PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15276840-1	2004	The structure of Mycobacterium tuberculosis dUTP nucleotidohydrolase (dUTPase) has been determined at 1.3 Angstrom resolution in complex with magnesium ion and the non-hydrolyzable substrate analog, alpha,beta-imido dUTP.	Magnesium	142-151	Deoxyuridine triphosphatase	Drosophila melanogaster	70-77	
23040389-6	2012	For Tpa dUTPase activity, we determined an optimum pH of 8.5 and temperature of 85  C. Magnesium ions strongly induced activity, with an optimum concentration of 0.75 mM.	Magnesium	87-96	Deoxyuridine triphosphatase	Drosophila melanogaster	8-15	
15364583-5	2004	The X-ray structure of the C.jejuni dUTPase in complex with the non-hydrolysable substrate analogue dUpNHp allows us to define the positions of three catalytically significant phosphate-binding magnesium ions and provides a starting point for a detailed understanding of the mechanism of dUTP/dUDP hydrolysis by dimeric dUTPases.	Magnesium	194-203	Deoxyuridine triphosphatase	Drosophila melanogaster	36-43