data_26926 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 13C and 15N Chemical Shift Assignments for Syrian Hamster Y145Stop Prion Protein Amyloid Fibrils ; _BMRB_accession_number 26926 _BMRB_flat_file_name bmr26926.str _Entry_type original _Submission_date 2016-10-26 _Accession_date 2016-10-26 _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 Theint Theint . . 2 Nadaud Philippe S. . 3 Surewicz Krystyna . . 4 Surewicz Witold K. . 5 Jaroniec Christopher P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 77 "15N chemical shifts" 27 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-03-14 update BMRB 'update entry citation' 2017-02-15 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 26924 'mouse PrP23-144 amyloid fibril' 26925 'huPrP23-144 amyloid fibrils' stop_ _Original_release_date 2016-10-27 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; 13C and 15N Chemical Shift Assignments of Mammalian Y145Stop Prion Protein Amyloid Fibrils ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28004358 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Theint Theint . . 2 Nadaud Philippe S. . 3 Surewicz Krystyna . . 4 Surewicz Witold K. . 5 Jaroniec Christopher P. . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 11 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 75 _Page_last 80 _Year 2017 _Details . loop_ _Keyword amyloid 'magic-angle spinning' 'prion protein' 'solid-state NMR' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'ShaPrP23-144 amyloid fibrils' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ShaPrP23-144 $ShaPrP23-144 stop_ _System_molecular_weight . _System_physical_state 'amyloid fibrils' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ShaPrP23-144 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ShaPrP23-144 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 126 _Mol_residue_sequence ; GSDPKKRPKPGGWNTGGSRY PGQGSPGGNRYPPQGGGTWG QPHGGGWGQPHGGGWGQPHG GGWGQPHGGGWGQGGGTHNQ WNKPSKPKTNMKHMAGAAAA GAVVGGLGGYMLGSAMSRPM MHFGND ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 19 GLY 2 20 SER 3 21 ASP 4 22 PRO 5 23 LYS 6 24 LYS 7 25 ARG 8 26 PRO 9 27 LYS 10 28 PRO 11 29 GLY 12 30 GLY 13 31 TRP 14 32 ASN 15 33 THR 16 34 GLY 17 35 GLY 18 36 SER 19 37 ARG 20 38 TYR 21 39 PRO 22 40 GLY 23 41 GLN 24 42 GLY 25 43 SER 26 44 PRO 27 45 GLY 28 46 GLY 29 47 ASN 30 48 ARG 31 49 TYR 32 50 PRO 33 51 PRO 34 52 GLN 35 53 GLY 36 54 GLY 37 55 GLY 38 56 THR 39 57 TRP 40 58 GLY 41 59 GLN 42 60 PRO 43 61 HIS 44 62 GLY 45 63 GLY 46 64 GLY 47 65 TRP 48 66 GLY 49 67 GLN 50 68 PRO 51 69 HIS 52 70 GLY 53 71 GLY 54 72 GLY 55 73 TRP 56 74 GLY 57 75 GLN 58 76 PRO 59 77 HIS 60 78 GLY 61 79 GLY 62 80 GLY 63 81 TRP 64 82 GLY 65 83 GLN 66 84 PRO 67 85 HIS 68 86 GLY 69 87 GLY 70 88 GLY 71 89 TRP 72 90 GLY 73 91 GLN 74 92 GLY 75 93 GLY 76 94 GLY 77 95 THR 78 96 HIS 79 97 ASN 80 98 GLN 81 99 TRP 82 100 ASN 83 101 LYS 84 102 PRO 85 103 SER 86 104 LYS 87 105 PRO 88 106 LYS 89 107 THR 90 108 ASN 91 109 MET 92 110 LYS 93 111 HIS 94 112 MET 95 113 ALA 96 114 GLY 97 115 ALA 98 116 ALA 99 117 ALA 100 118 ALA 101 119 GLY 102 120 ALA 103 121 VAL 104 122 VAL 105 123 GLY 106 124 GLY 107 125 LEU 108 126 GLY 109 127 GLY 110 128 TYR 111 129 MET 112 130 LEU 113 131 GLY 114 132 SER 115 133 ALA 116 134 MET 117 135 SER 118 136 ARG 119 137 PRO 120 138 MET 121 139 MET 122 140 HIS 123 141 PHE 124 142 GLY 125 143 ASN 126 144 ASP 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 $ShaPrP23-144 'golden hamster' 10036 Eukaryota Metazoa Mesocricetus auratus 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 $ShaPrP23-144 'recombinant technology' . Escherichia coli . pRSETB stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type 'fibrous protein' _Details ; Amyloid fibril formation was performed at 25C under quiescent conditions. (i.e. in absence of continuous agitation). ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ShaPrP23-144 20 mg '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_VnmrJ _Saveframe_category software _Name VnmrJ _Version 2.2C loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 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_ save_TALOS-N _Saveframe_category software _Name TALOS-N _Version . loop_ _Vendor _Address _Electronic_address 'Shen and Bax' . . stop_ loop_ _Task 'secondary structure analysis' stop_ _Details . save_ save_nmrglue _Saveframe_category software _Name nmrglue _Version . loop_ _Vendor _Address _Electronic_address 'Helmus, Jaroniec' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VNMRS _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NCA' _Sample_label $sample_1 save_ save_2D_NCACX_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NCACX' _Sample_label $sample_1 save_ save_3D_NCACX_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $sample_1 save_ save_3D_NCOCX_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $sample_1 save_ save_3D_CONCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CONCA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'The temperature controller setting is 273 K.