The raw correlated motion plots in Fig. -C resemble the raw GC plot for protein G in Fig. . (Each individual GC array for the independent MD simulations can be found in figure ). Several "blocks" or "bands" of high pairwise correlated motions can be found throughout the plot. Most of these, as in the case of protein G, are likely caused by the close proximity of rigid substructures within the protein, such as secondary structure elements. Specifically, in regions of the transmembrane domain, the highly ordered alpha helices appear highly correlated (e.g. residues 800 -994). The most interesting information that one can obtain from a pairwise correlated motion analysis, however, is the observation of the change of correlated motion upon binding of ATP from apo, binding of dATP from apo, or the exchange from ATP to dATP (Fig. ).