9cj7

Lineage IV Lassa virus glycoprotein (Josiah) in complex with monoclonal antibody 8.9F

Method: ELECTRON MICROSCOPY Dmax: 115.1 Å Quality: REASONABLE

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

Glycoprotein G1

Lassa virus Josiah

UniProt P08669

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 8 其他Polymer 27 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–259 Chain B; UniProt 1–259 Chain C; UniProt 1–259 Chain a; UniProt 260–424 Chain b; UniProt 260–424 Chain c; UniProt 260–424 Not recorded Fv region of 8.9F heavy chain × 1 Fv region of 8.9F light chain × 1 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 15 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;TBS cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLYC_LASSJ
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–259; UniProt 1–259 Author chain B; PDBConstruct 1–259; UniProt 1–259 Author chain C; PDBConstruct 1–259; UniProt 1–259 Author chain a; PDBConstruct 1–165; UniProt 260–424 Author chain b; PDBConstruct 1–165; UniProt 260–424 Author chain c; PDBConstruct 1–165; UniProt 260–424

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 9cj7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9cj7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9cj7
Deposition date deposition_date2024-07-05
Structure title titleLineage IV Lassa virus glycoprotein (Josiah) in complex with monoclonal antibody 8.9F
Keywords keywordsLassa, monoclonal antibody, 8.9F, glycoprotein, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex; VIRAL PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.84
Radius of gyration Rg (electron density) rg_electron34.15
Forward intensity I(0) i0436637000.00
Molecular weight molecular_weight164740.0 kDa
Excluded volume excluded_volume204110 ų
Envelope volume envelope_volume258860 ų
Hydration-shell volume shell_volume60609 ų
Envelope diameter envelope_diameter123.8
Shell Rg shell_rg42.43
Envelope Rg envelope_rg34.50
Shape Rg shape_rg34.14
Total Rg total_rg34.72
Total atoms total_atoms11501
Residues n_residues1271
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 dmax115.1
Rg (real space) rg_real34.77
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real4.3660e+08
I(0) uncertainty (real space) i0_real_error6.4180e+06
Rg (reciprocal space) rg_reciprocal34.81
I(0) (reciprocal space) i0_reciprocal436700000.0000
Solution quality estimate total_estimate0.6759
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.5
Skewness Skewness skewness0.372
Kurtosis Kurtosis kurtosis-0.074
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha197900000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.796; Stabil: 1.000; Sysdev: 0.186; Positv: 1.000; Valcen: 0.993; Smooth: 0.841

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)