BMRB Entry 16299
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16299
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Title: NMR assignment of a 48 kDa tetramer of the T1 domain of the mammalian voltage gated potassium channel Kv1.4 PubMed: 19888682
Deposition date: 2009-05-13 Original release date: 2009-07-22
Authors: Schreier, Christina; Auer, Alexandra; Kalbitzer, Hans Robert; Kremer, Werner
Citation: Schreier, Christina; Auer, Alexandra; Kalbitzer, Hans Robert; Kremer, Werner. "NMR assignments of a 48 kDa tetramer of the T1 domain of the mammalian voltage gated potassium channel Kv1.4." Biomol NMR Assign 3, 167-170 (2009).
Assembly members:
T1_domain_of_Kv1.4, polymer, 101 residues, Formula weight is not available
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET20b
Entity Sequences (FASTA):
T1_domain_of_Kv1.4: MERVVINVSGLRFETQMKTL
AQFPETLLGDPEKRTQYFDP
LRNEYFFDRNRPSFDAILYY
YQSGGRLKRPVNVPFDIFTE
EVKFYQLGKLAAALEHHHHH
H
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 244 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 90 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | T1 domain | 1 |
Entities:
Entity 1, T1 domain 101 residues - Formula weight is not available
| 1 | MET | GLU | ARG | VAL | VAL | ILE | ASN | VAL | SER | GLY | ||||
| 2 | LEU | ARG | PHE | GLU | THR | GLN | MET | LYS | THR | LEU | ||||
| 3 | ALA | GLN | PHE | PRO | GLU | THR | LEU | LEU | GLY | ASP | ||||
| 4 | PRO | GLU | LYS | ARG | THR | GLN | TYR | PHE | ASP | PRO | ||||
| 5 | LEU | ARG | ASN | GLU | TYR | PHE | PHE | ASP | ARG | ASN | ||||
| 6 | ARG | PRO | SER | PHE | ASP | ALA | ILE | LEU | TYR | TYR | ||||
| 7 | TYR | GLN | SER | GLY | GLY | ARG | LEU | LYS | ARG | PRO | ||||
| 8 | VAL | ASN | VAL | PRO | PHE | ASP | ILE | PHE | THR | GLU | ||||
| 9 | GLU | VAL | LYS | PHE | TYR | GLN | LEU | GLY | LYS | LEU | ||||
| 10 | ALA | ALA | ALA | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 11 | HIS |
Samples:
sample_1: T1 domain of Kv1.4, [U-13C; U-15N; U-2H], 1 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)NNH | sample_1 | isotropic | sample_conditions_1 |
Software:
AUREMOL, Bruker Biospin - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| GB | EHB17201 ELR56484 |
| REF | XP_003773706 XP_007497268 XP_007657298 XP_007657303 XP_007657307 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts