BMRB Entry 11100
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11100
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: The solution structure of the first thioredoxin domain of mouse Protein disulfide-isomerase A6
Deposition date: 2010-02-18 Original release date: 2011-02-17
Authors: Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation: Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "The solution structure of the first thioredoxin domain of mouse Protein disulfide-isomerase A6" . ., .-..
Assembly members:
1st thioredoxin domain, polymer, 130 residues, Formula weight is not available
Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
1st thioredoxin domain: GSSGSSGAVSGLYSSSDDVI
ELTPSNFNREVIQSDGLWLV
EFYAPWCGHCQRLTPEWKKA
ATALKDVVKVGAVNADKHQS
LGGQYGVQGFPTIKIFGANK
NKPEDYQGGRTGEAIVDAAL
SALRSGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 536 |
| 15N chemical shifts | 128 |
| 1H chemical shifts | 825 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | 1st thioredoxin domain | 1 |
Entities:
Entity 1, 1st thioredoxin domain 130 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | ALA | VAL | SER | |
| 2 | GLY | LEU | TYR | SER | SER | SER | ASP | ASP | VAL | ILE | |
| 3 | GLU | LEU | THR | PRO | SER | ASN | PHE | ASN | ARG | GLU | |
| 4 | VAL | ILE | GLN | SER | ASP | GLY | LEU | TRP | LEU | VAL | |
| 5 | GLU | PHE | TYR | ALA | PRO | TRP | CYS | GLY | HIS | CYS | |
| 6 | GLN | ARG | LEU | THR | PRO | GLU | TRP | LYS | LYS | ALA | |
| 7 | ALA | THR | ALA | LEU | LYS | ASP | VAL | VAL | LYS | VAL | |
| 8 | GLY | ALA | VAL | ASN | ALA | ASP | LYS | HIS | GLN | SER | |
| 9 | LEU | GLY | GLY | GLN | TYR | GLY | VAL | GLN | GLY | PHE | |
| 10 | PRO | THR | ILE | LYS | ILE | PHE | GLY | ALA | ASN | LYS | |
| 11 | ASN | LYS | PRO | GLU | ASP | TYR | GLN | GLY | GLY | ARG | |
| 12 | THR | GLY | GLU | ALA | ILE | VAL | ASP | ALA | ALA | LEU | |
| 13 | SER | ALA | LEU | ARG | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: 1st thioredoxin domain, [U-13C; U-15N], 1.3 mM; d-Tris-HCl, [U-2H], 20 mM; sodium chloride 100 mM; d-DTT, [U-2H], 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 120 M; pH: 7.0; pressure: 1 atm; temperature: 296 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr v3.5, Bruker - collection
NMRPipe v20031121, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.955, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - structure solution
NMR spectrometers:
- Bruker AVANCE 900 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts