BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27377

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments of HIV-1 Protease (Flap + mutant) bound to Darunavir   PubMed: 29457713

Deposition date: 2018-01-22 Original release date: 2018-03-07

Authors: Ishima, Rieko; Persons, John; Khan, Shahid

Citation: Khan, Shahid; Persons, John; Paulsen, Janet; Guerrero, Michel; Schiffer, Celia; Kurt-Yilmaz, Nese; Ishima, Rieko. "Probing Structural Changes among Analogous Inhibitor-Bound Forms of HIV-1 Protease and a Drug-Resistant Mutant in Solution by Nuclear Magnetic Resonance"  Biochemistry 57, 1652-1662 (2018).

Assembly members:
HIV-1_Protease, polymer, 99 residues, 10739.7 Da.
(3R,3aS,6aR)-hexahydrofuro[2,3-b]furan-3-yl [(1S,2R)-3-{[(4-aminophenyl)sulfonyl][(2S)-2-methylbutyl]amino}-1-benzyl-2-hydroxypropyl]carbamate, non-polymer, 561.690 Da.

Natural source:   Common Name: HIV-1   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV-1

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
HIV-1_Protease: PQITLWKRPIVTIRIGGQLK EALLDTGADDTVIEEMNLPG KWKPKMIVGIGGFVKVRQYD QIPIEIAGHKAIGTVLVGPT PANIIGRNLLTQIGATLNF

Data sets:
Data typeCount
13C chemical shifts178
15N chemical shifts163
1H chemical shifts163

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