SAXSdb — 2cse

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

major outer-capsid protein mu1

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	Protein heterocomplex Heteromer Protein × 1620 PDB declaration: 1620-MERIC（1620） Consistent with protein copy count	Chain A； UniProt 1–708 Chain B； UniProt 1–708 Chain C； UniProt 1–708 Chain J； UniProt 1–708 Chain K； UniProt 1–708 Chain L； UniProt 1–708 Chain P； UniProt 1–708 Chain Q； UniProt 1–708 Chain R； UniProt 1–708 Chain T； UniProt 1–708	Not recorded	major capsid surface protein sigma-3 × 600 （P07939） guanylyltransferase × 60 （P11079） major core protein lambda 1 × 120 （Q9WAB2） Sigma 2 protein × 180 （P11314） Minor core protein lambda 3 × 60 （P17376）	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
2	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain A； UniProt 1–708 Chain B； UniProt 1–708 Chain C； UniProt 1–708 Chain J； UniProt 1–708 Chain K； UniProt 1–708 Chain L； UniProt 1–708 Chain P； UniProt 1–708 Chain Q； UniProt 1–708 Chain R； UniProt 1–708 Chain T； UniProt 1–708	Not recorded	major capsid surface protein sigma-3 × 10 （P07939） guanylyltransferase × 1 （P11079） major core protein lambda 1 × 2 （Q9WAB2） Sigma 2 protein × 3 （P11314） Minor core protein lambda 3 × 1 （P17376）	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
3	Protein heterocomplex Heteromer Protein × 135 PDB declaration: 135-meric（135） Consistent with protein copy count	Chain A； UniProt 1–708 Chain B； UniProt 1–708 Chain C； UniProt 1–708 Chain J； UniProt 1–708 Chain K； UniProt 1–708 Chain L； UniProt 1–708 Chain P； UniProt 1–708 Chain Q； UniProt 1–708 Chain R； UniProt 1–708 Chain T； UniProt 1–708	Not recorded	major capsid surface protein sigma-3 × 50 （P07939） guanylyltransferase × 5 （P11079） major core protein lambda 1 × 10 （Q9WAB2） Sigma 2 protein × 15 （P11314） Minor core protein lambda 3 × 5 （P17376）	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
4	Protein heterocomplex Heteromer Protein × 162 PDB declaration: 162-meric（162） Consistent with protein copy count	Chain A； UniProt 1–708 Chain B； UniProt 1–708 Chain C； UniProt 1–708 Chain J； UniProt 1–708 Chain K； UniProt 1–708 Chain L； UniProt 1–708 Chain P； UniProt 1–708 Chain Q； UniProt 1–708 Chain R； UniProt 1–708 Chain T； UniProt 1–708	Not recorded	major capsid surface protein sigma-3 × 60 （P07939） guanylyltransferase × 6 （P11079） major core protein lambda 1 × 12 （Q9WAB2） Sigma 2 protein × 18 （P11314） Minor core protein lambda 3 × 6 （P17376）	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
5	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain A； UniProt 1–708 Chain B； UniProt 1–708 Chain C； UniProt 1–708 Chain J； UniProt 1–708 Chain K； UniProt 1–708 Chain L； UniProt 1–708 Chain P； UniProt 1–708 Chain Q； UniProt 1–708 Chain R； UniProt 1–708 Chain T； UniProt 1–708	Not recorded	major capsid surface protein sigma-3 × 10 （P07939） guanylyltransferase × 1 （P11079） major core protein lambda 1 × 2 （Q9WAB2） Sigma 2 protein × 3 （P11314） Minor core protein lambda 3 × 1 （P17376）	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

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 2CSE	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 oligomeric state 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
6XF8 DLP 5 fold Deposited 2020-06-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain F 43–675（633 aa） Chain K 43–675（633 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.50 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 Different structure-quality metrics	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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	VM2_REOVL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–708； UniProt 1–708 Author chain B； PDBConstruct 1–708； UniProt 1–708 Author chain C； PDBConstruct 1–708； UniProt 1–708 Author chain J； PDBConstruct 1–708； UniProt 1–708 Author chain K； PDBConstruct 1–708； UniProt 1–708 Author chain L； PDBConstruct 1–708； UniProt 1–708 Author chain P； PDBConstruct 1–708； UniProt 1–708 Author chain Q； PDBConstruct 1–708； UniProt 1–708 Author chain R； PDBConstruct 1–708； UniProt 1–708 Author chain T； PDBConstruct 1–708； UniProt 1–708

major capsid surface 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 × 1620 PDB declaration: 1620-MERIC（1620） Consistent with protein copy count	Chain D； UniProt 1–365 Chain E； UniProt 1–365 Chain F； UniProt 1–365 Chain G； UniProt 1–365 Chain H； UniProt 1–365 Chain I； UniProt 1–365 Chain M； UniProt 1–365 Chain N； UniProt 1–365 Chain O； UniProt 1–365 Chain S； UniProt 1–365	Not recorded	major outer-capsid protein mu1 × 600 （P11077） guanylyltransferase × 60 （P11079） major core protein lambda 1 × 120 （Q9WAB2） Sigma 2 protein × 180 （P11314） Minor core protein lambda 3 × 60 （P17376）	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
2	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain D； UniProt 1–365 Chain E； UniProt 1–365 Chain F； UniProt 1–365 Chain G； UniProt 1–365 Chain H； UniProt 1–365 Chain I； UniProt 1–365 Chain M； UniProt 1–365 Chain N； UniProt 1–365 Chain O； UniProt 1–365 Chain S； UniProt 1–365	Not recorded	major outer-capsid protein mu1 × 10 （P11077） guanylyltransferase × 1 （P11079） major core protein lambda 1 × 2 （Q9WAB2） Sigma 2 protein × 3 （P11314） Minor core protein lambda 3 × 1 （P17376）	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
3	Protein heterocomplex Heteromer Protein × 135 PDB declaration: 135-meric（135） Consistent with protein copy count	Chain D； UniProt 1–365 Chain E； UniProt 1–365 Chain F； UniProt 1–365 Chain G； UniProt 1–365 Chain H； UniProt 1–365 Chain I； UniProt 1–365 Chain M； UniProt 1–365 Chain N； UniProt 1–365 Chain O； UniProt 1–365 Chain S； UniProt 1–365	Not recorded	major outer-capsid protein mu1 × 50 （P11077） guanylyltransferase × 5 （P11079） major core protein lambda 1 × 10 （Q9WAB2） Sigma 2 protein × 15 （P11314） Minor core protein lambda 3 × 5 （P17376）	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
4	Protein heterocomplex Heteromer Protein × 162 PDB declaration: 162-meric（162） Consistent with protein copy count	Chain D； UniProt 1–365 Chain E； UniProt 1–365 Chain F； UniProt 1–365 Chain G； UniProt 1–365 Chain H； UniProt 1–365 Chain I； UniProt 1–365 Chain M； UniProt 1–365 Chain N； UniProt 1–365 Chain O； UniProt 1–365 Chain S； UniProt 1–365	Not recorded	major outer-capsid protein mu1 × 60 （P11077） guanylyltransferase × 6 （P11079） major core protein lambda 1 × 12 （Q9WAB2） Sigma 2 protein × 18 （P11314） Minor core protein lambda 3 × 6 （P17376）	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
5	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain D； UniProt 1–365 Chain E； UniProt 1–365 Chain F； UniProt 1–365 Chain G； UniProt 1–365 Chain H； UniProt 1–365 Chain I； UniProt 1–365 Chain M； UniProt 1–365 Chain N； UniProt 1–365 Chain O； UniProt 1–365 Chain S； UniProt 1–365	Not recorded	major outer-capsid protein mu1 × 10 （P11077） guanylyltransferase × 1 （P11079） major core protein lambda 1 × 2 （Q9WAB2） Sigma 2 protein × 3 （P11314） Minor core protein lambda 3 × 1 （P17376）	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

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 2CSE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6XF8 DLP 5 fold Deposited 2020-06-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain G 1–365（365 aa） Chain H 1–365（365 aa） Chain I 1–365（365 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.50 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 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 construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	VSI3_REOVL
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 1–365； UniProt 1–365 Author chain E； PDBConstruct 1–365； UniProt 1–365 Author chain F； PDBConstruct 1–365； UniProt 1–365 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 Author chain M； PDBConstruct 1–365； UniProt 1–365 Author chain N； PDBConstruct 1–365； UniProt 1–365 Author chain O； PDBConstruct 1–365； UniProt 1–365 Author chain S； PDBConstruct 1–365； UniProt 1–365

