PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34944467-5	2021	Using competitive binding experiments between Ca2+ and Zn2+ and QM/MM molecular modeling we conclude that Zn2+ high affinity sites are located in the EF-hand motifs of S100A1.	Zinc	55-59	carbonic anhydrase 2	Homo sapiens	46-49	
34944467-5	2021	Using competitive binding experiments between Ca2+ and Zn2+ and QM/MM molecular modeling we conclude that Zn2+ high affinity sites are located in the EF-hand motifs of S100A1.	Zinc	106-110	carbonic anhydrase 2	Homo sapiens	46-49	
34944467-6	2021	In addition, two lower affinity sites can bind Zn2+ even when the EF-hands are saturated by Ca2+, resulting in a 2Ca2+:S100A1:2Zn2+ conformer.	Zinc	47-51	carbonic anhydrase 2	Homo sapiens	92-95	
34944467-8	2021	We also determined a higher affinity to Ca2+ (KD~0.16 and 24 mum) than was previously reported for S100A1, which would allow this protein to function as a Ca2+/Zn2+-sensor both inside and outside cells, participating in diverse signaling pathways under normal and pathological conditions.	Zinc	160-164	carbonic anhydrase 2	Homo sapiens	40-43	
34944467-8	2021	We also determined a higher affinity to Ca2+ (KD~0.16 and 24 mum) than was previously reported for S100A1, which would allow this protein to function as a Ca2+/Zn2+-sensor both inside and outside cells, participating in diverse signaling pathways under normal and pathological conditions.	Zinc	160-164	carbonic anhydrase 2	Homo sapiens	155-158