BMRB Entry 34646

Name: Solution structures of HIV-1 and SIVmac p6 and their interaction with accessory proteins Vpr and Vpx in the presence of DPC micelles
Published: 2023-01-10

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PDB ID: 7p3o
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34646
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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:

Solution structures of HIV-1 and SIVmac p6 and their interaction with accessory proteins Vpr and Vpx in the presence of DPC micelles

Deposition date:

2021-07-08

Original release date:

2023-01-10

Authors:

Wang, X.; Bouaziz, S.

Citation:

Citation: Wang, X.; Bouaziz, S.. "Solution structures of HIV-1 and SIVmac p6 and their interaction with accessory proteins Vpr and Vpx in the presence of DPC micelles" .

Assembly members:

Assembly members:
entity_1, polymer, 52 residues, 5812.297 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: Synthecium

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: LQSRPEPTAPPEESFRFGEE TTTPSQKQEPIDKELYPLAS LRSLFGSDPSSQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	6
1H chemical shifts	285

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 52 residues - 5812.297 Da.

1

LEU

GLN

SER

ARG

PRO

GLU

PRO

THR

ALA

PRO

2

PRO

GLU

SER

PHE

ARG

PHE

GLY

GLU

3

THR

PRO

SER

GLN

LYS

GLN

GLU

PRO

4

ILE

ASP

LYS

GLU

LEU

TYR

PRO

LEU

ALA

SER

5

LEU

ARG

SER

LEU

PHE

GLY

SER

ASP

PRO

SER

6

SER

GLN

Samples:

sample_1: HIV-1 p6 1.0 mM

sample_conditions_1: ionic strength: 50 mM; pH: 4; pressure: 1 atm; temperature: 323 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - processing

ARIA, Linge, O'Donoghue and Nilges - structure calculation

CcpNmr Analysis, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

Bruker AVANCE 600 MHz

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