BMRB Entry 30297

Name: 1H, 13C, 15N chemical shift assignments of the HIV-1 gp41 cytoplasmic tail, residues 752-856
Published: 2017-11-02

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PDB ID: 5vwl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30297
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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, 15N chemical shift assignments of the HIV-1 gp41 cytoplasmic tail, residues 752-856

Deposition date:

2017-05-22

Original release date:

2017-11-02

Authors:

Saad, J.; Murphy, R.; Samal, A.; Vlach, J.

Citation:

Citation: Murphy, R Elliot; Samal, Alexandra; Vlach, Jiri; Saad, Jamil. "Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein" Structure 0969-2126, 30301-30305 (2017).
PubMed: 29056482

Assembly members:

Assembly members:
entity_1, polymer, 105 residues, 12398.524 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: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SLALIWDDLRSLCLFSYHRL RDLLLIVTRIVELLGRRGWE ALKYWWNLLQYWSQELKNSA VNLLNATAIAVAEGTDRVIE VLQAAYRAIRHIPRRIRQGL ERILL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	462
15N chemical shifts	107
1H chemical shifts	680

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 105 residues - 12398.524 Da.

1

SER

LEU

ALA

LEU

ILE

TRP

ASP

LEU

ARG

2

SER

LEU

CYS

LEU

PHE

SER

TYR

HIS

ARG

LEU

3

ARG

ASP

LEU

ILE

VAL

THR

ARG

ILE

4

VAL

GLU

LEU

GLY

ARG

GLY

TRP

GLU

5

ALA

LEU

LYS

TYR

TRP

ASN

LEU

GLN

6

TYR

TRP

SER

GLN

GLU

LEU

LYS

ASN

SER

ALA

7

VAL

ASN

LEU

ASN

ALA

THR

ALA

ILE

ALA

8

VAL

ALA

GLU

GLY

THR

ASP

ARG

VAL

ILE

GLU

9

VAL

LEU

GLN

ALA

TYR

ARG

ALA

ILE

ARG

10

HIS

ILE

PRO

ARG

ILE

ARG

GLN

GLY

LEU

11

GLU

ARG

ILE

LEU

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_3	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C HMQC NOESY	sample_3	isotropic	sample_conditions_1

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CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks

BMRB Entry 30297

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: