PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25794283-0	2015	Molecular dynamics simulations of acylpeptide hydrolase bound to chlorpyrifosmethyl oxon and dichlorvos.	fospirate	65-88	acylaminoacyl-peptide hydrolase	Homo sapiens	34-55	
25794283-4	2015	We report a computational study of APH bound to chlorpyrifosmethyl oxon and dichlorvos.	fospirate	48-71	acylaminoacyl-peptide hydrolase	Homo sapiens	35-38	
25794283-6	2015	Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site.	fospirate	101-124	acylaminoacyl-peptide hydrolase	Homo sapiens	149-152	
25794283-6	2015	Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site.	fospirate	101-124	acylaminoacyl-peptide hydrolase	Homo sapiens	236-239	
25794283-6	2015	Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site.	fospirate	201-224	acylaminoacyl-peptide hydrolase	Homo sapiens	149-152	
25794283-6	2015	Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site.	fospirate	201-224	acylaminoacyl-peptide hydrolase	Homo sapiens	236-239	
25794283-6	2015	Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site.	fospirate	201-224	acylaminoacyl-peptide hydrolase	Homo sapiens	149-152	
25794283-6	2015	Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the beta-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site.	fospirate	201-224	acylaminoacyl-peptide hydrolase	Homo sapiens	236-239