PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12121764-2	2002	KatGs, CCP and APXs contain identical amino acid triads in the heme pocket (distal Arg/Trp/His and proximal His/Trp/Asp), but differ dramatically in their reactivities towards hydrogen peroxide and various one-electron donors.	Aspartic Acid	116-119	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	7-10	
18232645-2	2008	The mutants include the conversion of all 20 glutamate residues and 24 of the 25 aspartate residues in CcP, one at a time, to lysine residues.	Aspartic Acid	81-90	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	103-106	
1332763-0	1992	Effect of Asp-235-->Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase.	Aspartic Acid	10-13	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	103-126	
1660723-1	1991	The double charge, aspartic acid to lysine, point mutations were constructed at positions 37, 79, and 217 on the surface of cytochrome c peroxidase, sites purported to be within or proximal to the recognition site for cytochrome c in an electron-transfer productive complex formed by the two proteins.	Aspartic Acid	19-32	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	124-147