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
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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
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STRONG residues
7: F;
21: R;
23: L;
24: L;
25: K;
27: L;
29: F;
52: F;
55: S;
120: N;
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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
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MEDIUM residues
8: L;
11: D;
26: E;
35: A;
41: A;
53: V;
70: T;
84: M;
86: T;
118: K;
119: L;
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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
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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;
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