A method for evaluating the structural quality of protein models by using higher-order – 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 – angles. The sliding window ranges in size from a length of 1–10 – pairs (3–12 residues). In this method, the conformation of each fragment is scored based on the fit of multiple – angles of the fragment to a database of multiple – 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 – score fit values (m) > 1.00.