BMRB Entry 18219

Name: Backbone structure of human membrane protein TMEM14A from NOE data
Published: 2012-05-22

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PDB ID: 2loo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18219
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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:

Backbone structure of human membrane protein TMEM14A from NOE data

Deposition date:

2012-01-26

Original release date:

2012-05-22

Authors:

Eichmann, Cedric; Klammt, Christian; Maslennikov, Innokentiy; Riek, Roland; Choe, Senyon

Citation:

Citation: Klammt, Christian; Maslennikov, Innokentiy; Bayrhuber, Monika; Eichmann, Cedric; Vajpai, Navratna; Chiu, Ellis Jeremy Chua; Blain, Katherine; Esquivies, Luis; Kwon, June Hyun Jung; Balana, Bartosz; Pieper, Ursula; Sali, Andrej; Slesinger, Paul; Kwiatkowski, Witek; Riek, Roland; Choe, Senyon. "Facile backbone structure determination of human membrane proteins by NMR spectroscopy." Nat. Methods 9, 834-839 (2012).
PubMed: 22609626

Assembly members:

Assembly members:
entity, polymer, 108 residues, 10725.127 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: cell free synthesis Host organism: E. coli - cell free Vector: p23-GWN

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MTSLYKKVGMDLIGFGYAAL VTFGSIFGYKRRGGVPSLIA GLFVGCLAGYGAYRVSNDKR DVKVSLFTAFFLATIMGVRF KRSKKIMPAGLVAGLSLMMI LRLVLLLL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	350
15N chemical shifts	97
1H chemical shifts	372

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TMEM14A	1

Entities:

Entity 1, TMEM14A 108 residues - 10725.127 Da.

Residues 1-9 represent GW cloning tag.

1

MET

THR

SER

LEU

TYR

LYS

VAL

GLY

MET

2

ASP

LEU

ILE

GLY

PHE

GLY

TYR

ALA

LEU

3

VAL

THR

PHE

GLY

SER

ILE

PHE

GLY

TYR

LYS

4

ARG

GLY

VAL

PRO

SER

LEU

ILE

ALA

5

GLY

LEU

PHE

VAL

GLY

CYS

LEU

ALA

GLY

TYR

6

GLY

ALA

TYR

ARG

VAL

SER

ASN

ASP

LYS

ARG

7

ASP

VAL

LYS

VAL

SER

LEU

PHE

THR

ALA

PHE

8

PHE

LEU

ALA

THR

ILE

MET

GLY

VAL

ARG

PHE

9

LYS

ARG

SER

LYS

ILE

MET

PRO

ALA

GLY

10

LEU

VAL

ALA

GLY

LEU

SER

LEU

MET

ILE

11

LEU

ARG

LEU

VAL

LEU

Samples:

sample_N: TMEM14A, [U-15N], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_NC: TMEM14A, [U-15N; U-13C], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_NCD: TMEM14A, [U-15N; U-13C; U-2H], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 40 mM; pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_N	isotropic	sample_conditions_1
3D HNCA	sample_NCD	isotropic	sample_conditions_1
3D HNCACB	sample_NCD	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_N	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

PROSA, Guntert - processing

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

Bruker DRX 700 MHz

BMRB	18220
PDB	2LOO 2LOP
DBJ	BAG34999
GB	AAD44496 AAF59948 AAH15097 AAH19328 ADQ32420
REF	NP_001253566 NP_054770 XP_002746732 XP_002817046 XP_003254199
SP	Q9Y6G1
AlphaFold	Q9Y6G1