Fig. 2.

Conformational dynamics of unphosphorylated and phosphorylated GTP-bound K-Ras4B. RMSDs of Cα atoms in unphosphorylated (black) and phosphorylated (red) systems within (A) all Ras residues and (B) switch I residues and (C) switch II residues. Gray and pink transparencies represent the error. Conformational landscapes of unphosphorylated (D) and phosphorylated (E) K-Ras4B generated using d₁ (distance from G60 Cα to GTP P_β) and d₂ (distance from T35 Cα to GTP P_β). (F-K) Representative structures of conformational clusters C1–C3 in the two systems. K-Ras4B P-loop, switch I and switch II regions are colored lime, pink, and light blue, respectively. Surface of T35 and G60 residues are colored red and marine. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)