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Evaluation of comparative protein modeling by M ODELLER
Author(s) -
Šali Andrej,
Potterton Liz,
Yuan Feng,
van Vlijmen Herman,
Karplus Martin
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340230306
Subject(s) - protein data bank (rcsb pdb) , protein structure , template , modeller , protein data bank , crystallography , protein structure prediction , chemistry , computational biology , biology , homology modeling , stereochemistry , biochemistry , materials science , nanotechnology , enzyme
We evaluate 3D models of human nucleoside diphosphate kinase, mouse cellular retinoic acid binding protein I, and human eosinophil neurotoxin that were calculated by M ODELLER , a program for comparative protein modeling by satisfaction of spatial restraints. The models have good stereochemistry and are at least as similar to the crystallographic structures as the closest template structures. The largest errors occur in the regions that were not aligned correctly or where the template structures are not similar to the correct structure. These regions correspond predominantly to exposed loops, insertions of any length, and non‐conserved side chains. When a template structure with more than 40% sequence identity to the target protein is available, the model is likely to have about 90% of the mainchain atoms modeled with an rms deviation from the X‐ray structure of ≈ 1 Å, in large part because the templates are likely to be that similar to the X‐ray structure of the target. This rms deviation is comparable to the overall differences between refined NMR and X‐ray crystallography structures of the same protein. © 1995 Wiley‐Liss, Inc.