BMRB Entry 51892
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51892
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Title: 1H, 15N and 13C backbone assignments for human PARP-1 BRCT domain PubMed: 37326024
Deposition date: 2023-03-31 Original release date: 2023-06-19
Authors: Yang, Ji-Chun; Wu, Wing-Fung; Neuhaus, David
Citation: Suskiewicz, Marcin; Munnur, Deeksha; Stromland, Oyvind; Yang, Ji-Chun; Easton, Laura; Chatrin, Chatrin; Zhu, Kang; Baretic, Domagoj; Goffinont, Stephane; Schuller, Marion; Wu, Wing-Fung; Elkins, Jonathan; Ahel, Dragana; Sanyal, Sumana; Neuhaus, David; Ahel, Ivan. "Updated protein domain annotation of the PARP protein family sheds new light on biological function" Nucleic Acids Res. 51, 8217-8236 (2023).
Assembly members:
entity_1, polymer, 146 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: pET28a-lip
Entity Sequences (FASTA):
entity_1: GNSSASADKPLSNMKILTLG
KLSRNKDEVKAMIEKLGGKL
TGTANKASLCISTKKEVEKM
NKKMEEVKEANIRVVSEDFL
QDVSASTKSLQELFLAHILS
PWGAEVKAEPVEVVAPRGKS
GAALSKKSKGQVKEEGINKS
EKRMKL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 221 |
| 15N chemical shifts | 138 |
| 1H chemical shifts | 244 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PARP1 BRCT domain | 1 |
Entities:
Entity 1, PARP1 BRCT domain 146 residues - Formula weight is not available
The first three residues Gly-Asn-Ser as shown above are a cloning artefact. The native sequence of PARP-1 BRCT starts at Ser 383 and runs to Leu 525.
| 1 | GLY | ASN | SER | SER | ALA | SER | ALA | ASP | LYS | PRO | ||||
| 2 | LEU | SER | ASN | MET | LYS | ILE | LEU | THR | LEU | GLY | ||||
| 3 | LYS | LEU | SER | ARG | ASN | LYS | ASP | GLU | VAL | LYS | ||||
| 4 | ALA | MET | ILE | GLU | LYS | LEU | GLY | GLY | LYS | LEU | ||||
| 5 | THR | GLY | THR | ALA | ASN | LYS | ALA | SER | LEU | CYS | ||||
| 6 | ILE | SER | THR | LYS | LYS | GLU | VAL | GLU | LYS | MET | ||||
| 7 | ASN | LYS | LYS | MET | GLU | GLU | VAL | LYS | GLU | ALA | ||||
| 8 | ASN | ILE | ARG | VAL | VAL | SER | GLU | ASP | PHE | LEU | ||||
| 9 | GLN | ASP | VAL | SER | ALA | SER | THR | LYS | SER | LEU | ||||
| 10 | GLN | GLU | LEU | PHE | LEU | ALA | HIS | ILE | LEU | SER | ||||
| 11 | PRO | TRP | GLY | ALA | GLU | VAL | LYS | ALA | GLU | PRO | ||||
| 12 | VAL | GLU | VAL | VAL | ALA | PRO | ARG | GLY | LYS | SER | ||||
| 13 | GLY | ALA | ALA | LEU | SER | LYS | LYS | SER | LYS | GLY | ||||
| 14 | GLN | VAL | LYS | GLU | GLU | GLY | ILE | ASN | LYS | SER | ||||
| 15 | GLU | LYS | ARG | MET | LYS | LEU |
Samples:
sample_1: PARP1 BRCT domain, [U-13C; U-15N], 0.5 mM; TRIS, [U-2H], 50 mM; sodium chloride 200 mM; zinc sulfate 0.1 mM; DTT, [U-2H], 4 mM; sodium azide 0.02%
sample_conditions_1: ionic strength: 0.2004 M; pH: 7.0; 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 constant-time | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3 - collection, processing
CcpNMR v2.1 - chemical shift assignment
NMR spectrometers:
- Bruker DRX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts