PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9636056-19	1998	Significantly, the Ca2+ affinity of the oncomodulin CD site is increased by mutations that weaken binding at the EF site, indicating a negatively cooperative interaction between the two sites.	Cadmium	52-54	oncomodulin	Homo sapiens	40-51	
9636056-0	1998	Interconversion of the ligand arrays in the CD and EF sites of oncomodulin.	Cadmium	44-46	oncomodulin	Homo sapiens	63-74	
7827057-0	1995	Interconversion of the CD and EF sites in oncomodulin.	Cadmium	23-25	oncomodulin	Homo sapiens	42-53	
8639547-5	1996	Interestingly, for oncomodulin, we observe that introduction of a fifth carboxylate residue at the +z position in the CD coordination sphere or at the -x position in the EF coordination sphere significantly increases the affinity of those sites for Ca2+.	Cadmium	118-120	oncomodulin	Homo sapiens	19-30	
7628071-2	1995	DESIGN AND METHODS: A mutant of oncomodulin with a cysteine residue at position 57 located in the CD binding loop was conjugated to a salicylic acid group.	Cadmium	98-100	oncomodulin	Homo sapiens	32-43	
7827057-7	1995	As in other parvalbumins, the liganding residues in the CD and EF sites of oncomodulin differ at the +z and -x coordination positions: serine and aspartate, respectively, in the CD site; aspartate and glycine in the EF site.	Cadmium	56-58	oncomodulin	Homo sapiens	75-86	
7827057-7	1995	As in other parvalbumins, the liganding residues in the CD and EF sites of oncomodulin differ at the +z and -x coordination positions: serine and aspartate, respectively, in the CD site; aspartate and glycine in the EF site.	Cadmium	178-180	oncomodulin	Homo sapiens	75-86	
7827057-20	1995	In wild-type oncomodulin, the CD site signal dominates the low-pH spectrum.	Cadmium	30-32	oncomodulin	Homo sapiens	13-24	
3571255-5	1987	Lineshape analyses of several 1H NMR resonances generated by the Lu(III) titration of Ca2-oncomodulin indicated that Ca(II)----Ln(III) exchange at the CD site was 15-20 s-1, approximately 100 times faster than exchange at the CD site of parvalbumins.	Cadmium	151-153	oncomodulin	Homo sapiens	90-101	
24233453-1	1994	The Ca(2+)-binding protein oncomodulin was altered by cassette mutagenesis of the CD site (CDOM33) with a sequence that was derived by a consensus method using over 250 known Ca(2+)-binding loop sequences.	Cadmium	82-84	oncomodulin	Homo sapiens	27-38	
8489002-1	1993	In this study, the CD loop of the Ca(2+)-binding protein oncomodulin was replaced by a high-affinity, metal-binding sequence that was found to reverse the order of fill of the two sites in the protein.	Cadmium	19-21	oncomodulin	Homo sapiens	57-68	
2108959-11	1990	The characteristics of Ca2+ binding to the specific site (likely the CD domain) are different from those of the Ca2+ specific sites in troponin C and in calmodulin and suggest that in oncomodulin hydrophobic forces do not play a predominant role in the binding process at the specific site.	Cadmium	69-71	oncomodulin	Homo sapiens	184-195	
3571255-5	1987	Lineshape analyses of several 1H NMR resonances generated by the Lu(III) titration of Ca2-oncomodulin indicated that Ca(II)----Ln(III) exchange at the CD site was 15-20 s-1, approximately 100 times faster than exchange at the CD site of parvalbumins.	Cadmium	226-228	oncomodulin	Homo sapiens	90-101	
3571255-8	1987	We attribute part of the reduced preference of small Ln(III)s for the CD site of oncomodulin to a combination of this site"s inherent incompressibility (Williams, T.C., Corson, D.C. & Sykes, B.D.	Cadmium	70-72	oncomodulin	Homo sapiens	81-92	
3571255-14	1987	Like the CD site in oncomodulin, site III in troponin C has not only a lower affinity for calcium relative to the CD site of parvalbumins but also aspartic acid at its -X position; a water molecule bridges the gap between bound metal and the carboxyl group of the relatively short side chain of Asp-114 (Herzberg, O.	Cadmium	9-11	oncomodulin	Homo sapiens	20-31	
3571255-16	1987	Hence, we suggest that Asp-59 in oncomodulin binds metal only indirectly through an intervening water molecule, a proposal which is consistent with the CD site"s reduced affinity for ions the size of Ca(II) or smaller.	Cadmium	152-154	oncomodulin	Homo sapiens	33-44