A method for evaluating the structural quality of protein models by using higher-order phi-psi pairs scoring.
A method is presented for scoring the model quality of experimental and theoretical protein structures. The structural model to be evaluated is dissected into small fragments via a sliding window, where each fragment is represented by a vector of multiple phi-psi angles. The sliding window ranges in size from a length of 1-10 phi-psi pairs (3-12 residues). In this method, the conformation of each fragment is scored based on the fit of multiple phi-psi angles of the fragment to a database of multiple phi-psi angles from high-resolution x-ray crystal structures. We show that measuring the fit of predicted structural models to the allowed conformational space of longer fragments is a significant discriminator for model quality. Reasonable models have higher-order phi-psi score fit values (m) > -1.00.
Berkeley Structural Genomics Center, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Gregory E
GE
Sims
Sung-Hou
SH
Kim
D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012107:Research Design
D011506:Proteins