| _Entry.Title | 1H and 15N Assignments and Secondary Structure of the Starch-binding Domain of ⏎Glucoamylase from Aspergillus niger⏎ |
| _Entry.Original_release_date | . |
| _Entry.Original_NMR_STAR_version | 2.1 |
| _Entry.Experimental_method | NMR |
| _Entry.Experimental_method_subtype | . |
| _Entry.Details | 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').⏎ |
| _Entry.BMRB_internal_directory_name | . |
