FIGURE 3.

Increases (red) and Decreases (blue) in Fuctuations upon Lgand (green spheres) Binding in (A) Mitogen-activated protein kinase 8, (B) Citrate synthase, (C) Uncharacterized protein VCA0042, (D) ATP sulfurylase, (E) Glutamate dehydrogenase, (F) Acetyl-Coenzyme A carboxylase, (G) Isocitrate dehydrogenase kinase/phosphatase, (H) Casein kinase II subunit alpha, (I) l-lactate dehydrogenase. While there appears to be a large variety of positions that are affected, the universal rule appears to be that the part of the structure furthest away from the binding site has the largest increases in fluctuations. If the binding site is near the outside of the protein, then the largest increases in fluctuations will be at the center of the protein. One particularly interesting such case is shown in part d where there are three occupied binding sites, which can be presumed, each to increase the fluctuations in the most distant part so with the three occupied binding sites all three domains have increased fluctuations near the center of the overall structure.