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 392

Title: Structural Characterization of the Interactions between Calmodulin and Skeletal Muscle Myosin Light Chain Kinase: Effect of Peptide (576-594)G Binding on the Ca2+-Binding Domains

Deposition date: 1995-07-31 Original release date: 1995-07-31

Authors: Seeholzer, Steven; Wand, A.

Citation: Seeholzer, Steven; Wand, A.. "Structural Characterization of the Interactions between Calmodulin and Skeletal Muscle Myosin Light Chain Kinase: Effect of Peptide (576-594)G Binding on the Ca2+-Binding Domains"  Biochemistry 28, 4011-4020 (1989).

Assembly members:
calmodulin, polymer, 139 residues, Formula weight is not available

Natural source:   Common Name: cow   Taxonomy ID: 9909   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos primigenius

Experimental source:   Production method: not available

Entity Sequences (FASTA):
calmodulin: XXXXXXXXXXXXXXXXXXXX XXGDGTITTKXXXXXXXXXX XXXXXXXXXXXXXXXXXXXN GTIDFXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXGNGYI SAAXXXXXXXXXXXXXXXXX XXXXXXXXXXXGDGQVNYE

Data sets:
Data typeCount
1H chemical shifts123

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1calmodulin1

Entities:

Entity 1, calmodulin 139 residues - Formula weight is not available

1   XXXXXXXXXX
2   XXXXXXXXXX
3   XXGLYASPGLYTHRILETHRTHRLYS
4   XXXXXXXXXX
5   XXXXXXXXXX
6   XXXXXXXXXASN
7   GLYTHRILEASPPHEXXXXX
8   XXXXXXXXXX
9   XXXXXXXXXX
10   XXXXXGLYASNGLYTYRILE
11   SERALAALAXXXXXXX
12   XXXXXXXXXX
13   XXXXXXXXXX
14   XGLYASPGLYGLNVALASNTYRGLU

Samples:

sample_one:

sample_condition_set_one: pH: 6.5 na; temperature: 330 K

Experiments:

NameSampleSample stateSample conditions
not availablesample_onenot availablesample_condition_set_one

Software:

No software information available

NMR spectrometers:

  • unknown unknown 0 MHz

Related Database Links:

BMRB 391