PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16849325-6	2006	We have cloned, overexpressed, and purified recombinant hPreP and its mutant with catalytic base Glu(78) in the inverted zinc-binding motif replaced by Gln.	Glutamic Acid	97-100	prolyl endopeptidase	Homo sapiens	56-61	
19290936-1	2009	The proline-, glutamic acid-, serine- and threonine-rich (PEST) family of protein tyrosine phosphatases (PTPs) includes proline-enriched phosphatase (PEP)/lymphoid tyrosine phosphatase (LYP), PTP-PEST, and PTP-hematopoietic stem cell fraction (HSCF).	Glutamic Acid	14-27	prolyl endopeptidase	Homo sapiens	120-148	
19290936-1	2009	The proline-, glutamic acid-, serine- and threonine-rich (PEST) family of protein tyrosine phosphatases (PTPs) includes proline-enriched phosphatase (PEP)/lymphoid tyrosine phosphatase (LYP), PTP-PEST, and PTP-hematopoietic stem cell fraction (HSCF).	Glutamic Acid	14-27	prolyl endopeptidase	Homo sapiens	150-153	
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).	Glutamic Acid	170-173	prolyl endopeptidase	Homo sapiens	56-59	
14514675-1	2003	The positive electrostatic environment of the active site of prolyl oligopeptidase was investigated by using substrates with glutamic acid at positions P2, P3, P4, and P5, respectively.	Glutamic Acid	125-138	prolyl endopeptidase	Homo sapiens	61-82	
11685249-2	2001	The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain.	Glutamic Acid	95-98	prolyl endopeptidase	Homo sapiens	129-132	
9128099-5	1997	The S2 binding subsite of POP can accommodate amino acid residues with a bulky side group, while it prefers a positively charged group (free Lys) instead of a negatively charged one (free Glu).	Glutamic Acid	188-191	prolyl endopeptidase	Homo sapiens	26-29