PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8038158-0	1994	Interaction domain for the reaction of cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I. Site-directed mutants of cytochrome c peroxidase (CcP) were created to modify the interaction domain between CcP and yeast iso-1-cytochrome c (yCC) seen in the crystal structure of the CcP-yCC complex [Pelletier & Kraut (1992) Science 258, 1748-1755].	Adenosine Monophosphate	344-347	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	95-118	
8038158-0	1994	Interaction domain for the reaction of cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I. Site-directed mutants of cytochrome c peroxidase (CcP) were created to modify the interaction domain between CcP and yeast iso-1-cytochrome c (yCC) seen in the crystal structure of the CcP-yCC complex [Pelletier & Kraut (1992) Science 258, 1748-1755].	Adenosine Monophosphate	344-347	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	156-179	
8038158-0	1994	Interaction domain for the reaction of cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I. Site-directed mutants of cytochrome c peroxidase (CcP) were created to modify the interaction domain between CcP and yeast iso-1-cytochrome c (yCC) seen in the crystal structure of the CcP-yCC complex [Pelletier & Kraut (1992) Science 258, 1748-1755].	Adenosine Monophosphate	344-347	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	181-184	
8038158-1	1994	In the crystalline CcP-yCC complex, two acidic regions of CcP contact lysine residues on yCC.	Lysine	70-76	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	19-22	
8038158-1	1994	In the crystalline CcP-yCC complex, two acidic regions of CcP contact lysine residues on yCC.	Lysine	70-76	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	58-61	
8038158-4	1994	Stopped-flow experiments carried out in 310 mM ionic strength buffer at pH 7 revealed that yCC initially reduced the indole radical on Trp-191 of the parent CcP compound I with a bimolecular rate constant ka = 2.5 x 10(8) M-1 s-1.	indole radical	117-131	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	157-160	
8038158-4	1994	Stopped-flow experiments carried out in 310 mM ionic strength buffer at pH 7 revealed that yCC initially reduced the indole radical on Trp-191 of the parent CcP compound I with a bimolecular rate constant ka = 2.5 x 10(8) M-1 s-1.	Tryptophan	135-138	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	157-160	
8038158-7	1994	CcP mutants D34N and E290N that are closest to a complementary yCC lysine residue in the crystalline CcP-yCC complex gave the lowest values for ka and kb, which were 25-50% of the values of the CcP parent.	Lysine	67-73	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	0-3	
8038158-7	1994	CcP mutants D34N and E290N that are closest to a complementary yCC lysine residue in the crystalline CcP-yCC complex gave the lowest values for ka and kb, which were 25-50% of the values of the CcP parent.	Lysine	67-73	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	101-104	
8038158-7	1994	CcP mutants D34N and E290N that are closest to a complementary yCC lysine residue in the crystalline CcP-yCC complex gave the lowest values for ka and kb, which were 25-50% of the values of the CcP parent.	Lysine	67-73	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	101-104