BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 5850

Title: Kinetic and Structural Studies of the Low Moleuclar Weight Protein Tyrosine Phosphatase from Tritrichomonas foetus   PubMed: 16195543

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

Data sets:
Data typeCount
1H chemical shifts900
13C chemical shifts439
15N chemical shifts153

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1protein tyrosine phosphatase1

Entities:

Entity 1, protein tyrosine phosphatase 146 residues - Formula weight is not available

1   ALAALAGLULYSLYSALAVALLEUPHEVAL
2   CYSLEUGLYASNILECYSARGSERPROALA
3   CYSGLUGLYILECYSARGASPMETVALGLY
4   ASPLYSLEUILEILEASPSERALAALATHR
5   SERGLYPHEHISVALGLYGLNSERPROASP
6   THRARGSERGLNLYSVALCYSLYSSERASN
7   GLYVALASPILESERLYSGLNARGALAARG
8   GLNILETHRLYSALAASPPHESERLYSPHE
9   ASPVALILEALAALALEUASPGLNSERILE
10   LEUSERASPILEASNSERMETLYSPROSER
11   ASNCYSARGALALYSVALVALLEUPHEASN
12   PROPROASNGLYVALASPASPPROTYRTYR
13   SERSERASPGLYPHEPROTHRMETPHEALA
14   SERILESERLYSGLUMETLYSPROPHELEU
15   THRGLUHISGLYLEUILE

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:

NameSampleSample stateSample conditions
3D 13C-separated NOESYnot availablenot availablenot available
HNHAnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot 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

Related Database Links:

PDB
GB AAB51113