8tnt

Crystal structure of Epstein-Barr virus gH/gL/gp42 in complex with antibodies F-2-1 and 769C2

Method: X-RAY DIFFRACTION Dmax: 213.7 Å Quality: GOOD

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

Envelope glycoprotein H

Epstein-Barr virus

UniProt P03231

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 19–674 Not recorded Envelope glycoprotein L × 1 (P03212) Glycoprotein 42 × 1 (P03205) 769C2 light chain × 1 769C2 heavy chain × 1 F-2-1 light chain × 1 F-2-1 heavy chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;280 K;20mM Tris pH7.5, 150mM NaCl, 4% Tacsimate pH 7.0, and 10% PEG 3,350 Resolution 3.15 Å R-free 0.287

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.

7 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GH_EBVB9
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–656; UniProt 19–674

Envelope glycoprotein L

Epstein-Barr virus

UniProt P03212

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 24–135 Not recorded Envelope glycoprotein H × 1 (P03231) Glycoprotein 42 × 1 (P03205) 769C2 light chain × 1 769C2 heavy chain × 1 F-2-1 light chain × 1 F-2-1 heavy chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;280 K;20mM Tris pH7.5, 150mM NaCl, 4% Tacsimate pH 7.0, and 10% PEG 3,350 Resolution 3.15 Å R-free 0.287

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.

7 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GL_EBVB9
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–112; UniProt 24–135

Glycoprotein 42

Epstein-Barr virus

UniProt P03205

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 33–223 Not recorded Envelope glycoprotein H × 1 (P03231) Envelope glycoprotein L × 1 (P03212) 769C2 light chain × 1 769C2 heavy chain × 1 F-2-1 light chain × 1 F-2-1 heavy chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;280 K;20mM Tris pH7.5, 150mM NaCl, 4% Tacsimate pH 7.0, and 10% PEG 3,350 Resolution 3.15 Å R-free 0.287

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.

5 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GP42_EBVB9
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–191; UniProt 33–223

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 8tnt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tnt
Deposition date deposition_date2023-08-02
Structure title titleCrystal structure of Epstein-Barr virus gH/gL/gp42 in complex with antibodies F-2-1 and 769C2
Keywords keywordsViral Protein, Antibody, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier60.80
Radius of gyration Rg (electron density) rg_electron62.02
Forward intensity I(0) i0546725000.00
Molecular weight molecular_weight195010.0 kDa
Excluded volume excluded_volume244100 ų
Envelope volume envelope_volume367790 ų
Hydration-shell volume shell_volume57198 ų
Envelope diameter envelope_diameter230.4
Shell Rg shell_rg49.86
Envelope Rg envelope_rg63.05
Shape Rg shape_rg62.00
Total Rg total_rg61.69
Total atoms total_atoms13731
Residues n_residues1810
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 dmax213.7
Rg (real space) rg_real62.00
Rg uncertainty (real space) rg_real_error2.20
I(0) (real space) i0_real5.4660e+08
I(0) uncertainty (real space) i0_real_error1.0900e+07
Rg (reciprocal space) rg_reciprocal59.74
I(0) (reciprocal space) i0_reciprocal544700000.0000
Solution quality estimate total_estimate0.7721
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.1
Skewness Skewness skewness0.646
Kurtosis Kurtosis kurtosis-0.149
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0006
Highest regularization parameter α highest_alpha19130000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.611; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.698; Smooth: 0.504

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)