6apd

Crystal structure of RSV F bound by AM22 and the infant antibody ADI-19425

Method: X-RAY DIFFRACTION Dmax: 192.2 Å Quality: REASONABLE

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

Fusion glycoprotein F0,Envelope glycoprotein

Human immunodeficiency virus 1

UniProt C3UPB8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 1–513 Chain B; UniProt 1–513 Chain C; UniProt 1–513 Mutation:N67I, P129A, S215P, I379V, M447V,N67I, P129A, S215P, I379V, M447V,N67I, P129A, S215P, I379V, M447V,N67I, P129A, S215P, I379V, M447V AM22 Fab Heavy Chain,IGH@ protein × 3 (Q6GMX6) AM22 Fab Light Chain,Uncharacterized protein × 3 (Q8TCD0) Immunoglobulin heavy variable 3-21,Immunoglobulin gamma-1 heavy chain × 3 (A0A0B4J1V1,P0DOX5) IGL@ protein × 3 (Q6GMX4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;10% PEG 4000 10% 2-propanol 0.1 M sodium citrate pH 5.5 Resolution 4.10 Å R-free 0.256

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3UPB8_9MONO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–513; UniProt 1–513 Author chain B; PDBConstruct 1–513; UniProt 1–513 Author chain C; PDBConstruct 1–513; UniProt 1–513

Fusion glycoprotein F0,Envelope glycoprotein

Human immunodeficiency virus 1

UniProt M1E1E4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 1–29 Chain B; UniProt 1–29 Chain C; UniProt 1–29 Mutation:N67I, P129A, S215P, I379V, M447V,N67I, P129A, S215P, I379V, M447V,N67I, P129A, S215P, I379V, M447V,N67I, P129A, S215P, I379V, M447V AM22 Fab Heavy Chain,IGH@ protein × 3 (Q6GMX6) AM22 Fab Light Chain,Uncharacterized protein × 3 (Q8TCD0) Immunoglobulin heavy variable 3-21,Immunoglobulin gamma-1 heavy chain × 3 (A0A0B4J1V1,P0DOX5) IGL@ protein × 3 (Q6GMX4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;10% PEG 4000 10% 2-propanol 0.1 M sodium citrate pH 5.5 Resolution 4.10 Å R-free 0.256

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.

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

View Construct and Data Evidence
UniProt name M1E1E4_9HIV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 518–546; UniProt 1–29 Author chain B; PDBConstruct 518–546; UniProt 1–29 Author chain C; PDBConstruct 518–546; UniProt 1–29

AM22 Fab Heavy Chain,IGH@ protein

Homo sapiens

UniProt Q6GMX6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain D; UniProt 123–239 Chain F; UniProt 123–239 Chain H; UniProt 123–239 Not recorded Fusion glycoprotein F0,Envelope glycoprotein × 3 (C3UPB8,M1E1E4) AM22 Fab Light Chain,Uncharacterized protein × 3 (Q8TCD0) Immunoglobulin heavy variable 3-21,Immunoglobulin gamma-1 heavy chain × 3 (A0A0B4J1V1,P0DOX5) IGL@ protein × 3 (Q6GMX4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;10% PEG 4000 10% 2-propanol 0.1 M sodium citrate pH 5.5 Resolution 4.10 Å R-free 0.256

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.

18 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6GMX6_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 112–228; UniProt 123–239 Author chain F; PDBConstruct 112–228; UniProt 123–239 Author chain H; PDBConstruct 112–228; UniProt 123–239

AM22 Fab Light Chain,Uncharacterized protein

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 Insufficient information Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain E; UniProt 132–239 Chain G; UniProt 132–239 Chain I; UniProt 132–239 Not recorded Fusion glycoprotein F0,Envelope glycoprotein × 3 (C3UPB8,M1E1E4) AM22 Fab Heavy Chain,IGH@ protein × 3 (Q6GMX6) Immunoglobulin heavy variable 3-21,Immunoglobulin gamma-1 heavy chain × 3 (A0A0B4J1V1,P0DOX5) IGL@ protein × 3 (Q6GMX4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;10% PEG 4000 10% 2-propanol 0.1 M sodium citrate pH 5.5 Resolution 4.10 Å R-free 0.256

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 3
Chains and sequence ranges Author chain E; PDBConstruct 108–215; UniProt 132–239 Author chain G; PDBConstruct 108–215; UniProt 132–239 Author chain I; PDBConstruct 108–215; UniProt 132–239

Immunoglobulin heavy variable 3-21,Immunoglobulin gamma-1 heavy chain

Homo sapiens

UniProt A0A0B4J1V1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain J; UniProt 20–117 Chain K; UniProt 20–117 Chain N; UniProt 20–117 Not recorded Fusion glycoprotein F0,Envelope glycoprotein × 3 (C3UPB8,M1E1E4) AM22 Fab Heavy Chain,IGH@ protein × 3 (Q6GMX6) AM22 Fab Light Chain,Uncharacterized protein × 3 (Q8TCD0) IGL@ protein × 3 (Q6GMX4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;10% PEG 4000 10% 2-propanol 0.1 M sodium citrate pH 5.5 Resolution 4.10 Å R-free 0.256

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name HV321_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain J; PDBConstruct 1–98; UniProt 20–117 Author chain K; PDBConstruct 1–98; UniProt 20–117 Author chain N; PDBConstruct 1–98; UniProt 20–117

Immunoglobulin heavy variable 3-21,Immunoglobulin gamma-1 heavy chain

Homo sapiens

UniProt P0DOX5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain J; UniProt 109–223 Chain K; UniProt 109–223 Chain N; UniProt 109–223 Not recorded Fusion glycoprotein F0,Envelope glycoprotein × 3 (C3UPB8,M1E1E4) AM22 Fab Heavy Chain,IGH@ protein × 3 (Q6GMX6) AM22 Fab Light Chain,Uncharacterized protein × 3 (Q8TCD0) IGL@ protein × 3 (Q6GMX4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;10% PEG 4000 10% 2-propanol 0.1 M sodium citrate pH 5.5 Resolution 4.10 Å R-free 0.256

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.

105 other PDB entries and 128 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGG1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain J; PDBConstruct 112–226; UniProt 109–223 Author chain K; PDBConstruct 112–226; UniProt 109–223 Author chain N; PDBConstruct 112–226; UniProt 109–223

IGL@ protein

Homo sapiens

UniProt Q6GMX4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain L; UniProt 20–236 Chain M; UniProt 20–236 Chain O; UniProt 20–236 Not recorded Fusion glycoprotein F0,Envelope glycoprotein × 3 (C3UPB8,M1E1E4) AM22 Fab Heavy Chain,IGH@ protein × 3 (Q6GMX6) AM22 Fab Light Chain,Uncharacterized protein × 3 (Q8TCD0) Immunoglobulin heavy variable 3-21,Immunoglobulin gamma-1 heavy chain × 3 (A0A0B4J1V1,P0DOX5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;10% PEG 4000 10% 2-propanol 0.1 M sodium citrate pH 5.5 Resolution 4.10 Å R-free 0.256

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.

4 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6GMX4_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain L; PDBConstruct 1–218; UniProt 20–236 Author chain M; PDBConstruct 1–218; UniProt 20–236 Author chain O; PDBConstruct 1–218; UniProt 20–236

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 6apd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6apd
Deposition date deposition_date2017-08-17
Structure title titleCrystal structure of RSV F bound by AM22 and the infant antibody ADI-19425
Keywords keywordsviral glycoprotein, immunoglobulin, infant, complex, 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_guinier61.05
Radius of gyration Rg (electron density) rg_electron60.80
Forward intensity I(0) i02567930000.00
Molecular weight molecular_weight426830.0 kDa
Excluded volume excluded_volume534620 ų
Envelope volume envelope_volume816100 ų
Hydration-shell volume shell_volume112580 ų
Envelope diameter envelope_diameter195.4
Shell Rg shell_rg60.61
Envelope Rg envelope_rg60.66
Shape Rg shape_rg60.82
Total Rg total_rg60.74
Total atoms total_atoms30005
Residues n_residues3887
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 dmax192.2
Rg (real space) rg_real60.86
Rg uncertainty (real space) rg_real_error1.45
I(0) (real space) i0_real2.5680e+09
I(0) uncertainty (real space) i0_real_error5.1600e+07
Rg (reciprocal space) rg_reciprocal61.18
I(0) (reciprocal space) i0_reciprocal2569000000.0000
Solution quality estimate total_estimate0.6294
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary81.3
Skewness Skewness skewness0.160
Kurtosis Kurtosis kurtosis-0.523
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha147900000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 0.985; Smooth: 0.260

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)