PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22192271-3	2011	FINDINGS: Here we present comparisons of the binding sites and the electrostatic potential surfaces (EPS) of DAT, NET and SERT homology models based on two different LeuTAa templates; with a substrate (leucine) in an occluded conformation (PDB id 2a65), and with an inhibitor (tryptophan) in an open-to-out conformation (PDB id 3f3a).	Leucine	202-209	solute carrier family 6 member 3	Homo sapiens	109-112	
17690258-3	2007	We determined the crystal structure at 2.9 angstroms of the bacterial leucine transporter (LeuT), a homolog of SERT, NET, and DAT, in complex with leucine and the antidepressant desipramine.	Leucine	70-77	solute carrier family 6 member 3	Homo sapiens	126-129	
2078309-3	1990	The CSF concentrations of glycine, leucine and valine were also significantly reduced in the DAT cases.	Leucine	35-42	solute carrier family 6 member 3	Homo sapiens	93-96	
15953370-3	2005	To test this hypothesis, here we analysed transport activity for DAT mutants where this Pro was mutated into different amino acids, including Ser, Val, Leu and Phe.	Leucine	152-155	solute carrier family 6 member 3	Homo sapiens	65-68	
34002696-6	2021	This is demonstrated by both Rosetta molecular modeling and fine-grained simulations using hDAT R445C, as well as EPR analysis and X-ray crystallography of the bacterial homolog leucine transporter.	Leucine	178-185	solute carrier family 6 member 3	Homo sapiens	91-95