ANALYSIS OF THE STRUCTURE OF CHEMICALLY SYNTHESIZED HIV-1 PROTEASE COMPLEXED WITH A HEXAPEPTIDE INHIBITOR .1. CRYSTALLOGRAPHIC REFINEMENT OF 2 ANGSTROM DATA

The structure of a complex between a hexapeptide-based inhibitor, MVT- 101, and the chemically synthesized (Aba 67,95,167,195; Aba: L-alpha-a mino-butyric acid) protease from the human immunodeficiency virus (HIV -1), reported previously at 2.3 Angstrom has now been refined to a cry stallographic R factor of 15.4% at 2.0 Angstrom resolution, Root mean square deviations from ideality are 0.18 Angstrom for bond lengths and 2.4 degrees for the angles, The inhibitor can be fitted to the differ ence electron density map in two alternative orientations, Drastic dif ferences are observed for positions and interactions at P3/S3 and P3'/ S3' subsites of the two orientations due to different crystallographic environments. (C) 1997 Wiley-Liss, Inc.