cogent 2000 graphic toolbox Search Results


porous graphitized carbon solid phase extraction columns  (Glygen Corporation)
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Glygen Corporation porous graphitized carbon solid phase extraction columns
Porous Graphitized Carbon Solid Phase Extraction Columns, supplied by Glygen Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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shelxtl  (Bruker Corporation)
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Bruker Corporation shelxtl
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pymol molecular graphics system  (DeLano Scientific)
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DeLano Scientific pymol molecular graphics system
Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the <t>PyMOL</t> <t>Molecular</t> Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).
Pymol Molecular Graphics System, supplied by DeLano Scientific, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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exfoliated graphene nanoplatelets xgnp-c-750  (XG Sciences Inc)
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XG Sciences Inc exfoliated graphene nanoplatelets xgnp-c-750
Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the <t>PyMOL</t> <t>Molecular</t> Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).
Exfoliated Graphene Nanoplatelets Xgnp C 750, supplied by XG Sciences Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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dedicated graphics workstation tdz 2000  (Intergraph Corporation)
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Intergraph Corporation dedicated graphics workstation tdz 2000
Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the <t>PyMOL</t> <t>Molecular</t> Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).
Dedicated Graphics Workstation Tdz 2000, supplied by Intergraph Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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laser particle size distribution analyzer (“sald-2000  (Shimadzu Corporation)
90
Shimadzu Corporation laser particle size distribution analyzer (“sald-2000
Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the <t>PyMOL</t> <t>Molecular</t> Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).
Laser Particle Size Distribution Analyzer (“Sald 2000, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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cogent 2000 graphics  (MathWorks Inc)
90
MathWorks Inc cogent 2000 graphics
Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the <t>PyMOL</t> <t>Molecular</t> Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).
Cogent 2000 Graphics, supplied by MathWorks Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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raman spectrometer renishaw invia 2000  (Renishaw Inc)
90
Renishaw Inc raman spectrometer renishaw invia 2000
Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the <t>PyMOL</t> <t>Molecular</t> Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).
Raman Spectrometer Renishaw Invia 2000, supplied by Renishaw Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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medi-trace 2000 silver chloride surface electrodes  (Graphic Controls Inc)
90
Graphic Controls Inc medi-trace 2000 silver chloride surface electrodes
Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the <t>PyMOL</t> <t>Molecular</t> Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).
Medi Trace 2000 Silver Chloride Surface Electrodes, supplied by Graphic Controls Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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carbon black superp  (TIMCAL Ltd)
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TIMCAL Ltd carbon black superp
Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the <t>PyMOL</t> <t>Molecular</t> Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).
Carbon Black Superp, supplied by TIMCAL Ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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xshell  (Bruker Corporation)
90
Bruker Corporation xshell
Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the <t>PyMOL</t> <t>Molecular</t> Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).
Xshell, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the PyMOL Molecular Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).

Journal: Handbook of Proteolytic Enzymes

Article Title: Arterivirus Papain-like Proteinase 1β

doi: 10.1016/B978-0-12-382219-2.00499-3

Figure Lengend Snippet: Ribbon diagram of the crystal structure of PRRSV Nsp1β. The figure was made using the PyMOL Molecular Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV . The structure of the Nsp1β monomer includes four domains colored differently: N-terminal domain (NTD: Ala181 to Ser228; green), linker domain (LKD: Phe229 to Thr264, red), PLPβ (Val265 to Pro361; blue), and C-terminal extension (CTE: Asn362 to Gly383, yellow). Also depicted are the main and side chains of the juxtaposed catalytic Cys270 and His339 residues (Cys and His, magenta) and C-terminal Gly383 residue (Gly, yellow).

Article Snippet: The figure was made using the PyMOL Molecular Graphics System (DeLano Scientific, Palo Alto, CA (2000)) and PDB entry 3MTV .

Techniques: Residue