Crystal structure of a putative flagella synthesis protein flgn (pa3352) from pseudomonas aeruginosa at 1.48 A resolution
Joint Center for Structural Genomics (JCSG)
Crystal structure of hypothetical protein (NP_252042.1) from Pseudomonas aeruginosa at 1.48 A resolution
G(MSE)PDSPTLLDLFAEDIGHANQLLQLVDEEFQALERRELPVLQQLLGAKQPL(MSE)QQLERNGRARAEILREAGVS LDREGLARYARERADGAELLARGDELGELLERCQQANLRNGRIIRANQASTGSLLNILRGQDAPSLYDSRGGTASSSRQR PLSQA
GMPDSPTLLDLFAEDIGHANQLLQLVDEEFQALERRELPVLQQLLGAKQPLMQQLERNGRARAEILREAGVSLDREGLAR YARERADGAELLARGDELGELLERCQQANLRNGRIIRANQASTGSLLNILRGQDAPSLYDSRGGTASSSRQRPLSQA
20.0% MPD, 0.1M Citrate, pH 4.0, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K
BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT OF A MONOMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.
SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 3. RESIDUES 115-116 WERE DISORDERED AND NOT INCLUDED IN THE MODEL. 4. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
Structural genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, biosynthetic protein
MPDSPTLLDLFAEDIGHANQLLQLVDEEFQALERRELPVLQQLLGAKQPLMQQLERNGRARAEILREAGVSLDREGLARY ARERADGAELLARGDELGELLERCQQANLRNGRIIRANQASTGSLLNILRGQDAPSLYDSRGGTASSSRQRPLSQA