SAXSdb — 6c53

▼

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

Type-1 fimbrial protein, A chain

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 homooligomer Homooligomer Protein × 11 PDB declaration: undecameric（11） Consistent with protein copy count	Chain A； UniProt 24–182 Chain B； UniProt 24–182 Chain C； UniProt 24–182 Chain D； UniProt 24–182 Chain E； UniProt 24–182 Chain F； UniProt 24–182 Chain G； UniProt 24–182 Chain H； UniProt 24–182 Chain I； UniProt 24–182 Chain J； UniProt 24–182 Chain K； UniProt 24–182	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.20 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 6C53	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2JTY Self-complemented variant of FimA, the main subunit of type 1 pilus Deposited 2007-08-09	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–182（159 aa） Fragment：Fusion protein of Type-1 fimbrial protein and type-1 fimbrial protein Chain A 24–42（19 aa） Fragment：Fusion protein of Type-1 fimbrial protein and type-1 fimbrial protein	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 18；Pressure ambient NMR sample composition 1.7 mM [U-98% 13C; U-98% 15N] FimA, 50 M H2O, 5 M D2O, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2M5G Solution structure of FimA wt Deposited 2013-02-24	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–182（159 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.08；Pressure ambient NMR sample composition 2 mM [U-99% 13C; U-99% 15N] FimA-1, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3SQB Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone Deposited 2011-07-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 37–182（146 aa） Fragment：UNP residues 37-182	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.20 Å R-free 0.300
3SQB Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone Deposited 2011-07-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 37–182（146 aa） Fragment：UNP residues 37-182	Not recorded	EDO 1,2-ETHANEDIOL × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.20 Å R-free 0.300
3SQB Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone Deposited 2011-07-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 37–182（146 aa） Fragment：UNP residues 37-182	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.20 Å R-free 0.300
3SQB Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone Deposited 2011-07-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 37–182（146 aa） Fragment：UNP residues 37-182	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；277 K；0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K	Resolution 3.20 Å R-free 0.300
4DWH Structure of the major type 1 pilus subunit FIMA bound to the FIMC (2.5 A resolution) Deposited 2012-02-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 41–182（142 aa）	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 7 PG4 TETRAETHYLENE GLYCOL × 1 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；40% (v/v) PEG 400 0.1 M phosphate/citrate pH 4.2 , VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.50 Å R-free 0.294
4DWH Structure of the major type 1 pilus subunit FIMA bound to the FIMC (2.5 A resolution) Deposited 2012-02-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 41–182（142 aa）	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 3 PG4 TETRAETHYLENE GLYCOL × 1 PGE TRIETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；40% (v/v) PEG 400 0.1 M phosphate/citrate pH 4.2 , VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.50 Å R-free 0.294
5NKT FimA wt from E. coli Deposited 2017-04-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–182（159 aa）	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 2.6；277 K；0.1 M Sodium Malonate, pH 2.6, 45% ammonium sulphate, 23 mg/ml of protein 1:1 mixture with reservoir	Resolution 1.50 Å R-free 0.188
5OH0 The Cryo-Electron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod Deposited 2017-07-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 24–182（159 aa） Chain B 24–182（159 aa） Chain C 24–182（159 aa） Chain D 24–182（159 aa） Chain E 24–182（159 aa） Chain F 24–182（159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
6R74 N-terminally reversed variant of FimA E. coli Deposited 2019-03-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 42–182（141 aa）	Not recorded	SO4 SULFATE ION × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 3.1；298 K；45% NH4SO2 and 0.1M Sodium Malonate buffer pH 3.1	Resolution 1.81 Å R-free 0.219
6SWH Crystal structure of the ternary complex between the type 1 pilus proteins FimC, FimI and FimA from E. coli Deposited 2019-09-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 37–182（146 aa）	Not recorded	PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.8 M sodium formate, 100 mM Tris/acetic acid pH 8.5, 16% PEG 4000 (w/v)	Resolution 2.80 Å R-free 0.207
6SWH Crystal structure of the ternary complex between the type 1 pilus proteins FimC, FimI and FimA from E. coli Deposited 2019-09-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 37–182（146 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.8 M sodium formate, 100 mM Tris/acetic acid pH 8.5, 16% PEG 4000 (w/v)	Resolution 2.80 Å R-free 0.207
6Y7S 2.85 A cryo-EM structure of the in vivo assembled type 1 pilus rod Deposited 2020-03-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–182（182 aa） Chain B 1–182（182 aa） Chain C 1–182（182 aa） Chain D 1–182（182 aa） Chain E 1–182（182 aa） Chain F 1–182（182 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7；in ddH2O. cryo-EM vitrification conditions Cryogen ETHANE；3 ul sample, 30 s wait time, 0.5 s drain time, 6 s blotting	Resolution 2.85 Å R-free 0.275
8PSV 2.7 A cryo-EM structure of in vitro assembled type 1 pilus rod Deposited 2023-07-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–182（182 aa） Chain B 1–182（182 aa） Chain C 1–182（182 aa） Chain D 1–182（182 aa） Chain E 1–182（182 aa） Chain F 1–182（182 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7；in ddH2O. cryo-EM vitrification conditions Cryogen ETHANE；3 ul sample, 30 s wait time, 0.5 s drain time, 6 s blotting	Resolution 2.70 Å
8PTU 2.5 A cryo-EM structure of the in vitro FimD-catalyzed assembly of type 1 pilus rod Deposited 2023-07-14	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–182（182 aa） Chain B 1–182（182 aa） Chain C 1–182（182 aa） Chain D 1–182（182 aa） Chain E 1–182（182 aa） Chain F 1–182（182 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7；in ddH2O. cryo-EM vitrification conditions Cryogen ETHANE；3 ul sample, 30 s wait time, 0.5 s drain time, 6 s blotting	Resolution 2.52 Å
9FTT Cryo-EM structure of the type 1 pilus rod as part of the FimA-bound usher complex (FimDHGFAnC) Deposited 2024-06-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain B 24–182（159 aa） Chain C 24–182（159 aa） Chain D 24–182（159 aa） Chain E 24–182（159 aa） Chain F 24–182（159 aa） Chain G 24–182（159 aa） Chain H 24–182（159 aa） Chain I 24–182（159 aa） Chain J 24–182（159 aa） Chain K 24–182（159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.60 Å
9FW9 Cryo-EM structure of the type 1 pilus assembly platform as part of the FimA-bound chaperone-usher pilus complex (FimDHGFAnC - body 2) Deposited 2024-06-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 24–182（159 aa） Chain B 24–182（159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.90 Å
9FWB Cryo-EM structure of the type 1 pilus assembly platform as part of the FimA-bound chaperone-usher pilus complex (Local refinement including FimD, FimC, FimAn and FimAn-1) Deposited 2024-06-28	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 24–182（159 aa） Chain B 24–182（159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.50 Å
9FWZ Cryo-EM structure of the type 1 pilus assembly platform as part of the FimA-bound chaperone-usher pilus complex (Local refinement including FimD, FimC, FimAn, FimAn-1 and FimAn-2) Deposited 2024-07-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 24–182（159 aa） Chain B 24–182（159 aa） Chain E 24–182（159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.60 Å
9FX0 Cryo-EM structure of the type 1 pilus tip-to-rod transition Deposited 2024-07-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric	Chain A 24–182（159 aa） Chain B 24–182（159 aa） Chain C 24–182（159 aa） Chain D 24–182（159 aa） Chain E 24–182（159 aa） Chain G 24–182（159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.10 Å
9FXA Cryo-EM structure of the type 1 pilus rod as part of the FimI-bound usher complex (FimDHGFAnIC - body 1) Deposited 2024-07-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain B 24–182（159 aa） Chain C 24–182（159 aa） Chain D 24–182（159 aa） Chain E 24–182（159 aa） Chain F 24–182（159 aa） Chain G 24–182（159 aa） Chain H 24–182（159 aa） Chain I 24–182（159 aa） Chain J 24–182（159 aa） Chain K 24–182（159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.00 Å
9FXB Cryo-EM structure of the type 1 pilus assembly platform as part of the FimI-bound chaperone-usher pilus complex (FimDHGFAnIC - body 2) Deposited 2024-07-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 24–182（159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 4.30 Å
9VKV Cryo-EM structure of the type I pilus from Escherichia Coli and the surrounding water network Deposited 2025-06-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 15 PDB declaration: pentadecameric	Chain A 24–182（159 aa） Chain B 24–182（159 aa） Chain C 24–182（159 aa） Chain D 24–182（159 aa） Chain E 24–182（159 aa） Chain F 24–182（159 aa） Chain G 24–182（159 aa） Chain H 24–182（159 aa） Chain I 24–182（159 aa） Chain J 24–182（159 aa） Chain K 24–182（159 aa） Chain L 24–182（159 aa） Chain M 24–182（159 aa） Chain N 24–182（159 aa） Chain O 24–182（159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 2.09 Å
9X67 Cryo-EM structure of the type I pilus from Escherichia Coli and the surrounding water network Deposited 2025-10-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 15 PDB declaration: 15-meric	Chain A 24–182（159 aa） Chain B 24–182（159 aa） Chain C 24–182（159 aa） Chain D 24–182（159 aa） Chain E 24–182（159 aa） Chain F 24–182（159 aa） Chain G 24–182（159 aa） Chain H 24–182（159 aa） Chain I 24–182（159 aa） Chain J 24–182（159 aa） Chain K 24–182（159 aa） Chain L 24–182（159 aa） Chain M 24–182（159 aa） Chain N 24–182（159 aa） Chain O 24–182（159 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 1.85 Å

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FIMA1_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–159； UniProt 24–182 Author chain B； PDBConstruct 1–159； UniProt 24–182 Author chain C； PDBConstruct 1–159； UniProt 24–182 Author chain D； PDBConstruct 1–159； UniProt 24–182 Author chain E； PDBConstruct 1–159； UniProt 24–182 Author chain F； PDBConstruct 1–159； UniProt 24–182 Author chain G； PDBConstruct 1–159； UniProt 24–182 Author chain H； PDBConstruct 1–159； UniProt 24–182 Author chain I； PDBConstruct 1–159； UniProt 24–182 Author chain J； PDBConstruct 1–159； UniProt 24–182 Author chain K； PDBConstruct 1–159； UniProt 24–182

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	6c53
Deposition date deposition_date	2018-01-13
Structure title title	Cryo-EM structure of the Type 1 pilus rod
Keywords keywords	Type 1 pili, helical rod, adhesive pili, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method method	ELECTRON MICROSCOPY

▼

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

Radius of gyration Rg (Guinier) rg_guinier	35.61 Å
Radius of gyration Rg (electron density) rg_electron	34.76 Å
Forward intensity I(0) i0	494459000.00
Molecular weight molecular_weight	170890.0 kDa
Excluded volume excluded_volume	210050 Å³
Envelope volume envelope_volume	271350 Å³
Hydration-shell volume shell_volume	62595 Å³
Envelope diameter envelope_diameter	120.9 Å
Shell Rg shell_rg	43.31 Å
Envelope Rg envelope_rg	34.35 Å
Shape Rg shape_rg	34.75 Å
Total Rg total_rg	35.35 Å
Total atoms total_atoms	12023
Residues n_residues	1716
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

▼

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

Maximum dimension Dmax dmax	112.9 Å
Rg (real space) rg_real	35.42 Å
Rg uncertainty (real space) rg_real_error	0.61 Å
I(0) (real space) i0_real	4.9450e+08
I(0) uncertainty (real space) i0_real_error	7.4780e+06
Rg (reciprocal space) rg_reciprocal	35.54 Å
I(0) (reciprocal space) i0_reciprocal	494500000.0000
Solution quality estimate total_estimate	0.8804
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	46.2 Å
Skewness Skewness skewness	0.209
Kurtosis Kurtosis kurtosis	-0.308
Angular range angular_range	— – 0.2200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	222300000.0000
Real-space data points n_real_points	45
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.836; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.951

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▶

8. Citations (1)

▶

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	1

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

Resolution resolution	4.20 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	72627

Description description	Type-1 fimbrial protein, A chain
Molecular weight formula_weight	15835.2 kDa
Source method src_method	nat
Copy count entity_count	11

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K
Atom count atom_count	12023

Cryo-EM structure of the Type 1 pilus rod

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

Type-1 fimbrial protein, A chain

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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/c5/6c53/6c53.fit
pddf	/app/data/pr_computation/c5/6c53/6c53.pr.out
profile	/app/data/saxs_computation/c5/6c53/6c53.dat