9o2u

BG505 SOSIP in complex with 007 bNAb IgG1 - trimer-dimer class

Method: ELECTRON MICROSCOPY Dmax: 223.3 Å Quality: EXCELLENT

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

Envelope glycoprotein gp120

Human immunodeficiency virus 1

UniProt Q2N0S6

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 × 24 其他Polymer 36 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 32–507 Chain B; UniProt 508–661 Chain C; UniProt 32–507 Chain D; UniProt 508–661 Chain E; UniProt 32–507 Chain F; UniProt 508–661 Chain O; UniProt 32–507 Chain P; UniProt 508–661 Chain Q; UniProt 32–507 Chain R; UniProt 508–661 Chain S; UniProt 32–507 Chain T; UniProt 508–661 Not recorded 007 IgG1 Heavy Chain × 6 007 Light Chain × 6 ;beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 6 ;alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 6 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 24 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 48 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

186 other PDB entries and 199 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S6_HV1
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–476; UniProt 32–507 Author chain C; PDBConstruct 1–476; UniProt 32–507 Author chain E; PDBConstruct 1–476; UniProt 32–507 Author chain O; PDBConstruct 1–476; UniProt 32–507 Author chain Q; PDBConstruct 1–476; UniProt 32–507 Author chain S; PDBConstruct 1–476; UniProt 32–507 Author chain B; PDBConstruct 3–156; UniProt 508–661 Author chain D; PDBConstruct 3–156; UniProt 508–661 Author chain F; PDBConstruct 3–156; UniProt 508–661 Author chain P; PDBConstruct 3–156; UniProt 508–661 Author chain R; PDBConstruct 3–156; UniProt 508–661 Author chain T; PDBConstruct 3–156; UniProt 508–661

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 9o2u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9o2u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9o2u
Deposition date deposition_date2025-04-04
最后修订 last_revision2025-10-01
Structure title titleBG505 SOSIP in complex with 007 bNAb IgG1 - trimer-dimer class
Keywords keywordsantibody, envelope, SOSIP, 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_guinier85.06
Radius of gyration Rg (electron density) rg_electron85.19
Forward intensity I(0) i06605750000.00
Molecular weight molecular_weight684710.0 kDa
Excluded volume excluded_volume853680 ų
Envelope volume envelope_volume1599900 ų
Hydration-shell volume shell_volume160670 ų
Envelope diameter envelope_diameter287.4
Shell Rg shell_rg88.10
Envelope Rg envelope_rg78.18
Shape Rg shape_rg85.20
Total Rg total_rg85.19
Total atoms total_atoms48054
Residues n_residues5904
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 dmax223.3
Rg (real space) rg_real81.39
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real6.3150e+09
I(0) uncertainty (real space) i0_real_error1.1060e+08
Rg (reciprocal space) rg_reciprocal84.51
I(0) (reciprocal space) i0_reciprocal6595000000.0000
Solution quality estimate total_estimate0.9081
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary111.6
Skewness Skewness skewness0.095
Kurtosis Kurtosis kurtosis-0.662
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha1.0050
Highest regularization parameter α highest_alpha219300000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.995; Stabil: 0.976; Sysdev: 1.000; Positv: 1.000; Valcen: 0.902; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)