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Open data
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Basic information
Entry | Database: PDB / ID: 1uf2 | ||||||
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Title | The Atomic Structure of Rice dwarf Virus (RDV) | ||||||
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![]() | VIRUS / VIRUS COMPONENTS / Icosahedral virus | ||||||
Function / homology | ![]() : / viral outer capsid / host cell cytoplasmic vesicle / viral capsid / molecular adaptor activity / host cell cytoplasm / host cell surface receptor binding / fusion of virus membrane with host plasma membrane / viral envelope / structural molecule activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Nakagawa, A. / Miyazaki, N. / Taka, J. / Naitow, H. / Ogawa, A. / Fujimoto, Z. / Mizuno, H. / Higashi, T. / Watanabe, Y. / Omura, T. ...Nakagawa, A. / Miyazaki, N. / Taka, J. / Naitow, H. / Ogawa, A. / Fujimoto, Z. / Mizuno, H. / Higashi, T. / Watanabe, Y. / Omura, T. / Cheng, R.H. / Tsukihara, T. | ||||||
![]() | ![]() Title: The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins. Authors: Nakagawa, A. / Miyazaki, N. / Taka, J. / Naitow, H. / Ogawa, A. / Fujimoto, Z. / Mizuno, H. / Higashi, T. / Watanabe, Y. / Omura, T. / Cheng, R.H. / Tsukihara, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.4 MB | Display | ![]() |
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PDB format | ![]() | 1.1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 570.3 KB | Display | ![]() |
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Full document | ![]() | 780.7 KB | Display | |
Data in XML | ![]() | 258.1 KB | Display | |
Data in CIF | ![]() | 347.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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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
#1: Protein | Mass: 114400.461 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Virus particle / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 46528.781 Da / Num. of mol.: 13 / Source method: isolated from a natural source / Details: Virus particle / Source: (natural) ![]() ![]() |
#3: Protein | Mass: 55409.137 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: Virus particle / Source: (natural) ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: His-Mg buffer, MgCl2, PEG8000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
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Crystal grow | *PLUS Details: Mizuno, H., (1991) J. Mol. Biol., 219, 665. |
-Data collection
Diffraction |
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Detector |
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Radiation |
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Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | ||||||||||||||||||
Reflection | Resolution: 3.5→230 Å / Num. all: 3072898 / Num. obs: 3072898 / % possible obs: 97.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.9 % / Biso Wilson estimate: 41.7 Å2 / Rmerge(I) obs: 0.186 / Net I/σ(I): 3.1 | ||||||||||||||||||
Reflection shell | Resolution: 3.5→3.59 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.783 / Mean I/σ(I) obs: 0.9 / Rsym value: 0.783 / % possible all: 91.5 | ||||||||||||||||||
Reflection | *PLUS Num. obs: 3001937 / Num. measured all: 17806888 |
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Processing
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Refinement | Method to determine structure: Molecular Replacement Averaging Starting model: Cryo-electronmicrograph Resolution: 3.5→228.74 Å / Rfactor Rfree error: 0.001 / Isotropic thermal model: Individual / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: flat model / Bsol: 89.8 Å2 / ksol: 0.399 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 39.5 Å2 | ||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.5→228.74 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: constraint | ||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 3.5→3.72 Å / Rfactor Rfree error: 0.003 / Total num. of bins used: 6
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Xplor file |
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Refine LS restraints | *PLUS
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