PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25411887-3	2014	Here, we describe crystallographic analyses of the mechanism of inhibition of the clinically relevant VIM-2 MBL by a rhodanine, which reveal that the rhodanine ring undergoes hydrolysis to give a thioenolate.	thioenolate	196-207	mannose-binding lectin family member 3, pseudogene	Homo sapiens	108-111	
25411887-5	2014	Crystallization of VIM-2 in the presence of the intact rhodanine led to observation of a ternary complex of MBL, a thioenolate fragment and rhodanine.	thioenolate	115-126	mannose-binding lectin family member 3, pseudogene	Homo sapiens	108-111	
25411887-6	2014	The crystallographic observations are supported by kinetic and biophysical studies, including (19)F NMR analyses, which reveal the rhodanine-derived thioenolate to be a potent broad-spectrum MBL inhibitor and a lead structure for the development of new types of clinically useful MBL inhibitors.	thioenolate	149-160	mannose-binding lectin family member 3, pseudogene	Homo sapiens	191-194	
25411887-6	2014	The crystallographic observations are supported by kinetic and biophysical studies, including (19)F NMR analyses, which reveal the rhodanine-derived thioenolate to be a potent broad-spectrum MBL inhibitor and a lead structure for the development of new types of clinically useful MBL inhibitors.	thioenolate	149-160	mannose-binding lectin family member 3, pseudogene	Homo sapiens	280-283