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Open data
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Basic information
| Entry | Database: PDB / ID: 2z5o | ||||||
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| Title | Complex of Transportin 1 with JKTBP NLS | ||||||
Components |
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Keywords | TRANSPORT PROTEIN/RNA BINDING PROTEIN / nuclear transport / importin / exportin / karyopherin / nucleocytoplasmic / hnRNP / NLS / NES / TRANSPORT PROTEIN-RNA BINDING PROTEIN COMPLEX | ||||||
| Function / homology | Function and homology informationTristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / Intraflagellar transport / nuclear localization sequence binding / Postmitotic nuclear pore complex (NPC) reformation / nuclear import signal receptor activity / small GTPase binding / protein import into nucleus / cilium / nucleolus / RNA binding ...Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / Intraflagellar transport / nuclear localization sequence binding / Postmitotic nuclear pore complex (NPC) reformation / nuclear import signal receptor activity / small GTPase binding / protein import into nucleus / cilium / nucleolus / RNA binding / extracellular exosome / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å | ||||||
Authors | Imasaki, T. / Shimizu, T. / Hashimoto, H. / Hidaka, Y. / Kose, S. / Imamoto, N. / Yamada, M. / Sato, M. | ||||||
Citation | Journal: Mol.Cell / Year: 2007Title: Structural basis for substrate recognition and dissociation by human transportin 1 Authors: Imasaki, T. / Shimizu, T. / Hashimoto, H. / Hidaka, Y. / Kose, S. / Imamoto, N. / Yamada, M. / Sato, M. | ||||||
| History |
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| Remark 999 | SEQUENCE Because the electron density for all amino acids of protein in chain B was poor, the ...SEQUENCE Because the electron density for all amino acids of protein in chain B was poor, the authors were unable to assign side chains of them. In addition, residue numbers are arbitrary, not consistent with the UNP residues numbering. The following is the one-letter sequence for the protein in chain B modeled in this structure, UniProtKB entry O14979(residues 396-420): YSGQQSTYGKASRGGGNHQNNYQPY |
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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 | 2z5o.cif.gz | 171.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2z5o.ent.gz | 135.5 KB | Display | PDB format |
| PDBx/mmJSON format | 2z5o.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2z5o_validation.pdf.gz | 433.7 KB | Display | wwPDB validaton report |
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| Full document | 2z5o_full_validation.pdf.gz | 451.6 KB | Display | |
| Data in XML | 2z5o_validation.xml.gz | 29.6 KB | Display | |
| Data in CIF | 2z5o_validation.cif.gz | 40.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z5/2z5o ftp://data.pdbj.org/pub/pdb/validation_reports/z5/2z5o | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 2z5jC ![]() 2z5kC ![]() 2z5mC ![]() 2z5nC ![]() 1qbkS S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 101408.438 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGEX6P3 / Species (production host): Escherichia coli / Production host: ![]() |
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| #2: Protein/peptide | Mass: 869.063 Da / Num. of mol.: 1 / Fragment: Region of interest in the sequence / Source method: obtained synthetically Details: Chemical synthesis. This sequence occurs naturally in humans. |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.76 Å3/Da / Density % sol: 67.28 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.6 Details: 0.1M Tris-HCl pH 8.6, 14% (w/v) PEG 8000, 0.1M NaH2PO4, 0.015mM Phenol, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1 Å |
| Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 7, 2005 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 3.2→50 Å / Num. all: 25190 / Num. obs: 23669 / % possible obs: 94.9 % / Rmerge(I) obs: 0.071 / Net I/σ(I): 13.2 |
| Reflection shell | Resolution: 3.2→3.31 Å / Rmerge(I) obs: 0.434 / Mean I/σ(I) obs: 3.6 / % possible all: 82.8 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRY 1QBK Resolution: 3.2→47.57 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.911 / SU B: 54.103 / SU ML: 0.408 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.491 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 129.703 Å2
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| Refinement step | Cycle: LAST / Resolution: 3.2→47.57 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 3.2→3.283 Å / Total num. of bins used: 20
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group |
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Homo sapiens (human)
X-RAY DIFFRACTION
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