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<html>

<head>
<title>
WHE, WHEEL
</title>
</head>

<h1 align=center>

WHE, WHEEL

</h1>

<hr size="3">

<font color=#880000>
<b>
NAME
<br>
</b>
</font>


WHE, WHEEL - draw helical wheel plot.
<br><br>


<font color=#880000>
<b>
SYNOPSIS
<br>
</b>
</font>

<table border=1 cellspacing=1 cellpading=0>

<td align="left">
<font color=#004400>
<b>
SHORT FORM
</b>
</font>
</td>

<td align="left">
<font color=#004400>
<b>
LONG FORM
</b>
</font>
</td>

<tr>

<td align="left">


WHE
<br>
WHE CLO
<br>
WHE start_index end_index
<br>
WHE start_index end_index CLO
<br>
WHE OFF

</td>

<td align="left">


WHEEL
<br>
WHEEL CLOCKWISE
<br>
WHEEL start_index end_index
<br>
WHEEL start_index end_index CLOCKWISE
<br>
WHEEL OFF

</td>

</table>

<br>

<font color=#880000>
<b>
DESCRIPTION
<br>
</b>
</font>


Draw helical wheel plot for the given sequence or sequence fragment. Helical
wheel may be used to recognize the amphiphilic character of the specified
sequence fragment. The sequence from the main sequence buffer (or part of it)
is used as input. Additional input: the rotation angle between adjacent
residues and hydrophobicity values. The angle should correspond to certain
structural motif. Default (hard-coded) angle is 100 degrees, which corresponds
to alpha helix, but this may be changed to some arbitrary value, using the
command ANGLE. The value of 160 degrees is suitable for beta strand and 115
or 125 is suitable for 3-10 helix.
<br><br>

While helical wheel may be drawn for any sequence length, it makes sense only
for short sequence fragments (up to about twenty residues). Hydrophobic
residues will be colored in shades of red, while hydrophilic residues will be
colored blue. Color intensity depends on the hydrophobicity: very hydrophobic
residues will be intensely red and weakly hydrophobic residues will be
almost white. Very hydrophilic residues will be intensely blue and weakly
hydrophilic residues will be almost white. The command SCALE may be used to
select the hydrophobicity scale.
<br><br>

The command WHEEL is usually used in combination with some other commands.
See the examples below.
<br><br>

<img src="wheel.gif">
<br><br>


<font color=#880000>
<b>
KEYWORDS AND PARAMETERS
<br>
</b>
</font>


The command WHEEL may be used alone, combined with one of two keywords (OFF
and CLOCKWISE) or with two residue numbers. Note that from version 1.4,
residue array indices are used instead of serial indices! There was some mess
with the structures which consist of multiple chains, so the actual residue
numbers (related to array indices) proved to be more reliable than the serial
numbers. If you specify the residue range from 1 to 10, the residues having
the array indices between 0 and 9 will be used. This is because the lowest
array index in the C programming language is zero, not one.
<br><br>

If used alone, the helical wheel will be drawn for the entire sequence stored
in the main sequence buffer. If this sequence is large the plot will be
useless. Two residue numbers may be used to specify the residue range.
<br><br>

By default, residues are drawn counterclockwise. This arrangement of residues
gives the top view of a helix. The keyword CLO (long form: CLOCKWISE) may be
used to force clockwise arrangement of residues (the bottom view of a helix). 
<br><br>

The keyword OFF is used to return to the main drawing mode (the structure
drawing mode).
<br><br>


<font color=#880000>
<b>
EXAMPLES
<br>
</b>
</font>

<table border=2 cellspacing=2 cellpading=0>

<td align="left">


COMMAND

</td>

<td align="left">


DESCRIPTION

</td>

<tr>

<td align="left">


seq = asp ile met ala glu ile
<br>
scale eis
<br>
angle 100
<br>
wheel

</td>

<td align="left">


Initialize the sequence fragment,
<br>
select Eisenberg hydrophobicity scale,
<br>
set angle to 100 degrees and draw
<br>
helical wheel. It is assumed that
<br>
that the specified sequence fragment
<br>
belongs to alpha helix.

</td>

<tr>

<td align="left">


load 2por.pdb
<br>
seq from 1
<br>
scale eis
<br>
angle 160
<br>
wheel 2-10

</td>

<td align="left">


Load porin coordinates, copy the sequence
<br>
of this protein to the main sequence
<br>
buffer, select Eisenberg hydrophobicity
<br>
scale, set angle to 160 degrees and draw
<br>
helical wheel for residues from 2 to 10.
<br>
It is assumed that the specified sequence
<br>
fragment belongs to beta strand.

</td>

<tr>

<td align="left">


whe clo

</td>

<td align="left">


Draw residues clockwise. This
<br>
gives the bottom view of a helix,
<br>
which is more common in books.

</td>

<tr>

<td align="left">


whe off

</td>

<td align="left">


Return to default drawing mode.
<br>
Instead using this command,
<br>
you can hit the ESCAPE key.

</td>

</table>

<br>

<font color=#880000>
<b>
NOTES
<br>
</b>
</font>


(1) Instead using the command WHEEL OFF, the ESCAPE key may be pressed to
return to the main drawing mode.
<br><br>

(2) Don't forget that WHEEL uses only the sequence stored to the main
sequence buffer. Read description of the command SEQ (SEQUENCE) to learn
how to initialize this buffer.
<br><br>



<font color=#880000>
<b>
RELATED COMMANDS
<br>
</b>
</font>


SEQUENCE is used to copy, define or load the sequence. ANGLE defines the
rotation angle between adjacent residues. SCALE is used to specify the
hydrophobicity scale.
<br><br>


<hr size="3">

</html>