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Yorodumi- PDB-1zo2: Structure of nuclear transport factor 2 (Ntf2) from Cryptosporidi... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1zo2 | ||||||
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| Title | Structure of nuclear transport factor 2 (Ntf2) from Cryptosporidium parvum | ||||||
Components | nuclear transport factor 2 | ||||||
Keywords | TRANSPORT PROTEIN / NUCLEAR TRANSPORT / Structural Genomics / Structural Genomics Consortium / SGC | ||||||
| Function / homology | Function and homology informationmRNA transport / protein import into nucleus / nuclear envelope / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Choe, J. / Artz, J.D. / Gao, M. / Lew, J. / Zhao, Y. / Arrowsmith, C. / Edwards, A. / Sundstrom, M. / Bochkarev, A. / Hui, R. / Structural Genomics Consortium (SGC) | ||||||
Citation | Journal: Mol.Biochem.Parasitol. / Year: 2007Title: Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Authors: Vedadi, M. / Lew, J. / Artz, J. / Amani, M. / Zhao, Y. / Dong, A. / Wasney, G.A. / Gao, M. / Hills, T. / Brokx, S. / Qiu, W. / Sharma, S. / Diassiti, A. / Alam, Z. / Melone, M. / Mulichak, A. ...Authors: Vedadi, M. / Lew, J. / Artz, J. / Amani, M. / Zhao, Y. / Dong, A. / Wasney, G.A. / Gao, M. / Hills, T. / Brokx, S. / Qiu, W. / Sharma, S. / Diassiti, A. / Alam, Z. / Melone, M. / Mulichak, A. / Wernimont, A. / Bray, J. / Loppnau, P. / Plotnikova, O. / Newberry, K. / Sundararajan, E. / Houston, S. / Walker, J. / Tempel, W. / Bochkarev, A. / Kozieradzki, I. / Edwards, A. / Arrowsmith, C. / Roos, D. / Kain, K. / Hui, R. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1zo2.cif.gz | 64.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1zo2.ent.gz | 47.2 KB | Display | PDB format |
| PDBx/mmJSON format | 1zo2.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1zo2_validation.pdf.gz | 436.5 KB | Display | wwPDB validaton report |
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| Full document | 1zo2_full_validation.pdf.gz | 441 KB | Display | |
| Data in XML | 1zo2_validation.xml.gz | 13.2 KB | Display | |
| Data in CIF | 1zo2_validation.cif.gz | 18.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zo/1zo2 ftp://data.pdbj.org/pub/pdb/validation_reports/zo/1zo2 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1txjC ![]() 1xccC ![]() 1y6zC ![]() 1z6gC ![]() 1z7dC ![]() 1z81C ![]() 2a22C ![]() 2a4aC ![]() 2aifC ![]() 2amxC ![]() 2aqwC ![]() 2av4C ![]() 2awpC ![]() 2ayvC ![]() 2b71C ![]() 2bddC ![]() 2f4zC ![]() 2fdsC ![]() 2ffcC ![]() 2fo3C ![]() 2fu0C ![]() 2ghiC ![]() 2h1rC ![]() 2h2yC ![]() 2h66C ![]() 2hjrC ![]() 2hteC ![]() 2hvgC ![]() 3pggC ![]() 3tb2C ![]() 1gybS S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 14698.395 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: 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: 2.1 Å3/Da / Density % sol: 41.7 % |
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| Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: PEG 3350, Ammonium phosphate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: ROTATING ANODE / Type: RIGAKU FR-E / Wavelength: 1.5418 Å |
| Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: May 11, 2005 |
| Radiation | Monochromator: CONFOCAL MAXFLUX OPTICS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
| Reflection | Resolution: 1.6→35.3 Å / Num. all: 28649 / Num. obs: 28649 / % possible obs: 91.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Biso Wilson estimate: 22.5 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 35.7 |
| Reflection shell | Resolution: 1.6→1.66 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.269 / Mean I/σ(I) obs: 5.2 / % possible all: 56.2 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDb entry 1GYB Resolution: 1.6→35.16 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 823352.82 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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| Solvent computation | Solvent model: FLAT MODEL / Bsol: 51.8368 Å2 / ksol: 0.404979 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 19.3 Å2
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| Refine analyze |
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| Refinement step | Cycle: LAST / Resolution: 1.6→35.16 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 1.6→1.7 Å / Rfactor Rfree error: 0.028 / Total num. of bins used: 6
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