2run

Solution Structure of Pre Transmembrane domain

Method: SOLUTION NMR Dmax: 32.5 Å Quality: REASONABLE

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

Pre-transmembrane domain 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 1185–1202 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 4.7;315 K NMR sample composition:0.5 mM Pre transmembrane domain-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 1–18; UniProt 1185–1202

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 2run

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2run
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2run
Deposition date deposition_date2014-11-06
Structure title titleSolution Structure of Pre Transmembrane domain
Keywords keywordsSARS-CoV, Pre transmembrane domain, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier7.27
Radius of gyration Rg (electron density) rg_electron8.73
Forward intensity I(0) i019338500.00
Molecular weight molecular_weight47216.0 kDa
Excluded volume excluded_volume62774 ų
Envelope volume envelope_volume4676 ų
Hydration-shell volume shell_volume4841 ų
Envelope diameter envelope_diameter33.5
Shell Rg shell_rg13.67
Envelope Rg envelope_rg10.09
Shape Rg shape_rg8.68
Total Rg total_rg9.19
Total atoms total_atoms6640
Residues n_residues360
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 dmax32.5
Rg (real space) rg_real7.37
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real1.9340e+07
I(0) uncertainty (real space) i0_real_error2.0670e+05
Rg (reciprocal space) rg_reciprocal7.37
I(0) (reciprocal space) i0_reciprocal19340000.0000
Solution quality estimate total_estimate0.6571
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary6.2
Skewness Skewness skewness0.337
Kurtosis Kurtosis kurtosis-1.237
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1060.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.234; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.008; Smooth: 0.828

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)