PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8186254-1	1994	The distal histidine (E7) of horse heart myoglobin (Mb) has been replaced by tyrosine using site-specific mutagenesis.	Histidine	11-20	myoglobin	Equus caballus	41-50	
10969024-0	2000	Salt effects on ionization equilibria of histidines in myoglobin.	Histidine	41-51	myoglobin	Equus caballus	55-64	
10969024-1	2000	The salt dependence of histidine pK(a) values in sperm whale and horse myoglobin and in histidine-containing peptides was measured by (1)H-NMR spectroscopy.	Histidine	23-32	myoglobin	Equus caballus	71-80	
10969024-4	2000	In myoglobin two histidines (His(48) and His(36)) exhibited a shallower dependence than the average, and one (His(113)) showed a steeper dependence.	Histidine	17-27	myoglobin	Equus caballus	3-12	
10969024-4	2000	In myoglobin two histidines (His(48) and His(36)) exhibited a shallower dependence than the average, and one (His(113)) showed a steeper dependence.	Histidine	29-32	myoglobin	Equus caballus	3-12	
10969024-4	2000	In myoglobin two histidines (His(48) and His(36)) exhibited a shallower dependence than the average, and one (His(113)) showed a steeper dependence.	Histidine	41-44	myoglobin	Equus caballus	3-12	
10969024-4	2000	In myoglobin two histidines (His(48) and His(36)) exhibited a shallower dependence than the average, and one (His(113)) showed a steeper dependence.	Histidine	41-44	myoglobin	Equus caballus	3-12	
11085653-4	2000	Saturation transfer between methyls on adjacent pyrroles in etioheme-reconstituted horse Mb in all accessible oxidation/spin states reveals rotational hopping rates that decrease dramatically with either loss of ligands or reduction of the heme, and correlate qualitatively with expectations based on the Fe-His bond strength and the rate of heme dissociation from Mb.	Histidine	308-311	myoglobin	Equus caballus	89-91	
7873545-1	1995	In either sperm whale or horse heart myoglobin, binding of NO and lowering of solution pH work together to weaken, and ultimately break, the bond between iron and the proximal histidine.	Histidine	176-185	myoglobin	Equus caballus	37-46	
4772291-0	1973	[Alkylation of histidine residues of horse myoglobin.	Histidine	15-24	myoglobin	Equus caballus	43-52	
4675202-0	1972	Hydrogen ion titration study of the histidine residues of horse myoglobin.	Histidine	36-45	myoglobin	Equus caballus	64-73	
11945956-0	1971	Proton magnetic resonance study of the histidine residues of horse myoglobin.	Histidine	39-48	myoglobin	Equus caballus	67-76	
4772291-1	1973	Study of 1-CM His-113 myoglobin].	Histidine	14-17	myoglobin	Equus caballus	22-31	
23978331-2	2013	A detailed study of the pH dependence of the midpoint potential of skeletal horse myoglobin (Mb) with a heme-bound fluoride ion (Mb-F) reveals how protonation of the distal histidine (H64) changes the redox properties of the protein with a determined pKa of 5.3.	Histidine	173-182	myoglobin	Equus caballus	82-91	
5882713-0	1965	[Alkylation of histidine radicals in the active center of horse myoglobin].	Histidine	15-24	myoglobin	Equus caballus	64-73	
23978331-2	2013	A detailed study of the pH dependence of the midpoint potential of skeletal horse myoglobin (Mb) with a heme-bound fluoride ion (Mb-F) reveals how protonation of the distal histidine (H64) changes the redox properties of the protein with a determined pKa of 5.3.	Histidine	173-182	myoglobin	Equus caballus	93-95	
23978331-2	2013	A detailed study of the pH dependence of the midpoint potential of skeletal horse myoglobin (Mb) with a heme-bound fluoride ion (Mb-F) reveals how protonation of the distal histidine (H64) changes the redox properties of the protein with a determined pKa of 5.3.	Histidine	173-182	myoglobin	Equus caballus	129-131	
22062184-3	2003	Western blot analyses confirmed the covalent modification of myoglobin (Mb) histidine residues by 4-HNE.	Histidine	76-85	myoglobin	Equus caballus	61-70	
17070916-6	2006	In sum, the current results establish that heme propionate esterification not only affects the electron transfer properties of myoglobin but also influences the titration behavior of specific His residues.	Histidine	192-195	myoglobin	Equus caballus	127-136	
16766034-3	2006	The pyrrole-protons of the hemin of myoglobin in the absence of external ligand appeared as four resonances between -10 and -18 ppm, indicating a mainly low-spin ferric hemin, with a ligated distal histidine (His64).	Histidine	198-207	myoglobin	Equus caballus	36-45