PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
7932578-5	1994	This heterocyclic nitrogen atom would provide a critical hydrogen-bond interaction with the histidine residue of the catalytic triad in PEP.	Histidine	92-101	prolyl endopeptidase	Homo sapiens	136-139	
22940581-5	2013	Here we determined kinetic and structural properties of POP with mutations in loop A, loop B, and in two additional flexible loops (the catalytic His loop, propeller Asp/Glu loop).	Histidine	146-149	prolyl endopeptidase	Homo sapiens	56-59	
2064618-7	1991	This residue (His-680) probably represents the active-site histidine of prolyl endopeptidase.	Histidine	14-17	prolyl endopeptidase	Homo sapiens	72-92	
2064618-7	1991	This residue (His-680) probably represents the active-site histidine of prolyl endopeptidase.	Histidine	59-68	prolyl endopeptidase	Homo sapiens	72-92