BMRB Entry 15853
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15853
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Title: Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR PubMed: 17945182
Deposition date: 2008-07-02 Original release date: 2008-08-07
Authors: Chill, Jordan; Louis, John; Delaglio, Frank; Bax, Ad
Citation: Chill, Jordan; Louis, John; Delaglio, Frank; Bax, Ad. "Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR" Biochim. Biophys. Acta. 1768, 3260-3270 (2007).
Assembly members:
KcsA, polymer, 145 residues, Formula weight is not available
Natural source: Common Name: Streptomyces coelicolor Taxonomy ID: 1902 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces coelicolor
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
KcsA: LLGRHGSALHWRAAGAATVL
LVIVLLAGSYLAVLAERGAP
GAQLITYPRALWWSVETATT
VGYGDLYPVTLWGRLVAVVV
MVAGITSFGLVTAALATWFV
GREQERRGHFVRHSEKAAEE
AYTRTTRALHERFDRLERML
DDNRR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 833 |
| 15N chemical shifts | 407 |
| 1H chemical shifts | 407 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | KcsA | 1 |
Entities:
Entity 1, KcsA 145 residues - Formula weight is not available
The first residue with number 1 is in reality the 16th residue.
| 1 | LEU | LEU | GLY | ARG | HIS | GLY | SER | ALA | LEU | HIS | ||||
| 2 | TRP | ARG | ALA | ALA | GLY | ALA | ALA | THR | VAL | LEU | ||||
| 3 | LEU | VAL | ILE | VAL | LEU | LEU | ALA | GLY | SER | TYR | ||||
| 4 | LEU | ALA | VAL | LEU | ALA | GLU | ARG | GLY | ALA | PRO | ||||
| 5 | GLY | ALA | GLN | LEU | ILE | THR | TYR | PRO | ARG | ALA | ||||
| 6 | LEU | TRP | TRP | SER | VAL | GLU | THR | ALA | THR | THR | ||||
| 7 | VAL | GLY | TYR | GLY | ASP | LEU | TYR | PRO | VAL | THR | ||||
| 8 | LEU | TRP | GLY | ARG | LEU | VAL | ALA | VAL | VAL | VAL | ||||
| 9 | MET | VAL | ALA | GLY | ILE | THR | SER | PHE | GLY | LEU | ||||
| 10 | VAL | THR | ALA | ALA | LEU | ALA | THR | TRP | PHE | VAL | ||||
| 11 | GLY | ARG | GLU | GLN | GLU | ARG | ARG | GLY | HIS | PHE | ||||
| 12 | VAL | ARG | HIS | SER | GLU | LYS | ALA | ALA | GLU | GLU | ||||
| 13 | ALA | TYR | THR | ARG | THR | THR | ARG | ALA | LEU | HIS | ||||
| 14 | GLU | ARG | PHE | ASP | ARG | LEU | GLU | ARG | MET | LEU | ||||
| 15 | ASP | ASP | ASN | ARG | ARG |
Samples:
sample_1_for_TableS2: KcsA 0.5-0.6 mM; sodium formate 25 mM; D2O 7%
sample_2_for_TableS3: KcsA 0.5-0.6 mM; MES 25 mM; D2O 7%
sample_3_for_TableS4: KcsA 0.5-0.6 mM; TRIS 25 mM; D2O 7%
sample_conditions_1: pH: 4.2; pressure: 14.1 Torr; temperature: 323 K
sample_conditions_2: pH: 6; pressure: 14.1 Torr; temperature: 323 K
sample_conditions_3: pH: 8; pressure: 14.1 Torr; temperature: 323 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1_for_TableS2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2_for_TableS3 | isotropic | sample_conditions_2 |
| 3D HNCO | sample_3_for_TableS4 | isotropic | sample_conditions_3 |
| 3D HN(CA)CO | sample_1_for_TableS2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2_for_TableS3 | isotropic | sample_conditions_2 |
| 3D HN(CA)CO | sample_3_for_TableS4 | isotropic | sample_conditions_3 |
| 3D HNCA | sample_1_for_TableS2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2_for_TableS3 | isotropic | sample_conditions_2 |
| 3D HNCA | sample_3_for_TableS4 | isotropic | sample_conditions_3 |
Software:
NMRPipe/NMRDraw, NIH - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
| PDB | |
| EMBL | CAA86025 CAC16993 |
| GB | AIJ11233 EFD64549 EOY52587 KKD16939 |
| REF | NP_631700 WP_003971485 WP_016328171 WP_030864493 |
| SP | P0A333 P0A334 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts