PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17192295-5	2007	RESULTS: Four homozygote mutations were identified by direct sequencing of the CYP17A1 gene corresponding to an alanin 302-proline (A302P) exchange; the loss of lysine 327 (K327del); the deletion of glutamate 331 (E331del); and the replacement of arginine 416 with a histidine (R416H).	Proline	123-130	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	79-86	
11243732-6	2001	This proline residue is conserved in P450c17 of other species and other human P450 proteins.	Proline	5-12	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	37-44	
11243732-8	2001	The proline residue probably causes a turn in the meander region of P450c17, and we hypothesize, by comparison to homologous proteins, that the change in the protein conformation may abolish heme incorporation or may prevent P450c17 from interacting with electron donors.	Proline	4-11	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	68-75	
11243732-8	2001	The proline residue probably causes a turn in the meander region of P450c17, and we hypothesize, by comparison to homologous proteins, that the change in the protein conformation may abolish heme incorporation or may prevent P450c17 from interacting with electron donors.	Proline	4-11	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	225-232	
8504753-3	1993	The spontaneous human P450c17 mutation Ser106-->Pro eliminates all enzymatic activity.	Proline	51-54	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	22-29