8off

Structure of BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes (Map1)

Method: ELECTRON MICROSCOPY Dmax: 121.8 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 × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain Ca; UniProt 1–135 Chain Cb; UniProt 1–135 Not recorded DNA (142-MER) × 2 Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H2A type 1 × 2 (P0C0S8) Histone H4 × 2 (P62805) BRCA1 associated RING domain 1 × 2 (M3WD26) Ubiquitin × 1 (P0CG48) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50 mM NaCl and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;blot force = 0 N blot time = 8 s Resolution 3.40 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 2
Chains and sequence ranges Author chain Ca; PDBConstruct 1–135; UniProt 1–135 Author chain Cb; PDBConstruct 1–135; UniProt 1–135

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 × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain Ba; UniProt 1–126 Chain Bb; UniProt 1–126 Not recorded DNA (142-MER) × 2 Histone H3.1 × 2 (P68431) Histone H2A type 1 × 2 (P0C0S8) Histone H4 × 2 (P62805) BRCA1 associated RING domain 1 × 2 (M3WD26) Ubiquitin × 1 (P0CG48) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50 mM NaCl and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;blot force = 0 N blot time = 8 s Resolution 3.40 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 3
Chains and sequence ranges Author chain Ba; PDBConstruct 1–126; UniProt 1–126 Author chain Bb; PDBConstruct 1–126; UniProt 1–126

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 × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain Aa; UniProt 1–130 Chain Ab; UniProt 1–130 Not recorded DNA (142-MER) × 2 Histone H3.1 × 2 (P68431) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H4 × 2 (P62805) BRCA1 associated RING domain 1 × 2 (M3WD26) Ubiquitin × 1 (P0CG48) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50 mM NaCl and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;blot force = 0 N blot time = 8 s Resolution 3.40 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 4
Chains and sequence ranges Author chain Aa; PDBConstruct 1–130; UniProt 1–130 Author chain Ab; PDBConstruct 1–130; UniProt 1–130

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 × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain Da; UniProt 1–103 Chain Db; UniProt 1–103 Not recorded DNA (142-MER) × 2 Histone H3.1 × 2 (P68431) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H2A type 1 × 2 (P0C0S8) BRCA1 associated RING domain 1 × 2 (M3WD26) Ubiquitin × 1 (P0CG48) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50 mM NaCl and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;blot force = 0 N blot time = 8 s Resolution 3.40 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 5
Chains and sequence ranges Author chain Da; PDBConstruct 1–103; UniProt 1–103 Author chain Db; PDBConstruct 1–103; UniProt 1–103

BRCA1 associated RING domain 1

Felis catus

UniProt M3WD26

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 × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain Ea; UniProt 1–773 Chain Eb; UniProt 1–773 Not recorded DNA (142-MER) × 2 Histone H3.1 × 2 (P68431) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H2A type 1 × 2 (P0C0S8) Histone H4 × 2 (P62805) Ubiquitin × 1 (P0CG48) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50 mM NaCl and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;blot force = 0 N blot time = 8 s Resolution 3.40 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 M3WD26_FELCA
Isoform
PDB entities 6
Chains and sequence ranges Author chain Ea; PDBConstruct 1–773; UniProt 1–773 Author chain Eb; PDBConstruct 1–773; UniProt 1–773

Ubiquitin

Homo sapiens

UniProt P0CG48

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 × 11 DNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain Fa; UniProt 1–76 Not recorded DNA (142-MER) × 2 Histone H3.1 × 2 (P68431) Histone H2B type 1-C/E/F/G/I × 2 (P62807) Histone H2A type 1 × 2 (P0C0S8) Histone H4 × 2 (P62805) BRCA1 associated RING domain 1 × 2 (M3WD26) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM HEPES pH 7.5, 50 mM NaCl and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE;blot force = 0 N blot time = 8 s Resolution 3.40 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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain Fa; 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 8off

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8off
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8off
Deposition date deposition_date2023-03-15
Structure title titleStructure of BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes (Map1)
Keywords keywordsBRCA1-BARD1, chromatin recognition, nucleosomes, ubiquitin, 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_guinier43.16
Radius of gyration Rg (electron density) rg_electron40.69
Forward intensity I(0) i01081860000.00
Molecular weight molecular_weight209910.0 kDa
Excluded volume excluded_volume237540 ų
Envelope volume envelope_volume396980 ų
Hydration-shell volume shell_volume78548 ų
Envelope diameter envelope_diameter125.0
Shell Rg shell_rg48.87
Envelope Rg envelope_rg39.43
Shape Rg shape_rg40.57
Total Rg total_rg41.32
Total atoms total_atoms14422
Residues n_residues1435
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 dmax121.8
Rg (real space) rg_real42.83
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real1.0820e+09
I(0) uncertainty (real space) i0_real_error1.7330e+07
Rg (reciprocal space) rg_reciprocal43.16
I(0) (reciprocal space) i0_reciprocal1082000000.0000
Solution quality estimate total_estimate0.8802
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.0
Skewness Skewness skewness-0.029
Kurtosis Kurtosis kurtosis-0.656
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha97370000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.982; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.512

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)