Figure 9 . Binding surface on HPr for its partners. (a) the binding surface for glycogen phosphorylase (GP); (b) the binding surface for IIAGlc; (c) the binding surface for EIN. Backbone chemical shift perturbations were mapped onto a ribbon diagram of HPr (left side of figure) and the accessible surface of HPr (right side of figure). The magnitude of the shifts are shown in colors varying from blue (no shift) through yellow (intermediate shift) to red (maximum shift). Secondary structure elements are labeled in the ribbon diagram shown in (a). The side chain of His15 of HPr is shown in red on the ribbon diagram (from Wang et al., 2000b).
