To remedy this problem, we developed an algorithm to perform local structural alignments. For each node of data (each residue center of mass, in this study), we choose all adjacent nodes within a certain cutoff value (10 Å in this study), not including the original node. We then align the entire molecule by this set of adjacent nodes, and then input the trajectory positions of the original node into the MI algorithm for analysis. All molecular MI results reported were made following such a local alignment -which functioned well to remove the anomalously large correlated motions observed at the protein extremities when such a local alignment was not performed.