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 5354

Title: Structure and Interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation   PubMed: 12377121

Deposition date: 2002-04-26 Original release date: 2003-01-27

Authors: Amezcua, Carlos; Harper, Shannon; Rutter, Jared; Gardner, Kevin

Citation: Amezcua, Carlos; Harper, Shannon; Rutter, Jared; Gardner, Kevin. "Structure and Interactions of PAS kinase N-terminal PAS domain: Model for Intramolecular Kinase Regulation"  Structure 10, 1349-1361 (2002).

Assembly members:
PAS Kinase PAS-A domain, polymer, 114 residues, 12644.5 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
PAS Kinase PAS-A domain: GAMDPEFNKAIFTVDAKTTE ILVANDKACGLLGYSSQDLI GQKLTQFFLRSDSDVVEALS EEHMEADGHAAVVFGTVVDI ISRSGEKIPVSVWMKRMRQE RRLCCVVVLEPVER

Data sets:
Data typeCount
15N chemical shifts120
1H chemical shifts808
13C chemical shifts502

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

PDB 1LL8
DBJ BAA09484 BAG09616 BAH13702
EMBL CAH18087
GB AAH50565 AAH63585 AAK69752 EAW71236 EAW71237
REF NP_001239048 NP_001239049 NP_001239051 NP_001239053 NP_055963
SP Q96RG2

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