8euv

Cryo-EM structure of HIV-1 BG505 DS-SOSIP ENV trimer bound to VRC34.01-COMBO1 FAB

Method: ELECTRON MICROSCOPY Dmax: 142.8 Å Quality: GOOD

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

Envelope glycoprotein gp120

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 30 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 30–510 Chain B; UniProt 509–661 Chain C; UniProt 30–510 Chain D; UniProt 509–661 Chain E; UniProt 30–510 Chain F; UniProt 509–661 Fragment:UNP residues 30-510 Fragment:UNP residues 509-661 VRC34.01-COMBO1 FAB variable heavy chain × 3 VRC34.01-COMBO1 FAB variable light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 24 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)-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 × 15 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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 1–481; UniProt 30–510 Author chain C; PDBConstruct 1–481; UniProt 30–510 Author chain E; PDBConstruct 1–481; UniProt 30–510 Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain D; PDBConstruct 1–153; UniProt 509–661 Author chain F; 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 8euv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8euv
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8euv
Deposition date deposition_date2022-10-19
Structure title titleCryo-EM structure of HIV-1 BG505 DS-SOSIP ENV trimer bound to VRC34.01-COMBO1 FAB
Keywords keywords;broadly neutralizing antibody, fusion peptide, HIV-1, glycoprotein, viral protein, FP-targeting vaccines, 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_guinier47.60
Radius of gyration Rg (electron density) rg_electron46.84
Forward intensity I(0) i01210840000.00
Molecular weight molecular_weight284430.0 kDa
Excluded volume excluded_volume354020 ų
Envelope volume envelope_volume489360 ų
Hydration-shell volume shell_volume84613 ų
Envelope diameter envelope_diameter145.5
Shell Rg shell_rg53.04
Envelope Rg envelope_rg46.10
Shape Rg shape_rg46.83
Total Rg total_rg47.07
Total atoms total_atoms19938
Residues n_residues2370
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 dmax142.8
Rg (real space) rg_real47.23
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real1.2110e+09
I(0) uncertainty (real space) i0_real_error2.3590e+07
Rg (reciprocal space) rg_reciprocal47.59
I(0) (reciprocal space) i0_reciprocal1211000000.0000
Solution quality estimate total_estimate0.8808
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.9
Skewness Skewness skewness0.022
Kurtosis Kurtosis kurtosis-0.568
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha66780000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.620

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)