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6xf8

DLP 5 fold

Method: ELECTRON MICROSCOPY Dmax: 284.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Outer capsid protein mu-1

OrganismNot specified

UniProt P11077

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 × 9 PDB declaration: nonameric（9） Consistent with protein copy count Chain F； UniProt 43–675 Chain K； UniProt 43–675 Not recorded Outer capsid protein sigma-3 × 3 （P07939） Inner capsid protein sigma-2 × 1 （P11314） Inner capsid protein lambda-1 × 2 （Q9WAB2） mRNA (guanine-N(7)-)-methyltransferase × 1 （Q91RA5） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 6.50 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 6XF8 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1JMU Crystal Structure of the Reovirus mu1/sigma3 Complex Deposited 2001-07-20 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain A 1–41（41 aa） Fragment：N-terminus (residues 2-42)
Chain B 43–708（666 aa） Fragment：C-terminus (residues 43-708)
Chain C 1–41（41 aa） Fragment：N-terminus (residues 2-42)
Chain D 43–708（666 aa） Fragment：C-terminus (residues 43-708)
Chain E 1–41（41 aa） Fragment：N-terminus (residues 2-42)
Chain F 43–708（666 aa） Fragment：C-terminus (residues 43-708)
Not recorded CL CHLORIDE ION × 1 BOG octyl beta-D-glucopyranoside × 3 SO4 SULFATE ION × 9 ZN ZINC ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；Ammonium sulfate, n-octyl-b-D-glucopyranoside, DTT, Pipes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.80 Å R-free 0.241
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 1620 PDB declaration: 1620-MERIC
Chain A 1–708（708 aa）
Chain B 1–708（708 aa）
Chain C 1–708（708 aa）
Chain J 1–708（708 aa）
Chain K 1–708（708 aa）
Chain L 1–708（708 aa）
Chain P 1–708（708 aa）
Chain Q 1–708（708 aa）
Chain R 1–708（708 aa）
Chain T 1–708（708 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain A 1–708（708 aa）
Chain B 1–708（708 aa）
Chain C 1–708（708 aa）
Chain J 1–708（708 aa）
Chain K 1–708（708 aa）
Chain L 1–708（708 aa）
Chain P 1–708（708 aa）
Chain Q 1–708（708 aa）
Chain R 1–708（708 aa）
Chain T 1–708（708 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 135 PDB declaration: 135-meric
Chain A 1–708（708 aa）
Chain B 1–708（708 aa）
Chain C 1–708（708 aa）
Chain J 1–708（708 aa）
Chain K 1–708（708 aa）
Chain L 1–708（708 aa）
Chain P 1–708（708 aa）
Chain Q 1–708（708 aa）
Chain R 1–708（708 aa）
Chain T 1–708（708 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 162 PDB declaration: 162-meric
Chain A 1–708（708 aa）
Chain B 1–708（708 aa）
Chain C 1–708（708 aa）
Chain J 1–708（708 aa）
Chain K 1–708（708 aa）
Chain L 1–708（708 aa）
Chain P 1–708（708 aa）
Chain Q 1–708（708 aa）
Chain R 1–708（708 aa）
Chain T 1–708（708 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain A 1–708（708 aa）
Chain B 1–708（708 aa）
Chain C 1–708（708 aa）
Chain J 1–708（708 aa）
Chain K 1–708（708 aa）
Chain L 1–708（708 aa）
Chain P 1–708（708 aa）
Chain Q 1–708（708 aa）
Chain R 1–708（708 aa）
Chain T 1–708（708 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
6ZTY Assembly intermediates of orthoreovirus captured in the cell Deposited 2020-07-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain H 10–675（666 aa）
Chain I 10–675（666 aa）
Chain J 10–675（666 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 5.60 Å
6ZTZ Assembly intermediates of orthoreovirus captured in the cell Deposited 2020-07-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric
Chain K 10–675（666 aa）
Chain L 10–675（666 aa）
Chain M 10–675（666 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 6.50 Å

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

View Construct and Data Evidence
UniProt name MU1_REOVL
Isoform —
PDB entities 1
Chains and sequence ranges Author chain F； PDBConstruct 1–633； UniProt 43–675 Author chain K； PDBConstruct 1–633； UniProt 43–675

