PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28588690-7	2017	Although there is no hydrophobic interaction around Tyr and Trp residues, the secondary structure of HSA changes through the formation of the KR-HSA complex.	kaempferol-7-O-alpha-L-rhamnopyranoside	142-144	albumin	Homo sapiens	101-104	
28588690-3	2017	The present study reports that kaempferol-7-O-alpha-L-rhamnopyranoside (KR) interacts with HSA as indicated by multiple fluorescence spectroscopy and molecular modeling.	kaempferol-7-O-alpha-L-rhamnopyranoside	31-70	albumin	Homo sapiens	91-94	
28588690-7	2017	Although there is no hydrophobic interaction around Tyr and Trp residues, the secondary structure of HSA changes through the formation of the KR-HSA complex.	kaempferol-7-O-alpha-L-rhamnopyranoside	142-144	albumin	Homo sapiens	145-148	
28588690-3	2017	The present study reports that kaempferol-7-O-alpha-L-rhamnopyranoside (KR) interacts with HSA as indicated by multiple fluorescence spectroscopy and molecular modeling.	kaempferol-7-O-alpha-L-rhamnopyranoside	72-74	albumin	Homo sapiens	91-94	
28588690-4	2017	KR can quench the intrinsic fluorescence of HSA through the formation of a KR-HSA complex in a static manner.	kaempferol-7-O-alpha-L-rhamnopyranoside	0-2	albumin	Homo sapiens	44-47	
28588690-4	2017	KR can quench the intrinsic fluorescence of HSA through the formation of a KR-HSA complex in a static manner.	kaempferol-7-O-alpha-L-rhamnopyranoside	0-2	albumin	Homo sapiens	78-81