PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34021366-1	2021	We have generated a mutant of C. elegans manganese superoxide dismutase at histidine 30 by site-directed mutagenesis.	Histidine	75-84	superoxide dismutase 2	Homo sapiens	41-71	
9685724-6	1998	Amino acid substitutions at a signal peptide-cleavage site, His-Ser-Leu4 to Pro-Met-Va14, in the mature Mn-SOD prevented the processing of the precursor protein, and thus resulted in the accumulation of the precursor protein within mitochondria, as judged on immunostaining with an anti-Mn-SOD antibody.	Histidine	60-63	superoxide dismutase 2	Homo sapiens	104-110	
9685724-6	1998	Amino acid substitutions at a signal peptide-cleavage site, His-Ser-Leu4 to Pro-Met-Va14, in the mature Mn-SOD prevented the processing of the precursor protein, and thus resulted in the accumulation of the precursor protein within mitochondria, as judged on immunostaining with an anti-Mn-SOD antibody.	Histidine	60-63	superoxide dismutase 2	Homo sapiens	287-293	
28165386-5	2017	Markedly, oxidative modifications of MNSOD were identified at histidine (H54 and H55), tyrosine (Y58), tryptophan (W147, W149, W205 and W210) and asparagine (N206 and N209) residues additional to methionine.	Histidine	62-71	superoxide dismutase 2	Homo sapiens	37-42	
23461587-4	2013	The major differences between the QM/MM optimized active sites of WT MnSOD and Mn(Fe)SOD are a smaller (His)N-Mn-N(His) equatorial angle and a longer (Gln146(69))NH   O(sol) H-bond distance in the metal-substituted protein.	Histidine	104-107	superoxide dismutase 2	Homo sapiens	69-74	
23461587-4	2013	The major differences between the QM/MM optimized active sites of WT MnSOD and Mn(Fe)SOD are a smaller (His)N-Mn-N(His) equatorial angle and a longer (Gln146(69))NH   O(sol) H-bond distance in the metal-substituted protein.	Histidine	104-107	superoxide dismutase 2	Homo sapiens	71-74	
10488113-1	1999	Histidine 30 in human manganese superoxide dismutase (MnSOD) is located at a site partially exposed to solvent with its side chain participating in a hydrogen-bonded network that includes the active-site residues Tyr(166) and Tyr(34) and extends to the manganese-bound solvent molecule.	Histidine	0-9	superoxide dismutase 2	Homo sapiens	22-52	
15128298-6	2004	The coding sequences were expressed in Escherichia coli as six-histidine tagged recombinant proteins and generated products with molecular masses of 86.1 kDa for HSP and 22.4 kDa for MnSOD.	Histidine	63-72	superoxide dismutase 2	Homo sapiens	183-188	
12651009-6	2003	The purification of MnSOD was performed by chromatography applying the His-tag technology.	Histidine	71-74	superoxide dismutase 2	Homo sapiens	20-25	
12627943-0	2003	Catalytic and structural effects of amino acid substitution at histidine 30 in human manganese superoxide dismutase: insertion of valine C gamma into the substrate access channel.	Histidine	63-72	superoxide dismutase 2	Homo sapiens	85-115	
11912930-5	2002	The active site of MnSOD is dominated by a hydrogen bond network comprising the manganese-bound aqueous ligand, the side chains of four residues (Gln-143, Tyr-34, His-30, and Tyr-166 from an adjacent subunit), as well as other water molecules.	Histidine	163-166	superoxide dismutase 2	Homo sapiens	19-24	
16910776-4	2006	To examine this question, we used site-directed mutagenesis to produce a mutant form of human MnSOD that has a leucine at amino acid 26 in the active site rather than the usual histidine.	Histidine	177-186	superoxide dismutase 2	Homo sapiens	94-99	
10488113-1	1999	Histidine 30 in human manganese superoxide dismutase (MnSOD) is located at a site partially exposed to solvent with its side chain participating in a hydrogen-bonded network that includes the active-site residues Tyr(166) and Tyr(34) and extends to the manganese-bound solvent molecule.	Histidine	0-9	superoxide dismutase 2	Homo sapiens	54-59	
10488113-2	1999	We have replaced His(30) with a series of amino acids and Tyr(166) with Phe in human MnSOD.	Histidine	17-20	superoxide dismutase 2	Homo sapiens	85-90