PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17962328-1	2008	Heteromeric NMDARs are composed of coagonist glycine-binding NR1 subunits and glutamate-binding NR2 subunits.	Glycine	45-52	glutamate ionotropic receptor NMDA type subunit 1 L homeolog	Xenopus laevis	61-64	
17962328-4	2008	This heterogeneity is specified by the particular NR2 subunit within the NMDAR complex since the glycine-binding NR1 subunit is common to all NMDARs investigated.	Glycine	97-104	glutamate ionotropic receptor NMDA type subunit 1 L homeolog	Xenopus laevis	113-116	
17962328-9	2008	We conclude that the variation in glycine potency is caused by interactions between the NR1 and NR2 ligand-binding domains that occur following agonist binding and which may be involved in the initial conformation changes that determine channel gating.	Glycine	34-41	glutamate ionotropic receptor NMDA type subunit 1 L homeolog	Xenopus laevis	88-91