PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6289876-1	1982	The titration curves of the C-2 histidine protons of RNase A and of derivative II--a covalent derivative obtained by reaction of the enzyme with the halogenated nucleotide 9-beta-D-ribofuranosyl-6-chloropurine 5"-phosphate--in the presence of a number of purine nucleosides, nucleoside monophosphates, and nucleoside diphosphates were studied by means of proton nuclear magnetic resonance at 270 MHz.	Histidine	32-41	complement C2	Bos taurus	28-31	
3410637-2	1988	The titration curves of the C-2 histidine protons of bovine pancreatic ribonuclease A in the presence of several dideoxynucleoside monophosphates (dNpdN) were studied by means of proton nuclear magnetic resonance at 270 MHz in order to obtain information on the ligand--RNase A interaction.	Histidine	32-41	complement C2	Bos taurus	28-31	
3410637-3	1988	The changes in the chemical shift and pKs of the C-2 proton resonances of His-12, -48, -119 in the complexes RNase A--dNpdN were smaller than those previously found when the enzyme interacted with mononucleotides.	Histidine	74-77	complement C2	Bos taurus	49-52	
3813569-2	1987	One of the histidine C-2 peaks titrated normally, with a pKa value of 6.8, but the other two histidines in this peptide had pKa values of 6.3.	Histidine	11-20	complement C2	Bos taurus	21-24	
3624221-5	1987	The 1H and 13C nuclear magnetic resonance data indicated that imidazole C-2 of histidine is linked to C-6 of norleucine (epsilon-deaminated lysine residue) which in turn is linked to the C-6 amino group of hydroxylysine.	Histidine	79-88	complement C2	Bos taurus	72-75	
921767-1	1977	The C-2 proton of one histidine residue in bovine erythrocyte superoxide dismutase is shown to be particularly labile.	Histidine	22-31	complement C2	Bos taurus	4-7	
393248-0	1979	The exchange of histidine C-2 protons in superoxide dismutases.	Histidine	16-25	complement C2	Bos taurus	26-29	
393248-2	1979	The rates of exchange of the C-2 protons of histidine residues in copper-zinc superoxide dismutase are substantially decreased by metal ion binding.	Histidine	44-53	complement C2	Bos taurus	29-32	
8090-0	1976	pH dependence of tritium exchange with the C-2 protons of the histidines in bovine trypsin.	Histidine	62-72	complement C2	Bos taurus	43-46	
8090-1	1976	At pH 8.9 and 37 degrees C the half-times for tritium exchange with the C-2 protons of the histidines of trypsin are 73 days for His-57, and greater than 1000 days for His-40 and His-91.	Histidine	91-101	complement C2	Bos taurus	72-75	
8090-1	1976	At pH 8.9 and 37 degrees C the half-times for tritium exchange with the C-2 protons of the histidines of trypsin are 73 days for His-57, and greater than 1000 days for His-40 and His-91.	Histidine	129-132	complement C2	Bos taurus	72-75	
8090-1	1976	At pH 8.9 and 37 degrees C the half-times for tritium exchange with the C-2 protons of the histidines of trypsin are 73 days for His-57, and greater than 1000 days for His-40 and His-91.	Histidine	168-171	complement C2	Bos taurus	72-75	
8090-1	1976	At pH 8.9 and 37 degrees C the half-times for tritium exchange with the C-2 protons of the histidines of trypsin are 73 days for His-57, and greater than 1000 days for His-40 and His-91.	Histidine	168-171	complement C2	Bos taurus	72-75	
8090-2	1976	These half-times are much longer than the half-life of exchange for the C-2 proton of free histidine (2.8 days at pD 8.2), and longer than any previously reported half-time of exchange at pH greater than 8.	Histidine	91-100	complement C2	Bos taurus	72-75	
4454-2	1976	One of the four titrating histidine ring C-2 proton resonances of bovine pancreatic ribonuclease has been assigned to histidine residue 12.	Histidine	26-35	complement C2	Bos taurus	41-44	
4454-2	1976	One of the four titrating histidine ring C-2 proton resonances of bovine pancreatic ribonuclease has been assigned to histidine residue 12.	Histidine	118-127	complement C2	Bos taurus	41-44	
4454-3	1976	This was accomplished by a direct comparison of the rate of tritium incorporation into position C-2 of histidine 12 of S-peptide (residues 1 to 20) derived from ribonuclease S, with the rates of deuterium exchange of the four histidine C-2 proton resonances of ribonuclease S under the same experimental conditions.	Histidine	103-112	complement C2	Bos taurus	96-99	
239193-2	1975	For neurophysin I alone, a normal titration curve for the C-2 proton resonance of the lone histidine residue was obtained with an apparent ionization constant of 6.9 addition of oxytocin to a solution of neurophysin I at pH 6.5 resulted in several changes in the spectrum.	Histidine	91-100	complement C2	Bos taurus	58-61