+Open data
-Basic information
Entry | Database: PDB / ID: 5xbk | ||||||
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Title | Crystal structure of human Importin4 | ||||||
Components |
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Keywords | PROTEIN TRANSPORT / Histone / Chromatin / Assembly | ||||||
Function / homology | Function and homology information nuclear import signal receptor activity / nuclear localization sequence binding / protein localization to nucleus / small GTPase binding / protein import into nucleus / structural constituent of chromatin / nucleosome / protein heterodimerization activity / chromatin / protein-containing complex ...nuclear import signal receptor activity / nuclear localization sequence binding / protein localization to nucleus / small GTPase binding / protein import into nucleus / structural constituent of chromatin / nucleosome / protein heterodimerization activity / chromatin / protein-containing complex / DNA binding / nucleoplasm / membrane / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Xenopus laevis (African clawed frog) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.223 Å | ||||||
Authors | Song, J.J. / Yoon, J. | ||||||
Citation | Journal: J. Mol. Biol. / Year: 2018 Title: Integrative Structural Investigation on the Architecture of Human Importin4_Histone H3/H4_Asf1a Complex and Its Histone H3 Tail Binding Authors: Yoon, J. / Kim, S.J. / An, S. / Cho, S. / Leitner, A. / Jung, T. / Aebersold, R. / Hebert, H. / Cho, U.S. / Song, J.J. #1: Journal: To Be Published Title: Structural insights into the Architecture of human Importin4_Histone H3/H4_Asfla complex and its histone H3 tail binding Authors: Yoon, J. / Song, J.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5xbk.cif.gz | 540.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5xbk.ent.gz | 454.9 KB | Display | PDB format |
PDBx/mmJSON format | 5xbk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xb/5xbk ftp://data.pdbj.org/pub/pdb/validation_reports/xb/5xbk | HTTPS FTP |
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-Related structure data
Related structure data | 5xahSC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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4 |
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Unit cell |
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-Components
#1: Protein | Mass: 44835.434 Da / Num. of mol.: 4 / Fragment: UNP residues 668-1081 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: IPO4, IMP4B, RANBP4 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: Q8TEX9 #2: Protein/peptide | | Mass: 1949.286 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xenopus laevis (African clawed frog) Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: P84233*PLUS |
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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: 2.36 Å3/Da / Density % sol: 47.95 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: Sodium tartrate, PEG3350 |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 5C (4A) / Wavelength: 0.9795 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: CCD / Date: Sep 9, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→50 Å / Num. obs: 26893 / % possible obs: 99.2 % / Redundancy: 7.3 % / Biso Wilson estimate: 90.87 Å2 / Rmerge(I) obs: 0.102 / Rpim(I) all: 0.041 / Rrim(I) all: 0.11 / Χ2: 3.232 / Net I/σ(I): 12.9 / Num. measured all: 247205 |
Reflection shell | Resolution: 3.2→3.36 Å / Mean I/σ(I) obs: 2.34 / Rsym value: 0.85 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5XAH Resolution: 3.223→49.977 Å / SU ML: 0.47 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 32.12 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.223→49.977 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -2.1702 Å / Origin y: -9.8608 Å / Origin z: -29.957 Å
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Refinement TLS group | Selection details: all |