PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12566087-7	2003	These findings strongly support the conclusion that the interaction of sulfonylureas and acidic analogues with SURs is favoured by the anionic group of these drugs and that a phosphate group allows more efficient ligand interaction with SUR1 than a carboxylic group.	Phosphates	175-184	ATP binding cassette subfamily C member 8	Homo sapiens	237-241	
15004210-5	2004	We show here that SUR1 modifies the ATP-binding pocket of Kir6.2, by increasing the width of the groove that binds the phosphate tail of ATP, without changing the length of the groove, and by enhancing interaction with the adenine ring.	Phosphates	119-128	ATP binding cassette subfamily C member 8	Homo sapiens	18-22