BMRB Entry 50216
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50216
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Title: HR1c domain from PRK1 PubMed: 32500230
Deposition date: 2020-03-25 Original release date: 2020-06-09
Authors: Sophocleous, Georgios; Mott, Helen
Citation: Sophocleous, Georgios; Wood, George; Owen, Darerca; Mott, Helen. "1 H, 15 N and 13 C Resonance Assignments of the HR1c Domain of PRK1, a Protein Kinase C-related Kinase" Biomol. NMR Assignments 14, 245-250 (2020).
Assembly members:
entity_1, polymer, 104 residues, Formula weight is not available
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: pGex6P
Entity Sequences (FASTA):
entity_1: GPLGSHMDTQGSPDLGAVEL
RIEELRHHFRVEHAVAEGAK
NVLRLLSAAKAPDRKAVSEA
QEKLTESNQKLGLLREALER
RLGELPADHPKGRLLREELA
AASS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 346 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 730 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PRK1 HR1c | 1 |
Entities:
Entity 1, PRK1 HR1c 104 residues - Formula weight is not available
| 1 | GLY | PRO | LEU | GLY | SER | HIS | MET | ASP | THR | GLN | ||||
| 2 | GLY | SER | PRO | ASP | LEU | GLY | ALA | VAL | GLU | LEU | ||||
| 3 | ARG | ILE | GLU | GLU | LEU | ARG | HIS | HIS | PHE | ARG | ||||
| 4 | VAL | GLU | HIS | ALA | VAL | ALA | GLU | GLY | ALA | LYS | ||||
| 5 | ASN | VAL | LEU | ARG | LEU | LEU | SER | ALA | ALA | LYS | ||||
| 6 | ALA | PRO | ASP | ARG | LYS | ALA | VAL | SER | GLU | ALA | ||||
| 7 | GLN | GLU | LYS | LEU | THR | GLU | SER | ASN | GLN | LYS | ||||
| 8 | LEU | GLY | LEU | LEU | ARG | GLU | ALA | LEU | GLU | ARG | ||||
| 9 | ARG | LEU | GLY | GLU | LEU | PRO | ALA | ASP | HIS | PRO | ||||
| 10 | LYS | GLY | ARG | LEU | LEU | ARG | GLU | GLU | LEU | ALA | ||||
| 11 | ALA | ALA | SER | SER |
Samples:
sample_1: PRK1 HR1c domain, [U-100% 15N], 1.6 mM; sodium phosphate 20 mM; sodium chloride 150 mM
sample_2: PRK1 HR1c domain, [U-100% 13C; U-100% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 150 mM
sample_conditions_1: ionic strength: 0.17 M; pH: 7.3; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CcpNmr Analysis v2.4 - chemical shift assignment
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts