We also applied Netsci towards a detailed analysis of allostery within the SERCA pump. A loss of correlated motion within the calcium binding site upon ATP and dATP binding constituted a potentially interesting observation, perhaps suggesting a mechanism for forced calcium traversal across the membrane through the use of a "disorder gradient." Additionally, pathway analyses of information travel through the protein suggest routes through which the allosteric signal is propagated from the bound nucleotide to the calcium binding domain. The differential effects of ATP vs. dATP binding have also been characterized -where ATP shows a "stiffening" of portions of the A and P domains of the SERCA pump, and pathway analyses indicate that ATP functions as a sort of information bottleneck through which communication of information across the protein tends to flow. In contrast, dATP binding shows more of general "stiffening" of many different domains, facilitating the traversal of information across the protein, but not through a bottleneck. Our novel local alignment approach also served to remove spurious systematic bias in the MI estimation caused by global protein "breathing" motions.