PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28577910-3	2017	Over the past decade, a variety of biochemical, spectroscopic, structural and mechanistic studies of IDI-2 have provided mounting evidence that the flavin coenzyme of IDI-2 acts in a most unusual manner - as an acid/base catalyst to mediate a 1,3-proton addition/elimination reaction.	4,6-dinitro-o-cresol	148-154	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	101-106	
28577910-3	2017	Over the past decade, a variety of biochemical, spectroscopic, structural and mechanistic studies of IDI-2 have provided mounting evidence that the flavin coenzyme of IDI-2 acts in a most unusual manner - as an acid/base catalyst to mediate a 1,3-proton addition/elimination reaction.	4,6-dinitro-o-cresol	148-154	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	167-172	
28577910-4	2017	While not entirely without precedent, IDI-2 is by far the most extensively studied flavoenzyme that employs flavin-mediated acid/base catalysis.	4,6-dinitro-o-cresol	108-114	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	38-43	
28577910-5	2017	Thus, IDI-2 serves as an important mechanistic model for understanding this often overlooked, but potentially widespread reactivity of flavin coenzymes.	4,6-dinitro-o-cresol	135-141	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	6-11