Assessment of the model refinement category in CASP12

被引:29
作者
Hovan, Ladislav [1 ]
Oleinikovas, Vladimiras [1 ]
Yalinca, Havva [1 ]
Kryshtafovych, Andriy [2 ]
Saladino, Giorgio [1 ]
Gervasio, Francesco Luigi [1 ,3 ]
机构
[1] UCL, Dept Chem, London WC1E 6BT, England
[2] Univ Calif Davis, Genome Ctr, Davis, CA 95616 USA
[3] UCL, Inst Struct & Mol Biol, London WC1E 6BT, England
基金
英国生物技术与生命科学研究理事会; 英国惠康基金; 英国工程与自然科学研究理事会;
关键词
CASP; CASP12; enhanced sampling algorithms; model refinement; molecular dynamics; protein structure prediction; PROTEIN-STRUCTURE REFINEMENT; MOLECULAR-DYNAMICS SIMULATIONS; STRUCTURE PREDICTIONS; STRUCTURE SELECTION; FORCE-FIELD; SIDE-CHAIN; POTENTIALS; ENSEMBLES; FF99SB;
D O I
10.1002/prot.25409
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We here report on the assessment of the model refinement predictions submitted to the 12th Experiment on the Critical Assessment of Protein Structure Prediction (CASP12). This is the fifth refinement experiment since CASP8 (2008) and, as with the previous experiments, the predictors were invited to refine selected server models received in the regular (nonrefinement) stage of the CASP experiment. We assessed the submitted models using a combination of standard CASP measures. The coefficients for the linear combination of Z-scores (the CASP12 score) have been obtained by a machine learning algorithm trained on the results of visual inspection. We identified eight groups that improve both the backbone conformation and the side chain positioning for the majority of targets. Albeit the top methods adopted distinctively different approaches, their overall performance was almost indistinguishable, with each of them excelling in different scores or target subsets. What is more, there were a few novel approaches that, while doing worse than average in most cases, provided the best refinements for a few targets, showing significant latitude for further innovation in the field.
引用
收藏
页码:152 / 167
页数:16
相关论文
共 48 条
[1]   An integrated in silico 3D model-driven discovery of a novel, potent, and selective amidosulfonamide 5-HT1A agonist (PRX-00023) for the treatment of anxiety and depression [J].
Becker, Oren M. ;
Dhanoa, Dale S. ;
Marantz, Yael ;
Chen, Dongli ;
Shacham, Sharon ;
Cheruku, Srinivasa ;
Heifetz, Alexander ;
Mohanty, Pradyumna ;
Fichman, Merav ;
Sharadendu, Anurag ;
Nudelman, Raphael ;
Kauffman, Michael ;
Noiman, Silvia .
JOURNAL OF MEDICINAL CHEMISTRY, 2006, 49 (11) :3116-3135
[2]   Are current molecular dynamics force fields too helical? [J].
Best, Robert B. ;
Buchete, Nicolae-Viorel ;
Hummer, Gerhard .
BIOPHYSICAL JOURNAL, 2008, 95 (01) :L7-L9
[3]   Optimization of the Additive CHARMM All-Atom Protein Force Field Targeting Improved Sampling of the Backbone φ, ψ and Side-Chain χ1 and χ2 Dihedral Angles [J].
Best, Robert B. ;
Zhu, Xiao ;
Shim, Jihyun ;
Lopes, Pedro E. M. ;
Mittal, Jeetain ;
Feig, Michael ;
MacKerell, Alexander D., Jr. .
JOURNAL OF CHEMICAL THEORY AND COMPUTATION, 2012, 8 (09) :3257-3273
[4]   Investigating Drug-Target Association and Dissociation Mechanisms Using Metadynamics-Based Algorithms [J].
Cavalli, Andrea ;
Spitaleri, Andrea ;
Saladino, Giorgio ;
Gervasio, Francesco L. .
ACCOUNTS OF CHEMICAL RESEARCH, 2015, 48 (02) :277-285
[5]   MolProbity: all-atom structure validation for macromolecular crystallography [J].
Chen, Vincent B. ;
Arendall, W. Bryan, III ;
Headd, Jeffrey J. ;
Keedy, Daniel A. ;
Immormino, Robert M. ;
Kapral, Gary J. ;
Murray, Laura W. ;
Richardson, Jane S. ;
Richardson, David C. .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2010, 66 :12-21
[6]   A Simple and Efficient Protein Structure Refinement Method [J].
Cheng, Qianyi ;
Joung, InSuk ;
Lee, Jooyoung .
JOURNAL OF CHEMICAL THEORY AND COMPUTATION, 2017, 13 (10) :5146-5162
[7]   Consistent refinement of submitted models at CASP using a knowledge-based potential [J].
Chopra, Gaurav ;
Kalisman, Nir ;
Levitt, Michael .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2010, 78 (12) :2668-2678
[8]   An automatic method for CASP9 free modeling structure prediction assessment [J].
Cong, Qian ;
Kinch, Lisa N. ;
Pei, Jimin ;
Shi, Shuoyong ;
Grishin, Vyacheslav N. ;
Li, Wenlin ;
Grishin, Nick V. .
BIOINFORMATICS, 2011, 27 (24) :3371-3378
[9]   Protein structure refinement with adaptively restrained homologous replicas [J].
Della Corte, Dennis ;
Wildberg, Andre ;
Schroeder, Gunnar F. .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2016, 84 :302-313
[10]   Protein structure refinement via molecular-dynamics simulations: What works and what does not? [J].
Feig, Michael ;
Mirjalili, Vahid .
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2016, 84 :282-292