SAXSdb — 5t3t

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

Fusion protein of Nucleoprotein and Minor nucleoprotein VP30

Zaire ebolavirus (strain Mayinga-76)

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 600–627 Chain B； UniProt 600–627	Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	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
2	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 600–627 Chain D； UniProt 600–627	Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	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
3	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 600–627 Chain F； UniProt 600–627	Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	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
4	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 600–627 Chain H； UniProt 600–627	Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	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
5	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain I； UniProt 600–627 Chain J； UniProt 600–627	Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	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

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 5T3T	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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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
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 ligand/ion Different experimental method 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 construct Different oligomeric state Different ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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
8Y9J Structure of the Ebola virus nucleocapsid subunit Deposited 2024-02-06	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 4 PDB declaration: pentameric	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 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

13 other PDB entries and 18 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 16–43； UniProt 600–627 Author chain B； PDBConstruct 16–43； UniProt 600–627 Author chain C； PDBConstruct 16–43； UniProt 600–627 Author chain D； PDBConstruct 16–43； UniProt 600–627 Author chain E； PDBConstruct 16–43； UniProt 600–627 Author chain F； PDBConstruct 16–43； UniProt 600–627 Author chain G； PDBConstruct 16–43； UniProt 600–627 Author chain H； PDBConstruct 16–43； UniProt 600–627 Author chain I； PDBConstruct 16–43； UniProt 600–627 Author chain J； PDBConstruct 16–43； UniProt 600–627

Fusion protein of Nucleoprotein and Minor nucleoprotein VP30

Zaire ebolavirus (strain Mayinga-76)

UniProt Q05323

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 139–288 Chain B； UniProt 139–288	Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	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
2	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 139–288 Chain D； UniProt 139–288	Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	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
3	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 139–288 Chain F； UniProt 139–288	Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	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
4	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 139–288 Chain H； UniProt 139–288	Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	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
5	Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain I； UniProt 139–288 Chain J； UniProt 139–288	Fragment：UNP P18272 residues 600-627,UNP Q05323 residues 139-288	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

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 5T3T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2I8B Crystal structure of the C-terminal domain of Ebola virus VP30 Deposited 2006-09-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 142–272（131 aa） Fragment：C-terminal domain, residues 142-272 Chain B 142–272（131 aa） Fragment：C-terminal domain, residues 142-272	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；0.1M ammonium acetate, 15mM magnesium acetate tetrahydrate, 0.05M sodium cacodylate, 10%(v/v) isopropanol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.00 Å R-free 0.241
5DVW Structure of minor nucleoprotein V30 from Zaire ebolavirus Deposited 2015-09-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 142–272（131 aa） Fragment：UNP residues 142-272 Chain B 142–272（131 aa） Fragment：UNP residues 142-272	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；290 K；Molecular Dimensions Morpheus screen e12: 40mM each Di-Ethyleneglycol, Tri-Ethyleneglycol, TetraEthyleneglycol, Penta-Ethyleneglycol; 12.% each MPD, PEG 1000; PEG 3350; 100mM Tris(base)/Bicine pH 8.5; EbzaA.17250.a.EW11.PD00370 at 22 mg/ml, tray 262514e12, puck otj5-3; cryo: direct	Resolution 1.75 Å R-free 0.208
5DVW Structure of minor nucleoprotein V30 from Zaire ebolavirus Deposited 2015-09-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 142–272（131 aa） Fragment：UNP residues 142-272 Chain D 142–272（131 aa） Fragment：UNP residues 142-272	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；290 K；Molecular Dimensions Morpheus screen e12: 40mM each Di-Ethyleneglycol, Tri-Ethyleneglycol, TetraEthyleneglycol, Penta-Ethyleneglycol; 12.% each MPD, PEG 1000; PEG 3350; 100mM Tris(base)/Bicine pH 8.5; EbzaA.17250.a.EW11.PD00370 at 22 mg/ml, tray 262514e12, puck otj5-3; cryo: direct	Resolution 1.75 Å R-free 0.208

