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. Author manuscript; available in PMC: 2017 Jul 7.
Published in final edited form as: Biochemistry. 2017 Apr 21;56(17):2338–2348. doi: 10.1021/acs.biochem.7b00165

Figure 5.

Figure 5

Structural models and RMSD analysis of EL2 in WT green opsin and its P186M and P205I substitutions. The 10 energetically favored structures were aligned and are displayed as cartoons from residue 180 to 224. (A) The Pro-Pro motif in the WT green opsin is highlighted with a red oval. The black oval indicates the region of variation in the structure caused by the P205I mutation. (B) Structures resulting from the P186M mutation. The red oval indicates a major variation in structure induced by the mutation (compare with the red oval region in panel A). (C) Major variations in structure are caused by the P205I mutation (black oval; compare to the black oval region in panel A). (D) Heat map of RMSD analysis of the 10 energetically favored structures shown in panels A–C. The red and black rectangles correspond to the ovals displayed in A–C.