BMRB Entry 27377

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments of HIV-1 Protease (Flap + mutant) bound to Darunavir
Published: 2018-03-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27377

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone 1H, 13C, and 15N Chemical Shift Assignments of HIV-1 Protease (Flap + mutant) 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, 10739.7 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:

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):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	178
15N chemical shifts	163
1H chemical shifts	163

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HIV-1_Protease, subunit 1	1
2	HIV-1_Protease, subunit 2	1
3	Ligand	2

Entities:

Entity 1, HIV-1_Protease, subunit 1 99 residues - 10739.7 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

VAL

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 - 561.690 Da.

1

K13

Samples:

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

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

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

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