PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23764826-7	2013	The analysis of existing crystallographic data for the reactivation conformation of MetH enzyme (1K7Y (@3.0 A); 1K98 (@3.8 A) and 3IVA (@2.7 A)) indicates that the Y1139 residue and the beta-axial H2O ligand in the MetH-bound Co(II)Cbx complex are equidistant from the Co(II) ion (Y1139Co(II)=3.97 A; H2OCo(II)=3.96 A).	Carboxin	232-235	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	84-88	
23764826-7	2013	The analysis of existing crystallographic data for the reactivation conformation of MetH enzyme (1K7Y (@3.0 A); 1K98 (@3.8 A) and 3IVA (@2.7 A)) indicates that the Y1139 residue and the beta-axial H2O ligand in the MetH-bound Co(II)Cbx complex are equidistant from the Co(II) ion (Y1139Co(II)=3.97 A; H2OCo(II)=3.96 A).	Carboxin	232-235	5-methyltetrahydrofolate-homocysteine methyltransferase	Homo sapiens	215-219