Allostery,in which the binding of a ligand at one site of a macromolecule can affect other distant sites in the same macromolecule,plays a key role in many biological processes.Theoretically,all non-fabric proteins are potentially allosteric.However,known allosteric proteins are few in number and the identification of novel allosteric sites remains a challenge.Because the motion of residues and subunits underlies protein function,we hypothesized that the motions of allosteric and orthosteric sites are correlated.