PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29610205-6	2018	Upon molecular dynamics simulations of relebactam in the KPC-2 active site, we found that the positioning of active-site water molecules is less favorable for desulfation in the KPC-2 active site than it is in the KPC-2-avibactam complex.	Water	121-126	carbapenem-hydrolyzing beta-lactamase KPC-2	Klebsiella pneumoniae	57-62	
33373730-0	2021	Complete genome sequencing and comparative plasmid analysis of KPC-2-producing Klebsiella pneumoniae isolated from a hospital sewage water in Japan.	Water	133-138	carbapenem-hydrolyzing beta-lactamase KPC-2	Klebsiella pneumoniae	63-68	
33373730-4	2021	METHODS: KPC-2-producing K. pneumoniae was isolated from a hospital sewage water in Japan in 2018.	Water	75-80	carbapenem-hydrolyzing beta-lactamase KPC-2	Klebsiella pneumoniae	9-14	
29610205-6	2018	Upon molecular dynamics simulations of relebactam in the KPC-2 active site, we found that the positioning of active-site water molecules is less favorable for desulfation in the KPC-2 active site than it is in the KPC-2-avibactam complex.	Water	121-126	carbapenem-hydrolyzing beta-lactamase KPC-2	Klebsiella pneumoniae	178-183	
29610205-6	2018	Upon molecular dynamics simulations of relebactam in the KPC-2 active site, we found that the positioning of active-site water molecules is less favorable for desulfation in the KPC-2 active site than it is in the KPC-2-avibactam complex.	Water	121-126	carbapenem-hydrolyzing beta-lactamase KPC-2	Klebsiella pneumoniae	178-183	
26340563-8	2015	Our observations provide a possible reason for the ability of KPC-2 beta-lactamase to slowly desulfate avibactam with a potential role for the stereochemistry around the N1 atom of avibactam and/or the presence of an active site water molecule that could aid in avibactam desulfation, an unexpected consequence of novel inhibition chemistry.	Water	229-234	carbapenem-hydrolyzing beta-lactamase KPC-2	Klebsiella pneumoniae	62-67