9mmm

H2AX containing nucleosomes, Parallel stack

Method: ELECTRON MICROSCOPY Dmax: 162.7 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 × 16 DNA 4 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Chain L; UniProt 1–136 Chain P; UniProt 1–136 Not recorded Histone H4 × 4 (P62805) Histone H2AX × 4 (P16104) Histone H2B type 1-J × 4 (P06899) DNA (145-MER) × 2 DNA (145-MER) × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

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 22–157; UniProt 1–136 Author chain E; PDBConstruct 22–157; UniProt 1–136 Author chain L; PDBConstruct 22–157; UniProt 1–136 Author chain P; PDBConstruct 22–157; 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 × 16 DNA 4 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Chain M; UniProt 1–103 Chain Q; UniProt 1–103 Not recorded Histone H3.1 × 4 (P68431) Histone H2AX × 4 (P16104) Histone H2B type 1-J × 4 (P06899) DNA (145-MER) × 2 DNA (145-MER) × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103 Author chain M; PDBConstruct 1–103; UniProt 1–103 Author chain Q; PDBConstruct 1–103; UniProt 1–103

Histone H2AX

Homo sapiens

UniProt P16104

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 × 16 DNA 4 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain C; UniProt 1–143 Chain G; UniProt 1–143 Chain N; UniProt 1–143 Chain R; UniProt 1–143 Not recorded Histone H3.1 × 4 (P68431) Histone H4 × 4 (P62805) Histone H2B type 1-J × 4 (P06899) DNA (145-MER) × 2 DNA (145-MER) × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

23 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2AX_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 22–164; UniProt 1–143 Author chain G; PDBConstruct 22–164; UniProt 1–143 Author chain N; PDBConstruct 22–164; UniProt 1–143 Author chain R; PDBConstruct 22–164; UniProt 1–143

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 × 16 DNA 4 PDB declaration: eicosameric(20) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Chain O; UniProt 1–126 Chain S; UniProt 1–126 Not recorded Histone H3.1 × 4 (P68431) Histone H4 × 4 (P62805) Histone H2AX × 4 (P16104) DNA (145-MER) × 2 DNA (145-MER) × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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
Chains and sequence ranges Author chain D; PDBConstruct 1–126; UniProt 1–126 Author chain H; PDBConstruct 1–126; UniProt 1–126 Author chain O; PDBConstruct 1–126; UniProt 1–126 Author chain S; 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 9mmm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9mmm
Deposition date deposition_date2024-12-20
Structure title titleH2AX containing nucleosomes, Parallel stack
Keywords keywordsphosphorylation, nucleosome, nucleosome stacking, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.79
Radius of gyration Rg (electron density) rg_electron51.48
Forward intensity I(0) i03095720000.00
Molecular weight molecular_weight346100.0 kDa
Excluded volume excluded_volume383720 ų
Envelope volume envelope_volume695050 ų
Hydration-shell volume shell_volume107890 ų
Envelope diameter envelope_diameter162.9
Shell Rg shell_rg60.53
Envelope Rg envelope_rg49.14
Shape Rg shape_rg51.35
Total Rg total_rg51.99
Total atoms total_atoms42546
Residues n_residues2076
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 dmax162.7
Rg (real space) rg_real53.44
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real3.0960e+09
I(0) uncertainty (real space) i0_real_error5.7970e+07
Rg (reciprocal space) rg_reciprocal54.06
I(0) (reciprocal space) i0_reciprocal3098000000.0000
Solution quality estimate total_estimate0.8736
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary78.5
Skewness Skewness skewness-0.028
Kurtosis Kurtosis kurtosis-0.590
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha660700000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.670

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)