OPUS-Rota2: An Improved Fast and Accurate Side-Chain Modeling Method

J Chem Theory Comput. 2019 Sep 10;15(9):5154-5160. doi: 10.1021/acs.jctc.9b00309. Epub 2019 Aug 26.

Abstract

Side-chain modeling plays a critical role in protein structure prediction. However, in many current methods, balancing the speed and accuracy is still challenging. In this paper, on the basis of our previous work OPUS-Rota (Protein Sci. 2008, 17, 1576-1585), we introduce a new side-chain modeling method, OPUS-Rota2, which is tested on both a 65-protein test set (DB65) in the OPUS-Rota paper and a 379-protein test set (DB379) in the SCWRL4 paper. If the main chain is native, OPUS-Rota2 is more accurate than OPUS-Rota, SCWRL4, and OSCAR-star but slightly less accurate than OSCAR-o. Also, if the main chain is non-native, OPUS-Rota2 is more accurate than any other method. Moreover, OPUS-Rota2 is significantly faster than any other method, in particular, 2 orders of magnitude faster than OSCAR-o. Thus, the combination of higher accuracy and speed of OPUS-Rota2 in modeling side chains on both the native and non-native main chains makes OPUS-Rota2 a very useful tool in protein structure modeling.

MeSH terms

  • Algorithms
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular*
  • Protein Conformation
  • Proteins / chemistry*

Substances

  • Proteins