BMRB Entry 16381
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16381
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Title: Sequence-specific resonance assignments of human VDAC-1 in LDAO micelles PubMed: 19916553
Deposition date: 2009-06-30 Original release date: 2010-03-01
Authors: Hiller, Sebastian; Garces, Robert; Malia, Thomas; Orekhov, Vladislav; Wagner, Gerhard
Citation: Raschle, Thomas; Hiller, Sebastian; Yu, Tsyr-Yan; Rice, Amanda; Walz, Thomas; Wagner, Gerhard. "Structural and functional characterization of the integral membrane protein VDAC-1 in lipid bilayer nanodiscs." J. Am. Chem. Soc. 131, 17777-17779 (2009).
Assembly members:
VDAC-1, polymer, 291 residues, 31050.059 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
KYRWTEYGLTFTEKWNTDNT
LGTEITVEDQLARGLKLTFD
SSFSPNTGKKNAKIKTGYKR
EHINLGCDMDFDIAGPSIRG
ALVLGYEGWLAGYQMNFETA
KSRVTQSNFAVGYKTDEFQL
HTNVNDGTEFGGSIYQKVNK
KLETAVNLAWTAGNSNTRFG
IAAKYQIDPDACFSAKVNNS
SLIGLGYTQTLKPGIKLTLS
ALLDGKNVNAGGHKLGLGLE
FQALEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 513 |
| 15N chemical shifts | 239 |
| 1H chemical shifts | 479 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | VDAC-1 | 1 |
Entities:
Entity 1, VDAC-1 291 residues - 31050.059 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: VDAC-1, [U-13C; U-15N; U-2H], 1 mM; LDAO 400 mM; NaPi 25 mM; DTT 5 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 25 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | 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 v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAB13473 BAE27004 BAE31716 BAE39878 BAE40179 |
| EMBL | CAA52962 CAB58127 |
| GB | AAA61272 AAB20246 AAB47777 AAD54939 AAF22835 |
| REF | NP_001075544 NP_001119824 NP_001248683 NP_001270163 NP_003365 |
| SP | P21796 P45879 Q60932 Q9MZ16 Q9TT15 |
| TPG | DAA27459 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts