BMRB Entry 19379

Name: NMR structures of the alpha7 nAChR transmembrane domain.
Published: 2013-11-11

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PDB ID: 2maw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19379
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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:

NMR structures of the alpha7 nAChR transmembrane domain.

Deposition date:

2013-07-19

Original release date:

2013-11-11

Authors:

Bondarenko, Vasyl; Mowrey, David; Xu, Yan; Tang, Pei

Citation:

Citation: Bondarenko, Vasyl; Mowrey, David; Tillman, Tommy; Seyoum, Edom; Xu, Yan; Tang, Pei. "NMR structures of the human 7 nAChR transmembrane domain and associated anesthetic binding sites." Biochim. Biophys. Acta ., .-. (2013).
PubMed: 24384062

Assembly members:

Assembly members:
entity, polymer, 137 residues, 14309.850 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SNAEEELYYGLNLLIPCVLI SALALLVFLLPADSGEKISL GITVLLSLTVFMLLVAEIMP STSDSSPSIAQYFASTMIIV GLSVVVTVIVLQYHHHDPDG GEGGGEGIDRLCLMAFSVFT IICTIGILMSAPNFVEE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	473
15N chemical shifts	128
1H chemical shifts	712

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	alpha7 nAChR transmembrane domain	1

Entities:

Entity 1, alpha7 nAChR transmembrane domain 137 residues - 14309.850 Da.

1

SER

ASN

ALA

GLU

LEU

TYR

GLY

2

LEU

ASN

LEU

ILE

PRO

CYS

VAL

LEU

ILE

3

SER

ALA

LEU

ALA

LEU

VAL

PHE

LEU

4

PRO

ALA

ASP

SER

GLY

GLU

LYS

ILE

SER

LEU

5

GLY

ILE

THR

VAL

LEU

SER

LEU

THR

VAL

6

PHE

MET

LEU

VAL

ALA

GLU

ILE

MET

PRO

7

SER

THR

SER

ASP

SER

PRO

SER

ILE

ALA

8

GLN

TYR

PHE

ALA

SER

THR

MET

ILE

VAL

9

GLY

LEU

SER

VAL

THR

VAL

ILE

VAL

10

LEU

GLN

TYR

HIS

ASP

PRO

ASP

GLY

11

GLY

GLU

GLY

GLU

GLY

ILE

ASP

ARG

12

LEU

CYS

LEU

MET

ALA

PHE

SER

VAL

PHE

THR

13

ILE

CYS

THR

ILE

GLY

ILE

LEU

MET

SER

14

ALA

PRO

ASN

PHE

VAL

GLU

Samples:

sample_1: alpha7 nAChR transmembrane domain, [U-100% 13C; U-100% 15N], 0.25 mM; NaCl, natural abundacne, 10 mM; sodium acetate buffer, natural abundacne, 5 mM

sample_conditions_1: ionic strength: 0.01 M; pH: 4.7; pressure: 1 atm; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	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
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

SPARKY, Goddard - chemical shift assignment, data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz