PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11731804-3	2002	The crystal structure of the PAPT from Thermotoga maritima (TmPAPT) has been solved to 1.5 A resolution in the presence and absence of AdoDATO (S-adenosyl-1,8-diamino-3-thiooctane), a compound containing both substrate and product moieties.	S-adenosyl-3-thio-1,8-diaminooctane	135-142	spermidine synthase	Homo sapiens	29-33	
11731804-3	2002	The crystal structure of the PAPT from Thermotoga maritima (TmPAPT) has been solved to 1.5 A resolution in the presence and absence of AdoDATO (S-adenosyl-1,8-diamino-3-thiooctane), a compound containing both substrate and product moieties.	S-adenosyl-3-thio-1,8-diaminooctane	144-179	spermidine synthase	Homo sapiens	29-33	
11731804-5	2002	The AdoDATO binding site is lined with residues conserved in PAPT enzymes from bacteria to humans, suggesting a universal catalytic mechanism.	S-adenosyl-3-thio-1,8-diaminooctane	4-11	spermidine synthase	Homo sapiens	61-65	
16428313-5	2006	Key regions in the active site, which are very highly conserved, were identified by structural studies with spermidine synthase from Thermotoga maritima bound to S-adenosyl-1,8-diamino-3-thiooctane, a multisubstrate analog inhibitor.	S-adenosyl-3-thio-1,8-diaminooctane	162-197	spermidine synthase	Homo sapiens	108-127