BMRB Entry 27727

Title:
Inhibitor-interaction, dimerization and activity change of HIV-1 protease mutants evolved under drug-pressure
Deposition date:
2018-12-13
Original release date:
2021-07-21
Authors:
Ishima, Rieko; Persons, John; Khan, Shahid
Citation:

Citation: Khan, Shahid; Persons, John; Guerrero, Michel; Ilina, Tatiana; Oda, Masayuki; Ishima, Rieko. "A synergy of activity, stability, and inhibitor-interaction of HIV-1 protease mutants evolved under drug-pressure"  Protein Sci. 30, 571-582 (2021).
PubMed: 33314454

Assembly members:

Assembly members:
HIV-1_Protease, polymer, 99 residues, 10753.73 Da.
entity_017, non-polymer, 547.664 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 shifts178
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, 11
2HIV-1 Protease, 21
3Ligand2

Entities:

Entity 1, HIV-1 Protease, 1 99 residues - 10753.73 Da.

1   PROGLNILETHRLEUTRPLYSARGPROILE
2   VALTHRILEARGILEGLYGLYGLNLEULYS
3   GLUALALEULEUASPTHRGLYALAASPASP
4   THRVALILEGLUGLUMETASNLEUPROGLY
5   LYSTRPLYSPROLYSMETILEVALGLYILE
6   GLYGLYPHEILELYSVALARGGLNTYRASP
7   GLNILEPROILEGLUILEALAGLYHISLYS
8   ALAILEGLYTHRVALLEUVALGLYPROTHR
9   PROALAASNILEILEGLYARGASNLEULEU
10   THRGLNILEGLYALATHRLEUASNPHE

Entity 2, Ligand - C27 H37 N3 O7 S - 547.664 Da.

1   017

Samples:

sample_1: HIV-1 Protease, [U-99% 13C; U-99% 15N], 250 uM; Darunavir 500 uM; phosphate buffer 20 mM

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

Experiments:

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

Software:

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

TOPSPIN, Bruker Biospin - collection

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

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

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