data_4011 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Assignments and Secondary Structure of the Starch-binding Domain of Glucoamylase from Aspergillus niger ; _BMRB_accession_number 4011 _BMRB_flat_file_name bmr4011.str _Entry_type update _Submission_date 1996-03-01 _Accession_date 1997-03-19 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _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'). ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jacks Amanda J. . 2 Sorimachi Kay . . 3 'Le Gal-Coeffet' Marie-Francoise . . 4 Williamson Gary . . 5 Archer David B. . 6 Williamson Michael P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 9 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 587 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-17 update BMRB 'Complete natural source information' 2000-11-10 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; 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). ; _Citation_title ; 1H and 15N Assignments and Secondary Structure of the Starch-binding Domain of Glucoamylase from Aspergillus niger ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 96067700 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jacks Amanda J. . 2 Sorimachi Kay . . 3 'Le Gal-Coeffet' Marie-Francoise . . 4 Williamson Gary . . 5 Archer David B. . 6 Williamson Michael P. . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full 'European Journal of Biochemistry' _Journal_volume 233 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 568 _Page_last 578 _Year 1995 _Details . loop_ _Keyword glucoamylase NMR 'nuclear magnetic resonance' protein 'resonance assignments' SBD 'secondary structure' 'starch binding domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_G1-SBD _Saveframe_category molecular_system _Mol_system_name 'Starch binding domain' _Abbreviation_common G1-SBD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Starch binding domain' $G1-SBD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'binding domain of a glucohydrolase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_G1-SBD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Starch binding domain' _Abbreviation_common G1-SBD _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 108 _Mol_residue_sequence ; CTTPTAVAVTFDLTATTTYG ENIYLVGSISQLGDWETSDG IALSADKYTSSDPLWYVTVT LPAGESFEYKFIRIESDDSV EWESDPNREYTVPQACGTST ATVTDTWR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 509 CYS 2 510 THR 3 511 THR 4 512 PRO 5 513 THR 6 514 ALA 7 515 VAL 8 516 ALA 9 517 VAL 10 518 THR 11 519 PHE 12 520 ASP 13 521 LEU 14 522 THR 15 523 ALA 16 524 THR 17 525 THR 18 526 THR 19 527 TYR 20 528 GLY 21 529 GLU 22 530 ASN 23 531 ILE 24 532 TYR 25 533 LEU 26 534 VAL 27 535 GLY 28 536 SER 29 537 ILE 30 538 SER 31 539 GLN 32 540 LEU 33 541 GLY 34 542 ASP 35 543 TRP 36 544 GLU 37 545 THR 38 546 SER 39 547 ASP 40 548 GLY 41 549 ILE 42 550 ALA 43 551 LEU 44 552 SER 45 553 ALA 46 554 ASP 47 555 LYS 48 556 TYR 49 557 THR 50 558 SER 51 559 SER 52 560 ASP 53 561 PRO 54 562 LEU 55 563 TRP 56 564 TYR 57 565 VAL 58 566 THR 59 567 VAL 60 568 THR 61 569 LEU 62 570 PRO 63 571 ALA 64 572 GLY 65 573 GLU 66 574 SER 67 575 PHE 68 576 GLU 69 577 TYR 70 578 LYS 71 579 PHE 72 580 ILE 73 581 ARG 74 582 ILE 75 583 GLU 76 584 SER 77 585 ASP 78 586 ASP 79 587 SER 80 588 VAL 81 589 GLU 82 590 TRP 83 591 GLU 84 592 SER 85 593 ASP 86 594 PRO 87 595 ASN 88 596 ARG 89 597 GLU 90 598 TYR 91 599 THR 92 600 VAL 93 601 PRO 94 602 GLN 95 603 ALA 96 604 CYS 97 605 GLY 98 606 THR 99 607 SER 100 608 THR 101 609 ALA 102 610 THR 103 611 VAL 104 612 THR 105 613 ASP 106 614 THR 107 615 TRP 108 616 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-04-08 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 11428 "a disulfide-deficient mutant of the starch-binding domain of glucoamylase" 99.07 110 99.07 99.07 2.81e-67 PDB 1AC0 "Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, Minimized Average Structure" 100.00 108 100.00 100.00 7.00e-70 PDB 1ACZ "Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, 5 Structures" 99.07 108 100.00 100.00 6.85e-69 PDB 1KUL "Glucoamylase, Granular Starch-Binding Domain, Nmr, 5 Structures" 100.00 108 100.00 100.00 7.00e-70 PDB 1KUM "Glucoamylase, Granular Starch-Binding Domain, Nmr, Minimized Average Structure" 100.00 108 100.00 100.00 7.00e-70 DBJ BAA00331 "glucoamylase I precursor [Aspergillus kawachii]" 100.00 639 97.22 99.07 7.47e-64 DBJ BAD06004 "glucoamylase [Aspergillus awamori]" 100.00 639 97.22 99.07 1.50e-63 DBJ GAA90865 "histidine-tagged glucoamylase [Aspergillus kawachii IFO 4308]" 100.00 639 97.22 99.07 7.47e-64 EMBL CAA25219 "glucoamylase G1 [Aspergillus niger]" 100.00 640 100.00 100.00 1.60e-65 EMBL CAA25303 "preproglucoamylase G1 [Aspergillus niger]" 100.00 640 100.00 100.00 1.60e-65 EMBL CAK38411 "glucan 1,4-alpha-glucosidase glaA-Aspergillus niger [Aspergillus niger]" 100.00 640 100.00 100.00 1.60e-65 GB AAB02927 "glucoamylase precursor [Aspergillus awamori]" 100.00 639 97.22 99.07 8.73e-64 GB AAB59296 "preproglucoamylase G1 [Aspergillus awamori]" 100.00 640 100.00 100.00 1.60e-65 GB AAP04499 "glucoamylase [Aspergillus niger]" 100.00 639 100.00 100.00 1.92e-65 GB AAT58037 "glucoamylase [Aspergillus ficuum]" 100.00 640 100.00 100.00 1.83e-65 GB AAT67041 "glucoamylase [Aspergillus niger]" 100.00 640 99.07 99.07 6.13e-65 PRF 1008149A "glucoamylase G1" 100.00 614 100.00 100.00 1.14e-65 PRF 1508161A "glucoamylase I" 100.00 640 97.22 99.07 7.58e-64 REF XP_001390530 "glucoamylase [Aspergillus niger CBS 513.88]" 100.00 640 100.00 100.00 1.60e-65 SP P23176 "RecName: Full=Glucoamylase I; AltName: Full=1,4-alpha-D-glucan glucohydrolase; AltName: Full=Glucan 1,4-alpha-glucosidase; Flag" 100.00 639 97.22 99.07 7.47e-64 SP P69327 "RecName: Full=Glucoamylase; AltName: Full=1,4-alpha-D-glucan glucohydrolase; AltName: Full=Glucan 1,4-alpha-glucosidase; Flags:" 100.00 640 100.00 100.00 1.60e-65 SP P69328 "RecName: Full=Glucoamylase; AltName: Full=1,4-alpha-D-glucan glucohydrolase; AltName: Full=Glucan 1,4-alpha-glucosidase; Flags:" 100.00 640 100.00 100.00 1.60e-65 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $G1-SBD 'Aspergillus niger' 5061 Eukaryota Fungi Aspergillus niger stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $G1-SBD 'recombinant technology' fungus Aspergillus niger AB4.1 plasmid 'pIGF containing the glaA gene and a KEX2 endoproteolytic cleavage site' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $G1-SBD 1.0 mM '[U-100% 15N]' H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer . _Model . _Field_strength 500 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.2 . n/a temperature 313 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 external direct . . . . H2O N 15 protons ppm 118.04 . indirect . . . 0.101329122 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts recorded in this saveframe are from amino acid residues where only a single set of shifts were observed. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Starch binding domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 THR H H 7.72 . 1 2 . 2 THR HA H 4.66 . 1 3 . 2 THR HB H 4.22 . 1 4 . 2 THR HG2 H 1.28 . 1 5 . 3 THR H H 8.92 . 1 6 . 3 THR HA H 4.35 . 1 7 . 3 THR HB H 3.93 . 1 8 . 3 THR HG2 H 1.19 . 1 9 . 3 THR N N 129.6 . 9 10 . 7 VAL H H 9.05 . 1 11 . 7 VAL HA H 4.11 . 1 12 . 7 VAL HB H 1.65 . 1 13 . 7 VAL HG1 H 0.48 . 1 14 . 7 VAL HG2 H 0.84 . 1 15 . 7 VAL N N 121.5 . 1 16 . 8 ALA H H 8.13 . 1 17 . 8 ALA HA H 4.55 . 1 18 . 8 ALA HB H 1.29 . 1 19 . 8 ALA N N 129.7 . 1 20 . 9 VAL H H 9.25 . 1 21 . 9 VAL HA H 4.44 . 1 22 . 9 VAL HB H 2.15 . 1 23 . 9 VAL HG1 H 1.02 . 1 24 . 9 VAL HG2 H -0.01 . 1 25 . 9 VAL N N 132.8 . 1 26 . 10 THR H H 9.17 . 1 27 . 10 THR HA H 5.17 . 1 28 . 10 THR HB H 4.04 . 1 29 . 10 THR HG2 H 1.15 . 1 30 . 10 THR N N 125.3 . 1 31 . 11 PHE H H 9.62 . 1 32 . 11 PHE HA H 4.75 . 1 33 . 11 PHE HB2 H 3.19 . 1 34 . 11 PHE HB3 H 3.03 . 1 35 . 11 PHE HD1 H 7.1 . 1 36 . 11 PHE HD2 H 7.1 . 1 37 . 11 PHE HE1 H 6.43 . 1 38 . 11 PHE HE2 H 6.43 . 1 39 . 11 PHE HZ H 6.53 . 1 40 . 11 PHE N N 127.6 . 1 41 . 12 ASP H H 9.09 . 1 42 . 12 ASP HA H 5.41 . 1 43 . 12 ASP HB3 H 2.93 . 1 44 . 12 ASP HB2 H 2.7 . 1 45 . 12 ASP N N 122.7 . 1 46 . 13 LEU H H 9.63 . 1 47 . 13 LEU HA H 5.08 . 1 48 . 13 LEU HB2 H 1.55 . 1 49 . 13 LEU HB3 H 0.5 . 1 50 . 13 LEU HG H 1.11 . 1 51 . 13 LEU HD1 H 0.43 . 1 52 . 13 LEU HD2 H 0.19 . 1 53 . 13 LEU N N 127.8 . 1 54 . 14 THR H H 8.75 . 1 55 . 14 THR HA H 4.98 . 1 56 . 14 THR HB H 4.29 . 1 57 . 14 THR HG2 H 1.27 . 1 58 . 14 THR N N 124.2 . 1 59 . 15 ALA H H 9.03 . 1 60 . 15 ALA HA H 4.54 . 1 61 . 15 ALA HB H 1.04 . 1 62 . 15 ALA N N 131.3 . 1 63 . 16 THR H H 8.54 . 1 64 . 16 THR HA H 4.86 . 1 65 . 16 THR HB H 4.08 . 1 66 . 16 THR HG2 H 1.28 . 1 67 . 16 THR N N 118.2 . 1 68 . 17 THR H H 8.83 . 1 69 . 17 THR HA H 4.67 . 1 70 . 17 THR HB H 4.11 . 1 71 . 17 THR HG2 H 1.32 . 1 72 . 17 THR N N 118.8 . 1 73 . 18 THR H H 8.71 . 1 74 . 18 THR HA H 4.62 . 1 75 . 18 THR HB H 4.2 . 1 76 . 18 THR HG2 H 1.16 . 1 77 . 18 THR N N 124.2 . 9 78 . 19 TYR H H 8.23 . 1 79 . 19 TYR HA H 4.26 . 1 80 . 19 TYR HB2 H 3.07 . 1 81 . 19 TYR HB3 H 2.93 . 1 82 . 19 TYR HD1 H 7.13 . 1 83 . 19 TYR HD2 H 7.13 . 1 84 . 19 TYR HE1 H 6.86 . 1 85 . 19 TYR HE2 H 6.86 . 1 86 . 19 TYR N N 120.9 . 1 87 . 20 GLY H H 8.53 . 1 88 . 20 GLY HA2 H 3.93 . 2 89 . 20 GLY HA3 H 3.39 . 2 90 . 20 GLY N N 108.6 . 1 91 . 21 GLU H H 7.48 . 1 92 . 21 GLU HA H 4.7 . 1 93 . 21 GLU HB2 H 1.87 . 2 94 . 21 GLU HB3 H 1.84 . 2 95 . 21 GLU HG2 H 2.06 . 1 96 . 21 GLU HG3 H 2.06 . 1 97 . 22 ASN H H 8.09 . 1 98 . 22 ASN HA H 5.17 . 1 99 . 22 ASN HB2 H 2.73 . 1 100 . 22 ASN HB3 H 2.54 . 1 101 . 22 ASN HD21 H 7.55 . 2 102 . 22 ASN HD22 H 6.68 . 2 103 . 22 ASN N N 120.7 . 1 104 . 23 ILE H H 5.48 . 1 105 . 23 ILE HA H 4.94 . 1 106 . 23 ILE HB H 0.47 . 1 107 . 23 ILE HG12 H -0.26 . 2 108 . 23 ILE HG13 H -0.37 . 2 109 . 23 ILE HG2 H 0.72 . 1 110 . 23 ILE HD1 H -0.43 . 1 111 . 23 ILE N N 119.5 . 1 112 . 24 TYR H H 8.98 . 1 113 . 24 TYR HA H 5.24 . 1 114 . 24 TYR HB2 H 2.56 . 1 115 . 24 TYR HB3 H 2.32 . 1 116 . 24 TYR HD1 H 6.62 . 1 117 . 24 TYR HD2 H 6.62 . 1 118 . 24 TYR N N 126.00 . 1 119 . 25 LEU H H 9.08 . 1 120 . 25 LEU HA H 4.61 . 1 121 . 25 LEU HB2 H 1.52 . 1 122 . 25 LEU HB3 H 1.25 . 1 123 . 25 LEU HG H 0.83 . 1 124 . 25 LEU HD1 H -0.09 . 1 125 . 25 LEU HD2 H -0.25 . 1 126 . 25 LEU N N 124.3 . 1 127 . 26 VAL H H 8.33 . 1 128 . 26 VAL HA H 5.06 . 1 129 . 26 VAL HB H 1.91 . 1 130 . 26 VAL HG1 H 0.86 . 1 131 . 26 VAL HG2 H 0.78 . 1 132 . 26 VAL N N 120.5 . 1 133 . 27 GLY H H 7.42 . 1 134 . 27 GLY HA2 H 3.56 . 2 135 . 27 GLY HA3 H 2.85 . 2 136 . 27 GLY N N 105.6 . 