Hi Walter, My suggestion would be to calculate OMIT map and construct alternative conformations based on it. At 1.1A resolution it either works or you don't have alternative conformations. Also, validation criteria are statistical measures (mostly), and they tend to be tuned to most occurring cases based on data bases (PDB). So obviously deviations are possible and expected. As Ed pointed out already you should trust your 1.1A map, and OMIT map should help you get most of it. Pavel On 8/17/12 8:07 AM, Walter R.P. Novak wrote:
Hi,
I have a relatively high-resolution (1.1 A) structure and one threonine residue has a C-beta deviation outlier that I cannot prevent via any traditional means. I would like to try to restrain the C-beta deviation for this residue by scaling the geometry restraints for this residue, but I am not sure of how I should define the restraint for C-beta. Any suggestions are greatly appreciated.
Thanks, Wally