guanylyltransferase

OrganismNot specified

UniProt P11079

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 × 1620 PDB declaration: 1620-MERIC（1620） Consistent with protein copy count	Chain U； UniProt 1–1289	Not recorded	major outer-capsid protein mu1 × 600 （P11077） major capsid surface protein sigma-3 × 600 （P07939） major core protein lambda 1 × 120 （Q9WAB2） Sigma 2 protein × 180 （P11314） Minor core protein lambda 3 × 60 （P17376）	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
2	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain U； UniProt 1–1289	Not recorded	major outer-capsid protein mu1 × 10 （P11077） major capsid surface protein sigma-3 × 10 （P07939） major core protein lambda 1 × 2 （Q9WAB2） Sigma 2 protein × 3 （P11314） Minor core protein lambda 3 × 1 （P17376）	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
3	Protein heterocomplex Heteromer Protein × 135 PDB declaration: 135-meric（135） Consistent with protein copy count	Chain U； UniProt 1–1289	Not recorded	major outer-capsid protein mu1 × 50 （P11077） major capsid surface protein sigma-3 × 50 （P07939） major core protein lambda 1 × 10 （Q9WAB2） Sigma 2 protein × 15 （P11314） Minor core protein lambda 3 × 5 （P17376）	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
4	Protein heterocomplex Heteromer Protein × 162 PDB declaration: 162-meric（162） Consistent with protein copy count	Chain U； UniProt 1–1289	Not recorded	major outer-capsid protein mu1 × 60 （P11077） major capsid surface protein sigma-3 × 60 （P07939） major core protein lambda 1 × 12 （Q9WAB2） Sigma 2 protein × 18 （P11314） Minor core protein lambda 3 × 6 （P17376）	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
5	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain U； UniProt 1–1289	Not recorded	major outer-capsid protein mu1 × 10 （P11077） major capsid surface protein sigma-3 × 10 （P07939） major core protein lambda 1 × 2 （Q9WAB2） Sigma 2 protein × 3 （P11314） Minor core protein lambda 3 × 1 （P17376）	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

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 2CSE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1EJ6 Reovirus core Deposited 2000-02-29	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 300 PDB declaration: complete icosahedral assembly	Chain A 1–1289（1289 aa）	Not recorded	ZN ZINC ION × 60	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；sodium chloride, sodium acetate, magnesium chloride, hepes, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.60 Å R-free 0.208
1EJ6 Reovirus core Deposited 2000-02-29	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–1289（1289 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；sodium chloride, sodium acetate, magnesium chloride, hepes, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.60 Å R-free 0.208
1EJ6 Reovirus core Deposited 2000-02-29	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric	Chain A 1–1289（1289 aa）	Not recorded	ZN ZINC ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；sodium chloride, sodium acetate, magnesium chloride, hepes, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.60 Å R-free 0.208
1EJ6 Reovirus core Deposited 2000-02-29	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain A 1–1289（1289 aa）	Not recorded	ZN ZINC ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；sodium chloride, sodium acetate, magnesium chloride, hepes, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.60 Å R-free 0.208
1EJ6 Reovirus core Deposited 2000-02-29	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–1289（1289 aa）	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；sodium chloride, sodium acetate, magnesium chloride, hepes, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.60 Å R-free 0.208
1EJ6 Reovirus core Deposited 2000-02-29	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 6 Protein heterocomplex Heteromer；Protein × 25 PDB declaration: 25-meric	Chain A 1–1289（1289 aa）	Not recorded	ZN ZINC ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；sodium chloride, sodium acetate, magnesium chloride, hepes, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K	Resolution 3.60 Å R-free 0.208
6ZTZ Assembly intermediates of orthoreovirus captured in the cell Deposited 2020-07-20	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 11 PDB declaration: undecameric	Chain O 2–1289（1288 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
9CYT Cryo-EM structure of MRV outer shell Deposited 2024-08-02	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain J 1–1289（1289 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；Phosphate-buffered saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.70 Å
9CYX Cryo-EM structure of MRV full core Deposited 2024-08-02	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–1289（1288 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；Phosphate-buffered saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9CYY Cryo-EM structure of MRV virion Deposited 2024-08-03	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 29 PDB declaration: 29-meric	Chain J 1–1289（1289 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；Phosphate-buffered saline cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å

5 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	MCE_REOVD
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain U； PDBConstruct 1–1289； UniProt 1–1289

major core 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 × 1620 PDB declaration: 1620-MERIC（1620） Consistent with protein copy count	Chain V； UniProt 1–1275 Chain W； UniProt 1–1275	Not recorded	major outer-capsid protein mu1 × 600 （P11077） major capsid surface protein sigma-3 × 600 （P07939） guanylyltransferase × 60 （P11079） Sigma 2 protein × 180 （P11314） Minor core protein lambda 3 × 60 （P17376）	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
2	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain V； UniProt 1–1275 Chain W； UniProt 1–1275	Not recorded	major outer-capsid protein mu1 × 10 （P11077） major capsid surface protein sigma-3 × 10 （P07939） guanylyltransferase × 1 （P11079） Sigma 2 protein × 3 （P11314） Minor core protein lambda 3 × 1 （P17376）	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
3	Protein heterocomplex Heteromer Protein × 135 PDB declaration: 135-meric（135） Consistent with protein copy count	Chain V； UniProt 1–1275 Chain W； UniProt 1–1275	Not recorded	major outer-capsid protein mu1 × 50 （P11077） major capsid surface protein sigma-3 × 50 （P07939） guanylyltransferase × 5 （P11079） Sigma 2 protein × 15 （P11314） Minor core protein lambda 3 × 5 （P17376）	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
4	Protein heterocomplex Heteromer Protein × 162 PDB declaration: 162-meric（162） Consistent with protein copy count	Chain V； UniProt 1–1275 Chain W； UniProt 1–1275	Not recorded	major outer-capsid protein mu1 × 60 （P11077） major capsid surface protein sigma-3 × 60 （P07939） guanylyltransferase × 6 （P11079） Sigma 2 protein × 18 （P11314） Minor core protein lambda 3 × 6 （P17376）	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
5	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain V； UniProt 1–1275 Chain W； UniProt 1–1275	Not recorded	major outer-capsid protein mu1 × 10 （P11077） major capsid surface protein sigma-3 × 10 （P07939） guanylyltransferase × 1 （P11079） Sigma 2 protein × 3 （P11314） Minor core protein lambda 3 × 1 （P17376）	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

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 2CSE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6XF8 DLP 5 fold Deposited 2020-06-15	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain B 217–1275（1059 aa） Chain C 217–1275（1059 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.50 Å
6ZTZ Assembly intermediates of orthoreovirus captured in the cell Deposited 2020-07-20	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q9WAB2_REOVL
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain V； PDBConstruct 1–1275； UniProt 1–1275 Author chain W； PDBConstruct 1–1275； UniProt 1–1275

Sigma 2 protein

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 × 1620 PDB declaration: 1620-MERIC（1620） Consistent with protein copy count	Chain X； UniProt 1–418 Chain Y； UniProt 1–418 Chain Z； UniProt 1–418	Not recorded	major outer-capsid protein mu1 × 600 （P11077） major capsid surface protein sigma-3 × 600 （P07939） guanylyltransferase × 60 （P11079） major core protein lambda 1 × 120 （Q9WAB2） Minor core protein lambda 3 × 60 （P17376）	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
2	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain X； UniProt 1–418 Chain Y； UniProt 1–418 Chain Z； UniProt 1–418	Not recorded	major outer-capsid protein mu1 × 10 （P11077） major capsid surface protein sigma-3 × 10 （P07939） guanylyltransferase × 1 （P11079） major core protein lambda 1 × 2 （Q9WAB2） Minor core protein lambda 3 × 1 （P17376）	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
3	Protein heterocomplex Heteromer Protein × 135 PDB declaration: 135-meric（135） Consistent with protein copy count	Chain X； UniProt 1–418 Chain Y； UniProt 1–418 Chain Z； UniProt 1–418	Not recorded	major outer-capsid protein mu1 × 50 （P11077） major capsid surface protein sigma-3 × 50 （P07939） guanylyltransferase × 5 （P11079） major core protein lambda 1 × 10 （Q9WAB2） Minor core protein lambda 3 × 5 （P17376）	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
4	Protein heterocomplex Heteromer Protein × 162 PDB declaration: 162-meric（162） Consistent with protein copy count	Chain X； UniProt 1–418 Chain Y； UniProt 1–418 Chain Z； UniProt 1–418	Not recorded	major outer-capsid protein mu1 × 60 （P11077） major capsid surface protein sigma-3 × 60 （P07939） guanylyltransferase × 6 （P11079） major core protein lambda 1 × 12 （Q9WAB2） Minor core protein lambda 3 × 6 （P17376）	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
5	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain X； UniProt 1–418 Chain Y； UniProt 1–418 Chain Z； UniProt 1–418	Not recorded	major outer-capsid protein mu1 × 10 （P11077） major capsid surface protein sigma-3 × 10 （P07939） guanylyltransferase × 1 （P11079） major core protein lambda 1 × 2 （Q9WAB2） Minor core protein lambda 3 × 1 （P17376）	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

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 2CSE	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6XF8 DLP 5 fold Deposited 2020-06-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain E 2–418（417 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.50 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 Different structure-quality metrics	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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	VSI2_REOVL
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain X； PDBConstruct 1–418； UniProt 1–418 Author chain Y； PDBConstruct 1–418； UniProt 1–418 Author chain Z； PDBConstruct 1–418； UniProt 1–418

