PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28967043-5	2018	FT-IR spectroscopy revealed hydrogen bond interactions between carvedilol and copovidone K28.	Hydrogen	28-36	keratin 28	Homo sapiens	89-92	
16766615-5	2006	The hairpin is stabilized by backbone hydrogen-bonding interactions between residues K28 and I31; S26 and G33; and by side-chain-to-side-chain interactions between N27 and I32.	Hydrogen	38-46	keratin 28	Homo sapiens	85-88	
16731963-6	2006	This bend is stabilized by a network of hydrogen bonds involving the side chain of residue D23 and the amide hydrogens of adjacent residues G25, S26, N27, and K28, as well as by a salt bridge formed between side chains of K28 and E22.	Hydrogen	40-48	keratin 28	Homo sapiens	159-162	
16731963-6	2006	This bend is stabilized by a network of hydrogen bonds involving the side chain of residue D23 and the amide hydrogens of adjacent residues G25, S26, N27, and K28, as well as by a salt bridge formed between side chains of K28 and E22.	Hydrogen	40-48	keratin 28	Homo sapiens	222-225	
16731963-6	2006	This bend is stabilized by a network of hydrogen bonds involving the side chain of residue D23 and the amide hydrogens of adjacent residues G25, S26, N27, and K28, as well as by a salt bridge formed between side chains of K28 and E22.	Hydrogen	109-118	keratin 28	Homo sapiens	159-162	
16731963-6	2006	This bend is stabilized by a network of hydrogen bonds involving the side chain of residue D23 and the amide hydrogens of adjacent residues G25, S26, N27, and K28, as well as by a salt bridge formed between side chains of K28 and E22.	Hydrogen	109-118	keratin 28	Homo sapiens	222-225	
34565139-7	2021	Moreover, the GV971 components mainly interact directly with the charged residues D1, R5, K16, and K28 by forming salt bridges and hydrogen bonds, which specifically bind to the N-terminal region of Abeta42.	Hydrogen	131-139	keratin 28	Homo sapiens	99-102