data_27408 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Axin RGS domain ; _BMRB_accession_number 27408 _BMRB_flat_file_name bmr27408.str _Entry_type original _Submission_date 2018-02-21 _Accession_date 2018-02-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone assignment of Axin RGS domain' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee Weontae . . 2 Yun Jihye . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 108 "13C chemical shifts" 216 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-11-14 update BMRB 'update entry citation' 2018-03-02 original author 'original release' stop_ _Original_release_date 2018-02-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Small-molecule binding of the axin RGS domain promotes beta-catenin and Ras degradation. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27294323 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cha Pu-Hyeon . . 2 Cho Yong-Hee . . 3 Lee Sang-Kyu . . 4 Lee JaeHeon . . 5 Jeong Woo-Jeong . . 6 Moon Byoung-San . . 7 Yun Jihye . . 8 Yang 'Jee Sun' . . 9 Choi Sooho . . 10 Soon Juyong . . 11 Kim Hyun-Yi . . 12 Kim Mi-Yeon . . 13 Kaduwal Saluja . . 14 Lee Weontae . . 15 Min 'Do Sik' . . 16 Kim Hoguen . . 17 Han Gyoonhee . . 18 Choi Kang-Yell . . stop_ _Journal_abbreviation 'Nat. Chem. Biol.' _Journal_volume 12 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 593 _Page_last 600 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Axin RGS domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Axin RGS domain' $Axin_RGS_domain stop_ _System_molecular_weight 16774 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Axin_RGS_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Axin_RGS_domain _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 147 _Mol_residue_sequence ; GSASPTPPYLKWAESLHSLL DDQDGISLFRTFLKQEGCAD LLDFWFACTGFRKLEPCDSN EEKRLKLARAIYRKYILDNN GIVSRQTKPATKSFIKGCIM KQLIDPAMFDQAQTEIQATM EENTYPSFLKSDIYLEYTRT GSESPKV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 74 GLY 2 75 SER 3 76 ALA 4 77 SER 5 78 PRO 6 79 THR 7 80 PRO 8 81 PRO 9 82 TYR 10 83 LEU 11 84 LYS 12 85 TRP 13 86 ALA 14 87 GLU 15 88 SER 16 89 LEU 17 90 HIS 18 91 SER 19 92 LEU 20 93 LEU 21 94 ASP 22 95 ASP 23 96 GLN 24 97 ASP 25 98 GLY 26 99 ILE 27 100 SER 28 101 LEU 29 102 PHE 30 103 ARG 31 104 THR 32 105 PHE 33 106 LEU 34 107 LYS 35 108 GLN 36 109 GLU 37 110 GLY 38 111 CYS 39 112 ALA 40 113 ASP 41 114 LEU 42 115 LEU 43 116 ASP 44 117 PHE 45 118 TRP 46 119 PHE 47 120 ALA 48 121 CYS 49 122 THR 50 123 GLY 51 124 PHE 52 125 ARG 53 126 LYS 54 127 LEU 55 128 GLU 56 129 PRO 57 130 CYS 58 131 ASP 59 132 SER 60 133 ASN 61 134 GLU 62 135 GLU 63 136 LYS 64 137 ARG 65 138 LEU 66 139 LYS 67 140 LEU 68 141 ALA 69 142 ARG 70 143 ALA 71 144 ILE 72 145 TYR 73 146 ARG 74 147 LYS 75 148 TYR 76 149 ILE 77 150 LEU 78 151 ASP 79 152 ASN 80 153 ASN 81 154 GLY 82 155 ILE 83 156 VAL 84 157 SER 85 158 ARG 86 159 GLN 87 160 THR 88 161 LYS 89 162 PRO 90 163 ALA 91 164 THR 92 165 LYS 93 166 SER 94 167 PHE 95 168 ILE 96 169 LYS 97 170 GLY 98 171 CYS 99 172 ILE 100 173 MET 101 174 LYS 102 175 GLN 103 176 LEU 104 177 ILE 105 178 ASP 106 179 PRO 107 180 ALA 108 181 MET 109 182 PHE 110 183 ASP 111 184 GLN 112 185 ALA 113 186 GLN 114 187 THR 115 188 GLU 116 189 ILE 117 190 GLN 118 191 ALA 119 192 THR 120 193 MET 121 194 GLU 122 195 GLU 123 196 ASN 124 197 THR 125 198 TYR 126 199 PRO 127 200 SER 128 201 PHE 129 202 LEU 130 203 LYS 131 204 SER 132 205 ASP 133 206 ILE 134 207 TYR 135 208 LEU 136 209 GLU 137 210 TYR 138 211 THR 139 212 ARG 140 213 THR 141 214 GLY 142 215 SER 143 216 GLU 144 217 SER 145 218 PRO 146 219 LYS 147 220 VAL 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 $Axin_RGS_domain 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 $Axin_RGS_domain 'recombinant technology' . Escherichia coli . pET32a 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 _Isotopic_labeling $Axin_RGS_domain 0.5 mM '[U-99% 13C; U-99% 15N]' $Axin_RGS_domain 0.5 mM '[U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ 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 Bruker _Model DRX _Field_strength 600 _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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Axin_RGS_domain_conditions _Saveframe_category sample_conditions _Details 'Final buffer condition for NMR' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.3 . M pH 6.8 . 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 0.00 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 CBCA(CO)NH' '3D HNCACB' '3D HNCA' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Axin_RGS_domain_conditions _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Axin RGS domain' _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 90 17 HIS H H 8.207 0.001 . 2 90 17 HIS CA C 60.383 0.010 . 3 90 17 HIS CB C 28.974 0.004 . 4 90 17 HIS N N 118.283 0.001 . 5 91 18 SER H H 7.690 0.001 . 6 91 18 SER CA C 60.988 0.132 . 7 91 18 SER CB C 62.610 0.026 . 8 91 18 SER N N 113.794 0.024 . 9 92 19 LEU H H 7.474 0.002 . 10 92 19 LEU CA C 57.610 0.053 . 11 92 19 LEU CB C 41.637 0.003 . 12 92 19 LEU N N 124.546 0.043 . 13 93 20 LEU H H 7.325 0.051 . 14 93 20 LEU CA C 56.566 0.023 . 15 93 20 LEU CB C 40.366 0.037 . 16 93 20 LEU N N 115.989 0.003 . 17 94 21 ASP H H 7.437 0.002 . 18 94 21 ASP CA C 54.626 0.024 . 19 94 21 ASP CB C 38.627 0.006 . 20 94 21 ASP N N 114.074 0.049 . 21 95 22 ASP H H 7.686 0.005 . 22 95 22 ASP CA C 52.963 0.066 . 23 95 22 ASP CB C 42.709 0.012 . 24 95 22 ASP N N 120.245 0.075 . 25 96 23 GLN H H 8.669 0.002 . 26 96 23 GLN CA C 59.081 0.042 . 27 96 23 GLN CB C 28.164 0.064 . 