PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3841691-2	1985	These studies indicated the presence of a new L-asparaginase amidohydrolase type enzyme in eel plasma which deamidates L-asparagine residue at the amino terminus of the angiotensin peptides, thereby implying that l-asparaginyl decapeptide (rather than l-aspartyl decapeptide) is the natural form of angiotensin inherent in eel plasma.	Asparagine	119-131	asparaginase and isoaspartyl peptidase 1	Homo sapiens	46-60	
3841691-2	1985	These studies indicated the presence of a new L-asparaginase amidohydrolase type enzyme in eel plasma which deamidates L-asparagine residue at the amino terminus of the angiotensin peptides, thereby implying that l-asparaginyl decapeptide (rather than l-aspartyl decapeptide) is the natural form of angiotensin inherent in eel plasma.	l-asparaginyl decapeptide	213-238	asparaginase and isoaspartyl peptidase 1	Homo sapiens	46-60	
3841691-2	1985	These studies indicated the presence of a new L-asparaginase amidohydrolase type enzyme in eel plasma which deamidates L-asparagine residue at the amino terminus of the angiotensin peptides, thereby implying that l-asparaginyl decapeptide (rather than l-aspartyl decapeptide) is the natural form of angiotensin inherent in eel plasma.	l-aspartyl decapeptide	252-274	asparaginase and isoaspartyl peptidase 1	Homo sapiens	46-60