Dear All, I am working with a protein, the structure of which is already published in the PDB (2 chains in asu) The published structure has a break of around 20 residues.
I have crystallized the same protein and saw some density near the gap (20 residues break). I could build 3-4 residues in ChainA and 8 residues in ChainB (in the 20 residue break region). After refinement these showed good density and b factor. But the issue is that in ChainA, it goes straight. While in ChainB, the 8 residues converge into a loop and goes to the other side. The protein is a monomer in solution, is it possible to have different conformation in different chains that is completely opposite. Also the 8 residues (ChainB) that is build now occupies the site where ligand was placed in the published structure. I am not sure how to interpret this (since in ChainA that site is unoccupied as contrast to ChainB). Any thoughts/suggestions will be really helpful. Thanks you ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
