PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23852030-3	2014	In a common two-step reaction, each aaRS first uses the energy stored in ATP to synthesize an activated aminoacyl adenylate intermediate.	Adenosine Triphosphate	73-76	alanyl-tRNA synthetase 1	Homo sapiens	36-40	
33260297-1	2020	The KARS gene encodes the aminoacyl-tRNA synthetase (aaRS), which activates and joins the lysin with its corresponding transfer RNA (tRNA) through the ATP-dependent aminoacylation of the amino acid.	Adenosine Triphosphate	151-154	alanyl-tRNA synthetase 1	Homo sapiens	26-51	
33260297-1	2020	The KARS gene encodes the aminoacyl-tRNA synthetase (aaRS), which activates and joins the lysin with its corresponding transfer RNA (tRNA) through the ATP-dependent aminoacylation of the amino acid.	Adenosine Triphosphate	151-154	alanyl-tRNA synthetase 1	Homo sapiens	53-57	
29659563-2	2018	One key component of this machinery are aminoacyl tRNA synthetases (aaRS), which ligate tRNAs to amino acids while consuming ATP.	Adenosine Triphosphate	125-128	alanyl-tRNA synthetase 1	Homo sapiens	40-66	
29659563-2	2018	One key component of this machinery are aminoacyl tRNA synthetases (aaRS), which ligate tRNAs to amino acids while consuming ATP.	Adenosine Triphosphate	125-128	alanyl-tRNA synthetase 1	Homo sapiens	68-72	
9204708-1	1997	Aminoacyl-tRNA synthetases (aaRS) bind their substrates-ATP, amino acids and tRNA- and stabilize putative transition states in the aminoacylation reaction.	Adenosine Triphosphate	56-59	alanyl-tRNA synthetase 1	Homo sapiens	0-26	
9204708-1	1997	Aminoacyl-tRNA synthetases (aaRS) bind their substrates-ATP, amino acids and tRNA- and stabilize putative transition states in the aminoacylation reaction.	Adenosine Triphosphate	56-59	alanyl-tRNA synthetase 1	Homo sapiens	28-32	
8422978-1	1993	Our present understanding of the molecular mechanisms responsible for the recognition of tRNAs by their cognate aminoacyl-tRNA synthetases (aaRS) is essentially based on three sources of information: 1) the characterization of tRNA identity determinants using in vivo and in vitro approaches, 2) the classification of synthetases from primary sequence analysis: aaRS can be partitioned into two classes according to the spatial structure of their ATP binding domain, and 3) the structural results of crystallographic investigations and solution studies.	Adenosine Triphosphate	447-450	alanyl-tRNA synthetase 1	Homo sapiens	112-138	
7647112-2	1995	The conservation of those residues which have been shown to be critical in some aaRS enables to predict their location and function in the other synthetases, particularly: i) a conserved negatively-charged residue which binds the alpha-amino group of the amino acid substrate; ii) conserved residues within the inserted domain bridging the two halves of the dinucleotide-binding fold; and iii) conserved residues in the second half of the fold which bind the amino acid and ATP substrate.	Adenosine Triphosphate	474-477	alanyl-tRNA synthetase 1	Homo sapiens	80-84	
8422978-1	1993	Our present understanding of the molecular mechanisms responsible for the recognition of tRNAs by their cognate aminoacyl-tRNA synthetases (aaRS) is essentially based on three sources of information: 1) the characterization of tRNA identity determinants using in vivo and in vitro approaches, 2) the classification of synthetases from primary sequence analysis: aaRS can be partitioned into two classes according to the spatial structure of their ATP binding domain, and 3) the structural results of crystallographic investigations and solution studies.	Adenosine Triphosphate	447-450	alanyl-tRNA synthetase 1	Homo sapiens	140-144