FIGURE 3.

Distance-restrained docking of DesKC ABD and DHp domains. A, the global Haddock score is plotted as a function of r.m.s.d. (calculated with respect to the best scoring model). Note that the best scoring models cluster at <1.5 Å r.m.s.d. B, three-dimensional structure of a representative high-scoring docked model of DesKC in the autophosphorylation state, in two orthogonal views. The solvent-accessible surface is rendered transparent to distinguish the relative organization of the domain-domain configuration (secondary structure elements are highlighted). Residues His¹⁸⁸ and ATP are shown as sticks. C, relative frequency of interacting residue pairs in the best 10 docked structures. The histogram is limited to >30% frequencies. Engaged residues are listed, distinguishing with a single prime those belonging to the second protomer within the dimer.