28 96 23 GLN N N 122.814 0.030 . 29 97 24 ASP H H 8.321 0.003 . 30 97 24 ASP CA C 56.747 0.069 . 31 97 24 ASP CB C 40.555 0.013 . 32 97 24 ASP N N 119.486 0.064 . 33 98 25 GLY H H 8.488 0.003 . 34 98 25 GLY CA C 46.516 0.065 . 35 98 25 GLY N N 111.169 0.049 . 36 99 26 ILE H H 8.545 0.003 . 37 99 26 ILE CA C 63.821 0.034 . 38 99 26 ILE CB C 37.796 0.041 . 39 99 26 ILE N N 121.328 0.058 . 40 100 27 SER H H 7.748 0.002 . 41 100 27 SER CA C 58.434 0.007 . 42 100 27 SER CB C 63.779 0.017 . 43 100 27 SER N N 116.406 0.027 . 44 101 28 LEU H H 8.294 0.003 . 45 101 28 LEU CA C 55.551 0.005 . 46 101 28 LEU CB C 41.047 0.096 . 47 101 28 LEU N N 122.486 0.023 . 48 102 29 PHE H H 7.365 0.010 . 49 102 29 PHE CA C 55.598 0.005 . 50 102 29 PHE CB C 38.535 0.004 . 51 102 29 PHE N N 119.011 0.095 . 52 103 30 ARG H H 8.424 0.004 . 53 103 30 ARG CA C 55.639 0.024 . 54 103 30 ARG CB C 30.510 0.099 . 55 103 30 ARG N N 115.387 0.021 . 56 104 31 THR H H 7.742 0.001 . 57 104 31 THR CA C 61.335 0.001 . 58 104 31 THR CB C 70.089 0.004 . 59 104 31 THR N N 108.290 0.043 . 60 105 32 PHE H H 8.173 0.002 . 61 105 32 PHE CA C 57.639 0.051 . 62 105 32 PHE CB C 38.648 0.023 . 63 105 32 PHE N N 124.226 0.037 . 64 106 33 LEU H H 8.016 0.001 . 65 106 33 LEU CA C 54.915 0.058 . 66 106 33 LEU CB C 42.666 0.031 . 67 106 33 LEU N N 125.202 0.026 . 68 107 34 LYS H H 7.736 0.004 . 69 107 34 LYS CA C 57.959 0.002 . 70 107 34 LYS CB C 31.158 0.004 . 71 107 34 LYS N N 126.531 0.038 . 72 108 35 GLN H H 7.594 0.003 . 73 108 35 GLN CA C 56.164 0.048 . 74 108 35 GLN CB C 33.026 0.105 . 75 108 35 GLN N N 116.395 0.025 . 76 109 36 GLU H H 7.693 0.001 . 77 109 36 GLU CA C 57.301 0.009 . 78 109 36 GLU CB C 28.724 0.073 . 79 109 36 GLU N N 116.207 0.024 . 80 110 37 GLY H H 7.736 0.001 . 81 110 37 GLY CA C 46.401 0.007 . 82 110 37 GLY N N 111.368 0.023 . 83 111 38 CYS H H 8.485 0.002 . 84 111 38 CYS CA C 56.224 0.089 . 85 111 38 CYS CB C 28.879 0.017 . 86 111 38 CYS N N 114.473 0.017 . 87 112 39 ALA H H 8.346 0.001 . 88 112 39 ALA CA C 56.154 0.001 . 89 112 39 ALA CB C 17.739 0.015 . 90 112 39 ALA N N 124.704 0.019 . 91 113 40 ASP H H 8.937 0.004 . 92 113 40 ASP CA C 57.742 0.027 . 93 113 40 ASP CB C 39.412 0.004 . 94 113 40 ASP N N 116.303 0.069 . 95 114 41 LEU H H 8.188 0.006 . 96 114 41 LEU CA C 54.697 0.081 . 97 114 41 LEU CB C 41.141 0.020 . 98 114 41 LEU N N 121.652 0.085 . 99 115 42 LEU H H 7.896 0.002 . 100 115 42 LEU CA C 54.588 0.004 . 101 115 42 LEU CB C 41.151 0.010 . 102 115 42 LEU N N 123.193 0.008 . 103 116 43 ASP H H 8.277 0.000 . 104 116 43 ASP CA C 59.009 0.006 . 105 116 43 ASP CB C 39.316 0.037 . 106 116 43 ASP N N 120.379 0.008 . 107 117 44 PHE H H 8.092 0.001 . 108 117 44 PHE CA C 58.985 0.062 . 109 117 44 PHE CB C 39.440 0.096 . 110 117 44 PHE N N 121.786 0.048 . 111 119 46 PHE CA C 62.254 0.019 . 112 119 46 PHE CB C 38.943 0.007 . 113 120 47 ALA H H 8.383 0.003 . 114 120 47 ALA CA C 55.018 0.017 . 115 120 47 ALA CB C 17.448 0.022 . 116 120 47 ALA N N 125.738 0.075 . 117 121 48 CYS H H 7.745 0.002 . 118 121 48 CYS CA C 64.386 0.096 . 119 121 48 CYS CB C 26.268 0.003 . 120 121 48 CYS N N 116.682 0.070 . 121 122 49 THR H H 7.241 0.004 . 122 122 49 THR CA C 66.398 0.002 . 123 122 49 THR CB C 68.404 0.069 . 124 122 49 THR N N 116.883 0.063 . 125 123 50 GLY H H 7.923 0.001 . 126 123 50 GLY CA C 46.858 0.017 . 127 123 50 GLY N N 107.066 0.064 . 128 124 51 PHE H H 7.950 0.002 . 129 124 51 PHE CA C 61.656 0.004 . 130 124 51 PHE CB C 39.342 0.025 . 131 124 51 PHE N N 122.262 0.050 . 132 125 52 ARG H H 8.117 0.002 . 133 125 52 ARG CA C 57.926 0.034 . 134 125 52 ARG CB C 30.759 0.027 . 135 125 52 ARG N N 120.519 0.089 . 136 126 53 LYS H H 7.070 0.004 . 137 126 53 LYS CA C 56.616 0.051 . 138 126 53 LYS CB C 32.926 0.051 . 139 126 53 LYS N N 114.376 0.047 . 140 127 54 LEU H H 7.050 0.003 . 141 127 54 LEU CA C 54.635 0.055 . 142 127 54 LEU CB C 41.490 0.036 . 143 127 54 LEU N N 120.269 0.070 . 144 128 55 GLU H H 8.667 0.002 . 145 128 55 GLU CA C 54.635 0.017 . 146 128 55 GLU CB C 29.825 0.032 . 147 128 55 GLU N N 127.903 0.046 . 148 129 56 PRO CA C 65.722 0.045 . 149 129 56 PRO CB C 32.282 0.011 . 150 130 57 CYS H H 8.419 0.004 . 151 130 57 CYS CA C 56.809 0.022 . 152 130 57 CYS CB C 33.379 0.028 . 153 130 57 CYS N N 116.006 0.076 . 154 132 59 SER H H 8.258 0.002 . 155 132 59 SER CA C 60.188 0.021 . 156 132 59 SER CB C 62.909 0.039 . 157 132 59 SER N N 121.158 0.020 . 158 133 60 ASN H H 7.694 0.003 . 159 133 60 ASN CA C 51.641 0.015 . 160 133 60 ASN CB C 39.391 0.009 . 161 133 60 ASN N N 118.571 0.060 . 162 134 61 GLU H H 7.735 0.002 . 163 134 61 GLU CA C 60.878 0.012 . 164 134 61 GLU CB C 29.872 0.013 . 165 134 61 GLU N N 122.934 0.082 . 166 135 62 GLU H H 8.618 0.001 . 167 135 62 GLU CA C 60.024 0.029 . 168 135 62 GLU CB C 29.002 0.051 . 169 135 62 GLU N N 119.416 0.040 . 170 136 63 LYS H H 8.121 0.003 . 171 136 63 LYS CA C 59.551 0.021 . 172 136 63 LYS CB C 32.505 0.014 . 173 136 63 LYS N N 120.273 0.037 . 174 138 65 LEU H H 7.755 0.009 . 175 138 65 LEU CA C 55.259 0.018 . 176 138 65 LEU CB C 41.897 0.070 . 177 138 65 LEU N N 120.900 0.018 . 178 139 66 LYS H H 8.112 0.007 . 179 139 66 LYS CA C 56.919 0.023 . 180 139 66 LYS CB C 35.919 0.047 . 181 139 66 LYS N N 122.137 0.052 . 182 140 67 LEU H H 7.680 0.003 . 183 140 67 LEU CA C 52.428 0.026 . 184 140 67 LEU CB C 43.835 0.060 . 185 140 67 LEU N N 128.087 0.025 . 186 142 69 ARG H H 9.214 0.000 . 187 142 69 ARG CA C 56.520 0.010 . 188 142 69 ARG CB C 30.242 0.044 . 189 142 69 ARG N N 118.020 0.000 . 190 143 70 ALA H H 8.172 0.001 . 191 143 70 ALA CA C 55.400 0.011 . 192 143 70 ALA CB C 18.333 0.119 . 193 143 70 ALA N N 122.706 0.035 . 194 144 71 ILE H H 8.609 0.002 . 195 144 71 ILE CA C 59.058 0.010 . 196 144 71 ILE CB C 40.120 0.014 . 197 144 71 ILE N N 120.785 0.022 . 198 145 72 TYR H H 8.800 0.001 . 199 145 72 TYR CA C 61.607 0.002 . 200 145 72 TYR CB C 39.204 0.007 . 201 145 72 TYR N N 116.535 0.060 . 202 146 73 ARG H H 9.043 0.002 . 203 146 73 ARG CA C 59.616 0.059 . 204 146 73 ARG CB C 30.253 0.108 . 205 146 73 ARG N N 119.493 0.044 . 206 147 74 LYS H H 7.963 0.002 . 207 147 74 LYS CA C 58.745 0.028 . 208 147 74 LYS CB C 33.059 0.001 . 209 147 74 LYS N N 116.854 0.044 . 210 148 75 TYR H H 7.800 0.002 . 211 148 75 TYR CA C 59.092 0.060 . 212 148 75 TYR CB C 41.115 0.027 . 213 148 75 TYR N N 110.454 0.035 . 214 149 76 ILE H H 7.666 0.001 . 215 149 76 ILE CA C 60.730 0.080 . 216 149 76 ILE CB C 36.647 0.007 . 217 149 76 ILE N N 117.510 0.071 . 218 150 77 LEU H H 7.469 0.001 . 219 150 77 LEU CA C 57.336 0.059 . 220 150 77 LEU CB C 42.998 0.024 . 221 150 77 LEU N N 120.306 0.034 . 222 151 78 ASP H H 7.280 0.001 . 223 151 78 ASP CA C 53.627 0.012 . 224 151 78 ASP CB C 39.900 0.013 . 225 151 78 ASP N N 114.411 0.018 . 226 152 79 ASN H H 7.956 0.018 . 227 152 79 ASN CA C 54.614 0.073 . 228 152 79 ASN CB C 37.358 0.025 . 229 152 79 ASN N N 120.131 0.043 . 230 153 80 ASN H H 8.473 0.002 . 231 153 80 ASN CA C 53.334 0.009 . 232 153 80 ASN CB C 38.996 0.019 . 233 153 80 ASN N N 119.420 0.035 . 234 154 81 GLY H H 7.783 0.005 . 235 154 81 GLY CA C 45.070 0.035 . 236 154 81 GLY N N 108.813 0.026 . 237 155 82 ILE H H 8.663 0.002 . 238 155 82 ILE CA C 63.010 0.090 . 239 155 82 ILE CB C 38.006 0.029 . 240 155 82 ILE N N 121.965 0.099 . 241 156 83 VAL H H 8.736 0.001 . 242 156 83 VAL CA C 66.605 0.070 . 243 156 83 VAL CB C 29.515 0.016 . 244 156 83 VAL N N 121.785 0.028 . 245 157 84 SER H H 7.390 0.001 . 246 157 84 SER CA C 61.418 0.032 . 247 157 84 SER CB C 63.375 0.048 . 248 157 84 SER N N 114.614 0.051 . 249 158 85 ARG H H 7.873 0.002 . 250 158 85 ARG CA C 58.400 0.010 . 251 158 85 ARG CB C 30.691 0.013 . 252 158 85 ARG N N 116.593 0.046 . 253 159 86 GLN H H 7.573 0.001 . 254 159 86 GLN CA C 55.164 0.080 . 255 159 86 GLN CB C 29.185 0.050 . 256 159 86 GLN N N 115.598 0.054 . 257 160 87 THR H H 7.238 0.002 . 258 160 87 THR CA C 60.576 0.042 . 259 160 87 THR CB C 71.364 0.018 . 260 160 87 THR N N 112.486 0.062 . 261 161 88 LYS H H 9.734 0.007 . 262 161 88 LYS CA C 55.551 0.035 . 263 161 88 LYS CB C 31.170 0.034 . 264 161 88 LYS N N 126.016 0.019 . 265 163 90 ALA H H 8.381 0.012 . 266 163 90 ALA CA C 55.250 0.007 . 267 163 90 ALA CB C 17.669 0.006 . 268 163 90 ALA N N 125.632 0.055 . 269 164 91 THR H H 7.752 0.001 . 270 164 91 THR CA C 56.172 0.033 . 271 164 91 THR CB C 68.815 0.004 . 272 164 91 THR N N 114.088 0.024 . 273 165 92 LYS H H 8.298 0.006 . 274 165 92 LYS CA C 55.134 0.073 . 275 165 92 LYS CB C 32.826 0.053 . 276 165 92 LYS N N 124.309 0.059 . 277 166 93 SER H H 7.522 0.002 . 278 166 93 SER CA C 58.948 0.033 . 279 166 93 SER CB C 63.689 0.006 . 280 166 93 SER N N 117.582 0.009 . 281 167 94 PHE H H 7.974 0.001 . 282 167 94 PHE CA C 61.110 0.086 . 283 167 94 PHE CB C 38.508 0.025 . 284 167 94 PHE N N 123.529 0.049 . 285 168 95 ILE H H 8.003 0.002 . 286 168 95 ILE CA C 58.626 0.007 . 287 168 95 ILE CB C 41.454 0.011 . 288 168 95 ILE N N 129.977 0.064 . 289 169 96 LYS H H 8.208 0.002 . 290 169 96 LYS CA C 60.200 0.011 . 291 169 96 LYS CB C 32.743 0.012 . 292 169 96 LYS N N 118.010 0.032 . 293 170 97 GLY H H 8.012 0.002 . 294 170 97 GLY CA C 47.244 0.044 . 295 170 97 GLY N N 104.973 0.020 . 296 171 98 CYS H H 7.497 0.003 . 297 171 98 CYS CA C 64.284 0.021 . 298 171 98 CYS CB C 26.242 0.097 . 299 171 98 CYS N N 119.500 0.064 . 300 172 99 ILE H H 7.746 0.001 . 301 172 99 ILE CA C 63.468 0.018 . 302 172 99 ILE CB C 36.210 0.030 . 303 172 99 ILE N N 118.426 0.047 . 304 174 101 LYS H H 9.384 0.004 . 305 174 101 LYS CA C 59.222 0.027 . 306 174 101 LYS CB C 32.070 0.024 . 307 174 101 LYS N N 123.578 0.019 . 308 175 102 GLN H H 7.761 0.003 . 309 175 102 GLN CA C 58.905 0.035 . 310 175 102 GLN CB C 28.520 0.025 . 311 175 102 GLN N N 120.967 0.075 . 312 176 103 LEU H H 7.524 0.002 . 313 176 103 LEU CA C 54.602 0.010 . 314 176 103 LEU CB C 40.940 0.011 . 315 176 103 LEU N N 115.635 0.025 . 316 177 104 ILE H H 7.911 0.007 . 317 177 104 ILE CA C 60.811 0.021 . 318 177 104 ILE CB C 38.758 0.055 . 319 177 104 ILE N N 119.183 0.019 . 320 178 105 ASP H H 8.434 0.002 . 321 178 105 ASP CA C 51.834 0.033 . 322 178 105 ASP CB C 41.689 0.021 . 323 178 105 ASP N N 127.087 0.018 . 324 179 106 PRO CA C 63.766 0.004 . 325 179 106 PRO CB C 32.084 0.010 . 326 180 107 ALA H H 8.348 0.001 . 327 180 107 ALA CA C 53.097 0.050 . 328 180 107 ALA CB C 18.775 0.011 . 329 180 107 ALA N N 121.703 0.016 . 330 181 108 MET H H 7.929 0.002 . 331 181 108 MET CA C 55.506 0.041 . 332 181 108 MET CB C 32.443 0.060 . 333 181 108 MET N N 117.390 0.034 . 334 182 109 PHE H H 7.868 0.001 . 335 182 109 PHE CA C 57.934 0.062 . 336 182 109 PHE CB C 39.498 0.023 . 337 182 109 PHE N N 120.200 0.030 . 338 183 110 ASP H H 8.039 0.005 . 339 183 110 ASP CA C 54.438 0.010 . 340 183 110 ASP CB C 41.080 0.021 . 341 183 110 ASP N N 123.581 0.021 . 342 184 111 GLN H H 8.200 0.002 . 343 184 111 GLN CA C 56.186 0.053 . 344 184 111 GLN CB C 29.288 0.026 . 345 184 111 GLN N N 120.885 0.043 . 346 185 112 ALA H H 8.277 0.003 . 347 185 112 ALA CA C 52.959 0.079 . 348 185 112 ALA CB C 18.961 0.021 . 349 185 112 ALA N N 124.288 0.069 . 350 186 113 GLN H H 8.254 0.005 . 351 186 113 GLN CA C 56.081 0.052 . 352 186 113 GLN CB C 29.181 0.016 . 353 186 113 GLN N N 118.784 0.027 . 