  87      10.962  75.492  35.093  1.00 13.49
ATOM    679  CA  LEU A  87      11.428  76.872  34.981  1.00 14.84
ATOM    680  C   LEU A  87      10.437  77.628  34.077  1.00 14.08
ATOM    681  O   LEU A  87      10.216  77.244  32.928  1.00 12.89
ATOM    682  CB  LEU A  87      12.815  76.899  34.335  1.00 15.31
ATOM    683  CG  LEU A  87      13.668  78.173  34.378  1.00 18.74
ATOM    684  CD1 LEU A  87      14.793  78.032  33.336  1.00 16.23
ATOM    685  CD2 LEU A  87      12.837  79.394  34.055  1.00 19.39
ATOM    686  N   ALA A  88       9.851  78.699  34.597  1.00 13.54
ATOM    687  CA  ALA A  88       8.898  79.487  33.826  1.00 13.63
ATOM    688  C   ALA A  88       8.864  80.951  34.255  1.00 13.93
ATOM    689  O   ALA A  88       9.092  81.283  35.423  1.00 13.70
ATOM    690  CB  ALA A  88       7.495  78.883  33.942  1.00 12.18
ATOM    691  N   VAL A  89       8.583  81.819  33.288  1.00 13.68
ATOM    692  CA  VAL A  89       8.482  83.254  33.523  1.00 12.62
ATOM    693  C   VAL A  89       7.131  83.755  33.014  1.00 13.44
ATOM    694  O   VAL A  89       6.616  83.271  32.001  1.00 12.50
ATOM    695  CB  VAL A  89       9.599  84.035  32.785  1.00 11.81
ATOM    696  CG1 VAL A  89       9.371  85.531  32.931  1.00  9.76
ATOM    697  CG2 VAL A  89      10.966  83.667  33.362  1.00 10.33
ATOM    698  N   SER A  90       6.561  84.720  33.727  1.00 14.16
ATOM    699  CA  SER A  90       5.288  85.320  33.344  1.00 16.48
ATOM    700  C   SER A  90       5.307  85.697  31.854  1.00 18.01
ATOM    701  O   SER A  90       6.312  86.201  31.343  1.00 17.80
ATOM    702  CB  SER A  90       5.044  86.576  34.182  1.00 17.26
ATOM    703  OG  SER A  90       3.951  87.332  33.683  1.00 19.79
ATOM    704  N   GLY A  91       4.198  85.446  31.167  1.00 18.35
ATOM    705  CA  GLY A  91       4.112  85.772  29.759  1.00 20.47
ATOM    706  C   GLY A  91       4.199  87.270  29.541  1.00 22.82
ATOM    707  O   GLY A  91       4.463  87.738  28.432  1.00 23.44
ATOM    708  N   GLU A  92       3.984  88.030  30.608  1.00 23.42
ATOM    709  CA  GLU A  92       4.036  89.484  30.528  1.00 25.71
ATOM    710  C   GLU A  92       5.406  90.024  30.911  1.00 23.73
ATOM    711  O   GLU A  92       5.619  91.236  30.947  1.00 24.61
ATOM    712  CB  GLU A  92       2.957  90.099  31.434  1.00 28.29
ATOM    713  CG  GLU A  92       1.530  89.819  30.975  1.00 32.96
ATOM    714  CD  GLU A  92       1.191  90.503  29.659  1.00 35.73
ATOM    715  OE1 GLU A  92       1.935  90.310  28.674  1.00 37.99
ATOM    716  OE2 GLU A  92       0.178  91.233  29.604  1.00 37.32
ATOM    717  N   HIS A  93       6.340  89.122  31.188  1.00 21.68
ATOM    718  CA  HIS A  93       7.682  89.532  31.571  1.00 20.41
ATOM    719  C   HIS A  93       8.768  88.748  30.838  1.00 20.76
ATOM    720  O   HIS A  93       9.884  88.613  31.339  1.00 20.98
ATOM    721  CB  HIS A  93       7.877  89.370  33.081  1.00 19.80
ATOM    722  CG  HIS A  93       6.860  90.094  33.911  1.00 18.81
ATOM    723  ND1 HIS A  93       5.536  89.718  33.965  1.00 19.24
ATOM    724  CD2 HIS A  93       6.975  91.169  34.732  1.00 19.10
ATOM    725  CE1 HIS A  93       4.880  90.524  34.783  1.00 17.94
