data_27992 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; MYB28 116-197 chemical shifts ; _BMRB_accession_number 27992 _BMRB_flat_file_name bmr27992.str _Entry_type original _Submission_date 2019-08-02 _Accession_date 2019-08-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Chemical shifts of residues 116 to 197 of MYB28 from Arabidopsis thaliana' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Millard Peter S. . 2 Bugge Katrine . . 3 Kragelund Birthe B. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 61 "13C chemical shifts" 190 "15N chemical shifts" 63 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-02-05 update BMRB 'update entry citation' 2019-10-29 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27993 'MYB29 residues 118-178' stop_ _Original_release_date 2019-08-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions - insights from transcription factors ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31642121 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Millard Peter S. . 2 Bugge Katrine . . 3 Marabini Riccardo . . 4 Boomsma Wouter K. . 5 Burow Meike . . 6 Kragelund Birthe B. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 29 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 169 _Page_last 183 _Year 2020 _Details . loop_ _Keyword 'DNA-binding domain' IDDomainSpotter IDPs NMR 'compositional bias' domain 'low-complexity regions' p53 'plant MYB protein' 'transactivation domain' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'MYB28 residues 116-197' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'MYB28 residues 116-197' $MYB28_residues_116-197 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_MYB28_residues_116-197 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MYB28_residues_116-197 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 82 _Mol_residue_sequence ; SMEQGIDPVTHKPLASSSNP TVDENLNSPNASSSDKQYSR SSSMPFLSRPPPSSCNMVSK VSELSSNDGTPIQGSSLSCK KR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 116 SER 2 117 MET 3 118 GLU 4 119 GLN 5 120 GLY 6 121 ILE 7 122 ASP 8 123 PRO 9 124 VAL 10 125 THR 11 126 HIS 12 127 LYS 13 128 PRO 14 129 LEU 15 130 ALA 16 131 SER 17 132 SER 18 133 SER 19 134 ASN 20 135 PRO 21 136 THR 22 137 VAL 23 138 ASP 24 139 GLU 25 140 ASN 26 141 LEU 27 142 ASN 28 143 SER 29 144 PRO 30 145 ASN 31 146 ALA 32 147 SER 33 148 SER 34 149 SER 35 150 ASP 36 151 LYS 37 152 GLN 38 153 TYR 39 154 SER 40 155 ARG 41 156 SER 42 157 SER 43 158 SER 44 159 MET 45 160 PRO 46 161 PHE 47 162 LEU 48 163 SER 49 164 ARG 50 165 PRO 51 166 PRO 52 167 PRO 53 168 SER 54 169 SER 55 170 CYS 56 171 ASN 57 172 MET 58 173 VAL 59 174 SER 60 175 LYS 61 176 VAL 62 177 SER 63 178 GLU 64 179 LEU 65 180 SER 66 181 SER 67 182 ASN 68 183 ASP 69 184 GLY 70 185 THR 71 186 PRO 72 187 ILE 73 188 GLN 74 189 GLY 75 190 SER 76 191 SER 77 192 LEU 78 193 SER 79 194 CYS 80 195 LYS 81 196 LYS 82 197 ARG 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 _Gene_mnemonic $MYB28_residues_116-197 'Thale cress' 3702 Eukaryota Viridiplantae Arabidopsis thaliana AT5G61420 