Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The crystal structures at 2.2-A resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations.
Journal, issue, pages	J. Biol. Chem., Vol. 267, Page 22770-22778, Year 1992
Publish date	Sep 21, 1992 (structure data deposition date)
Authors	Murthy, K.H. / Winborne, E.L. / Minnich, M.D. / Culp, J.S. / Debouck, C.
External links	PubMed:1429626
Methods	X-ray diffraction
Resolution	2.2 Å
Structure data	PDB-1hef: The crystal structures at 2.2 angstroms resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations Method: X-RAY DIFFRACTION / Resolution: 2.2 Å PDB-1heg: The crystal structures at 2.2 angstroms resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations Method: X-RAY DIFFRACTION / Resolution: 2.2 Å
Chemicals	ChemComp-HOH: WATER ChemComp-PSI: methyl N-{(4S,5S)-5-[(L-alanyl-L-alanyl)amino]-4-hydroxy-6-phenylhexanoyl}-L-valyl-L-valinate
Source	human immunodeficiency virus 1
Keywords	HYDROLASE/HYDROLASE INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR COMPLEX / ACID PROTEINASE