1H, 13C and 15N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus
- 1 January 1994
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 4 (1) , 123-128
- https://doi.org/10.1007/bf00178340
Abstract
The 1H, 13C and 15N NMR resonances of the backbone of serine protease PB92 have been assigned. This 269-residue protein is one of the largest monomeric proteins assigned so far. The amount and quality of information available suggest that even larger proteins could be assigned with present methods. Measured chemical shifts show excellent agreement with the secondary structure.Keywords
This publication has 12 references indexed in Scilit:
- Prospects for NMR of large proteinsJournal of Biomolecular NMR, 1993
- Complete assignments of magnetic resonances of ribonuclease H from Escherichia coli by double- and triple-resonance 2D and 3D NMR spectroscopiesBiochemistry, 1993
- 1H, 13C, and 15N assignments and secondary structure of the FK506 binding protein when bound to ascomycinBiopolymers, 1993
- Proton, carbon-13, and nitrogen-15 NMR backbone assignments and secondary structure of human interferon-.gamma.Biochemistry, 1992
- Protein engineering of the high-alkaline serine protease PB92 from Bacillus alcalophilus: functional and structural consequences of mutation at the S4 substrate binding pocketProtein Engineering, Design and Selection, 1992
- Crystal structure of the high-alkaline serine protease PB92 from Bacillus alcalophilusProtein Engineering, Design and Selection, 1992
- A new 3D HN(CA)HA experiment for obtaining fingerprint HN-Hα cross peaks in15N- and13C-labeled proteinsJournal of Biomolecular NMR, 1992
- Relationship between nuclear magnetic resonance chemical shift and protein secondary structureJournal of Molecular Biology, 1991
- Protein engineering. The design, synthesis and characterization of factitious proteinsBiochemical Journal, 1987
- Phosphorus-31 NMR and mass spectrometry of atropinesterase and some serine proteases phosphorylated with a transition-state analogBiochemistry, 1985