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	VP30_EBOZM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 44–193； UniProt 139–288 Author chain B； PDBConstruct 44–193； UniProt 139–288 Author chain C； PDBConstruct 44–193； UniProt 139–288 Author chain D； PDBConstruct 44–193； UniProt 139–288 Author chain E； PDBConstruct 44–193； UniProt 139–288 Author chain F； PDBConstruct 44–193； UniProt 139–288 Author chain G； PDBConstruct 44–193； UniProt 139–288 Author chain H； PDBConstruct 44–193； UniProt 139–288 Author chain I； PDBConstruct 44–193； UniProt 139–288 Author chain J； PDBConstruct 44–193； UniProt 139–288

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	5t3t
Deposition date deposition_date	2016-08-26
Structure title title	Ebola virus VP30 CTD bound to nucleoprotein
Keywords keywords	transcription, replication, regulator, co-factor, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	42.07 Å
Radius of gyration Rg (electron density) rg_electron	41.62 Å
Forward intensity I(0) i0	361428000.00
Molecular weight molecular_weight	156250.0 kDa
Excluded volume excluded_volume	196280 Å³
Envelope volume envelope_volume	264480 Å³
Hydration-shell volume shell_volume	53625 Å³
Envelope diameter envelope_diameter	140.3 Å
Shell Rg shell_rg	46.27 Å
Envelope Rg envelope_rg	40.71 Å
Shape Rg shape_rg	41.63 Å
Total Rg total_rg	41.80 Å
Total atoms total_atoms	10940
Residues n_residues	1363
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	136.4 Å
Rg (real space) rg_real	42.06 Å
Rg uncertainty (real space) rg_real_error	1.11 Å
I(0) (real space) i0_real	3.6140e+08
I(0) uncertainty (real space) i0_real_error	6.6820e+06
Rg (reciprocal space) rg_reciprocal	42.07 Å
I(0) (reciprocal space) i0_reciprocal	361400000.0000
Solution quality estimate total_estimate	0.8262
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	50.2 Å
Skewness Skewness skewness	0.278
Kurtosis Kurtosis kurtosis	-0.485
Angular range angular_range	— – 0.1900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	23750000.0000
Real-space data points n_real_points	39
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

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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	Fusion protein of Nucleoprotein and Minor nucleoprotein VP30
Molecular weight formula_weight	21829.6 kDa
Source method src_method	man
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J
Atom count atom_count	11795

MAHHHHHHVDDDDKMRTPTVAPPAPVYRDHSEKKELPQDEQQDGPKITLLTLIKTAEHWARQDIRTIEDSKLRALLTLCAVMTRKFSKSQLSLLCETHLRREGLGQDQAEPVLEVYQRLHSDKGGSFEAALWQQWDRQSLIMFITAFLNIALQLPCESSAVVVSGLRTLVPQSDNEEASTNPGTCSWSDEGTP

来源 Source

来源生物 organism	Zaire ebolavirus (strain Mayinga-76)
通用名 common_name	ZEBOV
NCBI Class编号 ncbi_taxonomy_id	128952
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	27

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	855

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7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id	5t3tA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1160 —

Domain ID domain_id	5t3tB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1160 —

Domain ID domain_id	5t3tC00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1160 —

Domain ID domain_id	5t3tD00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1160 —

Domain ID domain_id	5t3tE00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1160 —

Domain ID domain_id	5t3tF00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1160 —

Domain ID domain_id	5t3tG00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1160 —

Domain ID domain_id	5t3tH00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1160 —

Domain ID domain_id	5t3tI00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1160 —

Domain ID domain_id	5t3tJ00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	1160 —

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8. Citations (1)

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Unit-cell length a length_a	85.875 Å
Unit-cell length b length_b	116.784 Å
Unit-cell length c length_c	95.038 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	108.52 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	20

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	90.120 Å
R factor r_factor	0.2159
R_work r_work	0.2142
R_free r_free	0.2492

fit	/app/data/saxs_computation/t3/5t3t/5t3t.fit
pddf	/app/data/pr_computation/t3/5t3t/5t3t.pr.out
profile	/app/data/saxs_computation/t3/5t3t/5t3t.dat

Ebola virus VP30 CTD bound to nucleoprotein

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

Fusion protein of Nucleoprotein and Minor nucleoprotein VP30

State in the Current Structure

Other States of the Same Protein in the Database

Fusion protein of Nucleoprotein and Minor nucleoprotein VP30

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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)