8qku

SWR1-nucleosome complex in configuration 1

Method: ELECTRON MICROSCOPY Dmax: 249.8 Å Quality: GOOD

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

Histone H3

Saccharomyces cerevisiae S288C

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: eicosameric(20) Consistent with all polymer counts Chain A; UniProt 1–136 Chain B; UniProt 1–136 Not recorded Histone H4 × 2 (P02309) Histone H2A.2 × 2 (P04912) Histone H2B.1 × 2 (P02293) DNA (177-MER) × 1 DNA (177-MER) × 1 Helicase SWR1 × 1 (Q05471) Actin-like protein ARP6 × 1 (Q12509) Vacuolar protein sorting-associated protein 71 × 1 (Q03433) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Vacuolar protein sorting-associated protein 72 × 1 (Q03388) ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

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 B; PDBConstruct 1–136; UniProt 1–136

Histone H4

Saccharomyces cerevisiae S288C

UniProt P02309

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 C; UniProt 1–103 Chain D; UniProt 1–103 Not recorded Histone H3 × 2 (P61830) Histone H2A.2 × 2 (P04912) Histone H2B.1 × 2 (P02293) DNA (177-MER) × 1 DNA (177-MER) × 1 Helicase SWR1 × 1 (Q05471) Actin-like protein ARP6 × 1 (Q12509) Vacuolar protein sorting-associated protein 71 × 1 (Q03433) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Vacuolar protein sorting-associated protein 72 × 1 (Q03388) ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

43 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–103; UniProt 1–103 Author chain D; PDBConstruct 1–103; UniProt 1–103

Histone H2A.2

Saccharomyces cerevisiae S288C

UniProt P04912

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 E; UniProt 1–127 Chain F; UniProt 1–127 Not recorded Histone H3 × 2 (P61830) Histone H4 × 2 (P02309) Histone H2B.1 × 2 (P02293) DNA (177-MER) × 1 DNA (177-MER) × 1 Helicase SWR1 × 1 (Q05471) Actin-like protein ARP6 × 1 (Q12509) Vacuolar protein sorting-associated protein 71 × 1 (Q03433) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Vacuolar protein sorting-associated protein 72 × 1 (Q03388) ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 H2A2_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–127; UniProt 1–127 Author chain F; PDBConstruct 1–127; UniProt 1–127

Histone H2B.1

Saccharomyces cerevisiae S288C

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: eicosameric(20) Consistent with all polymer counts Chain G; UniProt 1–131 Chain H; UniProt 1–131 Not recorded Histone H3 × 2 (P61830) Histone H4 × 2 (P02309) Histone H2A.2 × 2 (P04912) DNA (177-MER) × 1 DNA (177-MER) × 1 Helicase SWR1 × 1 (Q05471) Actin-like protein ARP6 × 1 (Q12509) Vacuolar protein sorting-associated protein 71 × 1 (Q03433) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Vacuolar protein sorting-associated protein 72 × 1 (Q03388) ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

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 4
Chains and sequence ranges Author chain G; PDBConstruct 1–131; UniProt 1–131 Author chain H; PDBConstruct 1–131; UniProt 1–131

Helicase SWR1

Saccharomyces cerevisiae S288C

UniProt Q05471

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 1–1514 Not recorded Histone H3 × 2 (P61830) Histone H4 × 2 (P02309) Histone H2A.2 × 2 (P04912) Histone H2B.1 × 2 (P02293) DNA (177-MER) × 1 DNA (177-MER) × 1 Actin-like protein ARP6 × 1 (Q12509) Vacuolar protein sorting-associated protein 71 × 1 (Q03433) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Vacuolar protein sorting-associated protein 72 × 1 (Q03388) ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SWR1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain M; PDBConstruct 1–1514; UniProt 1–1514

Actin-like protein ARP6

Saccharomyces cerevisiae S288C

UniProt Q12509

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 R; UniProt 1–438 Not recorded Histone H3 × 2 (P61830) Histone H4 × 2 (P02309) Histone H2A.2 × 2 (P04912) Histone H2B.1 × 2 (P02293) DNA (177-MER) × 1 DNA (177-MER) × 1 Helicase SWR1 × 1 (Q05471) Vacuolar protein sorting-associated protein 71 × 1 (Q03433) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Vacuolar protein sorting-associated protein 72 × 1 (Q03388) ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 ARP6_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain R; PDBConstruct 1–438; UniProt 1–438

Vacuolar protein sorting-associated protein 71

Saccharomyces cerevisiae S288C

UniProt Q03433

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 S; UniProt 1–280 Not recorded Histone H3 × 2 (P61830) Histone H4 × 2 (P02309) Histone H2A.2 × 2 (P04912) Histone H2B.1 × 2 (P02293) DNA (177-MER) × 1 DNA (177-MER) × 1 Helicase SWR1 × 1 (Q05471) Actin-like protein ARP6 × 1 (Q12509) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) Vacuolar protein sorting-associated protein 72 × 1 (Q03388) ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 VPS71_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain S; PDBConstruct 1–280; UniProt 1–280

RuvB-like protein 1

Saccharomyces cerevisiae S288C

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: eicosameric(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 H4 × 2 (P02309) Histone H2A.2 × 2 (P04912) Histone H2B.1 × 2 (P02293) DNA (177-MER) × 1 DNA (177-MER) × 1 Helicase SWR1 × 1 (Q05471) Actin-like protein ARP6 × 1 (Q12509) Vacuolar protein sorting-associated protein 71 × 1 (Q03433) RuvB-like protein 2 × 3 (Q12464) Vacuolar protein sorting-associated protein 72 × 1 (Q03388) ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

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 10
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

Saccharomyces cerevisiae S288C

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: eicosameric(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 H4 × 2 (P02309) Histone H2A.2 × 2 (P04912) Histone H2B.1 × 2 (P02293) DNA (177-MER) × 1 DNA (177-MER) × 1 Helicase SWR1 × 1 (Q05471) Actin-like protein ARP6 × 1 (Q12509) Vacuolar protein sorting-associated protein 71 × 1 (Q03433) RuvB-like protein 1 × 3 (Q03940) Vacuolar protein sorting-associated protein 72 × 1 (Q03388) ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

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 11
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

Vacuolar protein sorting-associated protein 72

Saccharomyces cerevisiae S288C

UniProt Q03388

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 Z; UniProt 195–329 Chain Z; UniProt 579–623 Not recorded Histone H3 × 2 (P61830) Histone H4 × 2 (P02309) Histone H2A.2 × 2 (P04912) Histone H2B.1 × 2 (P02293) DNA (177-MER) × 1 DNA (177-MER) × 1 Helicase SWR1 × 1 (Q05471) Actin-like protein ARP6 × 1 (Q12509) Vacuolar protein sorting-associated protein 71 × 1 (Q03433) RuvB-like protein 1 × 3 (Q03940) RuvB-like protein 2 × 3 (Q12464) ADP ADENOSINE-5'-DIPHOSPHATE × 8 BEF BERYLLIUM TRIFLUORIDE ION × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS72_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain Z; PDBConstruct 1–135; UniProt 195–329 Author chain Z; PDBConstruct 136–180; UniProt 579–623

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 8qku

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8qku
Deposition date deposition_date2023-09-18
Structure title titleSWR1-nucleosome complex in configuration 1
Keywords keywordsChromatin remodelling complex, nucleosome, protein-DNA complex, 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_guinier66.35
Radius of gyration Rg (electron density) rg_electron64.46
Forward intensity I(0) i07332900000.00
Molecular weight molecular_weight652520.0 kDa
Excluded volume excluded_volume788000 ų
Envelope volume envelope_volume1291400 ų
Hydration-shell volume shell_volume161500 ų
Envelope diameter envelope_diameter213.9
Shell Rg shell_rg70.28
Envelope Rg envelope_rg62.36
Shape Rg shape_rg64.39
Total Rg total_rg64.74
Total atoms total_atoms45395
Residues n_residues5217
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 dmax249.8
Rg (real space) rg_real70.01
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real7.3900e+09
I(0) uncertainty (real space) i0_real_error1.5160e+08
Rg (reciprocal space) rg_reciprocal66.65
I(0) (reciprocal space) i0_reciprocal7342000000.0000
Solution quality estimate total_estimate0.8907
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary83.3
Skewness Skewness skewness0.553
Kurtosis Kurtosis kurtosis0.459
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.8804
Highest regularization parameter α highest_alpha548200000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.715; Stabil: 0.851; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.912

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)