5xjk

NMR Structure and Localization of a Large Fragment of the SARS-CoV Fusion Protein: Implications in Viral Cell Fusion

Method: SOLUTION NMR Dmax: 77.8 Å Quality: REASONABLE

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

Spike protein S2

Human SARS coronavirus

UniProt P59594

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 758–821 Fragment:UNP RESIDUES 758-821 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 50;Pressure 1 NMR sample composition:0.2 M [U-13C; U-15N] Large Fragment of the SARS-CoV Fusion Protein, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

76 other PDB entries and 98 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_CVHSA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–65; UniProt 758–821

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 5xjk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5xjk
Deposition date deposition_date2017-05-02
Structure title titleNMR Structure and Localization of a Large Fragment of the SARS-CoV Fusion Protein: Implications in Viral Cell Fusion
Keywords keywordsVIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier29.91
Radius of gyration Rg (electron density) rg_electron29.62
Forward intensity I(0) i0279473000.00
Molecular weight molecular_weight150460.0 kDa
Excluded volume excluded_volume192800 ų
Envelope volume envelope_volume88519 ų
Hydration-shell volume shell_volume24938 ų
Envelope diameter envelope_diameter134.0
Shell Rg shell_rg35.23
Envelope Rg envelope_rg33.07
Shape Rg shape_rg29.58
Total Rg total_rg29.98
Total atoms total_atoms21460
Residues n_residues1300
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 dmax77.8
Rg (real space) rg_real27.96
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real2.6660e+08
I(0) uncertainty (real space) i0_real_error3.2420e+06
Rg (reciprocal space) rg_reciprocal30.18
I(0) (reciprocal space) i0_reciprocal279400000.0000
Solution quality estimate total_estimate0.6241
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.6
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.974
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha2.0610
Highest regularization parameter α highest_alpha273600.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 0.976; Sysdev: 0.000; Positv: 1.000; Valcen: 0.397; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)