BMRB Entry 50712

Name: 1H, 13C and 15N backbone resonance assignment of HIV-1 Gag(276-432) encompassing the C-terminal domain of the capsid protein, the spacer peptide 1 and the nucleocapsid protein
Published: 2021-03-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50712

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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:

1H, 13C and 15N backbone resonance assignment of HIV-1 Gag(276-432) encompassing the C-terminal domain of the capsid protein, the spacer peptide 1 and the nucleocapsid protein

Deposition date:

2021-01-15

Original release date:

2021-03-29

Authors:

CHEN, Xiaowei; Coric, Pascale; Bouaziz, Serge

Citation:

Citation: Chen, Xiaowei; Coric, Pascale; Bouaziz, Serge. "1H, 13C and 15N backbone resonance assignment of HIV-1 Gag (276-432) encompassing the C-terminal domain of the capsid protein, the spacer peptide 1 and the nucleocapsid protein" Biomol. NMR Assignments 15, 267-271 (2021).
PubMed: 33754285

Assembly members:

Assembly members:
entity_1, polymer, 157 residues, Formula weight is not available

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: pLATE11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MYSPTSILDIRQGPKEPFRD YVDRFYKTLRAEQASQEVKN AATETLLVQNANPDCKTILK ALGPGATLEEMMTACQGVGG PGHKARVLAEAMSQVTNPAT IMIQKGNFRNQRKTVKCFNC GKEGHIAKNCRAPRKKGCWK CGKEGHQMKDCTERQAN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	417
15N chemical shifts	137
1H chemical shifts	137

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CActdSP1NC	1

Entities:

Entity 1, CActdSP1NC 157 residues - Formula weight is not available

1

MET

TYR

SER

PRO

THR

SER

ILE

LEU

ASP

ILE

2

ARG

GLN

GLY

PRO

LYS

GLU

PRO

PHE

ARG

ASP

3

TYR

VAL

ASP

ARG

PHE

TYR

LYS

THR

LEU

ARG

4

ALA

GLU

GLN

ALA

SER

GLN

GLU

VAL

LYS

ASN

5

ALA

THR

GLU

THR

LEU

VAL

GLN

ASN

6

ALA

ASN

PRO

ASP

CYS

LYS

THR

ILE

LEU

LYS

7

ALA

LEU

GLY

PRO

GLY

ALA

THR

LEU

GLU

8

MET

THR

ALA

CYS

GLN

GLY

VAL

GLY

9

PRO

GLY

HIS

LYS

ALA

ARG

VAL

LEU

ALA

GLU

10

ALA

MET

SER

GLN

VAL

THR

ASN

PRO

ALA

THR

11

ILE

MET

ILE

GLN

LYS

GLY

ASN

PHE

ARG

ASN

12

GLN

ARG

LYS

THR

VAL

LYS

CYS

PHE

ASN

CYS

13

GLY

LYS

GLU

GLY

HIS

ILE

ALA

LYS

ASN

CYS

14

ARG

ALA

PRO

ARG

LYS

GLY

CYS

TRP

LYS

15

CYS

GLY

LYS

GLU

GLY

HIS

GLN

MET

LYS

ASP

16

CYS

THR

GLU

ARG

GLN

ALA

ASN

Samples:

sample_1: CActdSP1NC, [U-99% 13C; U-99% 15N], 0.5 mM; beta-mercaptoethanol 0.1 mM; sodium acetate, [U-99% 2H], 25 mM; sodium chloride 25 mM; zinc chloride 0.1 mM; D2O, [U-99% 2H], 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N SOFAST-HMQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis - chemical shift assignment

TOPSPIN - collection

TALOS-N - secondary structure prediction

NMR spectrometers:

Bruker AVANCE III 600 MHz

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