As can be seen in Fig. , a wide range of correlations are observed between the motions of the ATP and dATP center of mass and the center of mass of each residue. Most notably, relatively low correlation is observed between ATP and the residues forming the calcium-binding sites Fig. as denoted by the white and blue coloring of the cartoon ribbon diagram in the lower third of the intermembrane domain. We see a similar low amount of correlation when dATP is bound as well (Fig. . Relatively high correlated motion to ATP and dATP is observed in the core regions of the transmembrane domain above the calcium binding sites, as colored by the pink regions. Upon the binding of ATP from the apo state, we see that there is a reduction in correlation in some of the calcium binding residues relative to the rest of the protein, specifically residues D800, V304, T799, and E908 (Fig ). The remaining calcium coordinates residues do no show any obvious change in correlation relative to the rest of the protein. Alternatively, upon dATP binding from apo, residues N796, A305, and E309 increase in correlated motion. Again, the other calcium residues do not show any visible difference in correlation.