Hi Modeller Caretaker,
Thanks very much for your explain on 'restraints failed' and this one.
I am sure that the alignment is correct because the target and template proteins are the same protein.
There are two chains in the template, it is kind of a dimer of one protein. The conformations of both chains are extended helix. What I want to do is to model a copper coordination, two ligands from one chain, the other two from the other chain. All the four ligands locate at the N-terminal.
I don't understand why the conformations of generared modelsl have folded conformations, the C-terminal is quite close to the N-terminal. Could you please give me some suggestions? Thanks in advance!
All the best, Qinghua
On 10/15/2013 12:27 AM, Modeller Caretaker wrote: > On 10/14/13 7:55 AM, fantasticqhl wrote: >> I am trying to construct a model with two chains, the conformation of >> the template is extended helix, >> However, the conformations of the model I got were folded, the >> C-terminal is very close to the N-terminal. > > This suggests that your alignment is incorrect. > > Ben Webb, Modeller Caretaker