BMRB Entry 11101
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Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11101
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Title: The solution structure of the first thioredoxin domain of mouse Protein disulfide-isomerase A4
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 A4" . ., .-..
Assembly members:
1st thioredoxin domain, polymer, 140 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: GSSGSSGDDDLEVKEENGVW
VLNDGNFDNFVADKDTVLLE
FYAPWCGHCKQFAPEYEKIA
STLKDNDPPIAVAKIDATSA
SMLASKFDVSGYPTIKILKK
GQAVDYDGSRTQEEIVAKVR
EVSQPDWTPPPEVTSGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 600 |
| 15N chemical shifts | 137 |
| 1H chemical shifts | 903 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | 1st thioredoxin domain | 1 |
Entities:
Entity 1, 1st thioredoxin domain 140 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | ASP | ASP | ASP | |
| 2 | LEU | GLU | VAL | LYS | GLU | GLU | ASN | GLY | VAL | TRP | |
| 3 | VAL | LEU | ASN | ASP | GLY | ASN | PHE | ASP | ASN | PHE | |
| 4 | VAL | ALA | ASP | LYS | ASP | THR | VAL | LEU | LEU | GLU | |
| 5 | PHE | TYR | ALA | PRO | TRP | CYS | GLY | HIS | CYS | LYS | |
| 6 | GLN | PHE | ALA | PRO | GLU | TYR | GLU | LYS | ILE | ALA | |
| 7 | SER | THR | LEU | LYS | ASP | ASN | ASP | PRO | PRO | ILE | |
| 8 | ALA | VAL | ALA | LYS | ILE | ASP | ALA | THR | SER | ALA | |
| 9 | SER | MET | LEU | ALA | SER | LYS | PHE | ASP | VAL | SER | |
| 10 | GLY | TYR | PRO | THR | ILE | LYS | ILE | LEU | LYS | LYS | |
| 11 | GLY | GLN | ALA | VAL | ASP | TYR | ASP | GLY | SER | ARG | |
| 12 | THR | GLN | GLU | GLU | ILE | VAL | ALA | LYS | VAL | ARG | |
| 13 | GLU | VAL | SER | GLN | PRO | ASP | TRP | THR | PRO | PRO | |
| 14 | PRO | GLU | VAL | THR | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: Thioredoxin domain, [U-13C; U-15N], 1.2 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 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-SEPARATED NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 13C-SEPARATED 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 |
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