Likewise, computational methods measure concerted structural changes using a variety of metrics on a myriad protein features. Some methods utilize sequence coevolution to group proteins regions into "sectors" that are coupled to one another . Recent work has highlighted that molecular simulations can capture atomistically detailed pictures of allosteric coupling between sites. The underlying assumption that a proteins functional states are encoded in the equilibrium simulations implies that observing correlated motions in MD simulations would be representative of the degree of coupling between residues. Indeed, a number of algorithms use a myriad of features and metrics to quantify coupling . Some features used could be the backbone Cα atoms of proteins, and measuring the degree of covariance in pairs of Cα atoms . Other methods infer mutual information on dihedral angles to quantify how much better one residue's dihedral angle predicts the dihedral angle of another residue . However, there has been growing recognition that allostery via concerted structural changes is not the only mechanism through which two sites may be coupled.