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1jmu

Crystal Structure of the Reovirus mu1/sigma3 Complex

Method: X-RAY DIFFRACTION Dmax: 147.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN MU-1

Reovirus sp.

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 A； UniProt 1–41 Chain B； UniProt 43–708 Chain C； UniProt 1–41 Chain D； UniProt 43–708 Chain E； UniProt 1–41 Chain F； UniProt 43–708 Fragment：N-terminus (residues 2-42) Fragment：C-terminus (residues 43-708) SIGMA 3 PROTEIN × 3 （Q86292） 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

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 1JMU 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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
6XF8 DLP 5 fold Deposited 2020-06-15 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 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 ligand/ion Different experimental method 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 ligand/ion Different experimental method 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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VM2_REOVL
Isoform —
PDB entities 1, 2
Chains and sequence ranges Author chain A； PDBConstruct 1–41； UniProt 1–41 Author chain C； PDBConstruct 1–41； UniProt 1–41 Author chain E； PDBConstruct 1–41； UniProt 1–41 Author chain B； PDBConstruct 1–666； UniProt 43–708 Author chain D； PDBConstruct 1–666； UniProt 43–708 Author chain F； PDBConstruct 1–666； UniProt 43–708

SIGMA 3 PROTEIN

Reovirus sp.

UniProt Q86292

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 Mutation：A104C Non-standard monomer：Yes (specific site not provided by mmCIF) PROTEIN MU-1 × 3 （P11077） PROTEIN MU-1 × 3 （P11077） 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

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 Q86292_9REOV
Isoform —
PDB entities 3
Chains and sequence ranges Author chain G； PDBConstruct 2–366； UniProt 1–365 Author chain H； PDBConstruct 2–366； UniProt 1–365 Author chain I； PDBConstruct 2–366； UniProt 1–365

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 1jmu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1jmu
Deposition date deposition_date2001-07-20
Structure title titleCrystal Structure of the Reovirus mu1/sigma3 Complex
Keywords keywordsProtein-protein complex, jelly roll, zinc finger, Viral protein; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier45.14 Å
Radius of gyration Rg (electron density) rg_electron44.38 Å
Forward intensity I(0) i01612900000.00
Molecular weight molecular_weight333390.0 kDa
Excluded volume excluded_volume417130 ų
Envelope volume envelope_volume518260 ų
Hydration-shell volume shell_volume93455 ų
Envelope diameter envelope_diameter152.4 Å
Shell Rg shell_rg51.61 Å
Envelope Rg envelope_rg44.33 Å
Shape Rg shape_rg44.37 Å
Total Rg total_rg44.66 Å
Total atoms total_atoms23386
Residues n_residues3018
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 dmax147.8 Å
Rg (real space) rg_real44.96 Å
Rg uncertainty (real space) rg_real_error0.93 Å
I(0) (real space) i0_real1.6130e+09
I(0) uncertainty (real space) i0_real_error2.5410e+07
Rg (reciprocal space) rg_reciprocal45.14 Å
I(0) (reciprocal space) i0_reciprocal1613000000.0000
Solution quality estimate total_estimate0.8776
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.1 Å
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.324
Angular range angular_range— – 0.1750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha273000000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.867
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (8)

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7. Fold Classification (SCOP + CATH) 24 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1jmu.1
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.35 — Membrane penetration protein mu1
Superfamily Superfamily superfamilye.35.1 — Membrane penetration protein mu1
Family Family familye.35.1.1 — Membrane penetration protein mu1
Domain ID domain_idd1jmu.2
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.35 — Membrane penetration protein mu1
Superfamily Superfamily superfamilye.35.1 — Membrane penetration protein mu1
Family Family familye.35.1.1 — Membrane penetration protein mu1
Domain ID domain_idd1jmu.3
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.35 — Membrane penetration protein mu1
Superfamily Superfamily superfamilye.35.1 — Membrane penetration protein mu1
Family Family familye.35.1.1 — Membrane penetration protein mu1
Domain ID domain_idd1jmug_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamilyd.196.1 — Outer capsid protein sigma 3
Family Family familyd.196.1.1 — Outer capsid protein sigma 3
Domain ID domain_idd1jmuh_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamilyd.196.1 — Outer capsid protein sigma 3
Family Family familyd.196.1.1 — Outer capsid protein sigma 3
Domain ID domain_idd1jmui_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.196 — Outer capsid protein sigma 3
Superfamily Superfamily superfamilyd.196.1 — Outer capsid protein sigma 3
Family Family familyd.196.1.1 — Outer capsid protein sigma 3

