PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10066748-3	1999	The binding reactions of the DNA duplexes to the fully cNMP-ligated CRP-mutant complexes were endothermic with binding constants as high as 6.6 +/- 1.1 x 10(6) M-1 (conDNA.CRP(cAMP)2).	Cyclic AMP	176-180	C-reactive protein	Homo sapiens	68-71	
10066748-3	1999	The binding reactions of the DNA duplexes to the fully cNMP-ligated CRP-mutant complexes were endothermic with binding constants as high as 6.6 +/- 1.1 x 10(6) M-1 (conDNA.CRP(cAMP)2).	Cyclic AMP	176-180	C-reactive protein	Homo sapiens	172-175	
10066748-4	1999	ConDNA binding to the unligated T127L and CRP* mutants was observed as well as conDNA and lacDNA binding to CRP with cAMP bound to only one monomer.	Cyclic AMP	117-121	C-reactive protein	Homo sapiens	108-111	
10066748-5	1999	The reduction of the binding constants with increase in KCl concentration indicated the formation of two ion pairs for the cAMP-ligated CRP and S128A complexes and four ion pairs for the cAMP-ligated T127L and CRP* complexes.	Cyclic AMP	123-127	C-reactive protein	Homo sapiens	136-139	
10066748-5	1999	The reduction of the binding constants with increase in KCl concentration indicated the formation of two ion pairs for the cAMP-ligated CRP and S128A complexes and four ion pairs for the cAMP-ligated T127L and CRP* complexes.	Cyclic AMP	187-191	C-reactive protein	Homo sapiens	210-213	
10066748-7	1999	Small angle neutron scattering measurements on the lacDNA.CRP(cAMP)2 complex in D2O/H2O mixtures show that the DNA is bent around the cAMP-ligated protein in solution.	Cyclic AMP	62-66	C-reactive protein	Homo sapiens	58-61