SAXSdb — 9x7s

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

Flagellin

OrganismNot specified

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 heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain A； UniProt 1–282 Chain D； UniProt 1–282 Chain G； UniProt 1–282 Chain J； UniProt 1–282 Chain M； UniProt 1–282 Chain P； UniProt 1–282 Chain S； UniProt 1–282 Chain V； UniProt 1–282 Chain Y； UniProt 1–282 Chain b； UniProt 1–282 Chain e； UniProt 1–282	Not recorded	Bacterial flagellar sheath protein × 7 （B0STJ8） Bacterial flagellar sheath protein × 6 （B0SR03）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.83 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 9X7S	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9X7V Sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the deleted fcpB_CL13 strain Deposited 2025-10-17	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain A 1–282（282 aa） Chain D 1–282（282 aa） Chain G 1–282（282 aa） Chain J 1–282（282 aa） Chain M 1–282（282 aa） Chain P 1–282（282 aa） Chain S 1–282（282 aa） Chain V 1–282（282 aa） Chain Y 1–282（282 aa） Chain b 1–282（282 aa） Chain e 1–282（282 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
9X80 sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa wild type Deposited 2025-10-18	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 23 PDB declaration: 23-meric	Chain A 1–282（282 aa） Chain D 1–282（282 aa） Chain G 1–282（282 aa） Chain J 1–282（282 aa） Chain M 1–282（282 aa） Chain P 1–282（282 aa） Chain S 1–282（282 aa） Chain V 1–282（282 aa） Chain Y 1–282（282 aa） Chain b 1–282（282 aa） Chain e 1–282（282 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	B0SQZ5_LEPBP
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–282； UniProt 1–282 Author chain D； PDBConstruct 1–282； UniProt 1–282 Author chain G； PDBConstruct 1–282； UniProt 1–282 Author chain J； PDBConstruct 1–282； UniProt 1–282 Author chain M； PDBConstruct 1–282； UniProt 1–282 Author chain P； PDBConstruct 1–282； UniProt 1–282 Author chain S； PDBConstruct 1–282； UniProt 1–282 Author chain V； PDBConstruct 1–282； UniProt 1–282 Author chain Y； PDBConstruct 1–282； UniProt 1–282 Author chain b； PDBConstruct 1–282； UniProt 1–282 Author chain e； PDBConstruct 1–282； UniProt 1–282

Bacterial flagellar sheath protein

OrganismNot specified

UniProt B0STJ8

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 heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain B； UniProt 1–300 Chain K； UniProt 1–300 Chain N； UniProt 1–300 Chain Q； UniProt 1–300 Chain Z； UniProt 1–300 Chain c； UniProt 1–300 Chain f； UniProt 1–300	Not recorded	Flagellin × 11 （B0SQZ5） Bacterial flagellar sheath protein × 6 （B0SR03）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.83 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 9X7S	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6NQW Flagellar protein FcpA from Leptospira biflexa - hexagonal form Deposited 2019-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 34–300（267 aa）	Not recorded	GOL GLYCEROL × 40 PO4 PHOSPHATE ION × 12 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；293 K；PEG 8000, Na/K phosphate, NaCl	Resolution 1.90 Å R-free 0.219
6NQX Flagellar protein FcpA from Leptospira biflexa / primitive monoclinic form Deposited 2019-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 34–300（267 aa） Fragment：residues 34-300 Chain B 34–300（267 aa） Fragment：residues 34-300 Chain C 34–300（267 aa） Fragment：residues 34-300 Chain D 34–300（267 aa） Fragment：residues 34-300	Not recorded	GOL GLYCEROL × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG 4000, TrisHCl	Resolution 2.95 Å R-free 0.222
6NQY Flagellar protein FcpA from Leptospira biflexa / ab-centered monoclinic form Deposited 2019-01-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 34–300（267 aa） Fragment：residues 34-300 Chain B 34–300（267 aa） Fragment：residues 34-300	Not recorded	GOL GLYCEROL × 4 IOD IODIDE ION × 29 PEG DI(HYDROXYETHYL)ETHER × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；PEG 400, TrisHCl	Resolution 2.50 Å R-free 0.221
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 AL 55–291（237 aa） Chain AM 55–291（237 aa） Chain AU 55–291（237 aa） Chain BE 55–291（237 aa） Chain BF 55–291（237 aa） Chain BG 55–291（237 aa） Chain BH 55–291（237 aa） Chain BN 55–291（237 aa） Chain BP 55–291（237 aa） Chain BZ 55–291（237 aa） Chain CA 55–291（237 aa） Chain CB 55–291（237 aa） Chain CC 55–291（237 aa） Chain CI 55–291（237 aa） Chain CK 55–291（237 aa） Chain CU 55–291（237 aa） Chain CV 55–291（237 aa） Chain CW 55–291（237 aa） Chain CX 55–291（237 aa） Chain DD 55–291（237 aa） Chain DF 55–291（237 aa） Chain DP 55–291（237 aa） Chain DQ 55–291（237 aa） Chain DR 55–291（237 aa） Chain DS 55–291（237 aa） Chain DY 55–291（237 aa） Chain EA 55–291（237 aa） Chain EK 55–291（237 aa） Chain EL 55–291（237 aa） Chain EM 55–291（237 aa） Chain EN 55–291（237 aa） Chain ET 55–291（237 aa） Chain EV 55–291（237 aa） Chain FF 55–291（237 aa） Chain FG 55–291（237 aa） Chain FH 55–291（237 aa） Chain FI 55–291（237 aa） Chain FO 55–291（237 aa） Chain FQ 55–291（237 aa） Chain GA 55–291（237 aa） Chain GB 55–291（237 aa） Chain GC 55–291（237 aa） Chain GJ 55–291（237 aa） Chain GL 55–291（237 aa） Chain GV 55–291（237 aa） Chain GW 55–291（237 aa） Chain HE 55–291（237 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
9X7V Sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the deleted fcpB_CL13 strain Deposited 2025-10-17	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric	Chain B 1–300（300 aa） Chain K 1–300（300 aa） Chain N 1–300（300 aa） Chain Q 1–300（300 aa） Chain Z 1–300（300 aa） Chain c 1–300（300 aa） Chain f 1–300（300 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
9X80 sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa wild type Deposited 2025-10-18	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 23 PDB declaration: 23-meric	Chain K 1–300（300 aa） Chain N 1–300（300 aa） Chain Q 1–300（300 aa） Chain Z 1–300（300 aa） Chain c 1–300（300 aa） Chain f 1–300（300 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	B0STJ8_LEPBP
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–300； UniProt 1–300 Author chain K； PDBConstruct 1–300； UniProt 1–300 Author chain N； PDBConstruct 1–300； UniProt 1–300 Author chain Q； PDBConstruct 1–300； UniProt 1–300 Author chain Z； PDBConstruct 1–300； UniProt 1–300 Author chain c； PDBConstruct 1–300； UniProt 1–300 Author chain f； PDBConstruct 1–300； UniProt 1–300

