Figure 1: Figure: Multiple sequence alignment. Small nonpolar: G, A, S, T, hydrophobic: C, V, I, L, P, F, Y, M, W, polar: N, Q, H, negatively charged: D, E, and positively charged: K, R.
Figure 2: Figure: Distribution of similarities between pairwise sequences.
Figure 3: Figure: Degree of conservation at each single site. The symbol before each amino acid is illustrated as follows, +: charged (side chains often form salt bridges), >: polar (form hydrogen bonds as proton donors or acceptors), *: hydrophobic (normally buried inside the protein core), and #: amphipathic (often found at the surface of proteins or lipid membranes, sometimes also classified as polar).
Figure 4: Figure: Inferred evolutionary couplings between pairwise amino acids. The symbol before each amino acid is illustrated as follows, +: charged (side chains often form salt bridges), >: polar (form hydrogen bonds as proton donors or acceptors), *: hydrophobic (normally buried inside the protein core), and #: amphipathic (often found at the surface of proteins or lipid membranes, sometimes also classified as polar).
Figure 5: Figure: Evolutionary networks of amino acids. The symbol before each amino acid is illustrated as follows, +: charged (side chains often form salt bridges), >: polar (form hydrogen bonds as proton donors or acceptors), *: hydrophobic (normally buried inside the protein core), and #: amphipathic (often found at the surface of proteins or lipid membranes, sometimes also classified as polar).
Figure 6: Figure: Evolutionary networks of amino acids. The symbol before each amino acid is illustrated as follows, +: charged (side chains often form salt bridges), >: polar (form hydrogen bonds as proton donors or acceptors), *: hydrophobic (normally buried inside the protein core), and #: amphipathic (often found at the surface of proteins or lipid membranes, sometimes also classified as polar).
Figure 7: Figure: Inferred contacts between pairwise amino acids from the multiple sequnece alignment.
Figure 8: Figure: Complete single mutagenesis. The matrix that is computed by the evolutionary coupling analysis (ECA) method shows ΔE — the energy difference of each mutant sequence with each mutation τ at the ith site and wild-type sequence, negative values representing favourable while positive representing unfavourable mutations. The symbol before each amino acid is illustrated as follows, +: charged (side chains often form salt bridges), >: polar (form hydrogen bonds as proton donors or acceptors), *: hydrophobic (normally buried inside the protein core), and #: amphipathic (often found at the surface of proteins or lipid membranes, sometimes also classified as polar).
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