ATOM    726  NE2 HIS A  93       5.734  91.412  35.258  1.00 17.61
ATOM    727  N   ARG A  94       8.444  88.231  29.655  1.00 19.80
ATOM    728  CA  ARG A  94       9.412  87.470  28.871  1.00 20.96
ATOM    729  C   ARG A  94      10.499  88.378  28.292  1.00 22.18
ATOM    730  O   ARG A  94      10.331  89.596  28.197  1.00 22.14
ATOM    731  CB  ARG A  94       8.722  86.737  27.711  1.00 20.19
ATOM    732  CG  ARG A  94       7.650  85.729  28.119  1.00 20.91
ATOM    733  CD  ARG A  94       8.229  84.592  28.937  1.00 20.04
ATOM    734  NE  ARG A  94       7.217  83.603  29.302  1.00 22.41
ATOM    735  CZ  ARG A  94       6.583  82.811  28.439  1.00 22.81
ATOM    736  NH1 ARG A  94       6.850  82.878  27.140  1.00 23.72
ATOM    737  NH2 ARG A  94       5.675  81.953  28.877  1.00 21.33
ATOM    738  N   ARG A  95      11.611  87.765  27.905  1.00 22.87
ATOM    739  CA  ARG A  95      12.737  88.475  27.308  1.00 25.04
ATOM    740  C   ARG A  95      13.227  89.660  28.144  1.00 24.40
ATOM    741  O   ARG A  95      13.630  90.686  27.597  1.00 25.96
ATOM    742  CB  ARG A  95      12.366  88.973  25.904  1.00 26.49
ATOM    743  CG  ARG A  95      11.502  88.026  25.079  1.00 28.25
ATOM    744  CD  ARG A  95      12.117  86.657  24.857  1.00 30.58
ATOM    745  NE  ARG A  95      13.373  86.688  24.111  1.00 33.89
ATOM    746  CZ  ARG A  95      13.941  85.611  23.573  1.00 34.85
ATOM    747  NH1 ARG A  95      13.361  84.422  23.698  1.00 36.18
ATOM    748  NH2 ARG A  95      15.091  85.714  22.918  1.00 34.04
ATOM    749  N   GLN A  96      13.187  89.516  29.463  1.00 24.30
ATOM    750  CA  GLN A  96      13.653  90.558  30.378  1.00 24.27
ATOM    751  C   GLN A  96      14.846  90.091  31.208  1.00 21.93
ATOM    752  O   GLN A  96      15.351  90.836  32.044  1.00 21.87
ATOM    753  CB  GLN A  96      12.541  90.982  31.341  1.00 26.18
ATOM    754  CG  GLN A  96      11.553  91.989  30.813  1.00 30.21
ATOM    755  CD  GLN A  96      10.546  92.398  31.882  1.00 32.67
ATOM    756  OE1 GLN A  96      10.919  92.734  33.016  1.00 33.42
ATOM    757  NE2 GLN A  96       9.267  92.382  31.524  1.00 33.64
ATOM    758  N   GLY A  97      15.268  88.850  31.002  1.00 20.89
ATOM    759  CA  GLY A  97      16.395  88.316  31.747  1.00 20.19
ATOM    760  C   GLY A  97      16.026  87.684  33.081  1.00 19.42
ATOM    761  O   GLY A  97      16.898  87.436  33.917  1.00 20.40
ATOM    762  N   ILE A  98      14.743  87.405  33.288  1.00 19.25
ATOM    763  CA  ILE A  98      14.301  86.815  34.548  1.00 18.24
ATOM    764  C   ILE A  98      14.745  85.368  34.717  1.00 17.16
ATOM    765  O   ILE A  98      15.263  84.997  35.768  1.00 16.24
ATOM    766  CB  ILE A  98      12.767  86.907  34.701  1.00 18.74
ATOM    767  CG1 ILE A  98      12.358  88.380  34.768  1.00 20.59
ATOM    768  CG2 ILE A  98      12.313  86.167  35.956  1.00 17.24
ATOM    769  CD1 ILE A  98      10.862  88.607  34.931  1.00 22.00
ATOM    770  N   ALA A  99      14.541  84.550  33.693  1.00 16.78
ATOM    771  CA  ALA A  99      14.963  83.160  33.774  1.00 18.41
ATOM    772  C   ALA A  99      16.479  83.164  33.974  1.00 18.60
ATOM    773  O   ALA A  99      17.019  82.373  34.750  1.00 18.00
ATOM    774  CB  ALA A  99      14.595  82.405  32.492  1.00 17.70
ATOM    775  N   THR A 100      17.162  84.067  33.275  1.00 17.94
ATOM    776  CA  THR A 100      18.611  84.168  33.403  1.00 17.92
ATOM    777  C   THR A 100      18.981  84.473  34.850  1.00 17.81
ATOM    778  O   THR A 100      19.917  83.886  35.402  1.00 16.83
ATOM    779  CB  THR A 100      19.175  85.281  32.514  1.00 18.96
ATOM    780  OG1 THR A 100      18.872  84.992  31.145  1.00 18.26
ATOM    781  CG2 THR A 100      20.698  85.387  32.695  1.00 18.87
ATOM    782  N   ALA A 101      18.242  85.398  35.459  1.00 15.68
ATOM    783  CA  ALA A 101      18.488  85.777  36.848  1.00 15.11
ATOM    784  C   ALA A 101      18.227  84.616  37.824  1.00 15.29
ATOM    785  O   ALA A 101      18.939  84.467  38.820  1.00 15.76
ATOM    786  CB  ALA A 101      17.628  86.974  37.226  1.00 13.52
ATOM    787  N   LEU A 102      17.218  83.797  37.547  1.00 12.77
ATOM    788  CA  LEU A 102      16.918  82.677  38.433  1.00 13.35
ATOM    789  C   LEU A 102      18.017  81.632  38.332  1.00 12.85
ATOM    790  O   LEU A 102      18.421  81.034  39.329  1.00 12.00
ATOM    791  CB  LEU A 102      15.564  82.054  38.081  1.00 11.69
ATOM    792  CG  LEU A 102      14.350  82.919  38.425  1.00 13.51
ATOM    793  CD1 LEU A 102      13.084  82.279  37.868  1.00 11.91
ATOM    794  CD2 LEU A 102      14.250  83.086  39.948  1.00 11.11
ATOM    795  N   ILE A 103      18.497  81.423  37.113  1.00 14.56
ATOM    796  CA  ILE A 103      19.561  80.468  36.862  1.00 16.44
ATOM    797  C   ILE A 103      20.890  80.929  37.472  1.00 16.03
ATOM    798  O   ILE A 103      21.663  80.106  37.949  1.00 16.68
ATOM    799  CB  ILE A 103      19.705  80.206  35.346  1.00 16.19
ATOM    800  CG1 ILE A 103      18.487  79.411  34.862  1.00 16.31
ATOM    801  CG2 ILE A 103      20.999  79.457  35.050  1.00 17.97
ATOM    802  CD1 ILE A 103      18.534  79.042  33.402  1.00 18.72
ATOM    803  N   ASN A 104      21.157  82.231  37.470  1.00 16.84
ATOM    804  CA  ASN A 104      22.393  82.710  38.078  1.00 18.91
ATOM    805  C   ASN A 104      22.340  82.494  39.584  1.00 17.98
ATOM    806  O   ASN A 104      23.344  82.138  40.203  1.00 17.89
ATOM    807  CB  ASN A 104      22.644  84.189  37.767  1.00 21.05
ATOM    808  CG  ASN A 104      23.012  84.418  36.316  1.00 25.42
ATOM    809  OD1 ASN A 104      23.847  83.699  35.758  1.00 25.77
ATOM    810  ND2 ASN A 104      22.409  85.430  35.701  1.00 26.87
ATOM    811  N   LEU A 105      21.168  82.713  40.174  1.00 16.86
ATOM    812  CA  LEU A 105      21.000  82.495  41.606  1.00 15.50
ATOM    813  C   LEU A 105      21.193  81.001  41.852  1.00 15.86
ATOM    814  O   LEU A 105      21.819  80.594  42.838  1.00 15.90
ATOM    815  CB  LEU A 105      19.601  82.923  42.054  1.00 13.65
ATOM    816  CG  LEU A 105      19.190  82.565  43.490  1.00 14.84
ATOM    817  CD1 LEU A 105      20.171  83.161  44.499  1.00 13.41
ATOM    818  CD2 LEU A 105      17.785  83.077  43.756  1.00 13.07
ATOM    819  N   LEU A 106      20.665  80.189  40.936  1.00 15.38
ATOM    820  CA  LEU A 106      20.775  78.734  41.047  1.00 16.00
ATOM    821  C   LEU A 106      22.247  78.317  41.056  1.00 16.69
