Salve!

I am refining a protein/ligand complex where the ligand is bound with two conformers.

Conformer A is covalently bound to a cysteine residue.

Conformer B is free.

I have prepared an appropriate cif dictionary for the ligand including info on handling the link.

The problem is that during refinement, non-bonded interactions between the two conformers appear to not be switched off and their geometry becomes distorted.

Is this diagnosis correct? If so, is there a way to manually switch off interactions?

With thanks,

a++

Aaron Oakley
Associate Professor
School of Chemistry and Molecular Bioscience | Molecular Horizons | Faculty of Science, Medicine and Health
University of Wollongong NSW 2522 Australia
T +61 2 4221 4347 | F +61 2 4221 4287