9nc3

AMC008 v4.2 SOSIP Env trimer in complex with b12 and 3BC315 Fabs

Method: ELECTRON MICROSCOPY Dmax: 193.1 Å Quality: GOOD

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

Envelope glycoprotein gp41

Human immunodeficiency virus 1

UniProt Q1AII4

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 × 18 其他Polymer 25 PDB declaration: octadecameric(18) Consistent with protein copy count Chain B; UniProt 1–154 Chain D; UniProt 1–154 Chain F; UniProt 1–154 Not recorded Envelope glycoprotein gp120 × 3 3BC315 Fab heavy chain × 3 3BC315 Fab light chain × 3 b12 Fab heavy chain × 3 b12 Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ;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 ; × 1 ;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 ; × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[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 ; × 1 ;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 ;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 ; × 2 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 22 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.74 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q1AII4_HV1
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–154; UniProt 1–154 Author chain D; PDBConstruct 1–154; UniProt 1–154 Author chain F; PDBConstruct 1–154; UniProt 1–154

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 9nc3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9nc3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9nc3
Deposition date deposition_date2025-02-14
Structure title titleAMC008 v4.2 SOSIP Env trimer in complex with b12 and 3BC315 Fabs
Keywords keywordsHIV-1 Envelope glycoprotein, broadly neutralizing antibodies, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.97
Radius of gyration Rg (electron density) rg_electron56.49
Forward intensity I(0) i02477440000.00
Molecular weight molecular_weight410540.0 kDa
Excluded volume excluded_volume510770 ų
Envelope volume envelope_volume762430 ų
Hydration-shell volume shell_volume112300 ų
Envelope diameter envelope_diameter194.6
Shell Rg shell_rg59.57
Envelope Rg envelope_rg55.16
Shape Rg shape_rg56.49
Total Rg total_rg56.56
Total atoms total_atoms28821
Residues n_residues3522
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 dmax193.1
Rg (real space) rg_real56.82
Rg uncertainty (real space) rg_real_error1.58
I(0) (real space) i0_real2.4770e+09
I(0) uncertainty (real space) i0_real_error4.4240e+07
Rg (reciprocal space) rg_reciprocal57.08
I(0) (reciprocal space) i0_reciprocal2478000000.0000
Solution quality estimate total_estimate0.8585
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.9
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.257
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha113100000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.782; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.823

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (1)

9. Files and Curves (10)