BMRB Entry 4318
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4318
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Title: Assignment of 1H, 13C, and 15N Resonances of Reduced Escherichia coli Glutaredoxin 2
Deposition date: 1999-03-12 Original release date: 1999-08-12
Authors: Xia, Bin; Chung, John; Vlamis-Gardikas, Alexios; Holmgren, Arne; Wright, Peter; Dyson, H.
Citation: Xia, Bin; Chung, John; Vlamis-Gardikas, Alexios; Holmgren, Arne; Wright, Peter; Dyson, H.. "Assignment of 1H, 13C, and 15N Resonances of Reduced Escherichia coli Glutaredoxin 2" J. Biomol. NMR 14, 197-198 (1999).
Assembly members:
glutaredoxin 2, polymer, 215 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
glutaredoxin 2: MKLYIYDHCPYCLKARMIFG
LKNIPVELHVLLNDDAETPT
RMVGQKQVPILQKDDSRYMP
ESMDIVHYVDKLDGKPLLTG
KRSPAIEEWLRKVNGYANKL
LLPRFAKSAFDEFSTPAARK
YFVDKKEASAGNFADLLAHS
DGLIKNISDDLRALDKLIVK
PNAVNGELSEDDIQLFPLLR
NLTLVAGINWPSRVADYRDN
MAKQTQINLLSSMAI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 788 |
| 15N chemical shifts | 193 |
| 1H chemical shifts | 1199 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | glutaredoxin 2 | 1 |
Entities:
Entity 1, glutaredoxin 2 215 residues - Formula weight is not available
| 1 | MET | LYS | LEU | TYR | ILE | TYR | ASP | HIS | CYS | PRO | ||||
| 2 | TYR | CYS | LEU | LYS | ALA | ARG | MET | ILE | PHE | GLY | ||||
| 3 | LEU | LYS | ASN | ILE | PRO | VAL | GLU | LEU | HIS | VAL | ||||
| 4 | LEU | LEU | ASN | ASP | ASP | ALA | GLU | THR | PRO | THR | ||||
| 5 | ARG | MET | VAL | GLY | GLN | LYS | GLN | VAL | PRO | ILE | ||||
| 6 | LEU | GLN | LYS | ASP | ASP | SER | ARG | TYR | MET | PRO | ||||
| 7 | GLU | SER | MET | ASP | ILE | VAL | HIS | TYR | VAL | ASP | ||||
| 8 | LYS | LEU | ASP | GLY | LYS | PRO | LEU | LEU | THR | GLY | ||||
| 9 | LYS | ARG | SER | PRO | ALA | ILE | GLU | GLU | TRP | LEU | ||||
| 10 | ARG | LYS | VAL | ASN | GLY | TYR | ALA | ASN | LYS | LEU | ||||
| 11 | LEU | LEU | PRO | ARG | PHE | ALA | LYS | SER | ALA | PHE | ||||
| 12 | ASP | GLU | PHE | SER | THR | PRO | ALA | ALA | ARG | LYS | ||||
| 13 | TYR | PHE | VAL | ASP | LYS | LYS | GLU | ALA | SER | ALA | ||||
| 14 | GLY | ASN | PHE | ALA | ASP | LEU | LEU | ALA | HIS | SER | ||||
| 15 | ASP | GLY | LEU | ILE | LYS | ASN | ILE | SER | ASP | ASP | ||||
| 16 | LEU | ARG | ALA | LEU | ASP | LYS | LEU | ILE | VAL | LYS | ||||
| 17 | PRO | ASN | ALA | VAL | ASN | GLY | GLU | LEU | SER | GLU | ||||
| 18 | ASP | ASP | ILE | GLN | LEU | PHE | PRO | LEU | LEU | ARG | ||||
| 19 | ASN | LEU | THR | LEU | VAL | ALA | GLY | ILE | ASN | TRP | ||||
| 20 | PRO | SER | ARG | VAL | ALA | ASP | TYR | ARG | ASP | ASN | ||||
| 21 | MET | ALA | LYS | GLN | THR | GLN | ILE | ASN | LEU | LEU | ||||
| 22 | SER | SER | MET | ALA | ILE |
Samples:
sample_one: glutaredoxin 2, [U-13C; U-15N], 1.5 – 2.5 mM
sample_conditions: pH: 7.0 na; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|
Software:
No software information available
NMR spectrometers:
- unknown unknown 0 MHz
Related Database Links:
| PDB | |
| DBJ | BAA35872 BAB34865 BAG76651 BAI24698 BAI29948 |
| EMBL | CAA63058 CAP75556 CAQ31585 CAQ97963 CAR02405 |
| GB | AAC74148 AAG55810 AAN42692 AAN79804 AAP16579 |
| REF | NP_309469 NP_415582 NP_706985 WP_000780905 WP_000780906 |
| SP | P0AC59 P0AC60 P0AC61 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts