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 30196

Title: Solution structure of the CaM34 with the iNOS CaM binding domain peptide   PubMed: 28121131

Deposition date: 2016-10-19 Original release date: 2017-09-25

Authors: Piazza, M.; Dieckmann, T.; Guillemette, J.

Citation: Piazza, Michael; Taiakina, Valentina; Dieckmann, Thorsten; Guillemette, J Guy. "Structural Consequences of Calmodulin EF Hand Mutations."  Biochemistry 56, 944-956 (2017).

Assembly members:
Calmodulin, polymer, 148 residues, 16633.330 Da.
Nitric oxide synthase, inducible, polymer, 29 residues, 3402.371 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 SEEEIREAFRVFAKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREAAIDGDGQVNYEE FVQMMTAK
Nitric oxide synthase, inducible: AGHMRPKRREIPLKVLVKAV LFACMLMRK

Data sets:
Data typeCount
13C chemical shifts438
15N chemical shifts161
1H chemical shifts1010

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