9qik

M2 nucleosome

Method: ELECTRON MICROSCOPY Dmax: 111.4 Å Quality: REASONABLE

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

Histone H2A type 1

Xenopus laevis laevis

UniProt P06897

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 1–130 Chain B; UniProt 1–130 Not recorded Histone H2B 1.1 × 2 (P02281) Histone H3 × 2 (A0A8T2P505) Histone H4 × 2 (A0A8J1LTD2) DNA (220-MER) × 1 DNA (220-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

136 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–130; UniProt 1–130 Author chain B; PDBConstruct 1–130; UniProt 1–130

Histone H2B 1.1

Xenopus laevis laevis

UniProt P02281

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 1–126 Chain D; UniProt 1–126 Not recorded Histone H2A type 1 × 2 (P06897) Histone H3 × 2 (A0A8T2P505) Histone H4 × 2 (A0A8J1LTD2) DNA (220-MER) × 1 DNA (220-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–126; UniProt 1–126 Author chain D; PDBConstruct 1–126; UniProt 1–126

Histone H3

Xenopus laevis

UniProt A0A8T2P505

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 E; UniProt 1–136 Chain F; UniProt 1–136 Not recorded Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Histone H4 × 2 (A0A8J1LTD2) DNA (220-MER) × 1 DNA (220-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A8T2P505_9TELE
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–136; UniProt 1–136 Author chain F; PDBConstruct 1–136; UniProt 1–136

Histone H4

Xenopus laevis laevis

UniProt A0A8J1LTD2

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 14–116 Chain H; UniProt 14–116 Not recorded Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Histone H3 × 2 (A0A8T2P505) DNA (220-MER) × 1 DNA (220-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

33 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J1LTD2_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–103; UniProt 14–116 Author chain H; PDBConstruct 1–103; UniProt 14–116

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 9qik

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9qik
Deposition date deposition_date2025-03-17
Structure title titleM2 nucleosome
Keywords keywordsNCP, chromatin remodeling, TRANSLOCASE; TRANSLOCASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.09
Radius of gyration Rg (electron density) rg_electron36.32
Forward intensity I(0) i0692238000.00
Molecular weight molecular_weight160120.0 kDa
Excluded volume excluded_volume177590 ų
Envelope volume envelope_volume261320 ų
Hydration-shell volume shell_volume58719 ų
Envelope diameter envelope_diameter116.7
Shell Rg shell_rg43.77
Envelope Rg envelope_rg35.75
Shape Rg shape_rg36.14
Total Rg total_rg37.07
Total atoms total_atoms10927
Residues n_residues966
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 dmax111.4
Rg (real space) rg_real38.84
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real6.9220e+08
I(0) uncertainty (real space) i0_real_error1.1710e+07
Rg (reciprocal space) rg_reciprocal39.00
I(0) (reciprocal space) i0_reciprocal692300000.0000
Solution quality estimate total_estimate0.6501
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.6
Skewness Skewness skewness0.096
Kurtosis Kurtosis kurtosis-0.668
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37720000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.994; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.991; Smooth: 0.287

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)