Methods of model accuracy estimation can help selecting the best models from decoy sets: Assessment of model accuracy estimations in CASP11

The article presents assessment of the model accuracy estimation methods participating in CASP11. The results of the assessment are expected to be useful to both—developers of the methods and users who way too often are presented with structural models without annotations of accuracy. The main emphasis is placed on the ability of techniques to identify the best models from among several available. Bivariate descriptive statistics and ROC analysis are used to additionally assess the overall correctness of the predicted model accuracy scores, the correlation between the predicted and observed accuracy of models, the effectiveness in distinguishing between good and bad models, the ability to discriminate between reliable and unreliable regions in models, and the accuracy of the coordinate error self‐estimates. A rigid‐body measure (GDT_TS) and three local‐structure‐based scores (LDDT, CADaa, and SphereGrinder) are used as reference measures for evaluating methods' performance. Consensus methods, taking advantage of the availability of several models for the same target protein, perform well on the majority of tasks. Methods that predict accuracy on the basis of a single model perform comparably to consensus methods in picking the best models and in the estimation of how accurate is the local structure. More groups than in previous experiments submitted reasonable error estimates of their own models, most likely in response to a recommendation from CASP and the increasing demand from users. Proteins 2016; 84(Suppl 1):349–369. © 2015 Wiley Periodicals, Inc.

[1]  Björn Wallner,et al.  Improved model quality assessment using ProQ2 , 2012, BMC Bioinformatics.

[2]  Krzysztof Fidelis,et al.  CASP prediction center infrastructure and evaluation measures in CASP10 and CASP ROLL , 2014, Proteins.

[3]  D. Eisenberg,et al.  VERIFY3D: assessment of protein models with three-dimensional profiles. , 1997, Methods in enzymology.

[4]  Anna Tramontano,et al.  Evaluation of CASP8 model quality predictions , 2009, Proteins.

[5]  Kliment Olechnovič,et al.  CAD‐score: A new contact area difference‐based function for evaluation of protein structural models , 2013, Proteins.

[6]  Anna Tramontano,et al.  Evaluation of model quality predictions in CASP9 , 2011, Proteins.

[7]  Pascal Benkert,et al.  QMEAN server for protein model quality estimation , 2009, Nucleic Acids Res..

[8]  Liam J. McGuffin,et al.  The ModFOLD4 server for the quality assessment of 3D protein models , 2013, Nucleic Acids Res..

[9]  Anna Tramontano,et al.  Assessment of the assessment: Evaluation of the model quality estimates in CASP10 , 2014, Proteins.

[10]  Vincent B. Chen,et al.  Correspondence e-mail: , 2000 .

[11]  Marcin J. Skwark,et al.  PconsD: ultra rapid, accurate model quality assessment for protein structure prediction , 2013, Bioinform..

[12]  Roland L Dunbrack,et al.  Outcome of a workshop on applications of protein models in biomedical research. , 2009, Structure.

[13]  Anna Tramontano,et al.  Assessment of predictions in the model quality assessment category , 2007, Proteins.

[14]  Adam Zemla,et al.  LGA: a method for finding 3D similarities in protein structures , 2003, Nucleic Acids Res..

[15]  K. Fidelis,et al.  Protein structure prediction and model quality assessment. , 2009, Drug discovery today.

[16]  Marco Biasini,et al.  lDDT: a local superposition-free score for comparing protein structures and models using distance difference tests , 2013, Bioinform..

[17]  M Wilmanns,et al.  Molecular replacement with NMR models using distance-derived pseudo B factors. , 1996, Acta crystallographica. Section D, Biological crystallography.