E. coli CheY Protein Crystal Structure Refined at 1.7-Angstrom Resolution

A three-dimensional atomic model of the wild-type CheY protein from Escherichia coli, refined to a crystallographic R-factor of 15.1% at 1.7-angstrom resolution. The structure contains coordinates for 1165 atoms, including all protein atoms, 147 water molecules, and three sulfate ions. The model was created by Karl Volz of the University of Illinois Chicago using stereochemically restrained least squares minimization.

Use Cases

• Analyzing the hydrogen bonding network in the phosphorylation region based on the detailed atomic coordinates.
• Studying structural rearrangements upon phosphorylation based on the described active site cavity and interactions.
• Modeling protein dynamics based on the seven amino acid side chains modeled in dual conformations.
• Investigating the role of the cis peptide bond conformation preceding Pro-110 based on the positioning of Lys-109.

Strengths

• High-resolution atomic coordinates refined to 1.7-angstrom resolution.
• Model includes 1165 atoms, 147 water molecules, and three sulfate ions, providing a detailed solvation environment.
• Final model has low root mean square deviations (0.018 A for bonds, 0.049 A for angles) from idealized geometry.

Limitations

• Row count and column-level documentation are absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.
• Data may reflect the specific experimental and modeling bias inherent to a single X-ray crystallography study.

Provenance

Source

University of Illinois Chicago

Collection Method

X-ray crystallography with stereochemically restrained least squares refinement.