BMRB Entry 34457
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34457
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Refined solution NMR structure of hVDAC-1 in detergent micelles PubMed: 31862297
Deposition date: 2019-11-22 Original release date: 2019-12-02
Authors: Boehm, R.; Hiller, S.; Wagner, G.
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:
entity_1, polymer, 291 residues, 31878.662 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):
entity_1: MAVPPTYADLGKSARDVFTK
GYGFGLIKLDLKTKSENGLE
FTSSGSANTETTKVTGSLET
KYRWTEYGLTFTEKWNTDNT
LGTEITVEDQLARGLKLTFD
SSFSPNTGKKNAKIKTGYKR
EHINLGCDMDFDIAGPSIRG
ALVLGYEGWLAGYQMNFETA
KSRVTQSNFAVGYKTDEFQL
HTNVNDGTEFGGSIYQKVNK
KLETAVNLAWTAGNSNTRFG
IAAKYQIDPDACFSAKVNNS
SLIGLGYTQTLKPGIKLTLS
ALLDGKNVNAGGHKLGLGLE
FQALEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 739 |
| 15N chemical shifts | 255 |
| 1H chemical shifts | 510 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 291 residues - 31878.662 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 | GLU | 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 | CYS | 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 | CYS | 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: hVDAC-1, [U-99%-2H; U-13C; U-15N], 0.6 mM; LDAO, no, 3%
sample_2: hVDAC-1, [U-99%-2H, 13C, 15N; 99%-1H delta-IL; 99%-1H gamma-V], 0.6 mM; LDAO, [U-99% 2H], 3%
sample_3: hVDAC-1, [U-99%-2H, 15N; 99%-1H delta, 13C delta-IL; 99%-1H gamma, 13C gamma-V], 0.6 mM; LDAO, [U-99% 2H], 3%
sample_conditions_1: ionic strength: 225 mM; pH: 6.5; pressure: 1 atm; temperature: 303.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 4D NUS-MDD-1H-13C-13C | sample_2 | isotropic | sample_conditions_1 |
| 4D NUS-MDD-1H-15N-13C | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
CARA, Keller and Wuthrich - chemical shift assignment
XEASY, Bartels et al. - peak picking
NMR spectrometers:
- Bruker AVANCE 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts