Hello everyone,
I am in the final rounds of refining my protein at high resolution
and currently trying to model an alternative conformation of a Chl a-phytol
chain. I inserted a second phytol chain with coot - worked out well
so far (alternate chain identifiers A and B for both phytol chains).
After using phenix.refine, however, the occupancy of the second
phytol chain was refined to 0. When splitting the whole Chl molecule
the occupancy refines to sensible values (0.34 and 0.66). We would
prefer to only model the phytol chain in alternate conformation as
the macrocycle superpose perfectly. Any suggestions regarding the
occupancy problem?
Another issue concerns restraints. We tried to turn of specific
nonbonded restraints and found a phenixbb message from 2007:
http://www.phenix-online.org/pipermail/phenixbb/2007-September/011734.html
Are there any news/updates on this matter?
Any help appreciated!
Thanks,
Moritz
--
Moritz M. Machelett
Ruhr University Bochum
Protein Crystallography, Department of Biophysics, ND04/396
44780 Bochum
Tel: +49-(0)234/32-25754