9zq9

Nucleosome with an SSB at SHL -2.8 in complex with the WGR domain of human PARP2, Class 1

Method: ELECTRON MICROSCOPY Dmax: 137.0 Å Quality: GOOD

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

Histone H2A

Drosophila melanogaster

UniProt P84051

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 × 11 DNA 3 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain A; UniProt 1–124 Chain B; UniProt 1–124 Not recorded Histone H2B × 2 (P02283) Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) Poly [ADP-ribose] polymerase 2 × 1 (Q9UGN5) DNA (197-MER) × 1 DNA (69-MER) × 1 DNA (128-MER) × 1 Ig-like domain-containing protein × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–124; UniProt 1–124 Author chain B; PDBConstruct 1–124; UniProt 1–124

Histone H2B

Drosophila melanogaster

UniProt P02283

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 × 11 DNA 3 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain C; UniProt 2–123 Chain D; UniProt 2–123 Not recorded Histone H2A × 2 (P84051) Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) Poly [ADP-ribose] polymerase 2 × 1 (Q9UGN5) DNA (197-MER) × 1 DNA (69-MER) × 1 DNA (128-MER) × 1 Ig-like domain-containing protein × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

21 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B_DROME
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 4–125; UniProt 2–123 Author chain D; PDBConstruct 4–125; UniProt 2–123

Histone H3

Drosophila melanogaster

UniProt P02299

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 × 11 DNA 3 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain E; UniProt 1–136 Chain F; UniProt 1–136 Not recorded Histone H2A × 2 (P84051) Histone H2B × 2 (P02283) Histone H4 × 2 (P84040) Poly [ADP-ribose] polymerase 2 × 1 (Q9UGN5) DNA (197-MER) × 1 DNA (69-MER) × 1 DNA (128-MER) × 1 Ig-like domain-containing protein × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3_DROME
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–136; UniProt 1–136 Author chain F; PDBConstruct 1–136; UniProt 1–136

Histone H4

Drosophila melanogaster

UniProt P84040

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 × 11 DNA 3 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain G; UniProt 2–103 Chain H; UniProt 2–103 Not recorded Histone H2A × 2 (P84051) Histone H2B × 2 (P02283) Histone H3 × 2 (P02299) Poly [ADP-ribose] polymerase 2 × 1 (Q9UGN5) DNA (197-MER) × 1 DNA (69-MER) × 1 DNA (128-MER) × 1 Ig-like domain-containing protein × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name H4_DROME
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 3–104; UniProt 2–103 Author chain H; PDBConstruct 3–104; UniProt 2–103

Poly [ADP-ribose] polymerase 2

Homo sapiens

UniProt Q9UGN5

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 × 11 DNA 3 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain P; UniProt 90–212 Not recorded Histone H2A × 2 (P84051) Histone H2B × 2 (P02283) Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) DNA (197-MER) × 1 DNA (69-MER) × 1 DNA (128-MER) × 1 Ig-like domain-containing protein × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

29 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PARP2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain P; PDBConstruct 1–123; UniProt 90–212

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 9zq9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9zq9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9zq9
Deposition date deposition_date2025-12-18
Structure title titleNucleosome with an SSB at SHL -2.8 in complex with the WGR domain of human PARP2, Class 1
Keywords keywordsDNA damage binding protein, 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_guinier44.17
Radius of gyration Rg (electron density) rg_electron42.38
Forward intensity I(0) i01454810000.00
Molecular weight molecular_weight250210.0 kDa
Excluded volume excluded_volume286320 ų
Envelope volume envelope_volume446490 ų
Hydration-shell volume shell_volume84909 ų
Envelope diameter envelope_diameter144.7
Shell Rg shell_rg50.06
Envelope Rg envelope_rg41.50
Shape Rg shape_rg42.28
Total Rg total_rg42.90
Total atoms total_atoms31827
Residues n_residues1682
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 dmax137.0
Rg (real space) rg_real43.86
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real1.4550e+09
I(0) uncertainty (real space) i0_real_error2.9220e+07
Rg (reciprocal space) rg_reciprocal44.17
I(0) (reciprocal space) i0_reciprocal1455000000.0000
Solution quality estimate total_estimate0.8874
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.1
Skewness Skewness skewness0.067
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha102900000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.895

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)