Evaluation of the template-based modeling in CASP12.

Evaluation of the template-based modeling in CASP12.
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DOI:
10.1002/prot.25425
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发表时间:
2018-03
期刊:
影响因子:
2.9
通讯作者:
Tramontano A
Tramontano A
中科院分区:
生物学4区
文献类型:
--
作者:
Kryshtafovych A;Monastyrskyy B;Fidelis K;Moult J;Schwede T;Tramontano A

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本文描述了提交的CASP12模型的数值评估结果,这些模型可以识别结构模板,并且服务器可以生成相对高精度的模型。重点是分析模型的细节,以及模型与实验结构的竞争程度。贡献研究小组的表现是根据主干精度、全原子局部几何形状和估计模型局部误差的能力来衡量的。对所有参与小组和自动服务器进行了单独的分析。与两年前的上一次CASP相比,在许多领域都有了显著的改进,特别是蛋白质主链原子的准确性,模型和可用结构之间序列比对的准确性,比简单复制最接近的模板获得的准确性增加,以及在最接近的模板中不存在的子结构建模的准确性。这些进步可能与更有效的从头开始构建目标的非模板区域的策略、更好的算法来组合来自多个模板的信息、增强的细化方法以及更好的估计模型准确性的方法有关。
The paper describes results of numerical evaluation of CASP12 models submitted on targets for which structural templates could be identified and for which servers produced models of relatively high accuracy. The emphasis is on analysis of details of models, and how well the models compete with experimental structures. Performance of contributing research groups is measured in terms of backbone accuracy, all-atom local geometry, and the ability to estimate local errors in models. Separate analyses for all participating groups and automatic servers were carried out. Compared with the last CASP, two years ago, there have been significant improvements in a number of areas, particularly the accuracy of protein backbone atoms, accuracy of sequence alignment between models and available structures, increased accuracy over that which can be obtained from simple copying of a closest template, and accuracy of modeling of sub-structures not present in the closest template. These advancements are likely associated with more effective strategies to build non-template regions of the targets ab initio, better algorithms to combine information from multiple templates, enhanced refinement methods, and better methods for estimating model accuracy.
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