1zdv

Solution Structure of the type 1 pilus assembly platform FimD(25-139)

Method: SOLUTION NMR Dmax: 43.5 Å Quality: REASONABLE

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

Outer membrane usher protein fimD

Escherichia coli

UniProt P30130

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 70–184 Fragment:N-TERMINAL DOMAIN Residues 70-184 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;293 K;Pressure ambient NMR sample composition:Uniform labeling with 13C, 15N; 90 % H2O, 10% D2O | 90% H2O/10% D2O Resolution not provided

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMD_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–115; UniProt 70–184

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 1zdv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1zdv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1zdv
Deposition date deposition_date2005-04-15
Structure title titleSolution Structure of the type 1 pilus assembly platform FimD(25-139)
Keywords keywordsBETA SHEET, ALPHA HELIX, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.70
Radius of gyration Rg (electron density) rg_electron13.33
Forward intensity I(0) i0918647000.00
Molecular weight molecular_weight247220.0 kDa
Excluded volume excluded_volume305260 ų
Envelope volume envelope_volume23378 ų
Hydration-shell volume shell_volume13512 ų
Envelope diameter envelope_diameter48.9
Shell Rg shell_rg20.53
Envelope Rg envelope_rg14.83
Shape Rg shape_rg13.34
Total Rg total_rg13.38
Total atoms total_atoms34420
Residues n_residues2300
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 dmax43.5
Rg (real space) rg_real13.59
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real9.1860e+08
I(0) uncertainty (real space) i0_real_error1.0210e+07
Rg (reciprocal space) rg_reciprocal13.60
I(0) (reciprocal space) i0_reciprocal918600000.0000
Solution quality estimate total_estimate0.7141
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.0
Skewness Skewness skewness0.022
Kurtosis Kurtosis kurtosis-0.433
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha287500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 0.991; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1zdva1
Class classb — All beta proteins
Fold Fold foldb.167 — FimD N-terminal domain-like
Superfamily Superfamily superfamilyb.167.1 — FimD N-terminal domain-like
Family Family familyb.167.1.1 — Usher N-domain

CATH v4.4 (1 domains)

Domain ID domain_id1zdvA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily410 — PapC, N-terminal domain

8. Citations (1)

9. Files and Curves (10)