PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10820001-5	2000	The best inhibitor of the current series was (1R)-1-phenylacetamido-2-(3-carboxyphenyl)ethylboronic acid (1, K(I) = 5.9 nM), which resembles most closely the best known substrate of TEM-1, benzylpenicillin (penicillin G).	Penicillin G	189-205	hypothetical protein	Escherichia coli	182-187	
10820001-5	2000	The best inhibitor of the current series was (1R)-1-phenylacetamido-2-(3-carboxyphenyl)ethylboronic acid (1, K(I) = 5.9 nM), which resembles most closely the best known substrate of TEM-1, benzylpenicillin (penicillin G).	Penicillin G	207-219	hypothetical protein	Escherichia coli	182-187	
9891008-3	1999	Evidence from the TEM-1/BLIP co-crystal suggests that two BLIP residues, Asp-49 and Phe-142, mimic interactions made by penicillin G when bound in the active site of TEM-1.	Penicillin G	120-132	hypothetical protein	Escherichia coli	18-23	
9891008-3	1999	Evidence from the TEM-1/BLIP co-crystal suggests that two BLIP residues, Asp-49 and Phe-142, mimic interactions made by penicillin G when bound in the active site of TEM-1.	Penicillin G	120-132	hypothetical protein	Escherichia coli	166-171