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1m0f

Structural Studies of Bacteriophage alpha3 Assembly, Cryo-electron microscopy

Method: ELECTRON MICROSCOPY Dmax: 108.9 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Capsid Protein F

Enterobacteria phage alpha3

UniProt P08767

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 420 PDB declaration: 420-MERIC（420） Consistent with protein copy count Chain F； UniProt 1–431 Not recorded Scaffolding protein D × 240 Major Spike Protein G × 60 （P31281） Scaffolding Protein B × 60 ELECTRON MICROSCOPY cryo-EM buffer：10 mM Tris and 1 mM EDTA；pH 7.5；10 mM Tris and 1 mM EDTA Resolution 16.00 Å
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count Chain F； UniProt 1–431 Not recorded Scaffolding protein D × 4 Major Spike Protein G × 1 （P31281） Scaffolding Protein B × 1 ELECTRON MICROSCOPY cryo-EM buffer：10 mM Tris and 1 mM EDTA；pH 7.5；10 mM Tris and 1 mM EDTA Resolution 16.00 Å
3 Protein heterocomplex Heteromer Protein × 35 PDB declaration: 35-meric（35） Consistent with protein copy count Chain F； UniProt 1–431 Not recorded Scaffolding protein D × 20 Major Spike Protein G × 5 （P31281） Scaffolding Protein B × 5 ELECTRON MICROSCOPY cryo-EM buffer：10 mM Tris and 1 mM EDTA；pH 7.5；10 mM Tris and 1 mM EDTA Resolution 16.00 Å
4 Protein heterocomplex Heteromer Protein × 42 PDB declaration: 42-meric（42） Consistent with protein copy count Chain F； UniProt 1–431 Not recorded Scaffolding protein D × 24 Major Spike Protein G × 6 （P31281） Scaffolding Protein B × 6 ELECTRON MICROSCOPY cryo-EM buffer：10 mM Tris and 1 mM EDTA；pH 7.5；10 mM Tris and 1 mM EDTA Resolution 16.00 Å
5 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count Chain F； UniProt 1–431 Not recorded Scaffolding protein D × 4 Major Spike Protein G × 1 （P31281） Scaffolding Protein B × 1 ELECTRON MICROSCOPY cryo-EM buffer：10 mM Tris and 1 mM EDTA；pH 7.5；10 mM Tris and 1 mM EDTA Resolution 16.00 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 1M0F Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 180 PDB declaration: 240-MERIC
Chain F 1–431（431 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric
Chain F 1–431（431 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein–DNA Heteromer；Protein × 15 PDB declaration: eicosameric
Chain F 1–431（431 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein–DNA Heteromer；Protein × 18 PDB declaration: 24-meric
Chain F 1–431（431 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric
Chain F 1–431（431 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein–DNA Heteromer；Protein × 180 PDB declaration: 240-meric
Chain F 1–431（431 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 180 PDB declaration: 240-MERIC
Chain F 1–431（431 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 360 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric
Chain F 1–431（431 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein–DNA Heteromer；Protein × 15 PDB declaration: eicosameric
Chain F 1–431（431 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 30 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein–DNA Heteromer；Protein × 18 PDB declaration: 24-meric
Chain F 1–431（431 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 36 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric
Chain F 1–431（431 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein–DNA Heteromer；Protein × 60 PDB declaration: 80-meric
Chain F 1–431（431 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 120 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236

2 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VGF_BPAL3
Isoform —
PDB entities 2
Chains and sequence ranges Author chain F； PDBConstruct 1–431； UniProt 1–431