Minor core protein lambda 3

OrganismNot specified

UniProt P17376

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 × 1620 PDB declaration: 1620-MERIC（1620） Consistent with protein copy count	Chain 1； UniProt 1–1267	Not recorded	major outer-capsid protein mu1 × 600 （P11077） major capsid surface protein sigma-3 × 600 （P07939） guanylyltransferase × 60 （P11079） major core protein lambda 1 × 120 （Q9WAB2） Sigma 2 protein × 180 （P11314）	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
2	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain 1； UniProt 1–1267	Not recorded	major outer-capsid protein mu1 × 10 （P11077） major capsid surface protein sigma-3 × 10 （P07939） guanylyltransferase × 1 （P11079） major core protein lambda 1 × 2 （Q9WAB2） Sigma 2 protein × 3 （P11314）	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
3	Protein heterocomplex Heteromer Protein × 135 PDB declaration: 135-meric（135） Consistent with protein copy count	Chain 1； UniProt 1–1267	Not recorded	major outer-capsid protein mu1 × 50 （P11077） major capsid surface protein sigma-3 × 50 （P07939） guanylyltransferase × 5 （P11079） major core protein lambda 1 × 10 （Q9WAB2） Sigma 2 protein × 15 （P11314）	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
4	Protein heterocomplex Heteromer Protein × 162 PDB declaration: 162-meric（162） Consistent with protein copy count	Chain 1； UniProt 1–1267	Not recorded	major outer-capsid protein mu1 × 60 （P11077） major capsid surface protein sigma-3 × 60 （P07939） guanylyltransferase × 6 （P11079） major core protein lambda 1 × 12 （Q9WAB2） Sigma 2 protein × 18 （P11314）	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
5	Protein heterocomplex Heteromer Protein × 27 PDB declaration: 27-meric（27） Consistent with protein copy count	Chain 1； UniProt 1–1267	Not recorded	major outer-capsid protein mu1 × 10 （P11077） major capsid surface protein sigma-3 × 10 （P07939） guanylyltransferase × 1 （P11079） major core protein lambda 1 × 2 （Q9WAB2） Sigma 2 protein × 3 （P11314）	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

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	VL3_REOVL
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain 1； PDBConstruct 1–1267； UniProt 1–1267

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	2cse
Deposition date deposition_date	2005-05-21
Structure title title	Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution
Keywords keywords	cryoEM, image processing, reovirus, membrane penetration protein, Icosahedral virus, Virus; VIRUS
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	91.15 Å
Radius of gyration Rg (electron density) rg_electron	90.82 Å
Forward intensity I(0) i0	43405900000.00
Molecular weight molecular_weight	1783100.0 kDa
Excluded volume excluded_volume	2185000 Å³
Envelope volume envelope_volume	2708500 Å³
Hydration-shell volume shell_volume	249490 Å³
Envelope diameter envelope_diameter	306.4 Å
Shell Rg shell_rg	89.94 Å
Envelope Rg envelope_rg	86.91 Å
Shape Rg shape_rg	90.52 Å
Total Rg total_rg	90.82 Å
Total atoms total_atoms	—
Residues n_residues	—
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	239.2 Å
Rg (real space) rg_real	87.93 Å
Rg uncertainty (real space) rg_real_error	0.58 Å
I(0) (real space) i0_real	4.1540e+10
I(0) uncertainty (real space) i0_real_error	8.2340e+08
Rg (reciprocal space) rg_reciprocal	91.28 Å
I(0) (reciprocal space) i0_reciprocal	43420000000.0000
Solution quality estimate total_estimate	0.9127
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	98.5 Å
Skewness Skewness skewness	0.174
Kurtosis Kurtosis kurtosis	-0.608
Angular range angular_range	— – 0.0850 Å⁻¹
Current regularization parameter α current_alpha	0.8444
Highest regularization parameter α highest_alpha	3053000000.0000
Real-space data points n_real_points	18
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 1.000; Stabil: 0.956; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	major outer-capsid protein mu1
Molecular weight formula_weight	76346.3 kDa
Source method src_method	nat
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,P,Q,R,J,K,L,T
Atom count atom_count	16111

MGNASSIVQTINVTGDGNVFKPSAETSSTAVPSLSLSPGMLNPGGVPWIAIGDETSVTSPGALRRMTSKDIPETAIINTDNSSGAVPSESALVPYNDEPLVVVTEHAIANFTKAEMALEFNREFLDKLRVLSVSPKYSDLLTYVDCYVGVSARQALNNFQKQVPVITPTRQTMYVDSIQAALKALEKWEIDLRVAQTLLPTNVPIGEVSCPMQSVVKLLDDQLPDDSLIRRYPKEAAVALAKRNGGIQWMDVSEGTVMNEAVNAVAASALAPSASAPPLEEKSKLTEQAMDLVTAAEPEIIASLVPVPAPVFAIPPKPADYNVRTLKIDEATWLRMIPKTMGTLFQIQVTDNTGTNWHFNLRGGTRVVNLDQIAPMRFVLDLGGKSYKETSWDPNGKKVGFIVFQSKIPFELWTAASQIGQATVVNYVQLYAEDSSFTAQSIIATTSLAYNYEPEQLNKTDPEMNYYLLATFIDSAAITPTNMTQPDVWDALLTMSPLSAGEVTVKGAVVSEVVPAELIGSYTPESLNASLPNDAARCMIDRASKIAEAIKIDDDAGPDEYSPNSVPIQGQLAISQLETGYGVRIFNPKGILSKIASRAMQAFIGDPSTIITQAAPVLSDKNNWIALAQGVKTSLRTKSLSAGVKTAVSKLSSSESIQNWTQGFLDKVSTHFPAPKPDCPTNGDGSEPSARRVKRDSYAGVVKRGYTR

