BMRB Entry 36180
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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/BMR36180
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Title: Solution Structure of Thioredoxin-Like Effector Protein (TRX3) from Edwardsiella tarda
Deposition date: 2018-04-16 Original release date: 2019-05-20
Authors: Sayed, A.; Mok, Y.
Citation: Sayed, A.; Mok, Y.. "Solution Structure of Thioredoxin-Like Effector Protein (TRX3) from Edwardsiella tarda" . ., .-..
Assembly members:
Thioredoxin (H-type,TRX-H), polymer, 122 residues, 13694.305 Da.
Natural source: Common Name: Edwardsiella tarda Taxonomy ID: 498217 Superkingdom: Bacteria Kingdom: not available Genus/species: Edwardsiella Edwardsiella tarda
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
Thioredoxin (H-type,TRX-H): MHHHHHHSSGLVPRGSQAAS
VEPYSDAAFTQAQASGAPVL
VDVYADWCPVCKRQERELTP
LFAQPAQRDLRVFKVNFDTQ
KAALQQFRVSQQSTLILYRN
GQEVRRSIGETSPSALSDFL
TR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 188 |
| 15N chemical shifts | 95 |
| 1H chemical shifts | 347 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 122 residues - 13694.305 Da.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | ||||
| 2 | LEU | VAL | PRO | ARG | GLY | SER | GLN | ALA | ALA | SER | ||||
| 3 | VAL | GLU | PRO | TYR | SER | ASP | ALA | ALA | PHE | THR | ||||
| 4 | GLN | ALA | GLN | ALA | SER | GLY | ALA | PRO | VAL | LEU | ||||
| 5 | VAL | ASP | VAL | TYR | ALA | ASP | TRP | CYS | PRO | VAL | ||||
| 6 | CYS | LYS | ARG | GLN | GLU | ARG | GLU | LEU | THR | PRO | ||||
| 7 | LEU | PHE | ALA | GLN | PRO | ALA | GLN | ARG | ASP | LEU | ||||
| 8 | ARG | VAL | PHE | LYS | VAL | ASN | PHE | ASP | THR | GLN | ||||
| 9 | LYS | ALA | ALA | LEU | GLN | GLN | PHE | ARG | VAL | SER | ||||
| 10 | GLN | GLN | SER | THR | LEU | ILE | LEU | TYR | ARG | ASN | ||||
| 11 | GLY | GLN | GLU | VAL | ARG | ARG | SER | ILE | GLY | GLU | ||||
| 12 | THR | SER | PRO | SER | ALA | LEU | SER | ASP | PHE | LEU | ||||
| 13 | THR | ARG |
Samples:
sample_1: TRX3, [U-13C; U-15N], 0.5 mM; phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
SPARKY, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts