PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22948827-3	2012	Here we utilized NMR to monitor the signals from the methionine residue at position 82 in neutral antagonist- and partial agonist-bound states of beta(2)-adrenergic receptor (beta(2)AR), which are correlated with the conformational changes of the transmembrane regions upon activation.	Methionine	53-63	adrenoceptor beta 2	Homo sapiens	146-173	
22948827-3	2012	Here we utilized NMR to monitor the signals from the methionine residue at position 82 in neutral antagonist- and partial agonist-bound states of beta(2)-adrenergic receptor (beta(2)AR), which are correlated with the conformational changes of the transmembrane regions upon activation.	Methionine	53-63	adrenoceptor beta 2	Homo sapiens	175-184	
23374348-4	2013	We labeled beta(2)AR with (13)CH(3)epsilon-methionine and obtained HSQC spectra of unliganded receptor as well as receptor bound to an inverse agonist, an agonist, and a G-protein-mimetic nanobody.	Methionine	42-53	adrenoceptor beta 2	Homo sapiens	11-20	
25284766-4	2014	The NMR sensitivities of the methionine methyl resonances from the beta2 -adrenergic receptor (beta2 AR) in lipid bilayers of reconstituted high-density lipoprotein (rHDL) increased by approximately 5-fold upon deuteration.	Methionine	29-39	adrenoceptor beta 2	Homo sapiens	67-93	
25284766-4	2014	The NMR sensitivities of the methionine methyl resonances from the beta2 -adrenergic receptor (beta2 AR) in lipid bilayers of reconstituted high-density lipoprotein (rHDL) increased by approximately 5-fold upon deuteration.	Methionine	29-39	adrenoceptor beta 2	Homo sapiens	95-103