5iqn

Crystal structure of the E. coli type 1 pilus subunit FimG (engineered variant with substitution Q134E; N-terminal FimG residues 1-12 truncated) in complex with the donor strand peptide DsF_SRIRIRGYVR

Method: X-RAY DIFFRACTION Dmax: 67.2 Å Quality: EXCELLENT

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

Protein FimG

Escherichia coli K-12

UniProt P08190

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 36–167 Fragment:UNP residues 36-167 Protein FimF × 1 (P08189) CO COBALT (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;MOPS-NaOH pH 6.8 (RT), PEG-1500, CoCl2, NaCl Resolution 1.00 Å R-free 0.146
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 36–167 Fragment:UNP residues 36-167 Protein FimF × 1 (P08189) CO COBALT (II) ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;MOPS-NaOH pH 6.8 (RT), PEG-1500, CoCl2, NaCl Resolution 1.00 Å R-free 0.146

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.

15 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMG_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–132; UniProt 36–167 Author chain G; PDBConstruct 1–132; UniProt 36–167

Protein FimF

OrganismNot specified

UniProt P08189

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 25–34 Fragment:UNP residues 35-34 Protein FimG × 1 (P08190) CO COBALT (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;MOPS-NaOH pH 6.8 (RT), PEG-1500, CoCl2, NaCl Resolution 1.00 Å R-free 0.146
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 25–34 Fragment:UNP residues 35-34 Protein FimG × 1 (P08190) CO COBALT (II) ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;MOPS-NaOH pH 6.8 (RT), PEG-1500, CoCl2, NaCl Resolution 1.00 Å R-free 0.146

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.

13 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMF_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 25–34 Author chain F; PDBConstruct 1–10; UniProt 25–34

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 5iqn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5iqn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5iqn
Deposition date deposition_date2016-03-11
Structure title titleCrystal structure of the E. coli type 1 pilus subunit FimG (engineered variant with substitution Q134E; N-terminal FimG residues 1-12 truncated) in complex with the donor strand peptide DsF_SRIRIRGYVR
Keywords keywordsComplex, Protein, FimGt, cell adhesion; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.34
Radius of gyration Rg (electron density) rg_electron20.39
Forward intensity I(0) i017666500.00
Molecular weight molecular_weight30047.0 kDa
Excluded volume excluded_volume36861 ų
Envelope volume envelope_volume44348 ų
Hydration-shell volume shell_volume18611 ų
Envelope diameter envelope_diameter68.8
Shell Rg shell_rg25.95
Envelope Rg envelope_rg20.38
Shape Rg shape_rg20.36
Total Rg total_rg21.20
Total atoms total_atoms4139
Residues n_residues284
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 dmax67.2
Rg (real space) rg_real21.26
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real1.7670e+07
I(0) uncertainty (real space) i0_real_error2.4640e+05
Rg (reciprocal space) rg_reciprocal21.28
I(0) (reciprocal space) i0_reciprocal17670000.0000
Solution quality estimate total_estimate0.9085
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.156
Kurtosis Kurtosis kurtosis-0.607
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3477000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5iqnA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain
Domain ID domain_id5iqnG00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1090 — Fimbrial-type adhesion domain

8. Citations (1)

9. Files and Curves (10)