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 30063

Title: Structure of calmodulin in a complex with a peptide derived from a calmodulin-dependent kinase   PubMed: 27499441

Authors: Alphonse, S.; Lee, K.; Piserchio, A.; Tavares, C.; Giles, D.; Wellmann, R.; Dalby, K.; Ghose, R.

Citation: Lee, K.; Alphonse, S.; Piserchio, A.; Tavares, C.; Giles, D.; Wellmann, R.; Dalby, K.; Ghose, R.. "Structural Basis for the Recognition of Eukaryotic Elongation Factor 2 Kinase by Calmodulin"  Structure 24, 1441-1451 (2016).

Assembly members:
Calmodulin, polymer, 148 residues, 16721.350 Da.
Eukaryotic elongation factor 2 kinase, polymer, 27 residues, 3167.618 Da.
CALCIUM ION, non-polymer, 40.078 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):
Calmodulin: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
Eukaryotic elongation factor 2 kinase: SPANSFHFKEAWKHAIQKAK HMPDPWA

Data sets:
Data typeCount
13C chemical shifts737
15N chemical shifts183
1H chemical shifts1125

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