CRYSTALLOGRAPHIC REFINEMENT OF JAPANESE QUAIL OVOMUCOID, A KAZAL-TYPE INHIBITOR, AND MODEL BUILDING STUDIES OF COMPLEXES WITH SERINE PROTEASES
RESIDUE 12 OF EACH CHAIN IS A CIS-PROLINE.
The Geometry of the Reactive Site and of the Peptide Groups in Trypsin, Trypsinogen and its Complexes with Inhibitors
Crystallization,Crystal Structure Analysis and Molecular Model of the Third Domain of Japanese Quail Ovomucoid,A Kazal Type Inhibitor
THE MATERIAL USED IS POLYMORPHIC WITH 20 PER CENT GLY 32 AND 80 PER CENT SER 32. IT IS PREMATURE AT THE PRESENT STAGE OF THE ANALYSIS TO DRAW CONCLUSIONS ABOUT AN ORDERED ARRANGEMENT OF THE VARIANTS IN THE CRYSTAL. THE MAJOR POLYMORPH HAS BEEN ASSIGNED TO THE FOUR DOMAINS IN THIS ENTRY.
AN OCCUPANCY OF 0.0 INDICATES THAT NO SIGNIFICANT ELECTRON DENSITY WAS FOUND IN THE FINAL FOURIER MAP.
THE MTRIX RECORDS BELOW DESCRIBE THE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE INDIVIDUAL DOMAINS IN THIS ENTRY. MTRIX 1 RELATES CHAIN A TO CHAIN B BY A PSEUDO-FOUR-FOLD ROTATION. MTRIX 2 RELATES CHAIN C TO CHAIN D BY A PSEUDO-TWO-FOLD ROTATION. SEE REFERENCE 2 ABOVE FOR A COMPLETE DESCRIPTION OF THESE SYMMETRY AXES. THESE MATRICES WERE OBTAINED BY COMPARING THE BACKBONE AND CB ATOMS OF THE MOLECULES. (THE FIRST SIX RESIDUES WERE EXCLUDED FROM THIS CALCULATION.)
VEVDCSRFPNTTNEEGKDEVVCPDELRLICGTDGVTYNHECMLCFYNKEYGTNISKEQDGECGETVPMDCSRYPNTTSED GKVTILCTKDFSFVCGTDGVTYDNECMLCAHNVVQGTSVGKKHDGECRKELAAVSVDCSEYPKPACPKDYRPVCGSDNKT YSNKCNFCNAVVESNGTLTLNHFGKC