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 15401

Title: Calcium binding protein in the free form   PubMed: 21330362

Deposition date: 2007-07-22 Original release date: 2011-05-03

Authors: Zhang, X.; Hu, Y.; Jin, C.

Citation: Hu, Yunfei; Zhang, Xinxin; Shi, Yunming; Zhou, Yanfeng; Zhang, Wei; Su, Xiao-Dong; Xia, Bin; Zhao, Jindong; Jin, Changwen. "Structures of Anabaena Calcium-binding Protein CcbP: INSIGHTS INTO CA2+ SIGNALING DURING HETEROCYST DIFFERENTIATION."  J. Biol. Chem. 286, 12381-12388 (2011).

Assembly members:
Alr1010_protein, polymer, 126 residues, Formula weight is not available

Natural source:   Common Name: Anabaena sp.   Taxonomy ID: 1167   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Anabaena Anabaena sp.

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):
Alr1010_protein: MASVERDETREHRIETEIIV DAEDKEERAMGWYYYLDDTL EFPFMGKWKKKSRKTSTIEE KTVEVLGMAPDDECLKDMYV EVADIGGKDDDVYTAKLSDI EAIDVDDDTQEAIADWLYWL ARGYKF

Data sets:
Data typeCount
13C chemical shifts532
15N chemical shifts127
1H chemical shifts805

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ccbp1

Entities:

Entity 1, ccbp 126 residues - Formula weight is not available

1   METALASERVALGLUARGASPGLUTHRARG
2   GLUHISARGILEGLUTHRGLUILEILEVAL
3   ASPALAGLUASPLYSGLUGLUARGALAMET
4   GLYTRPTYRTYRTYRLEUASPASPTHRLEU
5   GLUPHEPROPHEMETGLYLYSTRPLYSLYS
6   LYSSERARGLYSTHRSERTHRILEGLUGLU
7   LYSTHRVALGLUVALLEUGLYMETALAPRO
8   ASPASPGLUCYSLEULYSASPMETTYRVAL
9   GLUVALALAASPILEGLYGLYLYSASPASP
10   ASPVALTYRTHRALALYSLEUSERASPILE
11   GLUALAILEASPVALASPASPASPTHRGLN
12   GLUALAILEALAASPTRPLEUTYRTRPLEU
13   ALAARGGLYTYRLYSPHE

Samples:

sample: Alr1010 protein, [U-15N; U-13C], 1 mM; Tris 20 mM; NaCl 220 mM; DTT 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 220 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D_13C-separated_NOESYsampleisotropicsample_conditions_1
3D_15N-separated_NOESYsampleisotropicsample_conditions_1
HNCACB,CBCA(CO)NHsampleisotropicsample_conditions_1
HNCO,HN(CA)COsampleisotropicsample_conditions_1
HC(C)H-COSYsampleisotropicsample_conditions_1
HC(C)H-TOCSYsampleisotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v2.1, F.Delaglio, S.Grzesiek, G.W.Vuister, G.Zhu, J.Pfeifer, A.Bax - processing

NMRView v5, B.A.Johnson, R.A.Blevins - data analysis

DYANA vcyana2.0, P.Guntert, C.Mumenthaler, Wuthrich, K.W.Thrich - structure solution

AMBER v7.0, D.A.Case - refinement

NMR spectrometers:

  • Bruker AVANCE 800 MHz
  • Bruker AVANCE 500 MHz

Related Database Links:

BMRB 15402
PDB
DBJ BAB72967
GB AAX13998
REF WP_010995184

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