PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21645522-8	2011	Docking of the cephalosporins ceftazidime and cefotaxime into the VIM-2 and VIM-7 structures reveals that amino acid substitutions may cause the mode of substrate binding to differ between the two enzymes.	Cephalosporins	15-29	vimentin	Homo sapiens	66-69	
19901092-8	2010	This enzyme was inhibited by EDTA and hydrolyzed penicillins, cephalosporins, and carbapenems, as observed for other VIM-type carbapenemases but with greater catalytic efficiency against penicillins than VIM-1.	Cephalosporins	62-76	vimentin	Homo sapiens	117-120	
19901092-8	2010	This enzyme was inhibited by EDTA and hydrolyzed penicillins, cephalosporins, and carbapenems, as observed for other VIM-type carbapenemases but with greater catalytic efficiency against penicillins than VIM-1.	Cephalosporins	62-76	vimentin	Homo sapiens	204-207	
18559652-3	2008	A homology model suggests that the VIM-7 Tyr-218 Phe substitution may be responsible for the reduced catalytic efficiency against certain cephalosporins, including ceftazidime and cefepime.	Cephalosporins	138-152	vimentin	Homo sapiens	35-38