BMRB Entry 4516

Title:
Solution Structure of the PDZ2 Domain from Human Phosphatase hPTP1E and its Interactions with C-terminal Peptides from the Fas Receptor
Deposition date:
1999-10-08
Original release date:
2000-12-15
Authors:
Kozlov, G.; Gehring, K.; Ekiel, I.
Citation:

Citation: Kozlov, G.; Gehring, K.; Ekiel, I.. "Solution Structure of the PDZ2 Domain from Human Phosphatase hPTP1E and its Interactions with C-terminal Peptides from the Fas Receptor"  Biochemistry 39, 2572-2580 (2000).

Assembly members:

Assembly members:
HUMAN PHOSPHATASE HPTP1E, polymer, 96 residues, Formula weight is not available
peptide, polymer, 15 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts208
15N chemical shifts89
1H chemical shifts570
coupling constants71

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PDZ domain1
2peptide2

Entities:

Entity 1, PDZ domain 96 residues - Formula weight is not available

1   PROLYSPROGLYASPILEPHEGLUVALGLU
2   LEUALALYSASNASPASNSERLEUGLYILE
3   SERVALTHRGLYGLYVALASNTHRSERVAL
4   ARGHISGLYGLYILETYRVALLYSALAVAL
5   ILEPROGLNGLYALAALAGLUSERASPGLY
6   ARGILEHISLYSGLYASPARGVALLEUALA
7   VALASNGLYVALSERLEUGLUGLYALATHR
8   HISLYSGLNALAVALGLUTHRLEUARGASN
9   THRGLYGLNVALVALHISLEULEULEUGLU
10   LYSGLYGLNSERPROTHR

Entity 2, peptide 15 residues - Formula weight is not available

1   PHEALAASPSERGLUALAASPGLUASNGLU
2   GLNVALSERALAVAL

Samples:

sample_1: HUMAN PHOSPHATASE HPTP1E, [U-15N], 1.0 – 5.0 mM; peptide1.2 – 6.0 mM

sample_2: HUMAN PHOSPHATASE HPTP1E1.0 – 5.0 mM; peptide1.2 – 6.0 mM

sample_3: HUMAN PHOSPHATASE HPTP1E, [U-13C; U-15N], 1.0 – 5.0 mM; peptide1.2 – 6.0 mM

sample_cond_1: ionic strength: 0.15 M; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-SEPARATED_NOESYnot availablenot availablenot available
3D 15N-SEPARATED NOESYnot availablenot availablenot available
2D NOESYnot availablenot availablenot available

Software:

xwinnmr v2.1 - COLLECTION

GIFA v4.0 - PROCESSING

XEASY v1.3.13 - DATA ANALYSIS

CNS v0.5 - STRUCTURE SOLUTION

ARIA v0.1 - STRUCTURE SOLUTION

NMR spectrometers:

  • BRUKER DRX 500 MHz

Related Database Links:

BMRB 18833 18834 4123 4124
PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks