7m57

Crystallographic structure of a primitive orthorhombic crystal form of STMV

Method: X-RAY DIFFRACTION Dmax: 173.9 Å Quality: GOOD

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

Coat protein

OrganismNot specified

UniProt P17574

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–RNA Homooligomer Protein × 60 RNA 158 PDB declaration: 218-meric(218) Consistent with all polymer counts Chain A; UniProt 1–159 Chain B; UniProt 1–159 Chain BB; UniProt 1–159 Chain C; UniProt 1–159 Chain CC; UniProt 1–159 Chain D; UniProt 1–159 Chain DD; UniProt 1–159 Chain E; UniProt 1–159 Chain EE; UniProt 1–159 Chain F; UniProt 1–159 Chain FF; UniProt 1–159 Chain G; UniProt 1–159 Chain GG; UniProt 1–159 Chain H; UniProt 1–159 Chain HH; UniProt 1–159 Chain I; UniProt 1–159 Chain II; UniProt 1–159 Chain J; UniProt 1–159 Chain JJ; UniProt 1–159 Chain K; UniProt 1–159 Chain KK; UniProt 1–159 Chain L; UniProt 1–159 Chain LL; UniProt 1–159 Chain M; UniProt 1–159 Chain MM; UniProt 1–159 Chain N; UniProt 1–159 Chain NN; UniProt 1–159 Chain O; UniProt 1–159 Chain OO; UniProt 1–159 Chain PP; UniProt 1–159 Not recorded ;RNA (5'-R(P*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*A)-3') ; × 60 RNA (27-mer) × 98 PO4 PHOSPHATE ION × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;298 K;Crystals were grown by sitting drop vapor diffusion in Cryschem plates using 0.6 ml reservoirs. The drops were 6 to 8 ul and composed of equal volumes of a 5 mg/ml virus stock solution buffered with 0.1 M phosphate at pH 6.5, and the reservoir. The reservoirs were 16% ammonium sulfate buffered at pH 6.0 with 0.1 M phosphate. Crystallization was a room temperature. Resolution 4.00 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.

13 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COAT_STMV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–159; UniProt 1–159 Author chain B; PDBConstruct 1–159; UniProt 1–159 Author chain BB; PDBConstruct 1–159; UniProt 1–159 Author chain C; PDBConstruct 1–159; UniProt 1–159 Author chain CC; PDBConstruct 1–159; UniProt 1–159 Author chain D; PDBConstruct 1–159; UniProt 1–159 Author chain DD; PDBConstruct 1–159; UniProt 1–159 Author chain E; PDBConstruct 1–159; UniProt 1–159 Author chain EE; PDBConstruct 1–159; UniProt 1–159 Author chain F; PDBConstruct 1–159; UniProt 1–159 Author chain FF; PDBConstruct 1–159; UniProt 1–159 Author chain G; PDBConstruct 1–159; UniProt 1–159 Author chain GG; PDBConstruct 1–159; UniProt 1–159 Author chain H; PDBConstruct 1–159; UniProt 1–159 Author chain HH; PDBConstruct 1–159; UniProt 1–159 Author chain I; PDBConstruct 1–159; UniProt 1–159 Author chain II; PDBConstruct 1–159; UniProt 1–159 Author chain J; PDBConstruct 1–159; UniProt 1–159 Author chain JJ; PDBConstruct 1–159; UniProt 1–159 Author chain K; PDBConstruct 1–159; UniProt 1–159 Author chain KK; PDBConstruct 1–159; UniProt 1–159 Author chain L; PDBConstruct 1–159; UniProt 1–159 Author chain LL; PDBConstruct 1–159; UniProt 1–159 Author chain M; PDBConstruct 1–159; UniProt 1–159 Author chain MM; PDBConstruct 1–159; UniProt 1–159 Author chain N; PDBConstruct 1–159; UniProt 1–159 Author chain NN; PDBConstruct 1–159; UniProt 1–159 Author chain O; PDBConstruct 1–159; UniProt 1–159 Author chain OO; PDBConstruct 1–159; UniProt 1–159 Author chain PP; PDBConstruct 1–159; UniProt 1–159

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 7m57

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7m57
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7m57
Deposition date deposition_date2021-03-22
Structure title titleCrystallographic structure of a primitive orthorhombic crystal form of STMV
Keywords keywordsVIRUS/RNA, VIRUS-RNA complex; VIRUS/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier63.25
Radius of gyration Rg (electron density) rg_electron64.43
Forward intensity I(0) i06237530000.00
Molecular weight molecular_weight581700.0 kDa
Excluded volume excluded_volume692610 ų
Envelope volume envelope_volume1321200 ų
Hydration-shell volume shell_volume166050 ų
Envelope diameter envelope_diameter182.9
Shell Rg shell_rg73.74
Envelope Rg envelope_rg60.30
Shape Rg shape_rg64.52
Total Rg total_rg64.32
Total atoms total_atoms40402
Residues n_residues4654
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 dmax173.9
Rg (real space) rg_real62.81
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real6.2380e+09
I(0) uncertainty (real space) i0_real_error1.1000e+08
Rg (reciprocal space) rg_reciprocal63.57
I(0) (reciprocal space) i0_reciprocal6245000000.0000
Solution quality estimate total_estimate0.8464
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary90.5
Skewness Skewness skewness-0.009
Kurtosis Kurtosis kurtosis-0.777
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha416800000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)