| Hi modellers, I'm trying to build a homology model of a multi-chain heteromeric protein (with model-default.py script) using as template a homomeric protein as showed in the following example: #begin of "ali" file >P1;pdb structureX:pdb:1:A:10::::: AAAAAAAAAA/ AAAAAAAAAA/ AAAAAAAAAA/ AAAAAAAAAA/ AAAAAAAAAA* >P1;ABBAB sequence::::::::: AAAAAAAAAA/ BBBBBBBBBB/ BBBBBBBBBB/ AAAAAAAAAA/ BBBBBBBBBB* #End of "ali" file The model is built normally. However, I noticed that many residues in the active site (which is localized in the interface between each pair of monomers) that are supposed to exposed are turned inside out. I tried to model just as homomeric and so all important side chains in the active site kept the template position. Is there anything I can do to make the modeled residues to adopt the same position as in the template? Would it be reasonable? I'd appreciate any help! Best regards, Josmar Rocha |