BMRB Entry 36060
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36060
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Title: Solution Structure of the N-terminal Domain of TDP-43 PubMed: 28733604
Deposition date: 2017-02-13 Original release date: 2017-08-14
Authors: Jiang, L.-L., L.; Xue, W.; Hu, H.-Y., H.
Citation: Jiang, Lei-Lei; Xue, Wei; Hong, Jun-Ye; Zhang, Jun-Ting; Li, Min-Jun; Yu, Shao-Ning; He, Jian-Hua; Hu, Hong-Yu. "The N-terminal dimerization is required for TDP-43 splicing activity." Sci. Rep. 7, 6196-6196 (2017).
Assembly members:
entity_1, polymer, 77 residues, 8502.391 Da.
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
Entity Sequences (FASTA):
entity_1: MSEYIRVTEDENDEPIEIPS
EDDGTVLLSTVTAQFPGASG
LRYRNPVSQSMRGVRLVEGI
LHAPDAGWGNLVYVVNY
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 275 |
15N chemical shifts | 78 |
1H chemical shifts | 467 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 77 residues - 8502.391 Da.
1 | MET | SER | GLU | TYR | ILE | ARG | VAL | THR | GLU | ASP | ||||
2 | GLU | ASN | ASP | GLU | PRO | ILE | GLU | ILE | PRO | SER | ||||
3 | GLU | ASP | ASP | GLY | THR | VAL | LEU | LEU | SER | THR | ||||
4 | VAL | THR | ALA | GLN | PHE | PRO | GLY | ALA | SER | GLY | ||||
5 | LEU | ARG | TYR | ARG | ASN | PRO | VAL | SER | GLN | SER | ||||
6 | MET | ARG | GLY | VAL | ARG | LEU | VAL | GLU | GLY | ILE | ||||
7 | LEU | HIS | ALA | PRO | ASP | ALA | GLY | TRP | GLY | ASN | ||||
8 | LEU | VAL | TYR | VAL | VAL | ASN | TYR |
Samples:
sample_1: TDP(1-77)-GB1-C39/C50S, U-99% 13C; U-99% 15N, 1 mM; sodium azide 0.05 v/v; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 0.08 M; 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 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O'Donoghue and Nilges - structure calculation
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation
Molmol, Koradi, Billeter and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts