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Proteins often work as oligomers or multimers  in vivo . Therefore, elucidating their oligomeric or multimeric form (quaternary structure) is crucially important to ascertain their function. X-ray crystal structures of numerous proteins have been accumulated, providing information related to their biological units. Extracting information of biological units from protein crystal structures represents a meaningful task for modern biology. Nevertheless, although many methods have been proposed for identifying biological units appearing in protein crystal structures, it is difficult to distinguish biological protein–protein interfaces from crystallographic ones. Therefore, our simple but highly accurate classifier was developed to infer biological units in protein crystal structures using large amounts of protein sequence information and a modern contact prediction method to exploit covariation signals (CSs) in proteins. We demonstrate that our proposed method is promising even for weak signals of biological interfaces. We also discuss the relation between classification accuracy and conservation of biological units, and illustrate how the selection of sequences included in multiple sequence alignments as sources for obtaining CSs affects the results. With increased amounts of sequence data, the proposed method is expected to become increasingly useful.

Accurate Classification of Biological and non-Biological Interfaces in Protein Crystal Structures using Subtle Covariation Signals