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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 | ||||||
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![]() | TRANSPORT PROTEIN/RNA BINDING PROTEIN / nuclear transport / importin / exportin / karyopherin / nucleocytoplasmic / hnRNP / NLS / NES / TRANSPORT PROTEIN-RNA BINDING PROTEIN COMPLEX | ||||||
Function / homology | ![]() Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / Intraflagellar transport / Postmitotic nuclear pore complex (NPC) reformation / nuclear import signal receptor activity / nuclear localization sequence binding / small GTPase binding / cilium / protein import into nucleus / RNA binding / extracellular exosome ...Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / Intraflagellar transport / Postmitotic nuclear pore complex (NPC) reformation / nuclear import signal receptor activity / nuclear localization sequence binding / small GTPase binding / cilium / protein import into nucleus / RNA binding / extracellular exosome / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Imasaki, T. / Shimizu, T. / Hashimoto, H. / Hidaka, Y. / Kose, S. / Imamoto, N. / Yamada, M. / Sato, M. | ||||||
![]() | ![]() Title: 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 171.7 KB | Display | ![]() |
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PDB format | ![]() | 135.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 433.7 KB | Display | ![]() |
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Full document | ![]() | 451.6 KB | Display | |
Data in XML | ![]() | 29.6 KB | Display | |
Data in CIF | ![]() | 40.4 KB | Display | |
Arichive directory | ![]() ![]() | 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.) ![]() ![]() ![]() |
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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: ![]() |
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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: ![]() ![]() ![]() |
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: ![]() Starting 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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