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 18220

Title: Backbone structure of human membrane protein TMEM14A   PubMed: 22609626

Authors: Eichmann, Cedric; Klammt, Christian; Maslennikov, Innokentiy; Kwiatkowski, Witek; 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, 108 residues, 10725.127 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: MTSLYKKVGMDLIGFGYAAL VTFGSIFGYKRRGGVPSLIA GLFVGCLAGYGAYRVSNDKR DVKVSLFTAFFLATIMGVRF KRSKKIMPAGLVAGLSLMMI LRLVLLLL

Data sets:
Data typeCount
13C chemical shifts350
15N chemical shifts97
1H chemical shifts372

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TMEM14A1

Entities:

Entity 1, TMEM14A 108 residues - 10725.127 Da.

Residues 1-9 represent GW cloning tag.

1   METTHRSERLEUTYRLYSLYSVALGLYMET
2   ASPLEUILEGLYPHEGLYTYRALAALALEU
3   VALTHRPHEGLYSERILEPHEGLYTYRLYS
4   ARGARGGLYGLYVALPROSERLEUILEALA
5   GLYLEUPHEVALGLYCYSLEUALAGLYTYR
6   GLYALATYRARGVALSERASNASPLYSARG
7   ASPVALLYSVALSERLEUPHETHRALAPHE
8   PHELEUALATHRILEMETGLYVALARGPHE
9   LYSARGSERLYSLYSILEMETPROALAGLY
10   LEUVALALAGLYLEUSERLEUMETMETILE
11   LEUARGLEUVALLEULEULEULEU

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_ND: TMEM14A, [U-15N; U-2H], 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%

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

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

sample_CS: TMEM14A, [U-15N], 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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_CSisotropicsample_conditions_1
2D 1H-15N HSQCsamples_SLisotropicsample_conditions_1
2D 1H-15N HSQCsamples_DLisotropicsample_conditions_1
3D HNCOsample_NCDisotropicsample_conditions_1
3D HNCACBsample_NCDisotropicsample_conditions_1
3D 13C-15N HSQC-NOESY-HSQCsample_NCisotropicsample_conditions_1
3D 1H-15N NOESYsample_NDisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

PROSA, Guntert - processing

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:

BMRB 18219
PDB
DBJ BAG34999
GB AAD44496 AAF59948 AAH15097 AAH19328 ADQ32420
REF NP_001253566 NP_054770 XP_002746732 XP_002817046 XP_003254199
SP Q9Y6G1