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Analysis of the structure of chemically synthesized HIV‐1 protease complexed with a hexapeptide inhibitor. Part I: Crystallographic refinement of 2 Å data
Author(s) -
Miller Maria,
Geller Maciej,
Gribskov Michael,
Kent Stephen B. H.
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199702)27:2<184::aid-prot4>3.0.co;2-g
Subject(s) - crystallography , protease inhibitor (pharmacology) , chemistry , protease , resolution (logic) , human immunodeficiency virus (hiv) , hiv 1 protease , stereochemistry , enzyme , biochemistry , biology , virology , artificial intelligence , viral load , antiretroviral therapy , computer science
The structure of a complex between a hexapeptide‐based inhibitor, MVT‐101, and the chemically synthesized (Aba 67,95,167,195; Aba: l‐α‐amino‐ n ‐butyric acid) protease from the human immunodeficiency virus (HIV‐1), reported previously at 2.3 Å has now been refined to a crystallographic R factor of 15.4% at 2.0 Å resolution. Root mean square deviations from ideality are 0.18 Å for bond lengths and 2.4° for the angles. The inhibitor can be fitted to the difference electron density map in two alternative orientations. Drastic differences are observed for positions and interactions at P3/S3 and P3′/S3′ subsites of the two orientations due to different crystallographic environments. © 1997 Wiley‐Liss, Inc.