1 137 . 28 SER H H 8.3 . 1 138 . 28 SER HA H 3.36 . 1 139 . 28 SER N N 111.1 . 1 140 . 29 ILE H H 6.51 . 1 141 . 29 ILE HA H 4.89 . 1 142 . 29 ILE HB H 2.23 . 1 143 . 29 ILE HG12 H 0.92 . 2 144 . 29 ILE HG13 H 0.55 . 2 145 . 29 ILE HG2 H 1.06 . 1 146 . 29 ILE HD1 H 0.39 . 1 147 . 29 ILE N N 110.8 . 1 148 . 30 SER H H 9.05 . 1 149 . 30 SER HA H 4.55 . 1 150 . 30 SER HB2 H 3.88 . 1 151 . 30 SER HB3 H 3.88 . 1 152 . 30 SER N N 121.5 . 1 153 . 31 GLN H H 9.19 . 1 154 . 31 GLN HA H 3.99 . 1 155 . 31 GLN HB3 H 1.79 . 1 156 . 31 GLN HB2 H 1.58 . 1 157 . 31 GLN HG2 H 2.66 . 2 158 . 31 GLN HG3 H 2.52 . 2 159 . 31 GLN HE21 H 7.61 . 2 160 . 31 GLN HE22 H 6.78 . 2 161 . 31 GLN N N 120.6 . 1 162 . 31 GLN NE2 N 109.2 . 1 163 . 32 LEU H H 7.24 . 1 164 . 32 LEU HA H 4.39 . 1 165 . 32 LEU HB3 H 1.44 . 1 166 . 32 LEU HB2 H 0.84 . 1 167 . 32 LEU HG H 0.87 . 1 168 . 32 LEU HD1 H 0.35 . 2 169 . 32 LEU HD2 H 0.02 . 2 170 . 32 LEU N N 113.1 . 1 171 . 33 GLY H H 7.47 . 1 172 . 33 GLY HA2 H 4.05 . 2 173 . 33 GLY HA3 H 3.73 . 2 174 . 33 GLY N N 104.9 . 1 175 . 34 ASP H H 7.75 . 1 176 . 34 ASP HA H 4.15 . 1 177 . 34 ASP HB3 H 3.14 . 1 178 . 34 ASP HB2 H 2.45 . 1 179 . 34 ASP N N 122.3 . 1 180 . 35 TRP H H 7.6 . 1 181 . 35 TRP HA H 4.19 . 1 182 . 35 TRP HB2 H 3.7 . 2 183 . 35 TRP HB3 H 3.66 . 2 184 . 35 TRP HD1 H 7.13 . 1 185 . 35 TRP HE1 H 10.07 . 1 186 . 35 TRP HE3 H 7.56 . 1 187 . 35 TRP HZ2 H 7.42 . 1 188 . 35 TRP HZ3 H 7.02 . 1 189 . 35 TRP HH2 H 6.73 . 1 190 . 35 TRP N N 104.5 . 1 191 . 35 TRP NE1 N 127.5 . 1 192 . 36 GLU H H 7.92 . 1 193 . 36 GLU HA H 4.7 . 1 194 . 36 GLU HB2 H 2.2 . 2 195 . 36 GLU HB3 H 2.11 . 2 196 . 36 GLU HG2 H 2.48 . 2 197 . 36 GLU HG3 H 2.43 . 2 198 . 36 GLU N N 121.4 . 1 199 . 37 THR H H 8.55 . 1 200 . 37 THR HA H 3.48 . 1 201 . 37 THR HB H 3.13 . 1 202 . 37 THR HG2 H 1.23 . 1 203 . 37 THR N N 118.9 . 1 204 . 38 SER H H 8.21 . 1 205 . 38 SER HA H 4.15 . 1 206 . 38 SER HB2 H 3.92 . 1 207 . 38 SER HB3 H 3.84 . 1 208 . 38 SER N N 115.00 . 1 209 . 39 ASP H H 7.63 . 1 210 . 39 ASP HA H 5.09 . 1 211 . 39 ASP HB3 H 3.14 . 1 212 . 39 ASP HB2 H 2.6 . 1 213 . 39 ASP N N 120.4 . 1 214 . 40 GLY H H 7.33 . 1 215 . 40 GLY HA2 H 4.17 . 2 216 . 40 GLY HA3 H 3.3 . 2 217 . 40 GLY N N 104.3 . 1 218 . 41 ILE H H 8.96 . 1 219 . 41 ILE HA H 4.33 . 1 220 . 41 ILE HB H 1.81 . 1 221 . 41 ILE HG12 H 1.39 . 2 222 . 41 ILE HG13 H 1.32 . 2 223 . 41 ILE HG2 H 0.88 . 1 224 . 41 ILE HD1 H 0.83 . 1 225 . 41 ILE N N 120.00 . 1 226 . 42 ALA H H 8.59 . 1 227 . 42 ALA HA H 3.53 . 1 228 . 42 ALA HB H 1.18 . 1 229 . 42 ALA N N 131.00 . 1 230 . 43 LEU H H 7.91 . 1 231 . 43 LEU HA H 4.49 . 1 232 . 43 LEU HB3 H 2.11 . 1 233 . 43 LEU HB2 H 1.5 . 1 234 . 43 LEU HG H 1.67 . 1 235 . 43 LEU HD1 H 0.99 . 1 236 . 43 LEU HD2 H 0.81 . 1 237 . 43 LEU N N 123.2 . 1 238 . 44 SER H H 9.02 . 1 239 . 44 SER HA H 4.69 . 1 240 . 44 SER HB2 H 3.54 . 1 241 . 44 SER HB3 H 3.18 . 1 242 . 44 SER N N 112.7 . 1 243 . 45 ALA H H 8.64 . 1 244 . 45 ALA HA H 4.14 . 1 245 . 45 ALA HB H 0.08 . 1 246 . 45 ALA N N 130.5 . 1 247 . 46 ASP H H 8.28 . 1 248 . 46 ASP HA H 4.28 . 1 249 . 46 ASP HB2 H 2.9 . 1 250 . 46 ASP HB3 H 2.65 . 1 251 . 46 ASP N N 119.6 . 1 252 . 47 LYS H H 9.33 . 1 253 . 47 LYS HA H 4.49 . 1 254 . 47 LYS HB2 H 1.66 . 1 255 . 47 LYS HB3 H 1.66 . 1 256 . 47 LYS HG2 H 2.02 . 2 257 . 47 LYS HG3 H 1.33 . 2 258 . 47 LYS HD2 H 1.46 . 2 259 . 47 LYS HD3 H 1.24 . 2 260 . 47 LYS HE2 H 2.69 . 1 261 . 47 LYS HE3 H 2.69 . 1 262 . 47 LYS N N 119.9 . 1 263 . 48 TYR H H 7.45 . 1 264 . 48 TYR HA H 4.24 . 1 265 . 48 TYR HB2 H 2.97 . 1 266 . 48 TYR HB3 H 2.61 . 1 267 . 48 TYR HD1 H 6.58 . 1 268 . 48 TYR HD2 H 6.58 . 1 269 . 48 TYR HE1 H 7.19 . 1 270 . 48 TYR HE2 H 7.19 . 1 271 . 48 TYR N N 123.5 . 1 272 . 49 THR H H 7.79 . 1 273 . 49 THR HA H 4.69 . 1 274 . 49 THR HB H 3.86 . 1 275 . 49 THR HG2 H 1.23 . 1 276 . 49 THR N N 121.4 . 1 277 . 50 SER H H 8.56 . 1 278 . 50 SER HA H 4.09 . 1 279 . 50 SER HB2 H 3.96 . 1 280 . 50 SER HB3 H 3.96 . 1 281 . 50 SER N N 113.5 . 1 282 . 51 SER H H 7.69 . 1 283 . 51 SER HA H 4.35 . 1 284 . 51 SER HB2 H 3.8 . 2 285 . 51 SER HB3 H 3.74 . 2 286 . 51 SER N N 112.9 . 1 287 . 52 ASP H H 7.38 . 1 288 . 52 ASP HA H 4.91 . 1 289 . 52 ASP HB2 H 2.72 . 2 290 . 52 ASP HB3 H 2.36 . 2 291 . 52 ASP N N 120.9 . 1 292 . 53 PRO HA H 3.45 . 1 293 . 53 PRO HB2 H 1.57 . 1 294 . 53 PRO HB3 H 1.57 . 1 295 . 53 PRO HG2 H 1.88 . 2 296 . 53 PRO HG3 H 2.37 . 2 297 . 53 PRO HD2 H 3.58 . 2 298 . 53 PRO HD3 H 3.18 . 2 299 . 54 LEU H H 7.77 . 1 300 . 54 LEU HA H 4.88 . 1 301 . 54 LEU HB2 H 1.48 . 2 302 . 54 LEU HB3 H 1.26 . 2 303 . 54 LEU HG H 1.4 . 1 304 . 54 LEU HD1 H 0.87 . 2 305 . 54 LEU HD2 H 0.72 . 2 306 . 54 LEU N N 128.1 . 1 307 . 55 TRP H H 9.67 . 1 308 . 55 TRP HA H 5.11 . 1 309 . 55 TRP HB3 H 3.15 . 1 310 . 55 TRP HB2 H 2.89 . 1 311 . 55 TRP HD1 H 7.57 . 1 312 . 55 TRP HE1 H 9.44 . 1 313 . 55 TRP HE3 H 7.05 . 1 314 . 55 TRP HZ2 H 7.41 . 1 315 . 55 TRP HZ3 H 7.2 . 1 316 . 55 TRP HH2 H 7.46 . 1 317 . 55 TRP N N 128.6 . 1 318 . 55 TRP NE1 N 131.4 . 1 319 . 56 TYR H H 8.49 . 1 320 . 56 TYR HA H 6.56 . 1 321 . 56 TYR HB2 H 3.1 . 1 322 . 56 TYR HB3 H 3.1 . 1 323 . 56 TYR HD1 H 7.00 . 1 324 . 56 TYR HD2 H 7.00 . 1 325 . 56 TYR HE1 H 6.84 . 1 326 . 56 TYR HE2 H 6.84 . 1 327 . 56 TYR N N 115.8 . 1 328 . 57 VAL H H 8.66 . 1 329 . 57 VAL HA H 4.51 . 1 330 . 57 VAL HB H 2.49 . 1 331 . 57 VAL HG1 H 1.11 . 1 332 . 57 VAL HG2 H 0.86 . 1 333 . 57 VAL N N 117.9 . 1 334 . 58 THR H H 8.54 . 1 335 . 58 THR HA H 5.65 . 1 336 . 58 THR HB H 3.87 . 1 337 . 58 THR HG2 H 1.07 . 1 338 . 58 THR N N 124.7 . 1 339 . 59 VAL H H 9.37 . 1 340 . 59 VAL HA H 4.49 . 1 341 . 59 VAL HB H 1.97 . 1 342 . 59 VAL HG1 H 0.91 . 2 343 . 59 VAL HG2 H 0.89 . 2 344 . 59 VAL N N 126.4 . 1 345 . 60 THR H H 8.72 . 1 346 . 60 THR HA H 4.89 . 1 347 . 60 THR HB H 3.99 . 1 348 . 60 THR HG2 H 1.02 . 1 349 . 60 THR N N 124.2 . 1 350 . 61 LEU H H 8.97 . 1 351 . 61 LEU HA H 4.99 . 1 352 . 61 LEU HB2 H 1.59 . 1 353 . 61 LEU HB3 H 1.32 . 1 354 . 61 LEU HG H 1.54 . 1 355 . 61 LEU HD1 H 0.81 . 1 356 . 61 LEU HD2 H 0.59 . 1 357 . 61 LEU N N 129.4 . 1 358 . 65 GLU H H 7.21 . 1 359 . 65 GLU HA H 4.4 . 1 360 . 65 GLU HB2 H 2.15 . 2 361 . 65 GLU HB3 H 2.1 . 2 362 . 65 GLU HG2 H 2.5 . 2 363 . 65 GLU HG3 H 2.4 . 2 364 . 65 GLU N N 120.2 . 1 365 . 66 SER H H 8.65 . 1 366 . 66 SER HA H 5.66 . 1 367 . 66 SER HB2 H 3.89 . 1 368 . 66 SER HB3 H 3.74 . 1 369 . 66 SER N N 121.00 . 1 370 . 67 PHE H H 8.52 . 1 371 . 67 PHE HA H 4.94 . 1 372 . 67 PHE HB2 H 3.2 . 1 373 . 67 PHE HB3 H 3.2 . 1 374 . 67 PHE HD1 H 6.87 . 1 375 . 67 PHE HD2 H 6.87 . 1 376 . 67 PHE N N 117.8 . 1 377 . 68 GLU H H 8.62 . 1 378 . 68 GLU HA H 5.9 . 1 379 . 68 GLU HB2 H 2.39 . 2 380 . 68 GLU HB3 H 2.28 . 2 381 . 68 GLU HG2 H 2.55 . 2 382 . 68 GLU HG3 H 2.48 . 2 383 . 68 GLU N N 118.8 . 1 384 . 69 TYR H H 9.00 . 1 385 . 69 TYR HA H 5.26 . 1 386 . 69 TYR HB2 H 2.88 . 1 387 . 69 TYR HB3 H 2.88 . 1 388 . 69 TYR HD1 H 6.87 . 1 389 . 69 TYR HD2 H 6.87 . 1 390 . 69 TYR HE1 H 6.99 . 1 391 . 69 TYR HE2 H 6.99 . 1 392 . 69 TYR N N 116.8 . 1 393 . 70 LYS H H 9.13 . 1 394 . 70 LYS HA H 4.22 . 1 395 . 70 LYS HB2 H 1.94 . 2 396 . 70 LYS HB3 H 2.69 . 4 397 . 70 LYS HG2 H 2.47 . 4 398 . 70 LYS HG3 H 2.19 . 4 399 . 70 LYS HD2 H 0.89 . 4 400 . 70 LYS HE2 H 0.67 . 4 401 . 70 LYS N N 118.1 . 1 402 . 71 PHE H H 8.86 . 1 403 . 71 PHE HA H 5.58 . 1 404 . 71 PHE HB3 H 3.11 . 1 405 . 71 PHE HB2 H 2.78 . 1 406 . 71 PHE HD1 H 6.68 . 1 407 . 71 PHE HD2 H 6.68 . 1 408 . 71 PHE HE1 H 7.54 . 1 409 . 71 PHE HE2 H 7.54 . 1 410 . 71 PHE N N 116.4 . 1 411 . 72 ILE H H 8.96 . 1 412 . 72 ILE HA H 5.35 . 1 413 . 72 ILE HB H 1.28 . 1 414 . 72 ILE HG12 H 1.16 . 2 415 . 72 ILE HG13 H 0.69 . 2 416 . 72 ILE HG2 H -0.2 . 1 417 . 72 ILE HD1 H 0.2 . 1 418 . 72 ILE N N 110.9 . 1 419 . 73 ARG H H 9.14 . 1 420 . 73 ARG HA H 4.88 . 1 421 . 73 ARG HB2 H 1.28 . 2 422 . 73 ARG HB3 H 1.24 . 2 423 . 73 ARG HG2 H 1.65 . 2 424 . 73 ARG HG3 H 1.4 . 2 425 . 73 ARG HD2 H 3.09 . 1 426 . 73 ARG N N 120.4 . 1 427 . 74 ILE H H 8.74 . 1 428 . 74 ILE HA H 4.81 . 1 429 . 74 ILE HB H 1.74 . 1 430 . 74 ILE HG12 H 1.24 . 2 431 . 74 ILE HG13 H 0.85 . 2 432 . 74 ILE HG2 H 0.89 . 1 433 . 74 ILE HD1 H 0.23 . 1 434 . 74 ILE N N 121.1 . 1 435 . 75 GLU H H 8.79 . 1 436 . 75 GLU HA H 4.4 . 1 437 . 75 GLU HB3 H 2.24 . 1 438 . 75 GLU HB2 H 2.18 . 1 439 . 75 GLU HG2 H 2.39 . 2 440 . 75 GLU HG3 H 2.31 . 2 441 . 75 GLU N N 125.6 . 1 442 . 76 SER H H 9.04 . 1 443 . 76 SER HA H 4.21 . 1 444 . 76 SER HB3 H 4.05 . 1 445 . 76 SER HB2 H 3.88 . 1 446 . 76 SER N N 117.1 . 1 447 . 77 ASP H H 7.64 . 1 448 . 77 ASP HA H 4.6 . 1 449 . 77 ASP HB2 H 3.09 . 1 450 . 77 ASP HB3 H 2.53 . 1 451 . 77 ASP N N 119.1 . 1 452 . 78 ASP H H 8.24 . 1 453 . 78 ASP HA H 4.22 . 1 454 . 78 ASP HB3 H 3.13 . 1 455 . 78 ASP HB2 H 2.97 . 1 456 . 78 ASP N N 113.2 . 1 457 . 79 SER H H 8.02 . 1 458 . 79 SER HA H 4.34 . 1 459 . 79 SER HB2 H 3.87 . 1 460 . 79 SER HB3 H 3.87 . 1 461 . 79 SER N N 116.00 . 1 462 . 80 VAL H H 8.21 . 1 463 . 80 VAL HA H 4.95 . 1 464 . 80 VAL HB H 1.94 . 1 465 . 80 VAL HG1 H 0.86 . 1 466 . 80 VAL HG2 H 0.54 . 1 467 . 80 VAL N N 119.9 . 1 468 . 81 GLU H H 9.32 . 1 469 . 81 GLU HA H 4.97 . 1 470 . 81 GLU HB3 H 2.17 . 1 471 . 81 GLU HB2 H 1.98 . 1 472 . 81 GLU HG2 H 2.43 . 1 473 . 81 GLU HG3 H 2.43 . 1 474 . 81 GLU N N 126.6 . 1 475 . 82 TRP H H 9.19 . 1 476 . 82 TRP HA H 4.78 . 1 477 . 82 TRP HB3 H 3.43 . 1 478 . 82 TRP HB2 H 3.08 . 1 479 . 82 TRP HD1 H 7.33 . 1 480 . 82 TRP HE1 H 10.29 . 1 481 . 82 TRP HE3 H 7.37 . 1 482 . 82 TRP HZ2 H 7.51 . 1 483 . 82 TRP HZ3 H 7.01 . 1 484 . 82 TRP HH2 H 7.31 . 1 485 . 82 TRP N N 126.00 . 1 486 . 82 TRP NE1 N 130.1 . 1 487 . 83 GLU H H 7.49 . 1 488 . 83 GLU HA H 3.63 . 1 489 . 83 GLU HB2 H 1.89 . 1 490 . 83 GLU HB3 H 1.7 . 1 491 . 83 GLU HG2 H 2.02 . 1 492 . 83 GLU HG3 H 2.02 . 1 493 . 83 GLU N N 119.3 . 1 494 . 84 SER H H 9.27 . 1 495 . 84 SER HA H 4.3 . 1 496 . 84 SER HB2 H 4.04 . 1 497 . 84 SER HB3 H 3.72 . 1 498 . 84 SER N N 117.6 . 1 499 . 85 ASP H H 8.32 . 1 500 . 85 ASP HA H 4.12 . 1 501 . 85 ASP HB3 H 2.56 . 1 502 . 85 ASP HB2 H 2.38 . 1 503 . 85 ASP N N 121.1 . 1 504 . 86 PRO HA H 4.44 . 1 505 . 86 PRO HB2 H 2.3 . 1 506 . 86 PRO HB3 H 2.3 . 1 507 . 86 PRO HG2 H 1.9 . 2 508 . 86 PRO HG3 H 1.57 . 2 509 . 86 PRO HD2 H 3.37 . 1 510 . 86 PRO HD3 H 3.37 . 1 511 . 87 ASN H H 8.4 . 1 512 . 87 ASN HA H 4.35 . 1 513 . 87 ASN HB3 H 2.87 . 1 514 . 87 ASN HB2 H 2.71 . 1 515 . 87 ASN HD21 H 7.68 . 2 516 . 87 ASN HD22 H 6.38 . 2 517 . 87 ASN N N 114.7 . 1 518 . 87 ASN ND2 N 110.7 . 1 519 . 88 ARG H H 8.41 . 1 520 . 88 ARG HA H 4.16 . 1 521 . 88 ARG HB3 H 1.1 . 1 522 . 88 ARG HB2 H -0.06 . 1 523 . 88 ARG N N 121.9 . 1 524 . 89 GLU H H 8.36 . 1 525 . 89 GLU HA H 5.28 . 1 526 . 89 GLU HB2 H 2.08 . 1 527 . 89 GLU HB3 H 1.89 . 1 528 . 89 GLU HG2 H 2.29 . 1 529 . 89 GLU HG3 H 2.29 . 1 530 . 89 GLU N N 117.5 . 1 531 . 90 TYR H H 8.33 . 1 532 . 90 TYR HA H 4.59 . 1 533 . 90 TYR HB2 H 3.04 . 1 534 . 90 TYR HB3 H 1.74 . 1 535 . 90 TYR HD1 H 7.00 . 1 536 . 90 TYR HD2 H 7.00 . 1 537 . 90 TYR HE1 H 6.56 . 1 538 . 90 TYR HE2 H 6.56 . 1 539 . 90 TYR N N 123.6 . 1 540 . 91 THR H H 6.32 . 1 541 . 91 THR HA H 4.63 . 1 542 . 91 THR HB H 3.42 . 1 543 . 91 THR HG2 H 0.79 . 1 544 . 91 THR N N 121.1 . 1 545 . 92 VAL H H 8.64 . 1 546 . 92 VAL HA H 3.81 . 1 547 . 92 VAL HB H 2.3 . 1 548 . 92 VAL HG1 H 1.04 . 1 549 . 92 VAL HG2 H 1.35 . 1 550 . 92 VAL N N 128.4 . 1 551 . 93 PRO HA H 4.13 . 1 552 . 93 PRO HB2 H 2.33 . 2 553 . 93 PRO HB3 H 1.76 . 2 554 . 93 PRO HG2 H 1.99 . 2 555 . 93 PRO HG3 H 1.9 . 2 556 . 93 PRO HD2 H 3.52 . 2 557 . 93 PRO HD3 H 3.35 . 2 558 . 94 GLN H H 8.23 . 1 559 . 94 GLN HA H 4.37 . 1 560 . 94 GLN HB2 H 2.17 . 2 561 . 94 GLN HB3 H 2.09 . 2 562 . 94 GLN HG2 H 2.42 . 1 563 . 94 GLN HG3 H 2.42 . 1 564 . 94 GLN HE21 H 7.32 . 2 565 . 94 GLN HE22 H 6.72 . 2 566 . 94 GLN N N 122.7 . 1 567 . 94 GLN NE2 N 110.6 . 1 568 . 95 ALA H H 8.85 . 1 569 . 95 ALA HA H 4.38 . 1 570 . 95 ALA HB H 0.68 . 1 571 . 96 CYS H H 7.4 . 1 572 . 96 CYS HB2 H 3.95 . 2 573 . 96 CYS HB3 H 3.37 . 2 574 . 97 GLY H H 7.09 . 1 575 . 97 GLY HA2 H 3.33 . 2 576 . 97 GLY HA3 H 3.08 . 2 577 . 97 GLY N N 127.5 . 9 578 . 98 THR H H 8.68 . 1 579 . 98 THR HA H 4.37 . 1 580 . 98 THR HB H 4.00 . 1 581 . 98 THR HG2 H 1.12 . 1 582 . 98 THR N N 125.4 . 1 583 . 99 SER H H 8.7 . 1 584 . 99 SER HA H 4.72 . 1 585 . 99 SER HB2 H 4.15 . 2 586 . 99 SER HB3 H 3.89 . 2 587 . 99 SER N N 124.00 . 9 588 . 100 THR H H 7.89 . 1 589 . 100 THR HA H 5.28 . 1 590 . 100 THR HB H 4.28 . 1 591 . 100 THR HG2 H 1.23 . 1 592 . 100 THR N N 114.4 . 1 593 . 101 ALA H H 8.23 . 1 594 . 101 ALA HA H 4.57 . 1 595 . 101 ALA HB H 1.35 . 1 596 . 101 ALA N N 120.8 . 1 597 . 102 THR H H 8.46 . 1 598 . 102 THR HA H 5.12 . 1 599 . 102 THR HB H 3.82 . 1 600 . 102 THR HG2 H 1.03 . 1 601 . 102 THR N N 116.6 . 1 602 . 103 VAL H H 9.2 . 1 603 . 103 VAL HA H 4.05 . 1 604 . 103 VAL HB H 1.4 . 1 605 . 103 VAL HG1 H 0.76 . 1 606 . 103 VAL HG2 H -0.18 . 1 607 . 103 VAL N N 131.4 . 1 608 . 104 THR H H 8.5 . 1 609 . 104 THR HA H 5.03 . 1 610 . 104 THR HB H 4.11 . 1 611 . 104 THR HG2 H 1.19 . 1 612 . 104 THR N N 121.6 . 1 613 . 105 ASP H H 8.9 . 1 614 . 105 ASP HA H 5.41 . 1 615 . 105 ASP HB2 H 2.76 . 1 616 . 105 ASP HB3 H 2.76 . 1 617 . 105 ASP N N 125.7 . 1 618 . 106 THR H H 9.08 . 1 619 . 106 THR HA H 4.91 . 1 620 . 106 THR HB H 4.03 . 1 621 . 106 THR HG2 H 1.38 . 1 622 . 106 THR N N 117.6 . 1 623 . 107 TRP H H 8.43 . 1 624 . 107 TRP HA H 4.53 . 1 625 . 107 TRP HB3 H 3.28 . 1 626 . 107 TRP HB2 H 3.16 . 1 627 . 107 TRP HD1 H 7.19 . 1 628 . 107 TRP HE1 H 10.58 . 1 629 . 107 TRP HE3 H 7.25 . 1 630 . 107 TRP HZ2 H 7.32 . 1 631 . 107 TRP HZ3 H 6.67 . 1 632 . 107 TRP N N 128.1 . 1 633 . 107 TRP NE1 N 132.9 . 1 634 . 108 ARG H H 8.02 . 1 635 . 108 ARG HA H 4.43 . 1 636 . 108 ARG HB2 H 1.96 . 1 637 . 108 ARG HB3 H 1.79 . 1 638 . 108 ARG HD2 H 3.57 . 1 639 . 108 ARG HD3 H 3.57 . 1 640 . 108 ARG N N 135.2 . 1 stop_ save_ save_assigned_chemical_shifts_two _Saveframe_category assigned_chemical_shifts _Details ; This save frame contains the set of peak assignments for residues P512 and T513 arising from the cis conformer of P512. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Starch binding domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 4 PRO HA H 4.44 . 1 2 . 4 PRO HB2 H 1.34 . 1 3 . 4 PRO HB3 H 1.34 . 1 4 . 4 PRO HD3 H 3.51 . 1 5 . 4 PRO HD2 H 3.51 . 1 6 . 5 THR H H 8.4 . 1 7 . 5 THR HA H 4.3 . 1 8 . 5 THR HG2 H 1.27 . 1 9 . 5 THR N N 108.5 . 1 stop_ save_ save_assigned_chemical_shifts_three _Saveframe_category assigned_chemical_shifts _Details ; 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. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Starch binding domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 5 THR HG2 H 1.37 . 1 stop_ save_ save_assigned_chemical_shifts_four _Saveframe_category assigned_chemical_shifts _Details ; This save frame contains the set of peak assignments for residues P512 and T513 arising from the trans conformer of P512. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Starch binding domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 4 PRO HA H 4.47 . 1 2 . 4 PRO HB2 H 1.31 . 1 3 . 4 PRO HB3 H 1.31 . 1 4 . 4 PRO HD3 H 3.61 . 2 5 . 4 PRO HD2 H 3.54 . 2 6 . 5 THR H H 8.36 . 1 7 . 5 THR HA H 4.33 . 1 8 . 5 THR HG2 H 1.27 . 1 9 . 5 THR N N 122.8 . 1 stop_ save_ save_assigned_chemical_shifts_five _Saveframe_category assigned_chemical_shifts _Details ; 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. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Starch binding domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 5 THR HG2 H 1.39 . 1 stop_ save_ save_assigned_chemical_shifts_six _Saveframe_category assigned_chemical_shifts _Details ; This save frame contains the set of peak assignments for residues P570, A571 and G572 arising from the cis conformer of P570. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Starch binding domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 62 PRO HA H 4.55 . 1 2 . 62 PRO HB2 H 2.38 . 1 3 . 62 PRO HB3 H 2.38 . 1 4 . 62 PRO HD3 H 3.78 . 1 5 . 62 PRO HD2 H 3.78 . 1 6 . 63 ALA H H 7.62 . 1 7 . 63 ALA HA H 3.83 . 1 8 . 63 ALA HB H 1.22 . 1 9 . 63 ALA N N 124.8 . 1 10 . 64 GLY H H 7.3 . 1 11 . 64 GLY HA2 H 4.01 . 2 12 . 64 GLY HA3 H 3.6 . 2 13 . 64 GLY N N 110.3 . 1 stop_ save_ save_assigned_chemical_shifts_seven _Saveframe_category assigned_chemical_shifts _Details ; This save frame contains the set of peak assignments for residues P570, A571 and G572 arising from the trans conformer of P570. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Starch binding domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 62 PRO HA H 4.56 . 1 2 . 62 PRO HB2 H 2.4 . 2 3 . 62 PRO HB3 H 1.89 . 2 4 . 62 PRO HG2 H 2.12 . 2 5 . 62 PRO HG3 H 1.94 . 2 6 . 62 PRO HD3 H 3.76 . 2 7 . 62 PRO HD2 H 3.31 . 2 8 . 63 ALA H H 7.58 . 1 9 . 63 ALA HA H 3.82 . 1 10 . 63 ALA HB H 1.2 . 1 11 . 63 ALA N N 124.8 . 1 12 . 64 GLY H H 7.25 . 1 13 . 64 GLY HA2 H 3.99 . 2 14 . 64 GLY HA3 H 3.57 . 2 15 . 64 GLY N N 110.3 . 1 stop_ save_ save_assigned_chemical_shifts_eight _Saveframe_category assigned_chemical_shifts _Details ; 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' ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Starch binding domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 6 ALA H H 7.81 . 1 2 . 6 ALA HA H 4.95 . 1 3 . 6 ALA HB H 1.17 . 1 4 . 6 ALA N N 126.3 . 1 stop_ save_ save_assigned_chemical_shifts_nine _Saveframe_category assigned_chemical_shifts _Details ; 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. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Starch binding domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 6 ALA H H 7.76 . 1 2 . 6 ALA HA H 5.00 . 1 3 . 6 ALA HB H 1.23 . 1 stop_ save_