Many proteins need to form oligomers to be functional, so oligomer structures provide important clues to biological roles of proteins. Prediction of oligomer structures therefore can be a useful tool in the absence of experimentally resolved structures. In this article, we describe the server and human methods that we used to predict oligomer structures in the CASP13 experiment. Performances of the methods on the 42 CASP13 oligomer targets consisting of 30 homo-oligomers and 12 hetero-oligomers are discussed. Our server method, Seok-assembly, generated models with interface contact similarity measure greater than 0.2 as model 1 for 11 homo-oligomer targets when proper templates existed in the database. Model refinement methods such as loop modeling and molecular dynamics (MD)-based overall refinement failed to improve model qualities when target proteins have domains not covered by templates or when chains have very small interfaces. In human predictions, additional experimental data such as low-resolution electron microscopy (EM) map were utilized. EM data could assist oligomer structure prediction by providing a global shape of the complex structure.
Keywords: CASP13; cryo EM data-assisted complex structure prediction; protein model structure refinement; protein oligomer structure prediction.
© 2019 Wiley Periodicals, Inc.