2vq0

Capsid structure of Sesbania mosaic virus coat protein deletion mutant rCP(delta 48 to 59)

Method: X-RAY DIFFRACTION Dmax: 88.4 Å Quality: EXCELLENT

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

COAT PROTEIN

SESBANIA MOSAIC VIRUS

UniProt Q9EB06

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 homooligomer Homooligomer Protein × 180 PDB declaration: 180-MERIC(180) Consistent with protein copy count Chain A; UniProt 1–47 Chain A; UniProt 60–268 Chain B; UniProt 1–47 Chain B; UniProt 60–268 Chain C; UniProt 1–47 Chain C; UniProt 60–268 Fragment:RESIDUES 1-47,60-268 CA CALCIUM ION × 180 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;0.2 M LI2SO4 MONOHYDRATE, 0.1 M BISTRIS (PH7.5), 25 % PEG 3350 VAPOUR DIFFUSION, SITTING DROP Resolution 3.60 Å R-free 0.258
2 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–47 Chain A; UniProt 60–268 Chain B; UniProt 1–47 Chain B; UniProt 60–268 Chain C; UniProt 1–47 Chain C; UniProt 60–268 Fragment:RESIDUES 1-47,60-268 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;0.2 M LI2SO4 MONOHYDRATE, 0.1 M BISTRIS (PH7.5), 25 % PEG 3350 VAPOUR DIFFUSION, SITTING DROP Resolution 3.60 Å R-free 0.258
3 Protein homooligomer Homooligomer Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 1–47 Chain A; UniProt 60–268 Chain B; UniProt 1–47 Chain B; UniProt 60–268 Chain C; UniProt 1–47 Chain C; UniProt 60–268 Fragment:RESIDUES 1-47,60-268 CA CALCIUM ION × 15 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;0.2 M LI2SO4 MONOHYDRATE, 0.1 M BISTRIS (PH7.5), 25 % PEG 3350 VAPOUR DIFFUSION, SITTING DROP Resolution 3.60 Å R-free 0.258
4 Protein homooligomer Homooligomer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 1–47 Chain A; UniProt 60–268 Chain B; UniProt 1–47 Chain B; UniProt 60–268 Chain C; UniProt 1–47 Chain C; UniProt 60–268 Fragment:RESIDUES 1-47,60-268 CA CALCIUM ION × 18 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;0.2 M LI2SO4 MONOHYDRATE, 0.1 M BISTRIS (PH7.5), 25 % PEG 3350 VAPOUR DIFFUSION, SITTING DROP Resolution 3.60 Å R-free 0.258
5 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–47 Chain A; UniProt 60–268 Chain B; UniProt 1–47 Chain B; UniProt 60–268 Chain C; UniProt 1–47 Chain C; UniProt 60–268 Fragment:RESIDUES 1-47,60-268 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;0.2 M LI2SO4 MONOHYDRATE, 0.1 M BISTRIS (PH7.5), 25 % PEG 3350 VAPOUR DIFFUSION, SITTING DROP Resolution 3.60 Å R-free 0.258

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.

10 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9EB06_9VIRU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–47; UniProt 1–47 Author chain A; PDBConstruct 48–256; UniProt 60–268 Author chain B; PDBConstruct 1–47; UniProt 1–47 Author chain B; PDBConstruct 48–256; UniProt 60–268 Author chain C; PDBConstruct 1–47; UniProt 1–47 Author chain C; PDBConstruct 48–256; UniProt 60–268

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 2vq0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2vq0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2vq0
Deposition date deposition_date2008-03-10
Structure title titleCapsid structure of Sesbania mosaic virus coat protein deletion mutant rCP(delta 48 to 59)
Keywords keywordsCAPSID PROTEIN, SESBANIA MOSAIC VIRUS, VIRION, BETA-ANNULUS, COAT PROTEIN, VIRUS ASSEMBLY, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier28.28
Radius of gyration Rg (electron density) rg_electron27.16
Forward intensity I(0) i064329200.00
Molecular weight molecular_weight63432.0 kDa
Excluded volume excluded_volume79525 ų
Envelope volume envelope_volume94140 ų
Hydration-shell volume shell_volume29648 ų
Envelope diameter envelope_diameter92.5
Shell Rg shell_rg33.69
Envelope Rg envelope_rg27.73
Shape Rg shape_rg27.16
Total Rg total_rg27.82
Total atoms total_atoms4454
Residues n_residues606
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax88.4
Rg (real space) rg_real28.29
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real6.4330e+07
I(0) uncertainty (real space) i0_real_error1.0330e+06
Rg (reciprocal space) rg_reciprocal28.29
I(0) (reciprocal space) i0_reciprocal64330000.0000
Solution quality estimate total_estimate0.9056
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.0
Skewness Skewness skewness0.290
Kurtosis Kurtosis kurtosis-0.607
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8152000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.955; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2vq0a1
Class classb — All beta proteins
Fold Fold foldb.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamilyb.121.4 — Positive stranded ssRNA viruses
Family Family familyb.121.4.7 — Tombusviridae-like VP
Domain ID domain_idd2vq0b1
Class classb — All beta proteins
Fold Fold foldb.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamilyb.121.4 — Positive stranded ssRNA viruses
Family Family familyb.121.4.7 — Tombusviridae-like VP
Domain ID domain_idd2vq0c1
Class classb — All beta proteins
Fold Fold foldb.121 — Nucleoplasmin-like/VP (viral coat and capsid proteins)
Superfamily Superfamily superfamilyb.121.4 — Positive stranded ssRNA viruses
Family Family familyb.121.4.7 — Tombusviridae-like VP

CATH v4.4 (3 domains)

Domain ID domain_id2vq0A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20
Domain ID domain_id2vq0B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20
Domain ID domain_id2vq0C00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)