BMRB Entry 16850
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16850
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Dobrovolska, Olena; Rychkov, Georgy; Shumilina, Elena; Nerinovski, Kirill; Schmidt, Alexander; Shabalin, Konstantin; Yakimov, Alexander; Dikiy, Alexander. "Structural insights into interaction between mammalian methionine sulfoxide reductase B1 and thioredoxin" J. Biomed. Biotechnol. 2012, 586539-586539 (2012).
PubMed: 22505815
Assembly members:
thioredoxin, polymer, 113 residues, 12787.5293 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21
Entity Sequences (FASTA):
thioredoxin: MVKQIESKTAFQEALDAAGD
KLVVVDFSATWCGPSKMIKP
FFHSLSEKYSNVIFLEVDVD
DCQDVASECEVKCMPTFQFF
KKGQKVGEFSGANKEKLEAT
INELVLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 386 |
| 15N chemical shifts | 198 |
| 1H chemical shifts | 568 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | thioredoxin, 1 | 1 |
| 2 | thioredoxin, 2 | 1 |
Entities:
Entity 1, thioredoxin, 1 113 residues - 12787.5293 Da.
| 1 | MET | VAL | LYS | GLN | ILE | GLU | SER | LYS | THR | ALA | ||||
| 2 | PHE | GLN | GLU | ALA | LEU | ASP | ALA | ALA | GLY | ASP | ||||
| 3 | LYS | LEU | VAL | VAL | VAL | ASP | PHE | SER | ALA | THR | ||||
| 4 | TRP | CYS | GLY | PRO | SER | LYS | MET | ILE | LYS | PRO | ||||
| 5 | PHE | PHE | HIS | SER | LEU | SER | GLU | LYS | TYR | SER | ||||
| 6 | ASN | VAL | ILE | PHE | LEU | GLU | VAL | ASP | VAL | ASP | ||||
| 7 | ASP | CYS | GLN | ASP | VAL | ALA | SER | GLU | CYS | GLU | ||||
| 8 | VAL | LYS | CYS | MET | PRO | THR | PHE | GLN | PHE | PHE | ||||
| 9 | LYS | LYS | GLY | GLN | LYS | VAL | GLY | GLU | PHE | SER | ||||
| 10 | GLY | ALA | ASN | LYS | GLU | LYS | LEU | GLU | ALA | THR | ||||
| 11 | ILE | ASN | GLU | LEU | VAL | LEU | GLU | HIS | HIS | HIS | ||||
| 12 | HIS | HIS | HIS |
Samples:
one: thioredoxin, [U-98% 13C; U-98% 15N], 1.5 ± 0.0001 mM; H2O 95%; D2O 5%
standart: ionic strength: 0.025 M; pH: 5.1; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC/HMQC | one | isotropic | standart |
| CBCANH (h{CA|Cca}NH) | one | isotropic | standart |
| 3D CBCA(CO)NH | one | isotropic | standart |
| 3D HNCA | one | isotropic | standart |
| 3D HBHA(CO)NH | one | isotropic | standart |
| HBHANH (H{ca|cca}NH) | one | isotropic | standart |
| 2D 1H-13C HSQC/HMQC | one | isotropic | standart |
| 3D 1H-15N NOESY | one | isotropic | standart |
Software:
CcpNmr_Analysis v2.1, CCPN - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks