PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
15535684-6	2004	The present Ni-Ni systems replicate the structural and chemical properties of the A-cluster site in ACS/CODH and support the presence of Ni at Mp in the catalytically active enzyme.	ni-ni	12-17	acyl-CoA synthetase short chain family member 2	Homo sapiens	100-108
29808216-6	2018	Through analysing the difference between the cohesive energy and the clustering energy, we show the preference of Ni-Ni bond formation over Ni-surface interaction; this energy difference decreases with the increase of the Nin cluster size.	ni-ni	114-119	ninein	Homo sapiens	222-225
15221484-5	2004	Recent studies have revealed Ni-Ni to be the active state, unveiled the source of the heterogeneity that had plagued studies of CODH/ACS for decades, and produced a metal-replacement strategy to generate highly active and nearly homogeneous enzyme.	ni-ni	29-34	acyl-CoA synthetase short chain family member 2	Homo sapiens	133-136