PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30193557-4	2019	Analyses on hydrogen bond interactions show that the decrease in hydrogen bonding interactions of residues R126 and Y128 with three inhibitors and the increase in that of K58 with inhibitors ZGC and IBP in the R126A mutated systems mostly regulate the conformational changes of A-FABP.	Hydrogen	12-20	fatty acid binding protein 4	Homo sapiens	278-284	
18375128-4	2008	For aP2, the ability of the receptor protein to change its hydrogen bond interactions in the beta-strands to accommodate different ligand scaffolds seems to make this receptor difficult for structure based drug design.	Hydrogen	59-67	fatty acid binding protein 4	Homo sapiens	4-7	
30999003-3	2019	METHODS: The impact of circulating FABP4 on the cardiac neutral lipid content was measured by proton magnetic resonance spectroscopy (1H-MRS) in patients with type 2 diabetes.	Hydrogen	134-136	fatty acid binding protein 4	Homo sapiens	35-40