+Open data
-Basic information
Entry | Database: PDB / ID: 1rvf | |||||||||
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Title | FAB COMPLEXED WITH INTACT HUMAN RHINOVIRUS | |||||||||
Components |
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Keywords | Virus/Immune system / POLYPROTEIN / COAT PROTEIN / CORE PROTEIN / RNA-DIRECTED RNA POLYMERASE / HYDROLASE / THIOL PROTEASE / MYRISTYLATION / COMPLEX (COAT PROTEIN-IMMUNOGLOBULIN) / Icosahedral virus / Virus-Immune system COMPLEX | |||||||||
Function / homology | Function and homology information lysis of host organelle involved in viral entry into host cell / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / : ...lysis of host organelle involved in viral entry into host cell / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / : / nucleoside-triphosphate phosphatase / protein complex oligomerization / monoatomic ion channel activity / DNA replication / RNA helicase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / symbiont-mediated suppression of host gene expression / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | Human rhinovirus 14 Human rhinovirus sp. Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4 Å | |||||||||
Authors | Smith, T.J. | |||||||||
Citation | Journal: Nature / Year: 1996 Title: Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon. Authors: Smith, T.J. / Chase, E.S. / Schmidt, T.J. / Olson, N.H. / Baker, T.S. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Structure Determination of an Fab Fragment that Neutralizes Human Rhinovirus 14 and Analysis of the Fab-Virus Complex Authors: Liu, H. / Smith, T.J. / Lee, W.M. / Mosser, A.G. / Rueckert, R.R. / Olson, N.H. / Cheng, R.H. / Baker, T.S. #2: Journal: Nature / Year: 1985 Title: Structure of a Human Common Cold Virus and Functional Relationship to Other Picornaviruses Authors: Rossmann, M.G. / Arnold, E. / Erickson, J.W. / Frankenberger, E.A. / Griffith, J.P. / Hecht, H.J. / Johnson, J.E. / Kamer, G. / Luo, M. / Mosser, A.G. / Rueckert, R.R. / Sherry, B. / Vriend, G. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rvf.cif.gz | 194.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rvf.ent.gz | 147.7 KB | Display | PDB format |
PDBx/mmJSON format | 1rvf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rv/1rvf ftp://data.pdbj.org/pub/pdb/validation_reports/rv/1rvf | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Symmetry | Point symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral)) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
-HUMAN RHINOVIRUS 14 COAT ... , 4 types, 4 molecules 1234
#1: Protein | Mass: 32560.549 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human rhinovirus 14 / Genus: Rhinovirus / Species: Human rhinovirus B / Strain: SEROTYPE 14 / References: UniProt: P03303 |
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#2: Protein | Mass: 28501.361 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human rhinovirus 14 / Genus: Rhinovirus / Species: Human rhinovirus B / Strain: SEROTYPE 14 / References: UniProt: P03303 |
#3: Protein | Mass: 26236.754 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human rhinovirus 14 / Genus: Rhinovirus / Species: Human rhinovirus B / Strain: SEROTYPE 14 / References: UniProt: P03303 |
#4: Protein | Mass: 7183.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human rhinovirus sp. / Genus: Rhinovirus / Strain: SEROTYPE 14 / References: UniProt: P03303 |
-Antibody , 2 types, 2 molecules LH
#5: Antibody | Mass: 11884.286 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / References: EMBL: X79906, UniProt: Q8K1F2*PLUS |
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#6: Antibody | Mass: 13006.354 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / References: PIR: S38950 |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 103 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.918 |
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Nov 3, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Num. obs: 259123 / % possible obs: 64.5 % / Observed criterion σ(I): 0 / Redundancy: 1.5 % / Rmerge(I) obs: 0.166 |
Reflection shell | Resolution: 4→4.18 Å / Redundancy: 1.5 % / Rsym value: 0.293 / % possible all: 46.9 |
Reflection | *PLUS Highest resolution: 4 Å / Lowest resolution: 20 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: SEE REFERENCE 1 Resolution: 4→10 Å / σ(F): 0
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Displacement parameters | Biso mean: 20 Å2 | ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 4→10 Å
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Refine LS restraints NCS | NCS model details: ICOSAHEDRAL 20-FOLD | ||||||||||||||||||
Xplor file |
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