9be6

Cryo-EM structure of Human Nucleosome collected by Leginon on Krios at 3.0 Angstrom resolution

Method: ELECTRON MICROSCOPY Dmax: 115.5 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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 39–135 Chain E; UniProt 40–136 Not recorded Histone H4 × 1 (A0A9J8D176) Histone H2A type 1 × 1 (P0C0S8) Histone H2B type 1-J × 1 (P06899) Histone H4 × 1 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-J × 1 (P06899) DNA (145-MER) × 1 DNA (145-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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, 5
Chains and sequence ranges Author chain A; PDBConstruct 1–97; UniProt 39–135 Author chain E; PDBConstruct 1–97; UniProt 40–136

Histone H4

Homo sapiens

UniProt A0A9J8D176

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 10–92 Not recorded Histone H3.2 × 1 (Q71DI3) Histone H2A type 1 × 1 (P0C0S8) Histone H2B type 1-J × 1 (P06899) Histone H3.2 × 1 (Q71DI3) Histone H4 × 1 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-J × 1 (P06899) DNA (145-MER) × 1 DNA (145-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A9J8D176_CYPCA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–83; UniProt 10–92

Histone H2A type 1

Homo sapiens

UniProt P0C0S8

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 17–119 Not recorded Histone H3.2 × 1 (Q71DI3) Histone H4 × 1 (A0A9J8D176) Histone H2B type 1-J × 1 (P06899) Histone H3.2 × 1 (Q71DI3) Histone H4 × 1 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-J × 1 (P06899) DNA (145-MER) × 1 DNA (145-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

49 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–103; UniProt 17–119

Histone H2B type 1-J

Homo sapiens

UniProt P06899

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 48–126 Chain H; UniProt 33–125 Not recorded Histone H3.2 × 1 (Q71DI3) Histone H4 × 1 (A0A9J8D176) Histone H2A type 1 × 1 (P0C0S8) Histone H3.2 × 1 (Q71DI3) Histone H4 × 1 (P62805) Histone H2A type 1-B/E × 1 (P04908) DNA (145-MER) × 1 DNA (145-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

290 other PDB entries and 301 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1J_HUMAN
Isoform
PDB entities 4, 8
Chains and sequence ranges Author chain D; PDBConstruct 17–95; UniProt 48–126 Author chain H; PDBConstruct 1–93; UniProt 33–125

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 F; UniProt 26–103 Not recorded Histone H3.2 × 1 (Q71DI3) Histone H4 × 1 (A0A9J8D176) Histone H2A type 1 × 1 (P0C0S8) Histone H2B type 1-J × 1 (P06899) Histone H3.2 × 1 (Q71DI3) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-J × 1 (P06899) DNA (145-MER) × 1 DNA (145-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 6
Chains and sequence ranges Author chain F; PDBConstruct 1–78; UniProt 26–103

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain G; UniProt 15–119 Not recorded Histone H3.2 × 1 (Q71DI3) Histone H4 × 1 (A0A9J8D176) Histone H2A type 1 × 1 (P0C0S8) Histone H2B type 1-J × 1 (P06899) Histone H3.2 × 1 (Q71DI3) Histone H4 × 1 (P62805) Histone H2B type 1-J × 1 (P06899) DNA (145-MER) × 1 DNA (145-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 7
Chains and sequence ranges Author chain G; PDBConstruct 1–105; UniProt 15–119

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 9be6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9be6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9be6
Deposition date deposition_date2024-04-14
Structure title titleCryo-EM structure of Human Nucleosome collected by Leginon on Krios at 3.0 Angstrom resolution
Keywords keywordsNucleosome, krios, Falcon4, benchmark, 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_guinier39.83
Radius of gyration Rg (electron density) rg_electron37.07
Forward intensity I(0) i0698060000.00
Molecular weight molecular_weight163310.0 kDa
Excluded volume excluded_volume182650 ų
Envelope volume envelope_volume278220 ų
Hydration-shell volume shell_volume61428 ų
Envelope diameter envelope_diameter119.3
Shell Rg shell_rg44.41
Envelope Rg envelope_rg36.28
Shape Rg shape_rg36.91
Total Rg total_rg37.80
Total atoms total_atoms11163
Residues n_residues1005
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 dmax115.5
Rg (real space) rg_real39.56
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real6.9810e+08
I(0) uncertainty (real space) i0_real_error1.2660e+07
Rg (reciprocal space) rg_reciprocal39.73
I(0) (reciprocal space) i0_reciprocal698200000.0000
Solution quality estimate total_estimate0.8883
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.2
Skewness Skewness skewness0.089
Kurtosis Kurtosis kurtosis-0.671
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha43820000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.989; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.590

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)