2ruo

Solution Structure of Internal Fusion Peptide

Method: SOLUTION NMR Dmax: 29.3 Å Quality: REASONABLE

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

UNP residues 873-888 of Spike glycoprotein

OrganismNot specified

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 873–888 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 4.7;315 K NMR sample composition:0.5 mM Internal fusion peptide-1, 125 mM [U-99% 2H] DPC-2, 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 1–16; UniProt 873–888

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 2ruo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ruo
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2ruo
Deposition date deposition_date2014-11-06
Structure title titleSolution Structure of Internal Fusion Peptide
Keywords keywordsSARS-CoV, Internal fusion peptide, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier7.06
Radius of gyration Rg (electron density) rg_electron7.78
Forward intensity I(0) i016009900.00
Molecular weight molecular_weight35984.0 kDa
Excluded volume excluded_volume46059 ų
Envelope volume envelope_volume3748 ų
Hydration-shell volume shell_volume4319 ų
Envelope diameter envelope_diameter30.9
Shell Rg shell_rg12.71
Envelope Rg envelope_rg8.96
Shape Rg shape_rg7.76
Total Rg total_rg8.12
Total atoms total_atoms5040
Residues n_residues320
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 dmax29.3
Rg (real space) rg_real7.25
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.6010e+07
I(0) uncertainty (real space) i0_real_error1.7290e+05
Rg (reciprocal space) rg_reciprocal7.24
I(0) (reciprocal space) i0_reciprocal16010000.0000
Solution quality estimate total_estimate0.6552
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary5.9
Skewness Skewness skewness0.647
Kurtosis Kurtosis kurtosis-0.336
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha751.8000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.228; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.009; Smooth: 0.820

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)