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Pymol software version 4

Manufactured by Schrödinger
Sourced in United States

PyMOL is a molecular visualization software that allows users to create high-quality 3D images and animations of molecular structures. The latest version, 4.6.0, provides improved performance, new features, and bug fixes compared to previous versions.

Automatically generated - may contain errors

2 protocols using pymol software version 4

1

Homology Modeling of SPPV and GTPV RPO30 Proteins

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An automated homology model was constructed using SWISS-MODEL (Swiss Institute of Bioinformatics, BIOZENTRUM, University of Basel, Switzerland) for the consensus RPO30 gene sequences of the SPPV and GTPV isolates. The homology model for all SPPV and GTPV isolates of the RPO30 protein was predicted and proteins were matched from 1M to 204K of the E4L protein of VACV crystallized structure (6RIC_S), which has 259 amino acid residues. Further, the automated structural models were validated using RAMPAGE software (https://www.ccp4.ac.uk/html/rampage.html).
All modeled structures were generated using the X-ray crystallographic structure of the E4L protein (PDB ID: 6RIC_S) of the VACV (1M to 204K) as a reference and visualized using PyMol software version 4.6.0 (Schrödinger, Inc., New York, USA). Structural validation was performed using the Structural Analysis and Verification (SAVES) server (https://saves.mbi.ucla.edu/). Energy minimization and refinement were performed using the ModRefiner server (https://zhanggroup.org/ModRefiner/).
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2

Structural Modeling of CCHFV NP

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The structural data of the CCHFV NP molecule were obtained from Protein Data Bank (PDB) (PDB ID 3U3I). The missing amino acid residues at positions 182–194, 243, and 367–371 were added using Molecular Operating Environment (MOE) software (version 2018; Chemical Computing Group, Montreal, QC, Canada). The three-dimensional structure of the molecule was generated using PyMOL software version 4.6.0 (Schrödinger, New York, NY, USA).
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