Bacterial flagellar sheath protein

OrganismNot specified

UniProt B0SR03

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 heterocomplex Heteromer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain L； UniProt 1–277 Chain O； UniProt 1–277 Chain R； UniProt 1–277 Chain a； UniProt 1–277 Chain d； UniProt 1–277 Chain g； UniProt 1–277	Not recorded	Flagellin × 11 （B0SQZ5） Bacterial flagellar sheath protein × 7 （B0STJ8）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.83 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 9X7S	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 AO 37–257（221 aa） Chain BI 37–257（221 aa） Chain BJ 37–257（221 aa） Chain BK 37–257（221 aa） Chain BO 37–257（221 aa） Chain CD 37–257（221 aa） Chain CE 37–257（221 aa） Chain CF 37–257（221 aa） Chain CJ 37–257（221 aa） Chain CY 37–257（221 aa） Chain CZ 37–257（221 aa） Chain DA 37–257（221 aa） Chain DE 37–257（221 aa） Chain DT 37–257（221 aa） Chain DU 37–257（221 aa） Chain DV 37–257（221 aa） Chain DZ 37–257（221 aa） Chain EO 37–257（221 aa） Chain EP 37–257（221 aa） Chain EQ 37–257（221 aa） Chain EU 37–257（221 aa） Chain FJ 37–257（221 aa） Chain FK 37–257（221 aa） Chain FL 37–257（221 aa） Chain FP 37–257（221 aa） Chain GE 37–257（221 aa） Chain GF 37–257（221 aa） Chain GG 37–257（221 aa） Chain GK 37–257（221 aa） Chain GZ 37–257（221 aa） Chain HB 37–257（221 aa） Chain HF 37–257（221 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
9LRY Straight and symmetrical filament of the spirochete periplasmic flagella of Leptospira biflexa Deposited 2025-02-02	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–277（277 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
9X80 sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa wild type Deposited 2025-10-18	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 23 PDB declaration: 23-meric	Chain L 1–277（277 aa） Chain O 1–277（277 aa） Chain R 1–277（277 aa） Chain a 1–277（277 aa） Chain d 1–277（277 aa） Chain g 1–277（277 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å

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

View Construct and Data Evidence

UniProt name	B0SR03_LEPBP
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain L； PDBConstruct 1–277； UniProt 1–277 Author chain O； PDBConstruct 1–277； UniProt 1–277 Author chain R； PDBConstruct 1–277； UniProt 1–277 Author chain a； PDBConstruct 1–277； UniProt 1–277 Author chain d； PDBConstruct 1–277； UniProt 1–277 Author chain g； PDBConstruct 1–277； UniProt 1–277

