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Patterns of pairwise correlations in sequence alignments can be used to reconstruct the network of residue-residue contacts and thus the threedimensional structure of proteins. Less explored, and yet extremely intriguing, is the functional relevance of such coevolving networks: Do they encode for the collective motions occurring in proteins at thermal equilibrium? Here, by combining coevolutionary coupling analysis with a state-of-the-art dimensionality reduction approach, we show that thedoi:10.1073/pnas.ss11450 fatcat:czx6ow7gqnb3pnltw77vo2aoyi