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- PDB-5wcu: Crystal structure of 167 bp nucleosome bound to the globular doma... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5wcu | ||||||
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Title | Crystal structure of 167 bp nucleosome bound to the globular domain of linker histone H5 | ||||||
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![]() | CHROMATIN BINDING PROTEIN/DNA / NUCLEOSOME CORE PARTICLE / HISTONE FOLD / CHROMOSOME / CHROMATIN / GLOBULAR DOMAIN / HISTONE H5 / GH5 / 167 BP NUCLEOSOME / CHROMATOSOME / NUCLEOSOME PACKING / 30 NM CHROMATIN FIBER / LINKER HISTONE H5 / LINKER DNA / NUCLEOSOME BINDING PROTEIN / PROTEIN DNA COMPLEXES / DNA BINDING / CHROMATIN HIGHER ORDER STRUCTURE / CHROMATIN FOLDING / CHROMATIN BINDING PROTEIN-DNA complex | ||||||
Function / homology | ![]() HDMs demethylate histones / Interleukin-7 signaling / PKMTs methylate histone lysines / Chromatin modifying enzymes / Condensation of Prophase Chromosomes / SUMOylation of chromatin organization proteins / RCAF complex / Metalloprotease DUBs / Factors involved in megakaryocyte development and platelet production / E3 ubiquitin ligases ubiquitinate target proteins ...HDMs demethylate histones / Interleukin-7 signaling / PKMTs methylate histone lysines / Chromatin modifying enzymes / Condensation of Prophase Chromosomes / SUMOylation of chromatin organization proteins / RCAF complex / Metalloprotease DUBs / Factors involved in megakaryocyte development and platelet production / E3 ubiquitin ligases ubiquitinate target proteins / RMTs methylate histone arginines / SIRT1 negatively regulates rRNA expression / NoRC negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / RNA Polymerase I Promoter Escape / polytene chromosome band / Formation of the beta-catenin:TCF transactivating complex / PRC2 methylates histones and DNA / HDACs deacetylate histones / Ub-specific processing proteases / Transcriptional regulation by small RNAs / Estrogen-dependent gene expression / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / larval somatic muscle development / Senescence-Associated Secretory Phenotype (SASP) / HATs acetylate histones / Assembly of the ORC complex at the origin of replication / Oxidative Stress Induced Senescence / UCH proteinases / polytene chromosome / negative regulation of DNA recombination / chromosome condensation / nuclear chromosome / heterochromatin organization / nucleosomal DNA binding / structural constituent of chromatin / nucleosome / nucleosome assembly / chromatin organization / chromosome / double-stranded DNA binding / nucleic acid binding / protein heterodimerization activity / protein-containing complex binding / chromatin / DNA binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() synthetic construct (others) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Jiang, J.S. / Zhou, B.R. | ||||||
![]() | ![]() Title: Revisit of Reconstituted 30-nm Nucleosome Arrays Reveals an Ensemble of Dynamic Structures. Authors: Zhou, B.R. / Jiang, J. / Ghirlando, R. / Norouzi, D. / Sathish Yadav, K.N. / Feng, H. / Wang, R. / Zhang, P. / Zhurkin, V. / Bai, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 675.2 KB | Display | ![]() |
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PDB format | ![]() | 531.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 551.9 KB | Display | ![]() |
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Full document | ![]() | 597.1 KB | Display | |
Data in XML | ![]() | 73.4 KB | Display | |
Data in CIF | ![]() | 103.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4qlcS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 5 types, 18 molecules AEKOBFLPCGMQDHNRUV
#1: Protein | Mass: 11488.410 Da / Num. of mol.: 4 / Fragment: UNP residues 39-136 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: His3, His3:CG31613, CG31613, His3:CG33803, CG33803, His3:CG33806, CG33806, His3:CG33809, CG33809, His3:CG33812, CG33812, His3:CG33815, CG33815, His3:CG33818, CG33818, His3:CG33821, CG33821, ...Gene: His3, His3:CG31613, CG31613, His3:CG33803, CG33803, His3:CG33806, CG33806, His3:CG33809, CG33809, His3:CG33812, CG33812, His3:CG33815, CG33815, His3:CG33818, CG33818, His3:CG33821, CG33821, His3:CG33824, CG33824, His3:CG33827, CG33827, His3:CG33830, CG33830, His3:CG33833, CG33833, His3:CG33836, CG33836, His3:CG33839, CG33839, His3:CG33842, CG33842, His3:CG33845, CG33845, His3:CG33848, CG33848, His3:CG33851, CG33851, His3:CG33854, CG33854, His3:CG33857, CG33857, His3:CG33860, CG33860, His3:CG33863, CG33863, His3:CG33866, CG33866 