PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1397329-1	1992	In prolyl oligopeptidase and its homologues, which constitute a new serine protease family, the order of the catalytic Ser and His residues in the amino acid sequence is the reverse of what is found in the trypsin and subtilisin families.	Serine	119-122	prolyl endopeptidase	Homo sapiens	3-24	
1397329-3	1992	Recent determination of the three-dimensional structures of pancreatic and microbial lipases has shown that the order of their catalytic residues is Ser, Asp, His, and this fits the order Ser, His of prolyl oligopeptidase.	Serine	149-152	prolyl endopeptidase	Homo sapiens	200-221	
1397329-3	1992	Recent determination of the three-dimensional structures of pancreatic and microbial lipases has shown that the order of their catalytic residues is Ser, Asp, His, and this fits the order Ser, His of prolyl oligopeptidase.	Aspartic Acid	154-157	prolyl endopeptidase	Homo sapiens	200-221	
1397329-3	1992	Recent determination of the three-dimensional structures of pancreatic and microbial lipases has shown that the order of their catalytic residues is Ser, Asp, His, and this fits the order Ser, His of prolyl oligopeptidase.	Serine	188-191	prolyl endopeptidase	Homo sapiens	200-221	
1397329-3	1992	Recent determination of the three-dimensional structures of pancreatic and microbial lipases has shown that the order of their catalytic residues is Ser, Asp, His, and this fits the order Ser, His of prolyl oligopeptidase.	Histidine	193-196	prolyl endopeptidase	Homo sapiens	200-221	
1397329-5	1992	This comparison identifies the catalytic Asp residue in the prolyl oligopeptidase family.	Aspartic Acid	41-44	prolyl endopeptidase	Homo sapiens	60-81