9d3q

167-bp 5S rDNA nucleosome - open II

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 41–136 Chain E; UniProt 41–136 Not recorded Histone H4 × 2 (P62805) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-M × 2 (Q99879) 5S rDNA (noncoding strand) × 1 5S rDNA (coding strand) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 1–96; UniProt 41–136 Author chain E; PDBConstruct 1–96; UniProt 41–136

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain B; UniProt 23–103 Chain F; UniProt 23–103 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H2A type 2-A × 2 (Q6FI13) Histone H2B type 1-M × 2 (Q99879) 5S rDNA (noncoding strand) × 1 5S rDNA (coding strand) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 1–81; UniProt 23–103 Author chain F; PDBConstruct 1–81; UniProt 23–103

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain C; UniProt 13–107 Chain G; UniProt 13–107 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2B type 1-M × 2 (Q99879) 5S rDNA (noncoding strand) × 1 5S rDNA (coding strand) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 1–95; UniProt 13–107 Author chain G; PDBConstruct 1–95; UniProt 13–107

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain D; UniProt 33–126 Chain H; UniProt 33–126 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 2-A × 2 (Q6FI13) 5S rDNA (noncoding strand) × 1 5S rDNA (coding strand) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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
Chains and sequence ranges Author chain D; PDBConstruct 1–94; UniProt 33–126 Author chain H; PDBConstruct 1–94; UniProt 33–126

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 9d3q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9d3q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9d3q
Deposition date deposition_date2024-08-11
Structure title title167-bp 5S rDNA nucleosome - open II
Keywords keywords5S rDNA nucleosome, natural nucleosome positioning sequence, DNA sequence-dependent breathing, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.84
Radius of gyration Rg (electron density) rg_electron35.12
Forward intensity I(0) i0569714000.00
Molecular weight molecular_weight148140.0 kDa
Excluded volume excluded_volume166300 ų
Envelope volume envelope_volume239400 ų
Hydration-shell volume shell_volume55821 ų
Envelope diameter envelope_diameter109.2
Shell Rg shell_rg42.59
Envelope Rg envelope_rg34.54
Shape Rg shape_rg34.95
Total Rg total_rg35.89
Total atoms total_atoms10138
Residues n_residues940
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_real37.62
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real5.6970e+08
I(0) uncertainty (real space) i0_real_error9.1940e+06
Rg (reciprocal space) rg_reciprocal37.76
I(0) (reciprocal space) i0_reciprocal569800000.0000
Solution quality estimate total_estimate0.9001
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.2
Skewness Skewness skewness0.105
Kurtosis Kurtosis kurtosis-0.630
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27330000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.982; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.758

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)