PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10096879-3	1999	Using a human methemoglobin alpha beta dimer, it has been shown that at 235 K after 61 ps, a rearrangement occurs in the alpha-chain corresponding to the formation of a bond with the distal histidine.	Histidine	190-199	hemoglobin subunit gamma 2	Homo sapiens	14-27	
24342540-4	2014	Molecular simulation analysis suggest that the presence of Tyr or Glu may contribute to the formation of the breakwater network, the stabilization of distal histidine, the changes in the size of heme pocket, and eventually result in the inhibition of metHb formation.	Histidine	157-166	hemoglobin subunit gamma 2	Homo sapiens	251-256	
1627604-4	1992	The intramolecular binding reaction of the N epsilon of the distal histidine E7 which is observed in methemoglobin in solution cannot be detected in single crystals.	Histidine	67-76	hemoglobin subunit gamma 2	Homo sapiens	101-114	
7260037-0	1981	Resonance Raman and absorption spectroscopic detection of distal histidine--fluoride interactions in human methemoglobin fluoride and sperm whale metmyoglobin fluoride: measurements of distal histidine ionization constants.	Histidine	65-74	hemoglobin subunit gamma 2	Homo sapiens	107-120	
7352984-5	1980	A model study of the azide-methemoglobin complex suggested that the increase of the high-spin character of the beta heme iron is due to a conformational change of the proximal histidine which weakens the interaction between the heme iron and the proximal base.	Histidine	176-185	hemoglobin subunit gamma 2	Homo sapiens	27-40	
1599941-1	1992	The reversible intramolecular binding of the distal histidine side chain to the heme iron in methemoglobin is of special interest due to the very large negative reaction entropy which overcompensates the large reaction enthalpy.	Histidine	52-61	hemoglobin subunit gamma 2	Homo sapiens	93-106	
2174256-0	1990	Multiple heme pocket subconformations of methemoglobin associated with distal histidine interactions.	Histidine	78-87	hemoglobin subunit gamma 2	Homo sapiens	41-54	
2174256-1	1990	Electron paramagnetic resonance spectra of methemoglobin reveal that, in addition to the major tetragonal high-spin aqueous complex and the low-spin hydroxide complex, three other complexes associated with the interaction of the distal histidine are resolved.	Histidine	236-245	hemoglobin subunit gamma 2	Homo sapiens	43-56	
667106-4	1978	This observation was interpreted in terms of the stronger interaction between proximal histidine and ferric heme iron in methemoglobin than in metmyoglobin.	Histidine	87-96	hemoglobin subunit gamma 2	Homo sapiens	121-134