data_27515 ####################### # 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 27515 _BMRB_flat_file_name bmr27515.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 'Chemical shift assignments for teh V30M mutant of Transthyretin' 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_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 118 "13C chemical shifts" 224 "15N chemical shifts" 118 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' 27516 'V122I 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 V30M mutant stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name V30M _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'V30M Transthyretin' $Transthyretin_V30M 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_V30M _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Transthyretin_V30M _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 147 _Mol_residue_sequence ; MASHRLLLLCLAGLVFVSEA GPTGTGESKCPLMVKVLDAV RGSPAINVAMHVFRKAADDT WEPFASGKTSESGELHGLTT EEEFVEGIYKVEIDTKSYWK ALGISPFHEHAEVVFTANDS GPRRYTIAALLSPYSYSTTA VVTNPKE ; 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 MET 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 VAL 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_V30M 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_V30M '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 13C/15N ~70% 2H transthyretin' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'sodium phosphate' 10 mM 'natural abundance' 'potassium chloride' 100 mM 'natural abundance' transthyretin 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_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' 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 'V30M 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 62.939 0.00 1 2 3 23 THR H H 8.181 0.00 1 3 3 23 THR CA C 61.594 0.02 1 4 3 23 THR CB C 69.415 0.00 1 5 3 23 THR N N 114.149 0.03 1 6 4 24 GLY H H 8.267 0.00 1 7 4 24 GLY CA C 44.966 0.00 1 8 4 24 GLY N N 111.470 0.02 1 9 5 25 THR H H 8.043 0.00 1 10 5 25 THR CA C 61.619 0.05 1 11 5 25 THR CB C 69.535 0.41 1 12 5 25 THR N N 113.475 0.01 1 13 6 26 GLY H H 8.352 0.00 1 14 6 26 GLY CA C 44.915 0.00 1 15 6 26 GLY N N 111.415 0.11 1 16 7 27 GLU H H 8.119 0.00 1 17 7 27 GLU CA C 56.070 0.01 1 18 7 27 GLU CB C 29.578 0.01 1 19 7 27 GLU N N 121.104 0.01 1 20 8 28 SER H H 8.261 0.00 1 21 8 28 SER CA C 58.120 0.01 1 22 8 28 SER CB C 63.179 0.06 1 23 8 28 SER N N 117.516 0.04 1 24 9 29 LYS H H 8.351 0.00 1 25 9 29 LYS CA C 55.321 0.08 1 26 9 29 LYS CB C 31.985 0.00 1 27 9 29 LYS N N 123.711 0.04 1 28 10 30 CYS H H 8.178 0.00 1 29 10 30 CYS N N 122.743 0.00 1 30 11 31 PRO CA C 63.944 0.00 1 31 11 31 PRO CB C 32.147 0.00 1 32 12 32 LEU H H 6.906 0.00 1 33 12 32 LEU CA C 53.499 0.01 1 34 12 32 LEU CB C 43.385 0.01 1 35 12 32 LEU N N 121.006 0.00 1 36 13 33 MET H H 8.508 0.00 1 37 13 33 MET CA C 54.244 0.01 1 38 13 33 MET CB C 34.442 0.01 1 39 13 33 MET N N 127.120 0.01 1 40 14 34 VAL H H 7.445 0.00 1 41 14 34 VAL CA C 59.609 0.00 1 42 14 34 VAL CB C 33.785 0.01 1 43 14 34 VAL N N 122.239 0.02 1 44 15 35 LYS H H 8.769 0.00 1 45 15 35 LYS CA C 53.998 0.01 1 46 15 35 LYS CB C 35.154 0.01 1 47 15 35 LYS N N 127.277 0.02 1 48 16 36 VAL H H 8.954 0.00 1 49 16 36 VAL CA C 60.108 0.01 1 50 16 36 VAL CB C 32.409 0.01 1 51 16 36 VAL N N 124.200 0.02 1 52 17 37 LEU H H 8.500 0.00 1 53 17 37 LEU CA C 53.395 0.02 1 54 17 37 LEU CB C 44.817 0.04 1 55 17 37 LEU N N 126.836 0.03 1 56 18 38 ASP H H 8.585 0.00 1 57 18 38 ASP CA C 52.788 0.01 1 58 18 38 ASP CB C 41.194 0.00 1 59 18 38 ASP N N 121.948 0.02 1 60 19 39 ALA H H 8.977 0.00 1 61 19 39 ALA CA C 53.212 0.06 1 62 19 39 ALA CB C 18.482 0.00 1 63 19 39 ALA N N 127.911 0.04 1 64 20 40 VAL H H 9.597 0.00 1 65 20 40 VAL CA C 65.204 0.05 1 66 20 40 VAL CB C 30.807 0.05 1 67 20 40 VAL N N 120.888 0.00 1 68 21 41 ARG H H 8.200 0.01 1 69 21 41 ARG CA C 55.153 0.01 1 70 21 41 ARG CB C 30.857 0.00 1 71 21 41 ARG N N 117.063 0.05 1 72 22 42 GLY H H 7.467 0.00 1 73 22 42 GLY CA C 46.834 0.00 1 74 22 42 GLY N N 110.105 0.05 1 75 23 43 SER H H 7.297 0.00 1 76 23 43 SER CA C 54.866 0.00 1 77 23 43 SER CB C 66.096 0.00 1 78 23 43 SER N N 111.984 0.04 1 79 24 44 PRO CA C 62.536 0.00 1 80 24 44 PRO CB C 30.454 0.00 1 81 25 45 ALA H H 8.023 0.00 1 82 25 45 ALA CA C 50.316 0.00 1 83 25 45 ALA CB C 17.371 0.05 1 84 25 45 ALA N N 127.752 0.02 1 85 26 46 ILE H H 7.886 0.00 1 86 26 46 ILE CA C 61.392 0.02 1 87 26 46 ILE CB C 38.658 0.00 1 88 26 46 ILE N N 127.668 0.02 1 89 27 47 ASN H H 7.611 0.00 1 90 27 47 ASN CA C 54.128 0.02 1 91 27 47 ASN CB C 36.535 0.03 1 92 27 47 ASN N N 122.390 0.02 1 93 28 48 VAL H H 8.353 0.00 1 94 28 48 VAL CA C 61.802 0.01 1 95 28 48 VAL CB C 30.307 0.02 1 96 28 48 VAL N N 120.452 0.04 1 97 29 49 ALA H H 9.112 0.00 1 98 29 49 ALA CA C 51.560 0.01 1 99 29 49 ALA CB C 19.427 0.03 1 100 29 49 ALA N N 131.958 0.03 1 101 30 50 MET H H 8.459 0.00 1 102 30 50 MET CA C 53.751 0.01 1 103 30 50 MET CB C 36.307 0.00 1 104 30 50 MET N N 116.630 0.03 1 105 31 51 HIS H H 8.501 0.00 1 106 31 51 HIS CA C 55.162 0.00 1 107 31 51 HIS CB C 33.294 0.00 1 108 31 51 HIS N N 119.593 0.02 1 109 32 52 VAL H H 9.135 0.00 1 110 32 52 VAL CA C 59.470 0.01 1 111 32 52 VAL CB C 32.034 0.03 1 112 32 52 VAL N N 122.064 0.02 1 113 33 53 PHE H H 9.869 0.00 1 114 33 53 PHE CA C 55.864 0.00 1 115 33 53 PHE CB C 44.124 0.09 1 116 33 53 PHE N N 128.290 0.04 1 117 34 54 ARG H H 9.382 0.00 1 118 34 54 ARG CA C 53.786 0.00 1 119 34 54 ARG CB C 33.159 0.01 1 120 34 54 ARG N N 122.690 0.00 1 121 35 55 LYS H H 8.585 0.00 1 122 35 55 LYS CA C 56.966 0.00 1 123 35 55 LYS CB C 31.141 0.01 1 124 35 55 LYS N N 130.717 0.00 1 125 36 56 ALA H H 8.772 0.00 1 126 36 56 ALA CA C 50.605 0.01 1 127 36 56 ALA CB C 19.868 0.03 1 128 36 56 ALA N N 131.741 0.02 1 129 37 57 ALA H H 8.349 0.00 1 130 37 57 ALA CA C 53.787 0.03 1 131 37 57 ALA CB C 17.606 0.01 1 132 37 57 ALA N N 122.758 0.03 1 133 38 58 ASP H H 7.627 0.00 1 134 38 58 ASP CA C 52.780 0.01 1 135 38 58 ASP CB C 38.896 0.04 1 136 38 58 ASP N N 116.078 0.03 1 137 39 59 ASP H H 7.842 0.00 1 138 39 59 ASP CA C 55.834 0.01 1 139 39 59 ASP CB C 38.431 0.04 1 140 39 59 ASP N N 113.334 0.02 1 141 40 60 THR H H 7.188 0.00 1 142 40 60 THR CA C 61.088 0.00 1 143 40 60 THR CB C 70.457 0.06 1 144 40 60 THR N N 111.015 0.02 1 145 41 61 TRP H H 8.344 0.00 1 146 41 61 TRP HE1 H 9.845 0.00 1 147 41 61 TRP CA C 55.315 0.01 1 148 41 61 TRP CB C 29.643 0.04 1 149 41 61 TRP N N 120.437 0.03 1 150 41 61 TRP NE1 N 129.405 0.00 1 151 42 62 GLU H H 9.175 0.00 1 152 42 62 GLU CA C 52.836 0.00 1 153 42 62 GLU CB C 30.781 0.00 1 154 42 62 GLU N N 127.239 0.00 1 155 43 63 PRO CA C 64.385 0.00 1 156 43 63 PRO CB C 31.274 0.00 1 157 44 64 PHE H H 8.808 0.00 1 158 44 64 PHE CA C 58.817 0.01 1 159 44 64 PHE CB C 41.993 0.07 1 160 44 64 PHE N N 125.122 0.04 1 161 45 65 ALA H H 7.843 0.00 1 162 45 65 ALA CA C 52.009 0.00 1 163 45 65 ALA CB C 22.454 0.02 1 164 45 65 ALA N N 119.281 0.02 1 165 46 66 SER H H 8.475 0.00 1 166 46 66 SER CA C 57.601 0.00 1 167 46 66 SER CB C 65.388 0.00 1 168 46 66 SER N N 113.683 0.04 1 169 47 67 GLY H H 7.935 0.00 1 170 47 67 GLY CA C 45.407 0.01 1 171 47 67 GLY N N 106.046 0.00 1 172 48 68 LYS H H 8.359 0.00 1 173 48 68 LYS CA C 53.316 0.01 1 174 48 68 LYS CB C 35.325 0.01 1 175 48 68 LYS N N 119.254 0.01 1 176 49 69 THR H H 8.411 0.00 1 177 49 69 THR CA C 61.624 0.01 1 178 49 69 THR CB C 69.983 0.00 1 179 49 69 THR N N 111.407 0.00 1 180 50 70 SER H H 8.405 0.00 1 181 50 70 SER CA C 56.757 0.00 1 182 50 70 SER CB C 65.146 0.11 1 183 50 70 SER N N 118.237 0.04 1 184 51 71 GLU H H 8.992 0.00 1 185 51 71 GLU CA C 58.745 0.01 1 186 51 71 GLU CB C 28.071 0.00 1 187 51 71 GLU N N 118.887 0.02 1 188 52 72 SER H H 8.015 0.00 1 189 52 72 SER CA C 57.331 0.01 1 190 52 72 SER N N 112.118 0.01 1 191 53 73 GLY H H 8.441 0.00 1 192 53 73 GLY CA C 45.180 0.02 1 193 53 73 GLY N N 112.281 0.00 1 194 54 74 GLU H H 7.051 0.00 1 195 54 74 GLU CA C 53.877 0.04 1 196 54 74 GLU CB C 32.268 0.02 1 197 54 74 GLU N N 116.145 0.01 1 198 55 75 LEU H H 8.503 0.00 1 199 55 75 LEU CB C 42.591 0.00 1 200 55 75 LEU N N 123.992 0.00 1 201 57 77 GLY H H 8.119 0.00 1 202 57 77 GLY CA C 46.200 0.03 1 203 57 77 GLY N N 108.957 0.00 1 204 58 78 LEU H H 8.263 0.00 1 205 58 78 LEU CA C 57.020 0.02 1 206 58 78 LEU CB C 42.559 0.03 1 207 58 78 LEU N N 120.341 0.03 1 208 59 79 THR H H 7.171 0.00 1 209 59 79 THR CA C 59.206 0.03 1 210 59 79 THR CB C 67.646 0.00 1 211 59 79 THR N N 108.138 0.00 1 212 60 80 THR H H 8.385 0.00 1 213 60 80 THR CA C 59.394 0.00 1 214 60 80 THR CB C 71.912 0.04 1 215 60 80 THR N N 112.526 0.01 1 216 61 81 GLU H H 8.987 0.00 1 217 61 81 GLU CA C 59.638 0.01 1 218 61 81 GLU CB C 29.159 0.00 1 219 61 81 GLU N N 121.355 0.00 1 220 62 82 GLU H H 8.568 0.00 1 221 62 82 GLU CA C 58.699 0.03 1 222 62 82 GLU CB C 28.772 0.00 1 223 62 82 GLU N N 116.686 0.01 1 224 63 83 GLU H H 7.231 0.00 1 225 63 83 GLU CA C 56.650 0.03 1 226 63 83 GLU CB C 30.487 0.08 1 227 63 83 GLU N N 116.077 0.05 1 228 64 84 PHE H H 7.767 0.01 1 229 64 84 PHE CA C 54.657 0.01 1 230 64 84 PHE CB C 36.734 0.04 1 231 64 84 PHE N N 124.317 0.02 1 232 65 85 VAL H H 7.067 0.00 1 233 65 85 VAL CA C 59.867 0.01 1 234 65 85 VAL CB C 31.166 1.80 1 235 65 85 VAL N N 115.546 0.03 1 236 66 86 GLU H H 8.529 0.00 1 237 66 86 GLU CA C 56.427 0.02 1 238 66 86 GLU N N 122.132 0.00 1 239 67 87 GLY H H 7.851 0.00 1 240 67 87 GLY CA C 44.303 0.00 1 241 67 87 GLY N N 111.747 0.01 1 242 68 88 ILE H H 8.270 0.00 1 243 68 88 ILE CA C 60.564 0.01 1 244 68 88 ILE CB C 37.680 0.07 1 245 68 88 ILE N N 120.851 0.01 1 246 69 89 TYR H H 8.564 0.00 1 247 69 89 TYR CA C 55.996 0.01 1 248 69 89 TYR CB C 41.371 0.04 1 249 69 89 TYR N N 125.430 0.02 1 250 70 90 LYS H H 8.605 0.00 1 251 70 90 LYS CA C 53.114 0.01 1 252 70 90 LYS CB C 35.193 0.00 1 253 70 90 LYS N N 118.580 0.03 1 254 71 91 VAL H H 9.495 0.00 1 255 71 91 VAL CA C 60.572 0.00 1 256 71 91 VAL CB C 32.455 0.02 1 257 71 91 VAL N N 127.338 0.02 1 258 72 92 GLU H H 9.421 0.00 1 259 72 92 GLU CA C 55.032 0.01 1 260 72 92 GLU CB C 31.674 0.02 1 261 72 92 GLU N N 127.955 0.00 1 262 73 93 ILE H H 9.300 0.00 1 263 73 93 ILE CA C 60.436 0.00 1 264 73 93 ILE CB C 38.684 0.02 1 265 73 93 ILE N N 126.715 0.04 1 266 74 94 ASP H H 8.924 0.00 1 267 74 94 ASP CA C 52.952 0.03 1 268 74 94 ASP CB C 37.566 0.05 1 269 74 94 ASP N N 128.627 0.00 1 270 75 95 THR H H 8.211 0.00 1 271 75 95 THR CA C 64.175 0.01 1 272 75 95 THR CB C 65.658 0.03 1 273 75 95 THR N N 117.527 0.04 1 274 76 96 LYS H H 7.474 0.00 1 275 76 96 LYS CA C 60.049 0.01 1 276 76 96 LYS CB C 32.182 0.15 1 277 76 96 LYS N N 124.882 0.02 1 278 77 97 SER H H 8.133 0.00 1 279 77 97 SER CA C 61.537 0.02 1 280 77 97 SER N N 113.559 0.00 1 281 78 98 TYR H H 6.661 0.00 1 282 78 98 TYR CA C 60.810 0.01 1 283 78 98 TYR CB C 36.772 0.00 1 284 78 98 TYR N N 121.695 0.00 1 285 79 99 TRP H H 7.688 0.00 1 286 79 99 TRP HE1 H 10.269 0.00 1 287 79 99 TRP CA C 59.045 0.11 1 288 79 99 TRP N N 118.073 0.04 1 289 79 99 TRP NE1 N 127.518 0.00 1 290 80 100 LYS H H 8.768 0.00 1 291 80 100 LYS CA C 59.229 0.00 1 292 80 100 LYS CB C 30.538 0.04 1 293 80 100 LYS N N 119.211 0.03 1 294 81 101 ALA H H 7.473 0.00 1 295 81 101 ALA CA C 54.064 0.02 1 296 81 101 ALA CB C 16.911 0.04 1 297 81 101 ALA N N 122.551 0.03 1 298 82 102 LEU H H 7.208 0.00 1 299 82 102 LEU CA C 54.018 0.00 1 300 82 102 LEU CB C 41.608 0.07 1 301 82 102 LEU N N 118.002 0.01 1 302 83 103 GLY H H 7.882 0.00 1 303 83 103 GLY CA C 45.190 0.01 1 304 83 103 GLY N N 108.066 0.04 1 305 84 104 ILE H H 7.874 0.00 1 306 84 104 ILE CA C 59.365 0.01 1 307 84 104 ILE CB C 40.249 0.01 1 308 84 104 ILE N N 123.456 0.01 1 309 85 105 SER H H 8.408 0.00 1 310 85 105 SER CA C 54.421 0.00 1 311 85 105 SER CB C 62.587 0.00 1 312 85 105 SER N N 122.371 0.01 1 313 86 106 PRO CA C 61.107 0.00 1 314 87 107 PHE H H 7.266 0.00 1 315 87 107 PHE CA C 59.888 0.00 1 316 87 107 PHE CB C 40.045 0.00 1 317 87 107 PHE N N 116.064 0.02 1 318 88 108 HIS H H 7.694 0.00 1 319 88 108 HIS CA C 57.739 0.01 1 320 88 108 HIS CB C 33.456 0.00 1 321 88 108 HIS N N 114.362 0.00 1 322 89 109 GLU H H 8.971 0.00 1 323 89 109 GLU CA C 57.736 0.00 1 324 89 109 GLU CB C 30.505 0.02 1 325 89 109 GLU N N 122.367 0.03 1 326 90 110 HIS H H 7.176 0.00 1 327 90 110 HIS CA C 54.630 0.01 1 328 90 110 HIS N N 107.321 0.00 1 329 91 111 ALA H H 8.425 0.00 1 330 91 111 ALA CA C 51.094 0.01 1 331 91 111 ALA CB C 19.725 0.05 1 332 91 111 ALA N N 120.464 0.04 1 333 92 112 GLU H H 8.680 0.00 1 334 92 112 GLU CA C 53.987 0.00 1 335 92 112 GLU CB C 31.958 0.00 1 336 92 112 GLU N N 122.641 0.06 1 337 93 113 VAL H H 8.646 0.00 1 338 93 113 VAL CA C 61.588 0.01 1 339 93 113 VAL CB C 33.773 0.07 1 340 93 113 VAL N N 121.220 0.02 1 341 94 114 VAL H H 9.224 0.00 1 342 94 114 VAL CA C 60.779 0.02 1 343 94 114 VAL CB C 32.642 0.01 1 344 94 114 VAL N N 128.750 0.00 1 345 95 115 PHE H H 9.019 0.00 1 346 95 115 PHE CA C 55.859 0.00 1 347 95 115 PHE CB C 41.022 0.10 1 348 95 115 PHE N N 124.943 0.00 1 349 96 116 THR H H 8.671 0.00 1 350 96 116 THR CA C 62.751 0.01 1 351 96 116 THR CB C 68.378 0.08 1 352 96 116 THR N N 119.042 0.00 1 353 97 117 ALA H H 9.118 0.00 1 354 97 117 ALA CA C 49.580 0.01 1 355 97 117 ALA CB C 23.206 0.00 1 356 97 117 ALA N N 130.078 0.00 1 357 98 118 ASN H H 8.610 0.00 1 358 98 118 ASN CA C 54.011 0.02 1 359 98 118 ASN N N 112.912 0.05 1 360 99 119 ASP H H 8.820 0.00 1 361 99 119 ASP CA C 55.155 0.00 1 362 99 119 ASP CB C 39.747 0.00 1 363 99 119 ASP N N 117.903 0.00 1 364 100 120 SER H H 8.815 0.00 1 365 100 120 SER CA C 56.944 0.00 1 366 100 120 SER CB C 62.805 0.00 1 367 100 120 SER N N 117.881 0.00 1 368 101 121 GLY H H 7.088 0.00 1 369 101 121 GLY CA C 43.203 0.00 1 370 101 121 GLY N N 110.551 0.00 1 371 102 122 PRO CA C 63.313 0.00 1 372 102 122 PRO CB C 31.243 0.00 1 373 103 123 ARG H H 8.316 0.00 1 374 103 123 ARG CA C 52.993 0.00 1 375 103 123 ARG CB C 33.006 0.03 1 376 103 123 ARG N N 123.370 0.00 1 377 104 124 ARG H H 8.074 0.00 1 378 104 124 ARG CA C 54.319 0.01 1 379 104 124 ARG CB C 30.202 0.07 1 380 104 124 ARG N N 117.371 0.02 1 381 105 125 TYR H H 8.776 0.00 1 382 105 125 TYR CA C 57.473 0.01 1 383 105 125 TYR CB C 40.945 0.02 1 384 105 125 TYR N N 121.946 0.02 1 385 106 126 THR H H 8.700 0.00 1 386 106 126 THR CA C 61.404 0.01 1 387 106 126 THR CB C 69.480 0.07 1 388 106 126 THR N N 121.162 0.02 1 389 107 127 ILE H H 8.797 0.00 1 390 107 127 ILE CA C 58.435 0.00 1 391 107 127 ILE CB C 38.520 0.10 1 392 107 127 ILE N N 128.176 0.01 1 393 108 128 ALA H H 8.800 0.00 1 394 108 128 ALA CA C 49.157 0.03 1 395 108 128 ALA CB C 19.579 0.02 1 396 108 128 ALA N N 129.160 0.06 1 397 109 129 ALA H H 9.046 0.00 1 398 109 129 ALA CA C 49.593 0.04 1 399 109 129 ALA CB C 20.180 0.01 1 400 109 129 ALA N N 127.228 0.00 1 401 110 130 LEU H H 8.765 0.00 1 402 110 130 LEU CA C 53.609 0.01 1 403 110 130 LEU CB C 42.978 0.09 1 404 110 130 LEU N N 126.591 0.02 1 405 111 131 LEU H H 8.991 0.00 1 406 111 131 LEU CA C 55.003 0.01 1 407 111 131 LEU CB C 43.366 0.01 1 408 111 131 LEU N N 124.101 0.01 1 409 112 132 SER H H 8.932 0.00 1 410 112 132 SER CA C 57.671 0.00 1 411 112 132 SER CB C 63.774 0.00 1 412 112 132 SER N N 117.373 0.05 1 413 113 133 PRO CA C 66.350 0.00 1 414 114 134 TYR H H 8.257 0.00 1 415 114 134 TYR CA C 57.802 0.03 1 416 114 134 TYR N N 114.169 0.03 1 417 115 135 SER H H 7.335 0.00 1 418 115 135 SER CA C 57.338 0.00 1 419 115 135 SER CB C 65.093 0.00 1 420 115 135 SER N N 112.223 0.00 1 421 117 137 SER H H 8.198 0.00 1 422 117 137 SER CA C 55.046 0.02 1 423 117 137 SER N N 115.304 0.00 1 424 118 138 THR H H 8.894 0.00 1 425 118 138 THR CA C 58.563 0.02 1 426 118 138 THR CB C 70.978 0.00 1 427 118 138 THR N N 116.790 0.00 1 428 119 139 THR H H 8.313 0.00 1 429 119 139 THR CA C 60.891 0.01 1 430 119 139 THR CB C 71.415 0.00 1 431 119 139 THR N N 122.224 0.03 1 432 120 140 ALA H H 8.246 0.00 1 433 120 140 ALA CA C 49.620 0.01 1 434 120 140 ALA CB C 19.848 0.07 1 435 120 140 ALA N N 128.757 0.03 1 436 121 141 VAL H H 8.195 0.00 1 437 121 141 VAL CA C 60.127 0.00 1 438 121 141 VAL CB C 33.077 0.01 1 439 121 141 VAL N N 119.328 0.00 1 440 122 142 VAL H H 8.183 0.00 1 441 122 142 VAL CA C 60.732 0.02 1 442 122 142 VAL CB C 32.833 0.01 1 443 122 142 VAL N N 128.877 0.02 1 444 123 143 THR H H 8.655 0.00 1 445 123 143 THR CA C 59.906 0.00 1 446 123 143 THR CB C 71.091 0.11 1 447 123 143 THR N N 119.989 0.04 1 448 124 144 ASN H H 8.659 0.00 1 449 124 144 ASN CA C 50.008 0.00 1 450 124 144 ASN CB C 37.969 0.00 1 451 124 144 ASN N N 121.446 0.00 1 452 125 145 PRO CA C 63.052 0.00 1 453 126 146 LYS H H 7.953 0.00 1 454 126 146 LYS CA C 55.694 0.01 1 455 126 146 LYS CB C 31.899 0.08 1 456 126 146 LYS N N 120.741 0.01 1 457 127 147 GLU H H 7.615 0.00 1 458 127 147 GLU CA C 57.599 0.00 1 459 127 147 GLU CB C 30.290 0.00 1 460 127 147 GLU N N 127.210 0.01 1 stop_ save_