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Open data
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Basic information
| Entry | Database: PDB / ID: 9kyl | ||||||
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| Title | Crystal structure of human TRIP4 in complex with 11bp dsDNA | ||||||
Components |
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Keywords | DNA BINDING PROTEIN/DNA / ASCH domain / dsDNA / complex / DNA BINDING PROTEIN-DNA complex | ||||||
| Function / homology | Function and homology informationRQC-trigger complex / regulation of myoblast differentiation / ribosome disassembly / ribosome-associated ubiquitin-dependent protein catabolic process / histone acetyltransferase binding / ubiquitin-like protein ligase binding / estrogen receptor signaling pathway / rescue of stalled ribosome / nuclear estrogen receptor binding / nuclear receptor binding ...RQC-trigger complex / regulation of myoblast differentiation / ribosome disassembly / ribosome-associated ubiquitin-dependent protein catabolic process / histone acetyltransferase binding / ubiquitin-like protein ligase binding / estrogen receptor signaling pathway / rescue of stalled ribosome / nuclear estrogen receptor binding / nuclear receptor binding / neuromuscular junction / protease binding / transcription coactivator activity / nuclear body / centrosome / regulation of DNA-templated transcription / protein kinase binding / positive regulation of DNA-templated transcription / protein-containing complex / zinc ion binding / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human)synthetic construct (others) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15 Å | ||||||
Authors | Guo, W.T. / Meng, C.Y. / Wen, Y. / Wu, B.X. | ||||||
| Funding support | 1items
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Citation | Journal: Structure / Year: 2025Title: Structural analysis of ASCH domain-containing proteins and their implications for nucleotide processing. Authors: Meng, C. / Shi, X. / Guo, W. / Jian, X. / Zhao, J. / Wen, Y. / Wang, R. / Li, Y. / Xu, S. / Chen, H. / Zhang, J. / Chen, M. / Chen, H. / Wu, B. | ||||||
| History |
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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 | 9kyl.cif.gz | 105.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9kyl.ent.gz | 62.3 KB | Display | PDB format |
| PDBx/mmJSON format | 9kyl.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9kyl_validation.pdf.gz | 452.3 KB | Display | wwPDB validaton report |
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| Full document | 9kyl_full_validation.pdf.gz | 457.3 KB | Display | |
| Data in XML | 9kyl_validation.xml.gz | 17.7 KB | Display | |
| Data in CIF | 9kyl_validation.cif.gz | 23.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ky/9kyl ftp://data.pdbj.org/pub/pdb/validation_reports/ky/9kyl | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9kyfC ![]() 9kygC ![]() 9kyhC ![]() 9kyiC ![]() 9kyjC ![]() 9kykC C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: ens_1 / Beg auth comp-ID: GLY / Beg label comp-ID: GLY / End auth comp-ID: LYS / End label comp-ID: LYS / Auth seq-ID: 434 - 571 / Label seq-ID: 25 - 162
NCS oper: (Code: givenMatrix: (-0.868638088938, -0.495447132024, 9.90734408269E-5), (-0.491590185714, 0.861850996126, -0.124707456819), (0.0617005652791, -0.108374350498, -0.992193549867)Vector: 15. ...NCS oper: (Code: given Matrix: (-0.868638088938, -0.495447132024, 9.90734408269E-5), Vector: |
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Components
| #1: Protein | Mass: 19747.652 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TRIP4, RQT4 / Production host: ![]() #2: DNA chain | | Mass: 3035.003 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) #3: DNA chain | | Mass: 3062.045 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) #4: Water | ChemComp-HOH / | Has protein modification | N | |
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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: 2.18 Å3/Da / Density % sol: 43.61 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 0.2 M L-Proline, 0.1 M HEPES pH 7.5, 10% w/v Polyethylene glycol 3,350 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.97776 Å |
| Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 4, 2016 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.97776 Å / Relative weight: 1 |
| Reflection | Resolution: 2.15→30 Å / Num. obs: 21150 / % possible obs: 99.9 % / Redundancy: 5.3 % / Biso Wilson estimate: 26.5 Å2 / CC1/2: 0.96 / Rmerge(I) obs: 0.139 / Rpim(I) all: 0.065 / Rrim(I) all: 0.154 / Net I/σ(I): 3 |
| Reflection shell | Resolution: 2.15→2.23 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.458 / Mean I/σ(I) obs: 1.8 / Num. unique obs: 2072 / CC1/2: 0.918 / Rpim(I) all: 0.232 / Rrim(I) all: 0.516 / % possible all: 99.4 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.15→29.83 Å / SU ML: 0.2593 / Cross valid method: FREE R-VALUE / σ(F): 1.41 / Phase error: 28.5026 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 31.77 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.15→29.83 Å
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| Refine LS restraints |
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| Refine LS restraints NCS | Type: Torsion NCS / Rms dev position: 0.920594485762 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| LS refinement shell |
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Homo sapiens (human)
X-RAY DIFFRACTION
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