SAXSdb — 1oke

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

MAJOR ENVELOPE PROTEIN E

DENGUE VIRUS TYPE 2

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 281–674 Chain B； UniProt 281–674	Fragment：SOLUBLE ECTODOMAIN, RESIDUES 281-674	;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 BOG octyl beta-D-glucopyranoside × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 8.5；11% PEG 8K, 1M NACL, 0.1M TRIS/HCL PH 9.0, 20% GLYCEROL,0.5% OCTYLGLUCOSIDE	Resolution 2.40 Å R-free 0.294

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 1OKE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1L9K dengue methyltransferase Deposited 2002-03-25	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 2492–2784（293 aa） Fragment：NS5 N-terminal domain	Mutation：V135I, K139R, N173S, P188S, R193K, T196A, Y201H	SO4 SULFATE ION × 5 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；291 K；sodium citrate 100mM, lithium sulfate 1.2 M, ammonium sulfate 0.5 M, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.40 Å R-free 0.257
1L9K dengue methyltransferase Deposited 2002-03-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2492–2784（293 aa） Fragment：NS5 N-terminal domain	Mutation：V135I, K139R, N173S, P188S, R193K, T196A, Y201H	SO4 SULFATE ION × 10 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；291 K；sodium citrate 100mM, lithium sulfate 1.2 M, ammonium sulfate 0.5 M, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.40 Å R-free 0.257
1OAN Crystal structure of the dengue 2 virus envelope protein Deposited 2003-01-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 281–674（394 aa） Fragment：SOLUBLE ECTODOMAIN, RESIDUES 281-674 Chain B 281–674（394 aa） Fragment：SOLUBLE ECTODOMAIN, RESIDUES 281-674	Not recorded	NA SODIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 8.5；11% PEG 8000, 1 M NACL, 0.1 M TRIS/HCL PH 9.0, 20% GLYCEROL	Resolution 2.75 Å R-free 0.296
1OK8 Crystal structure of the dengue 2 virus envelope glycoprotein in the postfusion conformation Deposited 2003-07-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 281–674（394 aa） Fragment：SOLUBLE ECTODOMAIN, RESIDUES 281-674	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；20-30% PEG 400, 0.08 M NACL, 0.1 M MOPS PH 7-8.	Resolution 2.00 Å R-free 0.267
1P58 Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction Deposited 2003-04-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 360 PDB declaration: 360-MERIC	Chain A 281–775（495 aa） Chain B 281–775（495 aa） Chain C 281–775（495 aa） Chain D 206–280（75 aa） Chain E 206–280（75 aa） Chain F 206–280（75 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM TRIS, 75 mM NaCl, 1 mM EDTA；pH 7.6；50 mM TRIS, 75 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE	Resolution 9.50 Å
1P58 Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction Deposited 2003-04-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 281–775（495 aa） Chain B 281–775（495 aa） Chain C 281–775（495 aa） Chain D 206–280（75 aa） Chain E 206–280（75 aa） Chain F 206–280（75 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM TRIS, 75 mM NaCl, 1 mM EDTA；pH 7.6；50 mM TRIS, 75 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE	Resolution 9.50 Å
1P58 Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction Deposited 2003-04-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 30 PDB declaration: 30-meric	Chain A 281–775（495 aa） Chain B 281–775（495 aa） Chain C 281–775（495 aa） Chain D 206–280（75 aa） Chain E 206–280（75 aa） Chain F 206–280（75 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM TRIS, 75 mM NaCl, 1 mM EDTA；pH 7.6；50 mM TRIS, 75 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE	Resolution 9.50 Å
1P58 Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction Deposited 2003-04-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 36 PDB declaration: 36-meric	Chain A 281–775（495 aa） Chain B 281–775（495 aa） Chain C 281–775（495 aa） Chain D 206–280（75 aa） Chain E 206–280（75 aa） Chain F 206–280（75 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM TRIS, 75 mM NaCl, 1 mM EDTA；pH 7.6；50 mM TRIS, 75 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE	Resolution 9.50 Å
1P58 Complex Organization of Dengue Virus Membrane Proteins as Revealed by 9.5 Angstrom Cryo-EM reconstruction Deposited 2003-04-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 281–775（495 aa） Chain B 281–775（495 aa） Chain C 281–775（495 aa） Chain D 206–280（75 aa） Chain E 206–280（75 aa） Chain F 206–280（75 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM TRIS, 75 mM NaCl, 1 mM EDTA；pH 7.6；50 mM TRIS, 75 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE	Resolution 9.50 Å
1R6A Structure of the dengue virus 2'O methyltransferase in complex with s-adenosyl homocysteine and ribavirin 5' triphosphate Deposited 2003-10-15	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 2492–2784（293 aa） Fragment：RNA-directed RNA polymerase (residue 2492-2784)	Not recorded	SO4 SULFATE ION × 7 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 RVP RIBAVIRIN MONOPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；Na Citrate 0.1 M, AS 0.5 M, LiSO4 1.2 M, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.60 Å R-free 0.243
1R6A Structure of the dengue virus 2'O methyltransferase in complex with s-adenosyl homocysteine and ribavirin 5' triphosphate Deposited 2003-10-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2492–2784（293 aa） Fragment：RNA-directed RNA polymerase (residue 2492-2784)	Not recorded	SO4 SULFATE ION × 14 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 RVP RIBAVIRIN MONOPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；Na Citrate 0.1 M, AS 0.5 M, LiSO4 1.2 M, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.60 Å R-free 0.243
1R6R Solution Structure of Dengue Virus Capsid Protein Reveals a New Fold Deposited 2003-10-16	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–100（100 aa） Fragment：capsid protein C (residue 1-100) Chain B 1–100（100 aa） Fragment：capsid protein C (residue 1-100)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) 50 mM sodium phosphate and 200 mM NaCl；Pressure 1 NMR measurement conditions pH 6；305 K；Ionic strength (raw mmCIF value) 50 mM sodium phosphate and 200 mM NaCl；Pressure 1 NMR sample composition 0.8 mM DEN2C protein U-15N, 13C; in 90% H2O/10% D2O with 50 mM sodium phosphate and 200 mM NaCl at pH 6.0. in SHIGEMI tube \| 90% H2O/10% D2O NMR sample composition 1mM or 2 mM DEN2C protein U-15N; in 90% H2O/10% D2O with 50 mM sodium phosphate and 200 mM NaCl at pH 6.0. in SHIGEMI tube \| 90% H2O/10% D2O	Resolution not provided
1THD COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION Deposited 2004-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 180 PDB declaration: 180-MERIC	Chain A 281–675（395 aa） Chain B 281–675（395 aa） Chain C 281–675（395 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM TRIS, 75 mM NACL, 1 mM EDTA；pH 7.6；50 mM TRIS, 75 mM NACL, 1 mM EDTA cryo-EM vitrification conditions SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE	Resolution 9.50 Å
1THD COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION Deposited 2004-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 281–675（395 aa） Chain B 281–675（395 aa） Chain C 281–675（395 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM TRIS, 75 mM NACL, 1 mM EDTA；pH 7.6；50 mM TRIS, 75 mM NACL, 1 mM EDTA cryo-EM vitrification conditions SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE	Resolution 9.50 Å
1THD COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION Deposited 2004-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 15 PDB declaration: pentadecameric	Chain A 281–675（395 aa） Chain B 281–675（395 aa） Chain C 281–675（395 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM TRIS, 75 mM NACL, 1 mM EDTA；pH 7.6；50 mM TRIS, 75 mM NACL, 1 mM EDTA cryo-EM vitrification conditions SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE	Resolution 9.50 Å
1THD COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION Deposited 2004-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 18 PDB declaration: octadecameric	Chain A 281–675（395 aa） Chain B 281–675（395 aa） Chain C 281–675（395 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM TRIS, 75 mM NACL, 1 mM EDTA；pH 7.6；50 mM TRIS, 75 mM NACL, 1 mM EDTA cryo-EM vitrification conditions SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE	Resolution 9.50 Å
1THD COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION Deposited 2004-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 281–675（395 aa） Chain B 281–675（395 aa） Chain C 281–675（395 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 50 mM TRIS, 75 mM NACL, 1 mM EDTA；pH 7.6；50 mM TRIS, 75 mM NACL, 1 mM EDTA cryo-EM vitrification conditions SAMPLES WERE PREPARED AS THIN LAYERS OF VITREOUS ICE AND MAINTAINED AT LIQUID NITROGEN TEMPERATURE IN THE ELECTRON MICROSCOPE	Resolution 9.50 Å
3J8D Cryoelectron microscopy of dengue-Fab E104 complex at pH 5.5 Deposited 2014-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 420 PDB declaration: 420-MERIC	Chain G 281–674（394 aa） Fragment：UNP residues 281-674 Chain H 281–674（394 aa） Fragment：UNP residues 281-674 Chain I 281–674（394 aa） Fragment：UNP residues 281-674	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 120 mM NaCl, 20 mM Tris HCl, 1 mM EDTA；pH 5.5；120 mM NaCl, 20 mM Tris HCl, 1 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE；Plunged into liquid ethane	Resolution 26.00 Å
3J8D Cryoelectron microscopy of dengue-Fab E104 complex at pH 5.5 Deposited 2014-10-13	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 × 7 PDB declaration: heptameric	Chain G 281–674（394 aa） Fragment：UNP residues 281-674 Chain H 281–674（394 aa） Fragment：UNP residues 281-674 Chain I 281–674（394 aa） Fragment：UNP residues 281-674	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 120 mM NaCl, 20 mM Tris HCl, 1 mM EDTA；pH 5.5；120 mM NaCl, 20 mM Tris HCl, 1 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE；Plunged into liquid ethane	Resolution 26.00 Å
3J8D Cryoelectron microscopy of dengue-Fab E104 complex at pH 5.5 Deposited 2014-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 35 PDB declaration: 35-meric	Chain G 281–674（394 aa） Fragment：UNP residues 281-674 Chain H 281–674（394 aa） Fragment：UNP residues 281-674 Chain I 281–674（394 aa） Fragment：UNP residues 281-674	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 120 mM NaCl, 20 mM Tris HCl, 1 mM EDTA；pH 5.5；120 mM NaCl, 20 mM Tris HCl, 1 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE；Plunged into liquid ethane	Resolution 26.00 Å
3J8D Cryoelectron microscopy of dengue-Fab E104 complex at pH 5.5 Deposited 2014-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 42 PDB declaration: 42-meric	Chain G 281–674（394 aa） Fragment：UNP residues 281-674 Chain H 281–674（394 aa） Fragment：UNP residues 281-674 Chain I 281–674（394 aa） Fragment：UNP residues 281-674	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 120 mM NaCl, 20 mM Tris HCl, 1 mM EDTA；pH 5.5；120 mM NaCl, 20 mM Tris HCl, 1 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE；Plunged into liquid ethane	Resolution 26.00 Å
3J8D Cryoelectron microscopy of dengue-Fab E104 complex at pH 5.5 Deposited 2014-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain G 281–674（394 aa） Fragment：UNP residues 281-674 Chain H 281–674（394 aa） Fragment：UNP residues 281-674 Chain I 281–674（394 aa） Fragment：UNP residues 281-674	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 120 mM NaCl, 20 mM Tris HCl, 1 mM EDTA；pH 5.5；120 mM NaCl, 20 mM Tris HCl, 1 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE；Plunged into liquid ethane	Resolution 26.00 Å
5HHG Mouse importin alpha: Dengue 2 NS5 C-terminal NLS peptide complex Deposited 2016-01-11	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 3353–3388（36 aa） Fragment：UNP residues 3353-3388	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；296 K；1.5M Ammonium Sulfate, 0.1M Sodium HEPES	Resolution 2.20 Å R-free 0.214

9 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	POLG_DEN2P
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–394； UniProt 281–674 Author chain B； PDBConstruct 1–394； UniProt 281–674

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	1oke
Deposition date deposition_date	2003-07-22
Structure title title	Crystal structure of the dengue 2 virus envelope protein in complex with n-octyl-beta-D-glucoside
Keywords keywords	VIRAL PROTEIN, MEMBRANE FUSION, FLAVIVIRUS, FUSION PEPTIDE, LOW-PH CONFORMATIONAL CHANGE, CLASS 2 FUSION 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	42.15 Å
Radius of gyration Rg (electron density) rg_electron	43.06 Å
Forward intensity I(0) i0	123835000.00
Molecular weight molecular_weight	89954.0 kDa
Excluded volume excluded_volume	112630 Å³
Envelope volume envelope_volume	153760 Å³
Hydration-shell volume shell_volume	34135 Å³
Envelope diameter envelope_diameter	154.1 Å
Shell Rg shell_rg	40.28 Å
Envelope Rg envelope_rg	42.93 Å
Shape Rg shape_rg	43.06 Å
Total Rg total_rg	42.88 Å
Total atoms total_atoms	6290
Residues n_residues	788
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	144.5 Å
Rg (real space) rg_real	42.81 Å
Rg uncertainty (real space) rg_real_error	1.89 Å
I(0) (real space) i0_real	1.2380e+08
I(0) uncertainty (real space) i0_real_error	2.3720e+06
Rg (reciprocal space) rg_reciprocal	42.15 Å
I(0) (reciprocal space) i0_reciprocal	123700000.0000
Solution quality estimate total_estimate	0.7331
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	31.2 Å
Skewness Skewness skewness	0.628
Kurtosis Kurtosis kurtosis	-0.360
Angular range angular_range	— – 0.1850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7488000.0000
Real-space data points n_real_points	38
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.602; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.453; Smooth: 0.267

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	MAJOR ENVELOPE PROTEIN E
Molecular weight formula_weight	43819.4 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	6426

MRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPTLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFTCKKNMEGKIVQPENLEYTVVITPHSGEEHAVGNDTGKHGKEVKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQMKDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKK

来源 Source

来源生物 organism	DENGUE VIRUS TYPE 2
NCBI Class编号 ncbi_taxonomy_id	11060
宿主生物 host_organism	DROSOPHILA MELANOGASTER

Entity 2 Entity 2 branched

Description description	;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	732.7 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	octyl beta-D-glucopyranoside
Molecular weight formula_weight	292.4 kDa
Source method src_method	man
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	136

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1okea1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.18 — E set domains
Family Family family	b.1.18.4 — Class II viral fusion proteins C-terminal domain

Domain ID domain_id	d1okea2
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.10 — Viral glycoprotein, central and dimerisation domains
Superfamily Superfamily superfamily	f.10.1 — Viral glycoprotein, central and dimerisation domains
Family Family family	f.10.1.1 — Viral glycoprotein, central and dimerisation domains

Domain ID domain_id	d1okeb1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.18 — E set domains
Family Family family	b.1.18.4 — Class II viral fusion proteins C-terminal domain

Domain ID domain_id	d1okeb2
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.10 — Viral glycoprotein, central and dimerisation domains
Superfamily Superfamily superfamily	f.10.1 — Viral glycoprotein, central and dimerisation domains
Family Family family	f.10.1.1 — Viral glycoprotein, central and dimerisation domains

CATH v4.4 (8 domains)

Domain ID domain_id	1okeA01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	98 — Tick-borne Encephalitis virus Glycoprotein; domain 1
Homologous superfamily homologous superfamily	10 — Tick-borne Encephalitis virus Glycoprotein, domain 1

Domain ID domain_id	1okeA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	67 — Viral Envelope Glycoprotein; domain 2
Homologous superfamily homologous superfamily	10 — Viral Envelope Glycoprotein, domain 2

Domain ID domain_id	1okeA03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	387 — Viral Envelope Glycoprotein; domain 3
Homologous superfamily homologous superfamily	10 — Viral Envelope Glycoprotein, domain 3

Domain ID domain_id	1okeA04
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	350 —

Domain ID domain_id	1okeB01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	98 — Tick-borne Encephalitis virus Glycoprotein; domain 1
Homologous superfamily homologous superfamily	10 — Tick-borne Encephalitis virus Glycoprotein, domain 1

Domain ID domain_id	1okeB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	67 — Viral Envelope Glycoprotein; domain 2
Homologous superfamily homologous superfamily	10 — Viral Envelope Glycoprotein, domain 2

Domain ID domain_id	1okeB03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	387 — Viral Envelope Glycoprotein; domain 3
Homologous superfamily homologous superfamily	10 — Viral Envelope Glycoprotein, domain 3

Domain ID domain_id	1okeB04
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	350 —

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8. Citations (2)

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Unit-cell length a length_a	81.602 Å
Unit-cell length b length_b	81.602 Å
Unit-cell length c length_c	287.408 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 31 2 1
Space-group number int_tables_number	152
Crystal system crystal_system	—

Resolution resolution	2.400 Å
Low-resolution limit resolution_low	45.000 Å
R factor r_factor	0.2630
R_work r_work	0.2630
R_free r_free	0.2940

fit	/app/data/saxs_computation/ok/1oke/1oke.fit
pddf	/app/data/pr_computation/ok/1oke/1oke.pr.out
profile	/app/data/saxs_computation/ok/1oke/1oke.dat

Crystal structure of the dengue 2 virus envelope protein in complex with n-octyl-beta-D-glucoside