To explore for any possible H1R crossdockings, the 1588 children (Figure , red circles), were also ADV docked to the H2R, H3R, H4R and Kv1.5 cavities. The results predicted ~ 1000-fold extension of affinity differences between H1R and H2R, H3R, H4R and Kv1.5 (Figure , compare red with cyan, green, blue circles and red stars). All the corresponding 1588 ADV affinities per protein target (H1R, H2R, H3R, H4R and Kv1.5) affinities were tabulated in a DW Table with protein target sliders to facilitate selection of different combination preferences. To best compare optimal ADV affinities per children, the table also included their molecular weight, hydrophobicity (logP), brain-blood-barrier, glycoprotein P brain efflux pumps , and P450 (inhibition of detoxification by CYPs 1A2, 2C19, 2C9, 2D6 and 3A4). Adjusting the affinities of the protein targets (H2R, H3R, H4R and Kv1.5) to cut-offs of 200 nM, 299 (18.8 %) topchildren were identified predicting their highest H1R affinities between ~ 0.08 to 3.1 nM and several orders of magnitude difference crossreactivities with the other protein targets (Figure ).