1F4N

C2 CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.

Summary for 1F4N

Entry DOI	10.2210/pdb1f4n/pdb
Related	1B6Q 1F4M 1GTO 1NKD 1ROP 1RPO 1RPR
Descriptor	ROP ALA2ILE2-6, CALCIUM ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
Functional Keywords	rop, dimer, homodimer, helix-turn-helix, transcription regulation, hydrophobic core packing, thermodynamic stability, transcription
Biological source	Escherichia coli
Total number of polymer chains	2
Total formula weight	14386.02
Authors	Willis, M.A.,Bishop, B.,Regan, L.,Brunger, A.T. (deposition date: 2000-06-08, release date: 2001-01-10, Last modification date: 2024-02-07)
Primary citation	Willis, M.A.,Bishop, B.,Regan, L.,Brunger, A.T. Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core. Structure Fold.Des., 8:1319-1328, 2000 Cited by PubMed Abstract: Rop is an RNA binding, dimeric, four-helix bundle protein with a well-defined, regular hydrophobic core ideally suited for redesign studies. A family of Rop variants in which the hydrophobic core was systematically redesigned has previously been created and characterized. PubMed: 11188696 DOI: 10.1016/S0969-2126(00)00544-X PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation