Entry STF0050
Chemotactic protein Chey
Protein information
| Name of the protein: | Chemotaxis protein CheY |
| Organism: | Escherichia coli (strain K12) |
| Number of residues: | 128 |
| Related UniProt entry: | P0AE67 (Fragment: 2 - 129) |
| Related PDB entry: | 3CHY |
Visualize the data
Click here or on the image on the right to visualize the residues using JSmol. Warning: JSmol is known to load slowly on certain browsers, depending on the size of the macromolecule. The applet is optimized for Chrome, other browsers have limited support.
Experiment sets
STRONG
Method: Native exchange NMR
Conditions: pH 6.0; 25.0 Celsius; Probes: 38
Related publication:
PMID 9268672
Experiment details: "The H/D exchange of the peptide N1H groups in both proteins was monitored by recording successive magnitude COSY or HSQC spectra, following the transfer of the protein from H2O to D2O. For the wild-type CheY, by monitoring the H-ex with quickly acquired HSQC spectra on a uniformly 15N-labelled protein sample, it was possible to work at pH 6 despite the faster intrinsic exchange."
Protection threshold: log(P) > 4.3
Sequence:
ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM
CLICK TO DOWNLOAD SEQUENCE IN FASTA
STRONG residues
7: F;
21: R;
23: L;
24: L;
25: K;
27: L;
29: F;
52: F;
55: S;
120: N;
CLICK TO DOWNLOAD LIST OF RESIDUES
MEDIUM
Method: Native exchange NMR
Conditions: pH 6.0; 25.0 Celsius; Probes: 38
Related publication:
PMID 9268672
Experiment details: "The H/D exchange of the peptide N1H groups in both proteins was monitored by recording successive magnitude COSY or HSQC spectra, following the transfer of the protein from H2O to D2O. For the wild-type CheY, by monitoring the H-ex with quickly acquired HSQC spectra on a uniformly 15N-labelled protein sample, it was possible to work at pH 6 despite the faster intrinsic exchange."
Protection threshold: 4.0 < log(P) < 4.3
Sequence:
ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM
CLICK TO DOWNLOAD SEQUENCE IN FASTA
MEDIUM residues
8: L;
11: D;
26: E;
35: A;
41: A;
53: V;
70: T;
84: M;
86: T;
118: K;
119: L;
CLICK TO DOWNLOAD LIST OF RESIDUES
WEAK
Method: Native exchange NMR
Conditions: pH 6.0; 25.0 Celsius; Probes: 38
Related publication:
PMID 9268672
Experiment details: "The H/D exchange of the peptide N1H groups in both proteins was monitored by recording successive magnitude COSY or HSQC spectra, following the transfer of the protein from H2O to D2O. For the wild-type CheY, by monitoring the H-ex with quickly acquired HSQC spectra on a uniformly 15N-labelled protein sample, it was possible to work at pH 6 despite the faster intrinsic exchange."
Protection threshold: 3.3 < log(P) < 4.0
Sequence:
ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM
CLICK TO DOWNLOAD SEQUENCE IN FASTA
WEAK residues
9: V;
10: V;
33: E;
37: D;
42: L;
54: I;
71: I;
82: V;
83: L;
85: V;
106: V;
108: K;
115: L;
116: E;
117: E;
122: I;
123: F;
CLICK TO DOWNLOAD LIST OF RESIDUES