8oo7

CryoEM Structure INO80core Hexasome complex composite model state1

Method: ELECTRON MICROSCOPY Dmax: 202.7 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

RuvB-like protein 1

Thermochaetoides thermophila

UniProt G0RYI5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 16 DNA 2 PDB declaration: 18-meric(18) Consistent with all polymer counts Chain A; UniProt 1–462 Chain B; UniProt 1–462 Chain C; UniProt 1–462 Not recorded RuvB-like protein 2 × 3 (G0RYC2) Chromatin-remodeling ATPase Ino80 × 1 Ino eighty subunit 2 × 1 (G0RY01) Chromatin-remodeling complex subunit IES6 × 1 (G0S590) Actin-related protein 5 × 1 (G0S589) DNA Strand 1 × 1 DNA Strand 2 × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A × 1 (Q93077) Histone H2B × 1 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 7 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;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 cryo-EM vitrification conditions:Cryogen ETHANE;wait time of 5s, blot force at 3, and a blot time of 2s with Whatman blotting paper (Cytiva, CAT No. 10311807) Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0RYI5_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–462; UniProt 1–462 Author chain B; PDBConstruct 1–462; UniProt 1–462 Author chain C; PDBConstruct 1–462; UniProt 1–462

RuvB-like protein 2

Thermochaetoides thermophila

UniProt G0RYC2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 16 DNA 2 PDB declaration: 18-meric(18) Consistent with all polymer counts Chain D; UniProt 1–488 Chain E; UniProt 1–488 Chain F; UniProt 1–488 Not recorded RuvB-like protein 1 × 3 (G0RYI5) Chromatin-remodeling ATPase Ino80 × 1 Ino eighty subunit 2 × 1 (G0RY01) Chromatin-remodeling complex subunit IES6 × 1 (G0S590) Actin-related protein 5 × 1 (G0S589) DNA Strand 1 × 1 DNA Strand 2 × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A × 1 (Q93077) Histone H2B × 1 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 7 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;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 cryo-EM vitrification conditions:Cryogen ETHANE;wait time of 5s, blot force at 3, and a blot time of 2s with Whatman blotting paper (Cytiva, CAT No. 10311807) Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0RYC2_CHATD
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–488; UniProt 1–488 Author chain E; PDBConstruct 1–488; UniProt 1–488 Author chain F; PDBConstruct 1–488; UniProt 1–488

Ino eighty subunit 2

Thermochaetoides thermophila

UniProt G0RY01

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 16 DNA 2 PDB declaration: 18-meric(18) Consistent with all polymer counts Chain H; UniProt 1–492 Not recorded RuvB-like protein 1 × 3 (G0RYI5) RuvB-like protein 2 × 3 (G0RYC2) Chromatin-remodeling ATPase Ino80 × 1 Chromatin-remodeling complex subunit IES6 × 1 (G0S590) Actin-related protein 5 × 1 (G0S589) DNA Strand 1 × 1 DNA Strand 2 × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A × 1 (Q93077) Histone H2B × 1 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 7 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;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 cryo-EM vitrification conditions:Cryogen ETHANE;wait time of 5s, blot force at 3, and a blot time of 2s with Whatman blotting paper (Cytiva, CAT No. 10311807) Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0RY01_CHATD
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–492; UniProt 1–492

Chromatin-remodeling complex subunit IES6

Thermochaetoides thermophila

UniProt G0S590

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 16 DNA 2 PDB declaration: 18-meric(18) Consistent with all polymer counts Chain I; UniProt 1–219 Not recorded RuvB-like protein 1 × 3 (G0RYI5) RuvB-like protein 2 × 3 (G0RYC2) Chromatin-remodeling ATPase Ino80 × 1 Ino eighty subunit 2 × 1 (G0RY01) Actin-related protein 5 × 1 (G0S589) DNA Strand 1 × 1 DNA Strand 2 × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A × 1 (Q93077) Histone H2B × 1 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 7 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;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 cryo-EM vitrification conditions:Cryogen ETHANE;wait time of 5s, blot force at 3, and a blot time of 2s with Whatman blotting paper (Cytiva, CAT No. 10311807) Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S590_CHATD
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–219; UniProt 1–219

Actin-related protein 5

Thermochaetoides thermophila

UniProt G0S589

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 16 DNA 2 PDB declaration: 18-meric(18) Consistent with all polymer counts Chain J; UniProt 98–866 Not recorded RuvB-like protein 1 × 3 (G0RYI5) RuvB-like protein 2 × 3 (G0RYC2) Chromatin-remodeling ATPase Ino80 × 1 Ino eighty subunit 2 × 1 (G0RY01) Chromatin-remodeling complex subunit IES6 × 1 (G0S590) DNA Strand 1 × 1 DNA Strand 2 × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A × 1 (Q93077) Histone H2B × 1 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 7 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;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 cryo-EM vitrification conditions:Cryogen ETHANE;wait time of 5s, blot force at 3, and a blot time of 2s with Whatman blotting paper (Cytiva, CAT No. 10311807) Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S589_CHATD
Isoform
PDB entities 6
Chains and sequence ranges Author chain J; PDBConstruct 1–769; UniProt 98–866

Histone H3.1

Homo sapiens

UniProt P68431

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 16 DNA 2 PDB declaration: 18-meric(18) Consistent with all polymer counts Chain M; UniProt 2–136 Chain Q; UniProt 2–136 Not recorded RuvB-like protein 1 × 3 (G0RYI5) RuvB-like protein 2 × 3 (G0RYC2) Chromatin-remodeling ATPase Ino80 × 1 Ino eighty subunit 2 × 1 (G0RY01) Chromatin-remodeling complex subunit IES6 × 1 (G0S590) Actin-related protein 5 × 1 (G0S589) DNA Strand 1 × 1 DNA Strand 2 × 1 Histone H4 × 2 (P62805) Histone H2A × 1 (Q93077) Histone H2B × 1 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 7 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;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 cryo-EM vitrification conditions:Cryogen ETHANE;wait time of 5s, blot force at 3, and a blot time of 2s with Whatman blotting paper (Cytiva, CAT No. 10311807) Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain M; PDBConstruct 1–135; UniProt 2–136 Author chain Q; PDBConstruct 1–135; UniProt 2–136

Histone H4

Homo sapiens

UniProt P62805

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 16 DNA 2 PDB declaration: 18-meric(18) Consistent with all polymer counts Chain N; UniProt 2–103 Chain R; UniProt 2–103 Not recorded RuvB-like protein 1 × 3 (G0RYI5) RuvB-like protein 2 × 3 (G0RYC2) Chromatin-remodeling ATPase Ino80 × 1 Ino eighty subunit 2 × 1 (G0RY01) Chromatin-remodeling complex subunit IES6 × 1 (G0S590) Actin-related protein 5 × 1 (G0S589) DNA Strand 1 × 1 DNA Strand 2 × 1 Histone H3.1 × 2 (P68431) Histone H2A × 1 (Q93077) Histone H2B × 1 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 7 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;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 cryo-EM vitrification conditions:Cryogen ETHANE;wait time of 5s, blot force at 3, and a blot time of 2s with Whatman blotting paper (Cytiva, CAT No. 10311807) Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain N; PDBConstruct 1–102; UniProt 2–103 Author chain R; PDBConstruct 1–102; UniProt 2–103

Histone H2A

Homo sapiens

UniProt Q93077

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 16 DNA 2 PDB declaration: 18-meric(18) Consistent with all polymer counts Chain O; UniProt 2–130 Not recorded RuvB-like protein 1 × 3 (G0RYI5) RuvB-like protein 2 × 3 (G0RYC2) Chromatin-remodeling ATPase Ino80 × 1 Ino eighty subunit 2 × 1 (G0RY01) Chromatin-remodeling complex subunit IES6 × 1 (G0S590) Actin-related protein 5 × 1 (G0S589) DNA Strand 1 × 1 DNA Strand 2 × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B × 1 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 7 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;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 cryo-EM vitrification conditions:Cryogen ETHANE;wait time of 5s, blot force at 3, and a blot time of 2s with Whatman blotting paper (Cytiva, CAT No. 10311807) Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1C_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain O; PDBConstruct 1–129; UniProt 2–130

Histone H2B

Homo sapiens

UniProt P62807

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 16 DNA 2 PDB declaration: 18-meric(18) Consistent with all polymer counts Chain P; UniProt 2–126 Not recorded RuvB-like protein 1 × 3 (G0RYI5) RuvB-like protein 2 × 3 (G0RYC2) Chromatin-remodeling ATPase Ino80 × 1 Ino eighty subunit 2 × 1 (G0RY01) Chromatin-remodeling complex subunit IES6 × 1 (G0S590) Actin-related protein 5 × 1 (G0S589) DNA Strand 1 × 1 DNA Strand 2 × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A × 1 (Q93077) ADP ADENOSINE-5'-DIPHOSPHATE × 7 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;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 cryo-EM vitrification conditions:Cryogen ETHANE;wait time of 5s, blot force at 3, and a blot time of 2s with Whatman blotting paper (Cytiva, CAT No. 10311807) Resolution 2.80 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

79 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1C_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain P; PDBConstruct 1–125; UniProt 2–126

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8oo7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8oo7
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8oo7
Deposition date deposition_date2023-04-04
Structure title titleCryoEM Structure INO80core Hexasome complex composite model state1
Keywords keywordsATP-dependent chromatin remodeler, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier61.03
Radius of gyration Rg (electron density) rg_electron59.80
Forward intensity I(0) i05788890000.00
Molecular weight molecular_weight588170.0 kDa
Excluded volume excluded_volume714760 ų
Envelope volume envelope_volume1100100 ų
Hydration-shell volume shell_volume147750 ų
Envelope diameter envelope_diameter191.4
Shell Rg shell_rg66.23
Envelope Rg envelope_rg58.31
Shape Rg shape_rg59.77
Total Rg total_rg60.01
Total atoms total_atoms41024
Residues n_residues4919
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax202.7
Rg (real space) rg_real60.80
Rg uncertainty (real space) rg_real_error1.64
I(0) (real space) i0_real5.7890e+09
I(0) uncertainty (real space) i0_real_error1.2700e+08
Rg (reciprocal space) rg_reciprocal61.20
I(0) (reciprocal space) i0_reciprocal5792000000.0000
Solution quality estimate total_estimate0.8815
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.2
Skewness Skewness skewness0.187
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha390400000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.848

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (5)

9. Files and Curves (10)