BMRB Entry 18222

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18222
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Backbone structure of human membrane protein TMEM141
Deposition date:
2012-01-26
Original release date:
2012-05-22
Authors:
Bayrhuber, Monika; 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, 11886.771 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: MVNLGLSRVDDAVAAKHPGL GEYAACQSHAFMKGVFTFVT GTGMAFGLQMFIQRKFPYPL QWSLLVAVVAGSVVSYGVTR VESEKCNNLWLFLETGQLPK DRSTDQRS

Data sets:
Data typeCount
13C chemical shifts197
15N chemical shifts103
1H chemical shifts311

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TMEM1411

Entities:

Entity 1, TMEM141 108 residues - 11886.771 Da.

1   METVALASNLEUGLYLEUSERARGVALASP
2   ASPALAVALALAALALYSHISPROGLYLEU
3   GLYGLUTYRALAALACYSGLNSERHISALA
4   PHEMETLYSGLYVALPHETHRPHEVALTHR
5   GLYTHRGLYMETALAPHEGLYLEUGLNMET
6   PHEILEGLNARGLYSPHEPROTYRPROLEU
7   GLNTRPSERLEULEUVALALAVALVALALA
8   GLYSERVALVALSERTYRGLYVALTHRARG
9   VALGLUSERGLULYSCYSASNASNLEUTRP
10   LEUPHELEUGLUTHRGLYGLNLEUPROLYS
11   ASPARGSERTHRASPGLNARGSER

Samples:

sample_N: TMEM141, [U-15N], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 3%; H2O 95%; D2O 5%

sample_NC: TMEM141, [U-15N; U-13C], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 3%; H2O 95%; D2O 5%

sample_NCD: TMEM141, [U-15N; U-13C; U-2H], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 3%; H2O 95%; D2O 5%

samples_SL: TMEM141, [U-15N], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 3%; H2O 95%; D2O 5%

samples_DL: TMEM141, [U-15N], 0.2 mM; MES-Bis-TRIS 20 mM; LMPG 3%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 60 mM; pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_Nisotropicsample_conditions_1
3D HNCAsample_NCDisotropicsample_conditions_1
3D HNCACBsample_NCDisotropicsample_conditions_1
3D HN(CO)CAsample_NCDisotropicsample_conditions_1
3D 1H-15N NOESYsample_Nisotropicsample_conditions_1
2D 1H-15N HSQCsamples_SLisotropicsample_conditions_1
2D 1H-15N HSQCsamples_DLisotropicsample_conditions_1
3D HNCAsample_NCisotropicsample_conditions_1
3D HN(CO)CAsample_NCisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

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

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

SPARKY, Goddard - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker DRX 700 MHz

Related Database Links:

PDB
GB AAH07834 ADQ32379 AIC52656 EAW88275 EAW88277
REF NP_116317 XP_001162853 XP_002820449 XP_003279836 XP_003817020
SP Q96I45
AlphaFold Q96I45

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks