data_27074 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Chemical Shift Assignments for wild-type alpha-synuclein ; _BMRB_accession_number 27074 _BMRB_flat_file_name bmr27074.str _Entry_type original _Submission_date 2017-04-17 _Accession_date 2017-04-17 _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 'El Turk' Farah . . 2 'De Genst' Erwin . . 3 Guilliams Tim . . 4 Fauvet Bruno . . 5 Hejjaoui Mirva . . 6 Vendruscolo Michele . . 7 Lashuel Hilal A. . 8 Dobson Christopher M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 125 "15N chemical shifts" 125 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-07-20 update BMRB 'update entry citation' 2018-05-22 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27075 'phosphorylated S129 alpha-synuclein' 27076 'Y133F/Y136F mutant alpha-synuclein' 27077 'phosphorylated Y125 Y133F/Y136F mutant alpha-synuclein' stop_ _Original_release_date 2017-04-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29603451 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'El Turk' Farah . . 2 'De Genst' Erwin . . 3 Guilliams Tim . . 4 Fauvet Bruno . . 5 Hejjaoui Mirva . . 6 'Di Trani' Justin . . 7 Chiki Anass . . 8 Mittermaier Anthony . . 9 Vendruscolo Michele . . 10 Lashuel Hilal A. . 11 Dobson Christopher M. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 27 _Journal_issue 7 _Journal_ISSN 1469-896X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1262 _Page_last 1274 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'wild-type alpha-synuclein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'wild-type alpha-synuclein' $wild-type_alpha-synuclein stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_wild-type_alpha-synuclein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common wild-type_alpha-synuclein _Molecular_mass 14626 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 140 _Mol_residue_sequence ; MDVFMKGLSKAKEGVVAAAE KTKQGVAEAAGKTKEGVLYV GSKTKEGVVHGVATVAEKTK EQVTNVGGAVVTGVTAVAQK TVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 VAL 4 PHE 5 MET 6 LYS 7 GLY 8 LEU 9 SER 10 LYS 11 ALA 12 LYS 13 GLU 14 GLY 15 VAL 16 VAL 17 ALA 18 ALA 19 ALA 20 GLU 21 LYS 22 THR 23 LYS 24 GLN 25 GLY 26 VAL 27 ALA 28 GLU 29 ALA 30 ALA 31 GLY 32 LYS 33 THR 34 LYS 35 GLU 36 GLY 37 VAL 38 LEU 39 TYR 40 VAL 41 GLY 42 SER 43 LYS 44 THR 45 LYS 46 GLU 47 GLY 48 VAL 49 VAL 50 HIS 51 GLY 52 VAL 53 ALA 54 THR 55 VAL 56 ALA 57 GLU 58 LYS 59 THR 60 LYS 61 GLU 62 GLN 63 VAL 64 THR 65 ASN 66 VAL 67 GLY 68 GLY 69 ALA 70 VAL 71 VAL 72 THR 73 GLY 74 VAL 75 THR 76 ALA 77 VAL 78 ALA 79 GLN 80 LYS 81 THR 82 VAL 83 GLU 84 GLY 85 ALA 86 GLY 87 SER 88 ILE 89 ALA 90 ALA 91 ALA 92 THR 93 GLY 94 PHE 95 VAL 96 LYS 97 LYS 98 ASP 99 GLN 100 LEU 101 GLY 102 LYS 103 ASN 104 GLU 105 GLU 106 GLY 107 ALA 108 PRO 109 GLN 110 GLU 111 GLY 112 ILE 113 LEU 114 GLU 115 ASP 116 MET 117 PRO 118 VAL 119 ASP 120 PRO 121 ASP 122 ASN 123 GLU 124 ALA 125 TYR 126 GLU 127 MET 128 PRO 129 SER 130 GLU 131 GLU 132 GLY 133 TYR 134 GLN 135 ASP 136 TYR 137 GLU 138 PRO 139 GLU 140 ALA 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 $wild-type_alpha-synuclein 'E. coli' 562 Bacteria . Escherichia coli 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 $wild-type_alpha-synuclein 'recombinant technology' . Escherichia coli . pET stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; wild-type alpha-synuclein 25 mM tris, 100 mM NaCl 25 uM DSS ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $wild-type_alpha-synuclein 100 uM '[U-100% 13C; U-100% 15N]' NaCl 100 mM 'natural abundance' tris 25 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Zhengrong and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details ; Varian INOVA 800 MHz. 4 channels. Probe used was 13C-enhanced HCN cold probe with Z gradients. ; save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details ; 25 mM tris, 100 mM NaCl pH 7.40 25 uM DSS ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 123 . mM pH 7.40 0.02 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 H 1 'methyl protons' ppm 4.931 internal direct . . . 1 DSS N 15 'methyl protons' ppm 118.56 internal 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_ _Software_label $NMRPipe $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' 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 'wild-type alpha-synuclein' _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 3 3 VAL H H 8.295 . . 2 3 3 VAL N N 120.497 . . 3 4 4 PHE H H 8.399 . . 4 4 4 PHE N N 123.651 . . 5 5 5 MET H H 8.270 . . 6 5 5 MET N N 122.440 . . 7 6 6 LYS H H 8.329 . . 8 6 6 LYS N N 122.719 . . 9 8 8 LEU H H 8.112 . . 10 8 8 LEU N N 121.634 . . 11 9 9 SER H H 8.377 . . 12 9 9 SER N N 116.838 . . 13 10 10 LYS H H 8.426 . . 14 10 10 LYS N N 123.773 . . 15 11 11 ALA H H 8.356 . . 16 11 11 ALA N N 125.438 . . 17 12 12 LYS H H 8.397 . . 18 12 12 LYS N N 121.032 . . 19 13 13 GLU H H 8.496 . . 20 13 13 GLU N N 122.343 . . 21 15 15 VAL H H 8.037 . . 22 15 15 VAL N N 120.303 . . 23 17 17 ALA H H 8.511 . . 24 17 17 ALA N N 128.616 . . 25 18 18 ALA H H 8.377 . . 26 18 18 ALA N N 123.824 . . 27 19 19 ALA H H 8.335 . . 28 19 19 ALA N N 123.244 . . 29 20 20 GLU H H 8.390 . . 30 20 20 GLU N N 120.281 . . 31 21 21 LYS H H 8.396 . . 32 21 21 LYS N N 122.443 . . 33 22 22 THR H H 8.195 . . 34 22 22 THR N N 115.494 . . 35 23 23 LYS H H 8.409 . . 36 23 23 LYS N N 123.900 . . 37 24 24 GLN H H 8.486 . . 38 24 24 GLN N N 121.882 . . 39 25 25 GLY H H 8.538 . . 40 25 25 GLY N N 110.651 . . 41 26 26 VAL H H 8.075 . . 42 26 26 VAL N N 119.941 . . 43 27 27 ALA H H 8.481 . . 44 27 27 ALA N N 127.505 . . 45 28 28 GLU H H 8.461 . . 46 28 28 GLU N N 120.708 . . 47 29 29 ALA H H 8.358 . . 48 29 29 ALA N N 125.051 . . 49 30 30 ALA H H 8.293 . . 50 30 30 ALA N N 123.161 . . 51 31 31 GLY H H 8.366 . . 52 31 31 GLY N N 107.870 . . 53 32 32 LYS H H 8.160 . . 54 32 32 LYS N N 120.791 . . 55 33 33 THR H H 8.291 . . 56 33 33 THR N N 115.780 . . 57 34 34 LYS H H 8.535 . . 58 34 34 LYS N N 124.005 . . 59 36 36 GLY H H 8.484 . . 60 36 36 GLY N N 110.134 . . 61 37 37 VAL H H 7.966 . . 62 37 37 VAL N N 119.706 . . 63 38 38 LEU H H 8.343 . . 64 38 38 LEU N N 125.991 . . 65 39 39 TYR H H 8.337 . . 66 39 39 TYR N N 122.641 . . 67 40 40 VAL H H 8.138 . . 68 40 40 VAL N N 123.607 . . 69 41 41 GLY H H 8.091 . . 70 41 41 GLY N N 112.286 . . 71 43 43 LYS H H 8.536 . . 72 43 43 LYS N N 123.563 . . 73 44 44 THR H H 8.242 . . 74 44 44 THR N N 115.673 . . 75 45 45 LYS H H 8.498 . . 76 45 45 LYS N N 123.938 . . 77 48 48 VAL H H 7.969 . . 78 48 48 VAL N N 120.103 . . 79 49 49 VAL H H 8.365 . . 80 49 49 VAL N N 125.346 . . 81 51 51 GLY H H 8.461 . . 82 51 51 GLY N N 110.700 . . 83 52 52 VAL H H 8.096 . . 84 52 52 VAL N N 119.715 . . 85 53 53 ALA H H 8.552 . . 86 53 53 ALA N N 128.370 . . 87 54 54 THR H H 8.288 . . 88 54 54 THR N N 115.083 . . 89 55 55 VAL H H 8.310 . . 90 55 55 VAL N N 123.324 . . 91 56 56 ALA H H 8.474 . . 92 56 56 ALA N N 128.377 . . 93 57 57 GLU H H 8.436 . . 94 57 57 GLU N N 121.061 . . 95 58 58 LYS H H 8.497 . . 96 58 58 LYS N N 123.015 . . 97 59 59 THR H H 8.278 . . 98 59 59 THR N N 116.190 . . 99 60 60 LYS H H 8.452 . . 100 60 60 LYS N N 123.865 . . 101 61 61 GLU H H 8.505 . . 102 61 61 GLU N N 122.228 . . 103 62 62 GLN H H 8.486 . . 104 62 62 GLN N N 121.965 . . 105 63 63 VAL H H 8.350 . . 106 63 63 VAL N N 122.171 . . 107 64 64 THR H H 8.365 . . 108 64 64 THR N N 118.323 . . 109 65 65 ASN H H 8.579 . . 110 65 65 ASN N N 121.941 . . 111 66 66 VAL H H 8.305 . . 112 66 66 VAL N N 120.903 . . 113 67 67 GLY H H 8.615 . . 114 67 67 GLY N N 112.769 . . 115 68 68 GLY H H 8.286 . . 116 68 68 GLY N N 108.907 . . 117 69 69 ALA H H 8.221 . . 118 69 69 ALA N N 123.851 . . 119 70 70 VAL H H 8.283 . . 120 70 70 VAL N N 120.704 . . 121 71 71 VAL H H 8.462 . . 122 71 71 VAL N N 125.694 . . 123 72 72 THR H H 8.377 . . 124 72 72 THR N N 118.882 . . 125 73 73 GLY H H 8.496 . . 126 73 73 GLY N N 111.481 . . 127 74 74 VAL H H 8.144 . . 128 74 74 VAL N N 119.677 . . 129 75 75 THR H H 8.366 . . 130 75 75 THR N N 119.239 . . 131 76 76 ALA H H 8.436 . . 132 76 76 ALA N N 127.596 . . 133 77 77 VAL H H 8.215 . . 134 77 77 VAL N N 120.325 . . 135 78 78 ALA H H 8.487 . . 136 78 78 ALA N N 128.307 . . 137 79 79 GLN H H 8.460 . . 138 79 79 GLN N N 120.512 . . 139 80 80 LYS H H 8.500 . . 140 80 80 LYS N N 123.479 . . 141 81 81 THR H H 8.357 . . 142 81 81 THR N N 117.161 . . 143 82 82 VAL H H 8.371 . . 144 82 82 VAL N N 123.283 . . 145 83 83 GLU H H 8.636 . . 146 83 83 GLU N N 125.528 . . 147 84 84 GLY H H 8.580 . . 148 84 84 GLY N N 110.860 . . 149 85 85 ALA H H 8.319 . . 150 85 85 ALA N N 124.028 . . 151 86 86 GLY H H 8.554 . . 152 86 86 GLY N N 108.305 . . 153 87 87 SER H H 8.203 . . 154 87 87 SER N N 115.781 . . 155 88 88 ILE H H 8.255 . . 156 88 88 ILE N N 122.938 . . 157 89 89 ALA H H 8.412 . . 158 89 89 ALA N N 128.256 . . 159 90 90 ALA H H 8.276 . . 160 90 90 ALA N N 123.494 . . 161 91 91 ALA H H 8.354 . . 162 91 91 ALA N N 123.577 . . 163 92 92 THR H H 8.160 . . 164 92 92 THR N N 112.825 . . 165 93 93 GLY H H 8.364 . . 166 93 93 GLY N N 110.817 . . 167 94 94 PHE H H 8.144 . . 168 94 94 PHE N N 120.437 . . 169 95 95 VAL H H 8.113 . . 170 95 95 VAL N N 124.055 . . 171 96 96 LYS H H 8.455 . . 172 96 96 LYS N N 126.622 . . 173 97 97 LYS H H 8.534 . . 174 97 97 LYS N N 123.963 . . 175 98 98 ASP H H 8.461 . . 176 98 98 ASP N N 121.386 . . 177 99 99 GLN H H 8.406 . . 178 99 99 GLN N N 120.340 . . 179 100 100 LEU H H 8.360 . . 180 100 100 LEU N N 123.004 . . 181 101 101 GLY H H 8.538 . . 182 101 101 GLY N N 109.932 . . 183 102 102 LYS H H 8.267 . . 184 102 102 LYS N N 120.870 . . 185 103 103 ASN H H 8.680 . . 186 103 103 ASN N N 120.118 . . 187 104 104 GLU H H 8.533 . . 188 104 104 GLU N N 121.523 . . 189 105 105 GLU H H 8.526 . . 190 105 105 GLU N N 122.000 . . 191 106 106 GLY H H 8.492 . . 192 106 106 GLY N N 110.334 . . 193 107 107 ALA H H 8.181 . . 194 107 107 ALA N N 125.041 . . 195 109 109 GLN H H 8.653 . . 196 109 109 GLN N N 121.363 . . 197 110 110 GLU H H 8.590 . . 198 110 110 GLU N N 122.742 . . 199 111 111 GLY H H 8.545 . . 200 111 111 GLY N N 110.402 . . 201 112 112 ILE H H 8.063 . . 202 112 112 ILE N N 120.312 . . 203 113 113 LEU H H 8.477 . . 204 113 113 LEU N N 127.276 . . 205 114 114 GLU H H 8.487 . . 206 114 114 GLU N N 122.452 . . 207 115 115 ASP H H 8.422 . . 208 115 115 ASP N N 121.612 . . 209 116 116 MET H H 8.329 . . 210 116 116 MET N N 122.183 . . 211 118 118 VAL H H 8.374 . . 212 118 118 VAL N N 121.053 . . 213 119 119 ASP H H 8.592 . . 214 119 119 ASP N N 126.223 . . 215 121 121 ASP H H 8.435 . . 216 121 121 ASP N N 119.433 . . 217 122 122 ASN H H 8.169 . . 218 122 122 ASN N N 119.257 . . 219 123 123 GLU H H 8.437 . . 220 123 123 GLU N N 121.923 . . 221 124 124 ALA H H 8.289 . . 222 124 124 ALA N N 124.606 . . 223 125 125 TYR H H 8.096 . . 224 125 125 TYR N N 120.246 . . 225 126 126 GLU H H 8.188 . . 226 126 126 GLU N N 124.108 . . 227 127 127 MET H H 8.486 . . 228 127 127 MET N N 124.117 . . 229 129 129 SER H H 8.556 . . 230 129 129 SER N N 116.962 . . 231 130 130 GLU H H 8.642 . . 232 130 130 GLU N N 123.359 . . 233 131 131 GLU H H 8.528 . . 234 131 131 GLU N N 122.194 . . 235 132 132 GLY H H 8.463 . . 236 132 132 GLY N N 110.065 . . 237 133 133 TYR H H 8.125 . . 238 133 133 TYR N N 120.438 . . 239 134 134 GLN H H 8.276 . . 240 134 134 GLN N N 122.930 . . 241 135 135 ASP H H 8.290 . . 242 135 135 ASP N N 121.836 . . 243 136 136 TYR H H 8.099 . . 244 136 136 TYR N N 120.627 . . 245 137 137 GLU H H 8.314 . . 246 137 137 GLU N N 125.575 . . 247 139 139 GLU H H 8.581 . . 248 139 139 GLU N N 121.736 . . 249 140 140 ALA H H 8.067 . . 250 140 140 ALA N N 131.081 . . stop_ save_