PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9148758-7	1997	It is concluded that Z-Pro-prolinal, a putative transition-state analogue for prolyl oligopeptidase, forms a tetrahedral complex with the enzyme at its catalytic serine, rather than at a neighbouring cysteine that was found to be highly reactive according to chemical modification studies.	Cysteine	200-208	prolyl endopeptidase	Homo sapiens	78-99	
16849325-9	2006	Molecular modeling of hPreP based on the crystal structure at 2.1 A resolution of AtPreP allowed us to identify Cys(90) and Cys(527) that form disulfide bridges under oxidized conditions and might be involved in redox regulation of the enzyme.	Cysteine	112-115	prolyl endopeptidase	Homo sapiens	22-27	
16849325-9	2006	Molecular modeling of hPreP based on the crystal structure at 2.1 A resolution of AtPreP allowed us to identify Cys(90) and Cys(527) that form disulfide bridges under oxidized conditions and might be involved in redox regulation of the enzyme.	Cysteine	124-127	prolyl endopeptidase	Homo sapiens	22-27	
10747969-4	2000	This assumption was tested with the Cys-255 --> Thr, Cys-255 --> Ala, and Cys-255 --> Ser variants of prolyl oligopeptidase.	Cysteine	36-39	prolyl endopeptidase	Homo sapiens	111-132	
16700513-0	2006	Prolyl endopeptidase cleaves the apoptosis rescue peptide humanin and exhibits an unknown post-cysteine cleavage specificity.	Cysteine	95-103	prolyl endopeptidase	Homo sapiens	0-20