BMRB Entry 18234

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18234
MolProbity Validation Chart

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Title:
Solution structure of P1-CheY/P2 complex in bacterial chemotaxis
Deposition date:
2012-02-01
Original release date:
2012-10-22
Authors:
dahlquist, Frederick; Mo, Guoya; Zhou, Hongjun; Kamamura, Tetsuya
Citation:

Citation: Mo, Guoya; Zhou, Hongjun; Kamamura, Tetsuya; dahlquist, Frederick. "Solution structure of P1-CheY/P2 complex in bacterial chemotaxis"  Biochemistry ., .-..

Assembly members:

Assembly members:
CheA_P1P2, polymer, 225 residues, 24991.010 Da.
CheY, polymer, 128 residues, 13981.248 Da.

Natural source:

Natural source:   Common Name: Escherichia 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: pQE12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CheA_P1P2: MSMDISDFYQTFFDEADELL ADMEQHLLDLVPESPDAEQL NAIFRAAHSIKGGAGTFGFT ILQETTHLMENLLDEARRGE MQLNTDIINLFLETKDIMQE QLDAYKNSEEPDAASFEYIC NALRQLALEAKGETPSAVTR LSVVAKSEPQDEQSRSQSPR RIILSRLKAGEVDLLEEELG HLTTLTDVVKGADSLSAILP GDIAEDDITAVLCFVIEADQ ITFET
CheY: ADKELKFLVVDDFSTMRRIV RNLLKELGFNNVEEAEDGVD ALNKLQAGGYGFVISDWNMP NMDGLELLKTIRADGAMSAL PVLMVTAEAKKENIIAAAQA GASGYVVKPFTAATLEEKLN KIFEKLGM

Data sets:
Data typeCount
15N chemical shifts108
1H chemical shifts108

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CheA_P1P21
2CheY2

Entities:

Entity 1, CheA_P1P2 225 residues - 24991.010 Da.

1   METSERMETASPILESERASPPHETYRGLN
2   THRPHEPHEASPGLUALAASPGLULEULEU
3   ALAASPMETGLUGLNHISLEULEUASPLEU
4   VALPROGLUSERPROASPALAGLUGLNLEU
5   ASNALAILEPHEARGALAALAHISSERILE
6   LYSGLYGLYALAGLYTHRPHEGLYPHETHR
7   ILELEUGLNGLUTHRTHRHISLEUMETGLU
8   ASNLEULEUASPGLUALAARGARGGLYGLU
9   METGLNLEUASNTHRASPILEILEASNLEU
10   PHELEUGLUTHRLYSASPILEMETGLNGLU
11   GLNLEUASPALATYRLYSASNSERGLUGLU
12   PROASPALAALASERPHEGLUTYRILECYS
13   ASNALALEUARGGLNLEUALALEUGLUALA
14   LYSGLYGLUTHRPROSERALAVALTHRARG
15   LEUSERVALVALALALYSSERGLUPROGLN
16   ASPGLUGLNSERARGSERGLNSERPROARG
17   ARGILEILELEUSERARGLEULYSALAGLY
18   GLUVALASPLEULEUGLUGLUGLULEUGLY
19   HISLEUTHRTHRLEUTHRASPVALVALLYS
20   GLYALAASPSERLEUSERALAILELEUPRO
21   GLYASPILEALAGLUASPASPILETHRALA
22   VALLEUCYSPHEVALILEGLUALAASPGLN
23   ILETHRPHEGLUTHR

Entity 2, CheY 128 residues - 13981.248 Da.

1   ALAASPLYSGLULEULYSPHELEUVALVAL
2   ASPASPPHESERTHRMETARGARGILEVAL
3   ARGASNLEULEULYSGLULEUGLYPHEASN
4   ASNVALGLUGLUALAGLUASPGLYVALASP
5   ALALEUASNLYSLEUGLNALAGLYGLYTYR
6   GLYPHEVALILESERASPTRPASNMETPRO
7   ASNMETASPGLYLEUGLULEULEULYSTHR
8   ILEARGALAASPGLYALAMETSERALALEU
9   PROVALLEUMETVALTHRALAGLUALALYS
10   LYSGLUASNILEILEALAALAALAGLNALA
11   GLYALASERGLYTYRVALVALLYSPROPHE
12   THRALAALATHRLEUGLUGLULYSLEUASN
13   LYSILEPHEGLULYSLEUGLYMET

Samples:

sample_1: CheY, [U-15N; U-2H], 200 mM; CheA P1, [U-2H], 3000 mM; CheA P2, [U-2H], 250 mM; sodium phosphate 50 mM; DTT 5 mM; sodium azide 0.2%; H2O 92%; D2O 8%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

ANSIG3.3, Kraulis - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CQF39165 CAD05667 CAP76371 CAQ32359 CAQ98822 CAR03242
GB EIQ53621 AAA23570 AAA23577 AAA27037 AAC74952 AAG56872
REF WP_042351715 NP_288319 NP_310619 NP_416396 NP_456482 NP_460873
BMRB 2950 2951 3440 4083 4472
DBJ BAA15698 BAB36015 BAG77641 BAI25973 BAI30936
PIR AH0745
SP P0A2D5 P0A2D6 P0AE67 P0AE68 P0AE69
AlphaFold P0A2D5 P0A2D6 P0AE67 P0AE68 P0AE69

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