data_26706 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 13C, and 15 N Chemical Shift Assignments for fibrillar Islet Amyloid Polypeptide (IAPP) ; _BMRB_accession_number 26706 _BMRB_flat_file_name bmr26706.str _Entry_type original _Submission_date 2015-11-12 _Accession_date 2015-11-12 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Weirich Franziska . . 2 Heise Henrike . . 3 Mirecka Ewa A. . 4 Gremer Lothar . . 5 Hoyer Wolfgang . . 6 Schiefer Stephanie . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 109 "15N chemical shifts" 37 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-09-26 update author 'update entry citation' 2016-08-23 update author 'update natural source' 2016-08-08 original author 'original release' stop_ _Original_release_date 2016-08-08 save_ ############################# # Citation for this entry # ############################# save_Citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the beta-Sheet Core ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27607147 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Weirich Franziska . . 2 Mirecka Ewa A. . 3 Schiefer Stephanie . . 4 Gremer Lothar . . 5 Hoyer Wolfgang . . 6 Heise Henrike . . stop_ _Journal_abbreviation 'PLOS One' _Journal_volume 11 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e0161243 _Page_last e0161243 _Year 2016 _Details . loop_ _Keyword 'fibrillar aggregates' 'solid-state NMR' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Fibrils _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'recombinant fibrillar hIAPP' $IAPP stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IAPP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IAPP _Molecular_mass 3906.3 _Mol_thiol_state 'all disulfide bound' _Details 'When fully 13C-15N labeled, the molecular mass accounts for 4112 Da.' ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; KCNTATCATQRLANFLVHSS NNFGAILSSTNVGSNTY ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 CYS 3 ASN 4 THR 5 ALA 6 THR 7 CYS 8 ALA 9 THR 10 GLN 11 ARG 12 LEU 13 ALA 14 ASN 15 PHE 16 LEU 17 VAL 18 HIS 19 SER 20 SER 21 ASN 22 ASN 23 PHE 24 GLY 25 ALA 26 ILE 27 LEU 28 SER 29 SER 30 THR 31 ASN 32 VAL 33 GLY 34 SER 35 ASN 36 THR 37 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $IAPP Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $IAPP 'recombinant technology' . Escherichia coli . pET302/NT-His stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type 'gel solid' _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $IAPP 110 mM '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_CcpNMR _Saveframe_category software _Name CcpNMR _Version 2.4.2 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Oxford _Model AS600 _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model '600/54 Premium Shielded' _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Oxford _Model '2.2K 800/63' _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_13C-13C_PDSD_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C-13C PDSD' _Sample_label $sample_1 save_ save_3D_NCOCX_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_1 save_ save_3D_NCaCB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCaCB' _Sample_label $sample_1 save_ save_3D_NCaCX_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCaCX' _Sample_label $sample_1 save_ save_1D_INEPT_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1D INEPT' _Sample_label $sample_1 save_ save_2D_DQSQ_SPC5_3_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQSQ SPC5_3' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 C 13 'methyl carbons' ppm 0 external indirect cylindrical 'separate tube (no insert) similar to the experimental sample tube' 'magic angle' 0.251449530 'NH3 (liquid)' N 15 nitrogen ppm 0 external indirect cylindrical 'separate tube (no insert) similar to the experimental sample tube' 'magic angle' 0.101329120 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 13C-13C PDSD' '3D NCOCX' '3D NCaCB' '3D NCaCX' '2D DQSQ SPC5_3' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'recombinant fibrillar hIAPP' _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 1 1 LYS C C 174.1515 . . 2 1 1 LYS CA C 54.6071 . . 3 1 1 LYS CB C 32.8148 . . 4 1 1 LYS N N 122.9715 . . 