PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10920257-10	2000	The largest factor in the substantially low pK(a) of reduced flavin in DAO is probably the steric hindrance between the hydrogen atom of H-N(1)(flavin) and the hydrogen atom of H-N of Gly315, which becomes significant when a hydrogen is bound to N(1) of flavin.	Hydrogen	120-128	D-amino acid oxidase	Homo sapiens	71-74	
11754736-0	2002	Effects of hydrogen bonds in association with flavin and substrate in flavoenzyme d-amino acid oxidase.	Hydrogen	11-19	D-amino acid oxidase	Homo sapiens	82-102	
11754736-2	2002	According to the three-dimensional structure of a porcine kidney D-amino acid oxidase-substrate (D-leucine) complex model, the G313 backbone carbonyl recognizes the substrate amino group by hydrogen bonding and the side-chain hydroxyl of T317 forms a hydrogen bond with C(2)=O of the flavin moiety of FAD [Miura et al.	Hydrogen	190-198	D-amino acid oxidase	Homo sapiens	65-85	
11754736-2	2002	According to the three-dimensional structure of a porcine kidney D-amino acid oxidase-substrate (D-leucine) complex model, the G313 backbone carbonyl recognizes the substrate amino group by hydrogen bonding and the side-chain hydroxyl of T317 forms a hydrogen bond with C(2)=O of the flavin moiety of FAD [Miura et al.	Hydrogen	251-259	D-amino acid oxidase	Homo sapiens	65-85	
11754736-7	2002	The results imply that the hydrogen bond between the G313 backbone carbonyl and the substrate amino group plays important roles in substrate recognition and in defining the substrate specificity of D-amino acid oxidase.	Hydrogen	27-35	D-amino acid oxidase	Homo sapiens	198-218	
10920257-10	2000	The largest factor in the substantially low pK(a) of reduced flavin in DAO is probably the steric hindrance between the hydrogen atom of H-N(1)(flavin) and the hydrogen atom of H-N of Gly315, which becomes significant when a hydrogen is bound to N(1) of flavin.	Hydrogen	160-168	D-amino acid oxidase	Homo sapiens	71-74	
10920257-10	2000	The largest factor in the substantially low pK(a) of reduced flavin in DAO is probably the steric hindrance between the hydrogen atom of H-N(1)(flavin) and the hydrogen atom of H-N of Gly315, which becomes significant when a hydrogen is bound to N(1) of flavin.	Hydrogen	160-168	D-amino acid oxidase	Homo sapiens	71-74	
23382199-6	2013	Together with this finding, the crystal structural analysis of OxdA and spectroscopic and electrostatic potential analyses of the wild-type and mutant OxdAs suggest that S219 plays a key role in the catalysis, forming a hydrogen bond with the substrate.	Hydrogen	220-228	D-amino acid oxidase	Homo sapiens	63-67	
1680851-8	1991	The low affinity of Im for DAO may be due to a steric repulsion of the hydrogen atoms of Im at C(3) in the active site.	Hydrogen	71-79	D-amino acid oxidase	Homo sapiens	27-30	
2874262-4	1986	Based on the similar stereoposition of identically charged atoms and lateral side chain (R) with respect to the alpha-hydrogen atoms in beta-sheet conformation and in D-amino acids, it is proposed that its substrates may include several membrane-related proteins, partially in beta-sheet conformation, whose alpha-hydrogen atoms would be the real object of D-amino acid oxidase catalysis.	Hydrogen	118-126	D-amino acid oxidase	Homo sapiens	357-377	
2874262-4	1986	Based on the similar stereoposition of identically charged atoms and lateral side chain (R) with respect to the alpha-hydrogen atoms in beta-sheet conformation and in D-amino acids, it is proposed that its substrates may include several membrane-related proteins, partially in beta-sheet conformation, whose alpha-hydrogen atoms would be the real object of D-amino acid oxidase catalysis.	Hydrogen	314-322	D-amino acid oxidase	Homo sapiens	357-377