WISP can be used to identify how distal regions of a protein allosterically communicate with one another. In this method the protein is described as a graph or network, in which residues are treated as nodes (points on the graph/network) and residue-residue correlations are the edges (connections between the nodes). By defining a "source" and a "sink" (a start and an end residue respectively), the shortest pathways of communication are determined between these two residues to identify the key residues and key residue-residue interactions that are responsible for signal propagation. The pre-processing we described above gave rise to a graph/network where the nodes are residues; the edges are the residue pairs in contact with one another; and the edge weights are the correlations determined between each residue pair, enabling us to perform WISP calculations on our PTP1B dataset. As PTP1B has two known allosteric drug binding sites named the BB-site and K197-site (see Figure ), we focused our WISP analysis on these two sites, picking a residue at each site to be used as the "source" for the WISP analysis, with D181 define as the "sink".