5kgf

Structural model of 53BP1 bound to a ubiquitylated and methylated nucleosome, at 4.5 A resolution

Method: ELECTRON MICROSCOPY Dmax: 118.7 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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 Tumor suppressor p53-binding protein 1 × 2 (H7BZY0) Ubiquitin × 2 (P0CG47) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;High concentration NCP-ubme/GST-53BP1 complex at 200 mM salt was diluted just prior to grid freezing. cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Plunged into liquid ethane-propane (FEI VITROBOT MARK III) Resolution 4.54 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.

230 other PDB entries and 239 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 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Mutation:K20C Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H3.2 × 2 (P84233) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 Tumor suppressor p53-binding protein 1 × 2 (H7BZY0) Ubiquitin × 2 (P0CG47) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;High concentration NCP-ubme/GST-53BP1 complex at 200 mM salt was diluted just prior to grid freezing. cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Plunged into liquid ethane-propane (FEI VITROBOT MARK III) Resolution 4.54 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.

354 other PDB entries and 370 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 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Histone H2A type 1

Homo sapiens

UniProt P0C0S8

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Mutation:K13R, T16S, K36R Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 Tumor suppressor p53-binding protein 1 × 2 (H7BZY0) Ubiquitin × 2 (P0CG47) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;High concentration NCP-ubme/GST-53BP1 complex at 200 mM salt was diluted just prior to grid freezing. cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Plunged into liquid ethane-propane (FEI VITROBOT MARK III) Resolution 4.54 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.

49 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_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

Histone H2B type 1-C/E/F/G/I

Homo sapiens

UniProt P62807

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) DNA (145-MER) × 1 DNA (145-MER) × 1 Tumor suppressor p53-binding protein 1 × 2 (H7BZY0) Ubiquitin × 2 (P0CG47) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;High concentration NCP-ubme/GST-53BP1 complex at 200 mM salt was diluted just prior to grid freezing. cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Plunged into liquid ethane-propane (FEI VITROBOT MARK III) Resolution 4.54 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.

79 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1C_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

Tumor suppressor p53-binding protein 1

Homo sapiens

UniProt H7BZY0

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain K; UniProt 79–99 Chain L; UniProt 79–99 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 Ubiquitin × 2 (P0CG47) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;High concentration NCP-ubme/GST-53BP1 complex at 200 mM salt was diluted just prior to grid freezing. cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Plunged into liquid ethane-propane (FEI VITROBOT MARK III) Resolution 4.54 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name H7BZY0_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–21; UniProt 79–99 Author chain L; PDBConstruct 1–21; UniProt 79–99

Ubiquitin

Homo sapiens

UniProt P0CG47

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain M; UniProt 1–76 Chain O; UniProt 1–76 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P0C0S8) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (145-MER) × 1 DNA (145-MER) × 1 Tumor suppressor p53-binding protein 1 × 2 (H7BZY0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;High concentration NCP-ubme/GST-53BP1 complex at 200 mM salt was diluted just prior to grid freezing. cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;Plunged into liquid ethane-propane (FEI VITROBOT MARK III) Resolution 4.54 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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain M; PDBConstruct 1–76; UniProt 1–76 Author chain O; PDBConstruct 1–76; UniProt 1–76

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 5kgf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5kgf
Deposition date deposition_date2016-06-13
Structure title titleStructural model of 53BP1 bound to a ubiquitylated and methylated nucleosome, at 4.5 A resolution
Keywords keywordsDNA, chromatin, 53BP1, STRUCTURAL PROTEIN-DNA complex; STRUCTURAL PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.70
Radius of gyration Rg (electron density) rg_electron38.57
Forward intensity I(0) i01014780000.00
Molecular weight molecular_weight201290.0 kDa
Excluded volume excluded_volume227160 ų
Envelope volume envelope_volume337140 ų
Hydration-shell volume shell_volume70352 ų
Envelope diameter envelope_diameter122.3
Shell Rg shell_rg46.43
Envelope Rg envelope_rg38.01
Shape Rg shape_rg38.44
Total Rg total_rg39.20
Total atoms total_atoms13782
Residues n_residues1274
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 dmax118.7
Rg (real space) rg_real40.46
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real1.0150e+09
I(0) uncertainty (real space) i0_real_error1.6550e+07
Rg (reciprocal space) rg_reciprocal40.70
I(0) (reciprocal space) i0_reciprocal1015000000.0000
Solution quality estimate total_estimate0.8385
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.015
Kurtosis Kurtosis kurtosis-0.695
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha88970000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.975; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)