9zqc

Nucleosome with an SSB at SHL -2.8 in complex with human PARP2 and HPF1, Class 2

Method: ELECTRON MICROSCOPY Dmax: 131.7 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) mAb PL2-6 antibody × 2 DNA (60-MER) × 1 DNA (128-MER) × 1 DNA (197-MER) × 1 Poly [ADP-ribose] polymerase 2 × 1 (Q9UGN5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.37 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 1–123 Chain D; UniProt 1–123 Not recorded Histone H2A × 2 (P84051) Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) mAb PL2-6 antibody × 2 DNA (60-MER) × 1 DNA (128-MER) × 1 DNA (197-MER) × 1 Poly [ADP-ribose] polymerase 2 × 1 (Q9UGN5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.37 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 2–125; UniProt 1–123 Author chain D; PDBConstruct 2–125; UniProt 1–123

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 Mutation:C111S Histone H2A × 2 (P84051) Histone H2B × 2 (P02283) Histone H4 × 2 (P84040) mAb PL2-6 antibody × 2 DNA (60-MER) × 1 DNA (128-MER) × 1 DNA (197-MER) × 1 Poly [ADP-ribose] polymerase 2 × 1 (Q9UGN5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.37 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 1–103 Chain H; UniProt 1–103 Not recorded Histone H2A × 2 (P84051) Histone H2B × 2 (P02283) Histone H3 × 2 (P02299) mAb PL2-6 antibody × 2 DNA (60-MER) × 1 DNA (128-MER) × 1 DNA (197-MER) × 1 Poly [ADP-ribose] polymerase 2 × 1 (Q9UGN5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.37 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 1–104; UniProt 1–103 Author chain H; PDBConstruct 1–104; UniProt 1–103

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 90–583 Not recorded Histone H2A × 2 (P84051) Histone H2B × 2 (P02283) Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) mAb PL2-6 antibody × 2 DNA (60-MER) × 1 DNA (128-MER) × 1 DNA (197-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.37 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 9
Chains and sequence ranges Author chain P; PDBConstruct 1–494; UniProt 90–583

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 9zqc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zqc
Deposition date deposition_date2025-12-18
Structure title titleNucleosome with an SSB at SHL -2.8 in complex with human PARP2 and HPF1, Class 2
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_guinier42.86
Radius of gyration Rg (electron density) rg_electron41.18
Forward intensity I(0) i01442790000.00
Molecular weight molecular_weight249150.0 kDa
Excluded volume excluded_volume285030 ų
Envelope volume envelope_volume414250 ų
Hydration-shell volume shell_volume80786 ų
Envelope diameter envelope_diameter140.5
Shell Rg shell_rg49.02
Envelope Rg envelope_rg40.55
Shape Rg shape_rg41.09
Total Rg total_rg41.69
Total atoms total_atoms31669
Residues n_residues1674
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 dmax131.7
Rg (real space) rg_real42.58
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real1.4430e+09
I(0) uncertainty (real space) i0_real_error2.3560e+07
Rg (reciprocal space) rg_reciprocal42.86
I(0) (reciprocal space) i0_reciprocal1443000000.0000
Solution quality estimate total_estimate0.8885
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary56.9
Skewness Skewness skewness0.067
Kurtosis Kurtosis kurtosis-0.464
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha88540000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.950; Smooth: 0.876

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)