Hi,
assume you have a protein structure (P1) and a second protein sequence
(S1) without structure. Both sequences align with about 50% sequence
identity over a large portion of both sequences without gaps
(Smith+Waterman).
Is there a way to automatically exchange residues from P1 against the
respective residues in S1 (maybe using a script that exploits the
mutate wizzard residue by residue ?) and do a final bond relaxation /
sidechain orientation / H-bond-length correction ?
Yes, I know, this is more than visualizing ...
Best regards
Uwe Hobohm
