PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
35120937-1	2022	Ammonia dependent NAD+ synthetase from multi drug resistance Staphylococcus aureus catalyzes ATP dependent formation of NAD+ from deamido-NAD+ and ammonia at the synthetase active site.	nicotinic acid adenine dinucleotide	130-142	AT695_RS07645	Staphylococcus aureus	18-33	
33098904-1	2020	NAD synthetase (NadE) catalyzes the last step in NAD biosynthesis, transforming deamido-NAD+ into NAD+ by a two-step reaction with co-substrates ATP and amide donor ammonia.	nicotinic acid adenine dinucleotide	80-92	AT695_RS07645	Staphylococcus aureus	0-14	
33098904-1	2020	NAD synthetase (NadE) catalyzes the last step in NAD biosynthesis, transforming deamido-NAD+ into NAD+ by a two-step reaction with co-substrates ATP and amide donor ammonia.	nicotinic acid adenine dinucleotide	80-92	AT695_RS07645	Staphylococcus aureus	16-20	
33098904-3	2020	We used this structure to perform molecular dynamics simulations of apo-enzyme, enzyme-substrate (NadE with ATP and NaAD) and enzyme-intermediate complexes (NadE with NaAD-AMP) to investigate key binding interactions and explore the conformational transitions and flexibility of the binding pocket.	nicotinic acid adenine dinucleotide	116-120	AT695_RS07645	Staphylococcus aureus	98-102