data_27516 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR measurements reveal the structural basis of transthyretin destabilization by pathogenic mutations ; _BMRB_accession_number 27516 _BMRB_flat_file_name bmr27516.str _Entry_type original _Submission_date 2018-06-08 _Accession_date 2018-06-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NMR assignments for the V122I mutant of Transthyretin' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wright Peter E. . 2 Leach Benjamin I. . 3 Zhang Xin . . 4 Kelly Jeffery W. . 5 Dyson Jane H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 115 "13C chemical shifts" 122 "15N chemical shifts" 115 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-09-26 update BMRB 'update entry citation' 2019-01-07 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27513 transthyretin 27514 'wild-type transthyretin' 27515 'V30M Transthyretin' stop_ _Original_release_date 2018-06-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29972637 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Leach Benjamin I. . 2 Zhang Xin . . 3 Kelly Jeffery W. . 4 Dyson Jane H. . 5 Wright Peter E. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 57 _Journal_issue 30 _Journal_ISSN 1520-4995 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4421 _Page_last 4430 _Year 2018 _Details . loop_ _Keyword Transthyretin V122I mutant stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'V122I Transthyretin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Transthyretin $Transthyretin_V122I 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_Transthyretin_V122I _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Transthyretin_V122I _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 147 _Mol_residue_sequence ; MASHRLLLLCLAGLVFVSEA GPTGTGESKCPLMVKVLDAV RGSPAINVAVHVFRKAADDT WEPFASGKTSESGELHGLTT EEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDS GPRRYTIAALLSPYSYSTTA VITNPKE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -19 MET 2 -18 ALA 3 -17 SER 4 -16 HIS 5 -15 ARG 6 -14 LEU 7 -13 LEU 8 -12 LEU 9 -11 LEU 10 -10 CYS 11 -9 LEU 12 -8 ALA 13 -7 GLY 14 -6 LEU 15 -5 VAL 16 -4 PHE 17 -3 VAL 18 -2 SER 19 -1 GLU 20 0 ALA 21 1 GLY 22 2 PRO 23 3 THR 24 4 GLY 25 5 THR 26 6 GLY 27 7 GLU 28 8 SER 29 9 LYS 30 10 CYS 31 11 PRO 32 12 LEU 33 13 MET 34 14 VAL 35 15 LYS 36 16 VAL 37 17 LEU 38 18 ASP 39 19 ALA 40 20 VAL 41 21 ARG 42 22 GLY 43 23 SER 44 24 PRO 45 25 ALA 46 26 ILE 47 27 ASN 48 28 VAL 49 29 ALA 50 30 VAL 51 31 HIS 52 32 VAL 53 33 PHE 54 34 ARG 55 35 LYS 56 36 ALA 57 37 ALA 58 38 ASP 59 39 ASP 60 40 THR 61 41 TRP 62 42 GLU 63 43 PRO 64 44 PHE 65 45 ALA 66 46 SER 67 47 GLY 68 48 LYS 69 49 THR 70 50 SER 71 51 GLU 72 52 SER 73 53 GLY 74 54 GLU 75 55 LEU 76 56 HIS 77 57 GLY 78 58 LEU 79 59 THR 80 60 THR 81 61 GLU 82 62 GLU 83 63 GLU 84 64 PHE 85 65 VAL 86 66 GLU 87 67 GLY 88 68 ILE 89 69 TYR 90 70 LYS 91 71 VAL 92 72 GLU 93 73 ILE 94 74 ASP 95 75 THR 96 76 LYS 97 77 SER 98 78 TYR 99 79 TRP 100 80 LYS 101 81 ALA 102 82 LEU 103 83 GLY 104 84 ILE 105 85 SER 106 86 PRO 107 87 PHE 108 88 HIS 109 89 GLU 110 90 HIS 111 91 ALA 112 92 GLU 113 93 VAL 114 94 VAL 115 95 PHE 116 96 THR 117 97 ALA 118 98 ASN 119 99 ASP 120 100 SER 121 101 GLY 122 102 PRO 123 103 ARG 124 104 ARG 125 105 TYR 126 106 THR 127 107 ILE 128 108 ALA 129 109 ALA 130 110 LEU 131 111 LEU 132 112 SER 133 113 PRO 134 114 TYR 135 115 SER 136 116 TYR 137 117 SER 138 118 THR 139 119 THR 140 120 ALA 141 121 VAL 142 122 ILE 143 123 THR 144 124 ASN 145 125 PRO 146 126 LYS 147 127 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 $Transthyretin_V122I 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 $Transthyretin_V122I 'recombinant technology' . Escherichia coli . 'pET 29b+' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '800 uM Transthyretin V122I' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'sodium phosphate' 10 mM 'natural abundance' 'potassium chloride' 100 mM 'natural abundance' $Transthyretin_V122I 800 uM '[U-13C; U-15N; U-2H;]' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . Goddard . . stop_ loop_ _Task 'chemical shift assignment' collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 750 _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 7 . pH pressure 1 . atm temperature 298 . 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 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 external direct . . . 1 DSS N 15 'methyl protons' ppm 0 external 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 $xwinnmr stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' 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 Transthyretin _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 22 PRO CA C 62.931 0.00 1 2 3 23 THR H H 8.177 0.00 1 3 3 23 THR CA C 61.584 0.01 1 4 3 23 THR N N 114.096 0.01 1 5 4 24 GLY H H 8.259 0.00 1 6 4 24 GLY CA C 44.858 0.02 1 7 4 24 GLY N N 111.439 0.03 1 8 5 25 THR H H 8.038 0.00 1 9 5 25 THR CA C 61.532 0.05 1 10 5 25 THR N N 113.440 0.02 1 11 6 26 GLY H H 8.342 0.00 1 12 6 26 GLY CA C 44.800 0.01 1 13 6 26 GLY N N 111.466 0.02 1 14 7 27 GLU H H 8.114 0.00 1 15 7 27 GLU CA C 56.078 0.01 1 16 7 27 GLU N N 121.024 0.01 1 17 8 28 SER H H 8.251 0.00 1 18 8 28 SER CA C 58.132 0.02 1 19 8 28 SER N N 117.460 0.01 1 20 9 29 LYS H H 8.355 0.00 1 21 9 29 LYS CA C 55.285 0.07 1 22 9 29 LYS N N 123.633 0.00 1 23 10 30 CYS H H 8.168 0.00 1 24 10 30 CYS N N 122.610 0.03 1 25 11 31 PRO CA C 63.961 0.00 1 26 12 32 LEU H H 6.863 0.00 1 27 12 32 LEU CA C 53.345 0.01 1 28 12 32 LEU N N 120.809 0.00 1 29 13 33 MET H H 8.628 0.00 1 30 13 33 MET CA C 54.255 0.02 1 31 13 33 MET N N 127.041 0.02 1 32 14 34 VAL H H 7.356 0.01 1 33 14 34 VAL CA C 59.731 0.00 1 34 14 34 VAL N N 122.603 0.02 1 35 15 35 LYS H H 8.683 0.00 1 36 15 35 LYS CA C 54.180 0.00 1 37 15 35 LYS N N 127.422 0.01 1 38 16 36 VAL H H 8.941 0.00 1 39 16 36 VAL CA C 60.467 0.00 1 40 16 36 VAL N N 124.401 0.01 1 41 17 37 LEU H H 8.461 0.00 1 42 17 37 LEU CA C 53.373 0.01 1 43 17 37 LEU N N 126.862 0.01 1 44 18 38 ASP H H 8.576 0.00 1 45 18 38 ASP CA C 52.795 0.01 1 46 18 38 ASP N N 121.901 0.02 1 47 19 39 ALA H H 8.974 0.00 1 48 19 39 ALA CA C 53.232 0.00 1 49 19 39 ALA N N 127.854 0.00 1 50 20 40 VAL H H 9.574 0.00 1 51 20 40 VAL CA C 65.134 0.01 1 52 20 40 VAL N N 120.655 0.04 1 53 21 41 ARG H H 8.181 0.01 1 54 21 41 ARG CA C 55.054 0.00 1 55 21 41 ARG N N 117.069 0.00 1 56 22 42 GLY H H 7.398 0.01 1 57 22 42 GLY CA C 46.585 0.04 1 58 22 42 GLY N N 109.908 0.03 1 59 23 43 SER H H 7.337 0.00 1 60 23 43 SER CA C 54.874 0.00 1 61 23 43 SER N N 111.830 0.01 1 62 24 44 PRO CA C 62.584 0.00 1 63 25 45 ALA H H 8.019 0.00 1 64 25 45 ALA CA C 50.253 0.00 1 65 25 45 ALA N N 127.698 0.02 1 66 26 46 ILE H H 7.843 0.00 1 67 26 46 ILE CA C 61.439 0.01 1 68 26 46 ILE N N 127.438 0.00 1 69 27 47 ASN H H 7.716 0.00 1 70 27 47 ASN CA C 53.999 0.02 1 71 27 47 ASN N N 122.791 0.03 1 72 28 48 VAL H H 8.315 0.01 1 73 28 48 VAL CA C 61.405 0.01 1 74 28 48 VAL N N 120.544 0.14 1 75 29 49 ALA H H 9.091 0.00 1 76 29 49 ALA CA C 52.311 0.01 1 77 29 49 ALA N N 131.159 0.00 1 78 30 50 VAL H H 8.290 0.00 1 79 30 50 VAL CA C 60.225 0.00 1 80 30 50 VAL N N 122.593 0.01 1 81 31 51 HIS H H 8.915 0.00 1 82 31 51 HIS CA C 54.778 0.00 1 83 31 51 HIS N N 124.725 0.03 1 84 32 52 VAL H H 9.162 0.00 1 85 32 52 VAL CA C 59.609 0.02 1 86 32 52 VAL N N 122.072 0.01 1 87 33 53 PHE H H 9.859 0.00 1 88 33 53 PHE CA C 55.898 0.01 1 89 33 53 PHE N N 128.708 0.02 1 90 34 54 ARG H H 9.412 0.00 1 91 34 54 ARG CA C 53.805 0.02 1 92 34 54 ARG N N 122.887 0.00 1 93 35 55 LYS H H 8.535 0.00 1 94 35 55 LYS CA C 56.946 0.00 1 95 35 55 LYS N N 130.620 0.02 1 96 36 56 ALA H H 8.760 0.00 1 97 36 56 ALA CA C 50.566 0.01 1 98 36 56 ALA N N 131.715 0.01 1 99 37 57 ALA H H 8.353 0.00 1 100 37 57 ALA CA C 53.770 0.00 1 101 37 57 ALA N N 122.715 0.02 1 102 38 58 ASP H H 7.618 0.00 1 103 38 58 ASP CA C 52.713 0.02 1 104 38 58 ASP N N 115.986 0.01 1 105 39 59 ASP H H 7.836 0.00 1 106 39 59 ASP CA C 55.808 0.02 1 107 39 59 ASP N N 113.267 0.02 1 108 40 60 THR H H 7.184 0.00 1 109 40 60 THR CA C 61.111 0.02 1 110 40 60 THR N N 110.961 0.01 1 111 41 61 TRP H H 8.339 0.00 1 112 41 61 TRP CA C 55.269 0.01 1 113 41 61 TRP N N 120.334 0.03 1 114 42 62 GLU H H 9.161 0.00 1 115 42 62 GLU CA C 52.783 0.00 1 116 42 62 GLU N N 127.099 0.01 1 117 43 63 PRO CA C 64.528 0.00 1 118 44 64 PHE H H 8.759 0.00 1 119 44 64 PHE CA C 58.796 0.01 1 120 44 64 PHE N N 125.505 0.00 1 121 45 65 ALA H H 7.816 0.00 1 122 45 65 ALA CA C 51.993 0.00 1 123 45 65 ALA N N 119.292 0.04 1 124 46 66 SER H H 8.477 0.00 1 125 46 66 SER CA C 57.463 0.01 1 126 46 66 SER N N 113.610 0.02 1 127 47 67 GLY H H 8.357 0.00 1 128 47 67 GLY CA C 45.204 0.01 1 129 47 67 GLY N N 107.135 0.05 1 130 48 68 LYS H H 8.411 0.00 1 131 48 68 LYS CA C 53.329 0.01 1 132 48 68 LYS N N 120.510 0.02 1 133 49 69 THR H H 8.600 0.00 1 134 49 69 THR CA C 61.849 0.01 1 135 49 69 THR N N 112.090 0.01 1 136 50 70 SER H H 8.470 0.00 1 137 50 70 SER CA C 56.867 0.00 1 138 50 70 SER N N 118.714 0.02 1 139 51 71 GLU H H 8.970 0.00 1 140 51 71 GLU CA C 58.697 0.02 1 141 51 71 GLU N N 118.794 0.01 1 142 52 72 SER H H 8.028 0.00 1 143 52 72 SER CA C 57.264 0.03 1 144 52 72 SER N N 112.043 0.03 1 145 53 73 GLY H H 8.453 0.00 1 146 53 73 GLY CA C 45.007 0.01 1 147 53 73 GLY N N 112.659 0.04 1 148 54 74 GLU H H 7.080 0.00 1 149 54 74 GLU CA C 54.001 0.03 1 150 54 74 GLU N N 116.061 0.01 1 151 55 75 LEU H H 8.525 0.00 1 152 55 75 LEU CA C 53.555 0.00 1 153 55 75 LEU N N 123.903 0.00 1 154 56 76 HIS CA C 55.524 0.00 1 155 57 77 GLY H H 8.133 0.01 1 156 57 77 GLY CA C 46.224 0.07 1 157 57 77 GLY N N 108.874 0.01 1 158 58 78 LEU H H 8.322 0.00 1 159 58 78 LEU N N 120.340 0.00 1 160 59 79 THR H H 7.154 0.01 1 161 59 79 THR CA C 59.112 0.04 1 162 59 79 THR N N 107.820 0.05 1 163 60 80 THR H H 8.416 0.00 1 164 60 80 THR CA C 59.172 0.02 1 165 60 80 THR N N 112.137 0.02 1 166 61 81 GLU H H 8.957 0.00 1 167 61 81 GLU CA C 59.572 0.02 1 168 61 81 GLU N N 121.223 0.01 1 169 62 82 GLU H H 8.568 0.00 1 170 62 82 GLU CA C 58.755 0.02 1 171 62 82 GLU N N 116.415 0.01 1 172 63 83 GLU H H 7.208 0.00 1 173 63 83 GLU CA C 56.738 0.02 1 174 63 83 GLU N N 115.913 0.07 1 175 64 84 PHE H H 7.761 0.00 1 176 64 84 PHE CA C 54.913 0.01 1 177 64 84 PHE N N 124.063 0.02 1 178 65 85 VAL H H 7.040 0.00 1 179 65 85 VAL CA C 59.754 0.01 1 180 65 85 VAL N N 115.727 0.03 1 181 66 86 GLU H H 8.505 0.00 1 182 66 86 GLU CA C 56.549 0.01 1 183 66 86 GLU N N 121.981 0.03 1 184 67 87 GLY H H 7.844 0.00 1 185 67 87 GLY CA C 44.204 0.02 1 186 67 87 GLY N N 111.473 0.01 1 187 68 88 ILE H H 8.228 0.00 1 188 68 88 ILE CA C 60.529 0.02 1 189 68 88 ILE N N 120.864 0.01 1 190 69 89 TYR H H 8.557 0.00 1 191 69 89 TYR CA C 56.091 0.02 1 192 69 89 TYR N N 125.209 0.02 1 193 70 90 LYS H H 8.581 0.00 1 194 70 90 LYS CA C 53.176 0.00 1 195 70 90 LYS N N 118.864 0.01 1 196 71 91 VAL H H 9.558 0.00 1 197 71 91 VAL CA C 60.745 0.00 1 198 71 91 VAL N N 127.758 0.00 1 199 72 92 GLU H H 9.668 0.00 1 200 72 92 GLU CA C 54.794 0.05 1 201 72 92 GLU N N 128.737 0.01 1 202 73 93 ILE H H 9.134 0.00 1 203 73 93 ILE CA C 60.006 0.00 1 204 73 93 ILE N N 126.539 0.03 1 205 74 94 ASP H H 8.839 0.00 1 206 74 94 ASP CA C 52.900 0.03 1 207 74 94 ASP N N 128.426 0.01 1 208 75 95 THR H H 8.163 0.00 1 209 75 95 THR CA C 64.376 0.11 1 210 75 95 THR N N 117.949 0.01 1 211 76 96 LYS H H 7.589 0.00 1 212 76 96 LYS CA C 60.021 0.02 1 213 76 96 LYS N N 124.886 0.04 1 214 77 97 SER H H 8.077 0.00 1 215 77 97 SER CA C 61.501 0.01 1 216 77 97 SER N N 113.424 0.02 1 217 78 98 TYR H H 6.680 0.00 1 218 78 98 TYR CA C 60.802 0.02 1 219 78 98 TYR N N 121.570 0.01 1 220 79 99 TRP H H 7.735 0.01 1 221 79 99 TRP CA C 58.971 0.02 1 222 79 99 TRP N N 117.833 0.03 1 223 80 100 LYS H H 8.687 0.00 1 224 80 100 LYS CA C 59.222 0.00 1 225 80 100 LYS N N 118.914 0.00 1 226 81 101 ALA H H 7.465 0.00 1 227 81 101 ALA CA C 54.048 0.02 1 228 81 101 ALA N N 122.477 0.02 1 229 82 102 LEU H H 7.196 0.00 1 230 82 102 LEU CA C 54.073 0.00 1 231 82 102 LEU N N 117.957 0.02 1 232 83 103 GLY H H 7.868 0.00 1 233 83 103 GLY CA C 45.099 0.01 1 234 83 103 GLY N N 107.990 0.01 1 235 84 104 ILE H H 7.859 0.00 1 236 84 104 ILE CA C 59.340 0.01 1 237 84 104 ILE N N 123.365 0.00 1 238 85 105 SER H H 8.384 0.00 1 239 85 105 SER CA C 54.451 0.00 1 240 85 105 SER N N 122.304 0.01 1 241 86 106 PRO CA C 61.024 0.00 1 242 87 107 PHE H H 7.190 0.00 1 243 87 107 PHE CA C 59.852 0.02 1 244 87 107 PHE N N 116.150 0.02 1 245 88 108 HIS H H 7.652 0.00 1 246 88 108 HIS CA C 57.640 0.00 1 247 88 108 HIS N N 113.854 0.00 1 248 89 109 GLU H H 8.848 0.00 1 249 89 109 GLU CA C 57.748 0.00 1 250 89 109 GLU N N 121.591 0.01 1 251 90 110 HIS H H 7.243 0.00 1 252 90 110 HIS CA C 54.431 0.01 1 253 90 110 HIS N N 107.196 0.03 1 254 91 111 ALA H H 8.331 0.00 1 255 91 111 ALA CA C 51.439 0.00 1 256 91 111 ALA N N 120.008 0.02 1 257 92 112 GLU H H 8.336 0.01 1 258 92 112 GLU CA C 53.984 0.02 1 259 92 112 GLU N N 122.019 0.04 1 260 93 113 VAL H H 8.817 0.00 1 261 93 113 VAL CA C 61.196 0.01 1 262 93 113 VAL N N 122.289 0.04 1 263 94 114 VAL H H 9.120 0.00 1 264 94 114 VAL CA C 60.877 0.06 1 265 94 114 VAL N N 128.316 0.00 1 266 95 115 PHE H H 8.897 0.00 1 267 95 115 PHE CA C 55.639 0.00 1 268 95 115 PHE N N 124.811 0.04 1 269 96 116 THR H H 8.554 0.00 1 270 96 116 THR CA C 62.532 0.03 1 271 96 116 THR N N 118.407 0.05 1 272 97 117 ALA H H 9.057 0.00 1 273 97 117 ALA CA C 49.736 0.00 1 274 97 117 ALA N N 129.861 0.02 1 275 98 118 ASN CA C 53.646 0.00 1 276 99 119 ASP H H 8.854 0.00 1 277 99 119 ASP CA C 54.803 0.02 1 278 99 119 ASP N N 118.247 0.02 1 279 100 120 SER H H 8.714 0.00 1 280 100 120 SER CA C 56.984 0.00 1 281 100 120 SER N N 117.755 0.08 1 282 102 122 PRO CA C 63.297 0.00 1 283 103 123 ARG H H 8.243 0.00 1 284 103 123 ARG CA C 53.565 0.07 1 285 103 123 ARG N N 122.942 0.02 1 286 104 124 ARG H H 8.017 0.00 1 287 104 124 ARG CA C 54.238 0.02 1 288 104 124 ARG N N 118.005 0.04 1 289 105 125 TYR H H 8.800 0.00 1 290 105 125 TYR CA C 57.125 0.00 1 291 105 125 TYR N N 121.998 0.07 1 292 106 126 THR H H 8.648 0.00 1 293 106 126 THR CA C 61.570 0.00 1 294 106 126 THR N N 120.792 0.01 1 295 107 127 ILE H H 8.740 0.00 1 296 107 127 ILE CA C 58.127 0.02 1 297 107 127 ILE N N 127.772 0.01 1 298 108 128 ALA H H 8.700 0.00 1 299 108 128 ALA CA C 48.906 0.02 1 300 108 128 ALA N N 129.130 0.03 1 301 109 129 ALA H H 8.991 0.00 1 302 109 129 ALA CA C 49.925 0.02 1 303 109 129 ALA N N 126.307 0.04 1 304 110 130 LEU H H 8.707 0.00 1 305 110 130 LEU CA C 53.585 0.02 1 306 110 130 LEU N N 126.605 0.04 1 307 111 131 LEU H H 9.004 0.00 1 308 111 131 LEU CA C 55.220 0.00 1 309 111 131 LEU N N 124.416 0.01 1 310 112 132 SER H H 8.955 0.00 1 311 112 132 SER CA C 57.776 0.00 1 312 112 132 SER N N 117.090 0.01 1 313 114 134 TYR H H 8.050 0.00 1 314 114 134 TYR CA C 57.867 0.03 1 315 114 134 TYR N N 113.655 0.06 1 316 115 135 SER H H 7.333 0.00 1 317 115 135 SER CA C 57.052 0.02 1 318 115 135 SER N N 112.344 0.01 1 319 116 136 TYR H H 8.312 0.00 1 320 116 136 TYR CA C 56.798 0.02 1 321 116 136 TYR N N 120.251 0.02 1 322 117 137 SER H H 8.341 0.00 1 323 117 137 SER CA C 54.904 0.02 1 324 117 137 SER N N 114.181 0.02 1 325 118 138 THR H H 8.764 0.00 1 326 118 138 THR CA C 58.465 0.03 1 327 118 138 THR N N 116.435 0.01 1 328 119 139 THR H H 8.264 0.00 1 329 119 139 THR CA C 60.919 0.02 1 330 119 139 THR N N 122.457 0.03 1 331 120 140 ALA H H 8.229 0.01 1 332 120 140 ALA CA C 49.529 0.00 1 333 120 140 ALA N N 129.224 0.05 1 334 121 141 VAL H H 8.148 0.00 1 335 121 141 VAL CA C 60.054 0.00 1 336 121 141 VAL N N 118.766 0.03 1 337 122 142 ILE H H 8.260 0.00 1 338 122 142 ILE CA C 59.584 0.01 1 339 122 142 ILE N N 129.227 0.02 1 340 123 143 THR H H 8.538 0.00 1 341 123 143 THR CA C 59.808 0.02 1 342 123 143 THR N N 119.187 0.03 1 343 124 144 ASN H H 8.631 0.00 1 344 124 144 ASN CA C 50.133 0.00 1 345 124 144 ASN N N 121.397 0.01 1 346 125 145 PRO CA C 63.007 0.00 1 347 126 146 LYS H H 8.032 0.00 1 348 126 146 LYS CA C 55.722 0.01 1 349 126 146 LYS N N 121.105 0.00 1 350 127 147 GLU H H 7.661 0.00 1 351 127 147 GLU CA C 57.575 0.00 1 352 127 147 GLU N N 127.209 0.01 1 stop_ save_