BMRB Entry 17532

Title:
NMR structure of Ca2+-bound CaBP1 C-domain with RDC
Deposition date:
2011-03-16
Original release date:
2011-06-07
Authors:
Ames, James
Citation:

Citation: Park, Saebomi; Li, Congmin; Ames, James. "Nuclear magnetic resonance structure of calcium-binding protein 1 in a Ca(2+) -bound closed state: implications for target recognition."  Protein Sci. 20, 1356-1366 (2011).
PubMed: 21608059

Assembly members:

Assembly members:
CaBP1, polymer, 167 residues, Formula weight is not available
CA, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET3b

Data sets:
Data typeCount
13C chemical shifts484
15N chemical shifts139
1H chemical shifts731

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CaBP11
2CA2

Entities:

Entity 1, CaBP1 167 residues - Formula weight is not available

1   METGLYASNCYSVALLYSTYRPROLEUARG
2   ASNLEUSERARGLYSASPARGSERLEUARG
3   PROGLUGLUILEGLUGLULEUARGGLUALA
4   PHEARGGLUPHEASPLYSASPLYSASPGLY
5   TYRILEASNCYSARGASPLEUGLYASNCYS
6   METARGTHRMETGLYTYRMETPROTHRGLU
7   METGLULEUILEGLULEUSERGLNGLNILE
8   ASNMETASNLEUGLYGLYHISVALASPPHE
9   ASPASPPHEVALGLULEUMETGLYPROLYS
10   LEULEUALAGLUTHRALAASPMETILEGLY
11   VALLYSGLULEUARGASPALAPHEARGGLU
12   PHEASPTHRASNGLYASPGLYGLUILESER
13   THRSERGLULEUARGGLUALAMETARGLYS
14   LEULEUGLYHISGLNVALGLYHISARGASP
15   ILEGLUGLUILEILEARGASPVALASPLEU
16   ASNGLYASPGLYARGVALASPPHEGLUGLU
17   PHEVALARGMETMETSERARG

Entity 2, CA - Ca - 40.078 Da.

1   CA

Samples:

sample_1: CaBP1, [U-98% 13C; U-98% 15N], 1.0 mM; CA 5.0 mM; TRIS 10.0 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.01 M; pH: 7.4; 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 HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

X-PLOR NIH v2.23, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 15197 15623 16862
PDB
DBJ BAE24603
EMBL CAC43037 CAD20347
GB AAF25782 AAF25784 AAF25787 AAH30201 ABM86439
REF NP_001028847 NP_001028848 NP_001028849 NP_001297641 NP_001297644
SP O88751 Q9NZU7
AlphaFold Q9NZU7 O88751

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks