PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8762142-1	1996	The native state fluorescence and CD spectra of the predominantly beta-sheet cellular retinoic acid-binding protein I (CRABPI) include contributions from its three tryptophan residues and are influenced by the positions of these residues in the three-dimensional structure.	Cadmium	34-36	cellular retinoic acid binding protein 1	Homo sapiens	119-125	
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.	Cadmium	20-22	cellular retinoic acid binding protein 1	Homo sapiens	35-41