Entity 2 Entity 2 polymer

Description description	major capsid surface protein sigma-3
Molecular weight formula_weight	41237.1 kDa
Source method src_method	nat
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	S,D,E,F,M,N,O,G,H,I

MEVCLPNGHQIVDLINNAFEGRVSIYSAQEGWDKTISAQPDMMVCGGAVVCMHCLGVVGSLQRKLKHLPHHRCNQQIRHQDYVDVQFADRVTAHWKRGMLSFVCQMHAMMNDVSPEDLDRVRTEGGSLVELNWLQVDPNSMFRSIHSSWTDPLQVVDDLDTKLDQYWTALNLMIDSSDLVPNFMMRDPSHAFNGVRLEGDARQTQFSRTFDSRSSLEWGVMVYDYSELEHDPSKGRAYRKELVTPARDFGHFGLSHYSRATTPILGKMPAVFSGMLTGNCKMYPFIKGTAKLKTVRKLVDSVNHAWGVEKIRYALGPGGMTGWYNRTMQQAPIVLTPAALTMFSDTTKFGDLDYPVMIGDPMILG

Entity 3 Entity 3 polymer

Description description	guanylyltransferase
Molecular weight formula_weight	144098.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	U

MANVWGVRLADSLSSPTIETRTRQYTLHDLCSDLDANPGREPWKPLRNQRTNNIVAVQLFRPLQGLVLDTQLYGFPGAFDDWERFMREKLRVLKYEVLRIYPISNYSNEHVNVFVANALVGAFLSNQAFYDLLPLLIINDTMIGDLLGTGASLSQFFQSHGDVLEVAAGRKYLQMENYSNDDDDPPLFAKDLSDYAKAFYSDTYEVLDRFFWTHDSSAGVLVHYDKPTNGHHYLLGTLTQMVSAPPYIINATDAMLLESCLEQFSANVRARPAQPVTRLDQCYHLRWGAQYVGEDSLTYRLGVLSLLATNGYQLARPIPRQLTNRWLSSFVSQIMSDGVNETPLWPQERYVQIAYDSPSVVDGATQYGYVRKNQLRLGMRISALQSLSDTPSPVQWLPQYTIDQAAMDEGDLMVSRLTQLPLRPDYGNIWVGDALSYYVDYNRSHRVVLSSELPQLPDTYFDGDEQYGRSLFSLARKIGDRSLVKDTAVLKHAYQAIDPNTGKEYLRSRQSVAYFGASAGHSGADQPLVIEPWIQGKISGVPPPSSVRQFGYDVARGAIVDLARPFPSGDYQFVYSDVDQVVDGHDDLSISSGLVESLLSSCMHATAPGGSFVVKINFPTRPVWHYIEQKILPNITSYMLIKPFVTNNVELFFVAFGVHQHSSLTWTSGVYFFLVDHFYRYETLSTISRQLPSFGYVDDGSSVTGIETISIENPGFSNMTQAARIGISGLCANVGNARKSIAIYESHGARVLTITSRRSPASARRKSRLRYLPLIDPRSLEVQARTILPADPVLFENVSGASPHVCLTMMYNFEVSSAVYDGDVVLDLGTGPEAKILELIPATSPVTCVDIRPTAQPSGCWNVRTTFLELDYLSDGWITGVRGDIVTCMLSLGAAAAGKSMTFDAAFQQLIKVLSKSTANVVLVQVNCPTDVVRSIKGYLEIDSTNKRYRFPKFGRDEPYSDMDALEKICRTAWPNCSITWVPLSYDLRWTRLALLESTTLSSASIRIAELMYKYMPIMRIDIHGLPMEKRGNFIVGQNCSLVIPGFNAQDVFNCYFNSALAFSTEDVNAAMIPQVSAQFDATKGEWTLDMVFSDAGIYTMQALVGSNANPVSLGSFVVDSPDVDITDAWPAQLDFTIAGTDVDITVNPYYRLMTFVRIDGQWQIANPDKFQFFSSASGTLVMNVKLDIADKYLLYYIRDVQSRDVGFYIQHPLQLLNTITLPTNEDLFLSAPDMREWAVKESGNTICILNSQGFVLPQDWDVLTDTISWSPSIPTYIVPPGDYTLTPL

Entity 4 Entity 4 polymer

Description description	major core protein lambda 1
Molecular weight formula_weight	142008.4 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	V,W

