PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19500590-4	2009	Using metal quantitation methods, we determined that core RAG1 can bind up to four Zn(2+) ions.	Metals	6-11	recombination activating 1	Homo sapiens	58-62	
25903130-5	2015	The assembled RAG1/2 paired complex is active in the presence of Mg(2+), the physiologically relevant metal ion, in nicking and double-strand cleavage of both RSS DNAs to produce a signal-end complex.	Metals	102-107	recombination activating 1	Homo sapiens	14-18	
11390658-4	2001	Formation of stable target capture complexes depends upon the presence of active-site metal binding residues (the DDE motif), suggesting that active-site amino acids in RAG-1 are critical for target capture.	Metals	86-91	recombination activating 1	Homo sapiens	169-174	
18380906-0	2008	HMG-box domain stimulation of RAG1/2 cleavage activity is metal ion dependent.	Metals	58-63	recombination activating 1	Homo sapiens	30-34	
11971977-2	2002	RAG-1 contains three acidic active-site amino acids that are thought to coordinate catalytic metal ions.	Metals	93-98	recombination activating 1	Homo sapiens	0-5	
10678172-5	2000	The results support a model in which RAG1 contains a single, divalent metal ion binding active site structurally related to the active sites of transposases/integrases and responsible for all catalytic functions of the RAG protein complex.	Metals	70-75	recombination activating 1	Homo sapiens	37-41	
9671477-6	1998	Unlike the binding of RAG1 plus RAG2, RAG1 can bind to DNA in the absence of a divalent metal ion and does not require the presence of coding flank sequence.	Metals	88-93	recombination activating 1	Homo sapiens	38-42	
10601032-9	1999	These data suggest that RAG-mediated DNA cleavage involves coordination of divalent metal ion(s) by RAG1.	Metals	84-89	recombination activating 1	Homo sapiens	100-104