PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16459335-8	2006	These cephalosporins exhibit substantially smaller dissociation constants for the preacylation complex compared with the case of typical cephalosporins, but their pseudo-second-order rate constants for encounter with PBP 2a (k(2)/K(s)) are not very large (< or =200 m(-1) s(-1)).	Cephalosporins	6-20	AT695_RS11765	Staphylococcus aureus	217-220	
11796337-1	2002	RWJ-54428 (MC-02479) is a novel cephalosporin that binds to penicillin-binding protein (PBP) PBP 2" (PBP 2a) of methicillin-resistant staphylococci.	Cephalosporins	32-45	AT695_RS11765	Staphylococcus aureus	60-86	
11796337-1	2002	RWJ-54428 (MC-02479) is a novel cephalosporin that binds to penicillin-binding protein (PBP) PBP 2" (PBP 2a) of methicillin-resistant staphylococci.	Cephalosporins	32-45	AT695_RS11765	Staphylococcus aureus	88-91	
11796337-1	2002	RWJ-54428 (MC-02479) is a novel cephalosporin that binds to penicillin-binding protein (PBP) PBP 2" (PBP 2a) of methicillin-resistant staphylococci.	Cephalosporins	32-45	AT695_RS11765	Staphylococcus aureus	93-96	
11796337-1	2002	RWJ-54428 (MC-02479) is a novel cephalosporin that binds to penicillin-binding protein (PBP) PBP 2" (PBP 2a) of methicillin-resistant staphylococci.	Cephalosporins	32-45	AT695_RS11765	Staphylococcus aureus	93-96	
19180259-1	2008	Ceftobiprole is a novel parenteral cephalosporin with high affinity for most penicillin-binding proteins, including the mecA product penicillin-binding protein (PBP) 2a, rendering it active against methicillin-resistant staphylococci.	Cephalosporins	35-48	AT695_RS11765	Staphylococcus aureus	77-103	
19180259-1	2008	Ceftobiprole is a novel parenteral cephalosporin with high affinity for most penicillin-binding proteins, including the mecA product penicillin-binding protein (PBP) 2a, rendering it active against methicillin-resistant staphylococci.	Cephalosporins	35-48	AT695_RS11765	Staphylococcus aureus	161-164	
16459335-9	2006	It is documented herein that these cephalosporins facilitate a conformational change in PBP 2a, a process that is enhanced in the presence of a synthetic surrogate for cell wall, resulting in increases in the k(2)/K(s) parameter and in more facile enzyme inhibition.	Cephalosporins	35-49	AT695_RS11765	Staphylococcus aureus	88-91	
16459335-10	2006	These findings argue that the novel cephalosporins are able to co-opt interactions between PBP 2a and the cell wall in gaining access to the active site in the inhibition process, a set of events that leads to effective inhibition of PBP 2a and the attendant killing of the MRSA strains.	Cephalosporins	36-50	AT695_RS11765	Staphylococcus aureus	91-94	
16459335-10	2006	These findings argue that the novel cephalosporins are able to co-opt interactions between PBP 2a and the cell wall in gaining access to the active site in the inhibition process, a set of events that leads to effective inhibition of PBP 2a and the attendant killing of the MRSA strains.	Cephalosporins	36-50	AT695_RS11765	Staphylococcus aureus	234-237