MKRIPRKTKGKSSGKGNDSTERSDDGSSQLRDKQNNKAGPATTEPGTSNREQYRARPGIASVQRATESAELPMKNNDEGTPDKKGNTRGDLVNEHSEAKDEADEATQKQAKDTDKSKAQVTYSDTGINNANELSRSGNVDNEGGSNQKPMSTRIAEATSAIVSKHPARVGLPPTASSGHGYQCHVCSAVLFSPLDLDAHVASHGLHGNMTLTSSEIQRHITEFISSWQNHPIVQVSADVENKKTAQLLHADTPRLVTWDAGLCTSFKIVPIVPAQVPQDVLAYTFFTSSYAIQSPFPEAAVSRIVVHTRWASNVDFDRDSSVIMAPPTENNIHLFKQLLNTETLSVRGANPLMFRANVLHMLLEFVLDNLYLNRHTGFSQDHTPFTEGANLRSLPGPDAEKWYSIMYPTRMGTPNVSKICNFVASCVRNRVGRFDRAQMMNGAMSEWVDVFETSDALTVSIRGRWMARLARMNINPTEIEWALTECAQGYVTVTSPYAPSVNRLMPYRISNAERQISQIIRIMNIGNNATVIQPVLQDISVLLQRISPLQIDPTIISNTMSTVSESTTQTLSPASSILGKLRPSNSDFSSFRVALAGWLYNGVVTTVIDDSSYPKDGGSVTSLENLWDFFILALALPLTTDPCAPVKAFMTLANMMVGFETIPMDNQIYTQSRRASAFSTPHTWPRCFMNIQLISPIDAPILRQWAEIIHRYWPNPSQIRYGAPNVFGSANLFTPPEVLLLPIDHQPANVTTPTLDFTNELTNWRARVCELMKNLVDNQRYQPGWTQSLVSSMRGTLDKLKLIKSMTPMYLQQLAPVELAVIAPMLPFPPFQVPYVRLDRDRVPTMVGVTRQSRDTITQPALSLSTTNTTVGVPLALDARAITVALLSGKYPPDLVTNVWYADAIYPMYADTEVFSNLQRDMITCEAVQTLVTLVAQISETQYPVDRYLDWIPSLRASAATAATFAEWVNTSMKTAFDLSDMLLEPLLSGDPRMTQLAIQYQQYNGRTFNVIPEMPGSVIADCVQLTAEVFNHEYNLFGIARGDIIIGRVQSTHLWSPLAPPPDLVFDRDTPGVHIFGRDCRISFGMNGAAPMIRDETGMMVPFEGNWIFPLALWQMNTRYFNQQFDAWIKTGELRIRIEMGAYPYMLHYYDPRQYANAWNLTSAWLEEITPTSIPSVPFMVPISSDHDISSAPAVQYIISTEYNDRSLFCTNSSSPQTIAGPDKHIPVERYNILTNPDAPPTQIQLPEVVDLYNVVTRYAYETPPITAVVMGVP

Entity 5 Entity 5 polymer

Description description	Sigma 2 protein
Molecular weight formula_weight	47155.2 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	X,Y,Z

MARAAFLFKTVGFGGLQNVPINDELSSHLLRAGNSPWQLTQFLDWISLGRGLATSALVPTAGSRYYQMSCLLSGTLQIPFRPNHRWGDIRFLRLVWSAPTLDGLVVAPPQVLAQPALQAQADRVYDCDDYPFLARDPRFKHRVYQQLSAVTLLNLTGFGPISYVRVDEDMWSGDVNQLLMNYFGHTFAEIAYTLCQASANRPWEHDGTYARMTQIILSLFWLSYVGVIHQQNTYRTFYFQCNRRGDAAEVWILSCSLNHSAQIRPGNRSLFVMPTSPDWNMDVNLILSSTLTGCLCSGSQLPLIDNNSVPAVSRNIHGWTGRAGNQLHGFQVRRMVTEFCDRLRRDGVMTQAQQNQIEALADQTQQFKRDKLEAWAREDDQYNQANPNSTMFRTKPFTNAQWGRGNTGATSAAIAALI

Entity 6 Entity 6 polymer

Description description	Minor core protein lambda 3
Molecular weight formula_weight	142510.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	1

