BMRB Entry 27110

Name: 1H, 13C and 15N chemical shifts of HIV-1 gp41 cytoplasmic tail residues 707-751
Published: 2017-11-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27110

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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 chemical shifts of HIV-1 gp41 cytoplasmic tail residues 707-751

Deposition date:

2017-05-22

Original release date:

2017-11-02

Authors:

Murphy, R. Elliot; Vlach, Jiri; Samal, Alexandra; Saad, Jamil

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:
hiv1_env45, polymer, 46 residues, 5231.7453 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):
hiv1_env45: SRVRQGYSPLSFQTHLPIPR GPDRPEGIEEEGGERDRDRS IRLVNG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	179
15N chemical shifts	42
1H chemical shifts	290

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HIV-1 gp41CT_N	1

Entities:

Entity 1, HIV-1 gp41CT_N 46 residues - 5231.7453 Da.

1

SER

ARG

VAL

ARG

GLN

GLY

TYR

SER

PRO

LEU

2

SER

PHE

GLN

THR

HIS

LEU

PRO

ILE

PRO

ARG

3

GLY

PRO

ASP

ARG

PRO

GLU

GLY

ILE

GLU

4

GLU

GLY

GLU

ARG

ASP

ARG

ASP

ARG

SER

5

ILE

ARG

LEU

VAL

ASN

GLY

Samples:

Sample1: hiv1_env45, [[U-95% 13C; U-95% 15N]], 0.5 mM

Cond1: ionic strength: 100.000 mM; pH: 6.000; pressure: 1.000 atm; temperature: 308.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	Sample1	isotropic	Cond1
3D HNCACB	Sample1	isotropic	Cond1
hncoca (H[N[co[{CA\|ca[C]}]]])	Sample1	isotropic	Cond1
hncocacb (H[N[co[{CA\|ca[C]}]]])	Sample1	isotropic	Cond1
2D 1H-15N HSQC/HMQC	Sample1	isotropic	Cond1
3D 1H-15N NOESY	Sample1	isotropic	Cond1
3D 1H-15N TOCSY	Sample1	isotropic	Cond1
hCCH (H[C_[C]].Jmultibond)	Sample1	isotropic	Cond1
3D HNCO	Sample1	isotropic	Cond1

Software:

nmrDraw vany, F. Delaglio - Spectrum analysis, Spectrum display

nmrPipe vany, F. Delaglio - Spectrum processing

CcpNmr_Analysis v2.4, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance II 700 MHz

UniProt	Q6TAP9
AlphaFold	Q6TAP9