BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18223

Title: Backbone structure of human membrane protein TMEM14C   PubMed: 22609626

Authors: Klammt, Christian; Vajpai, Navratna; Maslennikov, Innokentiy; Riek, Roland; Choe, Senyon

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).

Assembly members:
entity, polymer, 121 residues, 11603.638 Da.

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

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free

Entity Sequences (FASTA):
entity: MTSLYKKVGMQDTSSVVPLH WFGFGYAALVASGGIIGYVK AGSVPSLAAGLLFGSLAGLG AYQLSQDPRNVWVFLATSGT LAGIMGMRFYHSGKFMPAGL IAGASLLMVAKVGVSMFNRP H

Data sets:
Data typeCount
13C chemical shifts257
15N chemical shifts101
1H chemical shifts169

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1TMEM14C1

Entities:

Entity 1, TMEM14C 121 residues - 11603.638 Da.

Residues 1-9 represent GW cloning tag

1   METTHRSERLEUTYRLYSLYSVALGLYMET
2   GLNASPTHRSERSERVALVALPROLEUHIS
3   TRPPHEGLYPHEGLYTYRALAALALEUVAL
4   ALASERGLYGLYILEILEGLYTYRVALLYS
5   ALAGLYSERVALPROSERLEUALAALAGLY
6   LEULEUPHEGLYSERLEUALAGLYLEUGLY
7   ALATYRGLNLEUSERGLNASPPROARGASN
8   VALTRPVALPHELEUALATHRSERGLYTHR
9   LEUALAGLYILEMETGLYMETARGPHETYR
10   HISSERGLYLYSPHEMETPROALAGLYLEU
11   ILEALAGLYALASERLEULEUMETVALALA
12   LYSVALGLYVALSERMETPHEASNARGPRO
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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_Nisotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D HNCAsample_NCisotropicsample_conditions_1
3D HNCACBsample_NDisotropicsample_conditions_1
3D HN(CO)CAsample_NCisotropicsample_conditions_1
3D 1H-15N NOESYsample_Nisotropicsample_conditions_1
3D 13C-15N HSQC-NOESY-HSQCsample_NCisotropicsample_conditions_1
2D 1H-15N HSQCsamples_SLisotropicsample_conditions_1
2D 1H-15N HSQCsamples_DLisotropicsample_conditions_1
3D 1H-15N NOESYsample_NDisotropicsample_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

Related Database Links:

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