SAXSdb — 3j42

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

Envelope protein E

OrganismNot specified

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 Heteromer Protein × 720 PDB declaration: 720-meric（720） Consistent with protein copy count	Chain A； UniProt 281–675 Chain B； UniProt 281–675 Chain C； UniProt 281–675	Fragment：UNP residues 281-675	PrM × 180 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 180 （P01783,Q6PIP8） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 180 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
2	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain A； UniProt 281–675 Chain B； UniProt 281–675 Chain C； UniProt 281–675	Fragment：UNP residues 281-675	PrM × 3 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 3 （P01783,Q6PIP8） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 3 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3	Insufficient information Heteromer Protein × 60 PDB declaration: 60-meric（60） Consistent with protein copy count	Chain A； UniProt 281–675 Chain B； UniProt 281–675 Chain C； UniProt 281–675	Fragment：UNP residues 281-675	PrM × 15 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 15 （P01783,Q6PIP8） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 15 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
4	Insufficient information Heteromer Protein × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain A； UniProt 281–675 Chain B； UniProt 281–675 Chain C； UniProt 281–675	Fragment：UNP residues 281-675	PrM × 18 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 18 （P01783,Q6PIP8） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 18 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
5	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain A； UniProt 281–675 Chain B； UniProt 281–675 Chain C； UniProt 281–675	Fragment：UNP residues 281-675	PrM × 3 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 3 （P01783,Q6PIP8） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 3 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 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 3J42	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3C6D The pseudo-atomic structure of dengue immature virus Deposited 2008-02-04	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 360 PDB declaration: 360-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 pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE	Resolution 12.50 Å
3C6D The pseudo-atomic structure of dengue immature virus Deposited 2008-02-04	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	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 pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE	Resolution 12.50 Å
3C6D The pseudo-atomic structure of dengue immature virus Deposited 2008-02-04	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-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 pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE	Resolution 12.50 Å
3C6D The pseudo-atomic structure of dengue immature virus Deposited 2008-02-04	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 36 PDB declaration: 36-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 pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE	Resolution 12.50 Å
3C6D The pseudo-atomic structure of dengue immature virus Deposited 2008-02-04	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	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 pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions Cryogen ETHANE	Resolution 12.50 Å
3IXY The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53 Deposited 2009-02-26	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 600 PDB declaration: 600-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 pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions A small vial of ethane is placed inside a larger liquid nitrogen reservoir. The grid holding a few microliters of the sample is held in place at the bottom of a plunger by the means of fine tweezers. Once the ethane in the vial is completely frozen, it needs to be slightly melted. When the liquid ethane is ready, a piece of filter paper is then pressed against the sample to blot of excess buffer, sufficient to leave a thin layer on the grid. After a predetermined time, the filter paper is removed, and the plunger is allowed to drop into the liquid ethane. Once the grid enters the liquid ethane, the sample is rapidly frozen, and the grid is transferred under liquid nitrogen to a storage box immersed liquid nitrogen for later use in the microscope.；Cryogen ETHANE	Resolution 23.00 Å
3IXY The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53 Deposited 2009-02-26	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	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 pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions A small vial of ethane is placed inside a larger liquid nitrogen reservoir. The grid holding a few microliters of the sample is held in place at the bottom of a plunger by the means of fine tweezers. Once the ethane in the vial is completely frozen, it needs to be slightly melted. When the liquid ethane is ready, a piece of filter paper is then pressed against the sample to blot of excess buffer, sufficient to leave a thin layer on the grid. After a predetermined time, the filter paper is removed, and the plunger is allowed to drop into the liquid ethane. Once the grid enters the liquid ethane, the sample is rapidly frozen, and the grid is transferred under liquid nitrogen to a storage box immersed liquid nitrogen for later use in the microscope.；Cryogen ETHANE	Resolution 23.00 Å
3IXY The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53 Deposited 2009-02-26	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 50 PDB declaration: 50-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 pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions A small vial of ethane is placed inside a larger liquid nitrogen reservoir. The grid holding a few microliters of the sample is held in place at the bottom of a plunger by the means of fine tweezers. Once the ethane in the vial is completely frozen, it needs to be slightly melted. When the liquid ethane is ready, a piece of filter paper is then pressed against the sample to blot of excess buffer, sufficient to leave a thin layer on the grid. After a predetermined time, the filter paper is removed, and the plunger is allowed to drop into the liquid ethane. Once the grid enters the liquid ethane, the sample is rapidly frozen, and the grid is transferred under liquid nitrogen to a storage box immersed liquid nitrogen for later use in the microscope.；Cryogen ETHANE	Resolution 23.00 Å
3IXY The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53 Deposited 2009-02-26	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 60 PDB declaration: 60-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 pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions A small vial of ethane is placed inside a larger liquid nitrogen reservoir. The grid holding a few microliters of the sample is held in place at the bottom of a plunger by the means of fine tweezers. Once the ethane in the vial is completely frozen, it needs to be slightly melted. When the liquid ethane is ready, a piece of filter paper is then pressed against the sample to blot of excess buffer, sufficient to leave a thin layer on the grid. After a predetermined time, the filter paper is removed, and the plunger is allowed to drop into the liquid ethane. Once the grid enters the liquid ethane, the sample is rapidly frozen, and the grid is transferred under liquid nitrogen to a storage box immersed liquid nitrogen for later use in the microscope.；Cryogen ETHANE	Resolution 23.00 Å
3IXY The pseudo-atomic structure of dengue immature virus in complex with Fab fragments of the anti-fusion loop antibody E53 Deposited 2009-02-26	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	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 pH 7.6；12 mM Tris-HCl, 120 mM NaCl, 1 mM EDTA cryo-EM vitrification conditions A small vial of ethane is placed inside a larger liquid nitrogen reservoir. The grid holding a few microliters of the sample is held in place at the bottom of a plunger by the means of fine tweezers. Once the ethane in the vial is completely frozen, it needs to be slightly melted. When the liquid ethane is ready, a piece of filter paper is then pressed against the sample to blot of excess buffer, sufficient to leave a thin layer on the grid. After a predetermined time, the filter paper is removed, and the plunger is allowed to drop into the liquid ethane. Once the grid enters the liquid ethane, the sample is rapidly frozen, and the grid is transferred under liquid nitrogen to a storage box immersed liquid nitrogen for later use in the microscope.；Cryogen ETHANE	Resolution 23.00 Å
6ZQU Cryo-EM structure of mature Dengue virus 2 at 3.1 angstrom resolution Deposited 2020-07-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 360 PDB declaration: 360-meric	Chain B 206–280（75 aa） Chain D 206–280（75 aa） Chain F 206–280（75 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 360	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；PBS buffer cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.10 Å

3 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	O11875_9FLAV
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–390； UniProt 281–675 Author chain B； PDBConstruct 1–390； UniProt 281–675 Author chain C； PDBConstruct 1–390； UniProt 281–675

PrM

OrganismNot specified

UniProt Q3BCY5

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 Heteromer Protein × 720 PDB declaration: 720-meric（720） Consistent with protein copy count	Chain D； UniProt 1–81 Chain E； UniProt 1–81 Chain F； UniProt 1–81	Fragment：UNP residues 1-81	Envelope protein E × 180 （O11875） Ig heavy chain V region MOPC 21, Igh protein chimera × 180 （P01783,Q6PIP8） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 180 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
2	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain D； UniProt 1–81 Chain E； UniProt 1–81 Chain F； UniProt 1–81	Fragment：UNP residues 1-81	Envelope protein E × 3 （O11875） Ig heavy chain V region MOPC 21, Igh protein chimera × 3 （P01783,Q6PIP8） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 3 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3	Insufficient information Heteromer Protein × 60 PDB declaration: 60-meric（60） Consistent with protein copy count	Chain D； UniProt 1–81 Chain E； UniProt 1–81 Chain F； UniProt 1–81	Fragment：UNP residues 1-81	Envelope protein E × 15 （O11875） Ig heavy chain V region MOPC 21, Igh protein chimera × 15 （P01783,Q6PIP8） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 15 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
4	Insufficient information Heteromer Protein × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain D； UniProt 1–81 Chain E； UniProt 1–81 Chain F； UniProt 1–81	Fragment：UNP residues 1-81	Envelope protein E × 18 （O11875） Ig heavy chain V region MOPC 21, Igh protein chimera × 18 （P01783,Q6PIP8） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 18 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
5	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain D； UniProt 1–81 Chain E； UniProt 1–81 Chain F； UniProt 1–81	Fragment：UNP residues 1-81	Envelope protein E × 3 （O11875） Ig heavy chain V region MOPC 21, Igh protein chimera × 3 （P01783,Q6PIP8） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 3 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	Q3BCY5_9FLAV
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–81； UniProt 1–81 Author chain E； PDBConstruct 1–81； UniProt 1–81 Author chain F； PDBConstruct 1–81； UniProt 1–81

Ig heavy chain V region MOPC 21, Igh protein chimera

Mus musculus

UniProt P01783

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 Heteromer Protein × 720 PDB declaration: 720-meric（720） Consistent with protein copy count	Chain G； UniProt 17–119 Chain I； UniProt 17–119 Chain K； UniProt 17–119	Fragment：SEE REMARK 999	Envelope protein E × 180 （O11875） PrM × 180 （Q3BCY5） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 180 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
2	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain G； UniProt 17–119 Chain I； UniProt 17–119 Chain K； UniProt 17–119	Fragment：SEE REMARK 999	Envelope protein E × 3 （O11875） PrM × 3 （Q3BCY5） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 3 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3	Insufficient information Heteromer Protein × 60 PDB declaration: 60-meric（60） Consistent with protein copy count	Chain G； UniProt 17–119 Chain I； UniProt 17–119 Chain K； UniProt 17–119	Fragment：SEE REMARK 999	Envelope protein E × 15 （O11875） PrM × 15 （Q3BCY5） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 15 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
4	Insufficient information Heteromer Protein × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain G； UniProt 17–119 Chain I； UniProt 17–119 Chain K； UniProt 17–119	Fragment：SEE REMARK 999	Envelope protein E × 18 （O11875） PrM × 18 （Q3BCY5） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 18 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
5	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain G； UniProt 17–119 Chain I； UniProt 17–119 Chain K； UniProt 17–119	Fragment：SEE REMARK 999	Envelope protein E × 3 （O11875） PrM × 3 （Q3BCY5） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 3 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 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 3J42	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1IGC IGG1 FAB FRAGMENT (MOPC21) COMPLEX WITH DOMAIN III OF PROTEIN G FROM STREPTOCOCCUS Deposited 1994-08-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 17–136（120 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
4KVC 2H2 Fab fragment of immature Dengue virus Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 17–119（103 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；25% PEG 6000 0.1 M MES 0.2M NH4Cl, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.31 Å R-free 0.234

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

View Construct and Data Evidence

UniProt name	HVM16_MOUSE
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain G； PDBConstruct 1–103； UniProt 17–119 Author chain I； PDBConstruct 1–103； UniProt 17–119 Author chain K； PDBConstruct 1–103； UniProt 17–119

Ig heavy chain V region MOPC 21, Igh protein chimera

Mus musculus

UniProt Q6PIP8

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 Heteromer Protein × 720 PDB declaration: 720-meric（720） Consistent with protein copy count	Chain G； UniProt 120–230 Chain I； UniProt 120–230 Chain K； UniProt 120–230	Fragment：SEE REMARK 999	Envelope protein E × 180 （O11875） PrM × 180 （Q3BCY5） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 180 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
2	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain G； UniProt 120–230 Chain I； UniProt 120–230 Chain K； UniProt 120–230	Fragment：SEE REMARK 999	Envelope protein E × 3 （O11875） PrM × 3 （Q3BCY5） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 3 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3	Insufficient information Heteromer Protein × 60 PDB declaration: 60-meric（60） Consistent with protein copy count	Chain G； UniProt 120–230 Chain I； UniProt 120–230 Chain K； UniProt 120–230	Fragment：SEE REMARK 999	Envelope protein E × 15 （O11875） PrM × 15 （Q3BCY5） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 15 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
4	Insufficient information Heteromer Protein × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain G； UniProt 120–230 Chain I； UniProt 120–230 Chain K； UniProt 120–230	Fragment：SEE REMARK 999	Envelope protein E × 18 （O11875） PrM × 18 （Q3BCY5） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 18 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
5	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain G； UniProt 120–230 Chain I； UniProt 120–230 Chain K； UniProt 120–230	Fragment：SEE REMARK 999	Envelope protein E × 3 （O11875） PrM × 3 （Q3BCY5） Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera × 3 （P01634,Q7TS98）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 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 3J42	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	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 H 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 7 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 10 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain H 21–234（214 aa） Chain J 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 12 GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 11 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain J 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 12 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 12 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain H 21–234（214 aa） Chain I 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 15 GOL GLYCEROL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	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 I 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 8 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	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 × 2 PDB declaration: dimeric	Chain J 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 5 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	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 × 2 PDB declaration: dimeric	Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	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 × 8 PDB declaration: octameric	Chain H 21–234（214 aa） Chain I 21–234（214 aa） Chain J 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 27 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain H 21–234（214 aa） Chain I 21–234（214 aa） Chain J 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 27 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 7 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain H 21–234（214 aa） Chain I 21–234（214 aa） Chain J 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 27 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 8 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain H 21–234（214 aa） Chain I 21–234（214 aa） Chain J 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 27 GOL GLYCEROL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2AI0 Anti-Cocaine Antibody 7.5.21, Crystal Form III Deposited 2005-07-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 9 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain I 21–234（214 aa） Chain K 21–234（214 aa）	Not recorded	SO4 SULFATE ION × 15 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；16% PEG8000, 0.3M ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.279
2IPT PFA1 Fab Fragment Deposited 2006-10-12	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 H 123–234（112 aa）	Not recorded	ACM ACETAMIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；294 K；0.1 M Hepes, 25% PEG3350, pH 7.5, VAPOR DIFFUSION, temperature 294K	Resolution 2.00 Å R-free 0.223
4KVC 2H2 Fab fragment of immature Dengue virus Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 120–230（111 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；25% PEG 6000 0.1 M MES 0.2M NH4Cl, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.31 Å R-free 0.234

3 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q6PIP8_MOUSE
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain G； PDBConstruct 106–216； UniProt 120–230 Author chain I； PDBConstruct 106–216； UniProt 120–230 Author chain K； PDBConstruct 106–216； UniProt 120–230

Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera

Mus musculus

UniProt P01634

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 Heteromer Protein × 720 PDB declaration: 720-meric（720） Consistent with protein copy count	Chain H； UniProt 30–136 Chain J； UniProt 30–136 Chain L； UniProt 30–136	Fragment：SEE REMARK 999	Envelope protein E × 180 （O11875） PrM × 180 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 180 （P01783,Q6PIP8）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
2	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain H； UniProt 30–136 Chain J； UniProt 30–136 Chain L； UniProt 30–136	Fragment：SEE REMARK 999	Envelope protein E × 3 （O11875） PrM × 3 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 3 （P01783,Q6PIP8）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3	Insufficient information Heteromer Protein × 60 PDB declaration: 60-meric（60） Consistent with protein copy count	Chain H； UniProt 30–136 Chain J； UniProt 30–136 Chain L； UniProt 30–136	Fragment：SEE REMARK 999	Envelope protein E × 15 （O11875） PrM × 15 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 15 （P01783,Q6PIP8）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
4	Insufficient information Heteromer Protein × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain H； UniProt 30–136 Chain J； UniProt 30–136 Chain L； UniProt 30–136	Fragment：SEE REMARK 999	Envelope protein E × 18 （O11875） PrM × 18 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 18 （P01783,Q6PIP8）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
5	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain H； UniProt 30–136 Chain J； UniProt 30–136 Chain L； UniProt 30–136	Fragment：SEE REMARK 999	Envelope protein E × 3 （O11875） PrM × 3 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 3 （P01783,Q6PIP8）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 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 3J42	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1IGC IGG1 FAB FRAGMENT (MOPC21) COMPLEX WITH DOMAIN III OF PROTEIN G FROM STREPTOCOCCUS Deposited 1994-08-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain L 30–136（107 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.60 Å
4KVC 2H2 Fab fragment of immature Dengue virus Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 30–136（107 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；25% PEG 6000 0.1 M MES 0.2M NH4Cl, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.31 Å R-free 0.234

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

View Construct and Data Evidence

UniProt name	KV5A2_MOUSE
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain H； PDBConstruct 1–107； UniProt 30–136 Author chain J； PDBConstruct 1–107； UniProt 30–136 Author chain L； PDBConstruct 1–107； UniProt 30–136

Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera

Mus musculus

UniProt Q7TS98

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 Heteromer Protein × 720 PDB declaration: 720-meric（720） Consistent with protein copy count	Chain H； UniProt 130–234 Chain J； UniProt 130–234 Chain L； UniProt 130–234	Fragment：SEE REMARK 999	Envelope protein E × 180 （O11875） PrM × 180 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 180 （P01783,Q6PIP8）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
2	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain H； UniProt 130–234 Chain J； UniProt 130–234 Chain L； UniProt 130–234	Fragment：SEE REMARK 999	Envelope protein E × 3 （O11875） PrM × 3 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 3 （P01783,Q6PIP8）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
3	Insufficient information Heteromer Protein × 60 PDB declaration: 60-meric（60） Consistent with protein copy count	Chain H； UniProt 130–234 Chain J； UniProt 130–234 Chain L； UniProt 130–234	Fragment：SEE REMARK 999	Envelope protein E × 15 （O11875） PrM × 15 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 15 （P01783,Q6PIP8）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
4	Insufficient information Heteromer Protein × 72 PDB declaration: 72-meric（72） Consistent with protein copy count	Chain H； UniProt 130–234 Chain J； UniProt 130–234 Chain L； UniProt 130–234	Fragment：SEE REMARK 999	Envelope protein E × 18 （O11875） PrM × 18 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 18 （P01783,Q6PIP8）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 Å
5	Insufficient information Heteromer Protein × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain H； UniProt 130–234 Chain J； UniProt 130–234 Chain L； UniProt 130–234	Fragment：SEE REMARK 999	Envelope protein E × 3 （O11875） PrM × 3 （Q3BCY5） Ig heavy chain V region MOPC 21, Igh protein chimera × 3 （P01783,Q6PIP8）	ELECTRON MICROSCOPY cryo-EM buffer：100 mM phosphate buffer；pH 7；100 mM phosphate buffer cryo-EM vitrification conditions：100 K；Cryogen ETHANE；Plunged into liquid ethane (homemade plunger)	Resolution 21.00 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 3J42	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1D5B UNLIGANDED MATURE OXY-COPE CATALYTIC ANTIBODY Deposited 1999-10-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 23–129（107 aa） Fragment：chimeric fab fragment (UNP Q7TS98 reisues 23-129, P01834 residues 1-104) Chain L 23–129（107 aa） Fragment：chimeric fab fragment (UNP Q7TS98 reisues 23-129, P01834 residues 1-104)	Not recorded	CD CADMIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；25%PEG 1000, 100mM sodium acetate, 300mM CdCl2, 100mM ammonium sulfate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.285
1D5B UNLIGANDED MATURE OXY-COPE CATALYTIC ANTIBODY Deposited 1999-10-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 23–129（107 aa） Fragment：chimeric fab fragment (UNP Q7TS98 reisues 23-129, P01834 residues 1-104)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；25%PEG 1000, 100mM sodium acetate, 300mM CdCl2, 100mM ammonium sulfate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.285
1D5B UNLIGANDED MATURE OXY-COPE CATALYTIC ANTIBODY Deposited 1999-10-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 23–129（107 aa） Fragment：chimeric fab fragment (UNP Q7TS98 reisues 23-129, P01834 residues 1-104)	Not recorded	CD CADMIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；25%PEG 1000, 100mM sodium acetate, 300mM CdCl2, 100mM ammonium sulfate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.285
1D5I UNLIGANDED GERMLINE PRECURSOR OF AN OXY-COPE CATALYTIC ANTIBODY Deposited 1999-10-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 23–129（107 aa） Fragment：chimeric fab fragment (UNP Q7TS98 reisues 23-129, P01834 residues 1-104)	Not recorded	CD CADMIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；75mM Hepes pH 7.0 9% PEG 4000 150 mM Ammonium Sulfate 20% 1,4 butanediol 100 mM Cadmium Chloride, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.00 Å R-free 0.263
1D6V CONFORMATION EFFECTS IN BIOLOGICAL CATALYSIS INTRODUCED BY OXY-COPE ANTIBODY MATURATION Deposited 1999-10-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 23–129（107 aa） Fragment：chimeric fab fragment (UNP Q7TS98 reisues 23-129, P01834 residues 1-104)	Not recorded	CD CADMIUM ION × 4 HOP (1S,2S,5S)2-(4-GLUTARIDYLBENZYL)-5-PHENYL-1-CYCLOHEXANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；292 K；9% polyethylene glycol 4000 250mM ammonium sulfate 80mM Cadmium Chloride 75mM Hepes 20% 1,4 butanediol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 19K	Resolution 2.00 Å R-free 0.264
4KVC 2H2 Fab fragment of immature Dengue virus Deposited 2013-05-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 130–234（105 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；25% PEG 6000 0.1 M MES 0.2M NH4Cl, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.31 Å R-free 0.234
5TR8 Crystal structure of vaccine-elicited pan- influenza H1N1 neutralizing murine antibody 441D6. Deposited 2016-10-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain L 132–234（103 aa）	Not recorded	NI NICKEL (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；273 K；12% PEG3350, 100 mM HEPES pH 7.5, 5 mM MgCl2, 5mM NiCl2	Resolution 2.01 Å R-free 0.198
5VPL CRYSTAL STRUCTURE OF DER F 1 COMPLEXED WITH FAB 4C1 Deposited 2017-05-05	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 × 3 PDB declaration: trimeric	Chain C 24–235（212 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7；293 K；0.1M HEPES, 18% W/V PEG12K, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K	Resolution 1.90 Å R-free 0.194

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

View Construct and Data Evidence

UniProt name	Q7TS98_MOUSE
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain H； PDBConstruct 108–212； UniProt 130–234 Author chain J； PDBConstruct 108–212； UniProt 130–234 Author chain L； PDBConstruct 108–212； UniProt 130–234

