PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8075981-6	1994	Comparison of these structures with previously determined structures of unligated CyPA and CyPA complexed with a candidate substrate for the isomerase activity, the dipeptide AlaPro, reveals that subtle conformational changes occur in both CsA and CyPA on complex formation.	alanylproline	175-181	peptidylprolyl isomerase A	Homo sapiens	82-86	
8075981-6	1994	Comparison of these structures with previously determined structures of unligated CyPA and CyPA complexed with a candidate substrate for the isomerase activity, the dipeptide AlaPro, reveals that subtle conformational changes occur in both CsA and CyPA on complex formation.	alanylproline	175-181	peptidylprolyl isomerase A	Homo sapiens	91-95	
8075981-6	1994	Comparison of these structures with previously determined structures of unligated CyPA and CyPA complexed with a candidate substrate for the isomerase activity, the dipeptide AlaPro, reveals that subtle conformational changes occur in both CsA and CyPA on complex formation.	alanylproline	175-181	peptidylprolyl isomerase A	Homo sapiens	91-95