BMRB Entry 27378

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments of WT HIV-1 Protease bound to Darunavir
Deposition date:
2018-01-22
Original release date:
2018-03-07
Authors:
Ishima, Rieko; Persons, John; Khan, Shahid
Citation:

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).
PubMed: 29457713

Assembly members:

Assembly members:
HIV-1_Protease, polymer, 99 residues, 10739.70 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:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pJ414

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts167
15N chemical shifts164
1H chemical shifts164

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HIV-1_Protease, subunit 11
2HIV-1_Protease, subunit 21
3ligand2

Entities:

Entity 1, HIV-1_Protease, subunit 1 99 residues - 10739.70 Da.

1   PROGLNILETHRLEUTRPLYSARGPROLEU
2   VALTHRILEARGILEGLYGLYGLNLEULYS
3   GLUALALEULEUASPTHRGLYALAASPASP
4   THRVALILEGLUGLUMETASNLEUPROGLY
5   LYSTRPLYSPROLYSMETILEGLYGLYILE
6   GLYGLYPHEILELYSVALARGGLNTYRASP
7   GLNILEPROILEGLUILEALAGLYHISLYS
8   ALAILEGLYTHRVALLEUVALGLYPROTHR
9   PROVALASNILEILEGLYARGASNLEULEU
10   THRGLNILEGLYALATHRLEUASNPHE

Entity 2, ligand - 561.690 Da.

1   K13

Samples:

sample_1: HIV-1 Protease, [U-99% 13C; U-99% 15N], 250 uM; Darunavir 2:1 ratio; phosphate buffer 20 mM

sample_conditions_1: pH: 5.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TopSpin, Bruker Biospin - collection

Analysis, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 900 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks