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 27128

Title: Voltage-dependent anion channel - VDAC E73V mutant   PubMed: 31862297

Deposition date: 2017-06-07 Original release date: 2019-11-22

Authors: Boehm, Raphael; Hiller, Sebastian; Wagner, Gerhard

Citation: Boehm, R.; Hiller, S.; Amodeo, G.; Murlidaran, S.; Chavali, S.; Wagner, G.; Brannigan, G.; Winterhalter, M.. "The Structural Basis for Low Conductance in the Membrane Protein VDAC upon beta-NADH Binding and Voltage Gating"  Structure 28, 206-214 (2020).

Assembly members:
VDAC-1, polymer, 291 residues, 31800 Da.

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):
VDAC-1: MAVPPTYADLGKSARDVFTK GYGFGLIKLDLKTKSENGLE FTSSGSANTETTKVTGSLET KYRWTEYGLTFTVKWNTDNT LGTEITVEDQLARGLKLTFD SSFSPNTGKKNAKIKTGYKR EHINLGCDMDFDIAGPSIRG ALVLGYEGWLAGYQMNFETA KSRVTQSNFAVGYKTDEFQL HTNVNDGTEFGGSIYQKVNK KLETAVNLAWTAGNSNTRFG IAAKYQIDPDACFSAKVNNS SLIGLGYTQTLKPGIKLTLS ALLDGKNVNAGGHKLGLGLE FQALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts470
15N chemical shifts259
1H chemical shifts259

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1VDAC-11

Entities:

Entity 1, VDAC-1 291 residues - 31800 Da.

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

Samples:

sample_1: VDAC-1, [U-13C; U-15N; U-2H], 0.6 mM; LDAO 3%

sample_conditions_1: ionic strength: 225 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CARA, Rochus Keller - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts