6x96

Cryo-EM model of HIV-1 Env BG505 SOSIP.664 in complex with rabbit monoclonal antibody 10A fragment antigen binding variable domain

Method: ELECTRON MICROSCOPY Dmax: 145.5 Å Quality: GOOD

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

BG505 HIV-1 Env 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 12 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 G; UniProt 30–510 Chain I; UniProt 509–661 Mutation:T332N, A501C, E509R, K510R, A512R, V513R Mutation:I559P, T605C monoclonal antibody 10A fragment antigen binding heavy chain × 3 monoclonal antibody 10A kappa chain × 3 ;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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 33 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;Detergent (DDM) added shortly prior to freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 36–516; UniProt 30–510 Author chain C; PDBConstruct 36–516; UniProt 30–510 Author chain G; PDBConstruct 36–516; UniProt 30–510 Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain D; PDBConstruct 1–153; UniProt 509–661 Author chain I; 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 6x96

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6x96
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6x96
Deposition date deposition_date2020-06-02
Structure title titleCryo-EM model of HIV-1 Env BG505 SOSIP.664 in complex with rabbit monoclonal antibody 10A fragment antigen binding variable domain
Keywords keywordsHIV-1, Env, glycan hole, antibody, vaccine design, 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_guinier48.12
Radius of gyration Rg (electron density) rg_electron47.42
Forward intensity I(0) i01089870000.00
Molecular weight molecular_weight269880.0 kDa
Excluded volume excluded_volume335970 ų
Envelope volume envelope_volume473760 ų
Hydration-shell volume shell_volume81904 ų
Envelope diameter envelope_diameter151.2
Shell Rg shell_rg52.84
Envelope Rg envelope_rg46.60
Shape Rg shape_rg47.41
Total Rg total_rg47.63
Total atoms total_atoms18915
Residues n_residues2286
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 dmax145.5
Rg (real space) rg_real47.80
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real1.0900e+09
I(0) uncertainty (real space) i0_real_error1.8030e+07
Rg (reciprocal space) rg_reciprocal48.12
I(0) (reciprocal space) i0_reciprocal1090000000.0000
Solution quality estimate total_estimate0.8843
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.1
Skewness Skewness skewness0.049
Kurtosis Kurtosis kurtosis-0.600
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76250000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.617

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)