PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10220355-4	1999	In this paper, we report that several divalent metal cations, such as Mn2+, Co2+, Ni2+, and Zn2+ bind to the second Mg2+-binding site of Csk with up to 13200-fold higher affinity than Mg2+.	Zinc	92-96	C-terminal Src kinase	Homo sapiens	137-140	
10220355-8	1999	Zn2+ has the highest affinity for the second Mg2+-binding site of Csk at 0.65 microM, but supports no kinase activity, acting as a dead-end inhibitor.	Zinc	0-4	C-terminal Src kinase	Homo sapiens	66-69	
11162381-2	2001	Zn2+ can bind to this site to replace Mg2+, which inhibits Csk kinase activity.	Zinc	0-4	C-terminal Src kinase	Homo sapiens	59-62	
11162381-3	2001	The binding is reversible and removal of Zn2+ results in an active Csk apoenzyme.	Zinc	41-45	C-terminal Src kinase	Homo sapiens	67-70	
11162381-6	2001	Since the binding of Csk to Zn2+ is not affected by up to 200 mM NaCl, high ionic strength conditions were used in the purification procedure, minimizing nonspecific binding due to ionic interactions.	Zinc	28-32	C-terminal Src kinase	Homo sapiens	21-24