BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25413

Title: Lipid-Bilayer-Bound Conformation of an Integral Membrane beta-Barrel Protein by Multidimensional MAS NMR   PubMed: 25634301

Authors: Eddy, Matthew; Su, Yongchao; Silvers, Robert; Andreas, Loren; Clark, Lindsay; Wagner, Gerhard; Pintacuda, Guido; Emsley, Lyndon; Griffin, Robert

Citation: Eddy, Matthew; Su, Yongchao; Silvers, Robert; Andreas, Loren; Clark, Lindsay; Wagner, Gerhard; Pintacuda, Guido; Emsley, Lyndon; Griffin, Robert. "Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR"  J. Biomol. NMR 61, 299-310 (2015).

Assembly members:
hVDAC1, polymer, 283 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
hVDAC1: MAVPPTYADLGKSARDVFTK GYGFGLIKLDLKTKSENGLE FTSSGSANTETTKVTGSLET KYRWTEYGLTFTEKWNTDNT LGTEITVEDQLARGLKLTFD SSFSPNTGKKNAKIKTGYKR EHINLGCDMDFDIAGPSIRG ALVLGYQGWLAGYQMNFETA KSRVTQSNFAVGYKTDEFQL HTNVNDGTEFGGSITQKVNK KLETAVNLAWTAGNSNTRFG IAAKYQIDPDACFSAKVNNS SLIGLGYTQTLKPGIKLTLS ALLDGKNVNAGGHKLGLGLE FQA

Data sets:
Data typeCount
13C chemical shifts250
15N chemical shifts77

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1hVDAC11

Entities:

Entity 1, hVDAC1 283 residues - Formula weight is not available

1   METALAVALPROPROTHRTYRALAASPLEU
2   GLYLYSSERALAARGASPVALPHETHRLYS
3   GLYTYRGLYPHEGLYLEUILELYSLEUASP
4   LEULYSTHRLYSSERGLUASNGLYLEUGLU
5   PHETHRSERSERGLYSERALAASNTHRGLU
6   THRTHRLYSVALTHRGLYSERLEUGLUTHR
7   LYSTYRARGTRPTHRGLUTYRGLYLEUTHR
8   PHETHRGLULYSTRPASNTHRASPASNTHR
9   LEUGLYTHRGLUILETHRVALGLUASPGLN
10   LEUALAARGGLYLEULYSLEUTHRPHEASP
11   SERSERPHESERPROASNTHRGLYLYSLYS
12   ASNALALYSILELYSTHRGLYTYRLYSARG
13   GLUHISILEASNLEUGLYCYSASPMETASP
14   PHEASPILEALAGLYPROSERILEARGGLY
15   ALALEUVALLEUGLYTYRGLNGLYTRPLEU
16   ALAGLYTYRGLNMETASNPHEGLUTHRALA
17   LYSSERARGVALTHRGLNSERASNPHEALA
18   VALGLYTYRLYSTHRASPGLUPHEGLNLEU
19   HISTHRASNVALASNASPGLYTHRGLUPHE
20   GLYGLYSERILETHRGLNLYSVALASNLYS
21   LYSLEUGLUTHRALAVALASNLEUALATRP
22   THRALAGLYASNSERASNTHRARGPHEGLY
23   ILEALAALALYSTYRGLNILEASPPROASP
24   ALACYSPHESERALALYSVALASNASNSER
25   SERLEUILEGLYLEUGLYTYRTHRGLNTHR
26   LEULYSPROGLYILELYSLEUTHRLEUSER
27   ALALEULEUASPGLYLYSASNVALASNALA
28   GLYGLYHISLYSLEUGLYLEUGLYLEUGLU
29   PHEGLNALA

Samples:

sample_1: hVDAC1, [U-100% 13C; U-100% 15N], 40 mg; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D NCACXsample_1solidsample_conditions_1
3D NCOCXsample_1solidsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Home-built Home-built 750 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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