9btv

Cryo-EM structure of rhesus antibody T646-a.01 in complex with HIV-1 Env trimer Q23.17 MD39

Method: ELECTRON MICROSCOPY Dmax: 138.1 Å Quality: GOOD

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

Envelope glycoprotein gp120

Human immunodeficiency virus 1

UniProt O55774

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 × 8 其他Polymer 41 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 30–498 Chain B; UniProt 502–654 Chain C; UniProt 30–498 Chain E; UniProt 30–498 Chain F; UniProt 502–654 Chain G; UniProt 502–654 Not recorded T646-a.01 heavy chain × 1 T646-a.01 light chain × 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 ;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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 24 ;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 ;alpha-D-mannopyranose-(1-6)-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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.48 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O55774_9HIV1
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–469; UniProt 30–498 Author chain C; PDBConstruct 1–469; UniProt 30–498 Author chain E; PDBConstruct 1–469; UniProt 30–498 Author chain B; PDBConstruct 1–153; UniProt 502–654 Author chain F; PDBConstruct 1–153; UniProt 502–654 Author chain G; PDBConstruct 1–153; UniProt 502–654

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 9btv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9btv
Deposition date deposition_date2024-05-15
Structure title titleCryo-EM structure of rhesus antibody T646-a.01 in complex with HIV-1 Env trimer Q23.17 MD39
Keywords keywordsNeutralizing antibody, HIV-1 V2 apex, SHIV-elicited, Viral protein, IMMUNE SYSTEM, 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_guinier43.45
Radius of gyration Rg (electron density) rg_electron42.74
Forward intensity I(0) i0873356000.00
Molecular weight molecular_weight240560.0 kDa
Excluded volume excluded_volume299700 ų
Envelope volume envelope_volume418430 ų
Hydration-shell volume shell_volume78189 ų
Envelope diameter envelope_diameter142.3
Shell Rg shell_rg50.60
Envelope Rg envelope_rg42.26
Shape Rg shape_rg42.73
Total Rg total_rg43.12
Total atoms total_atoms16852
Residues n_residues1882
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 dmax138.1
Rg (real space) rg_real43.23
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real8.7340e+08
I(0) uncertainty (real space) i0_real_error1.6130e+07
Rg (reciprocal space) rg_reciprocal43.44
I(0) (reciprocal space) i0_reciprocal873600000.0000
Solution quality estimate total_estimate0.8821
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.4
Skewness Skewness skewness0.118
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha156100000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.819

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)