1H and 15N Assignments and Secondary Structure of the Starch-binding Domain of
Glucoamylase from Aspergillus niger

The chemical shifts recorded in this saveframe are from amino acid residues
where only a single set of shifts were observed.

This save frame contains the set of peak assignments for residues
P512 and T513 arising from the cis conformer of P512.

This save frame contains the peak assignment for residue
T513 arising from the cis conformer of P512. The second
shift if T513 HG2 is only observed for proteolytically-derived
SBD samples (not in the recombinant sample) due to different
glycosylation levels of T513.

This save frame contains the set of peak assignments for residues
P512 and T513 arising from the trans conformer of P512.

This save frame contains the peak assignments for residue
T513 arising from the trans conformer of P512. The
shift if T513 HG2 is only observed for proteolytically-derived
SBD samples (not in the recombinant sample) due to different
glycosylation levels of T513.

This save frame contains the set of peak assignments for residues
P570, A571 and G572 arising from the cis conformer of P570.

This save frame contains the set of peak assignments for residues
P570, A571 and G572 arising from the trans conformer of P570.

This save frame contains the peak assignments for residue A514 only.
Two sets of shifts are observed due to partial glycosylation at T513.
The second set of shifts for A514 are given in the saveframe
'_assigned_chemical_shifts_eleven'

This save frame contains the peak assignments for residue A514 only.
The shifts observed are due to partial glycosylation at T513.
The shifts listed are not observed in SBD samples
derived by proteolysis of commercial glucoamylase due to lower levels of
glycosylation.

Jacks, A.J., Sorimachi, K., Le Gal-Coeffe, M-F., Williamson, G., Archer, D.B.,
and Williamson, M.P., "1H and 15N Assignments and Secondary Structure of the
Starch-binding Domain of Glucoamylase from Aspergillus niger," Eur. J. Biochem.,
233, 568-578 (1995).

1H and 15N assignments and secondary structure of the starch-binding domain of glucoamylase from Aspergillus niger.

a disulfide-deficient mutant of the starch-binding domain of glucoamylase

Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, Minimized Average Structure

Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, 5 Structures

Glucoamylase, Granular Starch-Binding Domain, Nmr, 5 Structures

Glucoamylase, Granular Starch-Binding Domain, Nmr, Minimized Average Structure

glucoamylase I precursor [Aspergillus kawachii]

histidine-tagged glucoamylase [Aspergillus kawachii IFO 4308]

preproglucoamylase G1 [Aspergillus niger]

glucan 1,4-alpha-glucosidase glaA-Aspergillus niger [Aspergillus niger]

glucoamylase precursor [Aspergillus awamori]

preproglucoamylase G1 [Aspergillus awamori]

glucoamylase [Aspergillus niger CBS 513.88]

RecName: Full=Glucoamylase I; AltName: Full=1,4-alpha-D-glucan glucohydrolase; AltName: Full=Glucan 1,4-alpha-glucosidase; Flag

RecName: Full=Glucoamylase; AltName: Full=1,4-alpha-D-glucan glucohydrolase; AltName: Full=Glucan 1,4-alpha-glucosidase; Flags:

pIGF containing the glaA gene and a KEX2 endoproteolytic cleavage site

The data reported here represents the starch binding domain
(residues 509-616) of intact glucoamylase (EC 3.2.1.3; 1,4-alpha-D-glucan
glucohydrolase).

In this study, multiple chemical shifts were observed for a number of
amino acid residues due to cis-trans isomerisation of proline residues
and/or glycosylation at threonine residues. The submitted chemical
shifts have been grouped into six different save frames:
(1) resonances from amino acid residues that do not exhibit multiple
chemical shifts (save frame 'single_shifts'),
(2) resonances showing multiple shifts due to cis-trans isomerisation of
residue P512 (save frames '512_cis' and '512_trans'),
(3) resonances showing multiple shifts due to cis-trans isomerisation of
residue P570 (save frames '570_cis' and '570_trans'), and
(4) residue A514 which is affected by glycosylation (save frame '514').