9zen

Competition for different elements of the nucleosome acidic patch yields distinct functional outcomes. VHH 1B2

Method: ELECTRON MICROSCOPY Dmax: 141.7 Å Quality: GOOD

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

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 × 10 DNA 2 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain A; UniProt 39–135 Chain E; UniProt 39–135 Mutation:C97S Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) DNA Tracking Strand × 1 DNA lagging strand × 1 Single-chain antibody (VHH) 1B2 × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;20 mM HEPES pH7.6, 50 mM NaCl, 0.5 mM MgCl2, 1 mM EDTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.17 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–97; UniProt 39–135 Author chain E; PDBConstruct 1–97; UniProt 39–135

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 × 10 DNA 2 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain B; UniProt 25–103 Chain F; UniProt 25–103 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) DNA Tracking Strand × 1 DNA lagging strand × 1 Single-chain antibody (VHH) 1B2 × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;20 mM HEPES pH7.6, 50 mM NaCl, 0.5 mM MgCl2, 1 mM EDTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.17 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–79; UniProt 25–103 Author chain F; PDBConstruct 1–79; UniProt 25–103

Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

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 × 10 DNA 2 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain C; UniProt 11–121 Chain G; UniProt 11–121 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2B type 1-K × 2 (O60814) DNA Tracking Strand × 1 DNA lagging strand × 1 Single-chain antibody (VHH) 1B2 × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;20 mM HEPES pH7.6, 50 mM NaCl, 0.5 mM MgCl2, 1 mM EDTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.17 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–111; UniProt 11–121 Author chain G; PDBConstruct 1–111; UniProt 11–121

Histone H2B type 1-K

Homo sapiens

UniProt O60814

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 × 10 DNA 2 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain D; UniProt 34–126 Chain H; UniProt 34–126 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) DNA Tracking Strand × 1 DNA lagging strand × 1 Single-chain antibody (VHH) 1B2 × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;20 mM HEPES pH7.6, 50 mM NaCl, 0.5 mM MgCl2, 1 mM EDTA cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.17 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.

82 other PDB entries and 82 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1K_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–93; UniProt 34–126 Author chain H; PDBConstruct 1–93; UniProt 34–126

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 9zen

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zen
Deposition date deposition_date2025-11-30
Structure title titleCompetition for different elements of the nucleosome acidic patch yields distinct functional outcomes. VHH 1B2
Keywords keywordschromatin, nucleosome, VHH, antibody, acidic-patch, AP, DE NOVO PROTEIN; DE NOVO PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier42.34
Radius of gyration Rg (electron density) rg_electron40.39
Forward intensity I(0) i01019110000.00
Molecular weight molecular_weight200650.0 kDa
Excluded volume excluded_volume225440 ų
Envelope volume envelope_volume349100 ų
Hydration-shell volume shell_volume70475 ų
Envelope diameter envelope_diameter154.1
Shell Rg shell_rg47.25
Envelope Rg envelope_rg39.75
Shape Rg shape_rg40.29
Total Rg total_rg40.90
Total atoms total_atoms13745
Residues n_residues1288
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 dmax141.7
Rg (real space) rg_real42.07
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real1.0190e+09
I(0) uncertainty (real space) i0_real_error1.7550e+07
Rg (reciprocal space) rg_reciprocal42.33
I(0) (reciprocal space) i0_reciprocal1019000000.0000
Solution quality estimate total_estimate0.8771
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.6
Skewness Skewness skewness0.033
Kurtosis Kurtosis kurtosis-0.569
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha67550000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.809; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)