BMRB Entry 34694
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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.
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Title: Magic-angle spinning NMR structure of the human voltage-dependent anion channel 1 (E73V/C127A/C232S) in DMPC lipid bilayers PubMed: 35164499
Deposition date: 2021-12-14 Original release date: 2022-03-14
Authors: Najbauer, E.; Andreas, L.
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).
Assembly members:
entity_1, polymer, 291 residues, 31800.553 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 BL21(DE3)
Entity Sequences (FASTA):
entity_1: MAVPPTYADLGKSARDVFTK
GYGFGLIKLDLKTKSENGLE
FTSSGSANTETTKVTGSLET
KYRWTEYGLTFTVKWNTDNT
LGTEITVEDQLARGLKLTFD
SSFSPNTGKKNAKIKTGYKR
EHINLGADMDFDIAGPSIRG
ALVLGYEGWLAGYQMNFETA
KSRVTQSNFAVGYKTDEFQL
HTNVNDGTEFGGSIYQKVNK
KLETAVNLAWTAGNSNTRFG
IAAKYQIDPDASFSAKVNNS
SLIGLGYTQTLKPGIKLTLS
ALLDGKNVNAGGHKLGLGLE
FQALEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 529 |
| 15N chemical shifts | 189 |
| 1H chemical shifts | 331 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 291 residues - 31800.553 Da.
| 1 | MET | ALA | VAL | PRO | PRO | THR | TYR | ALA | ASP | LEU | ||||
| 2 | GLY | LYS | SER | ALA | ARG | ASP | VAL | PHE | THR | LYS | ||||
| 3 | GLY | TYR | GLY | PHE | GLY | LEU | ILE | LYS | LEU | ASP | ||||
| 4 | LEU | LYS | THR | LYS | SER | GLU | ASN | GLY | LEU | GLU | ||||
| 5 | PHE | THR | SER | SER | GLY | SER | ALA | ASN | THR | GLU | ||||
| 6 | THR | THR | LYS | VAL | THR | GLY | SER | LEU | GLU | THR | ||||
| 7 | LYS | TYR | ARG | TRP | THR | GLU | TYR | GLY | LEU | THR | ||||
| 8 | PHE | THR | VAL | LYS | TRP | ASN | THR | ASP | ASN | THR | ||||
| 9 | LEU | GLY | THR | GLU | ILE | THR | VAL | GLU | ASP | GLN | ||||
| 10 | LEU | ALA | ARG | GLY | LEU | LYS | LEU | THR | PHE | ASP | ||||
| 11 | SER | SER | PHE | SER | PRO | ASN | THR | GLY | LYS | LYS | ||||
| 12 | ASN | ALA | LYS | ILE | LYS | THR | GLY | TYR | LYS | ARG | ||||
| 13 | GLU | HIS | ILE | ASN | LEU | GLY | ALA | ASP | MET | ASP | ||||
| 14 | PHE | ASP | ILE | ALA | GLY | PRO | SER | ILE | ARG | GLY | ||||
| 15 | ALA | LEU | VAL | LEU | GLY | TYR | GLU | GLY | TRP | LEU | ||||
| 16 | ALA | GLY | TYR | GLN | MET | ASN | PHE | GLU | THR | ALA | ||||
| 17 | LYS | SER | ARG | VAL | THR | GLN | SER | ASN | PHE | ALA | ||||
| 18 | VAL | GLY | TYR | LYS | THR | ASP | GLU | PHE | GLN | LEU | ||||
| 19 | HIS | THR | ASN | VAL | ASN | ASP | GLY | THR | GLU | PHE | ||||
| 20 | GLY | GLY | SER | ILE | TYR | GLN | LYS | VAL | ASN | LYS | ||||
| 21 | LYS | LEU | GLU | THR | ALA | VAL | ASN | LEU | ALA | TRP | ||||
| 22 | THR | ALA | GLY | ASN | SER | ASN | THR | ARG | PHE | GLY | ||||
| 23 | ILE | ALA | ALA | LYS | TYR | GLN | ILE | ASP | PRO | ASP | ||||
| 24 | ALA | SER | PHE | SER | ALA | LYS | VAL | ASN | ASN | SER | ||||
| 25 | SER | LEU | ILE | GLY | LEU | GLY | TYR | THR | GLN | THR | ||||
| 26 | LEU | LYS | PRO | GLY | ILE | LYS | LEU | THR | LEU | SER | ||||
| 27 | ALA | LEU | LEU | ASP | GLY | LYS | ASN | VAL | ASN | ALA | ||||
| 28 | GLY | GLY | HIS | LYS | LEU | GLY | LEU | GLY | LEU | GLU | ||||
| 29 | PHE | GLN | ALA | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| hCANH | sample_1 | anisotropic | sample_conditions_1 |
| hcoCAcoNH | sample_1 | anisotropic | sample_conditions_1 |
| hCONH | sample_1 | anisotropic | sample_conditions_1 |
| hCOcaNH | sample_1 | anisotropic | sample_conditions_1 |
| hcaCBcaNH | sample_1 | anisotropic | sample_conditions_1 |
| hcoCACONH | sample_1 | anisotropic | sample_conditions_1 |
| hCOCANH | sample_1 | anisotropic | sample_conditions_1 |
| hNcocaNH | sample_1 | anisotropic | sample_conditions_1 |
| hNcacoNH | sample_1 | anisotropic | sample_conditions_1 |
| hcaCBcacoNH | sample_1 | anisotropic | sample_conditions_1 |
| hNCAH | sample_2 | anisotropic | sample_conditions_1 |
| HNhhNH | sample_1 | anisotropic | sample_conditions_1 |
| hCOCAnH | sample_1 | anisotropic | sample_conditions_1 |
| hNcoCAH | sample_2 | anisotropic | sample_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 shifts
SPARKY: Backbone
or all simulated shifts