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. Author manuscript; available in PMC: 2009 Sep 11.
Published in final edited form as: J Med Chem. 2008 Aug 15;51(17):5264–5270. doi: 10.1021/jm800045t

Figure 3.

Figure 3

Crystal structures of 1 and 2 bound to the active site of μI–II. The electron density of 1 (calculated with coefficients 2mFobs – DFcalc, φcalc and contoured at 1σ) and the inhibitor’s polar contacts with μI–II are shown in panels A & C, respectively, while those for 2 are shown in panels B & D. The carve feature of PyMOL33 was used to limit the display of electron density to a distance of 2 Å from the inhibitors. Bonds are colored by atom type: carbon=gray (μI–II), carbon = green (1), carbon = cyan (2), nitrogen = blue, oxygen = red, sulfur = orange. The peptide subsites are labelled below panel C.