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
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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: Mo, Guoya; Zhou, Hongjun; Kamamura, Tetsuya; dahlquist, Frederick. "Solution structure of P1-CheY/P2 complex in bacterial chemotaxis" Biochemistry ., .-..
Assembly members:
CheA_P1P2, polymer, 225 residues, 24991.010 Da.
CheY, polymer, 128 residues, 13981.248 Da.
Natural source: Common Name: Escherichia coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
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
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 108 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CheA_P1P2 | 1 |
| 2 | CheY | 2 |
Entities:
Entity 1, CheA_P1P2 225 residues - 24991.010 Da.
| 1 | MET | SER | MET | ASP | ILE | SER | ASP | PHE | TYR | GLN | ||||
| 2 | THR | PHE | PHE | ASP | GLU | ALA | ASP | GLU | LEU | LEU | ||||
| 3 | ALA | ASP | MET | GLU | GLN | HIS | LEU | LEU | ASP | LEU | ||||
| 4 | VAL | PRO | GLU | SER | PRO | ASP | ALA | GLU | GLN | LEU | ||||
| 5 | ASN | ALA | ILE | PHE | ARG | ALA | ALA | HIS | SER | ILE | ||||
| 6 | LYS | GLY | GLY | ALA | GLY | THR | PHE | GLY | PHE | THR | ||||
| 7 | ILE | LEU | GLN | GLU | THR | THR | HIS | LEU | MET | GLU | ||||
| 8 | ASN | LEU | LEU | ASP | GLU | ALA | ARG | ARG | GLY | GLU | ||||
| 9 | MET | GLN | LEU | ASN | THR | ASP | ILE | ILE | ASN | LEU | ||||
| 10 | PHE | LEU | GLU | THR | LYS | ASP | ILE | MET | GLN | GLU | ||||
| 11 | GLN | LEU | ASP | ALA | TYR | LYS | ASN | SER | GLU | GLU | ||||
| 12 | PRO | ASP | ALA | ALA | SER | PHE | GLU | TYR | ILE | CYS | ||||
| 13 | ASN | ALA | LEU | ARG | GLN | LEU | ALA | LEU | GLU | ALA | ||||
| 14 | LYS | GLY | GLU | THR | PRO | SER | ALA | VAL | THR | ARG | ||||
| 15 | LEU | SER | VAL | VAL | ALA | LYS | SER | GLU | PRO | GLN | ||||
| 16 | ASP | GLU | GLN | SER | ARG | SER | GLN | SER | PRO | ARG | ||||
| 17 | ARG | ILE | ILE | LEU | SER | ARG | LEU | LYS | ALA | GLY | ||||
| 18 | GLU | VAL | ASP | LEU | LEU | GLU | GLU | GLU | LEU | GLY | ||||
| 19 | HIS | LEU | THR | THR | LEU | THR | ASP | VAL | VAL | LYS | ||||
| 20 | GLY | ALA | ASP | SER | LEU | SER | ALA | ILE | LEU | PRO | ||||
| 21 | GLY | ASP | ILE | ALA | GLU | ASP | ASP | ILE | THR | ALA | ||||
| 22 | VAL | LEU | CYS | PHE | VAL | ILE | GLU | ALA | ASP | GLN | ||||
| 23 | ILE | THR | PHE | GLU | THR |
Entity 2, CheY 128 residues - 13981.248 Da.
| 1 | ALA | ASP | LYS | GLU | LEU | LYS | PHE | LEU | VAL | VAL | ||||
| 2 | ASP | ASP | PHE | SER | THR | MET | ARG | ARG | ILE | VAL | ||||
| 3 | ARG | ASN | LEU | LEU | LYS | GLU | LEU | GLY | PHE | ASN | ||||
| 4 | ASN | VAL | GLU | GLU | ALA | GLU | ASP | GLY | VAL | ASP | ||||
| 5 | ALA | LEU | ASN | LYS | LEU | GLN | ALA | GLY | GLY | TYR | ||||
| 6 | GLY | PHE | VAL | ILE | SER | ASP | TRP | ASN | MET | PRO | ||||
| 7 | ASN | MET | ASP | GLY | LEU | GLU | LEU | LEU | LYS | THR | ||||
| 8 | ILE | ARG | ALA | ASP | GLY | ALA | MET | SER | ALA | LEU | ||||
| 9 | PRO | VAL | LEU | MET | VAL | THR | ALA | GLU | ALA | LYS | ||||
| 10 | LYS | GLU | ASN | ILE | ILE | ALA | ALA | ALA | GLN | ALA | ||||
| 11 | GLY | ALA | SER | GLY | TYR | VAL | VAL | LYS | PRO | PHE | ||||
| 12 | THR | ALA | ALA | THR | LEU | GLU | GLU | LYS | LEU | ASN | ||||
| 13 | LYS | ILE | PHE | GLU | LYS | LEU | GLY | MET |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_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 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts