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- EMDB-17025: INO80 core bound to hexasome composite map of state 2 -

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Basic information

Entry
Database: EMDB / ID: EMD-17025
TitleINO80 core bound to hexasome composite map of state 2
Map dataCtINO80 hexasome complex composite map
Sample
  • Complex: INO80 core module in complex with hexasome
    • Complex: Chromatin remodeler INO80
      • Protein or peptide: x 6 types
    • Complex: Histones
      • Protein or peptide: x 4 types
    • Complex: DNA
      • DNA: x 2 types
  • Ligand: x 4 types
KeywordsATP-dependent chromatin remodeler / DNA BINDING PROTEIN
Function / homology
Function and homology information


DASH complex / protein transport along microtubule to mitotic spindle pole body / mitotic sister chromatid biorientation / attachment of spindle microtubules to kinetochore / attachment of mitotic spindle microtubules to kinetochore / Ino80 complex / negative regulation of megakaryocyte differentiation / ATP-dependent activity, acting on DNA / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes ...DASH complex / protein transport along microtubule to mitotic spindle pole body / mitotic sister chromatid biorientation / attachment of spindle microtubules to kinetochore / attachment of mitotic spindle microtubules to kinetochore / Ino80 complex / negative regulation of megakaryocyte differentiation / ATP-dependent activity, acting on DNA / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Deposition of new CENPA-containing nucleosomes at the centromere / nucleosomal DNA binding / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / telomere organization / Meiotic synapsis / Interleukin-7 signaling / RNA Polymerase I Promoter Opening / epigenetic regulation of gene expression / Assembly of the ORC complex at the origin of replication / SUMOylation of chromatin organization proteins / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / DNA methylation / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Chromatin modifications during the maternal to zygotic transition (MZT) / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / HCMV Late Events / innate immune response in mucosa / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / HDACs deacetylate histones / Nonhomologous End-Joining (NHEJ) / helicase activity / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / NoRC negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / G2/M DNA damage checkpoint / HDMs demethylate histones / B-WICH complex positively regulates rRNA expression / DNA Damage/Telomere Stress Induced Senescence / heterochromatin formation / mitotic spindle / PKMTs methylate histone lysines / Metalloprotease DUBs / Meiotic recombination / kinetochore / Pre-NOTCH Transcription and Translation / RMTs methylate histone arginines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / Transcriptional regulation of granulopoiesis / structural constituent of chromatin / UCH proteinases / antimicrobial humoral immune response mediated by antimicrobial peptide / nucleosome / nucleosome assembly / E3 ubiquitin ligases ubiquitinate target proteins / antibacterial humoral response / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / chromatin organization / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / HATs acetylate histones / Processing of DNA double-strand break ends / gene expression / Senescence-Associated Secretory Phenotype (SASP) / DNA helicase / Oxidative Stress Induced Senescence / Estrogen-dependent gene expression / chromosome, telomeric region / Ub-specific processing proteases / defense response to Gram-positive bacterium / cadherin binding / chromatin remodeling / protein heterodimerization activity / Amyloid fiber formation / negative regulation of cell population proliferation / DNA repair / ATP hydrolysis activity / protein-containing complex / DNA binding / RNA binding / extracellular space / extracellular exosome / extracellular region / nucleoplasm / ATP binding / identical protein binding
Similarity search - Function
DASH complex subunit Dad4 / DASH complex subunit Dad4 / INO80 complex subunit B-like conserved region / INO80 complex, subunit Ies2 / INO80 complex, subunit Ies6 / PAPA-1-like conserved region / PAPA-1 / Vps72/YL1, C-terminal / YL1 nuclear protein C-terminal domain / YL1 nuclear protein C-terminal domain ...DASH complex subunit Dad4 / DASH complex subunit Dad4 / INO80 complex subunit B-like conserved region / INO80 complex, subunit Ies2 / INO80 complex, subunit Ies6 / PAPA-1-like conserved region / PAPA-1 / Vps72/YL1, C-terminal / YL1 nuclear protein C-terminal domain / YL1 nuclear protein C-terminal domain / RuvB-like / RuvB-like, AAA-lid domain / RuvBL1/2, DNA/RNA binding domain / TIP49 P-loop domain / TIP49 AAA-lid domain / TIP49, P-loop domain / Actin / Actin family / Actin / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / Histone H2A / Histone 2A / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / ATPase, nucleotide binding domain / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
INO80 complex subunit B-like conserved region domain-containing protein / RuvB-like helicase / RuvB-like helicase / Uncharacterized protein / Vps72/YL1 C-terminal domain-containing protein / Histone H4 / Histone H2B type 1-C/E/F/G/I / Histone H3.1 / Histone H2A type 1-C
Similarity search - Component
Biological speciesThermochaetoides thermophila (fungus) / Homo sapiens (human) / Synthetic construct (others) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.7 Å
AuthorsZhang M / Jungblut A / Hoffmann T / Eustermann S
Funding support Germany, European Union, 4 items
OrganizationGrant numberCountry
EIPOD fellowship under Marie Sklodowska-Curie Actions COFUND847543 Germany
European Research Council (ERC)833613European Union
German Research Foundation (DFG)CRC136 Germany
German Research Foundation (DFG)CRC1064 Germany
CitationJournal: Acta Crystallogr D Biol Crystallogr / Year: 2010
Title: Features and development of Coot.
Authors: P Emsley / B Lohkamp / W G Scott / K Cowtan /
Abstract: Coot is a molecular-graphics application for model building and validation of biological macromolecules. The program displays electron-density maps and atomic models and allows model manipulations ...Coot is a molecular-graphics application for model building and validation of biological macromolecules. The program displays electron-density maps and atomic models and allows model manipulations such as idealization, real-space refinement, manual rotation/translation, rigid-body fitting, ligand search, solvation, mutations, rotamers and Ramachandran idealization. Furthermore, tools are provided for model validation as well as interfaces to external programs for refinement, validation and graphics. The software is designed to be easy to learn for novice users, which is achieved by ensuring that tools for common tasks are 'discoverable' through familiar user-interface elements (menus and toolbars) or by intuitive behaviour (mouse controls). Recent developments have focused on providing tools for expert users, with customisable key bindings, extensions and an extensive scripting interface. The software is under rapid development, but has already achieved very widespread use within the crystallographic community. The current state of the software is presented, with a description of the facilities available and of some of the underlying methods employed.
History
DepositionApr 5, 2023-
Header (metadata) releaseJul 26, 2023-
Map releaseJul 26, 2023-
UpdateJul 24, 2024-
Current statusJul 24, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_17025.png

Downloads & links

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Map

FileDownload / File: emd_17025.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCtINO80 hexasome complex composite map
Projections & slices

Image control

Size
Brightness
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Others
AxesX (Sec.)Y (Row.)Z (Col.)
0.82 Å/pix.
x 360 pix.
= 295.92 Å		0.82 Å/pix.
x 360 pix.
= 295.92 Å		0.82 Å/pix.
x 360 pix.
= 295.92 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.822 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 1.1
Minimum - Maximum-5.4421988 - 11.5145035
Average (Standard dev.)0.012625556 (±0.32389066)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 295.92 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: CtINO80 hexasome complex overall refinement (used as reference...

Fileemd_17025_additional_1.map
AnnotationCtINO80 hexasome complex overall refinement (used as reference for composite)
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : INO80 core module in complex with hexasome

EntireName: INO80 core module in complex with hexasome
Components
  • Complex: INO80 core module in complex with hexasome
    • Complex: Chromatin remodeler INO80
      • Protein or peptide: RuvB-like protein 1
      • Protein or peptide: RuvB-like protein 2
      • Protein or peptide: Chromatin-remodeling ATPase Ino80
      • Protein or peptide: Ino eighty subunit 2
      • Protein or peptide: Chromatin-remodeling complex subunit IES6
      • Protein or peptide: Actin-related protein 5
    • Complex: Histones
      • Protein or peptide: Histone H3.1
      • Protein or peptide: Histone H4
      • Protein or peptide: Histone H2A
      • Protein or peptide: Histone H2B
    • Complex: DNA
      • DNA: DNA strand 1
      • DNA: DNA Strand 2
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
  • Ligand: MAGNESIUM ION
  • Ligand: TETRAFLUOROALUMINATE ION
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE

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Supramolecule #1: INO80 core module in complex with hexasome

SupramoleculeName: INO80 core module in complex with hexasome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#12
Details: 11-subunit ct INO80 contains two modules (core and Arp8 module) Each module was picked and analyzed separately The core module + hexasome has an overall weight of 0.861MDa The 11-subunit ct ...Details: 11-subunit ct INO80 contains two modules (core and Arp8 module) Each module was picked and analyzed separately The core module + hexasome has an overall weight of 0.861MDa The 11-subunit ct INO80 + hexasome has an overall weight of 1.1MDa Ino80, Ies2, Ies6, Ies4,Arp6, Rvb1, Rvb2, Arp8, Arp4, Actin, Taf14 Hexasome DNA, 2xH3, 2xH4, H2A, H2B
Molecular weightTheoretical: 861 KDa

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Supramolecule #2: Chromatin remodeler INO80

SupramoleculeName: Chromatin remodeler INO80 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#6
Source (natural)Organism: Thermochaetoides thermophila (fungus)

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Supramolecule #3: Histones

SupramoleculeName: Histones / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #9-#12
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #4: DNA

SupramoleculeName: DNA / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #7-#8
Source (natural)Organism: Synthetic construct (others)

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Macromolecule #1: RuvB-like protein 1

MacromoleculeName: RuvB-like protein 1 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Thermochaetoides thermophila (fungus)
Molecular weightTheoretical: 50.451848 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MVQISEVRGN TRDHRTAAHT HIKGLGLNSS GIAEKQAAGF VGQCAAREAC GVVVDLIKAH KMAGRGVLLA GGPGTGKTAL ALAISQELG TKIPFCPITG SEIYSTEVKK TEVLMENFRR AIGLRVRETK DVYEGEVTEM TPEEAENPLG GYGKTISTLL I GLKSARGQ ...String:
MVQISEVRGN TRDHRTAAHT HIKGLGLNSS GIAEKQAAGF VGQCAAREAC GVVVDLIKAH KMAGRGVLLA GGPGTGKTAL ALAISQELG TKIPFCPITG SEIYSTEVKK TEVLMENFRR AIGLRVRETK DVYEGEVTEM TPEEAENPLG GYGKTISTLL I GLKSARGQ KKLRLDPSIY EAIQKERVQV GDVIYIETNT GACKRVGRSD AYATEFDLEA EEYVPIPKGE VHKKKEIVQD VT LHDLDVA NARPQGGQDI ISMMGQLMKP KMTEITDKLR MEINKVVQKY INQGVAELIP GVLFIDEAHM LDIECFTYLN KAL ESPIAP IVVLASNRGI ATIRGADDLK AAHGIPPDFL QRLLIIPTHP YEPDEIRRIV RIRAQTEGVQ LTDAAVDRVA EHGV RISLR YCLQLLAPAS ILARVNGRTQ VDVQDIAEAE ELFLDARRSA NILTSTGESG GLHGFIS

UniProtKB: RuvB-like helicase

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Macromolecule #2: RuvB-like protein 2

MacromoleculeName: RuvB-like protein 2 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Thermochaetoides thermophila (fungus)
Molecular weightTheoretical: 53.212746 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAAPLVTSVT ETKELRGLNL IAAHSHIRGL GVDADTLEPR PSSQGLVGQE KARKAAAVVL EMIKQGKIAG RAVLIAGPPS TGKTAIAMG MAQSLGQDVP FTTLAASEIF SLEMSKTEAL TQAFRKSIGV RIKEESEIME GEVVEIQIDR SVTGGAKQGK L TIKTTDME ...String:
MAAPLVTSVT ETKELRGLNL IAAHSHIRGL GVDADTLEPR PSSQGLVGQE KARKAAAVVL EMIKQGKIAG RAVLIAGPPS TGKTAIAMG MAQSLGQDVP FTTLAASEIF SLEMSKTEAL TQAFRKSIGV RIKEESEIME GEVVEIQIDR SVTGGAKQGK L TIKTTDME AIYDMGSKMI DAMTKERVMA GDIISIDKSS GKITKLGRSY ARSRDYDAMG VDTKFLQCPE GELQKRKEVV HT VSLHEID VINSRTQGFL ALFSGDTGEI RSEIRDQINT KVAEWKEEGK AEIVPGVLFI DEVHMLDIEC FSYINRALES DLA PIVIMA SNRGVSRIRG TDYKSPHGLP LDFLDRVVII NTHPYTPDEL RQILSIRAQE EEVDLTPDAL ALLTKIGQEA GLRY ASNLI TTSQLIAAKR RAKQVGVEDV QRSFKLFYDP ARSVRFVQES EKRLIGNDGV VDFSYQGAAE AAAPTLPAAA PVDPV GGEK MDMS

UniProtKB: RuvB-like helicase

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Macromolecule #3: Chromatin-remodeling ATPase Ino80

MacromoleculeName: Chromatin-remodeling ATPase Ino80 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Thermochaetoides thermophila (fungus)
Molecular weightTheoretical: 130.887656 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: LELKFQSKGY NQIYDQIWRD LARKDVSKVF RLATDSYATK ASNLKKTAIL ASKEAKRWQL RTNKGTKDLQ ARAKRVMRDM MGFWKRNER EERDLRKAAE RLELENARKE EADREAARQR RKLNFLISQT ELYSHFISKK IKTHEVERST DHPDVATDEK D KIPEPTLN ...String:
LELKFQSKGY NQIYDQIWRD LARKDVSKVF RLATDSYATK ASNLKKTAIL ASKEAKRWQL RTNKGTKDLQ ARAKRVMRDM MGFWKRNER EERDLRKAAE RLELENARKE EADREAARQR RKLNFLISQT ELYSHFISKK IKTHEVERST DHPDVATDEK D KIPEPTLN INVPEPTGPI APKVTDFNSL DFDNEDESAL QAAAMANAQN AIAEAQKKAR EFNKDETKLD EDGEMNFQHP EL TEFEVAQ PKLLNCQLKE YQLKGLNWLV NLYEQGINGI LADEMGLGKT VQSISVMAYL AERYDIWGPF LVVAPASTLH NWQ QEVSKF VPDFKVLPYW GTAADRKVLR KFWDRKHTTY KKDSPFHVMI TSYQLVVSDV AYFQKMKWQY MILDEAQAIK SSQS SRWKC LLGFHCRNRL LLTGTPIQNN MQELWALLHF IMPSLFDSHD EFSEWFSKDI ESHAQSNTKL NEDQLKRLHM ILKPF MLRR VKKHVQKELG DKIEIDVFCE LSYRQRAMYQ SLRNQISIMD LIEKATVGDN EDSATLMNLV MQFRKVCNHP DLFERA DTS SPFFCGHFAE TGSFLREGTN VALGYSTRSL VEYRLPRLIW CDGGRLDKPG PGNLVAGFRS KYLNHMMNIW TPENIRS SL EGIENFTWLR FVDTSLQEAY RASHTDVFAR AVDLASKQNR LGHMQIVYDE PEDKKWTPVH ALFQICEREN PKAVAEIT T EGVLRDLMNI ARVKYRELGL CRLEKAARPR ASAPPIEVVC DSRSAVIERE NIMFHPAMRK ALFGPTPSEI KEASFGPRP VTLYPPRALL PAPDHDKQRF TNITVPSMAR FVTDSGKLAK LDELLRELKE GGHRVLLYFQ MTRMIDLMEE YLTYRNYKYC RLDGSTKLE DRRDTVADFQ TRPEIFIFLL STRAGGLGIN LTTADTVIFY DSDWNPTIDS QAMDRAHRLG QTKQVTVYRL I TRGTIEER IRKRALQKEE VQRVVITGTG SVDFSGRRPP ENRNRDIAMW LADDEQAEMI ERREKELIES GEYDKIMQQR RK GGKRKRG AANGDTVPSL EDMYHEGEGH FDDNKGSGAA TPVDADSLGR GGKRKKAGGS KKAKTTKQRL AIADGEIDID YKD DDDKGT DYKDDDDK

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Macromolecule #4: Ino eighty subunit 2

MacromoleculeName: Ino eighty subunit 2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Thermochaetoides thermophila (fungus)
Molecular weightTheoretical: 53.34598 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSTRPRRHAA QRASQAITDL ADRDRESDHS HGPISSRMSS FNSSSRSRLP GKGIASVSRS EAGGASDPEH IHLTVKLPSS KLRQATSSS GIKKAGSVGS SSSSSGGGKA AVKRARGGKR SRVLESSEEE EEENEVEVLG DEDEEEEEEE DEIEVREGEG Y DEDEEDVE ...String:
MSTRPRRHAA QRASQAITDL ADRDRESDHS HGPISSRMSS FNSSSRSRLP GKGIASVSRS EAGGASDPEH IHLTVKLPSS KLRQATSSS GIKKAGSVGS SSSSSGGGKA AVKRARGGKR SRVLESSEEE EEENEVEVLG DEDEEEEEEE DEIEVREGEG Y DEDEEDVE DEDEEMQDLG EEDADGEDDE MDVDAEGEED ADGDVNMDAG VVGARATTVR AVPPAIKVTK PPKESPSNGK AA TASKAND NAVPVKRPAP DSDDESLSSL ESEPEEEVNV AGGEDAEGED DDAEGEVDAE GEEEEEEEEI EVADEDAEGE DVE QDEDED EEEEDDDDEM ISRAQTPDMS RLTARQRARL GEASGEYLKL SDEVQSKKHF TAEELSMRRA EMARRRRNLS EKRN EEIKM ETVNKLLKKQ APRTTRRAAQ AAAAAEEAEE AAKQPKRPDP MMIRWVNNKM GSVVAVPEEL LGTHAGVVFG AGPGK GLPA GKMVEEVS

UniProtKB: INO80 complex subunit B-like conserved region domain-containing protein

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Macromolecule #5: Chromatin-remodeling complex subunit IES6

MacromoleculeName: Chromatin-remodeling complex subunit IES6 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Thermochaetoides thermophila (fungus)
Molecular weightTheoretical: 23.127523 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSNPDAQSAQ AAHQALVEQL DLHSIHKTFR NPNWRPNQRR NKTIKAILGE SQRKEASSTS AVATPRADDN GGGSGADTPA NNDNNDGLS TSGTSTPANG NGSGAGTPAS NGQPNLAQAS RSLQKLVLEK SLASAQAPDK KAANGFASSA PTATYTNIES A PSLAPMKH ...String:
MSNPDAQSAQ AAHQALVEQL DLHSIHKTFR NPNWRPNQRR NKTIKAILGE SQRKEASSTS AVATPRADDN GGGSGADTPA NNDNNDGLS TSGTSTPANG NGSGAGTPAS NGQPNLAQAS RSLQKLVLEK SLASAQAPDK KAANGFASSA PTATYTNIES A PSLAPMKH YCDVTGLPAP YLDPKTRLRY HNKEIFAMIR NLPQGMGEQF LEARGAHTVL K

UniProtKB: Vps72/YL1 C-terminal domain-containing protein

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Macromolecule #6: Actin-related protein 5

MacromoleculeName: Actin-related protein 5 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Thermochaetoides thermophila (fungus)
Molecular weightTheoretical: 87.773086 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAPSAVAEPP PIPQRDEPWK RLPPPTVYPV KEARFEKYIP PQLDGRERAL AQPPGQVAIV IDNGSHSVRA GWNFEDKPRL AIPPIMSKY RDRKMGKTFS FAGSDCYADT TARSHIRNAF EAGTGIVSNW DVMEHVLDYV FVKLGMNECD GAIDMPIVMT E AVANLPYS ...String:
MAPSAVAEPP PIPQRDEPWK RLPPPTVYPV KEARFEKYIP PQLDGRERAL AQPPGQVAIV IDNGSHSVRA GWNFEDKPRL AIPPIMSKY RDRKMGKTFS FAGSDCYADT TARSHIRNAF EAGTGIVSNW DVMEHVLDYV FVKLGMNECD GAIDMPIVMT E AVANLPYS RKSMSEIIFE CYGAPSLVYG IDSLFSFRHN QGQTGLVVSS SYSATHVIPV YNRKALLSQA IRLNWGGWHM AE YMLKLLK LKYYTGFPGK LNSSQTEHMV RDFCYVSLDY DRELAGYLDW TGLEDRERIV QYPYTEEVVV QKTEEELARI AER KKESGR RLQEQAAKMR LERLMKKEQE LEYYKDIQRR MQGESKKEIK RLLDEAELKD EAALERVIRD LERSIKRARQ KDLG EPEEE EVPDFSLLDV PDDQLDEAGL RQKRQQRLLK SNWEARQRAK AEKEAEKARL AEEARLDEER RKNDLEGWLE EKRQL RLAK LNQLKERERL KADLGNRKSL ASQIRMKNIA NLASDNPTGS GSRKRRRGGA GADQDDDFGA DDADWGVYRS VAIGAN KGD DSDDEEGEED LEAAIRSLEN DLLRYDKTFS YDMTLDAQRD WSKSLLHAFR YGPRPFDPSS QAETHRVHLN VERIRVP EV LFQPAAIAGV DQAGLVEIAG DILCQRLPSL PGIQDAPDAF LRDVFLTGGN TLFQNFDERL RQGLMALLPV GAPLRVRR A QDAILDAWRG AAGWACTEEA KAAWITREEY LEKGGEYIKE HDLGNAFA

UniProtKB: Uncharacterized protein

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Macromolecule #9: Histone H3.1

MacromoleculeName: Histone H3.1 / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.305969 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
ARTKQTARKS TGGKAPRKQL ATKAARKSAP ATGGVKKPHR YRPGTVALRE IRRYQKSTEL LIRKLPFQRL VREIAQDFKT DLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA

UniProtKB: Histone H3.1

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Macromolecule #10: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.263231 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SGRGKGGKGL GKGGAKRHRK VLRDNIQGIT KPAIRRLARR GGVKRISGLI YEETRGVLKV FLENVIRDAV TYTEHAKRKT VTAMDVVYA LKRQGRTLYG FGG

UniProtKB: Histone H4

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Macromolecule #11: Histone H2A

MacromoleculeName: Histone H2A / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.004329 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SGRGKQGGKA RAKAKSRSSR AGLQFPVGRV HRLLRKGNYA ERVGAGAPVY LAAVLEYLTA EILELAGNAA RDNKKTRIIP RHLQLAIRN DEELNKLLGR VTIAQGGVLP NIQAVLLPKK TESHHKAKGK

UniProtKB: Histone H2A type 1-C

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Macromolecule #12: Histone H2B

MacromoleculeName: Histone H2B / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.806018 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
PEPAKSAPAP KKGSKKAVTK AQKKDGKKRK RSRKESYSVY VYKVLKQVHP DTGISSKAMG IMNSFVNDIF ERIAGEASRL AHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSSK

UniProtKB: Histone H2B type 1-C/E/F/G/I

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Macromolecule #7: DNA strand 1

MacromoleculeName: DNA strand 1 / type: dna / ID: 7 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 69.527195 KDa
SequenceString: (DC)(DT)(DG)(DG)(DA)(DG)(DA)(DA)(DT)(DC) (DC)(DC)(DG)(DG)(DT)(DG)(DC)(DC)(DG)(DA) (DG)(DG)(DC)(DC)(DG)(DC)(DT)(DC)(DA) (DA)(DT)(DT)(DG)(DG)(DT)(DC)(DG)(DT)(DA) (DG) (DC)(DA)(DA)(DG)(DC)(DT) ...String:
(DC)(DT)(DG)(DG)(DA)(DG)(DA)(DA)(DT)(DC) (DC)(DC)(DG)(DG)(DT)(DG)(DC)(DC)(DG)(DA) (DG)(DG)(DC)(DC)(DG)(DC)(DT)(DC)(DA) (DA)(DT)(DT)(DG)(DG)(DT)(DC)(DG)(DT)(DA) (DG) (DC)(DA)(DA)(DG)(DC)(DT)(DC)(DT) (DA)(DG)(DC)(DA)(DC)(DC)(DG)(DC)(DT)(DT) (DA)(DA) (DA)(DC)(DG)(DC)(DA)(DC)(DG) (DT)(DA)(DC)(DG)(DC)(DG)(DC)(DT)(DG)(DT) (DC)(DC)(DC) (DC)(DC)(DG)(DC)(DG)(DT) (DT)(DT)(DT)(DA)(DA)(DC)(DC)(DG)(DC)(DC) (DA)(DA)(DG)(DG) (DG)(DG)(DA)(DT)(DT) (DA)(DC)(DT)(DC)(DC)(DC)(DT)(DA)(DG)(DT) (DC)(DT)(DC)(DC)(DA) (DG)(DG)(DC)(DA) (DC)(DG)(DT)(DG)(DT)(DC)(DA)(DG)(DA)(DT) (DA)(DT)(DA)(DT)(DA)(DC) (DA)(DT)(DC) (DC)(DT)(DG)(DT)(DG)(DC)(DA)(DT)(DG)(DT) (DA)(DT)(DT)(DG)(DA)(DA)(DC) (DA)(DG) (DC)(DG)(DA)(DC)(DC)(DT)(DT)(DG)(DC)(DC) (DG)(DG)(DT)(DG)(DC)(DC)(DA)(DG) (DT) (DC)(DG)(DG)(DA)(DT)(DA)(DG)(DT)(DG)(DT) (DT)(DC)(DC)(DG)(DA)(DG)(DC)(DT)(DC) (DC)(DC)(DA)(DC)(DT)(DC)(DT)(DA)(DG)(DA) (DG)(DG)(DA)(DT)(DC)(DC)(DC)(DC)(DG)(DG) (DG)(DT)(DA)(DC)(DC)(DG)

+
Macromolecule #8: DNA Strand 2

MacromoleculeName: DNA Strand 2 / type: dna / ID: 8 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 70.043562 KDa
SequenceString: (DC)(DG)(DG)(DT)(DA)(DC)(DC)(DC)(DG)(DG) (DG)(DG)(DA)(DT)(DC)(DC)(DT)(DC)(DT)(DA) (DG)(DA)(DG)(DT)(DG)(DG)(DG)(DA)(DG) (DC)(DT)(DC)(DG)(DG)(DA)(DA)(DC)(DA)(DC) (DT) (DA)(DT)(DC)(DC)(DG)(DA) ...String:
(DC)(DG)(DG)(DT)(DA)(DC)(DC)(DC)(DG)(DG) (DG)(DG)(DA)(DT)(DC)(DC)(DT)(DC)(DT)(DA) (DG)(DA)(DG)(DT)(DG)(DG)(DG)(DA)(DG) (DC)(DT)(DC)(DG)(DG)(DA)(DA)(DC)(DA)(DC) (DT) (DA)(DT)(DC)(DC)(DG)(DA)(DC)(DT) (DG)(DG)(DC)(DA)(DC)(DC)(DG)(DG)(DC)(DA) (DA)(DG) (DG)(DT)(DC)(DG)(DC)(DT)(DG) (DT)(DT)(DC)(DA)(DA)(DT)(DA)(DC)(DA)(DT) (DG)(DC)(DA) (DC)(DA)(DG)(DG)(DA)(DT) (DG)(DT)(DA)(DT)(DA)(DT)(DA)(DT)(DC)(DT) (DG)(DA)(DC)(DA) (DC)(DG)(DT)(DG)(DC) (DC)(DT)(DG)(DG)(DA)(DG)(DA)(DC)(DT)(DA) (DG)(DG)(DG)(DA)(DG) (DT)(DA)(DA)(DT) (DC)(DC)(DC)(DC)(DT)(DT)(DG)(DG)(DC)(DG) (DG)(DT)(DT)(DA)(DA)(DA) (DA)(DC)(DG) (DC)(DG)(DG)(DG)(DG)(DG)(DA)(DC)(DA)(DG) (DC)(DG)(DC)(DG)(DT)(DA)(DC) (DG)(DT) (DG)(DC)(DG)(DT)(DT)(DT)(DA)(DA)(DG)(DC) (DG)(DG)(DT)(DG)(DC)(DT)(DA)(DG) (DA) (DG)(DC)(DT)(DT)(DG)(DC)(DT)(DA)(DC)(DG) (DA)(DC)(DC)(DA)(DA)(DT)(DT)(DG)(DA) (DG)(DC)(DG)(DG)(DC)(DC)(DT)(DC)(DG)(DG) (DC)(DA)(DC)(DC)(DG)(DG)(DG)(DA)(DT)(DT) (DC)(DT)(DC)(DC)(DA)(DG)

+
Macromolecule #13: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 13 / Number of copies: 7 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

+
Macromolecule #14: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 14 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #15: TETRAFLUOROALUMINATE ION

MacromoleculeName: TETRAFLUOROALUMINATE ION / type: ligand / ID: 15 / Number of copies: 1 / Formula: ALF
Molecular weightTheoretical: 102.975 Da
Chemical component information

ChemComp-ALF:
TETRAFLUOROALUMINATE ION

+
Macromolecule #16: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 16 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.88 mg/mL
BufferpH: 7.5
Details: 30mM HEPES, pH7.5 50mM NaCl 0.25mM CaCl2 0.25mM DTT 2mM ADP 3.3mM MgCl2 10mM NaF 2mM AlCl3 0.05% octyl-beta-glucoside
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Time: 15 sec. / Details: 10% Oxygene 90% Argon
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV
Details: wait time of 5s, blot force at 3, and a blot time of 2s with Whatman blotting paper (Cytiva, CAT No. 10311807).
Details11-subunit ctINO80 reconstituted with hexasome

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number real images: 15384 / Average electron dose: 50.36 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

Particle selectionNumber selected: 2137460
Details: Particles were initially picked by WARP to generate an initial model, which was subsequently used for the 3D template picking
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.7 Å / Resolution method: OTHER / Software - Name: RELION (ver. 4) / Number images used: 98967
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4.0)
Details: de novo 3D model was generated by using gradient-driven algorithm implemented in RELION 4.0
Final angle assignmentType: MAXIMUM LIKELIHOOD

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Atomic model buiding 1

Initial model
PDB IDChain

6fml

source_name: PDB, initial_model_type: experimental model

7ohc

source_name: PDB, initial_model_type: experimental model

8a5q

source_name: PDB, initial_model_type: experimental model
RefinementProtocol: OTHER
Output model

PDB-8oop:
CryoEM Structure INO80core Hexasome complex composite model state2

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