data_27548 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Ressonance assignments for the human Smad5 MH1 domain ; _BMRB_accession_number 27548 _BMRB_flat_file_name bmr27548.str _Entry_type original _Submission_date 2018-07-17 _Accession_date 2018-07-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Ressonance assignments for the human Smad5 MH1 domain' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Macias Maria J. . 2 Martin-Malpartida Pau . . 3 Ruiz Lidia . . 4 Aragon Eric . . 5 Gomes Tiago . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 84 "13C chemical shifts" 196 "15N chemical shifts" 84 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-11-15 original BMRB . stop_ _Original_release_date 2018-07-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-beta signaling. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30060237 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guca Ewelina . . 2 Sunol David . . 3 Ruiz Lidia . . 4 Konkol Agnieszka . . 5 Cordero Jorge . . 6 Torner Carles . . 7 Aragon Eric . . 8 Martin-Malpartida Pau . . 9 Riera Antoni . . 10 Macias Maria J. . stop_ _Journal_abbreviation 'Nucleic Acids Res.' _Journal_name_full 'Nucleic acids research' _Journal_volume 46 _Journal_issue 17 _Journal_ISSN 1362-4962 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9220 _Page_last 9235 _Year 2018 _Details . loop_ _Keyword SMAD Smad5 TGF-beta stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name SMAD5-MH1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SMAD5-MH1 $SMAD5-MH1 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_SMAD5-MH1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SMAD5-MH1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 137 _Mol_residue_sequence ; GPSFTSPAVKRLLGWKQGDE EEKWAEKAVDALVKKLKKKK GAMEELEKALSSPGQPSKCV TIPRSLDGRLQVSHRKGLPH VIYCRVWRWPDLQSHHELKP LDICEFPFGSKQKEVCINPY HYKRVESPVLPPVLVPR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 7 GLY 2 8 PRO 3 9 SER 4 10 PHE 5 11 THR 6 12 SER 7 13 PRO 8 14 ALA 9 15 VAL 10 16 LYS 11 17 ARG 12 18 LEU 13 19 LEU 14 20 GLY 15 21 TRP 16 22 LYS 17 23 GLN 18 24 GLY 19 25 ASP 20 26 GLU 21 27 GLU 22 28 GLU 23 29 LYS 24 30 TRP 25 31 ALA 26 32 GLU 27 33 LYS 28 34 ALA 29 35 VAL 30 36 ASP 31 37 ALA 32 38 LEU 33 39 VAL 34 40 LYS 35 41 LYS 36 42 LEU 37 43 LYS 38 44 LYS 39 45 LYS 40 46 LYS 41 47 GLY 42 48 ALA 43 49 MET 44 50 GLU 45 51 GLU 46 52 LEU 47 53 GLU 48 54 LYS 49 55 ALA 50 56 LEU 51 57 SER 52 58 SER 53 59 PRO 54 60 GLY 55 61 GLN 56 62 PRO 57 63 SER 58 64 LYS 59 65 CYS 60 66 VAL 61 67 THR 62 68 ILE 63 69 PRO 64 70 ARG 65 71 SER 66 72 LEU 67 73 ASP 68 74 GLY 69 75 ARG 70 76 LEU 71 77 GLN 72 78 VAL 73 79 SER 74 80 HIS 75 81 ARG 76 82 LYS 77 83 GLY 78 84 LEU 79 85 PRO 80 86 HIS 81 87 VAL 82 88 ILE 83 89 TYR 84 90 CYS 85 91 ARG 86 92 VAL 87 93 TRP 88 94 ARG 89 95 TRP 90 96 PRO 91 97 ASP 92 98 LEU 93 99 GLN 94 100 SER 95 101 HIS 96 102 HIS 97 103 GLU 98 104 LEU 99 105 LYS 100 106 PRO 101 107 LEU 102 108 ASP 103 109 ILE 104 110 CYS 105 111 GLU 106 112 PHE 107 113 PRO 108 114 PHE 109 115 GLY 110 116 SER 111 117 LYS 112 118 GLN 113 119 LYS 114 120 GLU 115 121 VAL 116 122 CYS 117 123 ILE 118 124 ASN 119 125 PRO 120 126 TYR 121 127 HIS 122 128 TYR 123 129 LYS 124 130 ARG 125 131 VAL 126 132 GLU 127 133 SER 128 134 PRO 129 135 VAL 130 136 LEU 131 137 PRO 132 138 PRO 133 139 VAL 134 140 LEU 135 141 VAL 136 142 PRO 137 143 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value UNP Q99717 SMAD5_HUMAN . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SMAD5-MH1 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 $SMAD5-MH1 'recombinant technology' . Escherichia coli . pETM11 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 $SMAD5-MH1 0.4 mM '[U-100% 13C; U-100% 15N]' TRIS 20 mM [U-2H] 'sodium chloride' 100 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_MDDNMR _Saveframe_category software _Name MDDNMR _Version . loop_ _Vendor _Address _Electronic_address 'Orekhov, V.' . . stop_ loop_ _Task processing stop_ _Details . save_ 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_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . 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 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_2D_1H-15N_TROSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _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 pH 7.2 . 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 '3D HNCACB' '3D HN(CO)CACB' '2D 1H-15N TROSY' 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 SMAD5-MH1 _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 7 1 GLY H H 7.920 0.000 1 2 7 1 GLY CA C 41.687 0.000 1 3 7 1 GLY N N 108.965 0.000 1 4 8 2 PRO CA C 60.030 0.000 1 5 8 2 PRO CB C 28.691 0.000 1 6 9 3 SER H H 8.279 0.000 1 7 9 3 SER CA C 55.166 0.037 1 8 9 3 SER CB C 60.699 0.149 1 9 9 3 SER N N 116.720 0.000 1 10 10 4 PHE H H 8.133 0.000 1 11 10 4 PHE CA C 54.497 0.185 1 12 10 4 PHE CB C 36.637 0.000 1 13 10 4 PHE N N 122.636 0.000 1 14 11 5 THR H H 7.940 0.000 1 15 11 5 THR CA C 58.730 0.111 1 16 11 5 THR CB C 66.602 0.111 1 17 11 5 THR N N 117.364 0.000 1 18 12 6 SER H H 8.335 0.000 1 19 12 6 SER CA C 53.866 0.000 1 20 12 6 SER CB C 60.179 0.000 1 21 12 6 SER N N 120.950 0.000 1 22 13 7 PRO CA C 60.104 0.000 1 23 13 7 PRO CB C 28.691 0.000 1 24 14 8 ALA H H 8.128 0.000 1 25 14 8 ALA CA C 49.262 0.000 1 26 14 8 ALA CB C 15.769 0.074 1 27 14 8 ALA N N 124.646 0.000 1 28 15 9 VAL H H 7.885 0.000 1 29 15 9 VAL CA C 58.991 0.074 1 30 15 9 VAL CB C 29.471 0.037 1 31 15 9 VAL N N 120.527 0.000 1 32 16 10 LYS H H 8.202 0.000 1 33 16 10 LYS CA C 53.049 0.000 1 34 16 10 LYS CB C 29.285 0.000 1 35 16 10 LYS N N 126.966 0.000 1 36 20 14 GLY CA C 42.727 0.000 1 37 21 15 TRP H H 7.990 0.000 1 38 21 15 TRP CA C 53.495 0.000 1 39 21 15 TRP CB C 27.132 0.075 1 40 21 15 TRP N N 119.824 0.000 1 41 22 16 LYS H H 7.804 0.000 1 42 22 16 LYS CA C 54.126 0.037 1 43 22 16 LYS CB C 29.434 0.000 1 44 22 16 LYS N N 123.339 0.000 1 45 23 17 GLN H H 8.374 0.000 1 46 23 17 GLN CA C 51.527 0.111 1 47 23 17 GLN CB C 26.203 0.112 1 48 23 17 GLN N N 123.574 0.000 1 49 24 18 GLY H H 8.527 0.000 1 50 24 18 GLY CA C 41.761 0.000 1 51 24 18 GLY N N 112.654 0.000 1 52 25 19 ASP H H 8.265 0.000 1 53 25 19 ASP CA C 51.305 0.111 1 54 25 19 ASP CB C 38.420 0.074 1 55 25 19 ASP N N 120.059 0.000 1 56 26 20 GLU H H 8.363 0.000 1 57 26 20 GLU CA C 53.829 0.037 1 58 26 20 GLU CB C 27.317 0.037 1 59 26 20 GLU N N 120.982 0.000 1 60 27 21 GLU H H 7.655 0.000 1 61 27 21 GLU CA C 52.493 0.037 1 62 27 21 GLU CB C 26.537 0.000 1 63 27 21 GLU N N 118.277 0.000 1 64 28 22 GLU H H 8.153 0.000 1 65 28 22 GLU CA C 54.015 0.000 1 66 28 22 GLU N N 121.348 0.000 1 67 31 25 ALA CA C 52.975 0.000 1 68 31 25 ALA CB C 15.769 0.000 1 69 32 26 GLU H H 8.213 0.000 1 70 32 26 GLU CA C 52.381 0.000 1 71 32 26 GLU CB C 27.206 0.297 1 72 32 26 GLU N N 119.004 0.000 1 73 33 27 LYS H H 8.607 0.000 1 74 33 27 LYS CA C 55.500 0.297 1 75 33 27 LYS CB C 28.691 0.297 1 76 33 27 LYS N N 119.004 0.000 1 77 34 28 ALA H H 7.819 0.000 1 78 34 28 ALA CA C 51.713 0.000 1 79 34 28 ALA CB C 13.541 0.000 1 80 34 28 ALA N N 122.055 0.000 1 81 35 29 VAL H H 8.734 0.000 1 82 35 29 VAL CA C 64.374 0.111 1 83 35 29 VAL CB C 27.837 0.037 1 84 35 29 VAL N N 124.732 0.000 1 85 36 30 ASP H H 8.493 0.000 1 86 36 30 ASP CA C 55.278 0.075 1 87 36 30 ASP CB C 39.311 0.000 1 88 36 30 ASP N N 122.402 0.000 1 89 37 31 ALA H H 7.649 0.000 1 90 37 31 ALA CA C 51.898 0.111 1 91 37 31 ALA CB C 14.915 0.037 1 92 37 31 ALA N N 118.672 0.000 1 93 38 32 LEU H H 7.334 0.000 1 94 38 32 LEU CA C 54.683 0.000 1 95 38 32 LEU CB C 37.788 0.037 1 96 38 32 LEU N N 119.060 0.000 1 97 39 33 VAL H H 8.504 0.000 1 98 39 33 VAL CA C 63.855 0.037 1 99 39 33 VAL CB C 27.986 0.038 1 100 39 33 VAL N N 120.293 0.000 1 101 40 34 LYS H H 7.433 0.000 1 102 40 34 LYS CA C 56.986 0.075 1 103 40 34 LYS CB C 29.211 0.000 1 104 40 34 LYS N N 117.009 0.000 1 105 41 35 LYS H H 7.130 0.000 1 106 41 35 LYS CA C 55.649 0.000 1 107 41 35 LYS CB C 30.064 0.112 1 108 41 35 LYS N N 116.636 0.000 1 109 42 36 LEU H H 8.430 0.000 1 110 42 36 LEU CA C 53.681 0.037 1 111 42 36 LEU CB C 37.751 0.074 1 112 42 36 LEU N N 118.579 0.000 1 113 43 37 LYS H H 7.976 0.000 1 114 43 37 LYS CA C 55.723 0.074 1 115 43 37 LYS CB C 28.914 0.000 1 116 43 37 LYS N N 117.901 0.000 1 117 44 38 LYS H H 7.099 0.000 1 118 44 38 LYS CA C 53.421 0.000 1 119 44 38 LYS CB C 29.360 0.075 1 120 44 38 