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9x7m

core filament of the spirochete periplasmic flagella of Leptospira biflexa from the deleted fcpB_CL13 strain

Method: ELECTRON MICROSCOPY Dmax: 184.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Flagellin

OrganismNot specified

UniProt B0SSZ5

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 × 11 PDB declaration: undecameric（11） Consistent with protein copy count Chain A； UniProt 1–281 Chain B； UniProt 1–281 Chain C； UniProt 1–281 Chain D； UniProt 1–281 Chain E； UniProt 1–281 Chain F； UniProt 1–281 Chain G； UniProt 1–281 Chain H； UniProt 1–281 Chain I； UniProt 1–281 Chain J； UniProt 1–281 Chain K； UniProt 1–281 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.20 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.

Other PDB Difference from Current Entry 9X7M Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6PWB Rigid body fitting of flagellin FlaB, and flagellar coiling proteins, FcpA and FcpB, into a 10 Angstrom structure of the asymmetric flagellar filament purified from Leptospira biflexa Patoc WT cells resolved via subtomogram averaging Deposited 2019-07-22 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 163 PDB declaration: 163-meric
Chain AG 8–272（265 aa）
Chain AH 8–272（265 aa）
Chain AI 8–272（265 aa）
Chain AR 8–272（265 aa）
Chain BA 8–272（265 aa）
Chain BB 8–272（265 aa）
Chain BC 8–272（265 aa）
Chain BD 8–272（265 aa）
Chain BL 8–272（265 aa）
Chain BM 8–272（265 aa）
Chain BS 8–272（265 aa）
Chain BT 8–272（265 aa）
Chain BU 8–272（265 aa）
Chain BV 8–272（265 aa）
Chain BW 8–272（265 aa）
Chain BX 8–272（265 aa）
Chain BY 8–272（265 aa）
Chain CG 8–272（265 aa）
Chain CH 8–272（265 aa）
Chain CL 8–272（265 aa）
Chain CM 8–272（265 aa）
Chain CN 8–272（265 aa）
Chain CO 8–272（265 aa）
Chain CP 8–272（265 aa）
Chain CQ 8–272（265 aa）
Chain CR 8–272（265 aa）
Chain CS 8–272（265 aa）
Chain CT 8–272（265 aa）
Chain DB 8–272（265 aa）
Chain DC 8–272（265 aa）
Chain DG 8–272（265 aa）
Chain DH 8–272（265 aa）
Chain DI 8–272（265 aa）
Chain DJ 8–272（265 aa）
Chain DK 8–272（265 aa）
Chain DL 8–272（265 aa）
Chain DM 8–272（265 aa）
Chain DN 8–272（265 aa）
Chain DO 8–272（265 aa）
Chain DW 8–272（265 aa）
Chain DX 8–272（265 aa）
Chain EB 8–272（265 aa）
Chain EC 8–272（265 aa）
Chain ED 8–272（265 aa）
Chain EE 8–272（265 aa）
Chain EF 8–272（265 aa）
Chain EG 8–272（265 aa）
Chain EH 8–272（265 aa）
Chain EI 8–272（265 aa）
Chain EJ 8–272（265 aa）
Chain ER 8–272（265 aa）
Chain ES 8–272（265 aa）
Chain EW 8–272（265 aa）
Chain EX 8–272（265 aa）
Chain EY 8–272（265 aa）
Chain EZ 8–272（265 aa）
Chain FA 8–272（265 aa）
Chain FB 8–272（265 aa）
Chain FC 8–272（265 aa）
Chain FD 8–272（265 aa）
Chain FE 8–272（265 aa）
Chain FM 8–272（265 aa）
Chain FN 8–272（265 aa）
Chain FR 8–272（265 aa）
Chain FS 8–272（265 aa）
Chain FT 8–272（265 aa）
Chain FU 8–272（265 aa）
Chain FV 8–272（265 aa）
Chain FW 8–272（265 aa）
Chain FX 8–272（265 aa）
Chain GH 8–272（265 aa）
Chain GI 8–272（265 aa）
Chain GM 8–272（265 aa）
Chain GN 8–272（265 aa）
Chain GO 8–272（265 aa）
Chain GP 8–272（265 aa）
Chain GQ 8–272（265 aa）
Chain GR 8–272（265 aa）
Chain HC 8–272（265 aa）
Chain HH 8–272（265 aa）
Chain HI 8–272（265 aa）
Chain HJ 8–272（265 aa）
Chain HK 8–272（265 aa）
Chain HL 8–272（265 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8；Tris-HCl or ddH20, pH6.8 with <1% sodium azide as a preservative. FIDUCIAL MARKERS: Prior to vitrification, 1 uL of 6x concentrated Gold Tracer beads (10 nm colloidal gold) were mixed with 2 uL of purified flagella. To each grid, 3 uL of this mixture were applied.
cryo-EM vitrification conditions Cryogen ETHANE；2 minute incubation time; blot time of 6-7.5 seconds; and blot offset of -2 mm
Resolution 9.83 Å
9X7K core filament of the spirochete periplasmic flagella of Leptospira biflexa wild type Deposited 2025-10-17 Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 11 PDB declaration: undecameric
Chain A 1–281（281 aa）
Chain B 1–281（281 aa）
Chain C 1–281（281 aa）
Chain D 1–281（281 aa）
Chain E 1–281（281 aa）
Chain F 1–281（281 aa）
Chain G 1–281（281 aa）
Chain H 1–281（281 aa）
Chain I 1–281（281 aa）
Chain J 1–281（281 aa）
Chain K 1–281（281 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.35 Å
9X7L core filament of the spirochete periplasmic flagella of Leptospira biflexa from the flaA2-complemented stain Deposited 2025-10-17 Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 11 PDB declaration: undecameric
Chain A 1–281（281 aa）
Chain B 1–281（281 aa）
Chain C 1–281（281 aa）
Chain D 1–281（281 aa）
Chain E 1–281（281 aa）
Chain F 1–281（281 aa）
Chain G 1–281（281 aa）
Chain H 1–281（281 aa）
Chain I 1–281（281 aa）
Chain J 1–281（281 aa）
Chain K 1–281（281 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.32 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B0SSZ5_LEPBP
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–281； UniProt 1–281 Author chain B； PDBConstruct 1–281； UniProt 1–281 Author chain C； PDBConstruct 1–281； UniProt 1–281 Author chain D； PDBConstruct 1–281； UniProt 1–281 Author chain E； PDBConstruct 1–281； UniProt 1–281 Author chain F； PDBConstruct 1–281； UniProt 1–281 Author chain G； PDBConstruct 1–281； UniProt 1–281 Author chain H； PDBConstruct 1–281； UniProt 1–281 Author chain I； PDBConstruct 1–281； UniProt 1–281 Author chain J； PDBConstruct 1–281； UniProt 1–281 Author chain K； PDBConstruct 1–281； UniProt 1–281

