FIG 2.
X-ray crystal structures of HIV-1 protease complexed with GRL-0476, -015, -085, or -097. The profiles of polar contacts made by GRL-0476 (A), -015 (B), -085 (C), and -097 (D) with WTPRD25N are shown. In each structure, the inhibitor is bound in two alternate orientations with average occupancies of 0.49 and 0.51. In order to analyze the hydrogen bonds (H bonds), hydrogen atoms were added and their orientations were optimized sampling the crystallographic water molecules through the protein preparation wizard in Maestro (v9.0 Schrodinger LLC.). In each panel, the carbon atoms for the protease inhibitors are in white, while the carbon atoms of WTPRD25N are in green. Nitrogen, oxygen, and sulfur atoms are in blue, red, and yellow, respectively. Crystallographic water molecules are shown as red spheres.