Beyond those residues labeled as important from the work of Faure et al., our approach also identified several other residues with potentially interesting roles in allosteric communication (Figure ). For example, F400 sits on the α3-helix and is identified as the fifth most important residue due to its differing van der Waals interactions with several residues on the β2-β3 loop including G330 and G329 (Table ), both of which were determined as allosteric by Faure et al. Interestingly, the α3-helix (which F400 is located on) has previously been implicated in having a role in allosteric signaling upon peptide binding, supporting our observations herein.