Entry STF0021
Bacteriophage T4 lysozyme
Protein information
Name of the protein: | Lysozyme |
Organism: | Enterobacteria phage T4 |
Number of residues: | 164 |
Related UniProt entry: | D9IEF7 (Fragment: 1 - 164) |
Related PDB entry: | 2LZM |
Visualize the data
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Experiment sets
EARLY
Method: Dead time pulse labeling HDX NMR
Conditions: pH 10.2; 25.0 Celsius; Probes: 60
Related publication:
PMID 17097105
Experiment details: "Dead-time pulse-labeling experiment, in which the unfolded protein sample in D2O and 8.5 M D-urea was mixed with a H2O solution at pH 10.2 by a ratio of 1:9. After 13 ms, the sample was quenched at pH 3.0. At pH 10.2 and 25 °C, unprotected amide deuterons can exchange with solvent protons in less than 1 ms."
Protection threshold: proton occupancy < 0.6
Sequence:
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL
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EARLY residues
7: L;
71: V;
79: L;
98: A;
102: M;
103: V;
104: F;
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INTERMEDIATE
Method: Dead time pulse labeling HDX NMR
Conditions: pH 10.2; 25.0 Celsius; Probes: 60
Related publication:
PMID 17097105
Experiment details: "Dead-time pulse-labeling experiment, in which the unfolded protein sample in D2O and 8.5 M D-urea was mixed with a H2O solution at pH 10.2 by a ratio of 1:9. After 13 ms, the sample was quenched at pH 3.0. At pH 10.2 and 25 °C, unprotected amide deuterons can exchange with solvent protons in less than 1 ms."
Protection threshold: 0.6 < proton occupancy < 0.8
Sequence:
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL
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INTERMEDIATE residues
4: F;
64: E;
74: A;
78: I;
81: N;
84: L;
97: A;
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STRONG
Method: Native exchange NMR
Conditions: pH 6.0; 25.0 Celsius; Probes: 114
Related publication:
PMID 10542101
Experiment details: "The exchange of 114 of the 164 backbone amide protons in T4 lysozyme was monitored as a function of denaturant concentration (eleven samples between 0 M and 2 M GdmCl). Exchange was initiated by spinning the samples through a Quick-sep spin column packed with G-25 resin pre-equilibrated in deuterated buffer (50 mM sodium phosphate, pD 6.0, 0.1 M KCl) with varying amounts of per-deuterated GdmCl. All of these denaturant concentrations are below the folding transition measured by global probes. Exchange was measured by two-dimensional 1H-15N HSQC spectra taken over a period of hours to months."
Protection threshold: ΔG(op)(kcal/mol) > 15
Sequence:
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL
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STRONG residues
5: E;
7: L;
10: D;
66: L;
71: V;
72: D;
73: A;
74: A;
76: R;
79: L;
85: K;
96: R;
97: A;
98: A;
99: L;
100: I;
101: N;
102: M;
103: V;
104: F;
105: Q;
106: M;
121: L;
123: Q;
147: K;
149: V;
153: F;
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MEDIUM
Method: Native exchange NMR
Conditions: pH 6.0; 25.0 Celsius; Probes: 114
Related publication:
PMID 10542101
Experiment details: "The exchange of 114 of the 164 backbone amide protons in T4 lysozyme was monitored as a function of denaturant concentration (eleven samples between 0 M and 2 M GdmCl). Exchange was initiated by spinning the samples through a Quick-sep spin column packed with G-25 resin pre-equilibrated in deuterated buffer (50 mM sodium phosphate, pD 6.0, 0.1 M KCl) with varying amounts of per-deuterated GdmCl. All of these denaturant concentrations are below the folding transition measured by global probes. Exchange was measured by two-dimensional 1H-15N HSQC spectra taken over a period of hours to months."
Protection threshold: 13 < ΔG(op)(kcal/mol) < 15
Sequence:
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL
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MEDIUM residues
6: M;
8: R;
9: I;
11: E;
75: V;
80: R;
84: L;
88: Y;
91: L;
112: A;
122: Q;
131: V;
150: I;
151: T;
152: T;
154: R;
156: G;
157: T;
161: Y;
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WEAK
Method: Native exchange NMR
Conditions: pH 6.0; 25.0 Celsius; Probes: 114
Related publication:
PMID 10542101
Experiment details: "The exchange of 114 of the 164 backbone amide protons in T4 lysozyme was monitored as a function of denaturant concentration (eleven samples between 0 M and 2 M GdmCl). Exchange was initiated by spinning the samples through a Quick-sep spin column packed with G-25 resin pre-equilibrated in deuterated buffer (50 mM sodium phosphate, pD 6.0, 0.1 M KCl) with varying amounts of per-deuterated GdmCl. All of these denaturant concentrations are below the folding transition measured by global probes. Exchange was measured by two-dimensional 1H-15N HSQC spectra taken over a period of hours to months."
Protection threshold: 11 < ΔG(op)(kcal/mol) < 13
Sequence:
MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL
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WEAK residues
4: F;
14: R;
67: F;
70: D;
129: A;
130: A;
155: T;
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