6m4h

Structural mechanism of nucleosome dynamics governed by human histone variants H2A.B and H2A.Z.2.2

Method: ELECTRON MICROSCOPY Dmax: 113.2 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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded DNA (103-MER) × 1 DNA (103-MER) × 1 Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 2 (P0C5Z0) Histone H2B type 2-E × 2 (Q16778) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136

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 1–103 Chain F; UniProt 1–103 Not recorded DNA (103-MER) × 1 DNA (103-MER) × 1 Histone H3.1 × 2 (P68431) Histone H2A-Bbd type 2/3 × 2 (P0C5Z0) Histone H2B type 2-E × 2 (Q16778) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Histone H2A-Bbd type 2/3

Homo sapiens

UniProt P0C5Z0

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 1–115 Chain G; UniProt 1–115 Not recorded DNA (103-MER) × 1 DNA (103-MER) × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 2-E × 2 (Q16778) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2AB2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 1–115; UniProt 1–115 Author chain G; PDBConstruct 1–115; UniProt 1–115

Histone H2B type 2-E

Homo sapiens

UniProt Q16778

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 1–126 Chain H; UniProt 1–126 Not recorded DNA (103-MER) × 1 DNA (103-MER) × 1 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A-Bbd type 2/3 × 2 (P0C5Z0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

39 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B2E_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain D; PDBConstruct 1–126; UniProt 1–126 Author chain H; PDBConstruct 1–126; UniProt 1–126

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 6m4h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6m4h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6m4h
Deposition date deposition_date2020-03-07
Structure title titleStructural mechanism of nucleosome dynamics governed by human histone variants H2A.B and H2A.Z.2.2
Keywords keywordshistone; variant; H2A.B; nucleosome, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.42
Radius of gyration Rg (electron density) rg_electron35.49
Forward intensity I(0) i0492331000.00
Molecular weight molecular_weight137750.0 kDa
Excluded volume excluded_volume154590 ų
Envelope volume envelope_volume220740 ų
Hydration-shell volume shell_volume52144 ų
Envelope diameter envelope_diameter115.4
Shell Rg shell_rg41.82
Envelope Rg envelope_rg34.87
Shape Rg shape_rg35.31
Total Rg total_rg36.23
Total atoms total_atoms9420
Residues n_residues862
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 dmax113.2
Rg (real space) rg_real38.20
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real4.9230e+08
I(0) uncertainty (real space) i0_real_error9.1030e+06
Rg (reciprocal space) rg_reciprocal38.34
I(0) (reciprocal space) i0_reciprocal492400000.0000
Solution quality estimate total_estimate0.8914
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.9
Skewness Skewness skewness0.102
Kurtosis Kurtosis kurtosis-0.582
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13140000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.979; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.655

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)