LYS N N 115.470 0.000 1 121 45 39 LYS H H 7.637 0.000 1 122 45 39 LYS CA C 51.601 0.037 1 123 45 39 LYS CB C 29.767 0.111 1 124 45 39 LYS N N 122.015 0.000 1 125 46 40 LYS H H 8.368 0.000 1 126 46 40 LYS CA C 55.092 0.037 1 127 46 40 LYS CB C 28.394 0.000 1 128 46 40 LYS N N 126.911 0.000 1 129 47 41 GLY H H 9.035 0.000 1 130 47 41 GLY CA C 42.801 0.000 1 131 47 41 GLY N N 115.958 0.000 1 132 48 42 ALA H H 7.566 0.000 1 133 48 42 ALA CA C 52.418 0.037 1 134 48 42 ALA CB C 17.032 0.000 1 135 48 42 ALA N N 125.469 0.000 1 136 49 43 MET H H 8.679 0.000 1 137 49 43 MET CA C 54.535 0.000 1 138 49 43 MET CB C 27.614 0.037 1 139 49 43 MET N N 117.521 0.000 1 140 50 44 GLU H H 8.875 0.000 1 141 50 44 GLU CA C 57.431 0.000 1 142 50 44 GLU CB C 24.755 0.000 1 143 50 44 GLU N N 119.989 0.000 1 144 53 47 GLU CA C 57.208 0.000 1 145 53 47 GLU CB C 25.869 0.000 1 146 54 48 LYS H H 7.567 0.000 1 147 54 48 LYS CA C 56.503 0.037 1 148 54 48 LYS CB C 28.282 0.186 1 149 54 48 LYS N N 121.699 0.000 1 150 55 49 ALA H H 7.689 0.000 1 151 55 49 ALA CA C 51.193 0.000 1 152 55 49 ALA CB C 14.197 0.062 1 153 55 49 ALA N N 122.589 0.000 1 154 56 50 LEU H H 7.334 0.000 1 155 56 50 LEU CA C 52.641 0.037 1 156 56 50 LEU CB C 37.306 0.148 1 157 56 50 LEU N N 120.102 0.000 1 158 57 51 SER H H 7.118 0.000 1 159 57 51 SER CA C 55.871 0.074 1 160 57 51 SER CB C 61.181 0.111 1 161 57 51 SER N N 109.865 0.000 1 162 58 52 SER H H 6.905 0.000 1 163 58 52 SER CA C 51.787 0.000 1 164 58 52 SER CB C 59.882 0.000 1 165 58 52 SER N N 116.464 0.000 1 166 59 53 PRO CA C 60.847 0.000 1 167 59 53 PRO CB C 28.171 0.000 1 168 60 54 GLY H H 8.165 0.000 1 169 60 54 GLY CA C 41.984 0.000 1 170 60 54 GLY N N 108.619 0.000 1 171 61 55 GLN H H 7.244 0.000 1 172 61 55 GLN CA C 49.485 0.000 1 173 61 55 GLN CB C 25.720 0.000 1 174 61 55 GLN N N 120.245 0.000 1 175 62 56 PRO CA C 60.402 0.000 1 176 62 56 PRO CB C 28.691 0.000 1 177 63 57 SER H H 8.243 0.000 1 178 63 57 SER CA C 53.495 0.000 1 179 63 57 SER CB C 61.961 0.074 1 180 63 57 SER N N 115.723 0.000 1 181 64 58 LYS H H 9.045 0.000 1 182 64 58 LYS CA C 52.195 0.111 1 183 64 58 LYS CB C 30.437 0.186 1 184 64 58 LYS N N 123.258 0.000 1 185 65 59 CYS H H 7.986 0.000 1 186 65 59 CYS CA C 59.770 0.037 1 187 65 59 CYS CB C 28.245 0.000 1 188 65 59 CYS N N 117.246 0.000 1 189 66 60 VAL H H 7.939 0.000 1 190 66 60 VAL CA C 58.842 0.223 1 191 66 60 VAL CB C 30.622 0.074 1 192 66 60 VAL N N 124.394 0.000 1 193 67 61 THR H H 8.362 0.001 1 194 67 61 THR CA C 55.945 0.075 1 195 67 61 THR CB C 68.050 0.075 1 196 67 61 THR N N 116.175 0.000 1 197 68 62 ILE H H 8.074 0.000 1 198 68 62 ILE CA C 55.129 0.000 1 199 68 62 ILE CB C 36.266 0.000 1 200 68 62 ILE N N 111.593 0.000 1 201 69 63 PRO CA C 59.139 0.000 1 202 69 63 PRO CB C 29.582 0.000 1 203 70 64 ARG H H 8.370 0.000 1 204 70 64 ARG CA C 53.198 0.149 1 205 70 64 ARG CB C 27.057 0.074 1 206 70 64 ARG N N 125.566 0.000 1 207 71 65 SER H H 7.877 0.000 1 208 71 65 SER CA C 52.678 0.000 1 209 71 65 SER CB C 60.921 0.000 1 210 71 65 SER N N 116.426 0.000 1 211 76 70 LEU CA C 50.153 0.000 1 212 76 70 LEU CB C 42.801 0.000 1 213 77 71 GLN H H 8.922 0.000 1 214 77 71 GLN CA C 49.708 0.000 1 215 77 71 GLN CB C 32.478 0.000 1 216 77 71 GLN N N 121.230 0.000 1 217 80 74 HIS CA C 52.530 0.000 1 218 80 74 HIS CB C 30.102 0.000 1 219 81 75 ARG H H 8.025 0.000 1 220 81 75 ARG CA C 53.644 0.000 1 221 81 75 ARG CB C 25.646 0.074 1 222 81 75 ARG N N 122.051 0.000 1 223 82 76 LYS H H 8.101 0.000 1 224 82 76 LYS CA C 53.495 0.000 1 225 82 76 LYS CB C 25.832 0.112 1 226 82 76 LYS N N 121.079 0.000 1 227 83 77 GLY H H 8.356 0.000 1 228 83 77 GLY CA C 41.895 0.000 1 229 83 77 GLY N N 112.091 0.000 1 230 84 78 LEU H H 7.885 0.000 1 231 84 78 LEU CA C 49.856 0.000 1 232 84 78 LEU CB C 38.197 0.000 1 233 84 78 LEU N N 123.105 0.000 1 234 85 79 PRO CA C 60.253 0.000 1 235 85 79 PRO CB C 28.468 0.000 1 236 86 80 HIS H H 8.021 0.000 1 237 86 80 HIS CA C 53.346 0.000 1 238 86 80 HIS CB C 27.800 0.000 1 239 86 80 HIS N N 122.687 0.000 1 240 96 90 PRO CA C 61.813 0.000 1 241 96 90 PRO CB C 28.840 0.000 1 242 97 91 ASP H H 8.357 0.000 1 243 97 91 ASP CA C 49.708 0.075 1 244 97 91 ASP CB C 36.785 0.075 1 245 97 91 ASP N N 112.677 0.000 1 246 98 92 LEU H H 7.431 0.000 1 247 98 92 LEU CA C 53.569 0.000 1 248 98 92 LEU CB C 40.000 0.000 1 249 98 92 LEU N N 123.803 0.000 1 250 99 93 GLN CA C 53.866 0.000 1 251 99 93 GLN CB C 28.023 0.000 1 252 100 94 SER H H 7.893 0.000 1 253 100 94 SER CA C 54.015 0.000 1 254 100 94 SER CB C 62.629 0.000 1 255 100 94 SER N N 112.137 0.000 1 256 102 96 HIS CA C 57.505 0.000 1 257 102 96 HIS CB C 24.829 0.000 1 258 103 97 GLU H H 7.721 0.000 1 259 103 97 GLU CA C 55.389 0.037 1 260 103 97 GLU CB C 25.201 0.000 1 261 103 97 GLU N N 121.778 0.000 1 262 104 98 LEU H H 7.845 0.000 1 263 104 98 LEU CA C 54.015 0.000 1 264 104 98 LEU CB C 42.900 7.860 1 265 104 98 LEU N N 120.274 0.000 1 266 105 99 LYS H H 7.999 0.000 1 267 105 99 LYS CA C 57.357 0.000 1 268 105 99 LYS CB C 25.869 0.000 1 269 105 99 LYS N N 117.246 0.000 1 270 107 101 LEU CA C 51.341 0.000 1 271 107 101 LEU CB C 39.459 0.000 1 272 108 102 ASP H H 8.403 0.000 1 273 108 102 ASP CA C 53.718 0.074 1 274 108 102 ASP CB C 36.674 0.037 1 275 108 102 ASP N N 122.153 0.000 1 276 109 103 ILE H H 6.579 0.000 1 277 109 103 ILE CA C 57.802 0.000 1 278 109 103 ILE CB C 34.781 0.000 1 279 109 103 ILE N N 109.734 0.000 1 280 110 104 CYS H H 6.923 0.000 1 281 110 104 CYS CA C 59.213 0.000 1 282 110 104 CYS CB C 26.945 0.186 1 283 110 104 CYS N N 125.181 0.000 1 284 111 105 GLU H H 7.416 0.000 1 285 111 105 GLU CA C 54.015 0.074 1 286 111 