Assessment of template-based protein structure predictions in CASP10

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Abstract

Template-based modeling (TBM) is a major component of the critical assessment of protein structure prediction (CASP). In CASP10, some 41,740 predicted models submitted by 150 predictor groups were assessed as TBM predictions. The accuracy of protein structure prediction was assessed by geometric comparison with experimental X-ray crystal and NMR structures using a composite score that included both global alignment metrics and distance-matrix-based metrics. These included GDT-HA and GDC-all global alignment scores, and the superimposition-independent LDDT distance-matrix-based score. In addition, a superimposition-independent RPF metric, similar to that described previously for comparing protein models against experimental NMR data, was used for comparing predicted protein structure models against experimental protein structures. To score well on all four of these metrics, models must feature accurate predictions of both backbone and side-chain conformations. Performance rankings were determined independently for server and the combined server plus human-curated predictor groups. Final rankings were made using paired head-to-head Student's t-test analysis of raw metric scores among the top 25 performing groups in each category. © 2013 Wiley Periodicals, Inc.

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Huang, Y. J., Mao, B., Aramini, J. M., & Montelione, G. T. (2014). Assessment of template-based protein structure predictions in CASP10. Proteins: Structure, Function and Bioinformatics, 82(SUPPL.2), 43–56. https://doi.org/10.1002/prot.24488

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