Accurate protein structure modeling using sparse NMR data and homologous structure information.

ABSTRACT: While information from homologous structures plays a central role in X-ray structure determination by molecular replacement, such information is rarely used in NMR structure determination because it can be incorrect, both locally and globally, when evolutionary relationships are inferred incorrectly or there has been considerable evolutionary structural divergence. Here we describe a method that allows robust modeling of protein structures of up to 225 residues by combining (1)H(N), (13)C, and (15)N backbone and (13)Cβ chemical shift data, distance restraints derived from homologous structures, and a physically realistic all-atom energy function. Accurate models are distinguished from inaccurate models generated using incorrect sequence alignments by requiring that (i) the all-atom energie

SUBMITTER: Thompson JM 

PROVIDER: S-EPMC3382498 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature