BMRB Entry 34169
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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/BMR34169
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Title: Solution NMR structure of truncated, human Hv1/VSOP (Voltage-gated proton channel)
Deposition date: 2017-08-12 Original release date: 2019-03-28
Authors: Bayrhuber, M.; Maslennikov, I.; Kwiatowski, W.; Sobol, A.; Wierschem, C.; Eichmann, C.; Riek, R.
Citation: Bayrhuber, M.; Maslennikov, I.; Kwiatowski, W.; Sobol, A.; Wierschem, C.; Eichmann, C.; Riek, R.. "Insights into the mechanism of proton channels investigated by NMR" . ., .-..
Assembly members:
entity_1, polymer, 147 residues, 17352.062 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: SHMRAPLDFRGMLRKLFSSH
RFQVIIICLVVLDALLVLAE
LILDLKIIQPDKNNYAAMVF
HYMSITILVFFMMEIIFKLF
VFRLEFFHHKFEILDAVVVV
VSFILDIVLLFQEHQFEALG
LLILLRLWRVARIINGIIIS
VKTRSER
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 360 |
| 15N chemical shifts | 109 |
| 1H chemical shifts | 711 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 147 residues - 17352.062 Da.
| 1 | SER | HIS | MET | ARG | ALA | PRO | LEU | ASP | PHE | ARG | ||||
| 2 | GLY | MET | LEU | ARG | LYS | LEU | PHE | SER | SER | HIS | ||||
| 3 | ARG | PHE | GLN | VAL | ILE | ILE | ILE | CYS | LEU | VAL | ||||
| 4 | VAL | LEU | ASP | ALA | LEU | LEU | VAL | LEU | ALA | GLU | ||||
| 5 | LEU | ILE | LEU | ASP | LEU | LYS | ILE | ILE | GLN | PRO | ||||
| 6 | ASP | LYS | ASN | ASN | TYR | ALA | ALA | MET | VAL | PHE | ||||
| 7 | HIS | TYR | MET | SER | ILE | THR | ILE | LEU | VAL | PHE | ||||
| 8 | PHE | MET | MET | GLU | ILE | ILE | PHE | LYS | LEU | PHE | ||||
| 9 | VAL | PHE | ARG | LEU | GLU | PHE | PHE | HIS | HIS | LYS | ||||
| 10 | PHE | GLU | ILE | LEU | ASP | ALA | VAL | VAL | VAL | VAL | ||||
| 11 | VAL | SER | PHE | ILE | LEU | ASP | ILE | VAL | LEU | LEU | ||||
| 12 | PHE | GLN | GLU | HIS | GLN | PHE | GLU | ALA | LEU | GLY | ||||
| 13 | LEU | LEU | ILE | LEU | LEU | ARG | LEU | TRP | ARG | VAL | ||||
| 14 | ALA | ARG | ILE | ILE | ASN | GLY | ILE | ILE | ILE | SER | ||||
| 15 | VAL | LYS | THR | ARG | SER | GLU | ARG |
Samples:
sample_1: Hv1/VSOP, [U-99% 13C; U-99% 15N; 50% 2H], 0.4 mM; MES 20 mM; BisTris 20 mM; FC-12 2 mM; LDAO 2 mM; TCEP 1 mM; ZnCl2 10 mM
sample_conditions_1: ionic strength: 30 mM; pH: 5.8; pressure: 1 atm; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert P. - refinement
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