BMRB Entry 15063
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15063
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Title: NMR structure of the mouse thiamine triphosphatase PubMed: 18276586
Deposition date: 2006-12-05 Original release date: 2007-02-23
Authors: Song, Jikui; Markley, John
Citation: Song, Jikui; Bettendorff, Lucien; Tonelli, Marco; Markley, John. "Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase." J. Biol. Chem. 283, 10939-10948 (2008).
Assembly members:
ThTPase_MOUSE, polymer, 224 residues, 24253.369 Da.
Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ThTPase_MOUSE: SAQGLIEVERKFAPGPDTEE
RLQELGATLEHRVTFRDTYY
DTSELSLMLSDHWLRQREGS
GWELKCPGVTGVSGPHNEYV
EVTSEAAIVAQLFELLGSGE
QKPAGVAAVLGSLKLQEVAS
FITTRSSWKLALSGAHGQEP
QLTIDLDSADFGYAVGEVEA
MVHEKAEVPAALEKIITVSS
MLGVPAQEEAPAKLMVYLQR
FRPLDYQRLLEAASSGEATG
DSAS
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 876 |
| 15N chemical shifts | 229 |
| 1H chemical shifts | 1378 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ThTPase mouse | 1 |
Entities:
Entity 1, ThTPase mouse 224 residues - 24253.369 Da.
| 1 | SER | ALA | GLN | GLY | LEU | ILE | GLU | VAL | GLU | ARG | ||||
| 2 | LYS | PHE | ALA | PRO | GLY | PRO | ASP | THR | GLU | GLU | ||||
| 3 | ARG | LEU | GLN | GLU | LEU | GLY | ALA | THR | LEU | GLU | ||||
| 4 | HIS | ARG | VAL | THR | PHE | ARG | ASP | THR | TYR | TYR | ||||
| 5 | ASP | THR | SER | GLU | LEU | SER | LEU | MET | LEU | SER | ||||
| 6 | ASP | HIS | TRP | LEU | ARG | GLN | ARG | GLU | GLY | SER | ||||
| 7 | GLY | TRP | GLU | LEU | LYS | CYS | PRO | GLY | VAL | THR | ||||
| 8 | GLY | VAL | SER | GLY | PRO | HIS | ASN | GLU | TYR | VAL | ||||
| 9 | GLU | VAL | THR | SER | GLU | ALA | ALA | ILE | VAL | ALA | ||||
| 10 | GLN | LEU | PHE | GLU | LEU | LEU | GLY | SER | GLY | GLU | ||||
| 11 | GLN | LYS | PRO | ALA | GLY | VAL | ALA | ALA | VAL | LEU | ||||
| 12 | GLY | SER | LEU | LYS | LEU | GLN | GLU | VAL | ALA | SER | ||||
| 13 | PHE | ILE | THR | THR | ARG | SER | SER | TRP | LYS | LEU | ||||
| 14 | ALA | LEU | SER | GLY | ALA | HIS | GLY | GLN | GLU | PRO | ||||
| 15 | GLN | LEU | THR | ILE | ASP | LEU | ASP | SER | ALA | ASP | ||||
| 16 | PHE | GLY | TYR | ALA | VAL | GLY | GLU | VAL | GLU | ALA | ||||
| 17 | MET | VAL | HIS | GLU | LYS | ALA | GLU | VAL | PRO | ALA | ||||
| 18 | ALA | LEU | GLU | LYS | ILE | ILE | THR | VAL | SER | SER | ||||
| 19 | MET | LEU | GLY | VAL | PRO | ALA | GLN | GLU | GLU | ALA | ||||
| 20 | PRO | ALA | LYS | LEU | MET | VAL | TYR | LEU | GLN | ARG | ||||
| 21 | PHE | ARG | PRO | LEU | ASP | TYR | GLN | ARG | LEU | LEU | ||||
| 22 | GLU | ALA | ALA | SER | SER | GLY | GLU | ALA | THR | GLY | ||||
| 23 | ASP | SER | ALA | SER |
Samples:
sample: ThTPase_MOUSE, [U-100% 13C; U-100% 15N], 1.0 mM; MOPS 10 mM; NaCl 100 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H,15N-HSQC | sample | isotropic | sample_conditions_1 |
| 1H,13C-HSQC | sample | isotropic | sample_conditions_1 |
| HNCACB | sample | isotropic | sample_conditions_1 |
| CBCACONH | sample | isotropic | sample_conditions_1 |
| CCONH | sample | isotropic | sample_conditions_1 |
| HCCHTOCSY | sample | isotropic | sample_conditions_1 |
| HBACONH | sample | isotropic | sample_conditions_1 |
| 13C-EDITED 1H,1H-NOESY | sample | isotropic | sample_conditions_1 |
| 15N-EDITED 1H,1H-NOESY | sample | isotropic | sample_conditions_1 |
| 13C-EDITED AROMATIC 1H,1H-NOESY | sample | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement
xwinnmr v3.5, Bruker - collection
NMRPipe v97.027.12.56, Delagio,F. et al. - processing
SPARKY v3.113, Goddard,T.D. and Kneller,D.G. - data analysis
GARANT v2.1, Bartels,C. et al - data analysis
CYANA v2.1, Guntert,P. et al - structural calculation
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker DMX 750 MHz
- Varian INOVA 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts