data_34508 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR Structure of APP G38P mutant TM ; _BMRB_accession_number 34508 _BMRB_flat_file_name bmr34508.str _Entry_type original _Submission_date 2020-03-30 _Accession_date 2020-03-30 _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 Silber M. . . 2 Muhle-Goll C. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 159 "13C chemical shifts" 103 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-12-04 original BMRB . stop_ _Original_release_date 2020-07-14 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Altered hinge conformations in APP transmembrane helix mutants may affect complex formation with gamma-secretase ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Silber M. . . 2 Muhle-Goll C. . . 3 Hitzenberger M. . . 4 Zacharias M. . . stop_ _Journal_abbreviation 'To be published' _Journal_volume . _Journal_issue . _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Amyloid-beta precursor protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label unit_1 $entity_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 3110.988 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 30 _Mol_residue_sequence ; SNKGAIIGLMVGPVVIATVI VITLVMLKKK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 26 SER 2 27 ASN 3 28 LYS 4 29 GLY 5 30 ALA 6 31 ILE 7 32 ILE 8 33 GLY 9 34 LEU 10 35 MET 11 36 VAL 12 37 GLY 13 38 PRO 14 39 VAL 15 40 VAL 16 41 ILE 17 42 ALA 18 43 THR 19 44 VAL 20 45 ILE 21 46 VAL 22 47 ILE 23 48 THR 24 49 LEU 25 50 VAL 26 51 MET 27 52 LEU 28 53 LYS 29 54 LYS 30 55 LYS 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 $entity_1 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 $entity_1 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '500 uM APP G38P, 80% TFE-d2, 20% H2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 500 uM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CNS _Version 1.2.1 loop_ _Vendor _Address _Electronic_address 'Brunger A. T. et.al.' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_software_2 _Saveframe_category software _Name ARIA _Version 2.3.2 loop_ _Vendor _Address _Electronic_address "Linge, O'Donoghue and Nilges" . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name 'CcpNmr Analysis' _Version 2.4.2 loop_ _Vendor _Address _Electronic_address 'Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, Llinas M, Ulrich EL, Markley JL, Ionides J, Laue ED.' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'CP TCI' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H-NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-1H-NOESY _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 'ionic strength' 0 . mM pH 7.0 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 0.000 internal indirect . . . 0.25144953 DSS H 1 'methyl protons' ppm 0.000 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.000 internal indirect . . . 0.10132912 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 1H-1H-NOESY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name unit_1 _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 26 1 SER HA H 4.393 . . 2 26 1 SER HB2 H 3.962 . . 3 26 1 SER HB3 H 3.831 . . 4 26 1 SER HG H 7.766 . . 5 26 1 SER CA C 58.021 . . 6 26 1 SER CB C 63.143 . . 7 27 2 ASN HA H 4.792 . . 8 27 2 ASN HB2 H 2.909 . . 9 27 2 ASN HB3 H 2.909 . . 10 27 2 ASN CA C 52.409 . . 11 27 2 ASN CB C 37.119 . . 12 28 3 LYS H H 8.020 . . 13 28 3 LYS HA H 4.120 . . 14 28 3 LYS HB2 H 1.894 . . 15 28 3 LYS HB3 H 1.852 . . 16 28 3 LYS HD2 H 1.714 . . 17 28 3 LYS HD3 H 1.714 . . 18 28 3 LYS CA C 58.000 . . 19 28 3 LYS CB C 31.565 . . 20 28 3 LYS CD C 28.316 . . 21 29 4 GLY H H 8.209 . . 22 29 4 GLY HA2 H 3.853 . . 23 29 4 GLY HA3 H 3.855 . . 24 29 4 GLY CA C 45.739 . . 25 30 5 ALA H H 7.634 . . 26 30 5 ALA HA H 4.230 . . 27 30 5 ALA HB H 1.486 . . 28 30 5 ALA CA C 53.531 . . 29 30 5 ALA CB C 17.309 . . 30 31 6 ILE H H 7.484 . . 31 31 6 ILE HA H 3.945 . . 32 31 6 ILE HB H 2.019 . . 33 31 6 ILE HG12 H 1.627 . . 34 31 6 ILE HG13 H 1.296 . . 35 31 6 ILE HG2 H 0.980 . . 36 31 6 ILE HD1 H 0.896 . . 37 31 6 ILE CA C 62.951 . . 38 31 6 ILE CB C 37.407 . . 39 31 6 ILE CG1 C 27.515 . . 40 31 6 ILE CG2 C 16.218 . . 41 31 6 ILE CD1 C 11.280 . . 42 32 7 ILE H H 7.804 . . 43 32 7 ILE HA H 3.859 . . 44 32 7 ILE HB H 1.930 . . 45 32 7 ILE HG12 H 1.267 . . 46 32 7 ILE HG13 H 1.674 . . 47 32 7 ILE HG2 H 0.948 . . 48 32 7 ILE HD1 H 0.883 . . 49 32 7 ILE CA C 63.793 . . 50 32 7 ILE CB C 37.103 . . 51 32 7 ILE CG1 C 27.856 . . 52 32 7 ILE CG2 C 15.969 . . 53 32 7 ILE CD1 C 11.100 . . 54 33 8 GLY H H 7.935 . . 55 33 8 GLY HA2 H 3.843 . . 56 33 8 GLY HA3 H 3.841 . . 57 33 8 GLY CA C 46.211 . . 58 34 9 LEU H H 7.765 . . 59 34 9 LEU HA H 4.290 . . 60 34 9 LEU HB2 H 1.971 . . 61 34 9 LEU HB3 H 1.640 . . 62 34 9 LEU HG H 1.836 . . 63 34 9 LEU HD1 H 0.944 . . 64 34 9 LEU HD2 H 0.915 . . 65 34 9 LEU CA C 56.378 . . 66 34 9 LEU CB C 41.609 . . 67 34 9 LEU CG C 26.125 . . 68 34 9 LEU CD1 C 23.541 . . 69 34 9 LEU CD2 C 21.751 . . 70 35 10 MET H H 7.955 . . 71 35 10 MET HA H 4.436 . . 72 35 10 MET HB2 H 2.296 . . 73 35 10 MET HB3 H 2.158 . . 74 35 10 MET HG2 H 2.737 . . 75 35 10 MET HG3 H 2.588 . . 76 35 10 MET CA C 56.725 . . 77 35 10 MET CB C 32.454 . . 78 35 10 MET CG C 31.514 . . 79 36 11 VAL H H 8.112 . . 80 36 11 VAL HA H 4.252 . . 81 36 11 VAL HB H 2.266 . . 82 36 11 VAL HG1 H 1.033 . . 83 36 11 VAL HG2 H 1.134 . . 84 36 11 VAL CA C 62.614 . . 85 36 11 VAL CB C 32.041 . . 86 36 11 VAL CG1 C 19.502 . . 87 36 11 VAL CG2 C 21.818 . . 88 37 12 GLY H H 7.921 . . 89 37 12 GLY HA2 H 4.188 . . 90 37 12 GLY HA3 H 3.936 . . 91 37 12 GLY CA C 47.222 . . 92 38 13 PRO HA H 4.265 . . 93 38 13 PRO HB2 H 2.404 . . 94 38 13 PRO HG2 H 2.178 . . 95 38 13 PRO HG3 H 1.956 . . 96 38 13 PRO HD2 H 3.682 . . 97 38 13 PRO HD3 H 3.607 . . 98 38 13 PRO CA C 65.049 . . 99 38 13 PRO CB C 31.226 . . 100 38 13 PRO CG C 27.160 . . 101 38 13 PRO CD C 50.118 . . 102 39 14 VAL H H 7.423 . . 103 39 14 VAL HA H 3.803 . . 104 39 14 VAL HB H 2.310 . . 105 39 14 VAL HG1 H 1.060 . . 106 39 14 VAL HG2 H 0.992 . . 107 39 14 VAL CA C 64.953 . . 108 39 14 VAL CB C 31.192 . . 109 39 14 VAL CG1 C 21.114 . . 110 39 14 VAL CG2 C 19.842 . . 111 40 15 VAL H H 8.016 . . 112 40 15 VAL HA H 3.611 . . 113 40 15 VAL HB H 2.298 . . 114 40 15 VAL HG1 H 0.949 . . 115 40 15 VAL HG2 H 1.051 . . 116 40 15 VAL CA C 66.573 . . 117 40 15 VAL CB C 30.904 . . 118 40 15 VAL CG1 C 20.001 . . 119 40 15 VAL CG2 C 21.114 . . 120 41 16 ILE H H 8.129 . . 121 41 16 ILE HA H 3.697 . . 122 41 16 ILE HB H 1.868 . . 123 41 16 ILE HG12 H 1.235 . . 124 41 16 ILE HG13 H 1.671 . . 125 41 16 ILE HG2 H 0.943 . . 126 41 16 ILE HD1 H 0.829 . . 127 41 16 ILE CA C 64.154 . . 128 41 16 ILE CB C 36.930 . . 129 41 16 ILE CG1 C 27.900 . . 130 41 16 ILE CG2 C 15.969 . . 131 41 16 ILE CD1 C 10.631 . . 132 42 17 ALA H H 7.874 . . 133 42 17 ALA HA H 4.045 . . 134 42 17 ALA HB H 1.541 . . 135 42 17 ALA CA C 54.958 . . 136 42 17 ALA CB C 16.968 . . 137 43 18 THR H H 7.860 . . 138 43 18 THR HA H 3.890 . . 139 43 18 THR HB H 4.550 . . 140 43 18 THR HG2 H 1.281 . . 141 43 18 THR CA C 66.779 . . 142 43 18 THR CB C 68.350 . . 143 43 18 THR CG2 C 19.531 . . 144 44 19 VAL H H 8.252 . . 145 44 19 VAL HA H 3.634 . . 146 44 19 VAL HB H 2.338 . . 147 44 19 VAL HG1 H 1.106 . . 148 44 19 VAL HG2 H 0.944 . . 149 44 19 VAL CA C 67.376 . . 150 44 19 VAL CB C 30.880 . . 151 44 19 VAL CG1 C 21.648 . . 152 44 19 VAL CG2 C 20.001 . . 153 45 20 ILE H H 8.450 . . 154 45 20 ILE HA H 3.633 . . 155 45 20 ILE HB H 2.108 . . 156 45 20 ILE HG12 H 1.095 . . 157 45 20 ILE HG13 H 1.878 . . 158 45 20 ILE HG2 H 0.923 . . 159 45 20 ILE HD1 H 0.844 . . 160 45 20 ILE CA C 65.710 . . 161 45 20 ILE CB C 36.876 . . 162 45 20 ILE CG1 C 28.201 . . 163 45 20 ILE CG2 C 15.470 . . 164 45 20 ILE CD1 C 11.616 . . 165 46 21 VAL H H 8.247 . . 166 46 21 VAL HA H 3.635 . . 167 46 21 VAL HB H 2.273 . . 168 46 21 VAL HG1 H 1.135 . . 169 46 21 VAL HG2 H 0.985 . . 170 46 21 VAL CA C 66.443 . . 171 46 21 VAL CB C 30.894 . . 172 46 21 VAL CG1 C 21.818 . . 173 46 21 VAL CG2 C 19.842 . . 174 47 22 ILE H H 8.559 . . 175 47 22 ILE HA H 3.698 . . 176 47 22 ILE HB H 1.976 . . 177 47 22 ILE HG12 H 1.242 . . 178 47 22 ILE HG13 H 1.850 . . 179 47 22 ILE HG2 H 0.957 . . 180 47 22 ILE HD1 H 0.829 . . 181 47 22 ILE CA C 64.791 . . 182 47 22 ILE CB C 36.988 . . 183 47 22 ILE CG1 C 28.218 . . 184 47 22 ILE CG2 C 16.094 . . 185 47 22 ILE CD1 C 10.631 . . 186 48 23 THR H H 8.159 . . 187 48 23 THR HA H 3.845 . . 188 48 23 THR HB H 4.545 . . 189 48 23 THR HG1 H 5.683 . . 190 48 23 THR HG2 H 1.244 . . 191 48 23 THR CA C 67.296 . . 192 48 23 THR CB C 68.040 . . 193 48 23 THR CG2 C 19.366 . . 194 49 24 LEU H H 8.497 . . 195 49 24 LEU HA H 4.107 . . 196 49 24 LEU HB2 H 1.522 . . 197 49 24 LEU HB3 H 2.122 . . 198 49 24 LEU HG H 1.981 . . 199 49 24 LEU HD1 H 0.897 . . 200 49 24 LEU HD2 H 0.875 . . 201 49 24 LEU CA C 58.002 . . 202 49 24 LEU CB C 41.045 . . 203 49 24 LEU CG C 25.931 . . 204 49 24 LEU CD1 C 23.906 . . 205 49 24 LEU CD2 C 21.521 . . 206 50 25 VAL H H 8.627 . . 207 50 25 VAL HA H 3.610 . . 208 50 25 VAL HB H 2.334 . . 209 50 25 VAL HG1 H 1.085 . . 210 50 25 VAL HG2 H 0.952 . . 211 50 25 VAL CA C 66.573 . . 212 50 25 VAL CB C 30.880 . . 213 50 25 VAL CG1 C 21.337 . . 214 50 25 VAL CG2 C 19.498 . . 215 51 26 MET H H 8.557 . . 216 51 26 MET HA H 4.201 . . 217 51 26 MET HB2 H 2.107 . . 218 51 26 MET HB3 H 2.432 . . 219 51 26 MET HG2 H 2.804 . . 220 51 26 MET HG3 H 2.672 . . 221 51 26 MET CA C 58.059 . . 222 51 26 MET CB C 31.040 . . 223 51 26 MET CG C 31.949 . . 224 52 27 LEU H H 8.540 . . 225 52 27 LEU HA H 4.140 . . 226 52 27 LEU HB2 H 2.019 . . 227 52 27 LEU HB3 H 1.570 . . 228 52 27 LEU HG H 1.939 . . 229 52 27 LEU HD1 H 0.905 . . 230 52 27 LEU HD2 H 0.888 . . 231 52 27 LEU CA C 57.195 . . 232 52 27 LEU CB C 41.372 . . 233 52 27 LEU CG C 25.997 . . 234 52 27 LEU CD1 C 23.906 . . 235 52 27 LEU CD2 C 21.602 . . 236 53 28 LYS H H 8.205 . . 237 53 28 LYS HA H 4.123 . . 238 53 28 LYS HB2 H 2.072 . . 239 53 28 LYS HB3 H 1.989 . . 240 53 28 LYS HD2 H 1.714 . . 241 53 28 LYS HD3 H 1.714 . . 242 53 28 LYS CA C 57.707 . . 243 53 28 LYS CB C 31.342 . . 244 53 28 LYS CD C 28.316 . . 245 54 29 LYS H H 8.246 . . 246 54 29 LYS HA H 4.177 . . 247 54 29 LYS HB2 H 1.953 . . 248 54 29 LYS HB3 H 1.999 . . 249 54 29 LYS HD2 H 1.710 . . 250 54 29 LYS HD3 H 1.710 . . 251 54 29 LYS CA C 57.245 . . 252 54 29 LYS CB C 31.736 . . 253 54 29 LYS CD C 28.316 . . 254 55 30 LYS H H 8.000 . . 255 55 30 LYS HA H 4.222 . . 256 55 30 LYS HB2 H 1.947 . . 257 55 30 LYS HB3 H 1.947 . . 258 55 30 LYS HD2 H 1.715 . . 259 55 30 LYS HD3 H 1.715 . . 260 55 30 LYS CA C 56.207 . . 261 55 30 LYS CB C 32.030 . . 262 55 30 LYS CD C 28.316 . . stop_ save_