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	3j42
Deposition date deposition_date	2013-06-13
Structure title title	Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody
Keywords keywords	Dengue, maturation, immature, antibody, VIRUS-IMMUNE SYSTEM complex; VIRUS/IMMUNE SYSTEM
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	62.73 Å
Radius of gyration Rg (electron density) rg_electron	71.39 Å
Forward intensity I(0) i0	1321070000.00
Molecular weight molecular_weight	297300.0 kDa
Excluded volume excluded_volume	365440 Å³
Envelope volume envelope_volume	537970 Å³
Hydration-shell volume shell_volume	79573 Å³
Envelope diameter envelope_diameter	205.8 Å
Shell Rg shell_rg	53.50 Å
Envelope Rg envelope_rg	66.95 Å
Shape Rg shape_rg	49.56 Å
Total Rg total_rg	96.07 Å
Total atoms total_atoms	9813
Residues n_residues	1284
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	221.1 Å
Rg (real space) rg_real	62.91 Å
Rg uncertainty (real space) rg_real_error	2.16 Å
I(0) (real space) i0_real	1.3210e+09
I(0) uncertainty (real space) i0_real_error	2.8190e+07
Rg (reciprocal space) rg_reciprocal	62.56 Å
I(0) (reciprocal space) i0_reciprocal	1320000000.0000
Solution quality estimate total_estimate	0.6518
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	70.7 Å
Skewness Skewness skewness	0.278
Kurtosis Kurtosis kurtosis	-0.547
Angular range angular_range	— – 0.1250 Å⁻¹
Current regularization parameter α current_alpha	0.0087
Highest regularization parameter α highest_alpha	43990000.0000
Real-space data points n_real_points	26
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.848

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Envelope protein E
Molecular weight formula_weight	43400.9 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	11226

MRCIGISNRDFVEGVSSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFRCKKNMEGKVVQPENLEYTVVITPHSGEEHAVGNDTGKHGKEVKITPQSSITEAELTGYGTVTMECSPRTGLDEMVLLQMENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLDWFKKG

Entity 2 Entity 2 polymer

Description description	PrM
Molecular weight formula_weight	9261.5 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F

FHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCEDTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCT

Entity 3 Entity 3 polymer

Description description	Ig heavy chain V region MOPC 21, Igh protein chimera
Molecular weight formula_weight	23696.6 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,I,K

DVQLVESGGGLVQPGGSRKLSCAASGFTFSSFGMHWVRQAPEKGLEWVAYISSGSSTLHYADTVKGRFTISRDNPKNTLFLQMTSLRSEDTAMYYCARWGNYPHYAMDYWGQGTSVTVSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSGLYTLSSSVTVTSSTWPSQTITCNVAHPASSTKVDKKIEPRV

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	mouse
NCBI Class编号 ncbi_taxonomy_id	10090

Entity 4 Entity 4 polymer

Description description	Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera
Molecular weight formula_weight	23355.7 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,J,L

NIVMTQSPKSMSMSVGERVTLTCKASENVGTYVSWYQQKPEQSPKLLIYGASNRYTGVPDRFTGSGSATDFTLTISSVQAEDLADYHCGQSYSTPYTFGGGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRN

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	mouse
NCBI Class编号 ncbi_taxonomy_id	10090

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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	1

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

Resolution resolution	21.00 Å
Resolution测定方法 resolution_method	projection matching
颗粒数 num_particles	378

fit	/app/data/saxs_computation/j4/3j42/3j42.fit
pddf	/app/data/pr_computation/j4/3j42/3j42.pr.out
profile	/app/data/saxs_computation/j4/3j42/3j42.dat

Obstruction of Dengue Virus Maturation by Fab Fragments of the 2H2 Antibody

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

Envelope protein E

State in the Current Structure

Other States of the Same Protein in the Database

PrM

State in the Current Structure

Other States of the Same Protein in the Database

Ig heavy chain V region MOPC 21, Igh protein chimera

State in the Current Structure

Other States of the Same Protein in the Database

Ig heavy chain V region MOPC 21, Igh protein chimera

State in the Current Structure

Other States of the Same Protein in the Database

Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera

State in the Current Structure

Other States of the Same Protein in the Database

Ig kappa chain V-V region MOPC 21, Anti-colorectal carcinoma light chain chimera

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)