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 9x7m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x7m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9x7m
Deposition date deposition_date2025-10-17
Structure title titlecore filament of the spirochete periplasmic flagella of Leptospira biflexa from the deleted fcpB_CL13 strain
Keywords keywordsFilament, Flagellar motor, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier58.45 Å
Radius of gyration Rg (electron density) rg_electron58.23 Å
Forward intensity I(0) i01896330000.00
Molecular weight molecular_weight341630.0 kDa
Excluded volume excluded_volume419670 ų
Envelope volume envelope_volume796970 ų
Hydration-shell volume shell_volume116370 ų
Envelope diameter envelope_diameter199.5 Å
Shell Rg shell_rg62.41 Å
Envelope Rg envelope_rg53.84 Å
Shape Rg shape_rg58.22 Å
Total Rg total_rg58.36 Å
Total atoms total_atoms23892
Residues n_residues3080
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax184.1 Å
Rg (real space) rg_real58.04 Å
Rg uncertainty (real space) rg_real_error1.33 Å
I(0) (real space) i0_real1.8960e+09
I(0) uncertainty (real space) i0_real_error3.4940e+07
Rg (reciprocal space) rg_reciprocal58.78 Å
I(0) (reciprocal space) i0_reciprocal1898000000.0000
Solution quality estimate total_estimate0.8504
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary88.6 Å
Skewness Skewness skewness-0.018
Kurtosis Kurtosis kurtosis-0.383
Angular range angular_range— – 0.1350 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha125900000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.761; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.810
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)