7v9j

Telomeric trinucleosome

Method: ELECTRON MICROSCOPY Dmax: 191.1 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 × 24 DNA 2 PDB declaration: 26-meric(26) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Chain K; UniProt 1–136 Chain O; UniProt 1–136 Chain S; UniProt 1–136 Chain W; UniProt 1–136 Not recorded Histone H4 × 6 (P62805) Histone H2A type 1-B/E × 6 (P04908) Histone H2B type 1-K × 6 (O60814) DNA (408-mer) × 1 DNA (408-mer) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.00 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 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136 Author chain K; PDBConstruct 1–136; UniProt 1–136 Author chain O; PDBConstruct 1–136; UniProt 1–136 Author chain S; PDBConstruct 1–136; UniProt 1–136 Author chain W; 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 × 24 DNA 2 PDB declaration: 26-meric(26) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Chain L; UniProt 1–103 Chain P; UniProt 1–103 Chain T; UniProt 1–103 Chain X; UniProt 1–103 Not recorded Histone H3.1 × 6 (P68431) Histone H2A type 1-B/E × 6 (P04908) Histone H2B type 1-K × 6 (O60814) DNA (408-mer) × 1 DNA (408-mer) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.00 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 L; PDBConstruct 1–103; UniProt 1–103 Author chain P; PDBConstruct 1–103; UniProt 1–103 Author chain T; PDBConstruct 1–103; UniProt 1–103 Author chain X; PDBConstruct 1–103; UniProt 1–103

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 × 24 DNA 2 PDB declaration: 26-meric(26) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Chain M; UniProt 1–130 Chain Q; UniProt 1–130 Chain U; UniProt 1–130 Chain Y; UniProt 1–130 Not recorded Histone H3.1 × 6 (P68431) Histone H4 × 6 (P62805) Histone H2B type 1-K × 6 (O60814) DNA (408-mer) × 1 DNA (408-mer) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.00 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–130; UniProt 1–130 Author chain G; PDBConstruct 1–130; UniProt 1–130 Author chain M; PDBConstruct 1–130; UniProt 1–130 Author chain Q; PDBConstruct 1–130; UniProt 1–130 Author chain U; PDBConstruct 1–130; UniProt 1–130 Author chain Y; PDBConstruct 1–130; UniProt 1–130

Histone H2B type 1-K

Homo sapiens

UniProt O60814

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 × 24 DNA 2 PDB declaration: 26-meric(26) Consistent with all polymer counts Chain D; UniProt 28–126 Chain H; UniProt 28–126 Chain N; UniProt 28–126 Chain R; UniProt 28–126 Chain V; UniProt 28–126 Chain Z; UniProt 28–126 Not recorded Histone H3.1 × 6 (P68431) Histone H4 × 6 (P62805) Histone H2A type 1-B/E × 6 (P04908) DNA (408-mer) × 1 DNA (408-mer) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.00 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.

82 other PDB entries and 82 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1K_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–99; UniProt 28–126 Author chain H; PDBConstruct 1–99; UniProt 28–126 Author chain N; PDBConstruct 1–99; UniProt 28–126 Author chain R; PDBConstruct 1–99; UniProt 28–126 Author chain V; PDBConstruct 1–99; UniProt 28–126 Author chain Z; PDBConstruct 1–99; UniProt 28–126

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 7v9j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v9j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v9j
Deposition date deposition_date2021-08-25
Structure title titleTelomeric trinucleosome
Keywords keywordsTelomere, nucleosome, chromatin, 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_guinier58.80
Radius of gyration Rg (electron density) rg_electron56.99
Forward intensity I(0) i06586030000.00
Molecular weight molecular_weight516190.0 kDa
Excluded volume excluded_volume577960 ų
Envelope volume envelope_volume980160 ų
Hydration-shell volume shell_volume140100 ų
Envelope diameter envelope_diameter192.5
Shell Rg shell_rg62.63
Envelope Rg envelope_rg55.12
Shape Rg shape_rg56.89
Total Rg total_rg57.35
Total atoms total_atoms35276
Residues n_residues3174
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 dmax191.1
Rg (real space) rg_real58.59
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real6.5860e+09
I(0) uncertainty (real space) i0_real_error1.3200e+08
Rg (reciprocal space) rg_reciprocal58.95
I(0) (reciprocal space) i0_reciprocal6590000000.0000
Solution quality estimate total_estimate0.8633
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.8
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.369
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha659100000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.645

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)