PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15254036-5	2004	However, the CaM probe displayed large spatial fluctuations (presence of ATP but not ADP or no nucleotide) around the mean position, whereas the motor domain probe did not.	Adenosine Triphosphate	73-76	calmodulin 3	Homo sapiens	13-16	
9760234-5	1998	We report here similar scattering experiments on the CaM.MLCK complex with the addition of substrates; a nonhydrolyzable analogue of adenosine-triphosphate, AMPPNP, and a peptide substrate for MLCK, a phosphorylation sequence from myosin regulatory light chain (pRLC).	Adenosine Triphosphate	133-155	calmodulin 3	Homo sapiens	53-56	
11790804-8	2002	Peptide (AIP) and lipophilic (KN-62) protein kinase inhibitors prevented the Ca(2+)/CaM-induced changes in channel gating without altering basal Ca(v)3.2 channel activity (27 nM free Ca(2+)) as did replacing pipette ATP with adenylyl imidodiphosphate (AMP-PNP), a non-hydrolysable analogue.	Adenosine Triphosphate	216-219	calmodulin 3	Homo sapiens	84-87	
1993676-1	1991	Autophosphorylation of calmodulin (CaM)-dependent protein kinase II (CaM-kinase II) under limiting conditions (2 microM ATP) decreased progressively with increasing concentrations of a substrate, Pro-Leu-Ala-Arg-Thr-Leu-Ser-Val-Ala-Gly-Leu-Pro-Gly-Lys-Lys (syntide-2), suggesting a competition between the substrate and the autophosphorylation site(s) of the enzyme.	Adenosine Triphosphate	120-123	calmodulin 3	Homo sapiens	35-38	
1993676-1	1991	Autophosphorylation of calmodulin (CaM)-dependent protein kinase II (CaM-kinase II) under limiting conditions (2 microM ATP) decreased progressively with increasing concentrations of a substrate, Pro-Leu-Ala-Arg-Thr-Leu-Ser-Val-Ala-Gly-Leu-Pro-Gly-Lys-Lys (syntide-2), suggesting a competition between the substrate and the autophosphorylation site(s) of the enzyme.	Adenosine Triphosphate	120-123	calmodulin 3	Homo sapiens	69-72