BMRB Entry 5850
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5850
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Title: Kinetic and Structural Studies of the Low Moleuclar Weight Protein Tyrosine Phosphatase from Tritrichomonas foetus PubMed: 16195543
Deposition date: 2003-06-26 Original release date: 2005-10-21
Authors: Thomas, C.; Hallenga, K.; Stauffacher, C.; Van Etten, R.
Citation: Gustafson, Christin; Stauffacher, Cynthia; Hallenga, Klaas; Van Etten, Robert. "Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop" Protein Sci. 14, 2515-2525 (2005).
Assembly members:
protein tyrosine phosphatase (E.C.3.1.3.48), polymer, 146 residues, Formula weight is not available
Natural source: Common Name: Tritrichomonas foetus Taxonomy ID: 5724 Superkingdom: Eukaryota Kingdom: not available Genus/species: Tritrichomonas foetus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
protein tyrosine phosphatase (E.C.3.1.3.48): AAEKKAVLFVCLGNICRSPA
CEGICRDMVGDKLIIDSAAT
SGFHVGQSPDTRSQKVCKSN
GVDISKQRARQITKADFSKF
DVIAALDQSILSDINSMKPS
NCRAKVVLFNPPNGVDDPYY
SSDGFPTMFASISKEMKPFL
TEHGLI
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 900 |
| 13C chemical shifts | 439 |
| 15N chemical shifts | 153 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | protein tyrosine phosphatase | 1 |
Entities:
Entity 1, protein tyrosine phosphatase 146 residues - Formula weight is not available
| 1 | ALA | ALA | GLU | LYS | LYS | ALA | VAL | LEU | PHE | VAL | ||||
| 2 | CYS | LEU | GLY | ASN | ILE | CYS | ARG | SER | PRO | ALA | ||||
| 3 | CYS | GLU | GLY | ILE | CYS | ARG | ASP | MET | VAL | GLY | ||||
| 4 | ASP | LYS | LEU | ILE | ILE | ASP | SER | ALA | ALA | THR | ||||
| 5 | SER | GLY | PHE | HIS | VAL | GLY | GLN | SER | PRO | ASP | ||||
| 6 | THR | ARG | SER | GLN | LYS | VAL | CYS | LYS | SER | ASN | ||||
| 7 | GLY | VAL | ASP | ILE | SER | LYS | GLN | ARG | ALA | ARG | ||||
| 8 | GLN | ILE | THR | LYS | ALA | ASP | PHE | SER | LYS | PHE | ||||
| 9 | ASP | VAL | ILE | ALA | ALA | LEU | ASP | GLN | SER | ILE | ||||
| 10 | LEU | SER | ASP | ILE | ASN | SER | MET | LYS | PRO | SER | ||||
| 11 | ASN | CYS | ARG | ALA | LYS | VAL | VAL | LEU | PHE | ASN | ||||
| 12 | PRO | PRO | ASN | GLY | VAL | ASP | ASP | PRO | TYR | TYR | ||||
| 13 | SER | SER | ASP | GLY | PHE | PRO | THR | MET | PHE | ALA | ||||
| 14 | SER | ILE | SER | LYS | GLU | MET | LYS | PRO | PHE | LEU | ||||
| 15 | THR | GLU | HIS | GLY | LEU | ILE |
Samples:
sample_1: protein tyrosine phosphatase (E.C.3.1.3.48), [U-15N; U-13C], 1 – 2 mM; NaCl 130 mM; NaH2PO4 20 mM; DSS 1 mM; H20 90%; D2O 10%
sample_2: protein tyrosine phosphatase (E.C.3.1.3.48), [U-15N], 1 – 2 mM; NaCl 130 mM; NaH2PO4 20 mM; DSS 1 mM; H20 90%; D2O 10%
sample_cond_1: pH: 5.2; temperature: 298 K; ionic strength: 130 mM; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 13C-separated NOESY | not available | not available | not available |
| HNHA | not available | not available | not available |
| 3D 15N-separated NOESY | not available | not available | not available |
Software:
VNMR v6.1c - collection
NMRPipe vNA - processing
SPARKY v3 - data analysis
X-PLOR v3.851 - structure solution, refinement
NMR spectrometers:
- 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