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 18323

Title: Solution structure of the calcium-bound CaM C-terminal domain in a complex   PubMed: 22518098

Deposition date: 2012-03-10 Original release date: 2012-05-08

Authors: Liu, Zhihong

Citation: Liu, Zhihong; Vogel, Hans. "Structural basis for the regulation of L-type voltage-gated calcium channels: interactions between the N-terminal cytoplasmic domain and Ca(2+)-calmodulin."  Front. Mol. Neurosci. 5, 38-38 (2012).

Assembly members:
entity, polymer, 71 residues, 8155.886 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):
entity: DTDSEEEIREAFRVFDKDGN GYISAAELRHVMTNLGEKLT DEEVDEMIREADIDGDGQVN YEEFVQMMTAK

Data sets:
Data typeCount
13C chemical shifts261
15N chemical shifts68
1H chemical shifts250

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1calcium-bound CaM C-terminal domain in a complex1

Entities:

Entity 1, calcium-bound CaM C-terminal domain in a complex 71 residues - 8155.886 Da.

1   ASPTHRASPSERGLUGLUGLUILEARGGLU
2   ALAPHEARGVALPHEASPLYSASPGLYASN
3   GLYTYRILESERALAALAGLULEUARGHIS
4   VALMETTHRASNLEUGLYGLULYSLEUTHR
5   ASPGLUGLUVALASPGLUMETILEARGGLU
6   ALAASPILEASPGLYASPGLYGLNVALASN
7   TYRGLUGLUPHEVALGLNMETMETTHRALA
8   LYS

Samples:

sample_1: CaM 1.0 mM; TRIS 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 500 MHz

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