data_27527 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments of the N-terminal domain of FAT10 ; _BMRB_accession_number 27527 _BMRB_flat_file_name bmr27527.str _Entry_type original _Submission_date 2018-06-26 _Accession_date 2018-06-26 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Aichem Annette . . 2 Anders Samira . . 3 Catone Nicola . . 4 Roessler Philip . . 5 Stotz Sophie . . 6 Berg Andrej . . 7 Schwab Ricarda . . 8 Scheuermann Sophia . . 9 Bialas Johanna . . 10 Schuetz-Stoffregen Mira . . 11 Schmidtke Gunter . . 12 Peter Christine . . 13 Groettrup Marcus . . 14 Wiesner Silke . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 74 "13C chemical shifts" 159 "15N chemical shifts" 74 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-11-07 update BMRB 'update entry citation' 2018-07-31 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27467 'FAT10 C-terminal domain' stop_ _Original_release_date 2018-06-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30127417 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Aichem Annette . . 2 Anders Samira . . 3 Catone Nicola . . 4 Roessler Philip . . 5 Stotz Sophie . . 6 Berg Andrej . . 7 Schwab Ricarda . . 8 Scheuermann Sophia . . 9 Bialas Johanna . . 10 Schuetz-Stoffregen Mira . . 11 Schmidtke Gunter . . 12 Peter Christine . . 13 Groettrup Marcus . . 14 Wiesner Silke . . stop_ _Journal_abbreviation 'Nat. Commun.' _Journal_name_full 'Nature communications' _Journal_volume 9 _Journal_issue 1 _Journal_ISSN 2041-1723 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3321 _Page_last 3321 _Year 2018 _Details . loop_ _Keyword FAT10 'Ubiquitin-like domain' degradation proteasome stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of FAT10' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ndomain $ndomain 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_ndomain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ndomain _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'proteasomal degradation' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 83 _Mol_residue_sequence ; GASTLTVHVRSEEWDLMTFD ANPYDSVKKIKEHVRSKTKV PVQDQVLLLGSKILKPRRSL SSYGIDKEKTIHLTLKVVKP SDE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 SER 4 THR 5 LEU 6 THR 7 VAL 8 HIS 9 VAL 10 ARG 11 SER 12 GLU 13 GLU 14 TRP 15 ASP 16 LEU 17 MET 18 THR 19 PHE 20 ASP 21 ALA 22 ASN 23 PRO 24 TYR 25 ASP 26 SER 27 VAL 28 LYS 29 LYS 30 ILE 31 LYS 32 GLU 33 HIS 34 VAL 35 ARG 36 SER 37 LYS 38 THR 39 LYS 40 VAL 41 PRO 42 VAL 43 GLN 44 ASP 45 GLN 46 VAL 47 LEU 48 LEU 49 LEU 50 GLY 51 SER 52 LYS 53 ILE 54 LEU 55 LYS 56 PRO 57 ARG 58 ARG 59 SER 60 LEU 61 SER 62 SER 63 TYR 64 GLY 65 ILE 66 ASP 67 LYS 68 GLU 69 LYS 70 THR 71 ILE 72 HIS 73 LEU 74 THR 75 LEU 76 LYS 77 VAL 78 VAL 79 LYS 80 PRO 81 SER 82 ASP 83 GLU 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 NCBI AAD52982.1 'ubiquitin-like protein FAT10 [Homo sapiens]' . