Data from: Coevolution-based inference of amino acid interactions underlying protein function

Protein function arises from a poorly understood pattern of energetic
interactions between amino acid residues. Sequence-based strategies for
deducing this pattern have been proposed, but lack of benchmark data has
limited experimental verification. Here, we extend deep-mutation
technologies to enable measurement of many thousands of pairwise amino
acid couplings in several homologs of a protein family – a deep coupling
scan (DCS). The data show that cooperative interactions between residues
are loaded in a sparse, evolutionarily conserved, spatially contiguous
network of amino acids. The pattern of amino acid coupling is
quantitatively captured in the coevolution of amino acid positions,
especially as indicated by the statistical coupling analysis (SCA),
providing experimental confirmation of the key tenets of this method. This
work exposes the collective nature of physical constraints on protein
function and clarifies its link with sequence analysis, enabling a general
practical approach for understanding the structural basis for protein
function.