BMRB Entry 27640
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27640
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Title: Chemical Shifts of KCNE1TVG in LMPG micelles PubMed: 30603955
Deposition date: 2018-10-08 Original release date: 2018-10-12
Authors: Law, Cheryl; Sanders, Charles
Citation: Law, Cheryl; Sanders, Charles. "NMR resonance assignments and secondary structure of a mutant form of the human KCNE1 channel accessory protein that exhibits KCNE3-like function." Biomol. NMR Assignments 13, 143-147 (2019).
Assembly members:
KCNE1TVG, polymer, 136 residues, 15434.45 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 Vector: pET16b
Entity Sequences (FASTA):
KCNE1TVG: HHHHHHGMILSNTTAVTPFL
TKLWQETVQQGGNMSGLARR
SPRSGDGKLEALYVLMVLGF
FGFTVGGIMLSYIRSKKLEH
SNDPFNVYIESDAWQEKDKA
YVQARVLESYRSSYVVENHL
AIEQPNTHLPETKPSP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 300 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 118 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LMPG detergent | 1 |
Entities:
Entity 1, LMPG detergent 136 residues - 15434.45 Da.
Residues 1-7 represent a non native affinity tag
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | GLY | MET | ILE | LEU | ||||
| 2 | SER | ASN | THR | THR | ALA | VAL | THR | PRO | PHE | LEU | ||||
| 3 | THR | LYS | LEU | TRP | GLN | GLU | THR | VAL | GLN | GLN | ||||
| 4 | GLY | GLY | ASN | MET | SER | GLY | LEU | ALA | ARG | ARG | ||||
| 5 | SER | PRO | ARG | SER | GLY | ASP | GLY | LYS | LEU | GLU | ||||
| 6 | ALA | LEU | TYR | VAL | LEU | MET | VAL | LEU | GLY | PHE | ||||
| 7 | PHE | GLY | PHE | THR | VAL | GLY | GLY | ILE | MET | LEU | ||||
| 8 | SER | TYR | ILE | ARG | SER | LYS | LYS | LEU | GLU | HIS | ||||
| 9 | SER | ASN | ASP | PRO | PHE | ASN | VAL | TYR | ILE | GLU | ||||
| 10 | SER | ASP | ALA | TRP | GLN | GLU | LYS | ASP | LYS | ALA | ||||
| 11 | TYR | VAL | GLN | ALA | ARG | VAL | LEU | GLU | SER | TYR | ||||
| 12 | ARG | SER | SER | TYR | VAL | VAL | GLU | ASN | HIS | LEU | ||||
| 13 | ALA | ILE | GLU | GLN | PRO | ASN | THR | HIS | LEU | PRO | ||||
| 14 | GLU | THR | LYS | PRO | SER | PRO |
Samples:
sample_1: KCNE1TVG, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-99% 15N], 10%; imidazole 50 mM; potassium chloride 50 mM; EDTA 2 mM; LMPG detergent 8 % w/v
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | 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:
SPARKY vnmrfam-sparky, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts