6fml

CryoEM Structure INO80core Nucleosome complex

Method: ELECTRON MICROSCOPY Dmax: 238.5 Å Quality: GOOD

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

RuvB-like helicase

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain A; UniProt 1–462 Chain B; UniProt 1–462 Chain C; UniProt 1–462 Not recorded RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les2 × 1 (G0RY01) Ies6 × 1 (G0S590) Actin related protein 5 × 1 (G0S589) Nucleosomal DNA Strand 1 × 1 Nucleosomal DNA Strand 2 × 1 Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S9) Histone H2B type 1-C/E/F/G/I × 2 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.34 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 helicase

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain D; UniProt 1–488 Chain E; UniProt 1–488 Chain F; UniProt 1–488 Not recorded RuvB-like helicase × 3 (G0RYI5) Ino80 × 1 les2 × 1 (G0RY01) Ies6 × 1 (G0S590) Actin related protein 5 × 1 (G0S589) Nucleosomal DNA Strand 1 × 1 Nucleosomal DNA Strand 2 × 1 Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S9) Histone H2B type 1-C/E/F/G/I × 2 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.34 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

les2

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain H; UniProt 1–382 Chain H; UniProt 415–492 Not recorded RuvB-like helicase × 3 (G0RYI5) RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 Ies6 × 1 (G0S590) Actin related protein 5 × 1 (G0S589) Nucleosomal DNA Strand 1 × 1 Nucleosomal DNA Strand 2 × 1 Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S9) Histone H2B type 1-C/E/F/G/I × 2 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.34 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 1–382; UniProt 1–382 Author chain H; PDBConstruct 414–491; UniProt 415–492

Ies6

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain I; UniProt 1–219 Not recorded RuvB-like helicase × 3 (G0RYI5) RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les2 × 1 (G0RY01) Actin related protein 5 × 1 (G0S589) Nucleosomal DNA Strand 1 × 1 Nucleosomal DNA Strand 2 × 1 Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S9) Histone H2B type 1-C/E/F/G/I × 2 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.34 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

Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain J; UniProt 617–667 Chain J; UniProt 683–866 Chain J; UniProt 98–567 Not recorded RuvB-like helicase × 3 (G0RYI5) RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les2 × 1 (G0RY01) Ies6 × 1 (G0S590) Nucleosomal DNA Strand 1 × 1 Nucleosomal DNA Strand 2 × 1 Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S9) Histone H2B type 1-C/E/F/G/I × 2 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.34 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 521–571; UniProt 617–667 Author chain J; PDBConstruct 587–770; UniProt 683–866 Author chain J; PDBConstruct 1–470; UniProt 98–567

Histone H3.2

Homo sapiens

UniProt Q71DI3

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: eicosameric(20) Consistent with all polymer counts Chain M; UniProt 2–136 Chain Q; UniProt 2–136 Not recorded RuvB-like helicase × 3 (G0RYI5) RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les2 × 1 (G0RY01) Ies6 × 1 (G0S590) Actin related protein 5 × 1 (G0S589) Nucleosomal DNA Strand 1 × 1 Nucleosomal DNA Strand 2 × 1 Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S9) Histone H2B type 1-C/E/F/G/I × 2 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.34 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.

139 other PDB entries and 157 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain N; UniProt 2–103 Chain R; UniProt 2–103 Not recorded RuvB-like helicase × 3 (G0RYI5) RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les2 × 1 (G0RY01) Ies6 × 1 (G0S590) Actin related protein 5 × 1 (G0S589) Nucleosomal DNA Strand 1 × 1 Nucleosomal DNA Strand 2 × 1 Histone H3.2 × 2 (Q71DI3) Histone H2A type 1 × 2 (P0C0S9) Histone H2B type 1-C/E/F/G/I × 2 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.34 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 type 1

Homo sapiens

UniProt P0C0S9

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: eicosameric(20) Consistent with all polymer counts Chain O; UniProt 2–130 Chain S; UniProt 2–130 Not recorded RuvB-like helicase × 3 (G0RYI5) RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les2 × 1 (G0RY01) Ies6 × 1 (G0S590) Actin related protein 5 × 1 (G0S589) Nucleosomal DNA Strand 1 × 1 Nucleosomal DNA Strand 2 × 1 Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2B type 1-C/E/F/G/I × 2 (P62807) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.34 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name H2A1_BOVIN
Isoform
PDB entities 11
Chains and sequence ranges Author chain O; PDBConstruct 1–129; UniProt 2–130 Author chain S; PDBConstruct 1–129; UniProt 2–130

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

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 × 18 DNA 2 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain P; UniProt 2–126 Chain T; UniProt 2–126 Not recorded RuvB-like helicase × 3 (G0RYI5) RuvB-like helicase × 3 (G0RYC2) Ino80 × 1 les2 × 1 (G0RY01) Ies6 × 1 (G0S590) Actin related protein 5 × 1 (G0S589) Nucleosomal DNA Strand 1 × 1 Nucleosomal DNA Strand 2 × 1 Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1 × 2 (P0C0S9) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM HEPES pH 8, 60 mM KCl, 0.5% glycerol, 0.25 mM CaCl2, 20 uM ZnCl2, 0.25 mM DTT, 0.05% Octyl-beta-glucoside cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.34 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 Author chain T; 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 6fml

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6fml
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6fml
Deposition date deposition_date2018-01-31
Structure title titleCryoEM Structure INO80core Nucleosome complex
Keywords keywordsINO80, Nucleosome, ATP dependent Chromatin Remodeller, 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_guinier63.76
Radius of gyration Rg (electron density) rg_electron62.47
Forward intensity I(0) i06648190000.00
Molecular weight molecular_weight623780.0 kDa
Excluded volume excluded_volume754480 ų
Envelope volume envelope_volume1178600 ų
Hydration-shell volume shell_volume151930 ų
Envelope diameter envelope_diameter208.5
Shell Rg shell_rg68.37
Envelope Rg envelope_rg60.77
Shape Rg shape_rg62.43
Total Rg total_rg62.69
Total atoms total_atoms43460
Residues n_residues5114
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 dmax238.5
Rg (real space) rg_real67.13
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real6.6980e+09
I(0) uncertainty (real space) i0_real_error1.3130e+08
Rg (reciprocal space) rg_reciprocal63.88
I(0) (reciprocal space) i0_reciprocal6651000000.0000
Solution quality estimate total_estimate0.8928
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary76.3
Skewness Skewness skewness0.546
Kurtosis Kurtosis kurtosis0.222
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.8394
Highest regularization parameter α highest_alpha557900000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.748; Stabil: 0.868; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.899

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)