PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23267009-4	2013	FPA binds directly to RPA, resulting in a conformational shift as determined through quenching of intrinsic tryptophan fluorescence in full length RPA.	Tryptophan	108-118	replication protein A1	Homo sapiens	22-25	
23267009-4	2013	FPA binds directly to RPA, resulting in a conformational shift as determined through quenching of intrinsic tryptophan fluorescence in full length RPA.	Tryptophan	108-118	replication protein A1	Homo sapiens	147-150	
17583916-4	2007	Using a set of oligonucleotides (dT) with varying lengths as a molecular ruler and also as the substrate, we have determined at single-nucleotide resolution the relative positions of the ssDNA with interacting intrinsic tryptophans of RPA.	Tryptophan	220-231	replication protein A1	Homo sapiens	235-238	
7983760-5	1995	A Trp-to-Thr mutation within the acidic domain abolishes EBNA-2 transactivating activity and greatly compromises the association with TFIIB, TAF40, and RPA70, establishing a genetic linkage between transactivating activity and these associations.	Tryptophan	2-5	replication protein A1	Homo sapiens	152-157