Hi,
I have a file which contains a protein and a bunch of ligands. The
ligands come from a Monte Carlo simulation where they were allowed to talk
to the protein, but not to eachother. So, lots of the ligands overlap.
When PyMOL sees this, it draws bonds between the ligands. Every time I
load up one of these structures, I have to unbond things with something
like
for i in range(160,660):cmd.do('unbond resi %s, not resi %s'%(i,i))
which takes a *really* long time. Is there a faster way to do this? I
once hacked up the PyMOL source so that HETATMS with resi > N didn't get
bonded to anything else in the first place, but that's obviously a bad way
to do things (and I can't seem to compile things myself on our SGIs, so
it doesn't work there anyway).
Thanks,
-michael
--
This isn't a democracy;| _ |Michael Lerner
it's a cheer-ocracy. | ASCII ribbon campaign ( ) | Michigan
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| / \ | mler...@umich
