Solution structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii. Northeast Structural Genomics Consortium target JR19.
Northeast Structural Genomics Consortium (NESG)
Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
MAEDEGYPAEVIEIIGRTGTTGDVTQVKVRILEGRDKGRVIRRNVRGPVRVGDILILRETEREAREIKSRRAAALEHHHH HH
Northeast Structural Genomics Consortium
THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY. AUTOMATIC BACKBONE RESONANCE ASSIGNMENTS WERE MADE USING AUTOASSIGN. Manual side chain assignments. AUTOMATIC NOESY ASSIGNMENTS AS WELL AS DISTANCE AND HYDROGEN BOND RESTRAINTS WERE DETERMINED USING AUTOSTRUCTURE. DIHEDRAL ANGLE RESTRAINTS WERE DETERMINED USING HYPER AND TALOS. BACKBONE CONFORMATIONS FOR RESIDUES 1-3, 5-6, 18-20, 22-23, 34-35, 48-49, 57-71, ARE NOT WELL-DEFINED [S(PHI) + S(PSI) < 1.8] IN THIS SOLUTION NMR STRUCTURE.
3D 15N-NOESY, 3D 13C-NOESY (aliphatic and aromatic)
THE STRUCTURES ARE BASED ON A TOTAL OF 828 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE RESTRAINTS, 99 DIHEDRAL ANGLE RESTRAINTS, AND 28 HYDROGEN BOND RESTRAINTS. (13.5 CONSTRAINTS PER RESIDUE; 5.2 LONG-RANGE RESTRAINTS PER RESIDUE). STRUCTURE DETERMINATION WAS PERFORMED ITERATIVELY USING AUTOSTRUCTURE (DYANA). THE UNSTRUCTURED 11 RESIDUE C-TERMINAL TAG (AAALEHHHHHH) WAS INCLUDED IN THE STRUCTURE CALCULATIONS BUT IS OMITTED FROM THIS DEPOSITION.
1.0 MM JR19 U-15N,13C 20 mM MES, 100 mM NaCl, 5 mM CaCl2, 10 mM DTT, 0.02% NaN3, pH 6.5
JR19, AUTOSTRUCTURE, Ribosomal protein, Northeast Structural Genomics Consortium, PSI, Protein Structure Initiative, NESG, RNA binding protein