8ulr

Cryo-EM structure of the BG505 SOSIPv2 in complex with bNAb 05_B08 Fabs

Method: ELECTRON MICROSCOPY Dmax: 133.1 Å Quality: GOOD

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

Envelope glycoprotein gp160

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 28 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 32–501 Chain C; UniProt 32–501 Chain E; UniProt 32–501 Not recorded BG505 DS-SOSIP glycoprotein gp41 × 3 (Q2N0S5) 05_B08 Fab Heavy Chain × 3 05_B08 Light Chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 15 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 ; × 4 ;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 ; × 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 ; × 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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3s blot, 0 blot force Resolution 3.30 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–470; UniProt 32–501 Author chain C; PDBConstruct 1–470; UniProt 32–501 Author chain E; PDBConstruct 1–470; UniProt 32–501

BG505 DS-SOSIP glycoprotein gp41

Human immunodeficiency virus 1

UniProt Q2N0S5

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 28 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 509–661 Chain D; UniProt 509–661 Chain F; UniProt 509–661 Not recorded Envelope glycoprotein gp160 × 3 (Q2N0S6) 05_B08 Fab Heavy Chain × 3 05_B08 Light Chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 15 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 ; × 4 ;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 ; × 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 ; × 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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;3s blot, 0 blot force Resolution 3.30 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.

53 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S5_9HIV1
Isoform
PDB entities 2
Chains and sequence ranges 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 8ulr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ulr
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8ulr
Deposition date deposition_date2023-10-16
Structure title titleCryo-EM structure of the BG505 SOSIPv2 in complex with bNAb 05_B08 Fabs
Keywords keywordsHIV-1, ANTIBODY, CD4-BINDING SITE, IMMUNE COMPLEX, 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_guinier43.94
Radius of gyration Rg (electron density) rg_electron43.02
Forward intensity I(0) i01211960000.00
Molecular weight molecular_weight283110.0 kDa
Excluded volume excluded_volume352330 ų
Envelope volume envelope_volume481210 ų
Hydration-shell volume shell_volume88973 ų
Envelope diameter envelope_diameter137.1
Shell Rg shell_rg51.37
Envelope Rg envelope_rg42.13
Shape Rg shape_rg43.03
Total Rg total_rg43.37
Total atoms total_atoms19837
Residues n_residues2325
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 dmax133.1
Rg (real space) rg_real43.60
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real1.2120e+09
I(0) uncertainty (real space) i0_real_error2.0160e+07
Rg (reciprocal space) rg_reciprocal43.93
I(0) (reciprocal space) i0_reciprocal1212000000.0000
Solution quality estimate total_estimate0.8946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.2
Skewness Skewness skewness-0.001
Kurtosis Kurtosis kurtosis-0.563
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha114500000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.899

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)