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.	Metals	202-207	acyl-CoA synthetase short chain family member 2	Homo sapiens	74-77	
15221484-4	2004	Crystal structures of ACS revealed major differences in protein conformation and in A-cluster composition; for example, a [Fe(4)S(4)] cluster bridged to a binuclear center in which one of the metal binding sites was occupied by Ni, Cu, or Zn.	Metals	192-197	acyl-CoA synthetase short chain family member 2	Homo sapiens	22-25	
11599178-16	2001	ACS epsilon-sequence topology showed greater divergence and less consistency vis-a-vis the other subunits, possibly reflecting reduced evolutionary constraints due to the absence of metal centers.	Metals	182-187	acyl-CoA synthetase short chain family member 2	Homo sapiens	0-3