7pf2

Nucleosome stack of the 4x187 nucleosome array containing H1

Method: ELECTRON MICROSCOPY Dmax: 169.7 Å Quality: GOOD

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

Histone H3.2

Homo sapiens

UniProt Q71DI3

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 × 17 DNA 2 PDB declaration: nonadecameric(19) 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 Not recorded Histone H4 × 4 (P62805) Histone H2A type 1-B/E × 4 (P04908) Histone H2B type 1-K × 4 (O60814) Histone H1.4 × 1 (P10412) DNA (541-MER) × 1 DNA (541-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.10 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.

139 other PDB entries and 157 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_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

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 × 17 DNA 2 PDB declaration: nonadecameric(19) 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 Not recorded Histone H3.2 × 4 (Q71DI3) Histone H2A type 1-B/E × 4 (P04908) Histone H2B type 1-K × 4 (O60814) Histone H1.4 × 1 (P10412) DNA (541-MER) × 1 DNA (541-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.10 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

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 × 17 DNA 2 PDB declaration: nonadecameric(19) 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 Not recorded Histone H3.2 × 4 (Q71DI3) Histone H4 × 4 (P62805) Histone H2B type 1-K × 4 (O60814) Histone H1.4 × 1 (P10412) DNA (541-MER) × 1 DNA (541-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.10 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 18–147; UniProt 1–130 Author chain G; PDBConstruct 18–147; UniProt 1–130 Author chain M; PDBConstruct 18–147; UniProt 1–130 Author chain Q; PDBConstruct 18–147; 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 × 17 DNA 2 PDB declaration: nonadecameric(19) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Chain N; UniProt 1–126 Chain R; UniProt 1–126 Not recorded Histone H3.2 × 4 (Q71DI3) Histone H4 × 4 (P62805) Histone H2A type 1-B/E × 4 (P04908) Histone H1.4 × 1 (P10412) DNA (541-MER) × 1 DNA (541-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.10 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 1–126; UniProt 1–126 Author chain H; PDBConstruct 1–126; UniProt 1–126 Author chain N; PDBConstruct 1–126; UniProt 1–126 Author chain R; PDBConstruct 1–126; UniProt 1–126

Histone H1.4

Homo sapiens

UniProt P10412

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 × 17 DNA 2 PDB declaration: nonadecameric(19) Consistent with all polymer counts Chain U; UniProt 2–219 Not recorded Histone H3.2 × 4 (Q71DI3) Histone H4 × 4 (P62805) Histone H2A type 1-B/E × 4 (P04908) Histone H2B type 1-K × 4 (O60814) DNA (541-MER) × 1 DNA (541-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.10 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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H14_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain U; PDBConstruct 1–218; UniProt 2–219

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 7pf2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7pf2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7pf2
Deposition date deposition_date2021-08-11
Structure title titleNucleosome stack of the 4x187 nucleosome array containing H1
Keywords keywordsChromatin, Nucleosomes, Linker Histone, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.10
Radius of gyration Rg (electron density) rg_electron50.85
Forward intensity I(0) i04046840000.00
Molecular weight molecular_weight390660.0 kDa
Excluded volume excluded_volume430330 ų
Envelope volume envelope_volume723280 ų
Hydration-shell volume shell_volume114450 ų
Envelope diameter envelope_diameter175.0
Shell Rg shell_rg58.65
Envelope Rg envelope_rg49.30
Shape Rg shape_rg50.71
Total Rg total_rg51.34
Total atoms total_atoms26610
Residues n_residues2289
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 dmax169.7
Rg (real space) rg_real52.82
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real4.0470e+09
I(0) uncertainty (real space) i0_real_error7.6040e+07
Rg (reciprocal space) rg_reciprocal53.32
I(0) (reciprocal space) i0_reciprocal4050000000.0000
Solution quality estimate total_estimate0.8071
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary73.5
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha372500000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)