6nf2

Cryo-EM structure of vaccine-elicited antibody 0PV-c.01 in complex with HIV-1 Env BG505 DS-SOSIP and antibodies VRC03 and PGT122

Method: ELECTRON MICROSCOPY Dmax: 175.4 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 × 24 其他Polymer 48 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 30–509 Chain B; UniProt 509–661 Chain G; UniProt 30–509 Chain I; UniProt 509–661 Chain Q; UniProt 30–509 Chain R; UniProt 509–661 Mutation:I201C, T332N, A433C, A501C, E509R, K510R, A512R Mutation:I559P, T605C VRC03 Heavy Chain × 3 VRC03 Light Chain × 3 PGT122 Heavy Chain × 3 PGT122 Light Chain × 3 0PV-c.01 Heavy Chain × 3 0PV-c.01 Light Chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 15 ;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 ; × 6 ;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 ; × 6 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ;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-(1-6)]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-(1-2)-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 × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 1–480; UniProt 30–509 Author chain G; PDBConstruct 1–480; UniProt 30–509 Author chain Q; PDBConstruct 1–480; UniProt 30–509 Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain I; PDBConstruct 1–153; UniProt 509–661 Author chain R; 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 6nf2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6nf2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6nf2
Deposition date deposition_date2018-12-18
Structure title titleCryo-EM structure of vaccine-elicited antibody 0PV-c.01 in complex with HIV-1 Env BG505 DS-SOSIP and antibodies VRC03 and PGT122
Keywords keywordsFusion Peptide, FP, HIV-1, SOSIP, Vaccine, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.19
Radius of gyration Rg (electron density) rg_electron54.90
Forward intensity I(0) i03146300000.00
Molecular weight molecular_weight464520.0 kDa
Excluded volume excluded_volume578580 ų
Envelope volume envelope_volume867650 ų
Hydration-shell volume shell_volume128380 ų
Envelope diameter envelope_diameter181.4
Shell Rg shell_rg60.71
Envelope Rg envelope_rg53.76
Shape Rg shape_rg54.92
Total Rg total_rg54.98
Total atoms total_atoms32604
Residues n_residues3867
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 dmax175.4
Rg (real space) rg_real54.93
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real3.1460e+09
I(0) uncertainty (real space) i0_real_error6.2670e+07
Rg (reciprocal space) rg_reciprocal55.40
I(0) (reciprocal space) i0_reciprocal3148000000.0000
Solution quality estimate total_estimate0.8658
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.9
Skewness Skewness skewness0.164
Kurtosis Kurtosis kurtosis-0.348
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha213900000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.719

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)