PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28634231-0	2017	Hyperactivity of the Arabidopsis cryptochrome (cry1) L407F mutant is caused by a structural alteration close to the cry1 ATP-binding site.	Adenosine Triphosphate	121-124	cryptochrome 1	Arabidopsis thaliana	47-51	
28634231-0	2017	Hyperactivity of the Arabidopsis cryptochrome (cry1) L407F mutant is caused by a structural alteration close to the cry1 ATP-binding site.	Adenosine Triphosphate	121-124	cryptochrome 1	Arabidopsis thaliana	116-120	
28634231-5	2017	The previously characterized L407F mutant allele of Arabidopsis cry1 is biologically hyperactive and seems to mimic the ATP-bound state of cry1, but the reason for this phenotypic change is unclear.	Adenosine Triphosphate	120-123	cryptochrome 1	Arabidopsis thaliana	64-68	
28634231-5	2017	The previously characterized L407F mutant allele of Arabidopsis cry1 is biologically hyperactive and seems to mimic the ATP-bound state of cry1, but the reason for this phenotypic change is unclear.	Adenosine Triphosphate	120-123	cryptochrome 1	Arabidopsis thaliana	139-143	
28634231-6	2017	Here, we show that cry1L407F can still bind ATP, has less pronounced photoreduction and formation of FADH  than wild-type cry1, and has a dark reversion rate 1.7 times lower than that of the wild type.	Adenosine Triphosphate	44-47	cryptochrome 1	Arabidopsis thaliana	19-23	
28634231-8	2017	Moreover, we show that ATP binds to cry1 in both the dark and the lit states.	Adenosine Triphosphate	23-26	cryptochrome 1	Arabidopsis thaliana	36-40	
28634231-10	2017	Finally, we show that a recently discovered chemical inhibitor of cry1, 3-bromo-7-nitroindazole, competes for ATP binding and thereby diminishes FADH  formation, which demonstrates that both processes are important for cry1 function.	Adenosine Triphosphate	110-113	cryptochrome 1	Arabidopsis thaliana	66-70	
28634231-10	2017	Finally, we show that a recently discovered chemical inhibitor of cry1, 3-bromo-7-nitroindazole, competes for ATP binding and thereby diminishes FADH  formation, which demonstrates that both processes are important for cry1 function.	Adenosine Triphosphate	110-113	cryptochrome 1	Arabidopsis thaliana	219-223