MSSMILTQFRPFIESISGITDQSNDVFEDAAKAFSMFTRSDVYKALDEIPFSDDAMLPIPPTIYTKPSHDSYYYIDALNRVRRKTYQGPDDVYVPNCSIVELLEPHETLTSYGRLSEAIENRAKDGDSQARIATTYGRIAESQARQIKAPLEKFVLALLVSEAGGSLYDPVLQKYDEIPDLSHNCPLWCFREICRHISGPLPDRAPYLYLSAGVFWLMSPRMTSAIPPLLSDLVNLAILQQTAGLDPSLVKLGVQICLHAAASSSYAWFILKTKSIFPQNTLHSMYESLEGGYCPNLEWLEPRSDYKFMYMGVMPLSTKYARSAPSNDKKARELGEKYGLSSVVSELRKRTKTYVKHDFASVRYIRDAMACTSGIFLVRTPTETVLQEYTQSPEIKVPIPQKDWTGPVGEIRILKDTTSSIARYLYRTWYLAAARMAAQPRTWDPLFQAIMRSQYVTARGGSGAALRESLYAINVSLPDFKGLPVKAATKIFQAAQLANLPFSHTSVAILADTSMGLRNQVQRRPRSIMPLNVPQQQVSAPHTLTADYINYHMNLSTTSGSAVIEKVIPLGVYASSPPNQSINIDISACDASITWDFFLSVIMAAIHEGVASGSIGKPFMGVPASIVNDESVVGVRAARPISGMQNMIQHLSKLYKRGFSYRVNDSFSPGNDFTHMTTTFPSGSTATSTEHTANNSTMMETFLTVWGPEHTDDPDVLRLMKSLTIQRNYVCQGDDGLMIIDGNTAGKVNSETIQKMLELISKYGEEFGWKYDIAYDGTAEYLKLYFIFGCRIPNLSRHPIVGKERANSSAEEPWPAILDQIMGIFFNGVHDGLQWQRWIRYSWALCCAFSRQRTMIGESVGYLQYPMWSFVYWGLPLVKVFGSDPWIFSWYMPTGDLGMYSWISLIRPLMTRWMVANGYATDRCSPVFGNADYRRCFNEIKLYQGYYMAQLPRNPTKSGRAAPREVREQFTQALSDYLMQNPELKSRVLRGRSEWEKYGAGIIHNPPSLFDVPHKWYLGAQEAATATREELAEMDETLMRARRHSYSSFSKLLEAYLLVKWRMCEAREPSVDLRLPLCAGIDPLNSDPFLKMVSVGPMLQSTRKYFAQTLFMAKTVSGLDVNAIDSALLRLRTLGADKKALTAQLLMVGLQESEADALAGKIMLQDVSTVQLARVVNLAVPDTWMSLDFDSMFKHHVKLLPKDGRHLNTDIPPRMGWLRAILRFLGAGMVMTATGVAVDIYLEDIHGGGRALGQRFMTWMRQEGRSA

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7. Fold Classification (SCOP + CATH) 11 domains

SCOP 2.08 (11 domains)

Domain ID domain_id	d2csed1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamily	d.196.1 — Outer capsid protein sigma 3
Family Family family	d.196.1.1 — Outer capsid protein sigma 3

Domain ID domain_id	d2csee1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamily	d.196.1 — Outer capsid protein sigma 3
Family Family family	d.196.1.1 — Outer capsid protein sigma 3

Domain ID domain_id	d2csef1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamily	d.196.1 — Outer capsid protein sigma 3
Family Family family	d.196.1.1 — Outer capsid protein sigma 3

Domain ID domain_id	d2cseg1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamily	d.196.1 — Outer capsid protein sigma 3
Family Family family	d.196.1.1 — Outer capsid protein sigma 3

Domain ID domain_id	d2cseh1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamily	d.196.1 — Outer capsid protein sigma 3
Family Family family	d.196.1.1 — Outer capsid protein sigma 3

Domain ID domain_id	d2csei1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamily	d.196.1 — Outer capsid protein sigma 3
Family Family family	d.196.1.1 — Outer capsid protein sigma 3

Domain ID domain_id	d2csem1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamily	d.196.1 — Outer capsid protein sigma 3
Family Family family	d.196.1.1 — Outer capsid protein sigma 3

Domain ID domain_id	d2csen1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamily	d.196.1 — Outer capsid protein sigma 3
Family Family family	d.196.1.1 — Outer capsid protein sigma 3

Domain ID domain_id	d2cseo1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamily	d.196.1 — Outer capsid protein sigma 3
Family Family family	d.196.1.1 — Outer capsid protein sigma 3

Domain ID domain_id	d2cses1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamily	d.196.1 — Outer capsid protein sigma 3
Family Family family	d.196.1.1 — Outer capsid protein sigma 3

Domain ID domain_id	d2cseu1
Class class	i — Low resolution protein structures
Fold Fold fold	i.7 — Reovirus components
Superfamily Superfamily superfamily	i.7.1 — Reovirus components
Family Family family	i.7.1.1 — Reovirus components

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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	7.00 Å
Resolution测定方法 resolution_method	PFT, OOR, POR
颗粒数 num_particles	7939

fit	/app/data/saxs_computation/cs/2cse/2cse.fit
pddf	/app/data/pr_computation/cs/2cse/2cse.pr.out
profile	/app/data/saxs_computation/cs/2cse/2cse.dat

Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution

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

major outer-capsid protein mu1

State in the Current Structure

Other States of the Same Protein in the Database

major capsid surface protein sigma-3

State in the Current Structure

Other States of the Same Protein in the Database

guanylyltransferase

State in the Current Structure

Other States of the Same Protein in the Database

major core protein lambda 1

State in the Current Structure

Other States of the Same Protein in the Database

Sigma 2 protein

State in the Current Structure

Other States of the Same Protein in the Database

Minor core protein lambda 3

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 (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

Entity 6 Entity 6 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 11 domains

SCOP 2.08 (11 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)