8oos

CryoEM Structure INO80core Hexasome complex ATPase-hexasome refinement state 2

Method: ELECTRON MICROSCOPY Dmax: 143.9 Å Quality: GOOD

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

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 × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain M; UniProt 2–136 Chain Q; UniProt 2–136 Not recorded Chromatin-remodeling ATPase Ino80 × 1 DNA strand 1 × 1 DNA Strand 2 × 1 Histone H4 × 2 (P62805) Histone H2A × 1 (Q93077) Histone H2B × 1 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 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 3.29 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 4
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 × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain N; UniProt 2–103 Chain R; UniProt 2–103 Not recorded Chromatin-remodeling ATPase Ino80 × 1 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 × 1 MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 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 3.29 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 5
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 × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain O; UniProt 2–130 Not recorded Chromatin-remodeling ATPase Ino80 × 1 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 × 1 MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 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 3.29 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 6
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 × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain P; UniProt 2–126 Not recorded Chromatin-remodeling ATPase Ino80 × 1 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 × 1 MG MAGNESIUM ION × 1 ALF TETRAFLUOROALUMINATE ION × 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 3.29 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 7
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 8oos

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8oos
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8oos
Deposition date deposition_date2023-04-05
Structure title titleCryoEM Structure INO80core Hexasome complex ATPase-hexasome refinement state 2
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_guinier44.29
Radius of gyration Rg (electron density) rg_electron43.61
Forward intensity I(0) i0738494000.00
Molecular weight molecular_weight179130.0 kDa
Excluded volume excluded_volume205690 ų
Envelope volume envelope_volume305490 ų
Hydration-shell volume shell_volume60315 ų
Envelope diameter envelope_diameter146.6
Shell Rg shell_rg46.64
Envelope Rg envelope_rg42.58
Shape Rg shape_rg43.54
Total Rg total_rg43.90
Total atoms total_atoms12307
Residues n_residues1183
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 dmax143.9
Rg (real space) rg_real44.27
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real7.3850e+08
I(0) uncertainty (real space) i0_real_error1.4140e+07
Rg (reciprocal space) rg_reciprocal44.29
I(0) (reciprocal space) i0_reciprocal738500000.0000
Solution quality estimate total_estimate0.8790
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.0
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.493
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36650000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.610

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8oosG01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (5)

9. Files and Curves (10)