Figure 6.

Effect of PDEδ^F94A/I98A double mutation on farnesylated KRas4B HVR release in the mutated systems (systems 6^m and 7^m). (A) Initial and final positions of the farnesyl group and Phe133 side chain (left panels) and some key residues (Met20, Arg61, and Ile129) of PDEδ (right panels) in system 6^m (upper panels) and in system 7^m (lower panels). The structures at 10 ns are represented by orange, whereas structures at 500 ns are shown by gray. The HVR is removed in the right panels to be able to clearly see the movement of the residues. (B) RMSF plots of PDEδ in systems 2 and system 6^m (upper panel panel) and systems 3 and system 7^m (lower panel). The blue lines cover residues of systems 2 and 3, and the green lines cover residues of systems 6^m and 7^m. (C) Interactions between Arl2, PDEδ, and HVR in systems 6^m and 7^m. The pink and cyan molecules/sticks show Arl2 and PDEδ molecules/residues, respectively, whereas the dark blue molecules/sticks represent HVR molecules/residues. The black dashed lines show salt bridges, and the orange dashed lines show H-bond.