PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10580153-1	1999	Protein L-isoaspartyl methyltransferase (Pimt) is a highly conserved enzyme utilising S-adenosylmethionine (AdoMet) to methylate aspartate residues of proteins damaged by age-related isomerisation and deamidation.	Aspartic Acid	129-138	methionine adenosyltransferase 1A	Rattus norvegicus	108-114	
8119887-2	1994	Most mammalian S-adenosylmethionine (AdoMet)-dependent methyltransferases have a conserved aspartate residue in a sequence oDso (o denotes a hydrophobic amino acid and s denotes a small neutral amino acid).	Aspartic Acid	91-100	methionine adenosyltransferase 1A	Rattus norvegicus	37-43	
8119887-3	1994	Rat guanidinoacetate methyltransferase has two aspartate residues (Asp-129 and Asp-134) conforming to the motif in close proximity to Tyr-136 that is photoaffinity-labeled by AdoMet (Takata, Y., and Fujioka, M. (1992) Biochemistry 31, 4369-4374).	Aspartic Acid	47-56	methionine adenosyltransferase 1A	Rattus norvegicus	175-181	
8119887-3	1994	Rat guanidinoacetate methyltransferase has two aspartate residues (Asp-129 and Asp-134) conforming to the motif in close proximity to Tyr-136 that is photoaffinity-labeled by AdoMet (Takata, Y., and Fujioka, M. (1992) Biochemistry 31, 4369-4374).	Aspartic Acid	67-70	methionine adenosyltransferase 1A	Rattus norvegicus	175-181	
8119887-3	1994	Rat guanidinoacetate methyltransferase has two aspartate residues (Asp-129 and Asp-134) conforming to the motif in close proximity to Tyr-136 that is photoaffinity-labeled by AdoMet (Takata, Y., and Fujioka, M. (1992) Biochemistry 31, 4369-4374).	Aspartic Acid	79-82	methionine adenosyltransferase 1A	Rattus norvegicus	175-181	
8119887-12	1994	Thus, the large decreases in kcat/Km values for AdoMet indicate that Asp-134 is crucial for binding AdoMet.	Aspartic Acid	69-72	methionine adenosyltransferase 1A	Rattus norvegicus	48-54	
8119887-12	1994	Thus, the large decreases in kcat/Km values for AdoMet indicate that Asp-134 is crucial for binding AdoMet.	Aspartic Acid	69-72	methionine adenosyltransferase 1A	Rattus norvegicus	100-106	
8443166-9	1993	An important characteristic of the sequence is the presence of two adjacent aspartic acid residues (Asp117-Asp118) which most likely provide the negative charge environment for the sulfonium moiety of the AdoMet molecule.	Aspartic Acid	76-89	methionine adenosyltransferase 1A	Rattus norvegicus	205-211