Hello, I have a few questions pertaining to Marvin.
I'm working with a protein that is 189 residues in length and I have a total of 6900 restraints. Has anyone had much luck with Marvin on proteins of this size or larger? 1.) Would it sound logical to increase the number of structures to 1000 and just take the top 5% or would it be best to increase the number of passes? If I was to increase the number of passes would it be best to increase the number of passes with the linear NOE potential energy function or the pass with the Quadratic NOE potential energy function? 2.) Is there a script that can search for symmetry partners in both 15N and 13C-edited NOE spectra? 3.) I've noticed that there are a few restraints with degeneracy of 1 after the initialMatch script that should have a higher degree of degeneracy. I've noticed this with my protein as well as the interleukin-4 example. These assignments don't have a symmetry partner either. Has anyone else noticed this? Thank you very much for your time and appreciation! Aaron B. Cowley, PhD University of Georgia [email protected]
