Statistical investigations of protein residue direct couplings
Fig 1
Empirical values of Ŝ as a function of S yielded by randomly shuffled 100,000 DCA arrays (blue dots connected by lines), and by 100,000 DCA arrays derived from column-permuted MSAs, where the order of the columns and of the residues within each column were randomly permuted (red triangles connected by lines).
Solid straight lines represents agreement of Ŝ with S, and the dashed curves represent an error range of two standard deviations. Results are shown for six of the domains listed in Table 2, designated by their corresponding pdb identifiers 3fhkF, 1ijxA, 4cmlA, 1olzA, 1k30A, 1wznA, ordered by increasing numbers of sequences in their corresponding MSAs. For 1wxnA, the additional data points (faint red triangles connected by a dashed line) corresponds to an MSA of 5,117 sequences randomly drawn from the original MSA.