BMRB Entry 27727

Name: Inhibitor-interaction, dimerization and activity change of HIV-1 protease mutants evolved under drug-pressure
Published: 2021-07-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27727

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Inhibitor-interaction, dimerization and activity change of HIV-1 protease mutants evolved under drug-pressure PubMed: 33314454

Deposition date: 2018-12-13 Original release date: 2021-07-21

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

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).

Assembly members:
HIV-1_Protease, polymer, 99 residues, 10753.73 Da.
entity_017, non-polymer, 547.664 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 Vector: pJ414

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	178
15N chemical shifts	164
1H chemical shifts	164

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HIV-1 Protease, 1	1
2	HIV-1 Protease, 2	1
3	Ligand	2

Entities:

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

1

PRO

GLN

ILE

THR

LEU

TRP

LYS

ARG

PRO

ILE

2

VAL

THR

ILE

ARG

ILE

GLY

GLN

LEU

LYS

3

GLU

ALA

LEU

ASP

THR

GLY

ALA

ASP

4

THR

VAL

ILE

GLU

MET

ASN

LEU

PRO

GLY

5

LYS

TRP

LYS

PRO

LYS

MET

ILE

VAL

GLY

ILE

6

GLY

PHE

ILE

LYS

VAL

ARG

GLN

TYR

ASP

7

GLN

ILE

PRO

ILE

GLU

ILE

ALA

GLY

HIS

LYS

8

ALA

ILE

GLY

THR

VAL

LEU

VAL

GLY

PRO

THR

9

PRO

ALA

ASN

ILE

GLY

ARG

ASN

LEU

10

THR

GLN

ILE

GLY

ALA

THR

LEU

ASN

PHE

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:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_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 shifts
SPARKY: Backbone or all simulated shifts