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 $MYB28_residues_116-197 'recombinant technology' . Escherichia coli . pGEX-4T-1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1_MYB28_116-197 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling DSS 1 mM 'natural abundance' TCEP 100 uM 'natural abundance' 'sodium azide' 0.03 '% v/v' 'natural abundance' 'sodium phosphate' 50 mM 'natural abundance' $MYB28_residues_116-197 350 uM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CcpNmr _Saveframe_category software _Name CcpNmr _Version . loop_ _Vendor _Address _Electronic_address CCPN . . 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 III' _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_MYB28_116-197 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1_MYB28_116-197 save_ save_3D_HNCOCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCOCACB' _Sample_label $sample_1_MYB28_116-197 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1_MYB28_116-197 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1_MYB28_116-197 save_ save_HN(CA)NNH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)NNH _Sample_label $sample_1_MYB28_116-197 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . 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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 HNCACB' '3D HNCOCACB' '3D HN(CO)CA' '3D HNCO' HN(CA)NNH stop_ loop_ _Sample_label $sample_1_MYB28_116-197 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'MYB28 residues 116-197' _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 1 116 1 SER C C 171.986 0.013 1 2 116 1 SER CA C 58.358 0.000 1 3 116 1 SER CB C 63.554 0.000 1 4 117 2 MET H H 8.764 0.001 1 5 117 2 MET C C 173.620 0.007 1 6 117 2 MET CA C 55.661 0.060 1 7 117 2 MET CB C 32.333 0.026 1 8 117 2 MET N N 122.472 0.011 1 9 118 3 GLU H H 8.554 0.001 1 10 118 3 GLU C C 173.557 0.015 1 11 118 3 GLU CA C 56.981 0.000 1 12 118 3 GLU CB C 29.869 0.008 1 13 118 3 GLU N N 122.249 0.015 1 14 119 4 GLN H H 8.500 0.001 1 15 119 4 GLN C C 173.522 0.007 1 16 119 4 GLN CA C 55.836 0.014 1 17 119 4 GLN CB C 29.441 0.043 1 18 119 4 GLN N N 121.409 0.015 1 19 120 5 GLY H H 8.593 0.001 1 20 120 5 GLY C C 170.773 0.001 1 21 120 5 GLY CA C 45.232 0.089 1 22 120 5 GLY N N 110.173 0.014 1 23 121 6 ILE H H 8.067 0.001 1 24 121 6 ILE C C 172.899 0.020 1 25 121 6 ILE CA C 59.916 0.007 1 26 121 6 ILE CB C 39.267 0.112 1 27 121 6 ILE N N 119.569 0.016 1 28 122 7 ASP H H 8.667 0.001 1 29 122 7 ASP C C 172.132 0.000 1 30 122 7 ASP CA C 52.448 0.000 1 31 122 7 ASP CB C 41.714 0.000 1 32 122 7 ASP N N 127.875 0.019 1 33 128 13 PRO C C 174.124 0.012 1 34 128 13 PRO CA C 62.921 0.035 1 35 128 13 PRO CB C 31.875 0.000 1 36 128 13 PRO N N 130.118 0.000 1 37 129 14 LEU H H 8.430 0.004 1 38 129 14 LEU C C 174.456 0.017 1 39 129 14 LEU CA C 55.037 0.000 1 40 129 14 LEU CB C 42.321 0.048 1 41 129 14 LEU N N 123.848 0.035 1 42 130 15 ALA H H 8.536 0.001 1 43 130 15 ALA C C 174.824 0.005 1 44 130 15 ALA CA C 52.535 0.026 1 45 130 15 ALA CB C 19.074 0.000 1 46 130 15 ALA N N 125.351 0.020 1 