PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34321660-7	2021	Two amino acids-leucine 642 on GluN2A (homologous to leucine 643 on GluN2B) and asparagine 616 on GluN1-were identified as key residues that form hydrophobic and hydrogen-bond interactions with ketamine, and mutations at these residues reduced the potency of ketamine in blocking NMDA receptor channel activity.	Leucine	16-23	glutamate ionotropic receptor NMDA type subunit 2A	Homo sapiens	31-37	
23447622-9	2013	Mutating the GluN2 S/L site of GluN2A subunits from serine (found in GluN2A and GluN2B subunits) to leucine (found in GluN2C and GluN2D) greatly diminished both voltage-dependent gating and slow Mg(o)(2+) unblock.	Leucine	100-107	glutamate ionotropic receptor NMDA type subunit 2A	Homo sapiens	31-37	
22715100-6	2012	Significant interactions affecting ethanol inhibition and receptor deactivation were observed at four pairs of positions in GluN1/GluN2A: Gly-638/Met-823, Phe-639/Leu-824, Met-818/Phe-636, and Leu-819/Phe-637; the latter pair also interacted with respect to desensitization.	Leucine	163-166	glutamate ionotropic receptor NMDA type subunit 2A	Homo sapiens	130-136	
22715100-6	2012	Significant interactions affecting ethanol inhibition and receptor deactivation were observed at four pairs of positions in GluN1/GluN2A: Gly-638/Met-823, Phe-639/Leu-824, Met-818/Phe-636, and Leu-819/Phe-637; the latter pair also interacted with respect to desensitization.	Leucine	193-196	glutamate ionotropic receptor NMDA type subunit 2A	Homo sapiens	130-136	
22715100-7	2012	Two interactions involved a position in M4 of both subunits, GluN1(Met-818) and GluN2A(Leu-824), that does not by itself alter ethanol sensitivity, whereas a previously identified ethanol-sensitive position, GluN2A(Ala-825), did not unequivocally interact with any other position tested.	Leucine	87-90	glutamate ionotropic receptor NMDA type subunit 2A	Homo sapiens	80-86	
11053122-4	2000	The tryptophan was mutated to a leucine (W-5L) in both the NMDAR1 and NMDAR2A subunits.	Leucine	32-39	glutamate ionotropic receptor NMDA type subunit 2A	Homo sapiens	70-77	
34321660-7	2021	Two amino acids-leucine 642 on GluN2A (homologous to leucine 643 on GluN2B) and asparagine 616 on GluN1-were identified as key residues that form hydrophobic and hydrogen-bond interactions with ketamine, and mutations at these residues reduced the potency of ketamine in blocking NMDA receptor channel activity.	Leucine	53-60	glutamate ionotropic receptor NMDA type subunit 2A	Homo sapiens	31-37