2og3

structure of the rna binding domain of n protein from SARS coronavirus in cubic crystal form

Method: X-RAY DIFFRACTION Dmax: 47.5 Å Quality: GOOD

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

Nucleocapsid protein

SARS coronavirus Tor2

UniProt P59595

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 49–174 Fragment:rna binding domain of N protein No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8;277 K;40% MPD and 0.1 M Tris pH 8.0, typically crystals appear within 2 weeks, VAPOR DIFFUSION, temperature 277K Resolution 1.85 Å R-free 0.247

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.

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCAP_CVHSA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 13–93; UniProt 49–174

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 2og3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2og3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2og3
Deposition date deposition_date2007-01-05
Structure title titlestructure of the rna binding domain of n protein from SARS coronavirus in cubic crystal form
Keywords keywordsn protein, nucleocapsid, rna binding domain, sars coronavirus, 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_guinier14.71
Radius of gyration Rg (electron density) rg_electron13.24
Forward intensity I(0) i03122250.00
Molecular weight molecular_weight12281.0 kDa
Excluded volume excluded_volume15352 ų
Envelope volume envelope_volume17516 ų
Hydration-shell volume shell_volume11287 ų
Envelope diameter envelope_diameter46.2
Shell Rg shell_rg18.86
Envelope Rg envelope_rg13.65
Shape Rg shape_rg13.19
Total Rg total_rg14.64
Total atoms total_atoms873
Residues n_residues112
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 dmax47.5
Rg (real space) rg_real14.61
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real3.1220e+06
I(0) uncertainty (real space) i0_real_error3.5330e+04
Rg (reciprocal space) rg_reciprocal14.61
I(0) (reciprocal space) i0_reciprocal3122000.0000
Solution quality estimate total_estimate0.8849
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.2
Skewness Skewness skewness0.100
Kurtosis Kurtosis kurtosis-0.396
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha708700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.977

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)