Production host: ![]() ![]() #2: Protein | Mass: 9279.875 Da / Num. of mol.: 4 / Fragment: UNP residues 22-103 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: His4, H4, His4r, H4r, CG3379, His4:CG31611, CG31611, His4:CG33869, CG33869, His4:CG33871, CG33871, His4:CG33873, CG33873, His4:CG33875, CG33875, His4:CG33877, CG33877, His4:CG33879, CG33879, ...Gene: His4, H4, His4r, H4r, CG3379, His4:CG31611, CG31611, His4:CG33869, CG33869, His4:CG33871, CG33871, His4:CG33873, CG33873, His4:CG33875, CG33875, His4:CG33877, CG33877, His4:CG33879, CG33879, His4:CG33881, CG33881, His4:CG33883, CG33883, His4:CG33885, CG33885, His4:CG33887, CG33887, His4:CG33889, CG33889, His4:CG33891, CG33891, His4:CG33893, CG33893, His4:CG33895, CG33895, His4:CG33897, CG33897, His4:CG33899, CG33899, His4:CG33901, CG33901, His4:CG33903, CG33903, His4:CG33905, CG33905, His4:CG33907, CG33907, His4:CG33909, CG33909 Production host: ![]() ![]() #3: Protein | Mass: 11352.236 Da / Num. of mol.: 4 / Fragment: UNP residues 15-118 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: His2A, H2a, His2A:CG31618, CG31618, His2A:CG33808, CG33808, His2A:CG33814, CG33814, His2A:CG33817, CG33817, His2A:CG33820, CG33820, His2A:CG33823, CG33823, His2A:CG33826, CG33826, His2A: ...Gene: His2A, H2a, His2A:CG31618, CG31618, His2A:CG33808, CG33808, His2A:CG33814, CG33814, His2A:CG33817, CG33817, His2A:CG33820, CG33820, His2A:CG33823, CG33823, His2A:CG33826, CG33826, His2A:CG33829, CG33829, His2A:CG33832, CG33832, His2A:CG33835, CG33835, His2A:CG33838, CG33838, His2A:CG33841, CG33841, His2A:CG33844, CG33844, His2A:CG33847, CG33847, His2A:CG33850, CG33850, His2A:CG33862, CG33862, His2A:CG33865, CG33865 Production host: ![]() ![]() #4: Protein | Mass: 10592.202 Da / Num. of mol.: 4 / Fragment: UNP residues 29-122 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: His2B, His2B:CG17949, CG17949, His2B:CG33868, CG33868, His2B:CG33870, CG33870, His2B:CG33872, CG33872, His2B:CG33874, CG33874, His2B:CG33876, CG33876, His2B:CG33878, CG33878, His2B:CG33880, ...Gene: His2B, His2B:CG17949, CG17949, His2B:CG33868, CG33868, His2B:CG33870, CG33870, His2B:CG33872, CG33872, His2B:CG33874, CG33874, His2B:CG33876, CG33876, His2B:CG33878, CG33878, His2B:CG33880, CG33880, His2B:CG33882, CG33882, His2B:CG33884, CG33884, His2B:CG33886, CG33886, His2B:CG33888, CG33888, His2B:CG33890, CG33890, His2B:CG33892, CG33892, His2B:CG33894, CG33894, His2B:CG33896, CG33896, His2B:CG33898, CG33898, His2B:CG33900, CG33900, His2B:CG33902, CG33902, His2B:CG33904, CG33904, His2B:CG33906, CG33906, His2B:CG33908, CG33908, His2B:CG33910, CG33910 Production host: ![]() ![]() #7: Protein | Mass: 8199.485 Da / Num. of mol.: 2 / Fragment: UNP residues 23-98 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-DNA chain , 2 types, 4 molecules ISJT
#5: DNA chain | Mass: 51318.695 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: 167 BP WIDOM 601 DNA / Source: (synth.) synthetic construct (others) #6: DNA chain | Mass: 51789.977 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: 167 BP WIDOM 601 DNA / Source: (synth.) synthetic construct (others) |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.23 Å3/Da / Density % sol: 61.92 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 4 / Details: 0.1 M NH4NO3, 10% MPD (v/v) |
-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 18, 2016 |
Radiation | Monochromator: Double crystal cryo-cooled Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.033 Å / Relative weight: 1 |
Reflection | Resolution: 5.53→49.63 Å / Num. obs: 15268 / % possible obs: 97.5 % / Observed criterion σ(I): 0 / Redundancy: 2.2 % / Biso Wilson estimate: 176.6 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 7.3 |
Reflection shell | Resolution: 5.53→5.73 Å / Redundancy: 2.2 % / Rmerge(I) obs: 1.706 / Mean I/σ(I) obs: 0.7 / % possible all: 95.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4QLC Resolution: 5.53→48.62 Å / Cross valid method: THROUGHOUT / σ(F): 1.93 / Phase error: 29.56 / Stereochemistry target values: TWIN_LSQ_F
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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: 5.53→48.62 Å
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Refine LS restraints |
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LS refinement shell |
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