7k7g

nucleosome and Gal4 complex

Method: ELECTRON MICROSCOPY Dmax: 140.1 Å Quality: GOOD

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

Histone H3

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded Histone H4 × 2 (P02309) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) DNA (147-MER) × 1 DNA (147-MER) × 1 Centromere DNA-binding protein complex CBF3 subunit B × 1 (P40969) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 H4

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 9 DNA 2 PDB declaration: undecameric(11) 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) DNA (147-MER) × 1 DNA (147-MER) × 1 Centromere DNA-binding protein complex CBF3 subunit B × 1 (P40969) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Histone H2A.1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 1–132 Chain G; UniProt 1–132 Not recorded Histone H3 × 2 (P61830) Histone H4 × 2 (P02309) Histone H2B.1 × 2 (P02293) DNA (147-MER) × 1 DNA (147-MER) × 1 Centromere DNA-binding protein complex CBF3 subunit B × 1 (P40969) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 3
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 (strain ATCC 204508 / 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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 1–131 Chain H; UniProt 1–131 Not recorded Histone H3 × 2 (P61830) Histone H4 × 2 (P02309) Histone H2A.1 × 2 (P04911) DNA (147-MER) × 1 DNA (147-MER) × 1 Centromere DNA-binding protein complex CBF3 subunit B × 1 (P40969) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 D; PDBConstruct 1–131; UniProt 1–131 Author chain H; PDBConstruct 1–131; UniProt 1–131

Centromere DNA-binding protein complex CBF3 subunit B

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P40969

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain M; UniProt 1–48 Not recorded Histone H3 × 2 (P61830) Histone H4 × 2 (P02309) Histone H2A.1 × 2 (P04911) Histone H2B.1 × 2 (P02293) DNA (147-MER) × 1 DNA (147-MER) × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBF3B_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain M; PDBConstruct 1–48; UniProt 1–48

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 7k7g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7k7g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7k7g
Deposition date deposition_date2020-09-22
Structure title titlenucleosome and Gal4 complex
Keywords keywordsDNA 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_guinier41.32
Radius of gyration Rg (electron density) rg_electron38.64
Forward intensity I(0) i0685018000.00
Molecular weight molecular_weight162370.0 kDa
Excluded volume excluded_volume181960 ų
Envelope volume envelope_volume282820 ų
Hydration-shell volume shell_volume61685 ų
Envelope diameter envelope_diameter147.3
Shell Rg shell_rg44.27
Envelope Rg envelope_rg38.24
Shape Rg shape_rg38.44
Total Rg total_rg39.37
Total atoms total_atoms11098
Residues n_residues1012
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 dmax140.1
Rg (real space) rg_real41.23
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real6.8500e+08
I(0) uncertainty (real space) i0_real_error1.1200e+07
Rg (reciprocal space) rg_reciprocal41.32
I(0) (reciprocal space) i0_reciprocal685100000.0000
Solution quality estimate total_estimate0.8744
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.9
Skewness Skewness skewness0.268
Kurtosis Kurtosis kurtosis-0.246
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27290000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.896

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)