PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27704222-6	2016	We have observed that the addition of mainly Na+, K+, Rb+, NH4+, as well as Sr2+ and Ba2+ in water, shifts the equilibrium to the folded quadruplex form, whereby the NRAS sequence responds stronger than TERRA.	Water	93-98	NRAS proto-oncogene, GTPase	Homo sapiens	166-170	
30224050-0	2018	Water Distribution within Wild-Type NRas Protein and Q61 Mutants during Unrestrained QM/MM Dynamics.	Water	0-5	NRAS proto-oncogene, GTPase	Homo sapiens	36-40	
30224050-3	2018	The NRas-GTP complex is analyzed using a hybrid quantum mechanics/molecular mechanics approach, treating for the first time to our knowledge transient water molecules at the ab initio level and leading to results that account for the electrostatic coupling between the protein complex and the solvent.	Water	151-156	NRAS proto-oncogene, GTPase	Homo sapiens	4-8	
30224050-6	2018	The structural changes observed in NRas Gln 61 mutants result in the drastic delocalization of water molecules that we discuss.	Water	95-100	NRAS proto-oncogene, GTPase	Homo sapiens	35-39	
17044712-4	2006	Fully functional lipid-modified N-Ras protein was obtained by chemical-biological synthesis ligating the expressed water soluble N-terminus with a chemically synthesized (2)H or (13)C labeled lipidated heptapeptide.	Water	115-120	NRAS proto-oncogene, GTPase	Homo sapiens	32-37