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Garry W Lynch, Ana Paula Mello Lemgruber, Maria Rocha Costa, Stefanie Portelli, Christopher J Blasi, John S Sullivan, William Bret Church (Sydney University, School of Medicine & School of Veterinary Science. )Given the high profile and importance of Ebola virus as a globally significant pathogen it is quite astounding that about half of its envelope glycoprotein gp structure is unknown. Especially since Ebola's surface gp is essential for cell binding, fusion and entry, and is the target for immune protection and vaccine design. Particularly missing is structural information for the most peripheral and prominent Mucin-Like Domain (MLD), and the Ebola virus first point of contact for attachment to cell surfaces and receptors. Working towards bridging this knowledge gap we have performed in silico modeling of the missing regions for the Ebola Mayinga 1976 Zaire subtype (UniProt Taxon ID: 128952). Depicted is our refined and validated glycosylated MLD simulation and shown in context with the published core pdb trimer 3CSY structure resolved to 3.4 Å, and within the 3D topographical gp trimer low-resolution (25-30 Å) cryoelectron microscopic structure, EMD-6003. Servers, tools and programs used: Bioinformatics/ Proteomics/ Computational Modelling (Uniprot, Clustal W, pdb, EMD, Phyre2, iTasser, CABS-flex, Glyprot, Glycam, PyMol, Chimera,); Concept BioArt (ZBrush, Photoshop, After Effects).