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

Deposition date: 2001-09-06 Original release date: 2004-02-05

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:

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Related Database Links:

GenBank AAC42056 AAC42055
PDB 1VJ6 1GM1
BMRB 6092 6091 6060

Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts