+Open data
-Basic information
Entry | Database: PDB / ID: 4ftb | |||||||||
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Title | Crystal structure of the authentic Flock House virus particle | |||||||||
Components |
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Keywords | VIRUS / FLOCK HOUSE VIRUS / Nodavirus / RNA / BETA-BARREL / JELLYROLL / ASPARTYL PROTEASE / CAPSID PROTEIN / HYDROLASE / autoproteolysis / VIRION / ICOSAHEDRAL VIRUS | |||||||||
Function / homology | Function and homology information nodavirus endopeptidase / permeabilization of host organelle membrane involved in viral entry into host cell / symbiont entry into host cell via permeabilization of inner membrane / T=3 icosahedral viral capsid / aspartic-type endopeptidase activity / proteolysis / metal ion binding Similarity search - Function | |||||||||
Biological species | Flock house virus | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.7 Å | |||||||||
Authors | Speir, J.A. / Chen, Z. / Reddy, V.S. / Johnson, J.E. | |||||||||
Citation | Journal: to be published / Year: 2012 Title: Structural study of virus assembly intermediates reveals maturation event sequence and a staging position for externalized lytic peptides Authors: Speir, J.A. / Chen, Z. / Reddy, V.S. / Johnson, J.E. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4ftb.cif.gz | 221.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4ftb.ent.gz | 175.3 KB | Display | PDB format |
PDBx/mmJSON format | 4ftb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4ftb_validation.pdf.gz | 524.8 KB | Display | wwPDB validaton report |
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Full document | 4ftb_full_validation.pdf.gz | 550.4 KB | Display | |
Data in XML | 4ftb_validation.xml.gz | 46 KB | Display | |
Data in CIF | 4ftb_validation.cif.gz | 65 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ft/4ftb ftp://data.pdbj.org/pub/pdb/validation_reports/ft/4ftb | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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3 |
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Unit cell |
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Symmetry | Point symmetry: (Schoenflies symbol: I (icosahedral)) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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Details | biological unit is an icosahedral virus generated by applying the provided matrices |
-Components
-Capsid protein ... , 2 types, 6 molecules ABCDEF
#1: Protein | Mass: 39367.355 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Flock house virus / Gene: alpha, coat protein alpha / Cell line (production host): DL-1 / Production host: DROSOPHILA MELANOGASTER (fruit fly) / References: UniProt: P12870, nodavirus endopeptidase #2: Protein/peptide | Mass: 4399.056 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Flock house virus / Gene: alpha, coat protein alpha / Cell line (production host): DL-1 / Production host: DROSOPHILA MELANOGASTER (fruit fly) / References: UniProt: P12870 |
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-RNA chain , 1 types, 1 molecules R
#3: RNA chain | Mass: 4567.617 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Genomic RNA produced during virus replication in DL-1 cells. Source: (natural) Flock house virus |
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-Non-polymers , 4 types, 486 molecules
#4: Chemical | ChemComp-CA / #5: Chemical | #6: Chemical | ChemComp-CL / | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.91 Å3/Da / Density % sol: 69 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion / pH: 7.5 Details: 5-6% PEG 8K, 0.15M LITHIUM SULFATE, 0.1M HEPES AND 0.01M CALCIUM CHLORIDE, pH 7.5, VAPOR DIFFUSION, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: A1 |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.7→40 Å / Num. obs: 709014 / % possible obs: 83.5 % / Redundancy: 2.3 % / Rmerge(I) obs: 0.105 / Net I/σ(I): 9 |
Reflection shell | Resolution: 2.7→2.8 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.824 / Mean I/σ(I) obs: 1 / Num. unique all: 45803 / % possible all: 53.9 |
-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: Wild-type FHV coordinates (from 1992) Resolution: 2.7→40 Å / Occupancy max: 1 / Occupancy min: 1 / Cross valid method: NONE / σ(F): 0 Details: Cross-validation not used due to 20-fold non-crystallographic symmetry
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Solvent computation | Bsol: 53.3466 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 251.13 Å2 / Biso mean: 62.8606 Å2 / Biso min: 29.1 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→40 Å
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Refine LS restraints |
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LS refinement shell |
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Xplor file |
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