Author: Ivan Mercurio; Vincenzo Tragni; Francesco Busco; Anna De Grassi; Ciro Leonardo Pierri
                    Title: Protein structure analysis of the interactions between SARS-CoV-2 spike protein and the human ACE2 receptor: from conformational changes to novel neutralizing antibodies  Document date: 2020_4_18
                    ID: mswmkgl4_25
                    
                    Snippet: Starting from the cited multi-template sequence alignment and according to our validated protocols about multi-template 3D modeling (30, 36) , we built the 3D model of a monomer of SARS-CoV-2 spike protein in post fusion conformation (Fig. 2) . The modelled SARS-CoV-2 spike post-fusion conformation consists of residues 704-771 and 922-1147, YP_009724390.1 residues numbering, resulting from protein cleavage (11) and also the only protein fragments.....
                    
                    
                    
                     
                    
                    
                    
                    
                        
                            
                                Document: Starting from the cited multi-template sequence alignment and according to our validated protocols about multi-template 3D modeling (30, 36) , we built the 3D model of a monomer of SARS-CoV-2 spike protein in post fusion conformation (Fig. 2) . The modelled SARS-CoV-2 spike post-fusion conformation consists of residues 704-771 and 922-1147, YP_009724390.1 residues numbering, resulting from protein cleavage (11) and also the only protein fragments with a solved structure in 6b3o.pdb aligned (aminoacids 741-807 and 972-1248, NP_045300.1/6b3o.pdb residues numbering) counterpart (37) .
 
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