| 6 | CRYSTAL STRUCTURE OF THE COMPLEX OF MUNG BEAN TRYPSIN INHIBITOR LYSINE ACTIVE FRAGMENT WITH BOVINE TRYPSIN AT 1.8 A RESOLUTION显示文摘The structure of the complex of mung bean trypsin inhibitor lysineactive fragment with bovine trypsin has been determined at a resolution of1.8 A by A-ray crystallographic analysis and the complex model refined byrestrained least-squares minimization with the data between 10 and 1.8resolution.The current conventional R factor is 17.3%,and the model con-tains 1648 protein atoms,219 inhibitor atoms and 126 water molecules.Themost prominent feature of the inhibitor fragment is that it does not containany alpha-helices.Most of the chain fold in an irregular fashion.Theseven residues of the binding segment of the inhibitor lysine active frag-ment are in specific contact with bovine trypsin.The binding interactionand geometry around the reactive site are similar to that observed in otherstudies of trypsin-inhibitor complexes. | You Qi TANG Gen Pei LI Zhong Guo CHEN Jie ZENG(Institute of Physical Chemistry,Peking University,Beijing 100871)Tien Chin TSAO Guang Da LIN Rong Guang ZHANG Zheng Wu CHI(Institute of Biochemistry,Academic Sinica,Shanghai 200031) | 1990 | Chinese Chemical Letters1990，1，1： | 0 |
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