PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
26322377-4	2015	Using docking, molecular dynamics (MD), and hybrid quantum mechanical/molecular mechanics methods, we have investigated mechanisms by which methionyl-tRNA synthetase (MetRS) may edit against the highly toxic, noncognate, amino acids homocysteine (Hcy) and its oxygen analogue, homoserine (Hse).	amino acids homocysteine	221-245	methionyl-tRNA synthetase 1	Homo sapiens	140-165	
26322377-4	2015	Using docking, molecular dynamics (MD), and hybrid quantum mechanical/molecular mechanics methods, we have investigated mechanisms by which methionyl-tRNA synthetase (MetRS) may edit against the highly toxic, noncognate, amino acids homocysteine (Hcy) and its oxygen analogue, homoserine (Hse).	amino acids homocysteine	221-245	methionyl-tRNA synthetase 1	Homo sapiens	167-172	
26322377-4	2015	Using docking, molecular dynamics (MD), and hybrid quantum mechanical/molecular mechanics methods, we have investigated mechanisms by which methionyl-tRNA synthetase (MetRS) may edit against the highly toxic, noncognate, amino acids homocysteine (Hcy) and its oxygen analogue, homoserine (Hse).	Homocysteine	247-250	methionyl-tRNA synthetase 1	Homo sapiens	140-165	
26322377-4	2015	Using docking, molecular dynamics (MD), and hybrid quantum mechanical/molecular mechanics methods, we have investigated mechanisms by which methionyl-tRNA synthetase (MetRS) may edit against the highly toxic, noncognate, amino acids homocysteine (Hcy) and its oxygen analogue, homoserine (Hse).	Homocysteine	247-250	methionyl-tRNA synthetase 1	Homo sapiens	167-172	
26322377-4	2015	Using docking, molecular dynamics (MD), and hybrid quantum mechanical/molecular mechanics methods, we have investigated mechanisms by which methionyl-tRNA synthetase (MetRS) may edit against the highly toxic, noncognate, amino acids homocysteine (Hcy) and its oxygen analogue, homoserine (Hse).	Oxygen	260-266	methionyl-tRNA synthetase 1	Homo sapiens	140-165	
26322377-4	2015	Using docking, molecular dynamics (MD), and hybrid quantum mechanical/molecular mechanics methods, we have investigated mechanisms by which methionyl-tRNA synthetase (MetRS) may edit against the highly toxic, noncognate, amino acids homocysteine (Hcy) and its oxygen analogue, homoserine (Hse).	Oxygen	260-266	methionyl-tRNA synthetase 1	Homo sapiens	167-172	
26322377-4	2015	Using docking, molecular dynamics (MD), and hybrid quantum mechanical/molecular mechanics methods, we have investigated mechanisms by which methionyl-tRNA synthetase (MetRS) may edit against the highly toxic, noncognate, amino acids homocysteine (Hcy) and its oxygen analogue, homoserine (Hse).	Homoserine	277-287	methionyl-tRNA synthetase 1	Homo sapiens	140-165	
26322377-4	2015	Using docking, molecular dynamics (MD), and hybrid quantum mechanical/molecular mechanics methods, we have investigated mechanisms by which methionyl-tRNA synthetase (MetRS) may edit against the highly toxic, noncognate, amino acids homocysteine (Hcy) and its oxygen analogue, homoserine (Hse).	Homoserine	277-287	methionyl-tRNA synthetase 1	Homo sapiens	167-172	
26322377-4	2015	Using docking, molecular dynamics (MD), and hybrid quantum mechanical/molecular mechanics methods, we have investigated mechanisms by which methionyl-tRNA synthetase (MetRS) may edit against the highly toxic, noncognate, amino acids homocysteine (Hcy) and its oxygen analogue, homoserine (Hse).	Homoserine	289-292	methionyl-tRNA synthetase 1	Homo sapiens	140-165	
26322377-4	2015	Using docking, molecular dynamics (MD), and hybrid quantum mechanical/molecular mechanics methods, we have investigated mechanisms by which methionyl-tRNA synthetase (MetRS) may edit against the highly toxic, noncognate, amino acids homocysteine (Hcy) and its oxygen analogue, homoserine (Hse).	Homoserine	289-292	methionyl-tRNA synthetase 1	Homo sapiens	167-172	
26322377-9	2015	A similarly positioned aspartate or glutamate also occurs in the homologous enzymes LeuRS, IleRS, and ValRS, which also discriminate against Hcy.	Aspartic Acid	23-32	leucyl-tRNA synthetase 2, mitochondrial	Homo sapiens	84-89	
26322377-9	2015	A similarly positioned aspartate or glutamate also occurs in the homologous enzymes LeuRS, IleRS, and ValRS, which also discriminate against Hcy.	Aspartic Acid	23-32	isoleucyl-tRNA synthetase 2, mitochondrial	Homo sapiens	91-96	
26322377-9	2015	A similarly positioned aspartate or glutamate also occurs in the homologous enzymes LeuRS, IleRS, and ValRS, which also discriminate against Hcy.	Aspartic Acid	23-32	valyl-tRNA synthetase 2, mitochondrial	Homo sapiens	102-107	
26322377-9	2015	A similarly positioned aspartate or glutamate also occurs in the homologous enzymes LeuRS, IleRS, and ValRS, which also discriminate against Hcy.	Glutamic Acid	36-45	leucyl-tRNA synthetase 2, mitochondrial	Homo sapiens	84-89	
26322377-9	2015	A similarly positioned aspartate or glutamate also occurs in the homologous enzymes LeuRS, IleRS, and ValRS, which also discriminate against Hcy.	Glutamic Acid	36-45	isoleucyl-tRNA synthetase 2, mitochondrial	Homo sapiens	91-96	
26322377-9	2015	A similarly positioned aspartate or glutamate also occurs in the homologous enzymes LeuRS, IleRS, and ValRS, which also discriminate against Hcy.	Glutamic Acid	36-45	valyl-tRNA synthetase 2, mitochondrial	Homo sapiens	102-107	
26322377-9	2015	A similarly positioned aspartate or glutamate also occurs in the homologous enzymes LeuRS, IleRS, and ValRS, which also discriminate against Hcy.	Homocysteine	141-144	leucyl-tRNA synthetase 2, mitochondrial	Homo sapiens	84-89	
26322377-9	2015	A similarly positioned aspartate or glutamate also occurs in the homologous enzymes LeuRS, IleRS, and ValRS, which also discriminate against Hcy.	Homocysteine	141-144	isoleucyl-tRNA synthetase 2, mitochondrial	Homo sapiens	91-96	
26322377-9	2015	A similarly positioned aspartate or glutamate also occurs in the homologous enzymes LeuRS, IleRS, and ValRS, which also discriminate against Hcy.	Homocysteine	141-144	valyl-tRNA synthetase 2, mitochondrial	Homo sapiens	102-107