3bfq

Crystal structure of truncated FimG (FimGt) in complex with the donor strand peptide of FimF (DSF)

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

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

Protein fimG

Escherichia coli str. K12 substr.

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 G; UniProt 36–167 Fragment:sequence database 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;20 mM Tris/HCl, pH 8.0, 80 mM NaCl, 27.5% PEG 1500, 20 mM cobalt chloride, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.34 Å R-free 0.179

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 23 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 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 F; UniProt 23–37 Fragment:sequence database residues 23-37 Protein fimG × 1 (P08190) CO COBALT (II) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20 mM Tris/HCl, pH 8.0, 80 mM NaCl, 27.5% PEG 1500, 20 mM cobalt chloride, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.34 Å R-free 0.179

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 18 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 F; PDBConstruct 1–15; UniProt 23–37

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 3bfq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3bfq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3bfq
Deposition date deposition_date2007-11-23
Structure title titleCrystal structure of truncated FimG (FimGt) in complex with the donor strand peptide of FimF (DSF)
Keywords keywords;Incomplete Ig-like fold, donor strand exchange, Cell projection, Fimbrium, CELL ADHESION, STRUCTURAL PROTEIN-STRUCTURAL PROTEIN COMPLEX ;; STRUCTURAL PROTEIN/STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.63
Radius of gyration Rg (electron density) rg_electron16.83
Forward intensity I(0) i05151620.00
Molecular weight molecular_weight15451.0 kDa
Excluded volume excluded_volume18895 ų
Envelope volume envelope_volume21580 ų
Hydration-shell volume shell_volume11991 ų
Envelope diameter envelope_diameter65.3
Shell Rg shell_rg21.11
Envelope Rg envelope_rg17.19
Shape Rg shape_rg16.79
Total Rg total_rg17.64
Total atoms total_atoms1082
Residues n_residues147
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_real17.78
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real5.1520e+06
I(0) uncertainty (real space) i0_real_error7.1860e+04
Rg (reciprocal space) rg_reciprocal17.76
I(0) (reciprocal space) i0_reciprocal5152000.0000
Solution quality estimate total_estimate0.7697
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.9
Skewness Skewness skewness0.568
Kurtosis Kurtosis kurtosis-0.100
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha959400.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.493; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.524; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3bfqG00
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)