6sd2

Structure of the RBM2inner region of the Salmonella flagella MS-ring protein FliF with 21-fold symmetry applied.

Method: ELECTRON MICROSCOPY Dmax: 166.0 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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain A; UniProt 1–560 Chain C; UniProt 1–560 Chain D; UniProt 1–560 Chain F; UniProt 1–560 Chain G; UniProt 1–560 Chain I; UniProt 1–560 Chain J; UniProt 1–560 Chain L; UniProt 1–560 Chain N; UniProt 1–560 Chain O; UniProt 1–560 Chain Q; UniProt 1–560 Chain R; UniProt 1–560 Chain T; UniProt 1–560 Chain U; UniProt 1–560 Chain W; UniProt 1–560 Chain Y; UniProt 1–560 Chain Z; UniProt 1–560 Chain b; UniProt 1–560 Chain c; UniProt 1–560 Chain e; UniProt 1–560 Chain f; UniProt 1–560 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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 C; PDBConstruct 1–560; UniProt 1–560 Author chain D; 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 I; PDBConstruct 1–560; UniProt 1–560 Author chain J; PDBConstruct 1–560; UniProt 1–560 Author chain L; 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 Q; PDBConstruct 1–560; UniProt 1–560 Author chain R; 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 W; PDBConstruct 1–560; UniProt 1–560 Author chain Y; PDBConstruct 1–560; UniProt 1–560 Author chain Z; 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 e; PDBConstruct 1–560; UniProt 1–560 Author chain f; 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 6sd2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6sd2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6sd2
Deposition date deposition_date2019-07-26
Structure title titleStructure of the RBM2inner region of the Salmonella flagella MS-ring protein FliF with 21-fold symmetry applied.
Keywords keywordsFlagella, Secretion, Rotor, MS-ring, C-ring, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.84
Radius of gyration Rg (electron density) rg_electron59.31
Forward intensity I(0) i0534845000.00
Molecular weight molecular_weight192770.0 kDa
Excluded volume excluded_volume240830 ų
Envelope volume envelope_volume389740 ų
Hydration-shell volume shell_volume52742 ų
Envelope diameter envelope_diameter157.0
Shell Rg shell_rg69.97
Envelope Rg envelope_rg54.93
Shape Rg shape_rg59.30
Total Rg total_rg59.55
Total atoms total_atoms13566
Residues n_residues1848
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 dmax166.0
Rg (real space) rg_real59.58
Rg uncertainty (real space) rg_real_error1.45
I(0) (real space) i0_real5.3480e+08
I(0) uncertainty (real space) i0_real_error1.0150e+07
Rg (reciprocal space) rg_reciprocal59.99
I(0) (reciprocal space) i0_reciprocal535200000.0000
Solution quality estimate total_estimate0.5400
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary102.1
Skewness Skewness skewness-0.188
Kurtosis Kurtosis kurtosis-1.046
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10630000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.784; Stabil: 1.000; Sysdev: 0.001; Positv: 1.000; Valcen: 0.658; 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)