PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21291269-5	2011	In an effort to identify potential target sites for disruption of the CDK-cyclin interaction, we probed the extrinsic fluorophore 8-anilino-1-naphthalene sulfonate (ANS) with human CDK2 and cyclin A using fluorescence spectroscopy and protein crystallography.	8-anilino-1-naphthalenesulfonic acid	130-163	cyclin A2	Homo sapiens	190-198	
21291269-5	2011	In an effort to identify potential target sites for disruption of the CDK-cyclin interaction, we probed the extrinsic fluorophore 8-anilino-1-naphthalene sulfonate (ANS) with human CDK2 and cyclin A using fluorescence spectroscopy and protein crystallography.	8-anilino-1-naphthalenesulfonic acid	165-168	cyclin A2	Homo sapiens	190-198	
21291269-6	2011	ANS interacts with free CDK2 in a saturation-dependent manner with an apparent K(d) of 37 muM, and cyclin A displaced ANS from CDK2 with an EC(50) value of 0.6 muM.	8-anilino-1-naphthalenesulfonic acid	118-121	cyclin A2	Homo sapiens	99-107	
21291269-8	2011	Binding of ANS is accompanied by substantial structural changes in CDK2, resulting in a C-helix conformation that is incompatible for cyclin A association.	8-anilino-1-naphthalenesulfonic acid	11-14	cyclin A2	Homo sapiens	134-142