PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9128147-2	1997	While MPO shows significant sequence homology with other peroxidases and this homology is particularly striking among the active-site residues, MPO exhibits unusual spectral features and the unique ability to catalyze the oxidation of chloride ions.	Chlorides	235-243	myeloperoxidase	Homo sapiens	6-9	
9128147-2	1997	While MPO shows significant sequence homology with other peroxidases and this homology is particularly striking among the active-site residues, MPO exhibits unusual spectral features and the unique ability to catalyze the oxidation of chloride ions.	Chlorides	235-243	myeloperoxidase	Homo sapiens	144-147	
9128147-10	1997	This change suggests that loss of the distal ligand in MPO releases stress on the heme which may facilitate binding of chloride ion.	Chlorides	119-127	myeloperoxidase	Homo sapiens	55-58