NMR Structure of the Rpa2829 protein from Rhodopseudomonas palustris: Northeast Structural Genomics Target RpR43
Northeast Structural Genomics Consortium (NESG)
NMR Structure of the Rpa2829 protein from Rhodopseudomonas palustris
MAQRSEIPHFPRTAAIDAYGKGGFYFAGMSHQGSLLFLPDAVWGWDVTKPEQIDRYSLQRVFDNANAIDTLIVGTGADVW IAPRQLREALRGVNVVLDTMQTGPAIRTYNIMIGERRRVAAALIAVPLEHHHHHH
Northeast Structural Genomics Consortium
Sequence According to authors,this is a sequencing error or an isoform resulting from a slight difference in the sequenced strain and the cloning strain.
structures with lowest energy and fewest restraint violations
100 mM NaCl; 5mM CaCl2; 20 mM Ammonium acetate
THE STRUCTURES ARE BASED ON A TOTAL OF 1039 RESTRAINTS. SUMMARY OF EXPERIMENTAL CONSTRAINTS: RESTRAINING DISTANCE RESTRAINTS: TOTAL = 864; INTRA-RESIDUE [I=J] = 160; SEQUENTIAL [(I-J)=1] = 225; MEDIUM RANGE [1<(I-J)<5] = 131; LONG RANGE [(I-J)>=5] = 348; HYDROGEN BOND RESTRAINTS = 72 (2 PER H-BOND); NUMBER OF RESTRAINING DISTANCE RESTRAINTS PER RESTRAINED RESIDUE = 8.2; DIHEDRAL-ANGLE RESTRAINTS = 103 (50 PHI, 52 PSI, 1 CHI-1); TOTAL NUMBER OF RESTRAINTS PER RESTRAINED RESIDUE = 8.9; NUMBER OF LONG RANGE NOE DISTANCE RESTRAINTS PER RESTRAINED RESIDUE = 3.0; NUMBER OF STRUCTURES COMPUTED = 30; NUMBER OF STRUCTURES USED = 20. AVERAGE DISTANCE VIOLATIONS >0.0001 ANG = 26.8+/-6; AVERAGE R.M.S. DISTANCE VIOLATION = 0.005 +/- 0.001 ANG; MAXIMUM NUMBER OF DISTANCE VIOLATIONS 39.MAXIMUM DISTANCE VIOLATION = 0.26 ANG; AVERAGE DIHEDRAL ANGLE VIOLATIONS: >0.0001 DEG = 3.3+/-1.3; MAX NUMBER OF DIHEDRAL ANGLE VIOLATIONS = 5; AVERAGE R.M.S. ANGLE VIOLATION = 0.42 +/- .01 DEG.; RMSD VALUES: BACKBONE ATOMS (N,C,C' RESIDUES 10-126) = 0.86 ANG, ALL HEAVY ATOMS = 1.52 ANG; BACKBONE ATOMS (N,C,C' RESIDUES 33-126) = 0.68 ANG, ALL HEAVY ATOMS = 1.1.38 ANG; BACKBONE ATOMS (N,C,C' RESIDUES 12-16,24-26,34-39,41-49,52-74,79-92,95-114,119-126) = 0.67 ANG,ALL HEAVY ATOMS = 1.19 ANG; PROCHECK (RESDIUES 10-126): MOST FAVORED REGIONS = 83.8%; ADDITIONAL ALLOWED REGIONS = 14.9%; GENEROUSLY ALLOWED REGIONS = 1.9%; DISALLOWED REGIONS = 0.4%.
The initial structure was determined using automated structure determination (AutoStructure) and refined manually. A final refinement used simultated annealing in explicit solvent.
few violations and low energy and good geometery
1.2 mM Rpa2829 U-15N,13C; 20 mM ammonium acetate pH 5.0; 100 mM NaCl; 5mM CaCl2; 0.02% NaN3; 10 mM DTT; 95% H2O; 10% D2O
1.2 mM Rpa2829 U-15N,13C; 20 mM ammonium acetate pH 5.0; 100 mM NaCl, 5mM CaCl2, 0.02% NaN3; 100% D2O
0.8 mM Rpa2829 U-15N,5% fractionally labeled 13C; 20 mM ammonium acetate pH 4.5; 100 mM NaCl, 5mM CaCl2, 0.02% NaN3; 95% H2O; 10% D2O
MTH938-like fold, Structural Genomics, PSI, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG, UNKNOWN FUNCTION
MAQRSEIPHFPRTAAIDAYGKGGFYFADMSHQGSLLFLPDAVWGWDVTKPEQIDRYSLQRVFDNANAIDTLIVGTGADVW IAPRQLREALRGVNVVLDTMQTGPAIRTYNIMIGERRRVAAALIAVP