PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8307026-0	1994	1H resonance assignments and secondary structure of the carbon monoxide complex of soybean leghemoglobin determined by homonuclear two-dimensional and three-dimensional NMR spectroscopy.	Hydrogen	0-2	leghemoglobin A	Glycine max	91-104	
15147208-3	2004	In leghemoglobin, the imidazole side chain of His(E7) is confined to a single conformation, which only weakly hydrogen bonds to bound ligands.	Hydrogen	110-118	leghemoglobin A	Glycine max	3-16	
15147208-8	2004	If hydrogen bonding from His(E7) were as strong as it is in mammalian myoglobin, the resultant ultrahigh affinity of leghemoglobin would prevent oxygen transport in root nodules.	Hydrogen	3-11	leghemoglobin A	Glycine max	117-130	
8620875-0	1996	Hydrogen exchange in the carbon monoxide complex of soybean leghemoglobin.	Hydrogen	0-8	leghemoglobin A	Glycine max	60-73	
8620875-1	1996	Hydrogen/deuterium exchange rates for individual amide protons have been measured for the carbon monoxide complex of soybean leghemoglobin.	Hydrogen	0-8	leghemoglobin A	Glycine max	125-138	
8307026-1	1994	Homonuclear two-dimensional and three-dimensional 1H-NMR spectroscopy has been utilized to study the 15.9-kDa protein soybean leghemoglobin.	Hydrogen	50-52	leghemoglobin A	Glycine max	126-139	
8307026-4	1994	The secondary structure of leghemoglobin in solution has been determined on the basis of NOE connectivity patterns, hydrogen exchange and chemical-shift analyses.	Hydrogen	116-124	leghemoglobin A	Glycine max	27-40	
8307026-7	1994	The hydrogen exchange behavior for the F helix and at the beginning of the A helix suggests different dynamic stability compared to other helical regions in leghemoglobin.	Hydrogen	4-12	leghemoglobin A	Glycine max	157-170	
8218216-0	1993	Role of hydrogen bonding to bound dioxygen in soybean leghemoglobin.	Hydrogen	8-16	leghemoglobin A	Glycine max	54-67	
8218216-7	1993	A discussion of the contribution of this hydrogen bond to the pH-dependent O2 affinity of leghemoglobin is presented.	Hydrogen	41-49	leghemoglobin A	Glycine max	90-103	
26211916-4	2015	Extensive mutational analysis combined with kinetic and CO-FT-IR spectroscopic investigation led to the hypothesis that Lba depended on weakened electrostatic interaction between distal HisE7 and bound ligand achieved by invoking B10Tyr, which itself hydrogen bonds with HisE7 thus restricting it in a single conformation detrimental to Mb-like strong electrostatic interaction.	Hydrogen	251-259	leghemoglobin A	Glycine max	120-123	
26211916-6	2015	The investigation supports the presence of at least two major conformations of HisE7 in Lba brought about by imidazole ring flip, one of which makes hydrogen bonds effectively with B10Tyr affecting the former"s ability to stabilize bound ligand, while the other does not.	Hydrogen	149-157	leghemoglobin A	Glycine max	88-91	
26211916-8	2015	Thus, it appears that TyrB10 limits the conformational freedom of distal His in Lba, tuning down ligand dissociation rate constant by reducing the strength of hydrogen bonding to bound ligand, which the freedom of distal His of Mb allows.	Hydrogen	159-167	leghemoglobin A	Glycine max	80-83	
22940317-1	2012	Co-cultivation of Bradyrhizobium japonicum with Chlamydomonas reinhardtii strain cc849 or the transgenic strain lba, which was hetero-expressed the gene of the soybean leghemoglobin apoprotein Lba in chloroplasts of the strain cc849, in Tris-acetate-phosphate (TAP) or TAP-sulfur free media, improved H(2) yield.	Hydrogen	301-305	leghemoglobin A	Glycine max	112-115	
22940317-2	2012	H(2) production was 14 times and growth was 26% higher when strain lba and B. japonicum were co-cultured, as compared with cultivation of the algal strain alone under the same conditions.	Hydrogen	0-4	leghemoglobin A	Glycine max	67-70