5nl0

Crystal structure of a 197-bp palindromic 601L nucleosome in complex with linker histone H1

Method: X-RAY DIFFRACTION Dmax: 205.1 Å Quality: GOOD

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

Histone H3.2

Xenopus laevis

UniProt P84233

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (197-MER) × 1 DNA (197-MER) × 1 Histone H1.0-B × 1 (P22844) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;Mix of equal volumes of the nucleosome/H1 complex (25-30 microM) and a crystallization solution composed of MPD (6% v/v), 50 mM NaCl, and 50 mM sodium potassium phosphate pH 6.4. Resolution 5.40 Å R-free 0.265
2 Protein–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain K; UniProt 2–136 Not recorded Histone H4 × 1 (P62799) Histone H2A type 1 × 1 (P06897) Histone H2B 1.1 × 1 (P02281) DNA (197-MER) × 1 DNA (197-MER) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;Mix of equal volumes of the nucleosome/H1 complex (25-30 microM) and a crystallization solution composed of MPD (6% v/v), 50 mM NaCl, and 50 mM sodium potassium phosphate pH 6.4. Resolution 5.40 Å R-free 0.265

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.

230 other PDB entries and 238 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136 Author chain K; PDBConstruct 1–135; UniProt 2–136

Histone H4

Xenopus laevis

UniProt P62799

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain B; UniProt 2–103 Chain F; UniProt 2–103 Not recorded Histone H3.2 × 2 (P84233) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (197-MER) × 1 DNA (197-MER) × 1 Histone H1.0-B × 1 (P22844) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;Mix of equal volumes of the nucleosome/H1 complex (25-30 microM) and a crystallization solution composed of MPD (6% v/v), 50 mM NaCl, and 50 mM sodium potassium phosphate pH 6.4. Resolution 5.40 Å R-free 0.265
2 Protein–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain L; UniProt 2–103 Not recorded Histone H3.2 × 1 (P84233) Histone H2A type 1 × 1 (P06897) Histone H2B 1.1 × 1 (P02281) DNA (197-MER) × 1 DNA (197-MER) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;Mix of equal volumes of the nucleosome/H1 complex (25-30 microM) and a crystallization solution composed of MPD (6% v/v), 50 mM NaCl, and 50 mM sodium potassium phosphate pH 6.4. Resolution 5.40 Å R-free 0.265

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.

354 other PDB entries and 369 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 2–103 Author chain F; PDBConstruct 1–102; UniProt 2–103 Author chain L; PDBConstruct 1–102; UniProt 2–103

Histone H2A type 1

Xenopus 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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 2–130 Chain G; UniProt 2–130 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) DNA (197-MER) × 1 DNA (197-MER) × 1 Histone H1.0-B × 1 (P22844) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;Mix of equal volumes of the nucleosome/H1 complex (25-30 microM) and a crystallization solution composed of MPD (6% v/v), 50 mM NaCl, and 50 mM sodium potassium phosphate pH 6.4. Resolution 5.40 Å R-free 0.265
2 Protein–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain M; UniProt 2–130 Not recorded Histone H3.2 × 1 (P84233) Histone H4 × 1 (P62799) Histone H2B 1.1 × 1 (P02281) DNA (197-MER) × 1 DNA (197-MER) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;Mix of equal volumes of the nucleosome/H1 complex (25-30 microM) and a crystallization solution composed of MPD (6% v/v), 50 mM NaCl, and 50 mM sodium potassium phosphate pH 6.4. Resolution 5.40 Å R-free 0.265

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 143 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130 Author chain M; PDBConstruct 1–129; UniProt 2–130

Histone H2B 1.1

Xenopus 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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) DNA (197-MER) × 1 DNA (197-MER) × 1 Histone H1.0-B × 1 (P22844) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;Mix of equal volumes of the nucleosome/H1 complex (25-30 microM) and a crystallization solution composed of MPD (6% v/v), 50 mM NaCl, and 50 mM sodium potassium phosphate pH 6.4. Resolution 5.40 Å R-free 0.265
2 Protein–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain N; UniProt 5–126 Not recorded Histone H3.2 × 1 (P84233) Histone H4 × 1 (P62799) Histone H2A type 1 × 1 (P06897) DNA (197-MER) × 1 DNA (197-MER) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;Mix of equal volumes of the nucleosome/H1 complex (25-30 microM) and a crystallization solution composed of MPD (6% v/v), 50 mM NaCl, and 50 mM sodium potassium phosphate pH 6.4. Resolution 5.40 Å R-free 0.265

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 326 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–122; UniProt 5–126 Author chain H; PDBConstruct 1–122; UniProt 5–126 Author chain N; PDBConstruct 1–122; UniProt 5–126

Histone H1.0-B

Xenopus laevis

UniProt P22844

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain Z; UniProt 1–196 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) DNA (197-MER) × 1 DNA (197-MER) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;293.15 K;Mix of equal volumes of the nucleosome/H1 complex (25-30 microM) and a crystallization solution composed of MPD (6% v/v), 50 mM NaCl, and 50 mM sodium potassium phosphate pH 6.4. Resolution 5.40 Å R-free 0.265

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 H10B_XENLA
Isoform
PDB entities 7
Chains and sequence ranges Author chain Z; PDBConstruct 1–196; UniProt 1–196

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 5nl0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5nl0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5nl0
Deposition date deposition_date2017-04-03
Structure title titleCrystal structure of a 197-bp palindromic 601L nucleosome in complex with linker histone H1
Keywords keywordsnucleosome, chromatin, linker histones, histone H1, CHROMATIN BINDING PROTEIN / DNA, CHROMATIN BINDING PROTEIN - DNA complex; CHROMATIN BINDING PROTEIN / DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier67.70
Radius of gyration Rg (electron density) rg_electron65.91
Forward intensity I(0) i02706620000.00
Molecular weight molecular_weight316160.0 kDa
Excluded volume excluded_volume345400 ų
Envelope volume envelope_volume655450 ų
Hydration-shell volume shell_volume85491 ų
Envelope diameter envelope_diameter221.2
Shell Rg shell_rg62.93
Envelope Rg envelope_rg65.86
Shape Rg shape_rg65.77
Total Rg total_rg66.18
Total atoms total_atoms21492
Residues n_residues1793
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 dmax205.1
Rg (real space) rg_real67.95
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real2.7070e+09
I(0) uncertainty (real space) i0_real_error5.6610e+07
Rg (reciprocal space) rg_reciprocal66.67
I(0) (reciprocal space) i0_reciprocal2700000000.0000
Solution quality estimate total_estimate0.8325
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.4
Skewness Skewness skewness0.404
Kurtosis Kurtosis kurtosis-0.631
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha75690000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)