7x58

Cryo-EM structure of human subnucleosome (open form)

Method: ELECTRON MICROSCOPY Dmax: 115.8 Å Quality: EXCELLENT

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 2–136 Chain C; UniProt 2–136 Chain E; UniProt 2–136 Chain G; UniProt 2–136 Not recorded Histone H4 × 4 (P62805) Widom601 DNA FW (145-MER) × 1 Widom601 DNA RV (145-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 1
Chains and sequence ranges Author chain A; PDBConstruct 5–139; UniProt 2–136 Author chain C; PDBConstruct 5–139; UniProt 2–136 Author chain E; PDBConstruct 5–139; UniProt 2–136 Author chain G; PDBConstruct 5–139; UniProt 2–136

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 2–103 Chain D; UniProt 2–103 Chain F; UniProt 2–103 Chain H; UniProt 2–103 Not recorded Histone H3.1 × 4 (P68431) Widom601 DNA FW (145-MER) × 1 Widom601 DNA RV (145-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 5–106; UniProt 2–103 Author chain D; PDBConstruct 5–106; UniProt 2–103 Author chain F; PDBConstruct 5–106; UniProt 2–103 Author chain H; PDBConstruct 5–106; UniProt 2–103

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 7x58

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7x58
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7x58
Deposition date deposition_date2022-03-04
Structure title titleCryo-EM structure of human subnucleosome (open form)
Keywords keywordssubnucleosome, NUCLEAR 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_guinier39.96
Radius of gyration Rg (electron density) rg_electron37.24
Forward intensity I(0) i0568240000.00
Molecular weight molecular_weight143600.0 kDa
Excluded volume excluded_volume158620 ų
Envelope volume envelope_volume246690 ų
Hydration-shell volume shell_volume54847 ų
Envelope diameter envelope_diameter120.0
Shell Rg shell_rg43.92
Envelope Rg envelope_rg36.07
Shape Rg shape_rg37.07
Total Rg total_rg37.91
Total atoms total_atoms9775
Residues n_residues838
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 dmax115.8
Rg (real space) rg_real39.73
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real5.6820e+08
I(0) uncertainty (real space) i0_real_error9.7520e+06
Rg (reciprocal space) rg_reciprocal39.96
I(0) (reciprocal space) i0_reciprocal568400000.0000
Solution quality estimate total_estimate0.9023
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.1
Skewness Skewness skewness-0.023
Kurtosis Kurtosis kurtosis-0.590
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12800000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.855

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)