PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10455016-0	1999	Lysine mutagenesis identifies cationic charges of human CYP17 that interact with cytochrome b5 to promote male sex-hormone biosynthesis.	Lysine	0-6	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	56-61	
25315771-8	2014	The appositional surfaces include Lys-88, Arg-347, and Arg-358/Arg-449 of CYP17A1, which interact with Glu-61, Glu-42, and Glu-48/Glu-49 of b5, respectively.	Lysine	34-37	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	74-81	
19636199-4	2009	The molecular analysis of CYP17A1 revealed a novel homozygous missense mutation resulting in the substitution of arginine to lysine at the amino acid position 21 (p.R21L).	Lysine	125-131	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	26-33	
19040066-5	2008	RESULTS: The CYP17 genes of the patients were proved to hold a homozygous mutation with a base deletion and a base transversion (TAC/AA) in exon 6, which produced a missense mutation of Tyr-->Lys at codon 329 and changed the open reading frame following this codon.	Lysine	195-198	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	13-18	
10455016-5	1999	That the defect could be essentially reversed by lysine mutagenesis has led to the conclusion that the cationic charges on all three residues (at the positions of Arg(347), Arg(358), Arg(449)) are vital for the functional interaction of CYP17 with cytochrome b(5) and that the loss of any one of these cationic charges is catastrophic.	Lysine	49-55	cytochrome P450 family 17 subfamily A member 1	Homo sapiens	237-242