BMRB Entry 27189

Title:
N,H,Ca,Cb chemical shifts and methionine sidechain chemical shifts of the isolated P1 domain of CheA from Escherichia Coli
Deposition date:
2017-07-21
Original release date:
2017-12-14
Authors:
Minato, Yuichi; Ueda, Takumi; Machiyama, Asako; Iwai, Hideo; Shimada, Ichio
Citation:

Citation: Minato, Yuichi; Ueda, Takumi; Machiyama, Asako; Iwai, Hideo; Shimada, Ichio. "Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR"  Sci. Rep. 7, 16462-16462 (2017).
PubMed: 29184123

Assembly members:

Assembly members:
P1_domain_of_CheA, polymer, 132 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET43a

Data sets:
Data typeCount
13C chemical shifts254
15N chemical shifts128
1H chemical shifts168

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1P1 domain of CheA1

Entities:

Entity 1, P1 domain of CheA 132 residues - Formula weight is not available

1   METASPILESERASPPHETYRGLNTHRPHE
2   PHEASPGLUALAASPGLULEULEUALAASP
3   METGLUGLNHISLEULEUVALLEUGLNPRO
4   GLUALAPROASPALAGLUGLNLEUASNALA
5   ILEPHEARGALAALAHISSERILELYSGLY
6   GLYALAGLYTHRPHEGLYPHESERVALLEU
7   GLNGLUTHRTHRHISLEUMETGLUASNLEU
8   LEUASPGLUALAARGARGGLYGLUMETGLN
9   LEUASNTHRASPILEILEASNLEUPHELEU
10   GLUTHRLYSASPILEMETGLNGLUGLNLEU
11   ASPALATYRLYSGLNSERGLNGLUPROASP
12   ALAALASERPHEASPTYRILECYSGLNALA
13   LEUARGGLNLEUALALEUGLUALALYSGLY
14   GLUTHR

Samples:

sample_1: P1 domain of CheA, [U-13C; U-15N], 0.78 mM; sodium phosphate 20 mM; DTT 2 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 7.1; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

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