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

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:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Calmodulin C-Lobe1
2ER alpha peptide2
3CA2_13
4CA2_23

Entities:

Entity 1, Calmodulin C-Lobe 67 residues - 7737.527 Da.

1   GLUGLUGLUILEARGGLUALAPHEARGVAL
2   PHEASPLYSASPGLYASNGLYTYRILESER
3   ALAALAGLULEUARGHISVALMETTHRASN
4   LEUGLYGLULYSLEUTHRASPGLUGLUVAL
5   ASPGLUMETILEARGGLUALAASPILEASP
6   GLYASPGLYGLNVALASNTYRGLUGLUPHE
7   VALGLNMETMETTHRALALYS

Entity 2, ER alpha peptide 19 residues - 2202.663 Da.

1   ARGALAALAASNLEUTRPPROSERPROLEU
2   METILELYSARGSERLYSLYSASNSER

Entity 3, CA2_1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: Cal_C, [U-100% 13C; U-100% 15N], 1 mM; H2O 93%; D2O 7%; Tris-d11 20 mM; sodium chloride 50 mM; CaCl2 5 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 7.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 11440 16994 17881 17981 17982 17983 18323 19376 25344
PDB
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