354 187 114 THR H H 8.086 0.005 . 355 187 114 THR CA C 62.453 0.029 . 356 187 114 THR CB C 69.933 0.021 . 357 187 114 THR N N 115.007 0.022 . 358 188 115 GLU H H 8.343 0.008 . 359 188 115 GLU CA C 56.783 0.001 . 360 188 115 GLU CB C 30.209 0.014 . 361 188 115 GLU N N 123.207 0.093 . 362 189 116 ILE H H 8.139 0.004 . 363 189 116 ILE CA C 61.557 0.037 . 364 189 116 ILE CB C 38.564 0.003 . 365 189 116 ILE N N 122.187 0.044 . 366 190 117 GLN H H 8.395 0.001 . 367 190 117 GLN CA C 55.895 0.028 . 368 190 117 GLN CB C 29.323 0.050 . 369 190 117 GLN N N 124.706 0.039 . 370 191 118 ALA H H 8.351 0.004 . 371 191 118 ALA CA C 52.505 0.023 . 372 191 118 ALA CB C 19.180 0.013 . 373 191 118 ALA N N 125.588 0.014 . 374 192 119 THR H H 7.832 0.012 . 375 192 119 THR CA C 59.322 0.047 . 376 192 119 THR CB C 67.810 0.072 . 377 192 119 THR N N 118.391 0.096 . 378 193 120 MET H H 7.738 0.016 . 379 193 120 MET CA C 59.436 0.093 . 380 193 120 MET CB C 32.330 0.010 . 381 193 120 MET N N 126.455 0.115 . 382 194 121 GLU H H 8.526 0.001 . 383 194 121 GLU CA C 60.523 0.038 . 384 194 121 GLU CB C 29.786 0.021 . 385 194 121 GLU N N 118.689 0.038 . 386 195 122 GLU H H 8.311 0.003 . 387 195 122 GLU CA C 57.897 0.010 . 388 195 122 GLU CB C 30.820 0.092 . 389 195 122 GLU N N 114.331 0.061 . 390 196 123 ASN H H 8.004 0.005 . 391 196 123 ASN CA C 54.643 0.044 . 392 196 123 ASN CB C 41.092 0.018 . 393 196 123 ASN N N 115.062 0.054 . 394 197 124 THR H H 8.130 0.001 . 395 197 124 THR CA C 66.634 0.046 . 396 197 124 THR CB C 69.491 0.020 . 397 197 124 THR N N 116.107 0.012 . 398 200 127 SER H H 8.469 0.003 . 399 200 127 SER CB C 62.526 0.011 . 400 200 127 SER N N 114.110 0.028 . 401 201 128 PHE H H 8.233 0.003 . 402 201 128 PHE CA C 59.093 0.087 . 403 201 128 PHE CB C 38.641 0.056 . 404 201 128 PHE N N 126.405 0.070 . 405 202 129 LEU H H 7.328 0.002 . 406 202 129 LEU CA C 56.428 0.042 . 407 202 129 LEU CB C 41.542 0.023 . 408 202 129 LEU N N 118.025 0.026 . 409 203 130 LYS H H 8.509 0.003 . 410 203 130 LYS CA C 59.248 0.052 . 411 203 130 LYS CB C 32.051 0.037 . 412 203 130 LYS N N 119.357 0.056 . 413 204 131 SER H H 8.336 0.002 . 414 204 131 SER CA C 58.702 0.022 . 415 204 131 SER CB C 65.715 0.034 . 416 204 131 SER N N 120.594 0.032 . 417 205 132 ASP H H 8.645 0.001 . 418 205 132 ASP CA C 56.103 0.050 . 419 205 132 ASP CB C 39.982 0.090 . 420 205 132 ASP N N 121.093 0.034 . 421 206 133 ILE H H 7.592 0.001 . 422 206 133 ILE CA C 62.485 0.096 . 423 206 133 ILE CB C 38.316 0.004 . 424 206 133 ILE N N 117.233 0.050 . 425 207 134 TYR H H 7.235 0.002 . 426 207 134 TYR CA C 59.088 0.030 . 427 207 134 TYR CB C 39.316 0.011 . 428 207 134 TYR N N 120.317 0.034 . 429 208 135 LEU H H 7.461 0.002 . 430 208 135 LEU CA C 58.613 0.087 . 431 208 135 LEU CB C 42.829 0.062 . 432 208 135 LEU N N 120.966 0.045 . stop_ save_