PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29680579-4	2018	Most MBL inhibitors target active site zinc ions and vary in mechanism from ternary complex formation to metal ion stripping.	Metals	105-110	mannose-binding lectin family member 3, pseudogene	Homo sapiens	5-8	
34864439-6	2022	However, newer MBL variants incorporate mutations that improve their metal binding abilities or stabilize the metal-depleted form, revealing that metal starvation is a driving force acting on MBL evolution.	Metals	69-74	mannose-binding lectin family member 3, pseudogene	Homo sapiens	15-18	
34864439-6	2022	However, newer MBL variants incorporate mutations that improve their metal binding abilities or stabilize the metal-depleted form, revealing that metal starvation is a driving force acting on MBL evolution.	Metals	69-74	mannose-binding lectin family member 3, pseudogene	Homo sapiens	192-195	
34864439-6	2022	However, newer MBL variants incorporate mutations that improve their metal binding abilities or stabilize the metal-depleted form, revealing that metal starvation is a driving force acting on MBL evolution.	Metals	110-115	mannose-binding lectin family member 3, pseudogene	Homo sapiens	15-18	
34864439-6	2022	However, newer MBL variants incorporate mutations that improve their metal binding abilities or stabilize the metal-depleted form, revealing that metal starvation is a driving force acting on MBL evolution.	Metals	110-115	mannose-binding lectin family member 3, pseudogene	Homo sapiens	192-195	
34864439-6	2022	However, newer MBL variants incorporate mutations that improve their metal binding abilities or stabilize the metal-depleted form, revealing that metal starvation is a driving force acting on MBL evolution.	Metals	146-151	mannose-binding lectin family member 3, pseudogene	Homo sapiens	15-18	
34864439-6	2022	However, newer MBL variants incorporate mutations that improve their metal binding abilities or stabilize the metal-depleted form, revealing that metal starvation is a driving force acting on MBL evolution.	Metals	146-151	mannose-binding lectin family member 3, pseudogene	Homo sapiens	192-195	
32100311-4	2020	This review provides a detailed description of interaction modes of substrates and small-molecule inhibitors with various MBL enzymes and highlights the importance of metal- and "anchor residue"-binding features to achieve broad-spectrum MBL inhibition.	Metals	167-172	mannose-binding lectin family member 3, pseudogene	Homo sapiens	122-125	
32100311-4	2020	This review provides a detailed description of interaction modes of substrates and small-molecule inhibitors with various MBL enzymes and highlights the importance of metal- and "anchor residue"-binding features to achieve broad-spectrum MBL inhibition.	Metals	167-172	mannose-binding lectin family member 3, pseudogene	Homo sapiens	238-241	
32100311-6	2020	The metalloenzyme selectivity, metal-binding pharmacophore, and cellular permeability and accumulation should be properly considered in the further development of clinically useful inhibitors to combat MBL-mediated antibacterial resistance.	Metals	4-9	mannose-binding lectin family member 3, pseudogene	Homo sapiens	202-205	
34181945-5	2021	We investigated the kinetics of MBL inactivation in detail and report that AMA is a selective Zn2+ scavenger that indirectly inactivates NDM-1 by encouraging the dissociation of a metal cofactor.	Metals	180-185	mannose-binding lectin family member 3, pseudogene	Homo sapiens	32-35	
29271657-2	2018	We report how application of in silico fragment-based molecular design employing thiol-mediated metal anchorage leads to potent MBL inhibitors.	Metals	96-101	mannose-binding lectin family member 3, pseudogene	Homo sapiens	128-131	
26517410-1	2016	Metallo Beta (beta) Lactamases (MBL) are metal dependent bacterial enzymes that hydrolyze the beta-lactam antibiotics.	Metals	41-46	mannose-binding lectin family member 3, pseudogene	Homo sapiens	32-35