PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30188715-2	2018	Here we show that water dynamics and interactions can be controlled by the protonation state of ligand using continuous constant pH molecular dynamics simulations of two closely related model systems, beta-secretase 1 and 2 (BACE1 and BACE2), in complex with a small-molecule inhibitor.	Water	18-23	beta-secretase 2	Homo sapiens	235-240	
31140794-4	2019	When the concentration is in the mM range, the binding occurs with cis-VOL2(H2O), L = ma, koj, dhp, and mim, or with VO(acac)2: in the first case, the equatorial coordination of His68, Glu16, Glu18, or Asp21 residues yields species with formula n[VOL2]-Ub where n = 2-3, while with VO(acac)2 only noncovalent surface interactions are revealed.	Water	76-79	beta-secretase 2	Homo sapiens	202-207	
10587314-7	1999	cyclo(-D-Asp1-Asp2-Gly3-Ahd4-Ahd5-Gly6-) (C3) clearly exhibits two different conformations with a shifted beta,beta-turn motif in CDCI3 and SDS/H2O solutions.	Water	144-147	beta-secretase 2	Homo sapiens	9-13	
25246550-7	2014	We suggest that Asp21 and His84 provide a network of interactions that stabilize the positions of the gamma-phosphate and the nucleophilic water, respectively, and thus play an indirect catalytic role in the GTPase mechanism on the ribosome.	Water	139-144	beta-secretase 2	Homo sapiens	16-21