9d3k

Two Dsup molecules in complex with the nucleosome open from both sides

Method: ELECTRON MICROSCOPY Dmax: 111.7 Å Quality: EXCELLENT

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: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 42–136 Chain E; UniProt 42–136 Not recorded Histone H4 × 2 (P62805) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-M × 1 (Q99879) Histone H2B type 1-M × 1 (Q99879) 601 DNA × 1 601 DNA × 1 Damage suppressor protein × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 1–95; UniProt 42–136 Author chain E; PDBConstruct 1–95; UniProt 42–136

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 24–102 Chain F; UniProt 24–102 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-M × 1 (Q99879) Histone H2B type 1-M × 1 (Q99879) 601 DNA × 1 601 DNA × 1 Damage suppressor protein × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 24–102 Author chain F; PDBConstruct 1–79; UniProt 24–102

Histone H2A type 2-A

Homo sapiens

UniProt Q6FI13

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: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 16–117 Chain G; UniProt 16–117 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2B type 1-M × 1 (Q99879) Histone H2B type 1-M × 1 (Q99879) 601 DNA × 1 601 DNA × 1 Damage suppressor protein × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A2A_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–102; UniProt 16–117 Author chain G; PDBConstruct 1–102; UniProt 16–117

Histone H2B type 1-M

Homo sapiens

UniProt Q99879

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: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 35–124 Chain H; UniProt 36–125 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 2-A × 2 (Q6FI13) 601 DNA × 1 601 DNA × 1 Damage suppressor protein × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1M_HUMAN
Isoform
PDB entities 4, 5
Chains and sequence ranges Author chain D; PDBConstruct 1–90; UniProt 35–124 Author chain H; PDBConstruct 1–90; UniProt 36–125

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 9d3k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9d3k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9d3k
Deposition date deposition_date2024-08-11
Structure title titleTwo Dsup molecules in complex with the nucleosome open from both sides
Keywords keywordsDsup, nucleosome, tardigrade damage supressor protein, GENE REGULATION, GENE REGULATION-DNA complex; GENE REGULATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.22
Radius of gyration Rg (electron density) rg_electron34.44
Forward intensity I(0) i0489615000.00
Molecular weight molecular_weight140540.0 kDa
Excluded volume excluded_volume159730 ų
Envelope volume envelope_volume225520 ų
Hydration-shell volume shell_volume53875 ų
Envelope diameter envelope_diameter109.3
Shell Rg shell_rg41.67
Envelope Rg envelope_rg33.93
Shape Rg shape_rg34.27
Total Rg total_rg35.23
Total atoms total_atoms9646
Residues n_residues930
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 dmax111.7
Rg (real space) rg_real37.02
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real4.8960e+08
I(0) uncertainty (real space) i0_real_error8.0940e+06
Rg (reciprocal space) rg_reciprocal37.15
I(0) (reciprocal space) i0_reciprocal489700000.0000
Solution quality estimate total_estimate0.9019
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.2
Skewness Skewness skewness0.121
Kurtosis Kurtosis kurtosis-0.570
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21200000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.971; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.817

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)