BMRB Entry 34081
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34081
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title: Solution structure of TDP-43 (residues 1-102) PubMed: 28566288
Deposition date: 2016-12-22 Original release date: 2017-06-02
Authors: Mompean, M.; Romano, V.; Pantoja-Uceda, D.; Stuani, C.; Baralle, F.; Laurents, D.
Citation: Mompean, M.; Romano, V.; Pantoja-Uceda, D.; Stuani, C.; Baralle, F.; Buratti, E.; Laurents, D.. "Point mutations in transactive response DNA-binding protein 43 (TDP-43)'s N-terminal domain compromise its stability, dimerization and functions" J. Biol. Chem. 292, 11992-12006 (2017).
Assembly members:
entity_1, polymer, 114 residues, 12674.207 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: MAGSHHHHHHGSMSEYIRVT
EDENDEPIEIPSEDDGTVLL
STVTAQFPGACGLRYRNPVS
QCMRGVRLVEGILHAPDAGW
GNLVYVVNYPKDNKRKMDET
DASSAVKVKRAVQK
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 1 |
| 1H chemical shifts | 584 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 114 residues - 12674.207 Da.
| 1 | MET | ALA | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | GLY | SER | MET | SER | GLU | TYR | ILE | ARG | VAL | THR | ||||
| 3 | GLU | ASP | GLU | ASN | ASP | GLU | PRO | ILE | GLU | ILE | ||||
| 4 | PRO | SER | GLU | ASP | ASP | GLY | THR | VAL | LEU | LEU | ||||
| 5 | SER | THR | VAL | THR | ALA | GLN | PHE | PRO | GLY | ALA | ||||
| 6 | CYS | GLY | LEU | ARG | TYR | ARG | ASN | PRO | VAL | SER | ||||
| 7 | GLN | CYS | MET | ARG | GLY | VAL | ARG | LEU | VAL | GLU | ||||
| 8 | GLY | ILE | LEU | HIS | ALA | PRO | ASP | ALA | GLY | TRP | ||||
| 9 | GLY | ASN | LEU | VAL | TYR | VAL | VAL | ASN | TYR | PRO | ||||
| 10 | LYS | ASP | ASN | LYS | ARG | LYS | MET | ASP | GLU | THR | ||||
| 11 | ASP | ALA | SER | SER | ALA | VAL | LYS | VAL | LYS | ARG | ||||
| 12 | ALA | VAL | GLN | LYS |
Samples:
sample_1: TDP-43(1-102), [U-13C; U-15N], 0.35 mM
sample_conditions_1: pH: 3.9; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
NMR spectrometers:
- Bruker AvanceII 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts