9o8m

Ab1983 in complex with HIV-1 Env variant WIN332

Method: ELECTRON MICROSCOPY Dmax: 150.8 Å Quality: GOOD

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

Envelope glycoprotein gp160

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 × 10 其他Polymer 14 PDB declaration: decameric(10) Consistent with protein copy count Chain E; UniProt 32–510 Chain F; UniProt 509–661 Chain I; UniProt 32–510 Chain J; UniProt 509–661 Chain K; UniProt 32–510 Chain L; UniProt 509–661 Not recorded Antibody Ab1983 Heavy Chain variable fragment × 2 Ab1983 Light Chain variable fragment × 2 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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 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 × 22 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.79 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 3, 4
Chains and sequence ranges Author chain E; PDBConstruct 1–479; UniProt 32–510 Author chain I; PDBConstruct 1–479; UniProt 32–510 Author chain K; PDBConstruct 1–479; UniProt 32–510 Author chain F; PDBConstruct 1–153; UniProt 509–661 Author chain J; PDBConstruct 1–153; UniProt 509–661 Author chain L; 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 9o8m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9o8m
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9o8m
Deposition date deposition_date2025-04-16
Structure title titleAb1983 in complex with HIV-1 Env variant WIN332
Keywords keywordsHIV-1 Env, antibody, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.46
Radius of gyration Rg (electron density) rg_electron46.84
Forward intensity I(0) i0957912000.00
Molecular weight molecular_weight253070.0 kDa
Excluded volume excluded_volume315350 ų
Envelope volume envelope_volume454690 ų
Hydration-shell volume shell_volume79958 ų
Envelope diameter envelope_diameter152.1
Shell Rg shell_rg52.05
Envelope Rg envelope_rg45.86
Shape Rg shape_rg46.85
Total Rg total_rg47.01
Total atoms total_atoms17749
Residues n_residues2152
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 dmax150.8
Rg (real space) rg_real47.21
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real9.5790e+08
I(0) uncertainty (real space) i0_real_error1.9880e+07
Rg (reciprocal space) rg_reciprocal47.46
I(0) (reciprocal space) i0_reciprocal958200000.0000
Solution quality estimate total_estimate0.8744
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.0
Skewness Skewness skewness0.134
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha89310000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.769

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)