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 30065

Title: E73V mutant of the human voltage-dependent anion channel   PubMed: 27461260

Deposition date: 2016-04-17 Original release date: 2016-08-08

Authors: Jaremko, M.; Jaremko, L.; Villinger, S.; Schmidt, C.; Giller, K.; Griesinger, C.; Becker, S.; Zweckstetter, M.

Citation: Jaremko, M.; Jaremko, L.; Villinger, S.; Schmidt, C.; Giller, K.; Griesinger, C.; Becker, S.; Zweckstetter, M.. "High resolution determination of the dynamic structure of membrane proteins"  Angew. Chem. Int. Ed. Engl. 55, 10518-10521 (2016).

Assembly members:
Voltage-dependent anion-selective channel protein 1, polymer, 285 residues, 30977.699 Da.

Natural source:   Common Name: not available   Taxonomy ID: 9606   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
Voltage-dependent anion-selective channel protein 1: SAVPPTYADLGKSARDVFTK GYGFGLIKLDLKTKSENGLE FTSSGSANTETTKVTGSLET KYRWTEYGLTFTVKWNTDNT LGTEITVEDQLARGLKLTFD SSFSPNTGKKNAKIKTGYKR EHINLGCDMDFDIAGPSIRG ALVLGYEGWLAGYQMNFETA KSRVTQSNFAVGYKTDEFQL HTNVNDGTEFGGSIYQKVNK KLETAVNLAWTAGNSNTRFG IAAKYQIDPDACFSAKVNNS SLIGLGYTQTLKPGIKLTLS ALLDGKNVNAGGHKLGLGLE FQARS

Data typeCount
13C chemical shifts466
15N chemical shifts252
1H chemical shifts253
T1 relaxation values534
T2 relaxation values534

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 285 residues - 30977.699 Da.

1   SERALAVALPROPROTHRTYRALAASPLEU
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   PHEGLNALAARGSER

Samples:

sample_1: E73V mutant of the Voltage-dependent anion channel 1' '[U-2H; U-15N]; [U-2H]; [U-2H]

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
R1 relaxation ratesample_1isotropicsample_conditions_1
R2 relaxation ratesample_1isotropicsample_conditions_1
R1 relaxation ratesample_1isotropicsample_conditions_1
R2 relaxation ratesample_1isotropicsample_conditions_1
R1 relaxation ratesample_1isotropicsample_conditions_1
R2 relaxation ratesample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz

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