BMRB Entry 18223

Name: Backbone structure of human membrane protein TMEM14C
Published: 2012-05-22

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PDB ID: 2los
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18223
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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:

Backbone structure of human membrane protein TMEM14C

Deposition date:

2012-01-26

Original release date:

2012-05-22

Authors:

Klammt, Christian; Vajpai, Navratna; 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, 121 residues, 11603.638 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: MTSLYKKVGMQDTSSVVPLH WFGFGYAALVASGGIIGYVK AGSVPSLAAGLLFGSLAGLG AYQLSQDPRNVWVFLATSGT LAGIMGMRFYHSGKFMPAGL IAGASLLMVAKVGVSMFNRP H

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	257
15N chemical shifts	101
1H chemical shifts	169

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TMEM14C	1

Entities:

Entity 1, TMEM14C 121 residues - 11603.638 Da.

Residues 1-9 represent GW cloning tag

1

MET

THR

SER

LEU

TYR

LYS

VAL

GLY

MET

2

GLN

ASP

THR

SER

VAL

PRO

LEU

HIS

3

TRP

PHE

GLY

PHE

GLY

TYR

ALA

LEU

VAL

4

ALA

SER

GLY

ILE

GLY

TYR

VAL

LYS

5

ALA

GLY

SER

VAL

PRO

SER

LEU

ALA

GLY

6

LEU

PHE

GLY

SER

LEU

ALA

GLY

LEU

GLY

7

ALA

TYR

GLN

LEU

SER

GLN

ASP

PRO

ARG

ASN

8

VAL

TRP

VAL

PHE

LEU

ALA

THR

SER

GLY

THR

9

LEU

ALA

GLY

ILE

MET

GLY

MET

ARG

PHE

TYR

10

HIS

SER

GLY

LYS

PHE

MET

PRO

ALA

GLY

LEU

11

ILE

ALA

GLY

ALA

SER

LEU

MET

VAL

ALA

12

LYS

VAL

GLY

VAL

SER

MET

PHE

ASN

ARG

PRO

13

HIS

Samples:

sample_N: TMEM14C, [U-15N], 0.2 mM; MES-BisTris 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_NC: TMEM14C, [U-15N; U-13C], 0.2 mM; MES-BisTris 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_NCD: TMEM14C, [U-15N; U-13C; U-2H], 0.2 mM; MES-BisTris 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

sample_ND: TMEM14C, [U-15N; U-2H], 0.2 mM; MES-BisTris 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

samples_SL: TMEM14C, [U-15N], 0.2 mM; MES-BisTris 20 mM; LMPG 2%; DSS 0.5 mM; H2O 95%; D2O 5%

samples_DL: TMEM14C, [U-15N], 0.2 mM; MES-BisTris 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 HNCO	sample_NC	isotropic	sample_conditions_1
3D HNCA	sample_NC	isotropic	sample_conditions_1
3D HNCACB	sample_ND	isotropic	sample_conditions_1
3D HN(CO)CA	sample_NC	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_N	isotropic	sample_conditions_1
3D 13C-15N HSQC-NOESY-HSQC	sample_NC	isotropic	sample_conditions_1
2D 1H-15N HSQC	samples_SL	isotropic	sample_conditions_1
2D 1H-15N HSQC	samples_DL	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_ND	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

SPARKY, Goddard - chemical shift assignment

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure analysis, structure visualization

NMR spectrometers:

Bruker DRX 700 MHz

PDB	2LOS
DBJ	BAD97182
EMBL	CAH92409
GB	AAF36114 AAH02496 AAH10086 ABM83488 ABM86703
REF	NP_001129017 NP_001158730 NP_057546 XP_003263552 XP_003263553
SP	Q5R751 Q9P0S9
AlphaFold	Q5R751 Q9P0S9