volume 85, issue 3, P463-469 2016
DOI: 10.1002/prot.25182
View full text
|
Sign up to set email alerts
|
Share

Abstract: Many of the modeling targets in the blind CASP-11/CAPRI-30 experiment were protein homo-dimers and homo-tetramers. Here, we perform a retrospective docking-based analysis of the perfectly symmetrical CAPRI Round 30 targets whose crystal structures have been published. Starting from the CASP "stage-2" fold prediction models, we show that using our recently developed "SAM" polar Fourier symmetry docking algorithm combined with NAMD energy minimization often gives acceptable or better 3D models of the target comp…

Expand abstract