ATOM    822  O   LEU A 106      22.644  77.421  41.806  1.00 14.63
ATOM    823  CB  LEU A 106      20.017  78.064  39.891  1.00 15.74
ATOM    824  CG  LEU A 106      19.879  76.536  39.805  1.00 17.59
ATOM    825  CD1 LEU A 106      21.154  75.925  39.313  1.00 20.02
ATOM    826  CD2 LEU A 106      19.474  75.965  41.165  1.00 16.77
ATOM    827  N   LYS A 107      23.058  78.974  40.227  1.00 17.94
ATOM    828  CA  LYS A 107      24.484  78.674  40.180  1.00 19.53
ATOM    829  C   LYS A 107      25.099  79.046  41.527  1.00 20.36
ATOM    830  O   LYS A 107      25.986  78.358  42.031  1.00 21.13
ATOM    831  CB  LYS A 107      25.157  79.449  39.044  1.00 20.02
ATOM    832  CG  LYS A 107      24.686  79.010  37.663  1.00 22.99
ATOM    833  CD  LYS A 107      25.348  79.803  36.532  1.00 27.27
ATOM    834  CE  LYS A 107      24.874  79.298  35.169  1.00 28.44
ATOM    835  NZ  LYS A 107      25.452  80.055  34.021  1.00 28.91
ATOM    836  N   HIS A 108      24.613  80.131  42.115  1.00 20.33
ATOM    837  CA  HIS A 108      25.108  80.570  43.412  1.00 23.29
ATOM    838  C   HIS A 108      24.801  79.482  44.437  1.00 22.54
ATOM    839  O   HIS A 108      25.634  79.151  45.278  1.00 22.51
ATOM    840  CB  HIS A 108      24.427  81.874  43.826  1.00 27.06
ATOM    841  CG  HIS A 108      24.818  82.362  45.182  1.00 31.31
ATOM    842  ND1 HIS A 108      26.069  82.887  45.449  1.00 33.45
ATOM    843  CD2 HIS A 108      24.143  82.385  46.356  1.00 32.70
ATOM    844  CE1 HIS A 108      26.139  83.211  46.737  1.00 33.24
ATOM    845  NE2 HIS A 108      24.982  82.915  47.302  1.00 33.10
ATOM    846  N   GLU A 109      23.591  78.935  44.368  1.00 21.95
ATOM    847  CA  GLU A 109      23.181  77.874  45.280  1.00 21.89
ATOM    848  C   GLU A 109      24.003  76.606  45.058  1.00 21.72
ATOM    849  O   GLU A 109      24.421  75.957  46.012  1.00 21.12
ATOM    850  CB  GLU A 109      21.695  77.555  45.092  1.00 22.12
ATOM    851  CG  GLU A 109      20.744  78.683  45.464  1.00 22.97
ATOM    852  CD  GLU A 109      20.891  79.118  46.913  1.00 24.20
ATOM    853  OE1 GLU A 109      20.862  78.244  47.810  1.00 24.86
ATOM    854  OE2 GLU A 109      21.023  80.336  47.158  1.00 24.14
ATOM    855  N   ALA A 110      24.228  76.257  43.794  1.00 22.73
ATOM    856  CA  ALA A 110      25.002  75.069  43.455  1.00 23.97
ATOM    857  C   ALA A 110      26.398  75.153  44.061  1.00 25.30
ATOM    858  O   ALA A 110      26.862  74.215  44.711  1.00 25.09
ATOM    859  CB  ALA A 110      25.104  74.920  41.938  1.00 21.73
ATOM    860  N   ASN A 111      27.065  76.282  43.848  1.00 26.00
ATOM    861  CA  ASN A 111      28.407  76.459  44.375  1.00 27.39
ATOM    862  C   ASN A 111      28.458  76.295  45.888  1.00 27.46
ATOM    863  O   ASN A 111      29.351  75.630  46.408  1.00 27.69
ATOM    864  CB  ASN A 111      28.964  77.824  43.976  1.00 29.50
ATOM    865  CG  ASN A 111      30.350  78.080  44.556  1.00 31.80
ATOM    866  OD1 ASN A 111      30.508  78.260  45.764  1.00 32.71
ATOM    867  ND2 ASN A 111      31.361  78.082  43.694  1.00 33.24
ATOM    868  N   ALA A 112      27.507  76.898  46.595  1.00 27.63
ATOM    869  CA  ALA A 112      27.474  76.793  48.052  1.00 28.53
