PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18373354-2	2008	Glu162 in homotetrameric human MnSOD spans a dimeric interface and forms a hydrogen bond with His163 of an adjacent subunit which is a direct ligand of the manganese.	Hydrogen	75-83	superoxide dismutase 2	Homo sapiens	31-36	
18373354-4	2008	The X-ray crystal structures of E162D and E162A MnSOD reveal no significant structural changes compared with the wild type other than the removal of the hydrogen bond interaction with His163 in E162A MnSOD.	Hydrogen	153-161	superoxide dismutase 2	Homo sapiens	200-205	
18373354-5	2008	In the case of E162D MnSOD, an intervening solvent molecule fills the void created by the mutation to conserve the hydrogen bond interaction between His163 and residue 162.	Hydrogen	115-123	superoxide dismutase 2	Homo sapiens	21-26	
18373354-8	2008	Differential scanning calorimetry indicates that the hydrogen bond between Glu162 and His163 contributes to the stability of MnSOD, with the major unfolding transition occurring at 81 degrees C for E162A compared to 90 degrees C for wild-type MnSOD.	Hydrogen	53-61	superoxide dismutase 2	Homo sapiens	125-130	
18373354-8	2008	Differential scanning calorimetry indicates that the hydrogen bond between Glu162 and His163 contributes to the stability of MnSOD, with the major unfolding transition occurring at 81 degrees C for E162A compared to 90 degrees C for wild-type MnSOD.	Hydrogen	53-61	superoxide dismutase 2	Homo sapiens	243-248