Start2Fold

The database of hydrogen/deuterium exchange data on protein folding and stability

Entry STF0044

B1 immunoglobulin-binding domain of peptostreptococcal protein L

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Protein information

Name of the protein: Protein LG
Organism: Finegoldia magna (Peptostreptococcus magnus)
Number of residues: 62
Related UniProt entry:   Q53291 (Fragment: 24 - 101)
Related PDB entry:   2PTL

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Experiment sets

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STRONG

Method: Native exchange NMR

Conditions: pH 11.0; 60.0 Celsius; Probes: 33

Related publication:
 PMID 8762137

Experiment details: "4 mg/ml 15N-labeled protein L in H2O, and D2O adjusted to the desired pH with saturated ammonia were preequilibrated at the desired temperature. H-D exchange was initiated by manually injecting protein L in H2O into an Amicon concentrator containing 10 volumes of D2O with constant stirring, with a mixing dead time less than 2 s under these conditions. The exchange reaction was allowed to proceed for a variable length of time (4 s, 7 s, 10 s, and 10 min). At the end of the exchange period, ice cold D2O at pH 3.0 (adjusted by formic acid) was added directly into the exchange mixture at a 4:1 volume ratio to quench further exchange. The final pH of the mixture was 3.2."

Protection threshold: exchange rates close to 0.06 s(-1)

Sequence: ENKEETPETPETDSEEEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEYTVDVADKGYTLNIKFAG
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STRONG residues

20: I; 22: A; 24: L; 25: I; 36: F; 47: A; 48: Y; 49: A; 50: Y; 51: A; 52: D; 72: L; 74: I; 75: K;
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EARLY

Method: Dead time pulse labeling HDX NMR

Conditions: pH 8.5-10.0; 40.0 Celsius; Probes: 24

Related publication:
 PMID 9377710

Experiment details: "Deuterated denatured protein was rapidly diluted into H2O buffer lacking denaturant with pH 8.5, 9.0 or 10.0. After 3.5 ms, proton exchange was quenched by addition of low pH buffer. Protection factors were estimated from the fractional proton occupancy at each pH."

Protection threshold: P > 1.4

Sequence: ENKEETPETPETDSEEEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEYTVDVADKGYTLNIKFAG
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EARLY residues

22: A; 24: L; 34: A; 45: S; 47: A; 48: Y; 49: A; 50: Y; 51: A; 61: Y; 66: A; 74: I;
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