5kdm

Crystal structure of EBV tegument protein BNRF1 in complex with histone chaperone DAXX and histones H3.3-H4

Method: X-RAY DIFFRACTION Dmax: 84.0 Å Quality: EXCELLENT

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

Histone H3.3

Homo sapiens

UniProt P84243

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–136 Not recorded Histone H4 × 1 (P62805) Death domain-associated protein 6 × 1 (Q9UER7) Major tegument protein × 1 (Q1HVJ0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;0.1M MES pH 6.0, 0.8 M ammonium sulfate Resolution 3.50 Å R-free 0.280

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.

94 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H33_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 2–103 Not recorded Histone H3.3 × 1 (P84243) Death domain-associated protein 6 × 1 (Q9UER7) Major tegument protein × 1 (Q1HVJ0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;0.1M MES pH 6.0, 0.8 M ammonium sulfate Resolution 3.50 Å R-free 0.280

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 1–102; UniProt 2–103

Death domain-associated protein 6

Homo sapiens

UniProt Q9UER7

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 178–389 Fragment:residues 178-389 Histone H3.3 × 1 (P84243) Histone H4 × 1 (P62805) Major tegument protein × 1 (Q1HVJ0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;0.1M MES pH 6.0, 0.8 M ammonium sulfate Resolution 3.50 Å R-free 0.280

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.

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DAXX_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–212; UniProt 178–389

Major tegument protein

Epstein-Barr virus (strain AG876)

UniProt Q1HVJ0

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 381–599 Fragment:residues 381-599 Histone H3.3 × 1 (P84243) Histone H4 × 1 (P62805) Death domain-associated protein 6 × 1 (Q9UER7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;0.1M MES pH 6.0, 0.8 M ammonium sulfate Resolution 3.50 Å R-free 0.280

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 MTP_EBVA8
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–219; UniProt 381–599

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 5kdm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5kdm
Deposition date deposition_date2016-06-08
Structure title titleCrystal structure of EBV tegument protein BNRF1 in complex with histone chaperone DAXX and histones H3.3-H4
Keywords keywordshistone chaperone, Gene repression, CHAPERONE - DNA BINDING PROTEIN complex; CHAPERONE / DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.69
Radius of gyration Rg (electron density) rg_electron25.56
Forward intensity I(0) i062641800.00
Molecular weight molecular_weight61632.0 kDa
Excluded volume excluded_volume77290 ų
Envelope volume envelope_volume97575 ų
Hydration-shell volume shell_volume31424 ų
Envelope diameter envelope_diameter91.0
Shell Rg shell_rg33.14
Envelope Rg envelope_rg25.79
Shape Rg shape_rg25.53
Total Rg total_rg26.47
Total atoms total_atoms4341
Residues n_residues561
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 dmax84.0
Rg (real space) rg_real26.57
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real6.2640e+07
I(0) uncertainty (real space) i0_real_error8.3860e+05
Rg (reciprocal space) rg_reciprocal26.61
I(0) (reciprocal space) i0_reciprocal62640000.0000
Solution quality estimate total_estimate0.9064
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.8
Skewness Skewness skewness0.192
Kurtosis Kurtosis kurtosis-0.501
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13650000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id5kdmA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id5kdmB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id5kdmC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2170

8. Citations (1)

9. Files and Curves (10)