5c6b

Crystal Structure of Prefusion-stabilized RSV F variant SC-TM

Method: X-RAY DIFFRACTION Dmax: 108.7 Å Quality: GOOD

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

Fusion glycoprotein F0,Fibritin

Enterobacteria phage Ox2

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 Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 26–513 Fragment:ectodomain Mutation:N67I, S215P, E487Q, I379V, M447V,N67I, S215P, E487Q, I379V, M447V NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID × 6 SO4 SULFATE ION × 24 CL CHLORIDE ION × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 9.5;293 K;1.34M K/Na tartrate, 0.2M LiSO4, 0.1M CHES pH 9.5 Resolution 2.40 Å R-free 0.211

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 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FUS_HRSVA
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–466; UniProt 26–513

Fusion glycoprotein F0,Fibritin

Enterobacteria phage Ox2

UniProt Q38650

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 Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 458–484 Fragment:ectodomain Mutation:N67I, S215P, E487Q, I379V, M447V,N67I, S215P, E487Q, I379V, M447V NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID × 6 SO4 SULFATE ION × 24 CL CHLORIDE ION × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 9.5;293 K;1.34M K/Na tartrate, 0.2M LiSO4, 0.1M CHES pH 9.5 Resolution 2.40 Å R-free 0.211

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q38650_BPOX2
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 471–497; UniProt 458–484

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 5c6b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5c6b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5c6b
Deposition date deposition_date2015-06-22
Structure title titleCrystal Structure of Prefusion-stabilized RSV F variant SC-TM
Keywords keywordsclass I viral fusion protein, fusion, respiratory syncytial virus, prefusion, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.18
Radius of gyration Rg (electron density) rg_electron30.18
Forward intensity I(0) i042498900.00
Molecular weight molecular_weight50881.0 kDa
Excluded volume excluded_volume63709 ų
Envelope volume envelope_volume81399 ų
Hydration-shell volume shell_volume24134 ų
Envelope diameter envelope_diameter115.1
Shell Rg shell_rg34.65
Envelope Rg envelope_rg30.35
Shape Rg shape_rg30.14
Total Rg total_rg30.76
Total atoms total_atoms3552
Residues n_residues456
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 dmax108.7
Rg (real space) rg_real30.50
Rg uncertainty (real space) rg_real_error1.57
I(0) (real space) i0_real4.2500e+07
I(0) uncertainty (real space) i0_real_error7.5030e+05
Rg (reciprocal space) rg_reciprocal30.37
I(0) (reciprocal space) i0_reciprocal42490000.0000
Solution quality estimate total_estimate0.7893
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.507
Kurtosis Kurtosis kurtosis-0.429
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7895000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.606; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.466; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)