PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1681900-0	1991	Identification of the ATP binding sites of the carbamyl phosphate synthetase domain of the Syrian hamster multifunctional protein CAD by affinity labeling with 5"-[p-(fluorosulfonyl)benzoyl]adenosine.	Adenosine Triphosphate	22-25	CAD protein	Mesocricetus auratus	130-133	
1681900-3	1991	ATP protected CAD against inactivation by FSBA whereas the presence of the allosteric effectors UTP and PRPP afforded little protection, which suggests that the ATP binding sites were specifically labeled.	Adenosine Triphosphate	0-3	CAD protein	Mesocricetus auratus	14-17	
1681900-8	1991	Amino acid sequencing of the principal peaks resulting from tryptic digests of FSBA-modified CAD located the sites of FSBA modification in regions that exhibit high homology to ATP binding sites of other known proteins.	Adenosine Triphosphate	177-180	CAD protein	Mesocricetus auratus	93-96	
1681900-9	1991	Thus CAD has two ATP binding sites, one in each of the two highly homologous halves of the carbamyl phosphate domain which catalyze distinct ATP-dependent partial reactions in carbamyl phosphate synthesis.	Adenosine Triphosphate	17-20	CAD protein	Mesocricetus auratus	5-8	
1681900-9	1991	Thus CAD has two ATP binding sites, one in each of the two highly homologous halves of the carbamyl phosphate domain which catalyze distinct ATP-dependent partial reactions in carbamyl phosphate synthesis.	Adenosine Triphosphate	141-144	CAD protein	Mesocricetus auratus	5-8