BMRB Entry 34694

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34694
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Magic-angle spinning NMR structure of the human voltage-dependent anion channel 1 (E73V/C127A/C232S) in DMPC lipid bilayers
Deposition date:
2021-12-14
Original release date:
2022-03-14
Authors:
Najbauer, E.; Andreas, L.
Citation:

Citation: Najbauer, E.; Tekwani Movellan, K.; Giller, K.; Benz, R.; Becker, S.; Griesinger, C.; Andreas, L.. "Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer."  J. Am. Chem. Soc. 144, 2953-2967 (2022).
PubMed: 35164499

Assembly members:

Assembly members:
entity_1, polymer, 291 residues, 31800.553 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: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAVPPTYADLGKSARDVFTK GYGFGLIKLDLKTKSENGLE FTSSGSANTETTKVTGSLET KYRWTEYGLTFTVKWNTDNT LGTEITVEDQLARGLKLTFD SSFSPNTGKKNAKIKTGYKR EHINLGADMDFDIAGPSIRG ALVLGYEGWLAGYQMNFETA KSRVTQSNFAVGYKTDEFQL HTNVNDGTEFGGSIYQKVNK KLETAVNLAWTAGNSNTRFG IAAKYQIDPDASFSAKVNNS SLIGLGYTQTLKPGIKLTLS ALLDGKNVNAGGHKLGLGLE FQALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts529
15N chemical shifts189
1H chemical shifts331

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 291 residues - 31800.553 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   GLUHISILEASNLEUGLYALAASPMETASP
14   PHEASPILEALAGLYPROSERILEARGGLY
15   ALALEUVALLEUGLYTYRGLUGLYTRPLEU
16   ALAGLYTYRGLNMETASNPHEGLUTHRALA
17   LYSSERARGVALTHRGLNSERASNPHEALA
18   VALGLYTYRLYSTHRASPGLUPHEGLNLEU
19   HISTHRASNVALASNASPGLYTHRGLUPHE
20   GLYGLYSERILETYRGLNLYSVALASNLYS
21   LYSLEUGLUTHRALAVALASNLEUALATRP
22   THRALAGLYASNSERASNTHRARGPHEGLY
23   ILEALAALALYSTYRGLNILEASPPROASP
24   ALASERPHESERALALYSVALASNASNSER
25   SERLEUILEGLYLEUGLYTYRTHRGLNTHR
26   LEULYSPROGLYILELYSLEUTHRLEUSER
27   ALALEULEUASPGLYLYSASNVALASNALA
28   GLYGLYHISLYSLEUGLYLEUGLYLEUGLU
29   PHEGLNALALEUGLUHISHISHISHISHIS
30   HIS

Samples:

sample_1: u[2H,13C,15N]-hVDAC1(E73V/C127A/C232S), [U-13C; U-15N; U-2H], 66 % w/w; DMPC 33 % w/w; MES 10 mM; sodium chloride 150 mM; MgCl2 20 mM

sample_2: u[2H,13C,15N]-hVDAC1(E73V/C127A/C232S), [U-13C; U-15N]-alpha PET, 66 % w/w; DMPC 33 % w/w; MES 10 mM; sodium chloride 150 mM; MgCl2 20 mM

sample_conditions_1: ionic strength: 0.21 M; pH: 6.5; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
hCANHsample_1anisotropicsample_conditions_1
hcoCAcoNHsample_1anisotropicsample_conditions_1
hCONHsample_1anisotropicsample_conditions_1
hCOcaNHsample_1anisotropicsample_conditions_1
hcaCBcaNHsample_1anisotropicsample_conditions_1
hcoCACONHsample_1anisotropicsample_conditions_1
hCOCANHsample_1anisotropicsample_conditions_1
hNcocaNHsample_1anisotropicsample_conditions_1
hNcacoNHsample_1anisotropicsample_conditions_1
hcaCBcacoNHsample_1anisotropicsample_conditions_1
hNCAHsample_2anisotropicsample_conditions_1
HNhhNHsample_1anisotropicsample_conditions_1
hCOCAnHsample_1anisotropicsample_conditions_1
hNcoCAHsample_2anisotropicsample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure calculation

Sparky v3.113, Goddard - chemical shift assignment, peak picking

TopSpin v3.5pl7, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AVANCE III HD 800 MHz
  • Bruker AVANCE III HD 950 MHz

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