Data from: Sequence co-evolution gives 3D contacts and structures of protein complexes

Protein-protein interactions are fundamental to many biological processes.
Experimental screens have identified tens of thousands of interactions and
structural biology has provided detailed functional insight for select 3D
protein complexes. An alternative rich source of information about protein
interactions is the evolutionary sequence record. Building on earlier
work, we show that analysis of correlated evolutionary sequence changes
across proteins identifies residues that are close in space with
sufficient accuracy to determine the three-dimensional structure of the
protein complexes. We evaluate prediction performance in blinded tests on
76 complexes of known 3D structure, predict protein-protein contacts in 32
complexes of unknown structure, and demonstrate how evolutionary couplings
can be used to distinguish between interacting and non-interacting protein
pairs in a large complex. With the current growth of sequences, we expect
that the method can be generalized to genome-wide elucidation of
protein-protein interaction networks and used for interaction predictions
at residue resolution.