BMRB Entry 2285
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR2285
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Citation: Bachovchin, William; Kaiser, John; Richards, John; Roberts, John. "Catalytic mechanism of serine proteases: Reexamination of the pH dependence of
the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic
protease" Proc. Natl. Acad. Sci. U.S.A. 78, 7323-7326 (1981).
Assembly members:
alpha-lytic proteinase, polymer, 36 residues, Formula weight is not available
Natural source: Common Name: Myxobacter 495 Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: Lysobacter enzymogenes
Experimental source: Production method: not available
Entity Sequences (FASTA):
alpha-lytic proteinase: XXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 1 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | alpha-lytic proteinase | 1 |
Entities:
Entity 1, alpha-lytic proteinase 36 residues - Formula weight is not available
| 1 | X | X | X | X | X | X | X | X | X | X | ||||
| 2 | X | X | X | X | X | X | X | X | X | X | ||||
| 3 | X | X | X | X | X | X | X | X | X | X | ||||
| 4 | X | X | X | X | X | HIS |
Samples:
sample_one:
sample_condition_set_one: pH: 4.7 na; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|
Software:
No software information available
NMR spectrometers:
- unknown unknown 0 MHz