1cii

COLICIN IA

Method: X-RAY DIFFRACTION Dmax: 235.1 Å Quality: REASONABLE

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

COLICIN IA

Escherichia coli

UniProt P06716

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 23–624 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:vapor diffusion - hanging drop - streak seeding;pH 5.2;PROTEIN WAS CRYSTALLIZED BY HANGING-DROP VAPOR DIFFUSION AGAINST RESERVOIRS OF 1.0 M NH4(SO4)2, 20 MM NA-CITRATE (PH 5.2), 200 MM NACL, STARTING WITH 6 MICROLITERS OF PROTEIN AT 2 MG/ML IN 20 MM NA-CITRATE (PH 5.2), 200 MM NACL, 5 MM DTT, AND 4 MICROLITERS RESERVOIR SOLUTION. THESE DROPS OF MUTANT PROTEIN WERE STREAK-SEEDED FROM STOCKS GENERATED FROM CRUSHED DIFFRACTION-QUALITY WILD-TYPE COLICIN IA CRYSTALS. CRYSTALS WERE HARVESTED TO 1.1 M NA2SO4, 200 MM NACL, 20 MM NA-CITRATE (PH 5.2), AND 5 MM DTT. FOR DERIVATIZATION, CRYSTALS WERE WASHED IN DTT-FREE HARVEST BUFFER AND SOAKED FOR ONE WEEK IN 1 MM CH3HGCL., vapor diffusion - hanging drop - streak seeding Resolution 3.00 Å R-free 0.312

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CEIA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–602; UniProt 23–624

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 1cii

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cii
Deposition date deposition_date1997-01-08
Structure title titleCOLICIN IA
Keywords keywordsCOLICIN, BACTERIOCIN, ION CHANNEL FORMATION, TRANSMEMBRANE PROTEIN; TRANSMEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.66
Radius of gyration Rg (electron density) rg_electron58.91
Forward intensity I(0) i071522700.00
Molecular weight molecular_weight66948.0 kDa
Excluded volume excluded_volume83167 ų
Envelope volume envelope_volume130970 ų
Hydration-shell volume shell_volume24056 ų
Envelope diameter envelope_diameter218.2
Shell Rg shell_rg43.11
Envelope Rg envelope_rg59.66
Shape Rg shape_rg58.96
Total Rg total_rg58.05
Total atoms total_atoms4714
Residues n_residues602
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 dmax235.1
Rg (real space) rg_real58.46
Rg uncertainty (real space) rg_real_error4.79
I(0) (real space) i0_real7.1520e+07
I(0) uncertainty (real space) i0_real_error1.6600e+06
Rg (reciprocal space) rg_reciprocal55.14
I(0) (reciprocal space) i0_reciprocal71170000.0000
Solution quality estimate total_estimate0.6077
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary33.6
Skewness Skewness skewness0.702
Kurtosis Kurtosis kurtosis-0.569
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2690000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.005; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.001; Smooth: 0.882

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ciia1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.1 — Toxins' membrane translocation domains
Superfamily Superfamily superfamilyf.1.1 — Colicin
Family Family familyf.1.1.1 — Colicin
Domain ID domain_idd1ciia2
Class classh — Coiled coil proteins
Fold Fold foldh.4 — Antiparallel coiled-coil
Superfamily Superfamily superfamilyh.4.3 — Colicin Ia, N-terminal domain
Family Family familyh.4.3.1 — Colicin Ia, N-terminal domain

CATH v4.4 (3 domains)

Domain ID domain_id1ciiA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology250 — Colicin Ia; domain 1
Homologous superfamily homologous superfamily10 — Colicin Ia, domain 1
Domain ID domain_id1ciiA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology305 — Colicin Ia; domain 2
Homologous superfamily homologous superfamily10 — Colicin Ia; domain 2
Domain ID domain_id1ciiA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology490 — Globin-like
Homologous superfamily homologous superfamily30 — Colicin

8. Citations (3)

9. Files and Curves (10)