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9x7s
Deposition date deposition_date	2025-10-17
Structure title title	sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the flaA2-complemented stain
Keywords keywords	Filament, Flagellar motor, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	76.93 Å
Radius of gyration Rg (electron density) rg_electron	76.82 Å
Forward intensity I(0) i0	7410790000.00
Molecular weight molecular_weight	715470.0 kDa
Excluded volume excluded_volume	890320 Å³
Envelope volume envelope_volume	1802800 Å³
Hydration-shell volume shell_volume	193070 Å³
Envelope diameter envelope_diameter	239.1 Å
Shell Rg shell_rg	81.37 Å
Envelope Rg envelope_rg	71.73 Å
Shape Rg shape_rg	76.84 Å
Total Rg total_rg	76.83 Å
Total atoms total_atoms	50274
Residues n_residues	6218
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	250.3 Å
Rg (real space) rg_real	76.57 Å
Rg uncertainty (real space) rg_real_error	2.31 Å
I(0) (real space) i0_real	7.4110e+09
I(0) uncertainty (real space) i0_real_error	1.8570e+08
Rg (reciprocal space) rg_reciprocal	78.01 Å
I(0) (reciprocal space) i0_reciprocal	7432000000.0000
Solution quality estimate total_estimate	0.8496
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	100.1 Å
Skewness Skewness skewness	0.010
Kurtosis Kurtosis kurtosis	-0.633
Angular range angular_range	— – 0.1000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	612500000.0000
Real-space data points n_real_points	21
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.505

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Flagellin
Molecular weight formula_weight	31415.6 kDa
Source method src_method	nat
Copy count entity_count	11

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D,G,J,M,P,S,V,Y,b,e
Atom count atom_count	50274

MIINHNVSAIFAHRTLKSNDANLSKDIEKLSSGMRINKAGDDASGLAVSEKMRTQIAGLRRAEQNTEDGMSLIQTAEGYLQETHEIVQRVRVLAVQAANGIYSEEDRQQIQVEVSQLVDEIDRIASQAEFNKMKLLTGAFARLNPTASMWFHIGANMHQRERVYIETMNTAALGLRNPTVLTFISLSTAGKANSVIGLCDDALRVISKQRADLGAYYNRMEHAAKGLMNAYENTQASESRIRDTDMAEQMTSFTRYQILTQAATSMLAQANMKSQSVMRLLQ

Entity 2 Entity 2 polymer

Description description	Bacterial flagellar sheath protein
Molecular weight formula_weight	35876.8 kDa
Source method src_method	nat
Copy count entity_count	7

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,K,N,Q,Z,c,f

MKIIKYLLILQLVSGFSVLFAQTQPANAQESQAAKDQVDELLKGELVPENDDAELTEDQKKKKKEIMEQESLWKNPDFKGYNKTFQELHQLSKTFANNQFRLALSNYQSGVNTIMKNRDWVEQYRKEEAEKKRLDEKWYWQKVDRKAREERVVYREKMKAKQDALNYFSKAINHLDEIKNPDLRERPEFKRLLSDVYRSWIMAEYDLQNLPQTIPILELYIEIDDNEKEYPAHKYLASAYSFEENMIKKTKGPDDMLFKYRYKKNVHLLRATELKYGKDSPEYKHIVNVINRDEVISVAQ

Entity 3 Entity 3 polymer

Description description	Bacterial flagellar sheath protein
Molecular weight formula_weight	31565.7 kDa
Source method src_method	nat
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L,O,R,a,d,g

MKIKLILPILLLSIGVFAQTGSSETGSTSAGIDPSQSGKSMADTEKELDDNISEVNKRLRLHTVLFKMKVRTLPHKTVLYKGKPSADGERCEAADKQEAQDNTCLHLEVFDFVGSEDGKSSKNLGAKFKKMELFFEGSNNADPDPRKEQPRNLTKIRTYIYQNNFLLEDKVISVIADVAPNGEPAHNDKIELFYQHDDYPVWGTPETPSEKGVGKYILSNVENTKSNPIRNNFKKQFYFKNLDYFDKLFTKIFDYNDRDSNKHYKKNVEALKGSLKY

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	triclinic

Resolution resolution	2.83 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	2667344

fit	/app/data/saxs_computation/x7/9x7s/9x7s.fit
pddf	/app/data/pr_computation/x7/9x7s/9x7s.pr.out
profile	/app/data/saxs_computation/x7/9x7s/9x7s.dat

sheathed filament of the spirochete periplasmic flagella of Leptospira biflexa from the flaA2-complemented stain

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

Flagellin

State in the Current Structure

Other States of the Same Protein in the Database

Bacterial flagellar sheath protein

State in the Current Structure

Other States of the Same Protein in the Database

Bacterial flagellar sheath protein

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)