47 131 16 SER H H 8.449 0.003 1 48 131 16 SER C C 171.914 0.000 1 49 131 16 SER CA C 58.433 0.000 1 50 131 16 SER CB C 63.840 0.000 1 51 131 16 SER N N 115.473 0.026 1 52 132 17 SER H H 8.520 0.000 1 53 132 17 SER C C 171.618 0.000 1 54 132 17 SER N N 118.107 0.021 1 55 133 18 SER H H 8.441 0.002 1 56 133 18 SER C C 170.878 0.009 1 57 133 18 SER N N 117.691 0.038 1 58 134 19 ASN H H 8.505 0.001 1 59 134 19 ASN C C 170.056 0.000 1 60 134 19 ASN N N 121.585 0.026 1 61 135 20 PRO C C 174.157 0.007 1 62 135 20 PRO CA C 63.382 0.000 1 63 135 20 PRO CB C 32.103 0.061 1 64 136 21 THR H H 8.423 0.001 1 65 136 21 THR C C 171.736 0.005 1 66 136 21 THR CA C 62.159 0.023 1 67 136 21 THR CB C 69.719 0.033 1 68 136 21 THR N N 115.370 0.017 1 69 137 22 VAL H H 8.267 0.001 1 70 137 22 VAL C C 172.724 0.012 1 71 137 22 VAL CA C 62.118 0.034 1 72 137 22 VAL CB C 32.958 0.064 1 73 137 22 VAL N N 122.976 0.021 1 74 138 23 ASP H H 8.494 0.002 1 75 138 23 ASP C C 173.647 0.015 1 76 138 23 ASP CA C 54.261 0.006 1 77 138 23 ASP CB C 40.964 0.048 1 78 138 23 ASP N N 124.494 0.021 1 79 139 24 GLU H H 8.642 0.001 1 80 139 24 GLU C C 173.599 0.005 1 81 139 24 GLU CA C 57.025 0.099 1 82 139 24 GLU CB C 29.973 0.041 1 83 139 24 GLU N N 123.096 0.020 1 84 140 25 ASN H H 8.628 0.001 1 85 140 25 ASN C C 172.598 0.016 1 86 140 25 ASN CA C 53.612 0.000 1 87 140 25 ASN CB C 38.513 0.002 1 88 140 25 ASN N N 118.954 0.022 1 89 141 26 LEU H H 8.155 0.001 1 90 141 26 LEU C C 174.404 0.010 1 91 141 26 LEU CA C 55.656 0.000 1 92 141 26 LEU CB C 41.847 0.077 1 93 141 26 LEU N N 121.964 0.013 1 94 142 27 ASN H H 8.419 0.001 1 95 142 27 ASN C C 171.975 0.015 1 96 142 27 ASN CA C 53.079 0.035 1 97 142 27 ASN CB C 38.805 0.086 1 98 142 27 ASN N N 118.415 0.024 1 99 143 28 SER H H 8.206 0.001 1 100 143 28 SER C C 170.064 0.000 1 101 143 28 SER CA C 56.527 0.000 1 102 143 28 SER CB C 63.189 0.000 1 103 143 28 SER N N 117.046 0.020 1 104 144 29 PRO C C 173.873 0.035 1 105 144 29 PRO CA C 63.490 0.000 1 106 144 29 PRO CB C 31.737 0.000 1 107 145 30 ASN H H 8.555 0.002 1 108 145 30 ASN C C 172.232 0.019 1 109 145 30 ASN CA C 53.069 0.027 1 110 145 30 ASN CB C 38.719 0.094 1 111 145 30 ASN N N 118.453 0.058 1 112 146 31 ALA H H 8.331 0.002 1 113 146 31 ALA C C 175.007 0.004 1 114 146 31 ALA CA C 52.840 0.032 1 115 146 31 ALA CB C 19.029 0.038 1 116 146 31 ALA N N 124.849 0.016 1 117 147 32 SER H H 8.499 0.002 1 118 147 32 SER C C 172.002 0.001 1 119 147 32 SER CA C 58.494 0.000 1 120 147 32 SER CB C 63.836 0.000 1 121 147 32 SER N N 115.252 0.025 1 122 148 33 SER H H 8.463 0.001 1 123 148 33 SER C C 172.049 0.000 1 124 148 33 SER CA C 58.197 0.000 1 125 148 33 SER CB C 63.542 0.000 1 126 148 33 SER N N 117.984 0.030 1 127 149 34 SER H H 8.462 0.001 1 128 149 34 SER C C 171.544 0.008 1 129 149 34 SER CA C 58.611 0.095 1 130 149 34 SER CB C 63.580 0.097 1 131 149 34 SER N N 117.884 0.042 1 132 150 35 ASP H H 8.361 0.001 1 133 150 35 ASP C C 173.629 0.018 1 134 150 35 ASP CA C 54.482 0.007 1 135 150 35 ASP CB C 40.797 0.054 1 136 150 35 ASP N N 122.483 0.025 1 137 151 36 LYS H H 8.293 0.002 1 138 151 36 LYS C C 173.728 0.034 1 139 151 36 LYS CA C 56.484 0.068 1 140 151 36 LYS CB C 32.518 0.024 1 141 151 36 LYS N N 121.795 0.041 1 142 152 37 GLN H H 8.399 0.003 1 143 152 37 GLN C C 172.860 0.018 1 144 152 37 GLN CA C 55.853 0.088 1 145 152 37 GLN CB C 29.055 0.098 1 146 152 37 GLN N N 120.797 0.046 1 147 153 38 TYR H H 8.264 0.001 1 148 153 38 TYR C C 172.890 0.009 1 149 153 38 TYR CA C 57.937 0.033 1 150 153 38 TYR CB C 38.720 0.067 1 151 153 38 TYR N N 121.133 0.017 1 152 154 39 SER H H 8.261 0.002 1 153 154 39 SER C C 171.186 0.002 1 154 154 39 SER CA C 58.269 0.000 1 155 154 39 SER CB C 63.753 0.082 1 156 154 39 SER N N 117.879 0.026 1 157 155 40 ARG H H 8.502 0.003 1 158 155 40 ARG C C 172.637 0.010 1 159 155 40 ARG CA C 55.949 0.078 1 160 155 40 ARG CB C 30.734 0.040 1 161 155 40 ARG N N 123.931 0.057 1 162 156 41 SER H H 8.130 0.001 1 163 156 41 SER N N 122.858 0.040 1 164 160 45 PRO C C 173.558 0.022 1 165 160 45 PRO CA C 63.002 0.000 1 166 161 46 PHE H H 8.433 0.002 1 167 161 46 PHE C C 172.668 0.026 1 168 161 46 PHE CA C 58.010 0.047 1 169 161 46 PHE CB C 39.278 0.000 1 170 161 46 PHE N N 120.871 0.045 1 171 162 47 LEU H H 8.220 0.009 1 172 162 47 LEU C C 173.738 0.014 1 173 162 47 LEU CA C 54.703 0.035 1 174 162 47 LEU CB C 42.399 0.017 1 175 162 47 LEU N N 124.645 0.121 1 176 163 48 SER H H 8.299 0.005 1 177 163 48 SER C C 171.008 0.002 1 178 163 48 SER CA C 58.458 0.000 1 179 163 48 SER CB C 63.540 0.070 1 180 163 48 SER N N 117.480 0.091 1 181 164 49 ARG H H 8.357 0.008 1 182 164 49 ARG C C 170.761 0.000 1 183 164 49 ARG CA C 53.995 0.000 1 184 164 49 ARG CB C 30.280 0.000 1 185 164 49 ARG N N 123.962 0.038 1 186 167 52 PRO C C 174.151 0.000 1 187 167 52 PRO CA C 62.866 0.078 1 188 167 52 PRO CB C 31.931 0.079 1 189 171 56 ASN C C 171.389 0.000 1 190 172 57 MET H H 8.557 0.001 1 191 172 57 MET C C 172.099 0.013 1 192 172 57 MET N N 121.369 0.012 1 193 173 58 VAL H H 8.423 0.001 1 194 173 58 VAL C C 173.289 0.004 1 195 173 58 VAL CA C 62.196 0.000 1 196 173 58 VAL CB C 32.620 0.000 1 197 173 58 VAL N N 121.368 0.017 1 198 174 59 SER H H 8.548 0.005 1 199 174 59 SER C C 171.474 0.022 1 200 174 59 SER CA C 58.465 0.000 1 201 174 59 SER CB C 63.751 0.000 1 202 174 59 SER N N 120.452 0.051 1 203 175 60 LYS H H 8.550 0.003 1 204 175 60 LYS C C 173.730 0.016 1 205 175 60 LYS CA C 56.263 0.003 1 206 175 60 LYS CB C 33.082 0.000 1 207 175 60 LYS N N 124.314 0.056 1 208 176 61 VAL H H 8.335 0.003 1 209 176 61 VAL C C 173.446 0.010 1 210 176 61 VAL CA C 62.486 0.076 1 211 176 61 VAL CB C 32.636 0.112 1 212 176 61 VAL N N 122.099 0.071 1 213 177 62 SER H H 8.522 0.002 1 214 177 62 SER C C 171.645 0.002 1 215 177 62 SER CA C 58.523 0.000 1 216 177 62 SER CB C 63.733 0.000 1 217 177 62 SER N N 119.871 0.047 1 218 178 63 GLU H H 8.612 0.002 1 219 178 63 GLU C C 173.526 0.001 1 220 178 63 GLU CA C 56.640 0.032 1 221 178 63 GLU CB C 30.114 0.096 1 222 178 63 GLU N N 123.554 0.024 1 223 179 64 LEU H H 8.374 0.001 1 224 179 64 LEU C C 174.616 0.010 1 225 179 64 LEU CA C 55.280 0.008 1 226 179 64 LEU