Hello Charles and others,
I have refined some structures from solid-state NMR restraints. When we
compare the NMR structure of our protein with X-ray structures with
different binding partners, we find some PHE's aromatic rings present
rotamer difference between NMR structure and the X-ray structures. It is
hard for us to judge that this rotamer difference is a result of real
difference in structures or it is just because of lacking of restraints to
constrain the side-chain torsion angles.
We only used distance restraints and backbone torsion angle restraints
for the structure refinements. In our NMR restraints list for the
structure refinement, there is no restraints from the atoms of the aromatic
rings.
My question is there any way to constrain the side-chain torsion angle
in Xplor-NIH?
I saw a function named
*correctSymmetricSidechains in selectTools module.*
But I am not sure if this the correct thing I should include in my
refinements. If this is what I could use, how can I use it properly?
Thanks very much!
Best
Si
--
Si Yan
Department of Chemistry and Biochemistry
University of Delaware
Newark, DE, 19716
Email to s...@udel.edu
Phone: 302-831-8624
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