ATOM    870  C   ALA A 112      27.188  75.351  48.452  1.00 29.69
ATOM    871  O   ALA A 112      27.714  74.840  49.443  1.00 28.69
ATOM    872  CB  ALA A 112      26.397  77.708  48.621  1.00 27.52
ATOM    873  N   LEU A 113      26.350  74.703  47.654  1.00 30.66
ATOM    874  CA  LEU A 113      25.946  73.332  47.897  1.00 31.82
ATOM    875  C   LEU A 113      27.062  72.360  47.506  1.00 32.04
ATOM    876  O   LEU A 113      27.183  71.271  48.066  1.00 33.44
ATOM    877  CB  LEU A 113      24.675  73.050  47.093  1.00 32.11
ATOM    878  CG  LEU A 113      23.803  71.865  47.482  1.00 33.29
ATOM    879  CD1 LEU A 113      23.358  72.009  48.934  1.00 33.10
ATOM    880  CD2 LEU A 113      22.596  71.814  46.563  1.00 33.05
ATOM    881  N   GLY A 114      27.884  72.763  46.545  1.00 31.67
ATOM    882  CA  GLY A 114      28.973  71.911  46.109  1.00 30.18
ATOM    883  C   GLY A 114      28.708  71.172  44.809  1.00 29.26
ATOM    884  O   GLY A 114      29.610  70.518  44.277  1.00 29.59
ATOM    885  N   ALA A 115      27.483  71.266  44.295  1.00 27.65
ATOM    886  CA  ALA A 115      27.126  70.590  43.044  1.00 26.47
ATOM    887  C   ALA A 115      28.143  70.941  41.968  1.00 25.21
ATOM    888  O   ALA A 115      28.545  72.098  41.838  1.00 25.04
ATOM    889  CB  ALA A 115      25.729  71.005  42.597  1.00 26.44
ATOM    890  N   TYR A 116      28.552  69.947  41.188  1.00 23.94
ATOM    891  CA  TYR A 116      29.549  70.174  40.148  1.00 23.06
ATOM    892  C   TYR A 116      28.939  70.410  38.768  1.00 23.01
ATOM    893  O   TYR A 116      29.647  70.787  37.836  1.00 23.91
ATOM    894  CB  TYR A 116      30.530  68.986  40.098  1.00 22.43
ATOM    895  CG  TYR A 116      29.982  67.738  39.429  1.00 22.10
ATOM    896  CD1 TYR A 116      29.180  66.839  40.131  1.00 21.16
ATOM    897  CD2 TYR A 116      30.234  67.482  38.079  1.00 21.40
ATOM    898  CE1 TYR A 116      28.643  65.719  39.505  1.00 21.04
ATOM    899  CE2 TYR A 116      29.701  66.364  37.442  1.00 21.35
ATOM    900  CZ  TYR A 116      28.905  65.487  38.165  1.00 21.95
ATOM    901  OH  TYR A 116      28.367  64.383  37.546  1.00 22.03
ATOM    902  N   VAL A 117      27.633  70.191  38.635  1.00 22.73
ATOM    903  CA  VAL A 117      26.946  70.391  37.354  1.00 22.96
ATOM    904  C   VAL A 117      25.450  70.689  37.518  1.00 22.21
ATOM    905  O   VAL A 117      24.843  70.374  38.546  1.00 20.87
ATOM    906  CB  VAL A 117      27.117  69.157  36.418  1.00 23.45
ATOM    907  CG1 VAL A 117      26.289  69.317  35.154  1.00 24.37
ATOM    908  CG2 VAL A 117      28.558  69.033  36.006  1.00 28.88
ATOM    909  N   ILE A 118      24.878  71.301  36.486  1.00 20.79
ATOM    910  CA  ILE A 118      23.474  71.678  36.456  1.00 20.84
ATOM    911  C   ILE A 118      22.865  71.322  35.099  1.00 21.24
ATOM    912  O   ILE A 118      23.386  71.723  34.057  1.00 20.04
ATOM    913  CB  ILE A 118      23.318  73.205  36.660  1.00 20.01
ATOM    914  CG1 ILE A 118      23.913  73.613  38.008  1.00 19.68
ATOM    915  CG2 ILE A 118      21.850  73.606  36.553  1.00 19.50
ATOM    916  CD1 ILE A 118      23.978  75.117  38.216  1.00 18.28
