7m3r

Crystallographic Structure of the Rhombohedral Crystal Form of STMV Grown from Bromide

Method: X-RAY DIFFRACTION Dmax: 178.3 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 homooligomer Homooligomer Protein × 60 PDB declaration: 60-meric(60) Consistent with protein copy count Chain A; UniProt 1–159 Chain B; UniProt 1–159 Chain C; UniProt 1–159 Chain D; UniProt 1–159 Chain E; UniProt 1–159 Chain F; 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 M; UniProt 1–159 Chain N; UniProt 1–159 Chain O; UniProt 1–159 Not recorded BR BROMIDE ION × 573 MG MAGNESIUM ION × 24 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;279 K;Crystals were grown by sitting drop vapor diffusion in Cryschem plates with 0.6 ml reservoirs and 6 to 8 ul drops. The drops were equal amounts of a 5 mg/ml virus stock solution buffered at pH 6.5 with 0.1 M phosphate. The reservoirs were 5% w/v NaBr in 0.1 M phosphate at pH 6.0. Crystallization was at 4 degrees C and the time of development was about 10 days. Resolution 2.10 Å R-free 0.208

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 C; PDBConstruct 1–159; UniProt 1–159 Author chain D; PDBConstruct 1–159; UniProt 1–159 Author chain E; PDBConstruct 1–159; UniProt 1–159 Author chain F; 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 M; PDBConstruct 1–159; UniProt 1–159 Author chain N; PDBConstruct 1–159; UniProt 1–159 Author chain O; 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 7m3r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7m3r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7m3r
Deposition date deposition_date2021-03-18
Structure title titleCrystallographic Structure of the Rhombohedral Crystal Form of STMV Grown from Bromide
Keywords keywordshalide, RNA, twinning, absence, bromide ions, axis ions, ion channel, decapsidation, VIRUS; VIRUS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier58.95
Radius of gyration Rg (electron density) rg_electron58.53
Forward intensity I(0) i01942080000.00
Molecular weight molecular_weight337100.0 kDa
Excluded volume excluded_volume406260 ų
Envelope volume envelope_volume796910 ų
Hydration-shell volume shell_volume112870 ų
Envelope diameter envelope_diameter174.1
Shell Rg shell_rg63.81
Envelope Rg envelope_rg55.08
Shape Rg shape_rg58.47
Total Rg total_rg58.83
Total atoms total_atoms44901
Residues n_residues2915
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 dmax178.3
Rg (real space) rg_real58.72
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real1.9420e+09
I(0) uncertainty (real space) i0_real_error3.9280e+07
Rg (reciprocal space) rg_reciprocal59.10
I(0) (reciprocal space) i0_reciprocal1943000000.0000
Solution quality estimate total_estimate0.8530
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.6
Skewness Skewness skewness0.036
Kurtosis Kurtosis kurtosis-0.779
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha67630000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.985; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.134

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)