Major Spike Protein G

Enterobacteria phage alpha3

UniProt P31281

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 420 PDB declaration: 420-MERIC（420） Consistent with protein copy count Chain G； UniProt 1–187 Not recorded Scaffolding protein D × 240 Capsid Protein F × 60 （P08767） Scaffolding Protein B × 60 ELECTRON MICROSCOPY cryo-EM buffer：10 mM Tris and 1 mM EDTA；pH 7.5；10 mM Tris and 1 mM EDTA Resolution 16.00 Å
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count Chain G； UniProt 1–187 Not recorded Scaffolding protein D × 4 Capsid Protein F × 1 （P08767） Scaffolding Protein B × 1 ELECTRON MICROSCOPY cryo-EM buffer：10 mM Tris and 1 mM EDTA；pH 7.5；10 mM Tris and 1 mM EDTA Resolution 16.00 Å
3 Protein heterocomplex Heteromer Protein × 35 PDB declaration: 35-meric（35） Consistent with protein copy count Chain G； UniProt 1–187 Not recorded Scaffolding protein D × 20 Capsid Protein F × 5 （P08767） Scaffolding Protein B × 5 ELECTRON MICROSCOPY cryo-EM buffer：10 mM Tris and 1 mM EDTA；pH 7.5；10 mM Tris and 1 mM EDTA Resolution 16.00 Å
4 Protein heterocomplex Heteromer Protein × 42 PDB declaration: 42-meric（42） Consistent with protein copy count Chain G； UniProt 1–187 Not recorded Scaffolding protein D × 24 Capsid Protein F × 6 （P08767） Scaffolding Protein B × 6 ELECTRON MICROSCOPY cryo-EM buffer：10 mM Tris and 1 mM EDTA；pH 7.5；10 mM Tris and 1 mM EDTA Resolution 16.00 Å
5 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric（7） Consistent with protein copy count Chain G； UniProt 1–187 Not recorded Scaffolding protein D × 4 Capsid Protein F × 1 （P08767） Scaffolding Protein B × 1 ELECTRON MICROSCOPY cryo-EM buffer：10 mM Tris and 1 mM EDTA；pH 7.5；10 mM Tris and 1 mM EDTA Resolution 16.00 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 1M0F Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 180 PDB declaration: 240-MERIC
Chain G 1–187（187 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric
Chain G 1–187（187 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein–DNA Heteromer；Protein × 15 PDB declaration: eicosameric
Chain G 1–187（187 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein–DNA Heteromer；Protein × 18 PDB declaration: 24-meric
Chain G 1–187（187 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric
Chain G 1–187（187 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1M06 Structural Studies of Bacteriophage alpha3 Assembly, X-Ray Crystallography Deposited 2002-06-12 Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein–DNA Heteromer；Protein × 180 PDB declaration: 240-meric
Chain G 1–187（187 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；318.15 K；3-5% PEG8000, 100 mM sodium citrate pH 5.0, 1 mM EDTA, 300 mM NaCl, 0.1 mM-mercapto-ethanol, and 0.02 % sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 318.15K
Resolution 3.50 Å R-free 0.234
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 180 PDB declaration: 240-MERIC
Chain G 1–187（187 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 360 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric
Chain G 1–187（187 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein–DNA Heteromer；Protein × 15 PDB declaration: eicosameric
Chain G 1–187（187 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 30 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein–DNA Heteromer；Protein × 18 PDB declaration: 24-meric
Chain G 1–187（187 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 36 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein–DNA Heteromer；Protein × 3 PDB declaration: tetrameric
Chain G 1–187（187 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236
1RB8 The phiX174 DNA binding protein J in two different capsid environments. Deposited 2003-11-03 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein–DNA Heteromer；Protein × 60 PDB declaration: 80-meric
Chain G 1–187（187 aa）
Not recorded DC 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE × 120 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；298 K；4-7% PEG 8000, 100 mM sodium citrate pH 5.0, 40% glycerol, 0.02% sodium azide, 0.1% beta-mercapto-ethanol, 0.9M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.50 Å R-free 0.236

2 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VGG_BPAL3
Isoform —
PDB entities 3
Chains and sequence ranges Author chain G； PDBConstruct 1–187； UniProt 1–187

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1m0f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1m0f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1m0f
Deposition date deposition_date2002-06-12
Structure title titleStructural Studies of Bacteriophage alpha3 Assembly, Cryo-electron microscopy
Keywords keywordsBacteriophage, Cryo Electron Microscopy, Procapsid, morphogenesis, microviridae, assembly, Icosahedral virus, Virus; VIRUS
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier35.46 Å
Radius of gyration Rg (electron density) rg_electron34.83 Å
Forward intensity I(0) i0263696000.00
Molecular weight molecular_weight131960.0 kDa
Excluded volume excluded_volume161370 ų
Envelope volume envelope_volume144450 ų
Hydration-shell volume shell_volume36916 ų
Envelope diameter envelope_diameter109.1 Å
Shell Rg shell_rg39.13 Å
Envelope Rg envelope_rg32.48 Å
Shape Rg shape_rg34.87 Å
Total Rg total_rg35.06 Å
Total atoms total_atoms—
Residues n_residues—
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax108.9 Å
Rg (real space) rg_real35.25 Å
Rg uncertainty (real space) rg_real_error0.55 Å
I(0) (real space) i0_real2.6370e+08
I(0) uncertainty (real space) i0_real_error4.0790e+06
Rg (reciprocal space) rg_reciprocal35.38 Å
I(0) (reciprocal space) i0_reciprocal263700000.0000
Solution quality estimate total_estimate0.9087
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.4 Å
Skewness Skewness skewness0.049
Kurtosis Kurtosis kurtosis-0.633
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha31480000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.958
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd1m0f1_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1m0f2_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1m0f3_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1m0f4_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1m0fb_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1m0ff_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
Domain ID domain_idd1m0fg_
Class classi — Low resolution protein structures
Fold Fold foldi.6 — Viruses and virus-receptor complexes
Superfamily Superfamily superfamilyi.6.1 — Viruses and virus-receptor complexes
Family Family familyi.6.1.1 — Viruses and virus-receptor complexes
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8. Citations (1)

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9. Files and Curves (10)