BMRB Entry 19215

Name: Independently verified structure of gp41-M-MAT, a membrane associated MPER trimer from HIV-1 gp41
Published: 2013-05-13

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PDB ID: 2m7w
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19215
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Independently verified structure of gp41-M-MAT, a membrane associated MPER trimer from HIV-1 gp41

Deposition date:

2013-05-01

Original release date:

2013-05-13

Authors:

Martin, Jeffrey; Reardon, Patrick; Sage, Harvey; Dennison, S.; Alam, S.; Haynes, Barton; Spicer, Leonard; Donald, Bruce

Citation:

Citation: Reardon, Patrick; Sage, Harvey; Dennison, S. Moses; Martin, Jeffrey; Donald, Bruce; Alam, S. Munir; Haynes, Barton; Spicer, Leonard. "Structure of an HIV-1-neutralizing antibody target, the lipid-bound gp41 envelope membrane proximal region trimer." Proc. Natl. Acad. Sci. U.S.A. 111, 1391-1396 (2014).
PubMed: 24474763

Assembly members:

Assembly members:
gp41-M-MAT, polymer, 59 residues, 7010.886 Da.

Natural source:

Natural source: Common Name: Human immunodeficiency virus type 1 Taxonomy ID: 11676 Superkingdom: Viruses Kingdom: not available Genus/species: Lentivirus Human immunodeficiency virus 1

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: Ptcle

Entity Sequences (FASTA):

Entity Sequences (FASTA):
gp41-M-MAT: GYIPEAPRDGQAYVRKDGEW VLLSTFLGSSGNEQELLELD KWASLWNWFNITNWLWYIK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	152
15N chemical shifts	64
1H chemical shifts	269

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	gp41-M-MAT, chain 1	1
2	gp41-M-MAT, chain 2	1
3	gp41-M-MAT, chain 3	1

Entities:

Entity 1, gp41-M-MAT, chain 1 59 residues - 7010.886 Da.

1

GLY

TYR

ILE

PRO

GLU

ALA

PRO

ARG

ASP

GLY

2

GLN

ALA

TYR

VAL

ARG

LYS

ASP

GLY

GLU

TRP

3

VAL

LEU

SER

THR

PHE

LEU

GLY

SER

4

GLY

ASN

GLU

GLN

GLU

LEU

GLU

LEU

ASP

5

LYS

TRP

ALA

SER

LEU

TRP

ASN

TRP

PHE

ASN

6

ILE

THR

ASN

TRP

LEU

TRP

TYR

ILE

LYS

Samples:

sample_1: gp41-M-MAT, [U-99% 2H], 2 mM; sodium phosphate 50 mM; DPC 100 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 273 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
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

DISCO v1, Martin, Yan, Bailey-Kellogg, Zhou, and Donald - structure solution

X-PLOR NIH v2.33, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

Bruker Avance 950 MHz
Varian INOVA 800 MHz
Varian INOVA 600 MHz