Skip to main content
. Author manuscript; available in PMC: 2013 May 8.
Published in final edited form as: J Chem Theory Comput. 2012 Mar 15;8(5):1750–1764. doi: 10.1021/ct200680g

Fig. 9.

Fig. 9

Bottom panels: time evolution of the Cα(E318)···Cα(V425) (red), Cα(N458)···Cα (T563) (green), and Cα(G132)···Cα(A523) distances (blue), middle panels: time evolution of the angles δ (green) and τ (blue) defined in Figure 8, upper panels: time evolution of the kink angle η (red) for three representative trajectories shown in Figure 6: type I opening-binding (A), type II opening-binding (B), and binding-only (C). The circles at the start of the plots indicate the values of the distances and angles calculated from the 2KHO structure. All trajectories were obtained in the simulations with the RI-RII type restraints, i.e., without restraining the relative motion of the NBD-I and NBD-II domains.