3.4.23.4	-	36871, 36882, 36894	
3.4.23.4	doubly and singly glycosylated variants of chymosin, vapor diffusion method, using 2 M ammonium sulfate, 100 mM bis-Tris buffer in the pH range 5.1-6.5	731064	
3.4.23.4	loop exchange mutant	36892	
3.4.23.4	modeling of chymosin in complex with residues 97-112 of bovine kappa-casein. Substrate binds in an extended conformation with charged residues on either side of the scissile bond playing an important role in stabilizing the binding pose. Substrate residues Lys111 and Lys112 bind to the N-terminal domain of chymosin displacing a conserved water molecule. A cluster of histidine and proline residues, His98-Pro99-His100-Pro101-His102, in kappa-casein binds to the C-terminal domain of the protein, where neighboring conserved arginine residue Arg97 is important for stabilizing the binding pose. The catalytic site including the catalytic water molecule is stable in the starting conformation of the general acid/base catalytic mechanism for 18 ns of molecular dynamics simulations	707523	
3.4.23.4	point mutants	36880, 36891	
3.4.23.4	prochymosin mutant	36890	
3.4.23.4	unglycosylated chymosin, vapor diffusion method, using 100 mM NaH2PO4 pH 5.5, 1.5 M NaCl	731064