The analysis of amino acid coevolution has emerged as a practical method for protein structural modeling by providing structural contact information from alignments of amino acid sequences. In parallel, chemical cross-linking/mass spectrometry (XLMS) has gained attention as a universally applicable method for obtaining low-resolution distance constraints to model the quaternary arrangements of proteins, and more recently even protein tertiary structures. Here, we show that the structural information obtained by XLMS and coevolutionary analysis are effectively complementary: the distance constraints obtained by each method are almost exclusively associated with non-coincident pairs of residues, and modeling results obtained by the combination of both sets are improved relative to considering the same total number of constraints of a single type. The structural rationale behind the complementarity of the distance constraints is discussed and illustrated for a representative set of proteins with different sizes and folds.

中文翻译：

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从化学交联和氨基酸共进化获得的距离限制的结构互补性。

通过提供来自氨基酸序列比对的结构接触信息，氨基酸共进化分析已成为一种用于蛋白质结构建模的实用方法。同时，化学交联/质谱法（XLMS）作为一种普遍适用的方法获得了关注，该方法可用于获取低分辨率距离约束条件，以建模蛋白质的四级排列，以及最近建立的蛋白质三级结构。在这里，我们证明了通过XLMS和协进化分析获得的结构信息是有效的互补：每种方法获得的距离约束几乎都与残基的非一致对相关，并且通过将两组集合组合获得的建模结果相对得到了改进。考虑单个类型的约束总数相同。