PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3263690-8	1988	Synergy between clavulanate or sulbactam (2 micrograms/mL) and amoxicillin was greater against derivatives producing EBS-Bla than against those producing TEM-1, TEM-2, or SHV-1; this synergy was greater with clavulanate than with sulbactam against derivatives producing SHV-2 and the SHV-2-type enzyme but was similar with clavulanate and sulbactam against those producing CTX-1.	Clavulanic Acid	16-27	beta-lactamase	Escherichia coli	121-124	
18070972-6	2008	Escherichia coli harboring bla(CAD-1) exhibited resistance to penams (benzylpenicillin and amoxicillin) and remained susceptible to amoxicillin in combination with clavulanic acid.	Clavulanic Acid	164-179	beta-lactamase	Escherichia coli	27-30	
16870757-6	2006	A recombinant Escherichia coli strain carrying the bla(FUS-1) gene exhibited resistance to amoxicillin with a moderate decrease in the MICs with clavulanic acid.	Clavulanic Acid	145-160	beta-lactamase	Escherichia coli	51-54	
28039278-1	2017	Objectives: Mycobacterium tuberculosis and Mycobacterium abscessus produce broad-spectrum class A beta-lactamases, BlaC and Bla Mab , which are inhibited by clavulanate and avibactam, respectively.	Clavulanic Acid	157-168	beta-lactamase	Escherichia coli	115-118	
28039278-4	2017	Methods: Enzyme kinetics were determined to assess the impact of the substitutions G 132 N in BlaC and N 132 G in Bla Mab on beta-lactamase inhibition by clavulanate and avibactam.	Clavulanic Acid	154-165	beta-lactamase	Escherichia coli	94-97	
28039278-8	2017	Bla Mab efficiently hydrolysed clavulanate, but the substitution N 132 G led to a 5600-fold reduction in the hydrolysis rate constant k cat due to stabilization of Bla Mab -clavulanate covalent adducts.	Clavulanic Acid	31-42	beta-lactamase	Escherichia coli	0-3	
28039278-8	2017	Bla Mab efficiently hydrolysed clavulanate, but the substitution N 132 G led to a 5600-fold reduction in the hydrolysis rate constant k cat due to stabilization of Bla Mab -clavulanate covalent adducts.	Clavulanic Acid	173-184	beta-lactamase	Escherichia coli	0-3	
28039278-8	2017	Bla Mab efficiently hydrolysed clavulanate, but the substitution N 132 G led to a 5600-fold reduction in the hydrolysis rate constant k cat due to stabilization of Bla Mab -clavulanate covalent adducts.	Clavulanic Acid	173-184	beta-lactamase	Escherichia coli	164-167