3x1u

Crystal structure of nucleosome core particle in the presence of histone variants involved in reprogramming

Method: X-RAY DIFFRACTION Dmax: 119.0 Å Quality: EXCELLENT

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded DNA (146-MER) × 2 Histone H4 × 2 (P62805) Histone H2A × 2 (Q8CGP4) Histone H2B type 1-B × 2 (P33778) MN MANGANESE (II) ION × 4 CL CHLORIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;60-70 mM KCl, 70-90 mM MnCl2, 24% MPD, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.25 Å R-free 0.270

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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded DNA (146-MER) × 2 Histone H3.1 × 2 (P68431) Histone H2A × 2 (Q8CGP4) Histone H2B type 1-B × 2 (P33778) MN MANGANESE (II) ION × 4 CL CHLORIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;60-70 mM KCl, 70-90 mM MnCl2, 24% MPD, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.25 Å R-free 0.270

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 3
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103

Histone H2A

Mus musculus

UniProt Q8CGP4

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 2–129 Chain G; UniProt 2–129 Not recorded DNA (146-MER) × 2 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-B × 2 (P33778) MN MANGANESE (II) ION × 4 CL CHLORIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;60-70 mM KCl, 70-90 mM MnCl2, 24% MPD, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.25 Å R-free 0.270

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8CGP4_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–128; UniProt 2–129 Author chain G; PDBConstruct 1–128; UniProt 2–129

Histone H2B type 1-B

Homo sapiens

UniProt P33778

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 3–126 Chain H; UniProt 3–126 Not recorded DNA (146-MER) × 2 Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A × 2 (Q8CGP4) MN MANGANESE (II) ION × 4 CL CHLORIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;60-70 mM KCl, 70-90 mM MnCl2, 24% MPD, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.25 Å R-free 0.270

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1B_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain D; PDBConstruct 1–124; UniProt 3–126 Author chain H; PDBConstruct 1–124; UniProt 3–126

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 3x1u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3x1u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3x1u
Deposition date deposition_date2014-11-28
Structure title titleCrystal structure of nucleosome core particle in the presence of histone variants involved in reprogramming
Keywords keywordsnucleosome, histone, reprogramming, STRUCTURAL PROTEIN-DNA complex; STRUCTURAL PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.98
Radius of gyration Rg (electron density) rg_electron37.27
Forward intensity I(0) i0841179000.00
Molecular weight molecular_weight177630.0 kDa
Excluded volume excluded_volume197300 ų
Envelope volume envelope_volume292570 ų
Hydration-shell volume shell_volume63407 ų
Envelope diameter envelope_diameter120.5
Shell Rg shell_rg45.15
Envelope Rg envelope_rg36.83
Shape Rg shape_rg37.10
Total Rg total_rg38.00
Total atoms total_atoms12101
Residues n_residues1061
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 dmax119.0
Rg (real space) rg_real39.71
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real8.4120e+08
I(0) uncertainty (real space) i0_real_error1.2610e+07
Rg (reciprocal space) rg_reciprocal39.88
I(0) (reciprocal space) i0_reciprocal841300000.0000
Solution quality estimate total_estimate0.9065
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.083
Kurtosis Kurtosis kurtosis-0.700
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha71300000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.972; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.880

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id3x1uA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3x1uB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3x1uC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3x1uD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3x1uE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3x1uF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3x1uG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id3x1uH00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (1)

9. Files and Curves (10)