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Yorodumi- PDB-1s6n: NMR Structure of Domain III of the West Nile Virus Envelope Prote... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1s6n | ||||||
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Title | NMR Structure of Domain III of the West Nile Virus Envelope Protein, Strain 385-99 | ||||||
Components | envelope glycoprotein | ||||||
Keywords | VIRAL PROTEIN / BETA BARREL / FLAVIVIRUS | ||||||
Function / homology | Function and homology information membrane => GO:0016020 / protein dimerization activity / host cell endoplasmic reticulum membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / virion membrane Similarity search - Function | ||||||
Biological species | West Nile virus | ||||||
Method | SOLUTION NMR | ||||||
Authors | Volk, D.E. / Beasley, D.W. / Kallick, D.A. / Holbrook, M.R. / Barrett, A.D. / Gorenstein, D.G. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: Solution Structure and Antibody Binding Studies of the Envelope Protein Domain III from the New York Strain of West Nile Virus Authors: Volk, D.E. / Beasley, D.W. / Kallick, D.A. / Holbrook, M.R. / Barrett, A.D. / Gorenstein, D.G. #1: Journal: To be Published Title: Letter to the Editor: 1H, 13C, and 15N resonance assignments for domain III of the West Nile Virus envelope protein Authors: Volk, D.E. / Kallick, D.A. / Holbrook, M.R. / Beasley, D.W.C. / Barrett, A.D.T. / Gorenstein, D.G. | ||||||
History |
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Remark 999 | SEQUENCE Residues 1-5 and 113-115 are not in the native sequence. They were added to increase solubility. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1s6n.cif.gz | 501.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1s6n.ent.gz | 435.3 KB | Display | PDB format |
PDBx/mmJSON format | 1s6n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1s6n_validation.pdf.gz | 357.1 KB | Display | wwPDB validaton report |
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Full document | 1s6n_full_validation.pdf.gz | 421.9 KB | Display | |
Data in XML | 1s6n_validation.xml.gz | 24 KB | Display | |
Data in CIF | 1s6n_validation.cif.gz | 43.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s6/1s6n ftp://data.pdbj.org/pub/pdb/validation_reports/s6/1s6n | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12197.809 Da / Num. of mol.: 1 / Fragment: Domain III Source method: isolated from a genetically manipulated source Source: (gene. exp.) West Nile virus / Genus: Flavivirus / Strain: 385-99 / Plasmid: pMAL C2X / Production host: Escherichia coli (E. coli) / Strain (production host): C2X / References: UniProt: Q913C7 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: CHEMICAL SHIFTS WERE DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY. |
-Sample preparation
Details | Contents: 0.7MM WND3 PROTEIN, 50MM K2HPO4, 100MM NACL, 10MM NAN3, 0.1MM EDTA |
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Sample conditions | Ionic strength: 50mM PHOSPHATE, 100mM NACL, 10mM NAN3 / pH: 6.8 / Pressure: AMBIENT / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 15 |