Outer capsid protein sigma-3

OrganismNot specified

UniProt P07939

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 × 9 PDB declaration: nonameric（9） Consistent with protein copy count Chain G； UniProt 1–365 Chain H； UniProt 1–365 Chain I； UniProt 1–365 Not recorded Outer capsid protein mu-1 × 2 （P11077） Inner capsid protein sigma-2 × 1 （P11314） Inner capsid protein lambda-1 × 2 （Q9WAB2） mRNA (guanine-N(7)-)-methyltransferase × 1 （Q91RA5） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 6.50 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 6XF8 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 1620 PDB declaration: 1620-MERIC
Chain D 1–365（365 aa）
Chain E 1–365（365 aa）
Chain F 1–365（365 aa）
Chain G 1–365（365 aa）
Chain H 1–365（365 aa）
Chain I 1–365（365 aa）
Chain M 1–365（365 aa）
Chain N 1–365（365 aa）
Chain O 1–365（365 aa）
Chain S 1–365（365 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain D 1–365（365 aa）
Chain E 1–365（365 aa）
Chain F 1–365（365 aa）
Chain G 1–365（365 aa）
Chain H 1–365（365 aa）
Chain I 1–365（365 aa）
Chain M 1–365（365 aa）
Chain N 1–365（365 aa）
Chain O 1–365（365 aa）
Chain S 1–365（365 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 135 PDB declaration: 135-meric
Chain D 1–365（365 aa）
Chain E 1–365（365 aa）
Chain F 1–365（365 aa）
Chain G 1–365（365 aa）
Chain H 1–365（365 aa）
Chain I 1–365（365 aa）
Chain M 1–365（365 aa）
Chain N 1–365（365 aa）
Chain O 1–365（365 aa）
Chain S 1–365（365 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 162 PDB declaration: 162-meric
Chain D 1–365（365 aa）
Chain E 1–365（365 aa）
Chain F 1–365（365 aa）
Chain G 1–365（365 aa）
Chain H 1–365（365 aa）
Chain I 1–365（365 aa）
Chain M 1–365（365 aa）
Chain N 1–365（365 aa）
Chain O 1–365（365 aa）
Chain S 1–365（365 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain D 1–365（365 aa）
Chain E 1–365（365 aa）
Chain F 1–365（365 aa）
Chain G 1–365（365 aa）
Chain H 1–365（365 aa）
Chain I 1–365（365 aa）
Chain M 1–365（365 aa）
Chain N 1–365（365 aa）
Chain O 1–365（365 aa）
Chain S 1–365（365 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
6ZTY Assembly intermediates of orthoreovirus captured in the cell Deposited 2020-07-20 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain U 1–365（365 aa）
Chain V 1–365（365 aa）
Chain W 1–365（365 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 5.60 Å
6ZTZ Assembly intermediates of orthoreovirus captured in the cell Deposited 2020-07-20 Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric
Chain X 1–365（365 aa）
Chain Y 1–365（365 aa）
Chain Z 1–365（365 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 6.50 Å

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

View Construct and Data Evidence
UniProt name SIGM3_REOVL
Isoform —
PDB entities 2
Chains and sequence ranges Author chain G； PDBConstruct 1–365； UniProt 1–365 Author chain H； PDBConstruct 1–365； UniProt 1–365 Author chain I； PDBConstruct 1–365； UniProt 1–365

Inner capsid protein sigma-2

OrganismNot specified

UniProt P11314

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 × 9 PDB declaration: nonameric（9） Consistent with protein copy count Chain E； UniProt 2–418 Not recorded Outer capsid protein mu-1 × 2 （P11077） Outer capsid protein sigma-3 × 3 （P07939） Inner capsid protein lambda-1 × 2 （Q9WAB2） mRNA (guanine-N(7)-)-methyltransferase × 1 （Q91RA5） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 6.50 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 6XF8 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 1620 PDB declaration: 1620-MERIC
Chain X 1–418（418 aa）
Chain Y 1–418（418 aa）
Chain Z 1–418（418 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain X 1–418（418 aa）
Chain Y 1–418（418 aa）
Chain Z 1–418（418 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 135 PDB declaration: 135-meric
Chain X 1–418（418 aa）
Chain Y 1–418（418 aa）
Chain Z 1–418（418 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 162 PDB declaration: 162-meric
Chain X 1–418（418 aa）
Chain Y 1–418（418 aa）
Chain Z 1–418（418 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain X 1–418（418 aa）
Chain Y 1–418（418 aa）
Chain Z 1–418（418 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
6ZTZ Assembly intermediates of orthoreovirus captured in the cell Deposited 2020-07-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric
Chain D 2–418（417 aa）
Chain P 2–418（417 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 6.50 Å

