PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31661769-1	2019	Previous studies demonstrated that the 52-kDa FK506-binding protein (FKBP52) proline-rich loop is functionally relevant in the regulation of steroid hormone receptor activity.	isoleucyl-prolyl-proline	77-84	FKBP prolyl isomerase 4	Homo sapiens	69-75	
31661769-5	2019	In silico homology modeling suggests that alanine to valine substitution at position 111 in DrFKBP52 induces an open conformation of the proline-rich loop surface similar to that observed on human FKBP52, which may allow for sufficient surface area and increased hydrophobicity for interactions within the receptor-chaperone complex.	isoleucyl-prolyl-proline	137-144	FKBP prolyl isomerase 4	Homo sapiens	94-100	
31661769-7	2019	Collectively, these results confirm the functional importance of the FKBP52 proline-rich loop, suggest that an open conformation on the proline-rich loop surface is a predictor of activity, and highlight the importance of an additional residue within the FK2 domain.	isoleucyl-prolyl-proline	76-83	FKBP prolyl isomerase 4	Homo sapiens	69-75	
31661769-7	2019	Collectively, these results confirm the functional importance of the FKBP52 proline-rich loop, suggest that an open conformation on the proline-rich loop surface is a predictor of activity, and highlight the importance of an additional residue within the FK2 domain.	isoleucyl-prolyl-proline	136-143	FKBP prolyl isomerase 4	Homo sapiens	69-75