BMRB Entry 51645
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51645
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Title: Full-length NaK ILV chemical shifts PubMed: 36326620
Deposition date: 2022-09-29 Original release date: 2022-11-21
Authors: Henzler-Wildman, Katherine
Citation: Kurauskas, Vilius; Tonelli, Marco; Henzler-Wildman, Katherine. "Full opening of helix bundle does not lead to NaK channel activation" J. Gen. Physiol. 154, e202213196-e202213196 (2022).
Assembly members:
entity_1, polymer, 118 residues, Formula weight is not available
Natural source: Common Name: Bacillus cereus Taxonomy ID: 1396 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus cereus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b
Entity Sequences (FASTA):
entity_1: GSHMALSFLLTLKRMLRACL
RAWKDKEFQVLFVLTILTLI
SGTIFYSTVEGLRPIDALYF
SVVTLTTVGDGNFSPQTDFG
KIFTILYIFIGIGLVFGFIH
KLAVNVQLPSILSNRKKE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 51 |
| 15N chemical shifts | 21 |
| 1H chemical shifts | 174 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NaK | 1 |
Entities:
Entity 1, NaK 118 residues - Formula weight is not available
Residues -3 to 1 - residual after cleavage with thrombin
| 1 | GLY | SER | HIS | MET | ALA | LEU | SER | PHE | LEU | LEU | ||||
| 2 | THR | LEU | LYS | ARG | MET | LEU | ARG | ALA | CYS | LEU | ||||
| 3 | ARG | ALA | TRP | LYS | ASP | LYS | GLU | PHE | GLN | VAL | ||||
| 4 | LEU | PHE | VAL | LEU | THR | ILE | LEU | THR | LEU | ILE | ||||
| 5 | SER | GLY | THR | ILE | PHE | TYR | SER | THR | VAL | GLU | ||||
| 6 | GLY | LEU | ARG | PRO | ILE | ASP | ALA | LEU | TYR | PHE | ||||
| 7 | SER | VAL | VAL | THR | LEU | THR | THR | VAL | GLY | ASP | ||||
| 8 | GLY | ASN | PHE | SER | PRO | GLN | THR | ASP | PHE | GLY | ||||
| 9 | LYS | ILE | PHE | THR | ILE | LEU | TYR | ILE | PHE | ILE | ||||
| 10 | GLY | ILE | GLY | LEU | VAL | PHE | GLY | PHE | ILE | HIS | ||||
| 11 | LYS | LEU | ALA | VAL | ASN | VAL | GLN | LEU | PRO | SER | ||||
| 12 | ILE | LEU | SER | ASN | ARG | LYS | LYS | GLU |
Samples:
sample_1: Full-length NaK, [U-15N; U-2H, ILV 13C, 1H], 0.76 mM; MOPS 100 mM; KCl 100 mM; DMPC, [U-99% 2H], 44 mM; DHPC, [U-99% 2H], 113 mM; DSS 50 uM; NaN3 0.1 mg
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HMQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C, 13C NOESY HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe vVersion 9.0 - data analysis
TOPSPIN v3.6.2 - collection
NMR spectrometers:
- Bruker AVANCE III 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts