6chb

Crystal structure of a natively-glycosylated BG505 SOSIP.664 HIV-1 Envelope Trimer in complex with the broadly-neutralizing antibodies BG18 and IOMA

Method: X-RAY DIFFRACTION Dmax: 208.8 Å Quality: GOOD

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

Envelope glycoprotein gp41

Human immunodeficiency virus 1

UniProt Q2N0S7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 509–661 Chain B; UniProt 509–661 Chain C; UniProt 509–661 Not recorded Envelope glycoprotein gp120 × 3 (Q2N0S6) BG18 Heavy Chain × 3 BG18 Light Chain × 3 IOMA Heavy Chain × 3 IOMA Light Chain × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;5% Tacismate pH 8.0, 15% PEG 3350 Resolution 6.80 Å R-free 0.417

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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S7_9HIV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–153; UniProt 509–661 Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain C; PDBConstruct 1–153; UniProt 509–661

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 Protein heterocomplex Heteromer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain F; UniProt 30–508 Chain G; UniProt 30–508 Chain H; UniProt 30–508 Not recorded Envelope glycoprotein gp41 × 3 (Q2N0S7) BG18 Heavy Chain × 3 BG18 Light Chain × 3 IOMA Heavy Chain × 3 IOMA Light Chain × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;5% Tacismate pH 8.0, 15% PEG 3350 Resolution 6.80 Å R-free 0.417

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 2
Chains and sequence ranges Author chain F; PDBConstruct 1–479; UniProt 30–508 Author chain G; PDBConstruct 1–479; UniProt 30–508 Author chain H; PDBConstruct 1–479; UniProt 30–508

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 6chb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6chb
Deposition date deposition_date2018-02-22
Structure title titleCrystal structure of a natively-glycosylated BG505 SOSIP.664 HIV-1 Envelope Trimer in complex with the broadly-neutralizing antibodies BG18 and IOMA
Keywords keywordsEnv glycoprotein, broadly neutralizing antibodies, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier62.31
Radius of gyration Rg (electron density) rg_electron62.43
Forward intensity I(0) i02461240000.00
Molecular weight molecular_weight409260.0 kDa
Excluded volume excluded_volume509160 ų
Envelope volume envelope_volume803200 ų
Hydration-shell volume shell_volume111300 ų
Envelope diameter envelope_diameter199.0
Shell Rg shell_rg59.83
Envelope Rg envelope_rg62.50
Shape Rg shape_rg62.43
Total Rg total_rg62.37
Total atoms total_atoms28753
Residues n_residues3671
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 dmax208.8
Rg (real space) rg_real62.32
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real2.4610e+09
I(0) uncertainty (real space) i0_real_error4.7310e+07
Rg (reciprocal space) rg_reciprocal62.26
I(0) (reciprocal space) i0_reciprocal2461000000.0000
Solution quality estimate total_estimate0.8230
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary75.2
Skewness Skewness skewness0.273
Kurtosis Kurtosis kurtosis-0.560
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0020
Highest regularization parameter α highest_alpha116100000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)