PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21388959-6	2011	Comparison among the two structures and other state 1 and state 2 structures of H-Ras/M-Ras reveal two new structural features playing critical roles in state dynamics; interaction of residues 31/41 (H-Ras/M-Ras) with residues 29/39 and 30/40, which induces a conformational change of switch I favoring its interaction with the gamma-phosphate, and the hydrogen-bonding interaction of switch II with its neighboring alpha-helix, alpha3-helix, which induces a conformational change of switch II favoring its interaction with the gamma-phosphate.	gamma-phosphate	328-343	muscle RAS oncogene homolog	Homo sapiens	86-91	
21388959-6	2011	Comparison among the two structures and other state 1 and state 2 structures of H-Ras/M-Ras reveal two new structural features playing critical roles in state dynamics; interaction of residues 31/41 (H-Ras/M-Ras) with residues 29/39 and 30/40, which induces a conformational change of switch I favoring its interaction with the gamma-phosphate, and the hydrogen-bonding interaction of switch II with its neighboring alpha-helix, alpha3-helix, which induces a conformational change of switch II favoring its interaction with the gamma-phosphate.	gamma-phosphate	328-343	muscle RAS oncogene homolog	Homo sapiens	206-211