ATOM    917  N   TYR A 119      21.774  70.564  35.110  1.00 22.08
ATOM    918  CA  TYR A 119      21.100  70.208  33.865  1.00 24.71
ATOM    919  C   TYR A 119      19.795  70.981  33.739  1.00 27.22
ATOM    920  O   TYR A 119      19.099  71.207  34.732  1.00 25.28
ATOM    921  CB  TYR A 119      20.800  68.709  33.787  1.00 23.66
ATOM    922  CG  TYR A 119      22.015  67.826  33.628  1.00 24.10
ATOM    923  CD1 TYR A 119      22.868  67.573  34.703  1.00 24.04
ATOM    924  CD2 TYR A 119      22.316  67.246  32.395  1.00 24.02
ATOM    925  CE1 TYR A 119      23.989  66.763  34.558  1.00 24.38
ATOM    926  CE2 TYR A 119      23.434  66.437  32.237  1.00 25.15
ATOM    927  CZ  TYR A 119      24.268  66.198  33.322  1.00 25.90
ATOM    928  OH  TYR A 119      25.378  65.395  33.169  1.00 26.39
ATOM    929  N   VAL A 120      19.476  71.383  32.512  1.00 31.70
ATOM    930  CA  VAL A 120      18.256  72.130  32.229  1.00 36.89
ATOM    931  C   VAL A 120      17.421  71.397  31.180  1.00 40.66
ATOM    932  O   VAL A 120      17.902  70.482  30.515  1.00 40.43
ATOM    933  CB  VAL A 120      18.580  73.541  31.701  1.00 36.48
ATOM    934  CG1 VAL A 120      17.311  74.362  31.600  1.00 37.47
ATOM    935  CG2 VAL A 120      19.576  74.218  32.614  1.00 37.96
ATOM    936  N   GLN A 121      16.168  71.815  31.034  1.00 45.69
ATOM    937  CA  GLN A 121      15.245  71.206  30.085  1.00 50.15
ATOM    938  C   GLN A 121      15.535  71.569  28.624  1.00 52.61
ATOM    939  O   GLN A 121      15.498  72.741  28.249  1.00 52.73
ATOM    940  CB  GLN A 121      13.818  71.625  30.446  1.00 50.81
ATOM    941  CG  GLN A 121      12.727  71.050  29.565  1.00 53.59
ATOM    942  CD  GLN A 121      11.349  71.556  29.958  1.00 54.25
ATOM    943  OE1 GLN A 121      10.339  71.182  29.362  1.00 55.31
ATOM    944  NE2 GLN A 121      11.305  72.415  30.965  1.00 55.56
ATOM    945  N   ALA A 122      15.827  70.555  27.807  1.00 55.69
ATOM    946  CA  ALA A 122      16.086  70.750  26.379  1.00 58.75
ATOM    947  C   ALA A 122      14.694  70.827  25.757  1.00 61.08
ATOM    948  O   ALA A 122      14.430  70.328  24.661  1.00 61.85
ATOM    949  CB  ALA A 122      16.855  69.562  25.817  1.00 58.74
ATOM    950  N   ASP A 123      13.820  71.474  26.514  1.00 63.55
ATOM    951  CA  ASP A 123      12.414  71.678  26.218  1.00 65.57
ATOM    952  C   ASP A 123      11.895  71.976  24.822  1.00 66.84
ATOM    953  O   ASP A 123      12.521  72.656  24.006  1.00 67.33
ATOM    954  CB  ASP A 123      11.873  72.774  27.135  1.00 66.62
ATOM    955  CG  ASP A 123      12.387  74.153  26.763  1.00 67.30
ATOM    956  OD1 ASP A 123      13.610  74.304  26.565  1.00 67.10
ATOM    957  OD2 ASP A 123      11.564  75.091  26.677  1.00 67.29
ATOM    958  N   TYR A 124      10.698  71.448  24.612  1.00 67.81
ATOM    959  CA  TYR A 124       9.867  71.605  23.433  1.00 68.62
ATOM    960  C   TYR A 124       8.539  71.609  24.172  1.00 68.75
ATOM    961  O   TYR A 124       7.478  71.887  23.612  1.00 69.00
ATOM    962  CB  TYR A 124       9.985  70.408  22.480  1.00 69.32
ATOM    963  CG  TYR A 124      11.147  70.528  21.515  1.00 70.00
ATOM    964  CD1 TYR A 124      11.222  71.602  20.628  1.00 69.97
