1bf8

PERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 66.8 Å Quality: GOOD

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

CHAPERONE PROTEIN FIMC

Escherichia coli

UniProt P31697

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 37–241 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5;311 K 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.

22 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIMC_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–205; UniProt 37–241

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 1bf8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bf8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bf8
Deposition date deposition_date1998-05-28
Structure title titlePERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES
Keywords keywordsCHAPERONE, FIMC, PERIPLASMIC CHAPERONE, PILUS CHAPERONE, TYPE-I PILI; CHAPERONE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.71
Radius of gyration Rg (electron density) rg_electron19.31
Forward intensity I(0) i02764490000.00
Molecular weight molecular_weight454680.0 kDa
Excluded volume excluded_volume572970 ų
Envelope volume envelope_volume61056 ų
Hydration-shell volume shell_volume23083 ų
Envelope diameter envelope_diameter71.6
Shell Rg shell_rg29.35
Envelope Rg envelope_rg22.99
Shape Rg shape_rg19.25
Total Rg total_rg19.67
Total atoms total_atoms64680
Residues n_residues4100
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 dmax66.8
Rg (real space) rg_real19.72
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real2.7640e+09
I(0) uncertainty (real space) i0_real_error3.6240e+07
Rg (reciprocal space) rg_reciprocal19.72
I(0) (reciprocal space) i0_reciprocal2764000000.0000
Solution quality estimate total_estimate0.8691
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.9
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.619
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2568000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.812; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.858; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1bf8a1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.11 — PapD-like
Family Family familyb.1.11.1 — Pilus chaperone
Domain ID domain_idd1bf8a2
Class classb — All beta proteins
Fold Fold foldb.7 — C2 domain-like
Superfamily Superfamily superfamilyb.7.2 — Periplasmic chaperone C-domain
Family Family familyb.7.2.1 — Periplasmic chaperone C-domain

CATH v4.4 (2 domains)

Domain ID domain_id1bf8A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1bf8A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (2)

9. Files and Curves (10)