9zeo

Competition for different elements of the nucleosome acidic patch yields distinct functional outcomes. VHH 1G1

Method: ELECTRON MICROSCOPY Dmax: 117.5 Å Quality: GOOD

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

Histone H3.1

Homo sapiens

UniProt P68431

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: 11-meric(11) Consistent with all polymer counts Chain A; UniProt 39–136 Chain E; UniProt 39–136 Not recorded DNA Tracking Strand × 1 DNA Lagging Strand × 1 Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) Single-chain antibody (VHH) 1G1 × 1 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 3.10 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–98; UniProt 39–136 Author chain E; PDBConstruct 1–98; UniProt 39–136

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 × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain B; UniProt 21–103 Chain F; UniProt 21–103 Not recorded DNA Tracking Strand × 1 DNA Lagging Strand × 1 Histone H3.1 × 2 (P68431) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-K × 2 (O60814) Single-chain antibody (VHH) 1G1 × 1 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 3.10 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 4
Chains and sequence ranges Author chain B; PDBConstruct 1–83; UniProt 21–103 Author chain F; PDBConstruct 1–83; UniProt 21–103

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 × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain C; UniProt 11–121 Chain G; UniProt 11–121 Not recorded DNA Tracking Strand × 1 DNA Lagging Strand × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-K × 2 (O60814) Single-chain antibody (VHH) 1G1 × 1 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 3.10 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 5
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 × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain D; UniProt 32–126 Chain H; UniProt 32–126 Not recorded DNA Tracking Strand × 1 DNA Lagging Strand × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Single-chain antibody (VHH) 1G1 × 1 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 3.10 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 6
Chains and sequence ranges Author chain D; PDBConstruct 1–95; UniProt 32–126 Author chain H; PDBConstruct 1–95; UniProt 32–126

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 9zeo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zeo
Deposition date deposition_date2025-11-30
Structure title titleCompetition for different elements of the nucleosome acidic patch yields distinct functional outcomes. VHH 1G1
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_guinier41.25
Radius of gyration Rg (electron density) rg_electron38.81
Forward intensity I(0) i0925084000.00
Molecular weight molecular_weight188620.0 kDa
Excluded volume excluded_volume210720 ų
Envelope volume envelope_volume322620 ų
Hydration-shell volume shell_volume67398 ų
Envelope diameter envelope_diameter121.0
Shell Rg shell_rg46.44
Envelope Rg envelope_rg38.05
Shape Rg shape_rg38.67
Total Rg total_rg39.45
Total atoms total_atoms12895
Residues n_residues1174
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 dmax117.5
Rg (real space) rg_real41.02
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real9.2510e+08
I(0) uncertainty (real space) i0_real_error1.4570e+07
Rg (reciprocal space) rg_reciprocal41.25
I(0) (reciprocal space) i0_reciprocal925300000.0000
Solution quality estimate total_estimate0.8791
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.6
Skewness Skewness skewness0.027
Kurtosis Kurtosis kurtosis-0.690
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61480000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.991; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.454

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)