PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10346816-0	1999	Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex.	Adenosine Triphosphate	17-20	MRE11 homolog, double strand break repair nuclease	Homo sapiens	75-80	
10346816-0	1999	Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex.	Adenosine Triphosphate	17-20	nibrin	Homo sapiens	0-4	
10346816-0	1999	Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex.	Adenosine Triphosphate	17-20	RAD50 double strand break repair protein	Homo sapiens	81-86	
10346816-5	1999	On nonhairpin DNA ends, ATP controls a switch in endonuclease specificity that allows Mre11/Rad50/Nbs1 to cleave a 3"-protruding strand at a double-/single-strand transition.	Adenosine Triphosphate	24-27	MRE11 homolog, double strand break repair nuclease	Homo sapiens	86-91	
10346816-5	1999	On nonhairpin DNA ends, ATP controls a switch in endonuclease specificity that allows Mre11/Rad50/Nbs1 to cleave a 3"-protruding strand at a double-/single-strand transition.	Adenosine Triphosphate	24-27	RAD50 double strand break repair protein	Homo sapiens	92-97	
10346816-5	1999	On nonhairpin DNA ends, ATP controls a switch in endonuclease specificity that allows Mre11/Rad50/Nbs1 to cleave a 3"-protruding strand at a double-/single-strand transition.	Adenosine Triphosphate	24-27	nibrin	Homo sapiens	98-102	
10346816-6	1999	Mutational analysis demonstrates that Rad50 is responsible for ATP binding by the complex, but the ATP-dependent activities are expressed only with Nbs1 present.	Adenosine Triphosphate	63-66	RAD50 double strand break repair protein	Homo sapiens	38-43	
10346816-6	1999	Mutational analysis demonstrates that Rad50 is responsible for ATP binding by the complex, but the ATP-dependent activities are expressed only with Nbs1 present.	Adenosine Triphosphate	99-102	nibrin	Homo sapiens	148-152