6ous

Structure of fusion glycoprotein from human respiratory syncytial virus

Method: X-RAY DIFFRACTION Dmax: 259.5 Å Quality: GOOD

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

Fusion glycoprotein F2

Human respiratory syncytial virus A2

UniProt P03420

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 × 12 其他Polymer 3 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 26–109 Chain B; UniProt 137–513 Chain C; UniProt 26–109 Chain D; UniProt 137–513 Chain E; UniProt 26–109 Chain F; UniProt 137–513 Non-standard monomer:Yes (specific site not provided by mmCIF) RB1 Fab Heavy Chain × 3 RB1 Fab Light 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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;100 mM Tris 8.5, 10% PEG 8000, 200 mM ammonium sulfate Resolution 3.40 Å R-free 0.275
2 Insufficient information Heteromer Protein × 12 其他Polymer 3 PDB declaration: dodecameric(12) Consistent with protein copy count Chain G; UniProt 26–109 Chain H; UniProt 137–513 Chain I; UniProt 26–109 Chain J; UniProt 137–513 Chain K; UniProt 26–109 Chain L; UniProt 137–513 Non-standard monomer:Yes (specific site not provided by mmCIF) RB1 Fab Heavy Chain × 3 RB1 Fab Light 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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;100 mM Tris 8.5, 10% PEG 8000, 200 mM ammonium sulfate Resolution 3.40 Å R-free 0.275

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.

52 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FUS_HRSVA
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–84; UniProt 26–109 Author chain C; PDBConstruct 1–84; UniProt 26–109 Author chain E; PDBConstruct 1–84; UniProt 26–109 Author chain G; PDBConstruct 1–84; UniProt 26–109 Author chain I; PDBConstruct 1–84; UniProt 26–109 Author chain K; PDBConstruct 1–84; UniProt 26–109 Author chain B; PDBConstruct 1–377; UniProt 137–513 Author chain D; PDBConstruct 1–377; UniProt 137–513 Author chain F; PDBConstruct 1–377; UniProt 137–513 Author chain H; PDBConstruct 1–377; UniProt 137–513 Author chain J; PDBConstruct 1–377; UniProt 137–513 Author chain L; PDBConstruct 1–377; UniProt 137–513

Fusion glycoprotein F1 fused with Fibritin trimerization domain

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 × 12 其他Polymer 3 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1–28 Chain D; UniProt 1–28 Chain F; UniProt 1–28 Not recorded Fusion glycoprotein F2 × 3 (P03420) RB1 Fab Heavy Chain × 3 RB1 Fab Light 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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;100 mM Tris 8.5, 10% PEG 8000, 200 mM ammonium sulfate Resolution 3.40 Å R-free 0.275
2 Insufficient information Heteromer Protein × 12 其他Polymer 3 PDB declaration: dodecameric(12) Consistent with protein copy count Chain H; UniProt 1–28 Chain J; UniProt 1–28 Chain L; UniProt 1–28 Not recorded Fusion glycoprotein F2 × 3 (P03420) RB1 Fab Heavy Chain × 3 RB1 Fab Light 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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;100 mM Tris 8.5, 10% PEG 8000, 200 mM ammonium sulfate Resolution 3.40 Å R-free 0.275

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 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name M1E1E4_9HIV1
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 382–409; UniProt 1–28 Author chain D; PDBConstruct 382–409; UniProt 1–28 Author chain F; PDBConstruct 382–409; UniProt 1–28 Author chain H; PDBConstruct 382–409; UniProt 1–28 Author chain J; PDBConstruct 382–409; UniProt 1–28 Author chain L; PDBConstruct 382–409; UniProt 1–28

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 6ous

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ous
Deposition date deposition_date2019-05-05
Structure title titleStructure of fusion glycoprotein from human respiratory syncytial virus
Keywords keywordsAntibody, RSV, Neutralizing, VIRAL PROTEIN, VIRAL PROTEIN-Immune system complex; VIRAL PROTEIN/Immune system
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier74.65
Radius of gyration Rg (electron density) rg_electron74.46
Forward intensity I(0) i04839100000.00
Molecular weight molecular_weight592120.0 kDa
Excluded volume excluded_volume741950 ų
Envelope volume envelope_volume1193000 ų
Hydration-shell volume shell_volume134610 ų
Envelope diameter envelope_diameter279.2
Shell Rg shell_rg71.17
Envelope Rg envelope_rg73.68
Shape Rg shape_rg74.53
Total Rg total_rg74.17
Total atoms total_atoms41597
Residues n_residues5445
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 dmax259.5
Rg (real space) rg_real74.71
Rg uncertainty (real space) rg_real_error4.25
I(0) (real space) i0_real4.8390e+09
I(0) uncertainty (real space) i0_real_error1.1310e+08
Rg (reciprocal space) rg_reciprocal74.33
I(0) (reciprocal space) i0_reciprocal4835000000.0000
Solution quality estimate total_estimate0.8567
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary98.8
Skewness Skewness skewness0.291
Kurtosis Kurtosis kurtosis-0.297
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha216900000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.649

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id6ousM02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousN02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousO02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousP02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousQ02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousR02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousS02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousT02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousU02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousV02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousW02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6ousX02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)