PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21117944-7	2011	All the herbal compounds tested can be readily docked into the ligand-binding cavity of PXR mainly through hydrogen bond and aromatic interactions with Ser247, Gln285, His407, and Arg401.	Hydrogen	107-115	nuclear receptor subfamily 1 group I member 2	Homo sapiens	88-91	
18579710-3	2008	A recent novel pharmacophore for PXR antagonists was developed using three azoles and consisted of two hydrogen bond acceptor regions and two hydrophobic features.	Hydrogen	103-111	nuclear receptor subfamily 1 group I member 2	Homo sapiens	33-36	
17576789-8	2007	In contrast, a qualitative comparison with the corresponding PXR antagonist pharmacophore models using azoles and biphenyls showed that they are smaller and hydrophobic with increased emphasis on hydrogen bonding features.	Hydrogen	196-204	nuclear receptor subfamily 1 group I member 2	Homo sapiens	61-64	
15807509-7	2005	The results suggest that hydrogen bonding to Gln285 is indispensable for PXR activation.	Hydrogen	25-33	nuclear receptor subfamily 1 group I member 2	Homo sapiens	73-76	
15039302-7	2004	Therefore, a hydrophobic moiety at the 5-position and a hydrogen-bond acceptor being sufficiently separated from the phenyl-ring are responsible for activation of hPXR by barbiturates.	Hydrogen	56-64	nuclear receptor subfamily 1 group I member 2	Homo sapiens	163-167	
15039302-13	2004	These findings suggest that hydrophobicity of the ligand and adequate distance between the hydrogen-bond acceptor and the hydrophobic group are important for hPXR activation.	Hydrogen	91-99	nuclear receptor subfamily 1 group I member 2	Homo sapiens	158-162	
31561157-10	2020	Hydrogen bonding and hydrophobic interactions constituted the primary intermolecular forces between PFCs and the hPXR.	Hydrogen	0-8	nuclear receptor subfamily 1 group I member 2	Homo sapiens	113-117	
29757018-5	2018	The first use of hydrogen-deuterium exchange coupled with mass spectroscopy (HDX-MS) to study compound-protein interactions in the PXR-LBD is also addressed.	Hydrogen	17-25	nuclear receptor subfamily 1 group I member 2	Homo sapiens	131-134	
28963450-7	2017	Differential hydrogen/deuterium exchange analysis demonstrates that SPA70 and SJB7 interact with the hPXR LBD.	Hydrogen	13-21	nuclear receptor subfamily 1 group I member 2	Homo sapiens	101-105	
28115241-6	2017	Hydrogen bonding was characteristic of the interaction between PFCs and hPXR.	Hydrogen	0-8	nuclear receptor subfamily 1 group I member 2	Homo sapiens	72-76	
24828006-5	2014	Further structure-activity relationship studies of the most active PXR antagonist from the series (compound 20, IC50 = 11 muM) revealed the importance of hydroxyl groups as hydrogen-bond donors for PXR antagonistic activity.	Hydrogen	173-181	nuclear receptor subfamily 1 group I member 2	Homo sapiens	67-70	
24828006-5	2014	Further structure-activity relationship studies of the most active PXR antagonist from the series (compound 20, IC50 = 11 muM) revealed the importance of hydroxyl groups as hydrogen-bond donors for PXR antagonistic activity.	Hydrogen	173-181	nuclear receptor subfamily 1 group I member 2	Homo sapiens	198-201	
21805522-6	2011	PXR employs one hydrogen bond and fourteen van der Waals contacts to interact with the ligand, but allows two loops adjacent to the ligand-binding pocket to remain disordered in the structure.	Hydrogen	16-24	nuclear receptor subfamily 1 group I member 2	Homo sapiens	0-3	
21145880-8	2011	Secondly, the favorable hydrophobic interactions, mostly through aromatic pi-pi interactions, and the presence of suitable hydrogen bond(s) between the compounds and PXR are attributes of strong binders.	Hydrogen	123-131	nuclear receptor subfamily 1 group I member 2	Homo sapiens	166-169	
18768384-6	2008	The 2.8-A resolution crystal structure of the ligand binding domain of human PXR in complex with colupulone was elucidated, and colupulone was observed to bind in a single orientation stabilized by both van der Waals and hydrogen bonding contacts.	Hydrogen	221-229	nuclear receptor subfamily 1 group I member 2	Homo sapiens	77-80