8oof

CryoEM Structure INO80core Hexasome complex Arp5 Ies6 refinement state1

Method: ELECTRON MICROSCOPY Dmax: 86.6 Å Quality: GOOD

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

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 1–219 Not recorded Actin-related protein 5 × 1 (G0S589) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM 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 2.90 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 1
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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain J; UniProt 98–866 Not recorded Chromatin-remodeling complex subunit IES6 × 1 (G0S590) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM 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 2.90 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 2
Chains and sequence ranges Author chain J; PDBConstruct 1–769; UniProt 98–866

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 8oof

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8oof
Deposition date deposition_date2023-04-05
Structure title titleCryoEM Structure INO80core Hexasome complex Arp5 Ies6 refinement 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_guinier26.71
Radius of gyration Rg (electron density) rg_electron25.82
Forward intensity I(0) i068222000.00
Molecular weight molecular_weight63551.0 kDa
Excluded volume excluded_volume79189 ų
Envelope volume envelope_volume98570 ų
Hydration-shell volume shell_volume31287 ų
Envelope diameter envelope_diameter91.2
Shell Rg shell_rg33.68
Envelope Rg envelope_rg26.15
Shape Rg shape_rg25.83
Total Rg total_rg26.63
Total atoms total_atoms4479
Residues n_residues556
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 dmax86.6
Rg (real space) rg_real26.64
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real6.8220e+07
I(0) uncertainty (real space) i0_real_error9.8510e+05
Rg (reciprocal space) rg_reciprocal26.66
I(0) (reciprocal space) i0_reciprocal68220000.0000
Solution quality estimate total_estimate0.8991
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.256
Kurtosis Kurtosis kurtosis-0.491
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17430000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.899; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (3)

9. Files and Curves (10)