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 5131

Title: Structure, Dynamics and Binding Characteristics of the Second PDZ Domain of PTP-BL   PubMed: 11884147

Authors: Walma, Tine; Spronk, Chris; Tessari, Marco; Aelen, Jan; Schepens, Jan; Hendriks, Wiljan; Vuister, Geerten

Citation: Walma, Tine; Spronk, Chris; Tessari, Marco; Aelen, Jan; Schepens, Jan; Hendriks, Wiljan; Vuister, Geerten. "Structure, Dynamics and Binding Characteristics of the Second PDZ Domain of PTP-BL"  J. Mol. Biol. 316, 1101-1110 (2002).

Assembly members:
Protein Tyrosine Phosphatase-BAS Like, polymer, 102 residues, 10837.30 Da.

Natural source:   Common Name: 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):
Protein Tyrosine Phosphatase-BAS Like: MHHHHHHMKPGDTFEVELAK TDGSLGISVTGGVNTSVRHG GIYVKAIIPKGAAESDGRIH KGDRVLAVNGVSLEGATHKQ AVETLRNTGQVVHLLLEKGQ VP

Data sets:
Data typeCount
1H chemical shifts616
13C chemical shifts355
15N chemical shifts102
coupling constants101
T1 relaxation values78
residual dipolar couplings72

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PDZ21

Entities:

Entity 1, PDZ2 102 residues - 10837.30 Da.

1   METHISHISHISHISHISHISMETLYSPRO
2   GLYASPTHRPHEGLUVALGLULEUALALYS
3   THRASPGLYSERLEUGLYILESERVALTHR
4   GLYGLYVALASNTHRSERVALARGHISGLY
5   GLYILETYRVALLYSALAILEILEPROLYS
6   GLYALAALAGLUSERASPGLYARGILEHIS
7   LYSGLYASPARGVALLEUALAVALASNGLY
8   VALSERLEUGLUGLYALATHRHISLYSGLN
9   ALAVALGLUTHRLEUARGASNTHRGLYGLN
10   VALVALHISLEULEULEUGLULYSGLYGLN
11   VALPRO

Samples:

sample_1: Protein Tyrosine Phosphatase-BAS Like, [U-2H; U-15N; U-13C], 1.3 mM; K2HPO4/KH2PO4 50 mM; KCl 50 mM

conditions_1: pH: 6.3; temperature: 298 K; ionic strength: 0.1 M; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1not availableconditions_1
3D C(CO)NHsample_1not availableconditions_1
3D HNCOsample_1not availableconditions_1
3D HNCACBsample_1not availableconditions_1
3D CBCA(CO)NHsample_1not availableconditions_1
3D HBCBCA(CO)NHsample_1not availableconditions_1
3D HNHAsample_1not availableconditions_1
3D HNHBsample_1not availableconditions_1
3D HCCHsample_1not availableconditions_1
3D CCHsample_1not availableconditions_1
3D 13C NOESY HSQC (aliphatic)sample_1not availableconditions_1
3D 13C NOESY HMQC (aromatic)sample_1not availableconditions_1
3D 15N Noesy HSQCsample_1not availableconditions_1

Software:

nmrPipe v1.8 - spectral processing

XEASY v1.2 - peak integration and assignment

X-PLOR v3.851 - simulated annealing, restrained molecular dynamics

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Bruker DRX 600 MHz

Related Database Links:

GenBank AAC42056 AAC42055
PDB
BMRB 6092 6091 6060