ATOM    965  CD2 TYR A 124      12.180  69.591  21.502  1.00 70.00
ATOM    966  CE1 TYR A 124      12.296  71.745  19.753  1.00 70.00
ATOM    967  CE2 TYR A 124      13.265  69.724  20.628  1.00 70.00
ATOM    968  CZ  TYR A 124      13.315  70.807  19.758  1.00 70.00
ATOM    969  OH  TYR A 124      14.381  70.965  18.905  1.00 70.00
ATOM    970  N   GLY A 125       8.649  71.310  25.468  1.00 68.62
ATOM    971  CA  GLY A 125       7.512  71.285  26.367  1.00 68.76
ATOM    972  C   GLY A 125       6.548  70.130  26.199  1.00 68.83
ATOM    973  O   GLY A 125       6.253  69.418  27.159  1.00 69.01
ATOM    974  N   ASP A 126       6.056  69.954  24.978  1.00 68.49
ATOM    975  CA  ASP A 126       5.096  68.904  24.655  1.00 67.78
ATOM    976  C   ASP A 126       5.423  67.583  25.343  1.00 67.02
ATOM    977  O   ASP A 126       4.524  66.825  25.713  1.00 66.53
ATOM    978  CB  ASP A 126       5.060  68.686  23.139  1.00 68.21
ATOM    979  CG  ASP A 126       6.207  67.820  22.644  1.00 68.64
ATOM    980  OD1 ASP A 126       7.376  68.131  22.959  1.00 68.84
ATOM    981  OD2 ASP A 126       5.938  66.831  21.928  1.00 69.06
ATOM    982  N   ASP A 127       6.717  67.336  25.513  1.00 66.23
ATOM    983  CA  ASP A 127       7.251  66.122  26.128  1.00 65.12
ATOM    984  C   ASP A 127       6.337  65.411  27.131  1.00 63.48
ATOM    985  O   ASP A 127       6.385  65.682  28.331  1.00 64.01
ATOM    986  CB  ASP A 127       8.583  66.436  26.816  1.00 66.38
ATOM    987  CG  ASP A 127       9.544  67.201  25.922  1.00 67.53
ATOM    988  OD1 ASP A 127       9.780  66.760  24.776  1.00 67.61
ATOM    989  OD2 ASP A 127      10.078  68.237  26.375  1.00 68.48
ATOM    990  N   PRO A 128       5.489  64.486  26.653  1.00 61.41
ATOM    991  CA  PRO A 128       4.588  63.755  27.546  1.00 59.31
ATOM    992  C   PRO A 128       5.354  62.676  28.315  1.00 57.38
ATOM    993  O   PRO A 128       5.502  62.742  29.535  1.00 57.38
ATOM    994  CB  PRO A 128       3.587  63.153  26.571  1.00 59.76
ATOM    995  CG  PRO A 128       4.499  62.782  25.419  1.00 59.90
ATOM    996  CD  PRO A 128       5.247  64.091  25.251  1.00 61.04
ATOM    997  N   ALA A 129       5.847  61.691  27.569  1.00 54.84
ATOM    998  CA  ALA A 129       6.585  60.567  28.125  1.00 52.05
ATOM    999  C   ALA A 129       8.082  60.700  27.889  1.00 50.25
ATOM   1000  O   ALA A 129       8.832  59.738  28.057  1.00 49.69
ATOM   1001  CB  ALA A 129       6.074  59.272  27.510  1.00 52.37
ATOM   1002  N   VAL A 130       8.515  61.892  27.495  1.00 47.59
ATOM   1003  CA  VAL A 130       9.929  62.134  27.247  1.00 45.70
ATOM   1004  C   VAL A 130      10.385  63.353  28.036  1.00 44.13
ATOM   1005  O   VAL A 130       9.639  64.315  28.185  1.00 43.95
ATOM   1006  CB  VAL A 130      10.200  62.370  25.747  1.00 45.58
ATOM   1007  CG1 VAL A 130      11.691  62.557  25.510  1.00 45.72
ATOM   1008  CG2 VAL A 130       9.678  61.194  24.937  1.00 45.84
ATOM   1009  N   ALA A 131      11.609  63.304  28.548  1.00 42.55
ATOM   1010  CA  ALA A 131      12.158  64.408  29.324  1.00 41.67
ATOM   1011  C   ALA A 131      13.649  64.522  29.056  1.00 40.92
ATOM   1012  O   ALA A 131      14.453  63.782  29.619  1.00 40.96
ATOM   1013  CB  ALA A 131      11.907  64.181  30.809  1.00 41.45
ATOM   1014  N   LEU A 132      14.016  65.457  28.190  1.00 40.09
ATOM   1015  CA  LEU A 132      15.409  65.649  27.844  1.00 40.16
ATOM   1016  C   LEU A 132      16.043  66.775  28.642  1.00 40.27
ATOM   1017  O   LEU A 132      15.403  67.788  28.932  1.00 39.72
ATOM   1018  CB  LEU A 132      15.538  65.943  26.349  1.00 40.21
ATOM   1019  CG  LEU A 132      16.968  66.127  25.840  1.00 41.69
ATOM   1020  CD1 LEU A 132      17.789  64.897  26.188  1.00 42.10
ATOM   1021  CD2 LEU A 132      16.957  66.358  24.337  1.00 42.00
ATOM   1022  N   TYR A 133      17.305  66.584  29.004  1.00 39.82
ATOM   1023  CA  TYR A 133      18.039  67.592  29.746  1.00 39.98
ATOM   1024  C   TYR A 133      19.365  67.857  29.056  1.00 40.55
ATOM   1025  O   TYR A 133      19.934  66.975  28.416  1.00 40.99
ATOM   1026  CB  TYR A 133      18.310  67.149  31.186  1.00 38.74
ATOM   1027  CG  TYR A 133      17.086  66.979  32.058  1.00 38.16
ATOM   1028  CD1 TYR A 133      16.255  65.864  31.928  1.00 37.46
ATOM   1029  CD2 TYR A 133      16.770  67.929  33.030  1.00 36.69
ATOM   1030  CE1 TYR A 133      15.141  65.697  32.752  1.00 37.61
ATOM   1031  CE2 TYR A 133      15.665  67.776  33.855  1.00 36.81
ATOM   1032  CZ  TYR A 133      14.855  66.659  33.718  1.00 37.71
ATOM   1033  OH  TYR A 133      13.782  66.499  34.565  1.00 35.54
ATOM   1034  N   THR A 134      19.858  69.078  29.195  1.00 41.10
ATOM   1035  CA  THR A 134      21.121  69.455  28.598  1.00 42.18
ATOM   1036  C   THR A 134      21.969  70.010  29.722  1.00 42.65
ATOM   1037  O   THR A 134      21.444  70.557  30.689  1.00 43.58
ATOM   1038  CB  THR A 134      20.926  70.532  27.530  1.00 42.98
ATOM   1039  OG1 THR A 134      19.945  70.083  26.588  1.00 44.79
ATOM   1040  CG2 THR A 134      22.235  70.795  26.798  1.00 43.38
ATOM   1041  N   LYS A 135      23.279  69.870  29.594  1.00 43.06
ATOM   1042  CA  LYS A 135      24.180  70.343  30.621  1.00 43.54
ATOM   1043  C   LYS A 135      24.456  71.834  30.569  1.00 44.55
ATOM   1044  O   LYS A 135      24.992  72.352  29.590  1.00 45.29
ATOM   1045  CB  LYS A 135      25.503  69.580  30.547  1.00 43.07
ATOM   1046  CG  LYS A 135      26.542  70.034  31.556  1.00 42.82
ATOM   1047  CD  LYS A 135      27.773  69.131  31.522  1.00 41.95
ATOM   1048  CE  LYS A 135      27.402  67.693  31.865  1.00 42.58
ATOM   1049  NZ  LYS A 135      28.573  66.775  31.905  1.00 41.32
ATOM   1050  N   LEU A 136      24.064  72.524  31.630  1.00 45.16
ATOM   1051  CA  LEU A 136      24.321  73.948  31.745  1.00 45.40
ATOM   1052  C   LEU A 136      25.738  73.971  32.310  1.00 45.94
ATOM   1053  O   LEU A 136      26.595  74.724  31.854  1.00 46.20
ATOM   1054  CB  LEU A 136      23.345  74.583  32.735  1.00 44.96
ATOM   1055  CG  LEU A 136      23.478  76.078  33.029  1.00 45.50
ATOM   1056  CD1 LEU A 136      23.244  76.883  31.761  1.00 45.68
ATOM   1057  CD2 LEU A 136      22.475  76.472  34.093  1.00 45.37
ATOM   1058  N   GLY A 137      25.973  73.105  33.295  1.00 46.93
ATOM   1059  CA  GLY A 137      27.275  73.013  33.926  1.00 46.95
ATOM   1060  C   GLY A 137      27.253  73.457  35.375  1.00 46.70