PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26375627-1	2016	Through experimental and theoretical approaches, it has been shown that bovine beta-lactoglobulin (betalg) uses its hydrophobic cavity or calyx as the primary binding site for hydrophobic molecules, whereas the existence of a second ligand binding site at the dimeric interface has only been structurally identified for vitamin D3 (VD3).	Cholecalciferol	320-330	beta-lactoglobulin	Bos taurus	79-97	
18004750-0	2008	Crystal structure of a secondary vitamin D3 binding site of milk beta-lactoglobulin.	Cholecalciferol	33-43	beta-lactoglobulin	Bos taurus	65-83	
18004750-13	2008	Atomic coordinates for the crystal structure of beta-LG-vitamin D(3) complex described in this work have been deposited in the PDB (access code 2GJ5).	Cholecalciferol	56-68	beta-lactoglobulin	Bos taurus	48-55