PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28876052-2	2017	A recently discovered antiparallel coiled-coil hexamer (ACC-Hex, peptide 1) exhibits a unique interaction in which Phe and Ile residues from adjacent alpha-helices interact to form a Phe-Ile zipper within the hydrophobic core.	Phenylalanine	115-118	hematopoietically expressed homeobox	Homo sapiens	60-63	
31517530-4	2019	Results & conclusions: The binding free energy (DeltaGbind) and the change in the free energy surface (FES) computed from the funnel metadynamics (FMD) simulation, both support the idea that inhibitors (-)-phe and (-)-hex have better binding activities toward enzyme AChE, and that (-)-phe is stronger in binding than the present AD drug (-)-phy.	Phenylalanine	206-209	hematopoietically expressed homeobox	Homo sapiens	218-221	
31517530-4	2019	Results & conclusions: The binding free energy (DeltaGbind) and the change in the free energy surface (FES) computed from the funnel metadynamics (FMD) simulation, both support the idea that inhibitors (-)-phe and (-)-hex have better binding activities toward enzyme AChE, and that (-)-phe is stronger in binding than the present AD drug (-)-phy.	Phenylalanine	286-289	hematopoietically expressed homeobox	Homo sapiens	218-221	
28876052-2	2017	A recently discovered antiparallel coiled-coil hexamer (ACC-Hex, peptide 1) exhibits a unique interaction in which Phe and Ile residues from adjacent alpha-helices interact to form a Phe-Ile zipper within the hydrophobic core.	Phenylalanine	183-186	hematopoietically expressed homeobox	Homo sapiens	60-63	
28876052-3	2017	Analysis of the X-ray crystallographic structure of ACC-Hex suggests that the stability of the six-helix bundle relies on specific interactions between the Phe and Ile residues.	Phenylalanine	156-159	hematopoietically expressed homeobox	Homo sapiens	56-59	
28876052-6	2017	Using size exclusion chromatography and small-angle X-ray scattering, we found that the proper assembly of ACC-Hex from monomers is sensitive to subtle changes in side chain steric bulk and hydrophobicity introduced by mutations at the Phe and Ile residue positions.	Phenylalanine	236-239	hematopoietically expressed homeobox	Homo sapiens	111-114	
28876052-9	2017	Finally, we expanded on the generality of the Phe-Ile zipper, creating a unique sequence that forms an antiparallel hexamer that is topologically similar to ACC-Hex but atomistically unique.	Phenylalanine	46-49	hematopoietically expressed homeobox	Homo sapiens	161-164