Crystal structure of a binary complex between an engineered trypsin inhibitor and Bovine trypsin

Single mutation at P1 of a chymotrypsin inhibitor changes it to a trypsin inhibitor: X-ray structural (2.15 A) and biochemical basis

IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNT
LNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNM
FCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN

DDDLVDAEGNLVENGGTYYLLPHIWAHGGGIETAKTGNEPCPLTVVRSPNEVSKGEPIRISSQFRSLFIPRGSLVALGFA
NPPSCAASPWWTVVDSPQGPAVKLSQQKLPEKDILVFKFEKVSHSNIHVYKLLYCQHDEEDVKCDQYIGIHRDRNGNRRL
VVTEENPLELVLLKAKSETASSH

30% Jefamine, VAPOR DIFFUSION, temperature 293K

P1 mutant (Leu to Arg) Chymotrypsin Inhibitor

P1 mutant, trypsin inhibitor, bovine trypsin, complex, Calcium, Digestion, Hydrolase, Metal-binding, Protease, Secreted, Serine protease, Zymogen, Protease inhibitor, Serine protease inhibitor, Hydrolase-Hydrolase inhibitor COMPLEX

DDDLVDAEGNLVENGGTYYLLPHIWAHGGGIETAKTGNEPCPLTVVRSPNEVSKGEPIRISSQFLSLFIPRGSLVALGFA
NPPSCAASPWWTVVDSPQGPAVKLSQQKLPEKDILVFKFEKVSHSNIHVYKLLYCQHDEEDVKCDQYIGIHRDRNGNRRL
VVTEENPLELVLLKAKSETASSH