5 2 2 CYS C C 173.6279 . . 6 2 2 CYS CA C 59.1949 . . 7 2 2 CYS CB C 43.4829 . . 8 2 2 CYS N N 122.9145 . . 9 3 3 ASN C C 176.6414 . . 10 3 3 ASN CA C 51.2535 . . 11 3 3 ASN CB C 39.1333 . . 12 3 3 ASN N N 114.3015 . . 13 4 4 THR C C 175.8153 . . 14 4 4 THR CA C 62.0665 . . 15 4 4 THR CB C 66.0762 . . 16 4 4 THR N N 119.6837 . . 17 5 5 ALA C C 176.4711 . . 18 5 5 ALA CA C 50.9939 . . 19 5 5 ALA CB C 26.7852 . . 20 5 5 ALA N N 119.2725 . . 21 6 6 THR C C 174.0212 . . 22 6 6 THR CA C 61.7211 . . 23 6 6 THR CB C 70.2491 . . 24 6 6 THR N N 116.9076 . . 25 7 7 CYS C C 173.0523 . . 26 7 7 CYS CA C 53.1885 . . 27 7 7 CYS CB C 48.6479 . . 28 7 7 CYS N N 120.1359 . . 29 8 8 ALA C C 175.4973 . . 30 8 8 ALA CA C 50.6682 . . 31 8 8 ALA CB C 22.6600 . . 32 8 8 ALA N N 120.5870 . . 33 9 9 THR C C 172.6306 . . 34 9 9 THR CA C 62.0984 . . 35 9 9 THR CB C 70.3230 . . 36 9 9 THR N N 118.9805 . . 37 10 10 GLN C C 173.8905 . . 38 10 10 GLN CA C 54.3613 . . 39 10 10 GLN CB C 32.2601 . . 40 10 10 GLN N N 126.3833 . . 41 11 11 ARG C C 174.8049 . . 42 11 11 ARG CA C 54.1642 . . 43 11 11 ARG CB C 29.8001 . . 44 11 11 ARG N N 125.6574 . . 45 12 12 LEU C C 172.6737 . . 46 12 12 LEU CA C 54.4025 . . 47 12 12 LEU CB C 44.3117 . . 48 12 12 LEU N N 125.1208 . . 49 13 13 ALA C C 174.3871 . . 50 13 13 ALA CA C 51.3094 . . 51 13 13 ALA CB C 21.1349 . . 52 13 13 ALA N N 129.4373 . . 53 14 14 ASN C C 173.1809 . . 54 14 14 ASN CA C 52.5247 . . 55 14 14 ASN CB C 42.7848 . . 56 14 14 ASN N N 120.5578 . . 57 15 15 PHE C C 173.0723 . . 58 15 15 PHE CA C 56.5831 . . 59 15 15 PHE CB C 42.6863 . . 60 15 15 PHE N N 117.0007 . . 61 16 16 LEU C C 173.6250 . . 62 16 16 LEU CA C 56.9960 . . 63 16 16 LEU CB C 42.0574 . . 64 16 16 LEU N N 123.4458 . . 65 17 17 VAL C C 173.7281 . . 66 17 17 VAL CA C 60.7204 . . 67 17 17 VAL CB C 35.8009 . . 68 17 17 VAL N N 120.8243 . . 69 18 18 HIS C C 175.0351 . . 70 18 18 HIS CA C 54.2973 . . 71 18 18 HIS CB C 28.2108 . . 72 18 18 HIS N N 126.3277 . . 73 19 19 SER C C 174.0273 . . 74 19 19 SER CA C 55.9386 . . 75 19 19 SER CB C 64.6094 . . 76 19 19 SER N N 124.0111 . . 77 20 20 SER C C 174.6906 . . 78 20 20 SER CA C 55.8807 . . 79 20 20 SER CB C 64.5351 . . 80 20 20 SER N N 124.1678 . . 81 21 21 ASN C C 173.0120 . . 82 21 21 ASN CA C 54.1706 . . 83 21 21 ASN CB C 36.4411 . . 84 21 21 ASN N N 127.3458 . . 85 22 22 ASN C C 172.1744 . . 86 22 22 ASN CA C 52.5142 . . 87 22 22 ASN CB C 42.2986 . . 88 22 22 ASN N N 118.1055 . . 89 23 23 PHE C C 173.7361 . . 90 23 23 PHE CA C 57.0700 . . 91 23 23 PHE CB C 40.2057 . . 92 23 23 PHE N N 121.0738 . . 93 24 24 GLY C C 171.3322 . . 94 24 24 GLY CA C 43.9225 . . 95 24 24 GLY N N 109.8603 . . 96 25 25 ALA C C 176.8307 . . 97 25 25 ALA CA C 50.4099 . . 98 25 25 ALA CB C 21.7524 . . 99 25 25 ALA N N 127.9237 . . 100 26 26 ILE C C 177.0023 . . 101 26 26 ILE CA C 60.1306 . . 102 26 26 ILE CB C 40.4685 . . 103 26 26 ILE N N 120.3054 . . 104 27 27 LEU C C 173.5586 . . 105 27 27 LEU CA C 54.2344 . . 106 27 27 LEU CB C 44.4531 . . 107 27 27 LEU N N 121.4530 . . 108 28 28 SER C C 174.3802 . . 109 28 28 SER CA C 55.8054 . . 110 28 28 SER CB C 64.5263 . . 111 28 28 SER N N 116.2847 . . 112 29 29 SER C C 173.7457 . . 113 29 29 SER CA C 58.8195 . . 114 29 29 SER CB C 61.5784 . . 115 29 29 SER N N 125.2663 . . 116 30 30 THR C C 171.3728 . . 117 30 30 THR CA C 61.2595 . . 118 30 30 THR CB C 73.9506 . . 119 30 30 THR N N 114.3554 . . 120 31 31 ASN C C 173.8965 . . 121 31 31 ASN CA C 52.2670 . . 122 31 31 ASN CB C 41.3245 . . 123 31 31 ASN N N 122.2762 . . 124 32 32 VAL C C 174.7753 . . 125 32 32 VAL CA C 60.5004 . . 126 32 32 VAL CB C 34.5520 . . 127 32 32 VAL N N 121.6353 . . 128 33 33 GLY C C 173.9682 . . 129 33 33 GLY CA C 47.9720 . . 130 33 33 GLY N N 116.5293 . . 131 34 34 SER C C 171.7769 . . 132 34 34 SER CA C 58.3869 . . 133 34 34 SER CB C 68.3705 . . 134 34 34 SER N N 113.0155 . . 135 35 35 ASN C C 174.3036 . . 136 35 35 ASN CA C 52.4404 . . 137 35 35 ASN CB C 41.9895 . . 138 35 35 ASN N N 119.9910 . . 139 36 36 THR C C 173.2469 . . 140 36 36 THR CA C 60.7360 . . 141 36 36 THR CB C 71.3284 . . 142 36 36 THR N N 114.4399 . . 143 37 37 TYR C C 180.7377 . . 144 37 37 TYR CA C 60.0099 . . 145 37 37 TYR CB C 39.4446 . . 146 37 37 TYR N N 128.5357 . . stop_ save_