PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2851317-0	1988	Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation.	Tryptophan	0-10	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	67-90	
2851317-0	1988	Tryptophan-191----phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation.	Phenylalanine	14-31	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	67-90	
2851317-1	1988	On the basis of X-ray structural information, it was previously proposed that tryptophan-191 of yeast cytochrome c peroxidase (CCP) may be important in determining the spectroscopic and catalytic properties of the enzyme [Edwards, S. L., Xuong, Ng.	Tryptophan	78-88	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	102-125	
2851317-1	1988	On the basis of X-ray structural information, it was previously proposed that tryptophan-191 of yeast cytochrome c peroxidase (CCP) may be important in determining the spectroscopic and catalytic properties of the enzyme [Edwards, S. L., Xuong, Ng.	Tryptophan	78-88	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	127-130	
2851317-4	1988	By use of site-directed mutagenesis and an Escherichia coli expression system, a mutant phenylalanine-191 (F191) CCP was prepared in order to examine the effects of altering the H-bonding and pi-pi interactions that occur between Trp-191 and the iron-coordinated proximal His-175 in the parent enzyme.	Phenylalanine	88-101	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	113-116