8sic

Crystal structure of Epstein-Barr virus glycoprotein 350 (gp350) in complex with Cy137C02, a monoclonal antibody isolated from macaques immunized with a gp350 nanoparticle vaccine

Method: X-RAY DIFFRACTION Dmax: 230.9 Å Quality: REASONABLE

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

Envelope glycoprotein gp350

Human herpesvirus 4

UniProt P03200

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–425 Not recorded Cy137C02 Fab heavy chain × 1 Cy137C02 Fab light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;18% PEG 8000, 0.22 M sodium acetate, 0.1 M sodium cacodylate pH 6.5 Resolution 2.76 Å R-free 0.295
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–425 Not recorded Cy137C02 Fab heavy chain × 1 Cy137C02 Fab light chain × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;18% PEG 8000, 0.22 M sodium acetate, 0.1 M sodium cacodylate pH 6.5 Resolution 2.76 Å R-free 0.295

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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GP350_EBVB9
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–425; UniProt 1–425 Author chain G; PDBConstruct 1–425; UniProt 1–425

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 8sic

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8sic
Deposition date deposition_date2023-04-14
Structure title titleCrystal structure of Epstein-Barr virus glycoprotein 350 (gp350) in complex with Cy137C02, a monoclonal antibody isolated from macaques immunized with a gp350 nanoparticle vaccine
Keywords keywords;viral protein, envelope glycoprotein, monoclonal antibody, antiviral, immune system, macaques, Epstein-Barr virus, VIRAL PROTEIN-IMMUNE SYSTEM complex ;; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier64.66
Radius of gyration Rg (electron density) rg_electron67.50
Forward intensity I(0) i0510828000.00
Molecular weight molecular_weight186240.0 kDa
Excluded volume excluded_volume232120 ų
Envelope volume envelope_volume345310 ų
Hydration-shell volume shell_volume52318 ų
Envelope diameter envelope_diameter252.5
Shell Rg shell_rg48.43
Envelope Rg envelope_rg68.55
Shape Rg shape_rg67.49
Total Rg total_rg66.97
Total atoms total_atoms13106
Residues n_residues1670
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 dmax230.9
Rg (real space) rg_real66.76
Rg uncertainty (real space) rg_real_error3.23
I(0) (real space) i0_real5.1060e+08
I(0) uncertainty (real space) i0_real_error1.3090e+07
Rg (reciprocal space) rg_reciprocal62.80
I(0) (reciprocal space) i0_reciprocal507300000.0000
Solution quality estimate total_estimate0.6605
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.5
Skewness Skewness skewness0.729
Kurtosis Kurtosis kurtosis-0.204
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0010
Highest regularization parameter α highest_alpha15780000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.303; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.211; Smooth: 0.468

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)