[phenixbb] selective nonbonded restraint removal
cathy.lawson at rutgers.edu
Wed Sep 5 07:30:39 PDT 2007
Thanks to all who replied.
And thank you Ralf for your suggestion (quoted below), this worked
Somehow I missed this possibility in the online documentation.
To reply to Pavel's question regarding how I figured out that tris is
present at 1/2 occupancy:
(1) density was first modelled with waters but they were too close
together, and there was a fairly clear tetrahedral shape.
(2) phosphate didn't refine well -- lead to huge negative difference
peak at the P atom.
(3) only other tetrahedral shape molecule in the soup was tris (TAM),
and after refining just the tetrahedral core it was possible to see
where the three arms extended.
(4) b-factors for the tris were high relative surrounding protein
atoms, and extraneous density suggested two alternate conformations
for the nearby arg side-chain, one of which is too close to
realistically exist next to the tris ligand. the other clue was
that trial occupancy refinement of all atoms put most tris atoms in
the 0.4-0.6 occupancy range.
(5) tris with 0.5 occupancy, arg with two alt confs, plus a few
waters at 0.5 occupancy is so far the best model with no significant
different densities for this region.
(6) the modelling will need to be confirmed with an SA omit ...
> Hi Cathy,
> > The density suggests that when tris is not there,
> > a side chain moves very close to that position
> You could model this with alternative conformations. If you assign
> "altloc" A and B to two conformers of your protein, and just, say, B
> to your TAM, then the ligand would only "see" your B protein. If you
> don't define the B conformer (no atoms) then TAM wouldn't see that
> part of the protein at all.
> Actually, this approach seems better to me than working with
> atom selections.
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