PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30159555-8	2018	We anchored ZnF at the air/water interface via covalent linkage of ZnF to palmitic acid and controlled 2D crowding by introducing neutral lipid as a spacer.	Water	27-32	zinc finger protein 763	Homo sapiens	12-15	
35378434-8	2022	However, the total interaction energy of glycerol with DNA is lower than that of total water-DNA interaction energy indicating that it might be easier for an approaching DNA-binding protein to displace glycerol than water and thus contributing positively to protein-DNA binding.	Water	87-92	zinc finger protein 763	Homo sapiens	170-189	
35378434-8	2022	However, the total interaction energy of glycerol with DNA is lower than that of total water-DNA interaction energy indicating that it might be easier for an approaching DNA-binding protein to displace glycerol than water and thus contributing positively to protein-DNA binding.	Water	216-221	zinc finger protein 763	Homo sapiens	170-189	
24320225-2	2013	For example, X-ray diffraction studies demonstrate that [kappa(4)-Tptm]ZnF forms an adduct with water in which hydrogen bonding between the fluoride ligands and water molecules serves to link pairs of [kappa(4)-Tptm]ZnF molecules with a [F   (H-O-H)2   F] motif.	Water	96-101	zinc finger protein 763	Homo sapiens	71-74	
24320225-2	2013	For example, X-ray diffraction studies demonstrate that [kappa(4)-Tptm]ZnF forms an adduct with water in which hydrogen bonding between the fluoride ligands and water molecules serves to link pairs of [kappa(4)-Tptm]ZnF molecules with a [F   (H-O-H)2   F] motif.	Water	96-101	zinc finger protein 763	Homo sapiens	216-219	
24320225-2	2013	For example, X-ray diffraction studies demonstrate that [kappa(4)-Tptm]ZnF forms an adduct with water in which hydrogen bonding between the fluoride ligands and water molecules serves to link pairs of [kappa(4)-Tptm]ZnF molecules with a [F   (H-O-H)2   F] motif.	Water	161-166	zinc finger protein 763	Homo sapiens	71-74