PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2006161-3	1991	Endoproteinase Lys-C or a baby hamster kidney cell protease cleaves angiogenin at the peptide bond either between Lys-60 and Asn-61 or between Glu-67 and Asn-68, respectively.	Lysine	15-18	ribonuclease A family member k6	Gallus gallus	68-78	
1698454-0	1990	Mutagenesis of residues flanking Lys-40 enhances the enzymatic activity and reduces the angiogenic potency of angiogenin.	Lysine	33-36	ribonuclease A family member k6	Gallus gallus	110-120	
1698454-1	1990	The primary structure of the blood vessel inducing protein angiogenin is 35% identical with that of pancreatic ribonuclease (RNase) and contains counterparts for the critical RNase active-site residues His-12, Lys-41, and His-119.	Lysine	210-213	ribonuclease A family member k6	Gallus gallus	59-69	
1698454-3	1990	Comparison of the amino acid sequences of RNase and angiogenin reveals several striking differences in the region flanking the active-site lysine, including a deletion and a transposition of aspartic acid and proline residues.	Lysine	139-145	ribonuclease A family member k6	Gallus gallus	52-62	
1698454-7	1990	Thus, non-active-site residues near Lys-40 in angiogenin appear to play a significant role in determining enzymatic specificity and reactivity as well as angiogenic potency.	Lysine	36-39	ribonuclease A family member k6	Gallus gallus	46-56