4z9p

Crystal structure of Ebola virus nucleoprotein core domain at 1.8A resolution

Method: X-RAY DIFFRACTION Dmax: 74.5 Å Quality: GOOD

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

Nucleoprotein

Zaire ebolavirus (strain Mayinga-76)

UniProt P18272

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 36–351 Fragment:core domain (UNP RESIDUES 36-351) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7;289 K;200mM ammonium citrate tribasic pH 7.0, 20% (w/v) PEG 3350 Resolution 1.79 Å R-free 0.225

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.

13 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCAP_EBOZM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–317; UniProt 36–351

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 4z9p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4z9p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4z9p
Deposition date deposition_date2015-04-11
Structure title titleCrystal structure of Ebola virus nucleoprotein core domain at 1.8A resolution
Keywords keywordsEbola, Filoviridae, nucleoprotein, RNA binding protein, 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_guinier22.44
Radius of gyration Rg (electron density) rg_electron21.50
Forward intensity I(0) i017612800.00
Molecular weight molecular_weight32642.0 kDa
Excluded volume excluded_volume41330 ų
Envelope volume envelope_volume49588 ų
Hydration-shell volume shell_volume20203 ų
Envelope diameter envelope_diameter74.8
Shell Rg shell_rg27.27
Envelope Rg envelope_rg21.73
Shape Rg shape_rg21.47
Total Rg total_rg22.41
Total atoms total_atoms2301
Residues n_residues293
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 dmax74.5
Rg (real space) rg_real22.49
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real1.7610e+07
I(0) uncertainty (real space) i0_real_error2.2490e+05
Rg (reciprocal space) rg_reciprocal22.48
I(0) (reciprocal space) i0_reciprocal17610000.0000
Solution quality estimate total_estimate0.8776
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.449
Kurtosis Kurtosis kurtosis-0.178
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4920000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.943

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)