105 GLU CB C 27.986 0.038 1 287 111 105 GLU N N 131.879 0.000 1 288 112 106 PHE H H 8.241 0.000 1 289 112 106 PHE CA C 51.787 0.000 1 290 112 106 PHE CB C 37.380 0.000 1 291 112 106 PHE N N 119.004 0.000 1 292 113 107 PRO CA C 64.483 0.000 1 293 113 107 PRO CB C 26.686 0.000 1 294 114 108 PHE H H 8.336 0.000 1 295 114 108 PHE CA C 51.639 0.148 1 296 114 108 PHE CB C 38.011 0.037 1 297 114 108 PHE N N 120.996 0.000 1 298 115 109 GLY H H 7.982 0.000 1 299 115 109 GLY CA C 42.207 0.000 1 300 115 109 GLY N N 121.230 0.000 1 301 116 110 SER H H 7.705 0.000 1 302 116 110 SER CA C 56.094 0.000 1 303 116 110 SER CB C 61.293 0.000 1 304 116 110 SER N N 115.958 0.000 1 305 119 113 LYS CA C 55.277 0.000 1 306 119 113 LYS CB C 29.211 0.000 1 307 120 114 GLU H H 7.230 0.000 1 308 120 114 GLU CA C 54.113 0.590 1 309 120 114 GLU CB C 28.988 0.000 1 310 120 114 GLU N N 117.598 0.000 1 311 121 115 VAL H H 9.023 0.000 1 312 121 115 VAL CA C 56.614 0.223 1 313 121 115 VAL CB C 32.441 0.037 1 314 121 115 VAL N N 119.444 0.000 1 315 122 116 CYS H H 8.949 0.000 1 316 122 116 CYS CA C 57.097 0.037 1 317 122 116 CYS CB C 27.577 0.074 1 318 122 116 CYS N N 128.738 0.000 1 319 123 117 ILE H H 8.938 0.000 1 320 123 117 ILE CA C 55.166 0.111 1 321 123 117 ILE CB C 34.298 0.037 1 322 123 117 ILE N N 120.644 0.000 1 323 124 118 ASN H H 8.622 0.000 1 324 124 118 ASN CA C 48.222 0.000 1 325 124 118 ASN CB C 35.300 0.000 1 326 124 118 ASN N N 121.335 0.000 1 327 126 120 TYR CB C 41.093 0.000 1 328 127 121 HIS H H 9.387 0.000 1 329 127 121 HIS CA C 53.606 0.111 1 330 127 121 HIS CB C 28.320 0.149 1 331 127 121 HIS N N 125.566 0.000 1 332 128 122 TYR H H 6.977 0.000 1 333 128 122 TYR CA C 53.941 0.074 1 334 128 122 TYR CB C 39.756 0.000 1 335 128 122 TYR N N 114.903 0.000 1 336 129 123 LYS H H 9.334 0.000 1 337 129 123 LYS CA C 50.970 0.000 1 338 129 123 LYS CB C 32.367 0.111 1 339 129 123 LYS N N 119.004 0.000 1 340 130 124 ARG H H 7.855 0.000 1 341 130 124 ARG CA C 51.490 0.000 1 342 130 124 ARG CB C 26.352 0.037 1 343 130 124 ARG N N 123.691 0.000 1 344 131 125 VAL H H 8.443 0.000 1 345 131 125 VAL CA C 57.617 0.038 1 346 131 125 VAL CB C 30.548 0.075 1 347 131 125 VAL N N 124.507 0.000 1 348 132 126 GLU H H 8.234 0.000 1 349 132 126 GLU CA C 53.272 0.000 1 350 132 126 GLU CB C 26.983 0.074 1 351 132 126 GLU N N 123.578 0.000 1 352 133 127 SER H H 8.288 0.000 1 353 133 127 SER CA C 52.752 0.000 1 354 133 127 SER CB C 60.179 0.000 1 355 133 127 SER N N 118.613 0.000 1 356 134 128 PRO CA C 60.030 0.000 1 357 135 129 VAL H H 7.996 0.000 1 358 135 129 VAL CA C 59.325 0.037 1 359 135 129 VAL CB C 28.840 0.000 1 360 135 129 VAL N N 121.481 0.000 1 361 136 130 LEU H H 8.117 0.000 1 362 136 130 LEU CA C 49.633 0.000 1 363 136 130 LEU CB C 37.900 0.000 1 364 136 130 LEU N N 128.962 0.000 1 stop_ save_