BMRB Entry 27678
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27678
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Title: 1H/13C/15N Assignments for the TM domains of the KcsA potassium channel PubMed: 30631074
Deposition date: 2018-11-05 Original release date: 2019-11-05
Authors: Medeiros-Silva, Joao; Jekhmane, Shehrazade; Li, Jing; Kummerer, Felix; Muller-Hermes, Christoph; Baldus, Marc; Roux, Benoit; Weingarth, Markus
Citation: Jekhmane, Shehrazade; Medeiros-Silva, Joao; Li, Jing; Kummerer, Felix; Muller-Hermes, Christoph; Baldus, Marc; Roux, Benoit; Weingarth, Markus. "Shifts in the selectivity filter dynamics cause modal gating in K+ channels" Nat. Commun. 10, 123-123 (2019).
Assembly members:
KcsA_E71A, polymer, 166 residues, 17694 Da.
Natural source: Common Name: Streptomyces lividans Taxonomy ID: 1916 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces lividans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PQE60
Entity Sequences (FASTA):
KcsA_E71A: MPPMLSGLLARLVKLLLGRH
GSALHWRAAGAATVLLVIVL
LAGSYLAVLAERGAPGAQLI
TYPRALWWSVATATTVGYGD
LYPVTLWGRLVAVVVMVAGI
TSFGLVTAALATWFVGREQE
RRGHFVRHSEKAAEEAYTRT
TRALHERFDRLERMLDDNRR
HHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 97 |
15N chemical shifts | 35 |
1H chemical shifts | 35 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | KcsA Monomer E71A, 1 | 1 |
2 | KcsA Monomer E71A, 2 | 1 |
3 | KcsA Monomer E71A, 3 | 1 |
4 | KcsA Monomer E71A, 4 | 1 |
Entities:
Entity 1, KcsA Monomer E71A, 1 166 residues - 17694 Da.
Residues 1-27; 51-61; 82-87; 112-160 are in contact with the cytoplasmic/extracellular environment Residues 28-50; 62-81;88-111 are embedded in the membrane Residues 74-80 form the filter Residues 161-166 form the His-Tag
1 | MET | PRO | PRO | MET | LEU | SER | GLY | LEU | LEU | ALA | ||||
2 | ARG | LEU | VAL | LYS | LEU | LEU | LEU | GLY | ARG | HIS | ||||
3 | GLY | SER | ALA | LEU | HIS | TRP | ARG | ALA | ALA | GLY | ||||
4 | ALA | ALA | THR | VAL | LEU | LEU | VAL | ILE | VAL | LEU | ||||
5 | LEU | ALA | GLY | SER | TYR | LEU | ALA | VAL | LEU | ALA | ||||
6 | GLU | ARG | GLY | ALA | PRO | GLY | ALA | GLN | LEU | ILE | ||||
7 | THR | TYR | PRO | ARG | ALA | LEU | TRP | TRP | SER | VAL | ||||
8 | ALA | THR | ALA | THR | THR | VAL | GLY | TYR | GLY | ASP | ||||
9 | LEU | TYR | PRO | VAL | THR | LEU | TRP | GLY | ARG | LEU | ||||
10 | VAL | ALA | VAL | VAL | VAL | MET | VAL | ALA | GLY | ILE | ||||
11 | THR | SER | PHE | GLY | LEU | VAL | THR | ALA | ALA | LEU | ||||
12 | ALA | THR | TRP | PHE | VAL | GLY | ARG | GLU | GLN | GLU | ||||
13 | ARG | ARG | GLY | HIS | PHE | VAL | ARG | HIS | SER | GLU | ||||
14 | LYS | ALA | ALA | GLU | GLU | ALA | TYR | THR | ARG | THR | ||||
15 | THR | ARG | ALA | LEU | HIS | GLU | ARG | PHE | ASP | ARG | ||||
16 | LEU | GLU | ARG | MET | LEU | ASP | ASP | ASN | ARG | ARG | ||||
17 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: KcsA E71A, [U-100% 13C; U-100% 15N], 1.5 ± 0.3 mg; Potassium phosphate 15 mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.0; temperature: 273 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4.0.2, Bruker Biospin - collection, data analysis, processing
SPARKY, Goddard - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz
- Bruker Avance 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts