5viy

BG505 SOSIP.664 in complex with broadly neutralizing antibodies BG1 and 8ANC195

Method: ELECTRON MICROSCOPY Dmax: 216.9 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 × 16 其他Polymer 44 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 509–661 Chain B; UniProt 509–661 Chain C; UniProt 509–661 Chain D; UniProt 30–508 Chain E; UniProt 30–508 Chain F; UniProt 30–508 Fragment:UNP residues 509-661 Fragment:UNP residues 30-505 BG1 Fab light chain × 2 (P01834) BG1 Fab heavy chain × 2 (S6B291) 8ANC195 G52K5 Fab heavy chain × 3 (S6B291) 8ANC195 G52K5 Fab light chain × 3 (Q8TCD0) ;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 ; × 9 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ;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 ;alpha-D-mannopyranose-(1-2)-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 ;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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 7 alpha-L-fucopyranose-(1-6)-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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.20 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 1–153; UniProt 509–661 Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain C; PDBConstruct 1–153; UniProt 509–661 Author chain D; PDBConstruct 1–479; UniProt 30–508 Author chain E; PDBConstruct 1–479; UniProt 30–508 Author chain F; PDBConstruct 1–479; UniProt 30–508

BG1 Fab light chain

Homo sapiens

UniProt P01834

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 × 16 其他Polymer 44 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain G; UniProt 1–107 Chain I; UniProt 1–107 Not recorded Envelope glycoprotein gp160 × 3 (Q2N0S6) Envelope glycoprotein gp160 × 3 (Q2N0S6) BG1 Fab heavy chain × 2 (S6B291) 8ANC195 G52K5 Fab heavy chain × 3 (S6B291) 8ANC195 G52K5 Fab light chain × 3 (Q8TCD0) ;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 ; × 9 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ;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 ;alpha-D-mannopyranose-(1-2)-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 ;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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 7 alpha-L-fucopyranose-(1-6)-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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.20 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.

44 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGKC_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 108–214; UniProt 1–107 Author chain I; PDBConstruct 108–214; UniProt 1–107

BG1 Fab heavy chain

Homo sapiens

UniProt S6B291

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 × 16 其他Polymer 44 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain H; UniProt 137–236 Chain J; UniProt 137–236 Chain K; UniProt 137–237 Chain M; UniProt 137–237 Chain O; UniProt 137–237 Not recorded Envelope glycoprotein gp160 × 3 (Q2N0S6) Envelope glycoprotein gp160 × 3 (Q2N0S6) BG1 Fab light chain × 2 (P01834) 8ANC195 G52K5 Fab light chain × 3 (Q8TCD0) ;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 ; × 9 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ;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 ;alpha-D-mannopyranose-(1-2)-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 ;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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 7 alpha-L-fucopyranose-(1-6)-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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.20 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.

27 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name S6B291_HUMAN
Isoform
PDB entities 4, 5
Chains and sequence ranges Author chain H; PDBConstruct 134–233; UniProt 137–236 Author chain J; PDBConstruct 134–233; UniProt 137–236 Author chain K; PDBConstruct 133–233; UniProt 137–237 Author chain M; PDBConstruct 133–233; UniProt 137–237 Author chain O; PDBConstruct 133–233; UniProt 137–237

8ANC195 G52K5 Fab light chain

Homo sapiens

UniProt Q8TCD0

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 × 16 其他Polymer 44 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain L; UniProt 132–239 Chain N; UniProt 132–239 Chain P; UniProt 132–239 Not recorded Envelope glycoprotein gp160 × 3 (Q2N0S6) Envelope glycoprotein gp160 × 3 (Q2N0S6) BG1 Fab light chain × 2 (P01834) BG1 Fab heavy chain × 2 (S6B291) 8ANC195 G52K5 Fab heavy chain × 3 (S6B291) ;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 ; × 9 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ;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 ;alpha-D-mannopyranose-(1-2)-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 ;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 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 7 alpha-L-fucopyranose-(1-6)-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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 13 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.20 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.

39 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8TCD0_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain L; PDBConstruct 108–215; UniProt 132–239 Author chain N; PDBConstruct 108–215; UniProt 132–239 Author chain P; PDBConstruct 108–215; UniProt 132–239

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 5viy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5viy
Deposition date deposition_date2017-04-17
Structure title titleBG505 SOSIP.664 in complex with broadly neutralizing antibodies BG1 and 8ANC195
Keywords keywordsHIV-1 Env, broadly neutralizing antibodies, cryo-EM, single particle analysis, 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_guinier63.13
Radius of gyration Rg (electron density) rg_electron63.03
Forward intensity I(0) i03064240000.00
Molecular weight molecular_weight456530.0 kDa
Excluded volume excluded_volume567390 ų
Envelope volume envelope_volume897060 ų
Hydration-shell volume shell_volume122990 ų
Envelope diameter envelope_diameter208.7
Shell Rg shell_rg61.00
Envelope Rg envelope_rg61.82
Shape Rg shape_rg63.10
Total Rg total_rg62.72
Total atoms total_atoms32071
Residues n_residues3874
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 dmax216.9
Rg (real space) rg_real63.07
Rg uncertainty (real space) rg_real_error1.99
I(0) (real space) i0_real3.0640e+09
I(0) uncertainty (real space) i0_real_error6.1510e+07
Rg (reciprocal space) rg_reciprocal63.15
I(0) (reciprocal space) i0_reciprocal3065000000.0000
Solution quality estimate total_estimate0.8758
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary199.6
Skewness Skewness skewness0.260
Kurtosis Kurtosis kurtosis-0.490
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0006
Highest regularization parameter α highest_alpha130600000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.838; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (1)

9. Files and Curves (10)