CB C 42.207 0.033 1 227 179 64 LEU N N 122.930 0.032 1 228 180 65 SER H H 8.449 0.001 1 229 180 65 SER C C 171.741 0.034 1 230 180 65 SER CA C 58.024 0.000 1 231 180 65 SER CB C 63.766 0.073 1 232 180 65 SER N N 116.907 0.028 1 233 181 66 SER H H 8.524 0.001 1 234 181 66 SER C C 171.622 0.001 1 235 181 66 SER CA C 58.078 0.000 1 236 181 66 SER CB C 63.493 0.048 1 237 181 66 SER N N 118.038 0.042 1 238 182 67 ASN H H 8.636 0.001 1 239 182 67 ASN C C 172.195 0.002 1 240 182 67 ASN CA C 53.461 0.085 1 241 182 67 ASN CB C 38.856 0.071 1 242 182 67 ASN N N 120.893 0.023 1 243 183 68 ASP H H 8.343 0.001 1 244 183 68 ASP C C 173.846 0.027 1 245 183 68 ASP CA C 54.276 0.010 1 246 183 68 ASP CB C 40.823 0.047 1 247 183 68 ASP N N 120.550 0.018 1 248 184 69 GLY H H 8.423 0.002 1 249 184 69 GLY C C 171.312 0.000 1 250 184 69 GLY CA C 45.308 0.003 1 251 184 69 GLY N N 109.196 0.094 1 252 185 70 THR H H 8.175 0.001 1 253 185 70 THR C C 169.896 0.000 1 254 185 70 THR CA C 60.332 0.000 1 255 185 70 THR CB C 69.541 0.000 1 256 185 70 THR N N 117.508 0.040 1 257 186 71 PRO C C 174.039 0.007 1 258 186 71 PRO CA C 63.054 0.000 1 259 186 71 PRO CB C 32.019 0.000 1 260 186 71 PRO N N 122.445 0.000 1 261 187 72 ILE H H 8.460 0.005 1 262 187 72 ILE C C 173.632 0.009 1 263 187 72 ILE CA C 61.407 0.037 1 264 187 72 ILE CB C 38.457 0.012 1 265 187 72 ILE N N 122.344 0.043 1 266 188 73 GLN H H 8.693 0.003 1 267 188 73 GLN C C 173.519 0.005 1 268 188 73 GLN CA C 55.888 0.024 1 269 188 73 GLN CB C 29.235 0.066 1 270 188 73 GLN N N 125.700 0.096 1 271 189 74 GLY H H 8.669 0.002 1 272 189 74 GLY C C 171.231 0.023 1 273 189 74 GLY CA C 45.310 0.003 1 274 189 74 GLY N N 111.518 0.074 1 275 190 75 SER H H 8.396 0.005 1 276 190 75 SER C C 172.031 0.018 1 277 190 75 SER CA C 58.481 0.000 1 278 190 75 SER CB C 64.059 0.000 1 279 190 75 SER N N 115.713 0.055 1 280 191 76 SER H H 8.617 0.004 1 281 191 76 SER C C 171.926 0.029 1 282 191 76 SER CA C 58.578 0.000 1 283 191 76 SER CB C 63.708 0.000 1 284 191 76 SER N N 118.349 0.041 1 285 192 77 LEU H H 8.401 0.003 1 286 192 77 LEU C C 174.803 0.003 1 287 192 77 LEU CA C 55.563 0.000 1 288 192 77 LEU CB C 42.125 0.000 1 289 192 77 LEU N N 123.901 0.017 1 290 193 78 SER H H 8.353 0.001 1 291 193 78 SER C C 171.617 0.003 1 292 193 78 SER CA C 58.570 0.000 1 293 193 78 SER CB C 63.587 0.000 1 294 193 78 SER N N 116.270 0.039 1 295 194 79 CYS H H 8.380 0.003 1 296 194 79 CYS C C 171.549 0.002 1 297 194 79 CYS CA C 58.577 0.000 1 298 194 79 CYS CB C 27.913 0.000 1 299 194 79 CYS N N 121.527 0.015 1 300 195 80 LYS H H 8.438 0.002 1 301 195 80 LYS C C 173.439 0.000 1 302 195 80 LYS CA C 56.438 0.000 1 303 195 80 LYS CB C 32.966 0.050 1 304 195 80 LYS N N 124.305 0.046 1 305 196 81 LYS H H 8.518 0.001 1 306 196 81 LYS C C 172.730 0.013 1 307 196 81 LYS CA C 56.257 0.020 1 308 196 81 LYS CB C 32.953 0.016 1 309 196 81 LYS N N 124.310 0.018 1 310 197 82 ARG H H 8.179 0.001 1 311 197 82 ARG C C 173.566 0.000 1 312 197 82 ARG CA C 57.354 0.000 1 313 197 82 ARG CB C 31.314 0.000 1 314 197 82 ARG N N 128.522 0.091 1 stop_ save_