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

View Construct and Data Evidence
UniProt name SIGM2_REOVL
Isoform —
PDB entities 3
Chains and sequence ranges Author chain E； PDBConstruct 1–417； UniProt 2–418

Inner capsid protein lambda-1

OrganismNot specified

UniProt Q9WAB2

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 × 9 PDB declaration: nonameric（9） Consistent with protein copy count Chain B； UniProt 217–1275 Chain C； UniProt 217–1275 Not recorded Outer capsid protein mu-1 × 2 （P11077） Outer capsid protein sigma-3 × 3 （P07939） Inner capsid protein sigma-2 × 1 （P11314） mRNA (guanine-N(7)-)-methyltransferase × 1 （Q91RA5） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 6.50 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 6XF8 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 1620 PDB declaration: 1620-MERIC
Chain V 1–1275（1275 aa）
Chain W 1–1275（1275 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain V 1–1275（1275 aa）
Chain W 1–1275（1275 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 135 PDB declaration: 135-meric
Chain V 1–1275（1275 aa）
Chain W 1–1275（1275 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 162 PDB declaration: 162-meric
Chain V 1–1275（1275 aa）
Chain W 1–1275（1275 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
2CSE Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution Deposited 2005-05-21 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric
Chain V 1–1275（1275 aa）
Chain W 1–1275（1275 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 10 mM TRIS；pH 7.5；10 mM TRIS
cryo-EM vitrification conditions Cryogen ETHANE；PLUNGED INTO ETHANE
Resolution 7.00 Å
6ZTZ Assembly intermediates of orthoreovirus captured in the cell Deposited 2020-07-20 Different construct Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric
Chain B 241–1275（1035 aa）
Chain C 260–1275（1016 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 6.50 Å

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

View Construct and Data Evidence
UniProt name LMBD1_REOVL
Isoform —
PDB entities 4
Chains and sequence ranges Author chain B； PDBConstruct 1–1059； UniProt 217–1275 Author chain C； PDBConstruct 1–1059； UniProt 217–1275

mRNA (guanine-N(7)-)-methyltransferase

OrganismNot specified

UniProt Q91RA5

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 × 9 PDB declaration: nonameric（9） Consistent with protein copy count Chain A； UniProt 2–1289 Not recorded Outer capsid protein mu-1 × 2 （P11077） Outer capsid protein sigma-3 × 3 （P07939） Inner capsid protein sigma-2 × 1 （P11314） Inner capsid protein lambda-1 × 2 （Q9WAB2） ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 6.50 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 Q91RA5_REOVL
Isoform —
PDB entities 5
Chains and sequence ranges Author chain A； PDBConstruct 1–1288； UniProt 2–1289

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 6xf8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xf8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6xf8
Deposition date deposition_date2020-06-15
Structure title titleDLP 5 fold
Keywords keywordsorthoreovirus, VIRUS LIKE PARTICLE; VIRUS LIKE PARTICLE
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier81.49 Å
Radius of gyration Rg (electron density) rg_electron81.58 Å
Forward intensity I(0) i06304540000.00
Molecular weight molecular_weight679760.0 kDa
Excluded volume excluded_volume852080 ų
Envelope volume envelope_volume1382200 ų
Hydration-shell volume shell_volume144290 ų
Envelope diameter envelope_diameter285.0 Å
Shell Rg shell_rg76.74 Å
Envelope Rg envelope_rg78.36 Å
Shape Rg shape_rg81.61 Å
Total Rg total_rg81.42 Å
Total atoms total_atoms47829
Residues n_residues6093
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 dmax284.5 Å
Rg (real space) rg_real85.94 Å
Rg uncertainty (real space) rg_real_error1.77 Å
I(0) (real space) i0_real6.3330e+09
I(0) uncertainty (real space) i0_real_error1.4450e+08
Rg (reciprocal space) rg_reciprocal80.46 Å
I(0) (reciprocal space) i0_reciprocal6286000000.0000
Solution quality estimate total_estimate0.8742
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary74.9 Å
Skewness Skewness skewness0.446
Kurtosis Kurtosis kurtosis-0.366
Angular range angular_range— – 0.0950 Å−1
Current regularization parameter α current_alpha1.3630
Highest regularization parameter α highest_alpha288500000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 0.848; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.129
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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8. Citations (2)

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9. Files and Curves (10)