Fig. 4: Effects of phosphorylation on predicted residue-residue couplings.

a Histogram of median RV₂ coefficients comparing phosphorylated and non-phosphorylated mutual information matrices, indicating the degree of global change in residue-residue couplings upon phosphorylation. b Scatterplot comparing the degree of global change in residue-residue couplings, as measured by the RV₂ coefficient (y-axis) to the direction of overall change in mutual information for the entire structure (x-axis) upon phosphorylation. Dashed lines on the x-axis represent the median value ± one standard deviation. c Pie chart summarizing the observed changes in residue-residue couplings upon phosphorylation. d Three examples of clear and significant global changes in residue-residue couplings upon phosphorylation (highlighted in bold in (b)). Heatmaps on the left show the median difference in residue couplings between phosphorylated and non-phosphorylated structures. Residues shown in sticks indicate phosphorylated residues. Note that the phosphosite in 2bdw_B is in the pink cluster and buried between two helices, thus partially occluded in this view. Residues with the same colour indicate clusters of highly coupled residues; gray indicates residues not part of any cluster. For clarity, in the case of Ca²⁺/CaM-dependent protein kinase II, only clusters with more than seven residues are indicated, due to the higher number of clusters. Source data are provided as a Source Data file.