PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14735332-8	2004	Significantly,5 maintains the key features observed in the active site of ACS, namely a square-planar Ni coordinated to two deprotonated amides and two thiolates, where the thiolates bridge to a second metal, suggesting that 5 is a reasonable structural model for this unique enzyme.	Amides	137-143	acyl-CoA synthetase short chain family member 2	Homo sapiens	74-77	
14735332-0	2004	Modeling carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS): a trinuclear nickel complex employing deprotonated amides and bridging thiolates.	Amides	122-128	acyl-CoA synthetase short chain family member 2	Homo sapiens	60-69	
14735332-1	2004	Carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) utilizes a unique Ni-M bimetallic site in the biosynthesis of acetyl-CoA, where a square-planar Ni ion is coordinated to two thiolates and two deprotonated amides in a Cys-Gly-Cys motif.	Amides	217-223	acyl-CoA synthetase short chain family member 2	Homo sapiens	51-59	
34917239-0	2021	Amide-Substituted Condensed Pyridine Derivatives as ACSS2 Inhibitors for Treating Cancer.	Amides	0-5	acyl-CoA synthetase short chain family member 2	Homo sapiens	52-57	
21666847-1	2011	Nickel Superoxide Dismutase (NiSOD) and the A-cluster of Carbon Monoxide Dehydrogenase/Acetyl Coenzyme A Synthase (CODH/ACS) both feature active sites with Ni coordinated by thiolate and amide donors.	Amides	187-192	acyl-CoA synthetase short chain family member 2	Homo sapiens	115-123