9c9g

S.c INO80 in complex with S.c 0/80 nucleosome

Method: ELECTRON MICROSCOPY Dmax: 238.0 Å Quality: GOOD

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

Histone H3

Saccharomyces cerevisiae

UniProt P61830

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) Histone H4 × 2 (P62799) DNA (227-MER) × 1 DNA (227-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 2.91 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.

37 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136

Histone H2A.1

Saccharomyces cerevisiae

UniProt P04911

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain C; UniProt 1–132 Chain G; UniProt 1–132 Not recorded Histone H3 × 2 (P61830) Histone H2B.1 × 2 (P02293) Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) Histone H4 × 2 (P62799) DNA (227-MER) × 1 DNA (227-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 2.91 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.

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

View Construct and Data Evidence
UniProt name H2A1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–132; UniProt 1–132 Author chain G; PDBConstruct 1–132; UniProt 1–132

Histone H2B.1

Saccharomyces cerevisiae

UniProt P02293

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain D; UniProt 1–131 Chain H; UniProt 1–131 Not recorded Histone H3 × 2 (P61830) Histone H2A.1 × 2 (P04911) Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) Histone H4 × 2 (P62799) DNA (227-MER) × 1 DNA (227-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 2.91 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.

23 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–131; UniProt 1–131 Author chain H; PDBConstruct 1–131; UniProt 1–131

Chromatin-remodeling ATPase INO80

OrganismNot specified

UniProt P53115

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain Q; UniProt 1–1489 Not recorded Histone H3 × 2 (P61830) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) Histone H4 × 2 (P62799) DNA (227-MER) × 1 DNA (227-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 2.91 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.

16 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INO80_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain Q; PDBConstruct 1–1489; UniProt 1–1489

Actin-related protein 5

OrganismNot specified

UniProt P53946

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain R; UniProt 1–755 Not recorded Histone H3 × 2 (P61830) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) Chromatin-remodeling ATPase INO80 × 1 (P53115) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) Histone H4 × 2 (P62799) DNA (227-MER) × 1 DNA (227-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 2.91 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.

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

View Construct and Data Evidence
UniProt name ARP5_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain R; PDBConstruct 1–755; UniProt 1–755

Chromatin-remodeling complex subunit IES6

OrganismNot specified

UniProt P32617

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain S; UniProt 1–166 Not recorded Histone H3 × 2 (P61830) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) Histone H4 × 2 (P62799) DNA (227-MER) × 1 DNA (227-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 2.91 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.

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

View Construct and Data Evidence
UniProt name IES6_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain S; PDBConstruct 1–166; UniProt 1–166

RuvB-like protein 1

OrganismNot specified

UniProt Q03940

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain T; UniProt 1–463 Chain V; UniProt 1–463 Chain X; UniProt 1–463 Not recorded Histone H3 × 2 (P61830) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) Histone H4 × 2 (P62799) DNA (227-MER) × 1 DNA (227-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 2.91 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUVB1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain T; PDBConstruct 1–463; UniProt 1–463 Author chain V; PDBConstruct 1–463; UniProt 1–463 Author chain X; PDBConstruct 1–463; UniProt 1–463

RuvB-like protein 2

OrganismNot specified

UniProt Q12464

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain U; UniProt 1–471 Chain W; UniProt 1–471 Chain Y; UniProt 1–471 Not recorded Histone H3 × 2 (P61830) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) Ino eighty subunit 2 × 1 (P40154) Histone H4 × 2 (P62799) DNA (227-MER) × 1 DNA (227-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 2.91 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.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUVB2_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain U; PDBConstruct 1–471; UniProt 1–471 Author chain W; PDBConstruct 1–471; UniProt 1–471 Author chain Y; PDBConstruct 1–471; UniProt 1–471

Ino eighty subunit 2

OrganismNot specified

UniProt P40154

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain Z; UniProt 1–320 Not recorded Histone H3 × 2 (P61830) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Histone H4 × 2 (P62799) DNA (227-MER) × 1 DNA (227-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 2.91 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IES2_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain Z; PDBConstruct 1–320; UniProt 1–320

Histone H4

Xenopus laevis

UniProt P62799

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3 × 2 (P61830) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) Chromatin-remodeling ATPase INO80 × 1 (P53115) Actin-related protein 5 × 1 (P53946) Chromatin-remodeling complex subunit IES6 × 1 (P32617) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Ino eighty subunit 2 × 1 (P40154) DNA (227-MER) × 1 DNA (227-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen OTHER Resolution 2.91 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.

354 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 10
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

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 9c9g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c9g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c9g
Deposition date deposition_date2024-06-13
Structure title titleS.c INO80 in complex with S.c 0/80 nucleosome
Keywords keywordsChromatin Remodeler, nucleosome, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier63.94
Radius of gyration Rg (electron density) rg_electron62.69
Forward intensity I(0) i06411500000.00
Molecular weight molecular_weight616870.0 kDa
Excluded volume excluded_volume748190 ų
Envelope volume envelope_volume1186500 ų
Hydration-shell volume shell_volume152890 ų
Envelope diameter envelope_diameter211.1
Shell Rg shell_rg68.42
Envelope Rg envelope_rg60.73
Shape Rg shape_rg62.63
Total Rg total_rg62.98
Total atoms total_atoms43020
Residues n_residues5067
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 dmax238.0
Rg (real space) rg_real67.20
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real6.4560e+09
I(0) uncertainty (real space) i0_real_error1.2270e+08
Rg (reciprocal space) rg_reciprocal64.06
I(0) (reciprocal space) i0_reciprocal6415000000.0000
Solution quality estimate total_estimate0.8934
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary76.2
Skewness Skewness skewness0.544
Kurtosis Kurtosis kurtosis0.213
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.8429
Highest regularization parameter α highest_alpha558800000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.748; Stabil: 0.874; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.901

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)