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 18084

Title: SOLUTION NMR-DERIVED STRUCTURE OF CALMODULIN C-LOBE BOUND WITH ER ALPHA PEPTIDE   PubMed: 22275375

Deposition date: 2011-11-15 Original release date: 2012-01-30

Authors: Zhang, Yonghong

Citation: Zhang, Yonghong; Li, Zhigang; Sacks, David; Ames, James. "Structural basis for Ca2+-induced activation and dimerization of estrogen receptor by calmodulin."  J. Biol. Chem. 287, 9336-9344 (2012).

Assembly members:
Calmodulin C-Lobe, polymer, 67 residues, 7737.527 Da.
ER alpha peptide, polymer, 19 residues, 2202.663 Da.
CALCIUM ION, non-polymer, 40.078 Da.

Natural source:   Common Name: African clawed frog   Taxonomy ID: 8355   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Xenopus laevis

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

Entity Sequences (FASTA):
Calmodulin C-Lobe: EEEIREAFRVFDKDGNGYIS AAELRHVMTNLGEKLTDEEV DEMIREADIDGDGQVNYEEF VQMMTAK
ER alpha peptide: RAANLWPSPLMIKRSKKNS

Data sets:
Data typeCount
13C chemical shifts129
15N chemical shifts67
1H chemical shifts254

Additional metadata:

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Related Database Links:

BMRB 11440 16994 17881 17981 17982 17983 18323 19376 25344
PDB 1CMF 1CMG 1F71 1FW4 1J7P 1YRT 1YRU 1ZOT 2COL 2K3S 2KUH 2KZ2 2LLQ 2LQP 2RRT 4BYA 4RJD
DBJ BAC39089 BAF45809 BAI66109 BAI66110 BAI66111
EMBL CAB51566
GB AAB25484 AAH10730 AAO17827 AAQ14324 AAX61134
REF XP_001687795 XP_001869425 XP_007442524 XP_009577260 XP_010190430

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