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 6023

Title: 1H, 15N, and 13C Resonance Assignments of Calmodulin Complexed with the Calmodulin-Binding Domain of Protein Phosphatase 2B   PubMed: 15243184

Deposition date: 2003-11-28 Original release date: 2004-12-01

Authors: Lin, Ta-Hsien; Huang, Jian-Wen; Huang, Hsien-bin; Chen, Yi-chen; Liu, Chia-Yen; Lo, Chi-jen; Tang, Tzu-Chun; Chyan, Chia-Lin

Citation: Lin, Ta-Hsien; Huang, Jian-Wen; Huang, Hsien-bin; Chen, Yi-chen; Liu, Chia-Yen; Lo, Chi-jen; Tang, Tzu; Chyan, Chia-Lin. "Letter to the Editor: 1H, 15N, and 13C Resonance Assignments of Calmodulin Complexed with the Calmodulin-Binding Domain of calcineurin"  J. Biomol. NMR 29, 531-532 (2004).

Assembly members:
Calmodulin, polymer, 148 residues, 16706 Da.
protein phosphatase 2B peptide, polymer, 24 residues, 2812 Da.

Natural source:   Common Name: Chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

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

Entity Sequences (FASTA):
Calmodulin: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
protein phosphatase 2B peptide: ARKEVIRNKIRAIGKMARVF SVLR

Data sets:
Data typeCount
1H chemical shifts837
13C chemical shifts565
15N chemical shifts142

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Calmodulin1
2Protein Phosphatase 2B2

Entities:

Entity 1, Calmodulin 148 residues - 16706 Da.

1   ALAASPGLNLEUTHRGLUGLUGLNILEALA
2   GLUPHELYSGLUALAPHESERLEUPHEASP
3   LYSASPGLYASPGLYTHRILETHRTHRLYS
4   GLULEUGLYTHRVALMETARGSERLEUGLY
5   GLNASNPROTHRGLUALAGLULEUGLNASP
6   METILEASNGLUVALASPALAASPGLYASN
7   GLYTHRILEASPPHEPROGLUPHELEUTHR
8   METMETALAARGLYSMETLYSASPTHRASP
9   SERGLUGLUGLUILEARGGLUALAPHEARG
10   VALPHEASPLYSASPGLYASNGLYTYRILE
11   SERALAALAGLULEUARGHISVALMETTHR
12   ASNLEUGLYGLULYSLEUTHRASPGLUGLU
13   VALASPGLUMETILEARGGLUALAASPILE
14   ASPGLYASPGLYGLNVALASNTYRGLUGLU
15   PHEVALGLNMETMETTHRALALYS

Entity 2, Protein Phosphatase 2B 24 residues - 2812 Da.

1   ALAARGLYSGLUVALILEARGASNLYSILE
2   ARGALAILEGLYLYSMETALAARGVALPHE
3   SERVALLEUARG

Samples:

sample_1: Calmodulin, [U-99% 13C; U-99% 15N], 1.1 mM; protein phosphatase 2B peptide 1.1 mM; KCl 100 mM; CaCl2 5 mM; D2O 10%; H2O 90%

Ex-cond_1: pH: 6.5; temperature: 310 K; ionic strength: 0.13 M

Experiments:

NameSampleSample stateSample conditions
HNCAnot availablenot availablenot available
HN(CO)CAnot availablenot availablenot available
HNCOnot availablenot availablenot available
HN(CA)COnot availablenot availablenot available
CBCANHnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
15N-HSQCnot availablenot availablenot available
HBHA(CACBCO)NHnot availablenot availablenot available
H(CCO)NHnot availablenot availablenot available
C(CO)NHnot availablenot availablenot available
1H-15N HSQC-TOCSYnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

  • Bruker AVANCE 500 MHz
  • Bruker AVANCE 600 MHz

Related Database Links:

BMRB 15624
PDB
DBJ BAA14083 BAB19673 BAC36398 BAE27131 BAE29521 BAE29521 BAE27131 BAC36398 BAB19673 BAA14083
EMBL CAA40398 CAA54807 CAB89253 CAF94324 CAH91746 CAH91746 CAF94324 CAB89253 CAA54807 CAA40398
GB AAA02631 AAA35634 AAA37359 AAA37432 AAA40940
PRF 1714202A 2006264A 2006264A 1714202A
REF NP_000935 NP_001074063 NP_001076161 NP_001080813 NP_001087372 NP_001087372 NP_001080813 NP_001076161 NP_001074063 NP_000935
SP P48452 P63328 P63329 Q08209 Q27889
TPG DAA28842
SWISS-PROT Q27889 Q08209 P63329 P63328 P48452
GenBank AAA40940 AAA37432 AAA37359 AAA35634 AAA02631

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