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SARS Spike Proteins
por groliver
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3D Printable Models Based on the Following Paper:
In the absence of a known nCoV-Spike protein structure, we characterized the surface
glycoprotein sequence YP_009724390.1 [1] by constructing a homology-based structural model using the AS2TS system [2]. The structures of the Spike proteins from SARS (PDB entries: 5x58 [3], 6nb6 [4], 2dd8 [5], and 3bgf [6]) were identified as the closest and most complete PDB structural templates to use for the modeling. The last three listed templates provided additional important information about possible complexes with three antibodies: S230, M396, and F26G19. The PDB templates had been experimentally solved at a resolution of 3.2, 4.2, 2.3, and 3.0 Å respectively. The level of sequence identity between nCoV and SARS Spike proteins from the templates is 71%. In order to assess regions of sequence-structure conservation or variability in the modeled proteins, a set of initial structural models was created using an extensive set of available templ
In the absence of a known nCoV-Spike protein structure, we characterized the surface
glycoprotein sequence YP_009724390.1 [1] by constructing a homology-based structural model using the AS2TS system [2]. The structures of the Spike proteins from SARS (PDB entries: 5x58 [3], 6nb6 [4], 2dd8 [5], and 3bgf [6]) were identified as the closest and most complete PDB structural templates to use for the modeling. The last three listed templates provided additional important information about possible complexes with three antibodies: S230, M396, and F26G19. The PDB templates had been experimentally solved at a resolution of 3.2, 4.2, 2.3, and 3.0 Å respectively. The level of sequence identity between nCoV and SARS Spike proteins from the templates is 71%. In order to assess regions of sequence-structure conservation or variability in the modeled proteins, a set of initial structural models was created using an extensive set of available templ
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