8t8p

33-mer FliF MS-ring from Salmonella

Method: ELECTRON MICROSCOPY Dmax: 212.6 Å Quality: REASONABLE

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 × 33 PDB declaration: 33-meric(33) Consistent with protein copy count Chain A; UniProt 1–560 Chain AA; UniProt 1–560 Chain B; UniProt 1–560 Chain BA; UniProt 1–560 Chain C; UniProt 1–560 Chain CA; UniProt 1–560 Chain D; UniProt 1–560 Chain DA; UniProt 1–560 Chain E; UniProt 1–560 Chain EA; UniProt 1–560 Chain F; UniProt 1–560 Chain FA; UniProt 1–560 Chain G; UniProt 1–560 Chain GA; UniProt 1–560 Chain H; UniProt 1–560 Chain HA; 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 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 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 A; PDBConstruct 1–560; UniProt 1–560 Author chain AA; PDBConstruct 1–560; UniProt 1–560 Author chain B; PDBConstruct 1–560; UniProt 1–560 Author chain BA; PDBConstruct 1–560; UniProt 1–560 Author chain C; PDBConstruct 1–560; UniProt 1–560 Author chain CA; PDBConstruct 1–560; UniProt 1–560 Author chain D; PDBConstruct 1–560; UniProt 1–560 Author chain DA; PDBConstruct 1–560; UniProt 1–560 Author chain E; PDBConstruct 1–560; UniProt 1–560 Author chain EA; PDBConstruct 1–560; UniProt 1–560 Author chain F; PDBConstruct 1–560; UniProt 1–560 Author chain FA; PDBConstruct 1–560; UniProt 1–560 Author chain G; PDBConstruct 1–560; UniProt 1–560 Author chain GA; PDBConstruct 1–560; UniProt 1–560 Author chain H; PDBConstruct 1–560; UniProt 1–560 Author chain HA; 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 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 8t8p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t8p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t8p
Deposition date deposition_date2023-06-23
Structure title title33-mer FliF MS-ring from Salmonella
Keywords keywordsMS-ring, Symmetry mismatch, Flagellar component, Membrane protein, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier82.67
Radius of gyration Rg (electron density) rg_electron82.50
Forward intensity I(0) i013618700000.00
Molecular weight molecular_weight920840.0 kDa
Excluded volume excluded_volume1124400 ų
Envelope volume envelope_volume2291400 ų
Hydration-shell volume shell_volume230760 ų
Envelope diameter envelope_diameter244.2
Shell Rg shell_rg89.50
Envelope Rg envelope_rg75.21
Shape Rg shape_rg82.53
Total Rg total_rg82.51
Total atoms total_atoms64845
Residues n_residues9009
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 dmax212.6
Rg (real space) rg_real81.97
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.3580e+10
I(0) uncertainty (real space) i0_real_error2.6730e+08
Rg (reciprocal space) rg_reciprocal84.08
I(0) (reciprocal space) i0_reciprocal13670000000.0000
Solution quality estimate total_estimate0.6170
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary134.3
Skewness Skewness skewness-0.092
Kurtosis Kurtosis kurtosis-0.775
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.0264
Highest regularization parameter α highest_alpha1058000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 0.999; Sysdev: 0.008; Positv: 1.000; Valcen: 0.992; 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)