> Hi everybody,
> I’m trying to fold a protein sequence using the abinitio module in rosetta3. I know that two cysteins make a disulfide bond so I have tried to put distance constrains between CA atoms in a .cst file but the structures generated do not have this bond formed. How can I tell rosetta that two cys are forming a disulfide bond?
> Thanks a lot
I have a native structure and in the native structure I have the disulfide bond. I fix residues to native, I use a disulfide file giving -fix_disulf filename and -detect_disulfides in the flag file. I also use the cst file where I put some distance constrains but even like this during the folding the native conformation is not maintain and the disulfide bond is not there. I have also added cst_weigth 1000. I have taken a look to the log file and at the begining of the folding says: detected disulfide bond between residues 19 and 45 which is correct!!!
Have any idea?