9q0w

Cryo-EM Structure of HIV-1 BG505DS-SOSIP.664 Env Trimer Bound to DFPH-a.01_10R59P_LC Fab

Method: ELECTRON MICROSCOPY Dmax: 190.8 Å Quality: REASONABLE

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

HIV-1 BG505 DS-SOSIP 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 × 12 其他Polymer 30 PDB declaration: 12-meric(12) Consistent with protein copy count Chain A; UniProt 30–505 Chain C; UniProt 30–505 Chain E; UniProt 30–505 Fragment:UNP residues 30-505 BG505 DS-SOSIP GP41 × 3 (Q2N0S5) DFPH-a.01_10R59P_LC Fab heavy chain × 3 DFPH-a.01_10R59P_LC Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 27 ;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 ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

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

View Construct and Data Evidence
UniProt name Q2N0S6_9HIV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–476; UniProt 30–505 Author chain C; PDBConstruct 1–476; UniProt 30–505 Author chain E; PDBConstruct 1–476; UniProt 30–505

BG505 DS-SOSIP GP41

Human immunodeficiency virus 1

UniProt Q2N0S5

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 × 12 其他Polymer 30 PDB declaration: 12-meric(12) Consistent with protein copy count Chain B; UniProt 509–661 Chain D; UniProt 509–661 Chain F; UniProt 509–661 Not recorded HIV-1 BG505 DS-SOSIP gp120 × 3 (Q2N0S6) DFPH-a.01_10R59P_LC Fab heavy chain × 3 DFPH-a.01_10R59P_LC Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 27 ;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 ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

53 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S5_9HIV1
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain D; PDBConstruct 1–153; UniProt 509–661 Author chain F; PDBConstruct 1–153; UniProt 509–661

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 9q0w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9q0w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9q0w
Deposition date deposition_date2025-08-13
最后修订 last_revision2025-12-10
Structure title titleCryo-EM Structure of HIV-1 BG505DS-SOSIP.664 Env Trimer Bound to DFPH-a.01_10R59P_LC Fab
Keywords keywordsantibody improvement, broadly neutralizing antibody, epitope, fusion peptide, HIV-1 vaccine, paratope, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.30
Radius of gyration Rg (electron density) rg_electron56.13
Forward intensity I(0) i01841790000.00
Molecular weight molecular_weight352650.0 kDa
Excluded volume excluded_volume438960 ų
Envelope volume envelope_volume667310 ų
Hydration-shell volume shell_volume100840 ų
Envelope diameter envelope_diameter202.4
Shell Rg shell_rg56.98
Envelope Rg envelope_rg55.74
Shape Rg shape_rg56.12
Total Rg total_rg56.18
Total atoms total_atoms24735
Residues n_residues3042
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 dmax190.8
Rg (real space) rg_real56.28
Rg uncertainty (real space) rg_real_error1.64
I(0) (real space) i0_real1.8420e+09
I(0) uncertainty (real space) i0_real_error3.7900e+07
Rg (reciprocal space) rg_reciprocal56.30
I(0) (reciprocal space) i0_reciprocal1842000000.0000
Solution quality estimate total_estimate0.6551
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.2
Skewness Skewness skewness0.322
Kurtosis Kurtosis kurtosis-0.280
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha88570000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 0.041; Positv: 1.000; Valcen: 0.997; Smooth: 0.836

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)