9yhs

AM12-340 Fab in complex with HIV-1 Env 5MUT-3fill SOSIP

Method: ELECTRON MICROSCOPY Dmax: 158.7 Å Quality: GOOD

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

BG505 MD39 SOSIP 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 33 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 AM12-340 Fab heavy chain × 3 AM12-340 Fab light chain × 3 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 × 21 ;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 ;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-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 × 36 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 4.30 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 3, 4
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 9yhs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9yhs
Deposition date deposition_date2025-09-30
Structure title titleAM12-340 Fab in complex with HIV-1 Env 5MUT-3fill SOSIP
Keywords keywordsHIV-1, Envelope protein, Vaccine, Immunogen, Antibody, bNAb, 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_guinier50.39
Radius of gyration Rg (electron density) rg_electron50.11
Forward intensity I(0) i01308410000.00
Molecular weight molecular_weight295290.0 kDa
Excluded volume excluded_volume367180 ų
Envelope volume envelope_volume541540 ų
Hydration-shell volume shell_volume89708 ų
Envelope diameter envelope_diameter165.8
Shell Rg shell_rg54.56
Envelope Rg envelope_rg49.20
Shape Rg shape_rg50.14
Total Rg total_rg50.17
Total atoms total_atoms20691
Residues n_residues2343
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 dmax158.7
Rg (real space) rg_real50.20
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real1.3080e+09
I(0) uncertainty (real space) i0_real_error2.3660e+07
Rg (reciprocal space) rg_reciprocal50.53
I(0) (reciprocal space) i0_reciprocal1309000000.0000
Solution quality estimate total_estimate0.8891
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.5
Skewness Skewness skewness0.088
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha80770000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.812

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)