BMRB Entry 27667
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27667
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Title: Backbone resonance assignment of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime
Deposition date: 2018-10-30 Original release date: 2018-11-05
Authors: Zhou, Yuan
Citation: Zhou, Yuan. "Backbone resonance assignment of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime" Biomol. NMR Assignments ., .-..
Assembly members:
catalytic_and_ATP-binding_domain_of_HK853, polymer, 171 residues, Formula weight is not available
Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermotoga maritima
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet-28a
Entity Sequences (FASTA):
catalytic_and_ATP-binding_domain_of_HK853: SLQINREKVDLCDLVESAVN
AIKEFASSHNVNVLFESNVP
CPVEAYIDPTRIRQVLLNLL
NNGVKYSKKDAPDKYVKVIL
DEKDGGVLIIVEDNGIGIPD
HAKDRIFEQFYRVDSSLTYE
VPGTGLGLAITKEIVELHGG
RIWVESEVGKGSRFFVWIPK
DRAGEDNRQDN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 330 |
| 15N chemical shifts | 138 |
| 1H chemical shifts | 490 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | catalytic and ATP-binding domain of HK853 | 1 |
Entities:
Entity 1, catalytic and ATP-binding domain of HK853 171 residues - Formula weight is not available
| 1 | SER | LEU | GLN | ILE | ASN | ARG | GLU | LYS | VAL | ASP | ||||
| 2 | LEU | CYS | ASP | LEU | VAL | GLU | SER | ALA | VAL | ASN | ||||
| 3 | ALA | ILE | LYS | GLU | PHE | ALA | SER | SER | HIS | ASN | ||||
| 4 | VAL | ASN | VAL | LEU | PHE | GLU | SER | ASN | VAL | PRO | ||||
| 5 | CYS | PRO | VAL | GLU | ALA | TYR | ILE | ASP | PRO | THR | ||||
| 6 | ARG | ILE | ARG | GLN | VAL | LEU | LEU | ASN | LEU | LEU | ||||
| 7 | ASN | ASN | GLY | VAL | LYS | TYR | SER | LYS | LYS | ASP | ||||
| 8 | ALA | PRO | ASP | LYS | TYR | VAL | LYS | VAL | ILE | LEU | ||||
| 9 | ASP | GLU | LYS | ASP | GLY | GLY | VAL | LEU | ILE | ILE | ||||
| 10 | VAL | GLU | ASP | ASN | GLY | ILE | GLY | ILE | PRO | ASP | ||||
| 11 | HIS | ALA | LYS | ASP | ARG | ILE | PHE | GLU | GLN | PHE | ||||
| 12 | TYR | ARG | VAL | ASP | SER | SER | LEU | THR | TYR | GLU | ||||
| 13 | VAL | PRO | GLY | THR | GLY | LEU | GLY | LEU | ALA | ILE | ||||
| 14 | THR | LYS | GLU | ILE | VAL | GLU | LEU | HIS | GLY | GLY | ||||
| 15 | ARG | ILE | TRP | VAL | GLU | SER | GLU | VAL | GLY | LYS | ||||
| 16 | GLY | SER | ARG | PHE | PHE | VAL | TRP | ILE | PRO | LYS | ||||
| 17 | ASP | ARG | ALA | GLY | GLU | ASP | ASN | ARG | GLN | ASP | ||||
| 18 | ASN |
Samples:
sample_1: catalytic and ATP-binding domain of HK853, [U-99% 13C; U-99% 15N], 0.5 mM; HEPES 20 mM; KCl 50 mM
sample_conditions_1: ionic strength: 0.14 M; pH: 8.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Keller and Wuthrich - chemical shift assignment, collection
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts