Entry STF0045
Protein A B-domain
Protein information
Name of the protein: | Immunoglobulin G-binding protein A |
Organism: | Staphylococcus aureus |
Number of residues: | 58 |
Related UniProt entry: | P38507 (Fragment: 212 - 270) |
Related PDB entry: | 1BDD |
Visualize the data
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Experiment sets
STRONG
Method: Native exchange NMR
Conditions: pH 7.0; 20.0 Celsius; Probes: 28
Related publication:
PMID 9232646
Experiment details: "Equilibrium hydrogen exchange experiments were performed by dissolving lyophilized protein directly in potassium phosphate buffer (100 mM, pH* 7.0) in D2O containing various concentrations (0 - 3.0 M) of GdmC1. The GdmCl solution in D2O was prepared by addition of a measured volume of D2O to a weighed sample of deuterated GdmCl. Exchange rates were measured by recording 1H-15N HSQC spectra as a function of time without removing the sample from the magnet."
Protection threshold: ΔG(op) > 6 kcal/mol
Sequence:
TADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKA
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STRONG residues
28: R;
35: L;
49: A;
50: K;
51: K;
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EARLY
Method: Pulse labeling HDX NMR
Conditions: pH 5.0; 5.0 Celsius; Probes: 20
Related publication:
PMID 9232646
Experiment details: "Pulsed H/D exchange measurements were performed at 5 °C. The B-domain of protein A at a concentration of about 3 mg/mL was first unfolded in 6.0 M GdmC1 at pH 5.0 using 10 mM sodium acetate buffer in H2O. Folding was initiated by six times dilution with D2O buffer at pH* 5.0 and was allowed to continue for 6 ms before the labeling pulse was applied for 10 ms. The pulse buffer contained 0.5 M Tris adjusted to pH* 11.5 using KOD. This leads to a pulse of pH* 10.5 after mixing with the folding buffer. The exchange was quenched by D2O buffer containing 0.5 M Tris and 100 mM acetic acid at pH* 0.5. The final pH* of the solution was 4.8 after the quench."
Protection threshold: proton occupancy > 0.7 at 6 ms refolding time
Sequence:
TADNKFNKEQQNAFYEILHLPNLNEEQRNGFIQSLKDDPSQSANLLAEAKKLNDAQAPKA
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EARLY residues
14: F;
15: Y;
16: E;
17: I;
18: L;
20: L;
22: N;
23: L;
28: R;
29: N;
31: F;
34: S;
35: L;
36: K;
47: A;
48: E;
49: A;
50: K;
51: K;
52: L;
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