CATH v4.4 (18 domains)

Domain ID domain_id1jmuB01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1370 — Protein mu-1, chain B, domain 1
Homologous superfamily homologous superfamily10 — Protein mu-1, chain B, domain 1
Domain ID domain_id1jmuB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology2040 — Protein mu-1, chain B, domain 2
Homologous superfamily homologous superfamily10 — Protein mu-1, chain B, domain 2
Domain ID domain_id1jmuB03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology2050 — Protein mu-1, chain B, domain 3
Homologous superfamily homologous superfamily10 — Protein mu-1, chain B, domain 3
Domain ID domain_id1jmuB04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily420 — Membrane penetration protein mu1, Chain B, domain 4
Domain ID domain_id1jmuD01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1370 — Protein mu-1, chain B, domain 1
Homologous superfamily homologous superfamily10 — Protein mu-1, chain B, domain 1
Domain ID domain_id1jmuD02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology2040 — Protein mu-1, chain B, domain 2
Homologous superfamily homologous superfamily10 — Protein mu-1, chain B, domain 2
Domain ID domain_id1jmuD03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology2050 — Protein mu-1, chain B, domain 3
Homologous superfamily homologous superfamily10 — Protein mu-1, chain B, domain 3
Domain ID domain_id1jmuD04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily420 — Membrane penetration protein mu1, Chain B, domain 4
Domain ID domain_id1jmuF01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1370 — Protein mu-1, chain B, domain 1
Homologous superfamily homologous superfamily10 — Protein mu-1, chain B, domain 1
Domain ID domain_id1jmuF02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology2040 — Protein mu-1, chain B, domain 2
Homologous superfamily homologous superfamily10 — Protein mu-1, chain B, domain 2
Domain ID domain_id1jmuF03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology2050 — Protein mu-1, chain B, domain 3
Homologous superfamily homologous superfamily10 — Protein mu-1, chain B, domain 3
Domain ID domain_id1jmuF04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily420 — Membrane penetration protein mu1, Chain B, domain 4
Domain ID domain_id1jmuG01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1630 — Outer-capsid protein sigma 3, small lobe
Homologous superfamily homologous superfamily10 — Outer-capsid protein sigma 3, small lobe
Domain ID domain_id1jmuG02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1320 — Outer-capsid protein sigma 3, large lobe
Homologous superfamily homologous superfamily10 — Outer-capsid protein sigma 3, large lobe
Domain ID domain_id1jmuH01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1630 — Outer-capsid protein sigma 3, small lobe
Homologous superfamily homologous superfamily10 — Outer-capsid protein sigma 3, small lobe
Domain ID domain_id1jmuH02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1320 — Outer-capsid protein sigma 3, large lobe
Homologous superfamily homologous superfamily10 — Outer-capsid protein sigma 3, large lobe
Domain ID domain_id1jmuI01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1630 — Outer-capsid protein sigma 3, small lobe
Homologous superfamily homologous superfamily10 — Outer-capsid protein sigma 3, small lobe
Domain ID domain_id1jmuI02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1320 — Outer-capsid protein sigma 3, large lobe
Homologous superfamily homologous superfamily10 — Outer-capsid protein sigma 3, large lobe
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8. Citations (1)

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9. Files and Curves (10)