PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8999826-3	1997	However, the roles of two conserved arginine residues (Arg-111 and Arg-131 in CRABP-I; Arg-111 and Arg-132 in CRABP-II) that interact with the carboxyl group of retinoic acid have not been evaluated.	Arginine	36-44	cellular retinoic acid binding protein 1	Homo sapiens	78-85	
8762142-5	1996	Although the far-UV CD spectrum of CRABPI is largely determined by the protein"s secondary structure, aromatic clustering around Trp 87 and the aromatic-charge interaction between Arg 111 and Trp 109 give rise to a characteristic feature in the CD spectrum at 228 nm.	Arginine	180-183	cellular retinoic acid binding protein 1	Homo sapiens	35-41