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:
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