From pozharskibb at gmail.com Tue Sep 18 21:00:18 2018 From: pozharskibb at gmail.com (Edwin Pozharski) Date: Tue, 18 Sep 2018 15:00:18 -0400 Subject: [buster-discuss] target restraints Message-ID: Hello, it's entirely possible that this is a straightforward case of RTFM, please feel free to point it out (ideally with link to the actual manual pages that I need to look at). I am looking into using a higher resolution model to improve geometry at 3.7A resolution. What I found so far describes what to do when the reference model is that of the same protein. I don't have that here, instead it's a homologue with some 40% identity. From what I understood so far, buster doesn't do any sequence/structure alignment. Do I have options other than mutating/editing the reference model? Also, I got a general feeling that this option in buster is tailored to cases where changes are minimal - say, low resolution data on protein-ligand complex of lock-and-key type. And that with large conformational changes the strategy should be to include only parts of the reference model that stay constant. Is that a fair characterization? Thanks, Ed. -------------- next part -------------- An HTML attachment was scrubbed... URL: