data_27576 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for A97S TTR in 5% DMSO ; _BMRB_accession_number 27576 _BMRB_flat_file_name bmr27576.str _Entry_type original _Submission_date 2018-08-13 _Accession_date 2018-08-13 _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 Yu Tsyr-Yan . . 2 Yen Yueh-Jung . . 3 Chang Yu . . 4 Huang Shing-Jong . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 117 "13C chemical shifts" 126 "15N chemical shifts" 117 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-11-01 update BMRB 'update entry citation' 2018-09-12 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27575 'wt TTR in 5% DMSO' stop_ _Original_release_date 2018-08-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Biophysical characterization and modulation of Transthyretin Ala97Ser ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31502419 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Yo-Tsen T. . 2 Yen Yueh-Jung J. . 3 Ricardo Frans . . 4 Chang Yu . . 5 Wu Pei-Hao H. . 6 Huang Shing-Jong J. . 7 Lin Kon-Ping P. . 8 Yu Tsyr-Yan Y. . stop_ _Journal_abbreviation 'Ann. Clin. Transl. Neurol.' _Journal_name_full 'Annals of clinical and translational neurology' _Journal_volume 6 _Journal_issue 10 _Journal_ISSN 2328-9503 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1961 _Page_last 1970 _Year 2019 _Details . loop_ _Keyword 'A97S TTR' TTR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'A97S TTR' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'A97S TTR' $A97S_TTR stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_A97S_TTR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common A97S_TTR _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 127 _Mol_residue_sequence ; GPTGTGESKCPLMVKVLDAV RGSPAINVAVHVFRKAADDT WEPFASGKTSESGELHGLTT EEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTSNDS GPRRYTIAALLSPYSYSTTA VVTNPKE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PRO 3 THR 4 GLY 5 THR 6 GLY 7 GLU 8 SER 9 LYS 10 CYS 11 PRO 12 LEU 13 MET 14 VAL 15 LYS 16 VAL 17 LEU 18 ASP 19 ALA 20 VAL 21 ARG 22 GLY 23 SER 24 PRO 25 ALA 26 ILE 27 ASN 28 VAL 29 ALA 30 VAL 31 HIS 32 VAL 33 PHE 34 ARG 35 LYS 36 ALA 37 ALA 38 ASP 39 ASP 40 THR 41 TRP 42 GLU 43 PRO 44 PHE 45 ALA 46 SER 47 GLY 48 LYS 49 THR 50 SER 51 GLU 52 SER 53 GLY 54 GLU 55 LEU 56 HIS 57 GLY 58 LEU 59 THR 60 THR 61 GLU 62 GLU 63 GLU 64 PHE 65 VAL 66 GLU 67 GLY 68 ILE 69 TYR 70 LYS 71 VAL 72 GLU 73 ILE 74 ASP 75 THR 76 LYS 77 SER 78 TYR 79 TRP 80 LYS 81 ALA 82 LEU 83 GLY 84 ILE 85 SER 86 PRO 87 PHE 88 HIS 89 GLU 90 HIS 91 ALA 92 GLU 93 VAL 94 VAL 95 PHE 96 THR 97 SER 98 ASN 99 ASP 100 SER 101 GLY 102 PRO 103 ARG 104 ARG 105 TYR 106 THR 107 ILE 108 ALA 109 ALA 110 LEU 111 LEU 112 SER 113 PRO 114 TYR 115 SER 116 TYR 117 SER 118 THR 119 THR 120 ALA 121 VAL 122 VAL 123 THR 124 ASN 125 PRO 126 LYS 127 GLU 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 $A97S_TTR 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 $A97S_TTR 'recombinant technology' . Escherichia coli . pET21b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $A97S_TTR 0.75 mM 0.6 0.9 '[U-13C; U-15N; U-2H]' D2O 6 % . . '[U-99% 2H]' 'sodium phosphate' 25 mM . . 'natural abundance' 'sodium chloride' 100 mM . . 'natural abundance' EDTA 0.5 mM . . 'natural abundance' DMSO 5 % . . 'natural abundance' TCEP 1 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Rochus Keller' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . 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_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N 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' 25 . mM pH 6.5 . pH pressure 1 . atm temperature 37 . 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 internal direct . . . 1 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 internal direct . . . 1 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 1H-15N HSQC' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D 1H-15N NOESY' 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 'A97S TTR' _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 2 PRO CA C 62.986 . . 2 3 3 THR H H 8.199 . . 3 3 3 THR CA C 61.777 . . 4 3 3 THR N N 114.253 . . 5 4 4 GLY H H 8.319 . . 6 4 4 GLY CA C 45.084 . . 7 4 4 GLY N N 111.221 . . 8 5 5 THR H H 8.013 . . 9 5 5 THR CA C 61.664 . . 10 5 5 THR N N 113.244 . . 11 6 6 GLY H H 8.289 . . 12 6 6 GLY CA C 45.021 . . 13 6 6 GLY N N 111.328 . . 14 7 7 GLU H H 8.102 . . 15 7 7 GLU CA C 56.269 . . 16 7 7 GLU N N 120.886 . . 17 8 8 SER H H 8.215 . . 18 8 8 SER CA C 58.253 . . 19 8 8 SER N N 117.129 . . 20 9 9 LYS H H 8.341 . . 21 9 9 LYS CA C 55.375 . . 22 9 9 LYS N N 123.339 . . 23 10 10 CYS H H 8.115 . . 24 10 10 CYS CA C 55.127 . . 25 10 10 CYS N N 121.822 . . 26 11 11 PRO CA C 63.99 . . 27 12 12 LEU H H 6.861 . . 28 12 12 LEU CA C 53.424 . . 29 12 12 LEU N N 120.307 . . 30 13 13 MET H H 8.61 . . 31 13 13 MET CA C 54.476 . . 32 13 13 MET N N 126.545 . . 33 14 14 VAL H H 7.405 . . 34 14 14 VAL CA C 59.815 . . 35 14 14 VAL N N 122.517 . . 36 15 15 LYS H H 8.734 . . 37 15 15 LYS CA C 54.386 . . 38 15 15 LYS N N 127.413 . . 39 16 16 VAL H H 8.986 . . 40 16 16 VAL CA C 60.559 . . 41 16 16 VAL N N 124.43 . . 42 17 17 LEU H H 8.51 . . 43 17 17 LEU CA C 53.46 . . 44 17 17 LEU N N 126.66 . . 45 18 18 ASP H H 8.63 . . 46 18 18 ASP CA C 52.916 . . 47 18 18 ASP N N 122.095 . . 48 19 19 ALA H H 9.002 . . 49 19 19 ALA CA C 53.312 . . 50 19 19 ALA N N 127.644 . . 51 20 20 VAL H H 9.6 . . 52 20 20 VAL CA C 65.25 . . 53 20 20 VAL N N 120.678 . . 54 21 21 ARG H H 8.229 . . 55 21 21 ARG CA C 55.059 . . 56 21 21 ARG N N 116.715 . . 57 22 22 GLY H H 7.391 . . 58 22 22 GLY CA C 46.955 . . 59 22 22 GLY N N 109.488 . . 60 23 23 SER H H 7.367 . . 61 23 23 SER CA C 54.829 . . 62 23 23 SER N N 111.361 . . 63 24 24 PRO CA C 62.716 . . 64 25 25 ALA H H 8.039 . . 65 25 25 ALA CA C 50.377 . . 66 25 25 ALA N N 127.788 . . 67 26 26 ILE H H 7.8 . . 68 26 26 ILE CA C 61.526 . . 69 26 26 ILE N N 127.275 . . 70 27 27 ASN H H 7.722 . . 71 27 27 ASN CA C 54.176 . . 72 27 27 ASN N N 122.368 . . 73 28 28 VAL H H 8.303 . . 74 28 28 VAL CA C 61.61 . . 75 28 28 VAL N N 120.285 . . 76 29 29 ALA H H 9.08 . . 77 29 29 ALA CA C 52.408 . . 78 29 29 ALA N N 130.928 . . 79 30 30 VAL H H 8.33 . . 80 30 30 VAL CA C 60.338 . . 81 30 30 VAL N N 122.476 . . 82 31 31 HIS H H 8.946 . . 83 31 31 HIS CA C 54.6 . . 84 31 31 HIS N N 124.523 . . 85 32 32 VAL H H 9.152 . . 86 32 32 VAL CA C 59.82 . . 87 32 32 VAL N N 122.219 . . 88 33 33 PHE H H 9.885 . . 89 33 33 PHE CA C 55.979 . . 90 33 33 PHE N N 128.419 . . 91 34 34 ARG H H 9.4 . . 92 34 34 ARG CA C 53.891 . . 93 34 34 ARG N N 122.617 . . 94 35 35 LYS H H 8.481 . . 95 35 35 LYS CA C 57.006 . . 96 35 35 LYS N N 130.17 . . 97 36 36 ALA H H 8.744 . . 98 36 36 ALA CA C 50.673 . . 99 36 36 ALA N N 131.267 . . 100 37 37 ALA H H 8.305 . . 101 37 37 ALA CA C 53.803 . . 102 37 37 ALA N N 122.34 . . 103 38 38 ASP H H 7.644 . . 104 38 38 ASP CA C 52.983 . . 105 38 38 ASP N N 115.954 . . 106 39 39 ASP H H 7.86 . . 107 39 39 ASP CA C 55.816 . . 108 39 39 ASP N N 113.423 . . 109 40 40 THR H H 7.222 . . 110 40 40 THR CA C 61.28 . . 111 40 40 THR N N 110.979 . . 112 41 41 TRP H H 8.332 . . 113 41 41 TRP CA C 55.399 . . 114 41 41 TRP N N 120.498 . . 115 42 42 GLU H H 9.196 . . 116 42 42 GLU CA C 52.876 . . 117 42 42 GLU N N 126.706 . . 118 43 43 PRO CA C 64.489 . . 119 44 44 PHE H H 8.762 . . 120 44 44 PHE CA C 58.858 . . 121 44 44 PHE N N 125.153 . . 122 45 45 ALA H H 7.828 . . 123 45 45 ALA CA C 52.075 . . 124 45 45 ALA N N 119.035 . . 125 46 46 SER H H 8.462 . . 126 46 46 SER CA C 57.412 . . 127 46 46 SER N N 113.814 . . 128 47 47 GLY H H 8.363 . . 129 47 47 GLY CA C 45.349 . . 130 47 47 GLY N N 107.058 . . 131 48 48 LYS H H 8.386 . . 132 48 48 LYS CA C 53.547 . . 133 48 48 LYS N N 120.219 . . 134 49 49 THR H H 8.604 . . 135 49 49 THR CA C 61.957 . . 136 49 49 THR N N 111.894 . . 137 50 50 SER H H 8.469 . . 138 50 50 SER CA C 56.939 . . 139 50 50 SER N N 118.387 . . 140 51 51 GLU H H 9.003 . . 141 51 51 GLU CA C 58.888 . . 142 51 51 GLU N N 118.882 . . 143 52 52 SER H H 8.033 . . 144 52 52 SER CA C 57.349 . . 145 52 52 SER N N 111.815 . . 146 53 53 GLY H H 8.476 . . 147 53 53 GLY CA C 45.225 . . 148 53 53 GLY N N 112.355 . . 149 54 54 GLU H H 7.119 . . 150 54 54 GLU CA C 54.128 . . 151 54 54 GLU N N 116.055 . . 152 55 55 LEU H H 8.566 . . 153 55 55 LEU CA C 53.896 . . 154 55 55 LEU N N 123.769 . . 155 56 56 HIS CA C 53.984 . . 156 57 57 GLY H H 9.039 . . 157 57 57 GLY CA C 46.293 . . 158 57 57 GLY N N 109.487 . . 159 58 58 LEU H H 8.262 . . 160 58 58 LEU CA C 57.099 . . 161 58 58 LEU N N 120.087 . . 162 59 59 THR H H 7.232 . . 163 59 59 THR CA C 59.368 . . 164 59 59 THR N N 107.954 . . 165 60 60 THR H H 8.399 . . 166 60 60 THR CA C 59.491 . . 167 60 60 THR N N 112.36 . . 168 61 61 GLU H H 8.758 . . 169 61 61 GLU CA C 59.486 . . 170 61 61 GLU N N 121.176 . . 171 62 62 GLU H H 8.587 . . 172 62 62 GLU CA C 58.616 . . 173 62 62 GLU N N 116.563 . . 174 63 63 GLU H H 7.295 . . 175 63 63 GLU CA C 56.78 . . 176 63 63 GLU N N 115.88 . . 177 64 64 PHE H H 7.812 . . 178 64 64 PHE CA C 55.974 . . 179 64 64 PHE N N 124.254 . . 180 65 65 VAL H H 7.154 . . 181 65 65 VAL CA C 60.11 . . 182 65 65 VAL N N 117.509 . . 183 66 66 GLU H H 8.441 . . 184 66 66 GLU CA C 56.932 . . 185 66 66 GLU N N 121.961 . . 186 67 67 GLY H H 7.947 . . 187 67 67 GLY CA C 44.541 . . 188 67 67 GLY N N 110.615 . . 189 68 68 ILE H H 8.166 . . 190 68 68 ILE CA C 60.635 . . 191 68 68 ILE N N 121.085 . . 192 69 69 TYR H H 8.55 . . 193 69 69 TYR CA C 56.535 . . 194 69 69 TYR N N 124.899 . . 195 70 70 LYS H H 8.608 . . 196 70 70 LYS CA C 53.357 . . 197 70 70 LYS N N 118.831 . . 198 71 71 VAL H H 9.596 . . 199 71 71 VAL CA C 60.948 . . 200 71 71 VAL N N 127.684 . . 201 72 72 GLU H H 9.648 . . 202 72 72 GLU CA C 54.922 . . 203 72 72 GLU N N 128.396 . . 204 73 73 ILE H H 9.099 . . 205 73 73 ILE CA C 60.157 . . 206 73 73 ILE N N 126.252 . . 207 74 74 ASP H H 8.873 . . 208 74 74 ASP CA C 53.245 . . 209 74 74 ASP N N 128.459 . . 210 75 75 THR H H 8.166 . . 211 75 75 THR CA C 64.343 . . 212 75 75 THR N N 117.681 . . 213 76 76 LYS H H 7.513 . . 214 76 76 LYS CA C 60.128 . . 215 76 76 LYS N N 124.712 . . 216 77 77 SER H H 8.133 . . 217 77 77 SER CA C 61.483 . . 218 77 77 SER N N 113.391 . . 219 78 78 TYR H H 6.701 . . 220 78 78 TYR CA C 60.917 . . 221 78 78 TYR N N 121.451 . . 222 79 79 TRP H H 7.724 . . 223 79 79 TRP CA C 59.03 . . 224 79 79 TRP N N 117.578 . . 225 80 80 LYS H H 8.703 . . 226 80 80 LYS CA C 59.303 . . 227 80 80 LYS N N 118.747 . . 228 81 81 ALA H H 7.479 . . 229 81 81 ALA CA C 54.167 . . 230 81 81 ALA N N 122.394 . . 231 82 82 LEU H H 7.223 . . 232 82 82 LEU CA C 54.183 . . 233 82 82 LEU N N 117.7 . . 234 83 83 GLY H H 7.889 . . 235 83 83 GLY CA C 45.31 . . 236 83 83 GLY N N 107.697 . . 237 84 84 ILE H H 7.883 . . 238 84 84 ILE CA C 59.441 . . 239 84 84 ILE N N 123.1 . . 240 85 85 SER H H 8.374 . . 241 85 85 SER CA C 54.526 . . 242 85 85 SER N N 121.983 . . 243 86 86 PRO CA C 61.185 . . 244 87 87 PHE H H 7.229 . . 245 87 87 PHE CA C 60.312 . . 246 87 87 PHE N N 116.436 . . 247 88 88 HIS H H 7.627 . . 248 88 88 HIS CA C 57.815 . . 249 88 88 HIS N N 113.52 . . 250 89 89 GLU H H 8.037 . . 251 89 89 GLU CA C 54.495 . . 252 89 89 GLU N N 121.472 . . 253 90 90 HIS H H 8.056 . . 254 90 90 HIS CA C 54.414 . . 255 90 90 HIS N N 119.576 . . 256 91 91 ALA H H 8.352 . . 257 91 91 ALA CA C 51.541 . . 258 91 91 ALA N N 120.07 . . 259 92 92 GLU H H 8.219 . . 260 92 92 GLU CA C 54.25 . . 261 92 92 GLU N N 121.792 . . 262 93 93 VAL H H 8.805 . . 263 93 93 VAL CA C 61.293 . . 264 93 93 VAL N N 122.055 . . 265 94 94 VAL H H 9.08 . . 266 94 94 VAL CA C 60.791 . . 267 94 94 VAL N N 128.282 . . 268 95 95 PHE H H 8.934 . . 269 95 95 PHE CA C 55.687 . . 270 95 95 PHE N N 124.884 . . 271 96 96 THR H H 8.575 . . 272 96 96 THR CA C 61.466 . . 273 96 96 THR N N 116.632 . . 274 97 97 SER H H 9.019 . . 275 97 97 SER CA C 56.648 . . 276 97 97 SER N N 121.343 . . 277 98 98 ASN H H 8.245 . . 278 98 98 ASN CA C 53.228 . . 279 98 98 ASN N N 121.017 . . 280 99 99 ASP H H 8.591 . . 281 99 99 ASP CA C 54.453 . . 282 99 99 ASP N N 121.041 . . 283 100 100 SER H H 8.29 . . 284 100 100 SER CA C 58.12 . . 285 100 100 SER N N 115.71 . . 286 101 101 GLY H H 7.816 . . 287 101 101 GLY CA C 43.988 . . 288 101 101 GLY N N 110.855 . . 289 102 102 PRO CA C 57.812 . . 290 103 103 ARG H H 8.847 . . 291 103 103 ARG CA C 57.856 . . 292 103 103 ARG N N 121.281 . . 293 104 104 ARG H H 7.228 . . 294 104 104 ARG CA C 54.350 . . 295 104 104 ARG N N 106.823 . . 296 105 105 TYR H H 8.724 . . 297 105 105 TYR CA C 56.779 . . 298 105 105 TYR N N 122.143 . . 299 106 106 THR H H 8.776 . . 300 106 106 THR CA C 61.718 . . 301 106 106 THR N N 120.747 . . 302 107 107 ILE H H 8.76 . . 303 107 107 ILE CA C 58.251 . . 304 107 107 ILE N N 127.567 . . 305 108 108 ALA H H 8.775 . . 306 108 108 ALA CA C 49.023 . . 307 108 108 ALA N N 129.012 . . 308 109 109 ALA H H 9.024 . . 309 109 109 ALA CA C 50.122 . . 310 109 109 ALA N N 126.368 . . 311 110 110 LEU H H 8.734 . . 312 110 110 LEU CA C 53.735 . . 313 110 110 LEU N N 126.153 . . 314 111 111 LEU H H 9.018 . . 315 111 111 LEU CA C 55.366 . . 316 111 111 LEU N N 124.254 . . 317 112 112 SER H H 8.982 . . 318 112 112 SER CA C 57.896 . . 319 112 112 SER N N 117.125 . . 320 113 113 PRO CA C 66.641 . . 321 114 114 TYR H H 8.066 . . 322 114 114 TYR CA C 58.113 . . 323 114 114 TYR N N 114.403 . . 324 115 115 SER H H 7.408 . . 325 115 115 SER CA C 57.182 . . 326 115 115 SER N N 112.691 . . 327 116 116 TYR H H 8.368 . . 328 116 116 TYR CA C 56.847 . . 329 116 116 TYR N N 120.714 . . 330 117 117 SER H H 8.399 . . 331 117 117 SER CA C 55.002 . . 332 117 117 SER N N 114.138 . . 333 118 118 THR H H 8.83 . . 334 118 118 THR CA C 58.612 . . 335 118 118 THR N N 116.557 . . 336 119 119 THR H H 8.33 . . 337 119 119 THR CA C 61.114 . . 338 119 119 THR N N 122.753 . . 339 120 120 ALA H H 8.426 . . 340 120 120 ALA CA C 49.57 . . 341 120 120 ALA N N 129.843 . . 342 121 121 VAL H H 8.263 . . 343 121 121 VAL CA C 60.014 . . 344 121 121 VAL N N 119.693 . . 345 122 122 VAL H H 8.409 . . 346 122 122 VAL CA C 60.733 . . 347 122 122 VAL N N 128.746 . . 348 123 123 THR H H 8.448 . . 349 123 123 THR CA C 60.056 . . 350 123 123 THR N N 118.321 . . 351 124 124 ASN H H 8.493 . . 352 124 124 ASN CA C 50.459 . . 353 124 124 ASN N N 120.478 . . 354 125 125 PRO CA C 62.96 . . 355 126 126 LYS H H 8.109 . . 356 126 126 LYS CA C 55.985 . . 357 126 126 LYS N N 121.345 . . 358 127 127 GLU H H 7.663 . . 359 127 127 GLU CA C 57.592 . . 360 127 127 GLU N N 126.785 . . stop_ save_