SAXSdb — 8y9j

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

Nucleoprotein

Zaire ebolavirus

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–RNA Heteromer Protein × 4 RNA 1 PDB declaration: pentameric（5） Consistent with all polymer counts	Chain A； UniProt 1–739 Chain B； UniProt 1–739	Not recorded	Membrane-associated protein VP24 × 2 （Q05322） RNA (12-MER) × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；The sample was applied to both sides of the grid. The grids were blotted for 14 seconds.	Resolution 4.60 Å

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.

Other PDB	Difference from Current Entry 8Y9J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4QAZ The crystal structure of the C-terminal domain of Ebola (Zaire) nucleoprotein Deposited 2014-05-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 641–739（99 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；19.3% PEG3350, 0.3M Magnesium Formate, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.98 Å R-free 0.229
4QB0 The crystal structure of the C-terminal domain of Ebola (Zaire) nucleoprotein Deposited 2014-05-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 641–739（99 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；19.3% PEG3350, 0.05M Magnesium Formate, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 1.75 Å R-free 0.225
4YPI Structure of Ebola virus nucleoprotein N-terminal fragment bound to a peptide derived from Ebola VP35 Deposited 2015-03-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 38–385（348 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；streak seeding in well solution containing 100 mM Tris pH 7.2, 50 mM Hepes pH 7, and 23% PEG400	Resolution 3.71 Å R-free 0.285
4YPI Structure of Ebola virus nucleoprotein N-terminal fragment bound to a peptide derived from Ebola VP35 Deposited 2015-03-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 38–385（348 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；streak seeding in well solution containing 100 mM Tris pH 7.2, 50 mM Hepes pH 7, and 23% PEG400	Resolution 3.71 Å R-free 0.285
4YPI Structure of Ebola virus nucleoprotein N-terminal fragment bound to a peptide derived from Ebola VP35 Deposited 2015-03-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 38–385（348 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；streak seeding in well solution containing 100 mM Tris pH 7.2, 50 mM Hepes pH 7, and 23% PEG400	Resolution 3.71 Å R-free 0.285
4YPI Structure of Ebola virus nucleoprotein N-terminal fragment bound to a peptide derived from Ebola VP35 Deposited 2015-03-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 38–385（348 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；streak seeding in well solution containing 100 mM Tris pH 7.2, 50 mM Hepes pH 7, and 23% PEG400	Resolution 3.71 Å R-free 0.285
4Z9P Crystal structure of Ebola virus nucleoprotein core domain at 1.8A resolution Deposited 2015-04-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 36–351（316 aa） Fragment：core domain (UNP RESIDUES 36-351)	Not recorded	No recorded non-water small molecule	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
4ZTA Ebola virus nucleoprotein bound to VP35 chaperoning peptide I212121 Deposited 2015-05-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 33–367（335 aa） Fragment：UNP Q05127 residues 15-59,UNP P18272 residues 33-367,UNP Q05127 residues 15-59,UNP P18272 residues 33-367	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.7；277 K；2.2M Sodium formate, 100mM NaOAc pH 4.7	Resolution 2.40 Å R-free 0.233
4ZTG Ebola virus nucleoprotein bound to VP35 chaperoning peptide P22121 Deposited 2015-05-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 33–367（335 aa） Fragment：UNP Q05127 residues 15-59, UNP P18272 residues 33-367	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；12% PEG 6000, 100 mM MES pH 5.0	Resolution 2.80 Å R-free 0.293
4ZTI Ebola virus nucleoprotein bound to VP35 chaperoning peptide P212121 Deposited 2015-05-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 33–367（335 aa） Fragment：UNP Q05127 residues 15-59,UNP P18272 residues 33-367	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.4；277 K；2.0 M sodium formate, 100 mM sodium acetate pH 4.4	Resolution 2.40 Å R-free 0.247
4ZTI Ebola virus nucleoprotein bound to VP35 chaperoning peptide P212121 Deposited 2015-05-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain B 33–367（335 aa） Fragment：UNP Q05127 residues 15-59,UNP P18272 residues 33-367	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.4；277 K；2.0 M sodium formate, 100 mM sodium acetate pH 4.4	Resolution 2.40 Å R-free 0.247
5T3T Ebola virus VP30 CTD bound to nucleoprotein Deposited 2016-08-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 600–627（28 aa） Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288 Chain B 600–627（28 aa） Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；298 K；0.3 uL of 20 mg/mL protein mixed with 0.3 uL of 2.2 M ammonium sulfate, 100 mM sodium acetate pH 4.9	Resolution 2.20 Å R-free 0.249
5T3T Ebola virus VP30 CTD bound to nucleoprotein Deposited 2016-08-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 600–627（28 aa） Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288 Chain D 600–627（28 aa） Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；298 K；0.3 uL of 20 mg/mL protein mixed with 0.3 uL of 2.2 M ammonium sulfate, 100 mM sodium acetate pH 4.9	Resolution 2.20 Å R-free 0.249
5T3T Ebola virus VP30 CTD bound to nucleoprotein Deposited 2016-08-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain E 600–627（28 aa） Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288 Chain F 600–627（28 aa） Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	Not recorded	SO4 SULFATE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；298 K；0.3 uL of 20 mg/mL protein mixed with 0.3 uL of 2.2 M ammonium sulfate, 100 mM sodium acetate pH 4.9	Resolution 2.20 Å R-free 0.249
5T3T Ebola virus VP30 CTD bound to nucleoprotein Deposited 2016-08-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain G 600–627（28 aa） Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288 Chain H 600–627（28 aa） Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	Not recorded	SO4 SULFATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；298 K；0.3 uL of 20 mg/mL protein mixed with 0.3 uL of 2.2 M ammonium sulfate, 100 mM sodium acetate pH 4.9	Resolution 2.20 Å R-free 0.249
5T3T Ebola virus VP30 CTD bound to nucleoprotein Deposited 2016-08-26	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain I 600–627（28 aa） Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288 Chain J 600–627（28 aa） Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	Not recorded	SO4 SULFATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.9；298 K；0.3 uL of 20 mg/mL protein mixed with 0.3 uL of 2.2 M ammonium sulfate, 100 mM sodium acetate pH 4.9	Resolution 2.20 Å R-free 0.249
6EHL Model of the Ebola virus nucleoprotein in recombinant nucleocapsid-like assemblies Deposited 2017-09-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–739（739 aa）	Mutation：Truncation mutant (residues 1-450)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.60 Å
6EHM Model of the Ebola virus nucleocapsid subunit from recombinant virus-like particles Deposited 2017-09-13	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–739（739 aa） Chain B 1–739（739 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.30 Å
6NUT Ebola virus nucleoprotein - RNA complex Deposited 2019-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Homooligomer；Protein × 50 PDB declaration: 100-meric	Chain A 1–450（450 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
6NUT Ebola virus nucleoprotein - RNA complex Deposited 2019-02-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 1–450（450 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8USN Intracellular cryo-tomography structure of EBOV nucleocapsid at 8.9 Angstrom Deposited 2023-10-27	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 7 PDB declaration: nonameric	Chain A 1–739（739 aa） Chain B 1–739（739 aa） Chain E 1–739（739 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 8.90 Å
8UST In-virion structure of Ebola virus nucleocapsid-like assemblies from recombinant virus-like particles (nucleoprotein, VP24,VP35,VP40) Deposited 2023-10-29	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 7 PDB declaration: nonameric	Chain A 1–739（739 aa） Chain B 1–739（739 aa） Chain E 1–739（739 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.30 Å

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 1–739； UniProt 1–739 Author chain B； PDBConstruct 1–739； UniProt 1–739

Membrane-associated protein VP24

Zaire ebolavirus

UniProt Q05322

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–RNA Heteromer Protein × 4 RNA 1 PDB declaration: pentameric（5） Consistent with all polymer counts	Chain C； UniProt 1–251 Chain D； UniProt 1–251	Not recorded	Nucleoprotein × 2 （P18272） RNA (12-MER) × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE；The sample was applied to both sides of the grid. The grids were blotted for 14 seconds.	Resolution 4.60 Å

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.

Other PDB	Difference from Current Entry 8Y9J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4M0Q Ebola virus VP24 structure Deposited 2013-08-01	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 11–237（227 aa） Fragment：UNP residues 11-231 Chain B 11–237（227 aa） Fragment：UNP residues 11-231	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.4；298 K；150 mM MES, pH 6.4, 20% Jeffamine M-600, pH 7.0, 50 mM cesium chloride, 6 mM barium chloride, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.92 Å R-free 0.232
4U2X Ebola virus VP24 in complex with Karyopherin alpha 5 C-terminus Deposited 2014-07-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 16–231（216 aa） Fragment：eVP24	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；3.5M ammonium chloride, 0.1 M Bis-Tris propane	Resolution 3.15 Å R-free 0.249
4U2X Ebola virus VP24 in complex with Karyopherin alpha 5 C-terminus Deposited 2014-07-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 16–231（216 aa） Fragment：eVP24	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；3.5M ammonium chloride, 0.1 M Bis-Tris propane	Resolution 3.15 Å R-free 0.249
4U2X Ebola virus VP24 in complex with Karyopherin alpha 5 C-terminus Deposited 2014-07-18	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 16–231（216 aa） Fragment：eVP24	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；3.5M ammonium chloride, 0.1 M Bis-Tris propane	Resolution 3.15 Å R-free 0.249
6EHM Model of the Ebola virus nucleocapsid subunit from recombinant virus-like particles Deposited 2017-09-13	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–251（251 aa） Chain D 1–251（251 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.30 Å
8USN Intracellular cryo-tomography structure of EBOV nucleocapsid at 8.9 Angstrom Deposited 2023-10-27	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 7 PDB declaration: nonameric	Chain I 1–251（251 aa） Chain J 1–251（251 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 8.90 Å
8UST In-virion structure of Ebola virus nucleocapsid-like assemblies from recombinant virus-like particles (nucleoprotein, VP24,VP35,VP40) Deposited 2023-10-29	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 7 PDB declaration: nonameric	Chain I 1–251（251 aa） Chain J 1–251（251 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.30 Å

5 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	VP24_EBOZM
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–251； UniProt 1–251 Author chain D； PDBConstruct 1–251； UniProt 1–251

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8y9j
Deposition date deposition_date	2024-02-06
Structure title title	Structure of the Ebola virus nucleocapsid subunit
Keywords keywords	Complex, VIRAL PROTEIN, VIRAL PROTEIN-RNA complex; VIRAL PROTEIN/RNA
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	36.30 Å
Radius of gyration Rg (electron density) rg_electron	35.79 Å
Forward intensity I(0) i0	295578000.00
Molecular weight molecular_weight	139020.0 kDa
Excluded volume excluded_volume	174510 Å³
Envelope volume envelope_volume	240440 Å³
Hydration-shell volume shell_volume	55436 Å³
Envelope diameter envelope_diameter	130.3 Å
Shell Rg shell_rg	42.43 Å
Envelope Rg envelope_rg	35.59 Å
Shape Rg shape_rg	35.79 Å
Total Rg total_rg	36.29 Å
Total atoms total_atoms	9770
Residues n_residues	1217
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	121.7 Å
Rg (real space) rg_real	36.20 Å
Rg uncertainty (real space) rg_real_error	0.81 Å
I(0) (real space) i0_real	2.9560e+08
I(0) uncertainty (real space) i0_real_error	4.8410e+06
Rg (reciprocal space) rg_reciprocal	36.26 Å
I(0) (reciprocal space) i0_reciprocal	295600000.0000
Solution quality estimate total_estimate	0.6696
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	47.0 Å
Skewness Skewness skewness	0.278
Kurtosis Kurtosis kurtosis	-0.252
Angular range angular_range	— – 0.2200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	82050000.0000
Real-space data points n_real_points	45
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 0.101; Positv: 1.000; Valcen: 1.000; Smooth: 0.910

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Nucleoprotein
Molecular weight formula_weight	83387.5 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	9770

MDSRPQKIWMAPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAFEAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEELLPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQARFSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLFPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAESRELDHLGLDDQEKKILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITAASLPKTSGHYDDDDDIPFPGPINDDDNPGHQDDDPTDSQDTTIPDVVVDPDDGSYGEYQSYSENGMNAPDDLVLFDLDEDDEDTKPVPNRSTKGGQQKNSQKGQHIEGRQTQSRPIQNVPGPHRTIHHASAPLTDNDRRNEPSGSTSPRMLTPINEEADPLDDADDETSSLPPLESDDEEQDRDGTSNRTPTVAPPAPVYRDHSEKKELPQDEQQDQDHTQEARNQDSDNTQSEHSFEEMYRHILRSQGPFDAVLYYHMMKDEPVVFSTSDGKEYTYPDSLEEEYPPWLTEKEAMNEENRFVTLDGQQFYWPVMNHKNKFMAILQHHQ

来源 Source

来源生物 organism	Zaire ebolavirus
NCBI Class编号 ncbi_taxonomy_id	186538
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Membrane-associated protein VP24
Molecular weight formula_weight	28250.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

MAKATGRYNLISPKKDLEKGVVLSDLCNFLVSQTIQGWKVYWAGIEFDVTHKGMALLHRLKTNDFAPAWSMTRNLFPHLFQNPNSTIESPLWALRVILAAGIQDQLIDQSLIEPLAGALGLISDWLLTTNTNHFNMRTQRVKEQLSLKMLSLIRSNILKFINKLDALHVVNYNGLLSSIEIGTQNHTIIITRTNMGFLVELQEPDKSAMNRMKPGPAKFSLLHESTLKAFTQGSSTRMQSLILEFNSSLAI

来源 Source

来源生物 organism	Zaire ebolavirus
NCBI Class编号 ncbi_taxonomy_id	186538
宿主生物 host_organism	Homo sapiens

Entity 3 Entity 3 polymer

Description description	RNA (12-MER)
Molecular weight formula_weight	3629.0 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polyribonucleotide
Chain IDs strand_id	K

UUUUUUUUUUUU

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	4.60 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	204348

fit	/app/data/saxs_computation/y9/8y9j/8y9j.fit
pddf	/app/data/pr_computation/y9/8y9j/8y9j.pr.out
profile	/app/data/saxs_computation/y9/8y9j/8y9j.dat

Structure of the Ebola virus nucleocapsid subunit

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

Nucleoprotein

State in the Current Structure

Other States of the Same Protein in the Database

Membrane-associated protein VP24

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)