NMR structure of Antheraea polyphemus pheromone-binding protein 1 at pH 4.5
Structural Basis of Ligand Binding and Release in Insect Pheromone-Binding Proteins: NMR Structure of Antheraea polyphemus PBP1 at pH 4.5
Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
Protein NMR structure determination with automated NOE assignment using the new software candid and the torsion angle dynamics algorithm DYANA
Torsion angle dynamics for NMR structure calculation with the new program DYANA
The new program opal for molecular dynamics simulations and energy refinement of biological macromolecules
Point-centered domain decomposition for parallel molecular dynamics simulation
The computer-aided resonance assignment tutorial
SPEIMKNLSNNFGKAMDQCKDELSLPDSVVADLYNFWKDDYVMTDRLAGCAINCLATKLDVVDPDGNLHHGNAKDFAMKH GADETMAQQLVDIIHGCEKSAPPNDDKCMKTIDVAMCFKKEIHKLNWVPNMDLVIGEVLAEV
Bombyx mori pheromone-binding protein at pH 4.5.
Antheraea polyphemus pheromone-binding protein 1 at pH 5.2.
Bombyx mori pheromone-binding protein at pH 6.5.
Antheraea polyphemus pheromone-binding protein 1 at pH 6.3
Protein with 67% sequence identity truncated to remove c-terminal 12 residues
Protein with 67% sequence identity bound to natural ligand bombykol
HELIX DETERMINATION METHOD: KAPSCH AND SANDER APPLIED TO MEAN BACKBONE COORDINATES DERIVED FROM ALIGNING BACKBONE HEAVY ATOMS OF RESIDUES 10-142.
TWO 13C-RESOLVED NOESY SPECTRA WERE MEASURED, ONE WITH THE 13C CARRIER CENTERED AT 35 PPM (ALIPHATICS), AND THE OTHER WITH THE CARRIER AT 125 PPM (AROMATICS). ALL PROTONS WERE EXCITED AND DECOUPLED WITH A REFOCUSSING 180 IN THE NOE DIMENSION, WHERE AS BROADBAND 13C-DECOUPLING WAS ONLY APPLIED TO ONE OF THE TWO CLASSES OF 1H DURING ACQUISITION.
SIMULATED ANNEALING USING TORSION ANGLE DYNAMICS FOLLOWED BY REFINEMENT IN A WATER BATH
TORSION ANGLE DYNAMICS, SIMULATED ANNEALING
0.9 MM [U-99% 13C; U-99% 15N] APOLPBP1, 2MM NAN3, 50MM PHOSPHATE BUFFER, 95% H2O/5% D2O
LUGINBUHL, GUNTERT, BILLETER, AND WUTHRICH
The structure determination of ApolPBP1 was performed at pH 4.5 in the absense of signals from the alternate high pH conformation and contains a helix formed by the C-terminal dodecapeptide in the binding site.
insect odorant-binding protein, pH-dependent conformation, helix insertion, TRANSPORT PROTEIN