9yii

V645-158 Fab in complex with HIV-1 Env 5MUT-3fill SOSIP

Method: ELECTRON MICROSCOPY Dmax: 150.8 Å Quality: GOOD

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

Transmembrane protein gp41

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 24 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 509–661 Chain B; UniProt 509–661 Chain C; UniProt 509–661 Chain E; UniProt 32–510 Chain F; UniProt 32–510 Chain G; UniProt 32–510 Not recorded V645-158 Fab heavy chain × 3 V645-158 Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 15 ;alpha-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-glucopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;alpha-D-mannopyranose-(1-3)-[alpha-D-glucopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-glucopyranose-(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 × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;150 mM NaCl, 20 mM Tris-HCl, pH 8.0 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_9HIV1
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–153; UniProt 509–661 Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain C; PDBConstruct 1–153; UniProt 509–661 Author chain E; PDBConstruct 1–479; UniProt 32–510 Author chain F; PDBConstruct 1–479; UniProt 32–510 Author chain G; PDBConstruct 1–479; UniProt 32–510

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 9yii

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9yii
Deposition date deposition_date2025-10-01
Structure title titleV645-158 Fab in complex with HIV-1 Env 5MUT-3fill SOSIP
Keywords keywordsHIV-1, Envelope protein, Vaccine, Immunogen, Antibody, bNAb, Viral Protein; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.88
Radius of gyration Rg (electron density) rg_electron49.49
Forward intensity I(0) i01194280000.00
Molecular weight molecular_weight283320.0 kDa
Excluded volume excluded_volume352800 ų
Envelope volume envelope_volume515090 ų
Hydration-shell volume shell_volume86103 ų
Envelope diameter envelope_diameter154.6
Shell Rg shell_rg53.91
Envelope Rg envelope_rg48.83
Shape Rg shape_rg49.51
Total Rg total_rg49.58
Total atoms total_atoms19863
Residues n_residues2301
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_real49.56
Rg uncertainty (real space) rg_real_error1.11
I(0) (real space) i0_real1.1940e+09
I(0) uncertainty (real space) i0_real_error2.2670e+07
Rg (reciprocal space) rg_reciprocal49.88
I(0) (reciprocal space) i0_reciprocal1195000000.0000
Solution quality estimate total_estimate0.8749
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.0
Skewness Skewness skewness0.067
Kurtosis Kurtosis kurtosis-0.568
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha100200000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.959; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.508

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)