Dear Herman,
On Thu, Feb 07, 2019 at 10:26:09AM +, Herman Schreuder wrote:
> I did understand your question correctly and (at least for ligands)
> the procedure I and also Diana Tomchick described, worked. However,
> I just did a test with both Refmac and Buster and it seems that
> these progr
Ed,
I did understand your question correctly and (at least for ligands) the
procedure I and also Diana Tomchick described, worked. However, I just did a
test with both Refmac and Buster and it seems that these programs have now so
far been perfected that “errors” like this cannot occur anymore.
I agree. We have encountered refinement problems similar to those Ed
describes for models with mixtures of modified cysteine species, which is
a fairly common occurrence.
Best regards,
Mark
Mark A. Wilson
Associate Professor
Department of Biochemistry/Redox Biology Center
University of Nebraska
N1
The situation might not be so rare, if you consider 50% Lys and
50% Acetyl-Lys or other post-translational modifications.
Gottfried
On Wednesday, 06-02-2019 at 18:05 Diana Tomchick wrote:
If you have the odd case where one residue (of the same number in the
polypeptide chain) is a Leu and the
If you have the odd case where one residue (of the same number in the
polypeptide chain) is a Leu and the alternative residue is a Phe, then it would
be ALEU and BPHE, both residues would have the same residue number, and reset
the occupancies to fractions that sum to 1.0.
Diana
**
Dear Edwin,
I do not know whether your question has been answered already, but the answer
is simple: you have to define alternative conformations. Easiest is to generate
them in coot with the “add alternate conformation” option in the right panel.
You may have to delete the original unlabeled a
