BMRB Entry 16518
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16518
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Title: Backbone resonance assignments for oxidised Trypanosoma cruzi glutathione peroxidase PubMed: 19886864
Deposition date: 2009-09-24 Original release date: 2009-11-20
Authors: Driscoll, Paul; Harris, Richard; Patel, Shreenal; Djordjevic, Snezana
Citation: Patel, Shreenal; Hussain, Syeed; Harris, Richard; Sardiwal, Sunita; Kelly, John; Wilkinson, Shane; Driscoll, Paul; Djordjevic, Snezana. "Structural insights into the catalytic mechanism of Trypanosoma cruzi GPXI (glutathione peroxidase-like enzyme I)." Biochem. J. 425, 513-522 (2010).
Assembly members:
TcGPXI, polymer, 168 residues, Formula weight is not available
Natural source: Common Name: Trypanosoma cruzi Taxonomy ID: 5693 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma cruzi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TcGPXI: GAKSIYEFQVNAADGKPYDL
SQHKGHPLLIYNVASRCGYT
KGGYETATTLYNKYKGQGFT
VLAFPCNQFAGQEPGTALEV
KEFACTRFKADFPIMAKIDV
NGSGAKAHPLYEFMKATIPG
LFGTKAIKWNFTSFLIDRHG
VPVERFSPGASVEDIEKKLL
PLLGGARI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 473 |
| 15N chemical shifts | 149 |
| 1H chemical shifts | 323 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TcGPXI | 1 |
Entities:
Entity 1, TcGPXI 168 residues - Formula weight is not available
| 1 | GLY | ALA | LYS | SER | ILE | TYR | GLU | PHE | GLN | VAL | ||||
| 2 | ASN | ALA | ALA | ASP | GLY | LYS | PRO | TYR | ASP | LEU | ||||
| 3 | SER | GLN | HIS | LYS | GLY | HIS | PRO | LEU | LEU | ILE | ||||
| 4 | TYR | ASN | VAL | ALA | SER | ARG | CYS | GLY | TYR | THR | ||||
| 5 | LYS | GLY | GLY | TYR | GLU | THR | ALA | THR | THR | LEU | ||||
| 6 | TYR | ASN | LYS | TYR | LYS | GLY | GLN | GLY | PHE | THR | ||||
| 7 | VAL | LEU | ALA | PHE | PRO | CYS | ASN | GLN | PHE | ALA | ||||
| 8 | GLY | GLN | GLU | PRO | GLY | THR | ALA | LEU | GLU | VAL | ||||
| 9 | LYS | GLU | PHE | ALA | CYS | THR | ARG | PHE | LYS | ALA | ||||
| 10 | ASP | PHE | PRO | ILE | MET | ALA | LYS | ILE | ASP | VAL | ||||
| 11 | ASN | GLY | SER | GLY | ALA | LYS | ALA | HIS | PRO | LEU | ||||
| 12 | TYR | GLU | PHE | MET | LYS | ALA | THR | ILE | PRO | GLY | ||||
| 13 | LEU | PHE | GLY | THR | LYS | ALA | ILE | LYS | TRP | ASN | ||||
| 14 | PHE | THR | SER | PHE | LEU | ILE | ASP | ARG | HIS | GLY | ||||
| 15 | VAL | PRO | VAL | GLU | ARG | PHE | SER | PRO | GLY | ALA | ||||
| 16 | SER | VAL | GLU | ASP | ILE | GLU | LYS | LYS | LEU | LEU | ||||
| 17 | PRO | LEU | LEU | GLY | GLY | ALA | ARG | ILE |
Samples:
sample_1: TcGPXI, [U-99% 13C; U-99% 15N], 0.8 mM; phosphate 50 mM; sodium chloride 300 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.350 M; pH: 6.5; pressure: 1.0 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HA(CA)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
ANSIG, Kraulis - chemical shift assignment
NMR spectrometers:
- Varian UnityPlus 500 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts