BMRB Entry 30065
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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/BMR30065
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
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).
PubMed: 27461260
Assembly members:
Voltage-dependent anion-selective channel protein 1, polymer, 285 residues, 30977.699 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):
Voltage-dependent anion-selective channel protein 1: SAVPPTYADLGKSARDVFTK
GYGFGLIKLDLKTKSENGLE
FTSSGSANTETTKVTGSLET
KYRWTEYGLTFTVKWNTDNT
LGTEITVEDQLARGLKLTFD
SSFSPNTGKKNAKIKTGYKR
EHINLGCDMDFDIAGPSIRG
ALVLGYEGWLAGYQMNFETA
KSRVTQSNFAVGYKTDEFQL
HTNVNDGTEFGGSIYQKVNK
KLETAVNLAWTAGNSNTRFG
IAAKYQIDPDACFSAKVNNS
SLIGLGYTQTLKPGIKLTLS
ALLDGKNVNAGGHKLGLGLE
FQARS
- assigned_chemical_shifts
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 466 |
| 15N chemical shifts | 252 |
| 1H chemical shifts | 253 |
| T1 relaxation values | 534 |
| T2 relaxation values | 534 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 285 residues - 30977.699 Da.
| 1 | SER | 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 | 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 | ARG | SER |
Samples:
sample_1: E73V mutant of the Voltage-dependent anion channel 1, [U-2H; U-15N], 0.8 mM; LDAO, [U-2H], 2%; TRIS, [U-2H], 20 mM
sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| R1 relaxation rate | sample_1 | isotropic | sample_conditions_1 |
| R2 relaxation rate | sample_1 | isotropic | sample_conditions_1 |
| R1 relaxation rate | sample_1 | isotropic | sample_conditions_1 |
| R2 relaxation rate | sample_1 | isotropic | sample_conditions_1 |
| R1 relaxation rate | sample_1 | isotropic | sample_conditions_1 |
| R2 relaxation rate | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks