PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28607419-5	2017	The study allows the thorough analysis of the opening events at the atomic scale: i) ATP hydrolysis at the Smc1A site, evaluating the role of the carboxy-terminal domain of Rad21 in the process; ii) the activation of the Smc3 site potentially mediated by the movement of specific amino acids; and iii) opening of the head domains after the two ATP hydrolysis events.	Adenosine Triphosphate	344-347	structural maintenance of chromosomes 3	Homo sapiens	221-225	
31201089-3	2019	Using in vivo cysteine cross-linking, we show that when Smc1 and Smc3 ATPases are engaged in the presence of ATP (E heads), cohesin rings generate a "SMC (S) compartment" between hinge and E heads and a "kleisin (K) compartment" between E heads and their associated kleisin subunit.	Adenosine Triphosphate	70-73	structural maintenance of chromosomes 3	Homo sapiens	65-69	
28607419-6	2017	Our study suggests that the cohesin ring opening is triggered by a sequential activation of the ATP sites in which ATP hydrolysis at the Smc1A site induces ATPase activity at the Smc3 site.	Adenosine Triphosphate	96-99	structural maintenance of chromosomes 3	Homo sapiens	179-183	
28607419-6	2017	Our study suggests that the cohesin ring opening is triggered by a sequential activation of the ATP sites in which ATP hydrolysis at the Smc1A site induces ATPase activity at the Smc3 site.	Adenosine Triphosphate	115-118	structural maintenance of chromosomes 3	Homo sapiens	179-183	
25220052-9	2014	Subsequently, ATP hydrolysis by cohesin leads to entrapment of DNA and converts Smc3 into a state that can be acetylated.	Adenosine Triphosphate	14-17	structural maintenance of chromosomes 3	Homo sapiens	80-84	
17055978-7	2006	RESULTS: Characterization of cohesin"s ATPase activity suggests that hydrolysis depends on the binding of ATP to both Smc1 and Smc3 heads.	Adenosine Triphosphate	39-42	structural maintenance of chromosomes 3	Homo sapiens	127-131	
17055978-9	2006	We show that the C-terminal winged-helix domain of Scc1 stimulates the ATPase activity of the Smc1/Smc3 heterodimer by promoting ATP binding to Smc1"s head.	Adenosine Triphosphate	71-74	structural maintenance of chromosomes 3	Homo sapiens	99-103	
14614819-5	2003	RESULTS: To investigate the role of Smc1 and Smc3"s ATPase domains, we engineered smc1 and smc3 mutations predicted to abolish either ATP binding or hydrolysis.	Adenosine Triphosphate	52-55	structural maintenance of chromosomes 3	Homo sapiens	45-49	
34624221-5	2021	Our results suggest that DNA is translocated by a spontaneous 50 nm-swing of cohesin"s hinge, which hands DNA over to the ATPase head of SMC3, where upon binding of ATP, DNA is clamped by NIPBL.	Adenosine Triphosphate	165-168	structural maintenance of chromosomes 3	Homo sapiens	137-141	
34624221-6	2021	During this process, NIPBL "jumps ship" from the hinge toward the SMC3 head and might thereby couple the spontaneous hinge swing to ATP-dependent DNA clamping.	Adenosine Triphosphate	132-135	structural maintenance of chromosomes 3	Homo sapiens	66-70	
27307603-8	2016	We show by molecular dynamics and biochemistry that wild-type Smc3 can adopt distinct conformations, and that adenosine triphosphate (ATP) induces the conformational change.	Adenosine Triphosphate	110-132	structural maintenance of chromosomes 3	Homo sapiens	62-66	
27307603-8	2016	We show by molecular dynamics and biochemistry that wild-type Smc3 can adopt distinct conformations, and that adenosine triphosphate (ATP) induces the conformational change.	Adenosine Triphosphate	134-137	structural maintenance of chromosomes 3	Homo sapiens	62-66	
34259632-2	2021	This involves DNA being "clamped" by Scc2 and ATP-dependent engagement of cohesin"s Smc1 and Smc3 head domains.	Adenosine Triphosphate	46-49	structural maintenance of chromosomes 3	Homo sapiens	93-97