PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27641460-2	2016	Studying the crystal structure of human estrogen receptor alpha (hERalpha) and using nuclear magnetic resonance, we show here that the short V(364)PGF(367) sequence, which is located within its ligand-binding domain and adopts a type II beta-turn conformation in the protein, binds the peptidyl-prolyl isomerase (PPIase or rotamase) FK1 domain of FKBP52.	Prostaglandins F	147-150	FKBP prolyl isomerase 4	Homo sapiens	313-319	
27641460-2	2016	Studying the crystal structure of human estrogen receptor alpha (hERalpha) and using nuclear magnetic resonance, we show here that the short V(364)PGF(367) sequence, which is located within its ligand-binding domain and adopts a type II beta-turn conformation in the protein, binds the peptidyl-prolyl isomerase (PPIase or rotamase) FK1 domain of FKBP52.	Prostaglandins F	147-150	FKBP prolyl isomerase 4	Homo sapiens	323-331	
27641460-2	2016	Studying the crystal structure of human estrogen receptor alpha (hERalpha) and using nuclear magnetic resonance, we show here that the short V(364)PGF(367) sequence, which is located within its ligand-binding domain and adopts a type II beta-turn conformation in the protein, binds the peptidyl-prolyl isomerase (PPIase or rotamase) FK1 domain of FKBP52.	Prostaglandins F	147-150	FKBP prolyl isomerase 4	Homo sapiens	347-353