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 . pH pressure 1 . atm temperature 277 . 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 protons' ppm 0 na indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0 na indirect . . . 0.101329118 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 NCA' '2D NCACX' '3D NCACX' '3D NCOCX' '3D CONCA' 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 ShaPrP23-144 _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 1 112 94 MET C C 174.67 0 1 2 113 95 ALA C C 175.474 0.181 1 3 113 95 ALA CA C 50.587 0.103 1 4 113 95 ALA CB C 22.645 0.034 1 5 113 95 ALA N N 128.802 0.344 1 6 114 96 GLY C C 170.451 0.037 1 7 114 96 GLY CA C 45.111 0.14 1 8 114 96 GLY N N 106.554 0.34 1 9 115 97 ALA C C 175.733 0.027 1 10 115 97 ALA CA C 50.259 0.155 1 11 115 97 ALA CB C 24.954 0.122 1 12 115 97 ALA N N 122.828 0.199 1 13 116 98 ALA C C 175.269 0.002 1 14 116 98 ALA CA C 50.336 0.077 1 15 116 98 ALA CB C 26.718 0.037 1 16 116 98 ALA N N 120.684 0.182 1 17 117 99 ALA C C 176.169 0 1 18 117 99 ALA CA C 50.004 0.028 1 19 117 99 ALA CB C 20.447 0 1 20 117 99 ALA N N 124.632 0.077 1 21 118 100 ALA C C 175.766 0.137 1 22 118 100 ALA CA C 50.501 0.15 1 23 118 100 ALA CB C 21.069 0 1 24 118 100 ALA N N 125.022 0.153 1 25 119 101 GLY C C 172.846 0.135 1 26 119 101 GLY CA C 45.599 0.113 1 27 119 101 GLY N N 105.243 0.246 1 28 120 102 ALA C C 177.476 0.114 1 29 120 102 ALA CA C 50.581 0.093 1 30 120 102 ALA CB C 21.072 0.035 1 31 120 102 ALA N N 127.615 0.194 1 32 121 103 VAL C C 174.937 0.054 1 33 121 103 VAL CA C 61.031 0.112 1 34 121 103 VAL CB C 34.295 0.137 1 35 121 103 VAL CG1 C 23.117 0.14 2 36 121 103 VAL CG2 C 21.868 0.031 2 37 121 103 VAL N N 114.914 0.189 1 38 122 104 VAL C C 175.791 0.139 1 39 122 104 VAL CA C 58.54 0.123 1 40 122 104 VAL CB C 36.113 0 1 41 122 104 VAL CG1 C 22.309 0.003 2 42 122 104 VAL CG2 C 20.01 0 2 43 122 104 VAL N N 125.369 0.208 1 44 123 105 GLY C C 173.208 0.164 1 45 123 105 GLY CA C 47.146 0.102 1 46 123 105 GLY N N 109.246 0.142 1 47 124 106 GLY C C 175.55 0.262 1 48 124 106 GLY CA C 49.97 0.178 1 49 124 106 GLY N N 111.426 0.156 1 50 125 107 LEU C C 176.804 0.154 1 51 125 107 LEU CA C 53.88 0.232 1 52 125 107 LEU CB C 38.787 0 1 53 125 107 LEU CD1 C 27.577 0 2 54 125 107 LEU CD2 C 25.714 0 2 55 125 107 LEU N N 118.277 0.271 1 56 126 108 GLY C C 175.287 0 1 57 126 108 GLY CA C 46.73 0.176 1 58 126 108 GLY N N 110.538 0.41 1 59 127 109 GLY C C 171.901 0.206 1 60 127 109 GLY CA C 46.364 0.167 1 61 127 109 GLY N N 102.739 0.225 1 62 128 110 TYR C C 174.154 0.032 1 63 128 110 TYR CA C 56.823 0.07 1 64 128 110 TYR N N 118.633 0.18 1 65 129 111 MET C C 173.361 0 1 66 129 111 MET CA C 54.397 0.128 1 67 129 111 MET N N 124.379 0.203 1 68 130 112 LEU C C 174.55 0.082 1 69 130 112 LEU CA C 55.257 0.038 1 70 130 112 LEU N N 127.24 0.256 1 71 131 113 GLY C C 172.108 0.04 1 72 131 113 GLY CA C 44.118 0.074 1 73 131 113 GLY N N 108.949 0.387 1 74 132 114 SER C C 172.447 0.123 1 75 132 114 SER CA C 56.253 0.115 1 76 132 114 SER CB C 66.456 0 1 77 132 114 SER N N 114.296 0.202 1 78 133 115 ALA C C 175.624 0 1 79 133 115 ALA CA C 50.564 0.051 1 80 133 115 ALA CB C 22.993 0.126 1 81 133 115 ALA N N 124.488 0.123 1 82 134 116 MET C C 175.059 0 1 83 134 116 MET CA C 54.524 0 1 84 134 116 MET N N 123.427 0 1 85 135 117 SER C C 173.87 0.079 1 86 135 117 SER CA C 56.104 0.12 1 87 135 117 SER CB C 63.358 0.177 1 88 135 117 SER N N 122.537 0.127 1 89 136 118 ARG C C 170.978 0 1 90 136 118 ARG CA C 53.336 0.028 1 91 136 118 ARG N N 127.369 0.133 1 92 137 119 PRO C C 175.401 0 1 93 137 119 PRO CA C 62.937 0.079 1 94 137 119 PRO CD C 49.37 0 1 95 137 119 PRO N N 135.72 0.239 1 96 138 120 MET C C 173.687 0 1 97 138 120 MET CA C 54.753 0 1 98 138 120 MET N N 123.662 0 1 99 139 121 MET CA C 55.549 0.192 1 100 139 121 MET N N 128.66 0.242 1 101 128 110 TYR CB C 42.2 0 1 102 136 118 ARG CB C 32.4 0 1 103 137 119 PRO CB C 32.1 0 1 104 139 121 MET C C 173.2 0 1 stop_ save_