2iji

Structure of F14H mutant of ColE1 Rom protein

Method: X-RAY DIFFRACTION Dmax: 51.9 Å Quality: GOOD

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

Regulatory protein rop

Escherichia coli

UniProt P03051

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–63 Mutation:M1G, F14H No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;1uL protein solution (0.5-1 mM) was mixed with 1 uL well buffer (0.1M sodium acetate pH 5.5, 0.1M sodium chloride, 37 40% ethanol, and 20% glycerol), VAPOR DIFFUSION, HANGING DROP Resolution 2.30 Å R-free 0.292

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.

18 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ROP_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–63; UniProt 1–63

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 2iji

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2iji
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2iji
Deposition date deposition_date2006-09-29
Structure title titleStructure of F14H mutant of ColE1 Rom protein
Keywords keywordsRom, Rop, ColE1 plasmid copy control, TRANSCRIPTION REGULATOR; TRANSCRIPTION REGULATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.03
Radius of gyration Rg (electron density) rg_electron13.38
Forward intensity I(0) i01074320.00
Molecular weight molecular_weight6348.0 kDa
Excluded volume excluded_volume7720 ų
Envelope volume envelope_volume9499 ų
Hydration-shell volume shell_volume6939 ų
Envelope diameter envelope_diameter50.3
Shell Rg shell_rg17.09
Envelope Rg envelope_rg13.98
Shape Rg shape_rg13.38
Total Rg total_rg14.31
Total atoms total_atoms444
Residues n_residues56
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 dmax51.9
Rg (real space) rg_real14.23
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real1.0740e+06
I(0) uncertainty (real space) i0_real_error1.3360e+04
Rg (reciprocal space) rg_reciprocal14.21
I(0) (reciprocal space) i0_reciprocal1074000.0000
Solution quality estimate total_estimate0.7905
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.1
Skewness Skewness skewness0.604
Kurtosis Kurtosis kurtosis-0.111
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha144300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.633; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.379; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2ijia_
Class classa — All alpha proteins
Fold Fold folda.30 — ROP-like
Superfamily Superfamily superfamilya.30.1 — ROP protein
Family Family familya.30.1.1 — ROP protein

CATH v4.4 (1 domains)

Domain ID domain_id2ijiA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily230

8. Citations (1)

9. Files and Curves (10)