BMRB Entry 26771
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26771
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Title: Backbone and Side-chain chemical shift assignments of C. elegans TDP2 Ubiquitin Association domain PubMed: 27543075
Deposition date: 2016-03-24 Original release date: 2016-09-02
Authors: Rao, Timsi; Aihara, Hideki
Citation: Rao, Timsi; Gao, Rui; Takada, Saeko; Al Abo, Muthana; Chen, Xiang; Walters, Kylie; Pommier, Yves; Aihara, Hideki. "Novel TDP2-ubiquitin interactions and their importance for the repair of topoisomerase II-mediated DNA damage" Nucleic Acids Res. 44, 10201-10215 (2016).
Assembly members:
UBA_domain_of_Tyrosyl_DNA_phosphodiesterase_2_protein, polymer, 60 residues, 6501.1 Da.
Natural source: Common Name: nematodes Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: chemical synthesis Host organism: Escherichia coli
Entity Sequences (FASTA):
UBA_domain_of_Tyrosyl_DNA_phosphodiesterase_2_protein: SSMSDEQKLHEFAIITATDE
AFAQSILQDVDWDLKKALDV
FYGSEAFAEARSAAVMGASS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 232 |
15N chemical shifts | 59 |
1H chemical shifts | 317 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | C. elegans TDP2 Ubiquitin Association domain | 1 |
Entities:
Entity 1, C. elegans TDP2 Ubiquitin Association domain 60 residues - 6501.1 Da.
1 | SER | SER | MET | SER | ASP | GLU | GLN | LYS | LEU | HIS | |
2 | GLU | PHE | ALA | ILE | ILE | THR | ALA | THR | ASP | GLU | |
3 | ALA | PHE | ALA | GLN | SER | ILE | LEU | GLN | ASP | VAL | |
4 | ASP | TRP | ASP | LEU | LYS | LYS | ALA | LEU | ASP | VAL | |
5 | PHE | TYR | GLY | SER | GLU | ALA | PHE | ALA | GLU | ALA | |
6 | ARG | SER | ALA | ALA | VAL | MET | GLY | ALA | SER | SER |
Samples:
sample_1: UBA domain of Tyrosyl DNA phosphodiesterase 2 protein, [U-99% 13C; U-99% 15N], 1.0 mM; sodium phosphate 25.0 mM; sodium chloride 50.0 mM; DSS 1.0 mM; H2O 95.0%; D2O 5.0%
sample_conditions_1: pH: 6.5; 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 aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe v8.7, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 900 MHz
Related Database Links:
NCBI | CAA21707.1 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts