Results on allosteric causality and energetics obtained for proteins analyzed in this work.

Data for only one representative structure is given in this table (for the complete list of proteins see S1 Table). First column provides protein names, degree of oligomerization and total number of residues. Second column: PDB ID of the protein and names of ligands (if not the apo form). Third column: number, name, and type ((†)(A) allosteric activator, (I) allosteric inhibitor, and (S) substrate) of ligated binding sites in our model. Fourth column: the mean allosteric free energy difference of the ligated binding site A averaged over all the residues belonging to A in all protein monomers, and the mean allosteric free energy difference averaged over all the residues of the protein monomers (in parentheses). Fifth column: names of the binding site under allosteric regulation, typically catalytic sites. Sixth column: the mean allosteric free energy difference (or work exerted at) of the regulated binding site F averaged over all the residues belonging to F in all protein monomers, and the mean allosteric free energy difference averaged over all the residues of the protein monomers (in parentheses ). ATCase: (*) and (**) the values corresponding to the regulatory ΔgR − mer and catalytic ΔgC − mer monomers, respectively. AnthS: (⋆) and (⋆⋆) the values corresponding to the monomers containing TRP ΔgTRP − mer and GLU ΔgGLU − mer. CAP: (*) and (**) the values corresponding to the bound monomer ΔgB − mer and free monomer ΔgF − mer.