PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12667067-0	2003	Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery.	Cyclic AMP	29-33	C-reactive protein	Homo sapiens	15-18	
12667067-0	2003	Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery.	Cyclic AMP	29-33	C-reactive protein	Homo sapiens	42-45	
12667067-0	2003	Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery.	Cyclic AMP	29-33	C-reactive protein	Homo sapiens	42-45	
12667067-0	2003	Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery.	Cyclic AMP	46-50	C-reactive protein	Homo sapiens	15-18	
12667067-0	2003	Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery.	Cyclic AMP	46-50	C-reactive protein	Homo sapiens	42-45	
12667067-0	2003	Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery.	Cyclic AMP	46-50	C-reactive protein	Homo sapiens	42-45	
12667067-0	2003	Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery.	Cyclic AMP	46-50	C-reactive protein	Homo sapiens	15-18	
12667067-0	2003	Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery.	Cyclic AMP	46-50	C-reactive protein	Homo sapiens	42-45	
12667067-0	2003	Interaction of CRP L124 with cAMP affects CRP cAMP binding constants, cAMP binding cooperativity, and CRP allostery.	Cyclic AMP	46-50	C-reactive protein	Homo sapiens	42-45	
12667067-4	2003	Wild-type (WT) apo-CRP is a 47 kDa protease-resistant dimer composed of identical subunits that exhibits a biphasic isotherm in cAMP titration studies.	Cyclic AMP	128-132	C-reactive protein	Homo sapiens	19-22	
12667067-5	2003	The WT CRP-cAMP complex is a protease-sensitive dimer degraded by protease to a dimer core that ranges between 26.5 and 30.5 kDa.	Cyclic AMP	11-15	C-reactive protein	Homo sapiens	7-10	
12667067-7	2003	Differences in the affinity of the position 124 CRP variants for cAMP were observed.	Cyclic AMP	65-69	C-reactive protein	Homo sapiens	48-51	
12667067-8	2003	The binding constants that drive the formation of the WT and L124I CRP-cAMP complexes deviated by not more than a factor of 1.5.	Cyclic AMP	71-75	C-reactive protein	Homo sapiens	67-70	
12667067-10	2003	The data indicate that the van der Waals volume and/or the hyrophobicity of the L124 side chain are important determinants of CRP cAMP binding properties and affect, either directly or indirectly, cAMP-mediated conformation changes in CRP.	Cyclic AMP	130-134	C-reactive protein	Homo sapiens	126-129	
12667067-10	2003	The data indicate that the van der Waals volume and/or the hyrophobicity of the L124 side chain are important determinants of CRP cAMP binding properties and affect, either directly or indirectly, cAMP-mediated conformation changes in CRP.	Cyclic AMP	130-134	C-reactive protein	Homo sapiens	235-238	
12667067-10	2003	The data indicate that the van der Waals volume and/or the hyrophobicity of the L124 side chain are important determinants of CRP cAMP binding properties and affect, either directly or indirectly, cAMP-mediated conformation changes in CRP.	Cyclic AMP	197-201	C-reactive protein	Homo sapiens	126-129	
12667067-10	2003	The data indicate that the van der Waals volume and/or the hyrophobicity of the L124 side chain are important determinants of CRP cAMP binding properties and affect, either directly or indirectly, cAMP-mediated conformation changes in CRP.	Cyclic AMP	197-201	C-reactive protein	Homo sapiens	235-238