6tre

Structure of the RBM3/collar region of the Salmonella flagella MS-ring protein FliF with 32-fold symmetry applied

Method: ELECTRON MICROSCOPY Dmax: 212.7 Å Quality: GOOD

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

Flagellar M-ring protein

Salmonella enterica subsp. enterica serovar Typhimurium

UniProt P15928

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain 1; UniProt 1–560 Chain 2; UniProt 1–560 Chain 3; UniProt 1–560 Chain 4; UniProt 1–560 Chain 5; UniProt 1–560 Chain 6; UniProt 1–560 Chain A; UniProt 1–560 Chain B; UniProt 1–560 Chain C; UniProt 1–560 Chain D; UniProt 1–560 Chain E; UniProt 1–560 Chain F; UniProt 1–560 Chain G; UniProt 1–560 Chain H; UniProt 1–560 Chain I; UniProt 1–560 Chain J; UniProt 1–560 Chain K; UniProt 1–560 Chain L; UniProt 1–560 Chain M; UniProt 1–560 Chain N; UniProt 1–560 Chain O; UniProt 1–560 Chain P; UniProt 1–560 Chain Q; UniProt 1–560 Chain R; UniProt 1–560 Chain S; UniProt 1–560 Chain T; UniProt 1–560 Chain U; UniProt 1–560 Chain V; UniProt 1–560 Chain W; UniProt 1–560 Chain X; UniProt 1–560 Chain Y; UniProt 1–560 Chain Z; UniProt 1–560 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

47 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLIF_SALTY
Isoform
PDB entities 1
Chains and sequence ranges Author chain 1; PDBConstruct 1–560; UniProt 1–560 Author chain 2; PDBConstruct 1–560; UniProt 1–560 Author chain 3; PDBConstruct 1–560; UniProt 1–560 Author chain 4; PDBConstruct 1–560; UniProt 1–560 Author chain 5; PDBConstruct 1–560; UniProt 1–560 Author chain 6; PDBConstruct 1–560; UniProt 1–560 Author chain A; PDBConstruct 1–560; UniProt 1–560 Author chain B; PDBConstruct 1–560; UniProt 1–560 Author chain C; PDBConstruct 1–560; UniProt 1–560 Author chain D; PDBConstruct 1–560; UniProt 1–560 Author chain E; PDBConstruct 1–560; UniProt 1–560 Author chain F; PDBConstruct 1–560; UniProt 1–560 Author chain G; PDBConstruct 1–560; UniProt 1–560 Author chain H; PDBConstruct 1–560; UniProt 1–560 Author chain I; PDBConstruct 1–560; UniProt 1–560 Author chain J; PDBConstruct 1–560; UniProt 1–560 Author chain K; PDBConstruct 1–560; UniProt 1–560 Author chain L; PDBConstruct 1–560; UniProt 1–560 Author chain M; PDBConstruct 1–560; UniProt 1–560 Author chain N; PDBConstruct 1–560; UniProt 1–560 Author chain O; PDBConstruct 1–560; UniProt 1–560 Author chain P; PDBConstruct 1–560; UniProt 1–560 Author chain Q; PDBConstruct 1–560; UniProt 1–560 Author chain R; PDBConstruct 1–560; UniProt 1–560 Author chain S; PDBConstruct 1–560; UniProt 1–560 Author chain T; PDBConstruct 1–560; UniProt 1–560 Author chain U; PDBConstruct 1–560; UniProt 1–560 Author chain V; PDBConstruct 1–560; UniProt 1–560 Author chain W; PDBConstruct 1–560; UniProt 1–560 Author chain X; PDBConstruct 1–560; UniProt 1–560 Author chain Y; PDBConstruct 1–560; UniProt 1–560 Author chain Z; PDBConstruct 1–560; UniProt 1–560

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 6tre

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6tre
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6tre
Deposition date deposition_date2019-12-18
Structure title titleStructure of the RBM3/collar region of the Salmonella flagella MS-ring protein FliF with 32-fold symmetry applied
Keywords keywordsFlagella, T3SS, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier80.29
Radius of gyration Rg (electron density) rg_electron81.16
Forward intensity I(0) i04686570000.00
Molecular weight molecular_weight543390.0 kDa
Excluded volume excluded_volume666260 ų
Envelope volume envelope_volume1347800 ų
Hydration-shell volume shell_volume145450 ų
Envelope diameter envelope_diameter230.6
Shell Rg shell_rg83.18
Envelope Rg envelope_rg71.61
Shape Rg shape_rg81.13
Total Rg total_rg81.29
Total atoms total_atoms38176
Residues n_residues4832
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 dmax212.7
Rg (real space) rg_real79.94
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real4.6860e+09
I(0) uncertainty (real space) i0_real_error9.3580e+07
Rg (reciprocal space) rg_reciprocal81.16
I(0) (reciprocal space) i0_reciprocal4698000000.0000
Solution quality estimate total_estimate0.8463
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary134.3
Skewness Skewness skewness-0.094
Kurtosis Kurtosis kurtosis-0.816
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha108800000.0000
Real-space data points n_real_points20
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: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)