5v8l

BG505 SOSIP.664 trimer in complex with broadly neutralizing HIV antibodies 3BNC117 and PGT145

Method: ELECTRON MICROSCOPY Dmax: 150.2 Å Quality: REASONABLE

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

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 × 14 其他Polymer 43 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain A; UniProt 30–505 Chain B; UniProt 509–661 Chain C; UniProt 30–505 Chain D; UniProt 30–505 Chain E; UniProt 509–661 Chain F; UniProt 509–661 Fragment:UNP residues 30-505 Fragment:UNP residues 509-661 3BNC117 antibody, heavy chain × 3 PGT145 antibody, heavy chain × 1 3BNC117 antibody, light chain × 3 PGT145 antibody, light chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 28 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ;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)]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)-[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)-[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-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE 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 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–476; UniProt 30–505 Author chain C; PDBConstruct 1–476; UniProt 30–505 Author chain D; PDBConstruct 1–476; UniProt 30–505 Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain E; 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 5v8l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5v8l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5v8l
Deposition date deposition_date2017-03-22
Structure title titleBG505 SOSIP.664 trimer in complex with broadly neutralizing HIV antibodies 3BNC117 and PGT145
Keywords keywordsHIV, broadly neutralizing antibody, PGT145, 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_guinier47.70
Radius of gyration Rg (electron density) rg_electron46.87
Forward intensity I(0) i01615650000.00
Molecular weight molecular_weight327070.0 kDa
Excluded volume excluded_volume406450 ų
Envelope volume envelope_volume590870 ų
Hydration-shell volume shell_volume101570 ų
Envelope diameter envelope_diameter161.7
Shell Rg shell_rg54.16
Envelope Rg envelope_rg45.90
Shape Rg shape_rg46.86
Total Rg total_rg47.17
Total atoms total_atoms22934
Residues n_residues2572
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 dmax150.2
Rg (real space) rg_real47.35
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real1.6160e+09
I(0) uncertainty (real space) i0_real_error2.8230e+07
Rg (reciprocal space) rg_reciprocal47.70
I(0) (reciprocal space) i0_reciprocal1616000000.0000
Solution quality estimate total_estimate0.6562
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.7
Skewness Skewness skewness0.105
Kurtosis Kurtosis kurtosis-0.361
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha164900000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 0.044; Positv: 1.000; Valcen: 0.955; Smooth: 0.848

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)