BMRB Entry 26898

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26898

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Title:
Conformational dynamics as a key factor of activation of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana
Deposition date:
2016-09-14
Original release date:
2021-07-26
Authors:
Otrusinov, Olga; Demo, Gabriel; Padrta, Petr; Jasenakova, Zuzana; Pekarova, Blanka; Gelova, Zuzana; Szmitkowska, Agnieszka; Kaderavek, Pavel; Jansen, Severine; Zachrdla, Milan; Klumler, Tomas; Marek, Jaromir; Hritz, Jozef; Janda, Lubomir; Iwai, Hideo; Wimmerova, Michaela; Hejatko, Jan; Zidek, Lukas
Citation:

Citation: Otrusinova, Olga; Demo, Gabriel; Padrta, Petr; Jasenakova, Zuzana; Pekarova, Blanka; Gelova, Zuzana; Szmitkowska, Agnieszka; Kaderavek, Pavel; Jansen, Severine; Zachrdla, Milan; Klumpler, Tomas; Marek, Jaromir; Hritz, Jozef; Janda, Lubomir; Iwai, Hideo; Wimmerova, Michaela; Hejatko, Jan; Zidek, Lukas. "Conformational dynamics are a key factor in signaling mediated by the receiver domain of a sensor histidine kinase from Arabidopsis thaliana"  J. Biol. Chem. 292, 17525-17540 (2017).
PubMed: 28860196

Assembly members:

Assembly members:
CKI1RD, polymer, 207 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a+

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
15N chemical shifts141
1H chemical shifts140

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CKI1RD1

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   PROGLUMETGLUASNTYRGLUALATHRARG
15   GLUILEARGLYSVALGLULYSSERTYRGLY
16   VALARGTHRPROILEILEALAVALSERGLY
17   HISASPPROGLYSERGLUGLUALAARGGLU
18   THRILEGLNALAGLYMETASPALAPHELEU
19   ASPLYSSERLEUASNGLNLEUALAASNVAL
20   ILEARGGLUILEGLUSERLYSARGHISLEU
21   GLUHISHISHISHISHISHIS

Samples:

sample_1: CKI1RD 0.3 mM; TRIS 20 mM; sodium chloride 150 mM; EDTA 1 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 170 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_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 950 MHz

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