4mmq

Crystal Structure of Prefusion-stabilized RSV F Variant DS

Method: X-RAY DIFFRACTION Dmax: 107.8 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 26–107 Chain B; UniProt 137–513 Mutation:P102A Mutation:S155C, S290C, I379V, M447V SO4 SULFATE ION × 18 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9.5;298 K;1.4 M K/Na tartrate, 0.1M CHES pH 9.5, 0.2 M LiSO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.25 Å R-free 0.274

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–82; UniProt 26–107 Author chain B; PDBConstruct 1–377; UniProt 137–513

Fusion glycoprotein F1 fused with Fibritin trimerization domain

Enterobacteria phage T4

UniProt P10104

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 458–484 Mutation:S155C, S290C, I379V, M447V Fusion glycoprotein F2 × 3 (P03420) SO4 SULFATE ION × 18 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9.5;298 K;1.4 M K/Na tartrate, 0.1M CHES pH 9.5, 0.2 M LiSO4, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 3.25 Å R-free 0.274

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.

104 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WAC_BPT4
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 382–408; 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 4mmq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4mmq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4mmq
Deposition date deposition_date2013-09-09
Structure title titleCrystal Structure of Prefusion-stabilized RSV F Variant DS
Keywords keywordsfusion, membrane, 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_guinier28.30
Radius of gyration Rg (electron density) rg_electron28.30
Forward intensity I(0) i032653200.00
Molecular weight molecular_weight43916.0 kDa
Excluded volume excluded_volume54798 ų
Envelope volume envelope_volume72606 ų
Hydration-shell volume shell_volume22659 ų
Envelope diameter envelope_diameter111.7
Shell Rg shell_rg33.39
Envelope Rg envelope_rg28.98
Shape Rg shape_rg28.27
Total Rg total_rg28.90
Total atoms total_atoms3065
Residues n_residues390
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 dmax107.8
Rg (real space) rg_real28.59
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real3.2650e+07
I(0) uncertainty (real space) i0_real_error4.9920e+05
Rg (reciprocal space) rg_reciprocal28.50
I(0) (reciprocal space) i0_reciprocal32650000.0000
Solution quality estimate total_estimate0.7736
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.478
Kurtosis Kurtosis kurtosis-0.372
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5218000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.576; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.369; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)