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Open data
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Basic information
Entry | Database: PDB / ID: 6fml | ||||||||||||||||||||||||
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Title | CryoEM Structure INO80core Nucleosome complex | ||||||||||||||||||||||||
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Function / homology | TIP49 AAA-lid domain / UCH proteinases / Histone H3 signature 1. / Histone H2B signature. / Histone H3 signature 2. / HDACs deacetylate histones / HATs acetylate histones / RMTs methylate histone arginines / Ub-specific processing proteases / Histone H2A signature. ...TIP49 AAA-lid domain / UCH proteinases / Histone H3 signature 1. / Histone H2B signature. / Histone H3 signature 2. / HDACs deacetylate histones / HATs acetylate histones / RMTs methylate histone arginines / Ub-specific processing proteases / Histone H2A signature. / Metalloprotease DUBs / Meiotic synapsis / Interleukin-7 signaling / Packaging Of Telomere Ends / Pre-NOTCH Transcription and Translation / Formation of the beta-catenin:TCF transactivating complex / Histone H4 signature. / C-terminus of histone H2A / Condensation of Prophase Chromosomes / RuvB-like helicase 1 / P-loop containing nucleoside triphosphate hydrolase / Actin-related protein 5 / INO80 complex, subunit Ies6 / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | ||||||||||||||||||||||||
Specimen source | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() synthetic construct (others) | ||||||||||||||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||||||||||||||
![]() | Eustermann, S. / Schall, K. / Kostrewa, D. / Strauss, M. / Hopfner, K. | ||||||||||||||||||||||||
![]() | Journal: Nature / Year: 2018 Title: Structural basis for ATP-dependent chromatin remodelling by the INO80 complex. ![]() | ||||||||||||||||||||||||
Validation Report | ![]() ![]() ![]() | ||||||||||||||||||||||||
Date | Deposition: Jan 31, 2018 / Release: Apr 25, 2018
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmcif format | ![]() ![]() |
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PDB format | ![]() ![]() |
PDBML Plus | ![]() |
Others | ![]() |
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Links
-Related structure data
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Protein/peptide , 10 types, 18 molecules ABCDEFGHIJMQNROSPT
#1: Protein/peptide | Mass: 50451.848 Da / Num. of mol.: 3 Source: (gene. exp.) ![]() ![]() ![]() Gene: CTHT_0006820 / Production host: ![]() ![]() ![]() #2: Protein/peptide | Mass: 53212.746 Da / Num. of mol.: 3 Source: (gene. exp.) ![]() ![]() ![]() Gene: CTHT_0006170 / Production host: ![]() ![]() ![]() #3: Protein/peptide | | Mass: 210443.344 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Production host: ![]() ![]() #4: Protein/peptide | | Mass: 52018.512 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() Gene: CTHT_0004910 / Production host: ![]() ![]() #5: Protein/peptide | | Mass: 23127.523 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() Gene: CTHT_0032670 / Production host: ![]() ![]() #6: Protein/peptide | | Mass: 85996.453 Da / Num. of mol.: 1 Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() Gene: CTHT_0032660 / Production host: ![]() ![]() #9: Protein/peptide | Mass: 15289.904 Da / Num. of mol.: 2 / Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #10: Protein/peptide | ![]() Mass: 11263.231 Da / Num. of mol.: 2 / Source: (gene. exp.) ![]() ![]() Gene: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 Production host: ![]() ![]() ![]() #11: Protein/peptide | Mass: 13990.342 Da / Num. of mol.: 2 / Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #12: Protein/peptide | Mass: 13806.018 Da / Num. of mol.: 2 / Source: (gene. exp.) ![]() ![]() Gene: HIST1H2BC, H2BFL, HIST1H2BE, H2BFH, HIST1H2BF, H2BFG, HIST1H2BG, H2BFA, HIST1H2BI, H2BFK Production host: ![]() ![]() ![]() |
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-Nucleosomal DNA Strand ... , 2 types, 2 molecules KL
#7: DNA chain | Mass: 60652.645 Da / Num. of mol.: 1 / Source: (synth.) synthetic construct (others) |
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#8: DNA chain | Mass: 60376.426 Da / Num. of mol.: 1 / Source: (synth.) synthetic construct (others) |
-Non-polymers , 2 types, 7 molecules 


#13: Chemical | ChemComp-ADP / #14: Chemical | ChemComp-ATP / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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EM experiment | Aggregation state: PARTICLE / Reconstruction method: ![]() |
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Sample preparation
Component |
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Molecular weight | Value: 1 MDa / Experimental value: NO | ||||||||||||||||||||||||||||||
Source (natural) |
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Source (recombinant) |
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Buffer solution | Details: 20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside pH: 8 | ||||||||||||||||||||||||||||||
Specimen | Conc.: 1 mg/ml Details: Monodisperse sample: INO80core complex reconstituted with nucleosomal substrate was purified by gelfiltration. Addition of nucleotides or crosslinking was not required. Embedding applied: NO / Shadowing applied: NO / Staining applied ![]() ![]() | ||||||||||||||||||||||||||||||
Specimen support | Grid material: COPPER / Grid mesh size: 200 / Grid type: Quantifoil R2/1 | ||||||||||||||||||||||||||||||
Vitrification![]() | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 281 kelvins |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Microscope model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN![]() |
Electron lens | Mode: BRIGHT FIELD![]() |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 59.6 e/Å2 Details: Images were collected in movie mode with 4 frames per second and 10s total aquisition Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Number of grids imaged: 1 / Number of real images: 3992 |
Image scans | Movie frames/image: 40 / Used frames/image: 1-40 |
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Processing
Software | Name: PHENIX / Version: 1.13_2998: / Classification: refinement | ||||||||||||||||||||||||||||||||||||
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EM software |
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CTF correction![]() | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
Particle selection | Number of particles selected: 251692 | ||||||||||||||||||||||||||||||||||||
Symmetry | Point symmetry: C1 | ||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 4.34 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 33937 / Symmetry type: POINT |