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Yorodumi- PDB-5e06: Structure of Sin Nombre virus nucleoprotein in long-axis crystal form -
+Open data
-Basic information
Entry | Database: PDB / ID: 5000000 | ||||||
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Title | Structure of Sin Nombre virus nucleoprotein in long-axis crystal form | ||||||
Components | Nucleocapsid protein | ||||||
Keywords | NUCLEAR PROTEIN / hantavirus / Sin Nombre virus / nucleoprotein | ||||||
Function / homology | Function and homology information regulation of translation / host cell Golgi apparatus / viral nucleocapsid / endonuclease activity / Hydrolases; Acting on ester bonds / host cell perinuclear region of cytoplasm / hydrolase activity / ribonucleoprotein complex / RNA binding Similarity search - Function | ||||||
Biological species | Sin Nombre virus | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.001 Å | ||||||
Authors | Guo, Y. / Wang, W.M. / Lou, Z.Y. | ||||||
Citation | Journal: J.Virol. / Year: 2015 Title: Crystal Structure of the Core Region of Hantavirus Nucleocapsid Protein Reveals the Mechanism for Ribonucleoprotein Complex Formation Authors: Guo, Y. / Wang, W. / Sun, Y. / Ma, C. / Wang, X. / Wang, X. / Liu, P. / Shen, S. / Li, B. / Lin, J. / Deng, F. / Wang, H. / Lou, Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5e06.cif.gz | 122.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5e06.ent.gz | 95.9 KB | Display | PDB format |
PDBx/mmJSON format | 5e06.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5e06_validation.pdf.gz | 422.9 KB | Display | wwPDB validaton report |
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Full document | 5e06_full_validation.pdf.gz | 428.4 KB | Display | |
Data in XML | 5e06_validation.xml.gz | 11.9 KB | Display | |
Data in CIF | 5e06_validation.cif.gz | 14.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e0/5e06 ftp://data.pdbj.org/pub/pdb/validation_reports/e0/5e06 | HTTPS FTP |
-Related structure data
Related structure data | 5e04C 5e05C 5e07 C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 32158.184 Da / Num. of mol.: 1 / Fragment: UNP residues 112-395 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sin Nombre virus / Production host: Escherichia coli (E. coli) / References: UniProt: Q9E1J8, UniProt: Q89462*PLUS |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.37 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop Details: 200 mM lithium sulfate monohydrate and 20% (w/v) PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9798 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 17, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9798 Å / Relative weight: 1 |
Reflection | Resolution: 3→50 Å / Num. obs: 7053 / % possible obs: 100 % / Redundancy: 11.8 % / Net I/σ(I): 45 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.001→42.72 Å / SU ML: 0.33 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 29.47 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.001→42.72 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -1.2379 Å / Origin y: -10.6394 Å / Origin z: -16.0217 Å
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Refinement TLS group | Selection details: chain A |