On 11/12/2017 15:44, wtempel wrote:
Hello all, the documentation https://www.phenix-online.org/documentation/faqs/refine.html states that
This is somewhat controversial, but absolute upper limits for a well-refined protein structure at high resolution are typically 0.02 for RMS(bonds) and 2.0 for RMS(angles); usually they will be significantly lower.
I understand that exceedingly high RMSDs from ideal could indicate overfitting.
Do you mean _low_ RMSDs from ideal?
On the other hand, local deviations from ideal geometry may point to correctable modeling errors,
Yes.
and I am concerned that overly tight restraints may cause that diagnostic tool to become less sensitive, or local errors to be spread in to the model.
Refinement (with conventional-style restraints) will try to "spread the load" to other geometric parameters - not only tightly-restrained refinement. A tightly-restrained structure will have less geometric distortions than a less tightly restrained one (as measured by the geometry against which the model is refined), so yes, a diagnostic tool designed to look for issues in geometric restraints will be less sensitive in that case (at least on the absolute scale, it is quite likely that they will nevertheless be larger than "neighbouring" restraints). In my experience looking at high resolution structures, there is less "real" distortions of side-chain angles than for the main-chain angles (bonds are not so noticeably distorted).
For what bond and angle rms deviations from ideal do my colleagues on the BB aim and how have they arrived at those targets? Did my web search miss a relevant paper?
I don't know about that, but I see nothing with which I would disagree in the phenix.refine documentation. I would add though that, as a rule of thumb, the lower the resolution of the structure, the more the model should comport with known geometry (again, as measured by the geometry against which the model has been refined). Paul.