1 nformations (conformer 1 and conformer 2) of isepamicin.

2 onformation of the aminoglycoside antibiotic isepamicin, a psuedo-trisaccharide, bound to aminoglycos

3 , was used to determine the conformations of isepamicin and butirosin A in the active site of aminogl

4 ults suggest two enzyme-bound conformers for isepamicin and one for butirosin A.

5 assignments of the aminoglycoside antibiotic isepamicin at pH 6.8 as well as the pKa values for it's

6                          The conformation of isepamicin bound to the aminoglycoside nucleotidyltransf

7 gement of substrates in the enzyme.metal-ATP.isepamicin complex was determined on the basis of the me

8 eptamine ring, one enzyme-bound conformer of isepamicin (conformer 1) places the reactive 6' nitrogen

9              Conformer 2 of AAC(6')-Ii-bound isepamicin may represent an unproductive binding mode.

10 were used to determine relative distances of isepamicin protons to the Cr3+.

11  modifying enzymes) could provide one reason isepamicin remains one of the more effective aminoglycos

12  comparison of enzyme-bound conformations of isepamicin to the RNA-bound conformation of gentamycin C

13 s for the two conformers of AAC(6')-Ii-bound isepamicin were phi AB = -7.9 +/- 2.0 degrees and psi AB

14                           Both conformers of isepamicin yielded arrangements that satisfied the NOE r