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 16918

Title: Mg(2+)-bound receiver domain of sensor histidine kinase CKI1RD of Arabidopsis thaliana   PubMed: 21569135

Deposition date: 2010-05-10 Original release date: 2011-05-23

Authors: Pekarova, Blanka; Klumpler, Tomas; Triskova, Olga; Horak, Jakub; Jansen, Severine; Dopitova, Radka; Motackova, Veronika; Nejedla, Eliska; Zidek, Lukas; Marek, Jaromir; Sklenar, Vladimir; Hejatko, Jan; Janda, Lubomir

Citation: Pekarova, Blanka; Klumpler, Toma; Tiskova, Olga; Horak, Jakub; Jansen, Severine; Dopitova, Radka; Borkovcova, Petra; Papoukova, Veronika; Nejedla, Elika; Sklena, Vladimir; Marek, Jaromir; Zidek, Luka; Hejatko, Jan; Janda, Lubomir. "Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana."  Plant J. 67, 827-839 (2011).

Assembly members:
CKI1RD, polymer, 207 residues, Formula weight is not available
MG, non-polymer, 24.305 Da.

Natural source:   Common Name: thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

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

Entity Sequences (FASTA):
CKI1RD: MGSSHHHHHHSSGLVPRGSH MASTDSESETRVKSVRTGRK PIGNPEDEQETSKPSDDEFL RGKRVLVVDDNFISRKVATG KLKKMGVSEVEQCDSGKEAL RLVTEGLTQREEQGSVDKLP FDYIFMDCQMPEMDGYEATR EIRKVEKSYGVRTPIIAVSG HDPGSEEARETIQAGMDAFL DKSLNQLANVIREIESKRHL EHHHHHH

Data sets:
Data typeCount
13C chemical shifts325
15N chemical shifts161
1H chemical shifts161
General relaxation values291
chemical shift anisotropy values97
heteronuclear NOE values97
order parameters97
tensors97

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CKI1RD1
2MG2

Entities:

Entity 1, CKI1RD 207 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALASERTHRASPSERGLUSERGLUTHR
4   ARGVALLYSSERVALARGTHRGLYARGLYS
5   PROILEGLYASNPROGLUASPGLUGLNGLU
6   THRSERLYSPROSERASPASPGLUPHELEU
7   ARGGLYLYSARGVALLEUVALVALASPASP
8   ASNPHEILESERARGLYSVALALATHRGLY
9   LYSLEULYSLYSMETGLYVALSERGLUVAL
10   GLUGLNCYSASPSERGLYLYSGLUALALEU
11   ARGLEUVALTHRGLUGLYLEUTHRGLNARG
12   GLUGLUGLNGLYSERVALASPLYSLEUPRO
13   PHEASPTYRILEPHEMETASPCYSGLNMET
14   PROGLUMETASPGLYTYRGLUALATHRARG
15   GLUILEARGLYSVALGLULYSSERTYRGLY
16   VALARGTHRPROILEILEALAVALSERGLY
17   HISASPPROGLYSERGLUGLUALAARGGLU
18   THRILEGLNALAGLYMETASPALAPHELEU
19   ASPLYSSERLEUASNGLNLEUALAASNVAL
20   ILEARGGLUILEGLUSERLYSARGHISLEU
21   GLUHISHISHISHISHISHIS

Entity 2, MG - Mg - 24.305 Da.

1   MG

Samples:

sample_1: CKI1RD, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM; EDTA 1 mM; sodium azide 0.05%; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 171 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

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

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

NMR spectrometers:

  • Bruker Avance 600 MHz

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