7vbm

The mouse nucleosome structure containing H3mm18 aided by PL2-6 scFv

Method: ELECTRON MICROSCOPY Dmax: 117.8 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone H4

Mus musculus

UniProt P62806

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 Histone H3mm18 × 2 Histone H2A type 1-B × 2 (C0HKE1) Histone H2B type 3-A × 2 (Q9D2U9) DNA (126-MER) × 1 DNA (126-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.40 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.

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

View Construct and Data Evidence
UniProt name H4_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–106; UniProt 1–103 Author chain F; PDBConstruct 4–106; UniProt 1–103

Histone H2A type 1-B

Mus musculus

UniProt C0HKE1

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 1–130 Chain G; UniProt 1–130 Not recorded Histone H3mm18 × 2 Histone H4 × 2 (P62806) Histone H2B type 3-A × 2 (Q9D2U9) DNA (126-MER) × 1 DNA (126-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.40 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 H2A1B_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–133; UniProt 1–130 Author chain G; PDBConstruct 4–133; UniProt 1–130

Histone H2B type 3-A

Mus musculus

UniProt Q9D2U9

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 Histone H3mm18 × 2 Histone H4 × 2 (P62806) Histone H2A type 1-B × 2 (C0HKE1) DNA (126-MER) × 1 DNA (126-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.40 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B3A_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 4–129; UniProt 1–126 Author chain H; PDBConstruct 4–129; 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 7vbm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7vbm
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7vbm
Deposition date deposition_date2021-08-31
Structure title titleThe mouse nucleosome structure containing H3mm18 aided by PL2-6 scFv
Keywords keywordscomplex, chromatin, nucleosome, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.27
Radius of gyration Rg (electron density) rg_electron36.46
Forward intensity I(0) i0637220000.00
Molecular weight molecular_weight153540.0 kDa
Excluded volume excluded_volume170360 ų
Envelope volume envelope_volume257660 ų
Hydration-shell volume shell_volume58093 ų
Envelope diameter envelope_diameter126.5
Shell Rg shell_rg43.47
Envelope Rg envelope_rg35.91
Shape Rg shape_rg36.28
Total Rg total_rg37.19
Total atoms total_atoms10475
Residues n_residues929
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 dmax117.8
Rg (real space) rg_real39.04
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real6.3720e+08
I(0) uncertainty (real space) i0_real_error1.0380e+07
Rg (reciprocal space) rg_reciprocal39.19
I(0) (reciprocal space) i0_reciprocal637300000.0000
Solution quality estimate total_estimate0.9103
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.1
Skewness Skewness skewness0.115
Kurtosis Kurtosis kurtosis-0.621
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha32000000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.969; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.938

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)