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ndomain 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 $ndomain 'recombinant technology' . Escherichia coli BL21(DE3) pET-M30 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 $ndomain 1 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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 _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_C(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _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' 0.1 . M pH 7.5 . 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 water C 13 protons ppm 4.7 na indirect . . . 1 water H 1 protons ppm 4.7 internal indirect . . . 1 water N 15 protons ppm 4.7 na indirect . . . 1 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 C(CO)NH' 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 ndomain _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 3 3 SER CA C 60.185 0.000 . 2 3 3 SER CB C 54.637 0.000 . 3 4 4 THR H H 7.877 0.000 . 4 4 4 THR CA C 58.225 0.109 . 5 4 4 THR CB C 67.040 0.084 . 6 4 4 THR N N 113.859 0.000 . 7 5 5 LEU H H 8.689 0.000 . 8 5 5 LEU CA C 50.427 0.000 . 9 5 5 LEU CB C 40.902 0.000 . 10 5 5 LEU N N 123.174 0.000 . 11 6 6 THR H H 8.383 0.000 . 12 6 6 THR CA C 59.185 0.223 . 13 6 6 THR CB C 66.179 0.164 . 14 6 6 THR N N 120.867 0.000 . 15 7 7 VAL H H 9.034 0.000 . 16 7 7 VAL CA C 56.979 0.085 . 17 7 7 VAL CB C 29.623 0.092 . 18 7 7 VAL N N 127.265 0.000 . 19 8 8 HIS H H 8.646 0.000 . 20 8 8 HIS CA C 50.542 0.000 . 21 8 8 HIS CB C 29.097 0.130 . 22 8 8 HIS N N 125.640 0.000 . 23 9 9 VAL H H 9.476 0.000 . 24 9 9 VAL CA C 58.526 0.095 . 25 9 9 VAL CB C 30.230 0.000 . 26 9 9 VAL N N 122.492 0.000 . 27 10 10 ARG H H 8.304 0.000 . 28 10 10 ARG CA C 51.689 0.000 . 29 10 10 ARG CB C 29.197 0.000 . 30 10 10 ARG N N 126.319 0.099 . 31 11 11 SER H H 8.999 0.000 . 32 11 11 SER CA C 54.289 0.155 . 33 11 11 SER CB C 63.682 0.172 . 34 11 11 SER N N 117.210 0.000 . 35 12 12 GLU H H 9.110 0.000 . 36 12 12 GLU CA C 54.915 0.000 . 37 12 12 GLU CB C 26.804 0.000 . 38 12 12 GLU N N 119.063 0.000 . 39 13 13 GLU H H 8.063 0.000 . 40 13 13 GLU CA C 54.060 0.269 . 41 13 13 GLU CB C 26.078 0.120 . 42 13 13 GLU N N 115.484 0.000 . 43 14 14 TRP H H 7.741 0.000 . 44 14 14 TRP CA C 54.439 0.084 . 45 14 14 TRP CB C 27.757 0.200 . 46 14 14 TRP N N 117.921 0.000 . 47 15 15 ASP H H 8.428 0.000 . 48 15 15 ASP CA C 51.087 0.116 . 49 15 15 ASP CB C 37.876 0.000 . 50 15 15 ASP N N 120.257 0.000 . 51 16 16 LEU H H 8.438 0.000 . 52 16 16 LEU CA C 53.388 0.160 . 53 16 16 LEU CB C 39.492 0.088 . 54 16 16 LEU N N 124.015 0.000 . 55 17 17 MET H H 8.181 0.000 . 56 17 17 MET CA C 50.944 0.162 . 57 17 17 MET CB C 33.888 0.125 . 58 17 17 MET N N 126.757 0.000 . 59 18 18 THR H H 8.103 0.000 . 60 18 18 THR CA C 57.652 0.194 . 61 18 18 THR CB C 67.951 0.150 . 62 18 18 THR N N 117.718 0.000 . 63 19 19 PHE H H 8.885 0.000 . 64 19 19 PHE CA C 51.951 0.229 . 65 19 19 PHE CB C 38.198 0.016 . 66 19 19 PHE N N 123.507 0.000 . 67 20 20 ASP H H 8.349 0.000 . 68 20 20 ASP CA C 50.322 0.198 . 69 20 20 ASP CB C 38.486 0.117 . 70 20 20 ASP N N 121.679 0.000 . 71 21 21 ALA H H 8.796 0.000 . 72 21 21 ALA CA C 47.542 0.145 . 73 21 21 ALA CB C 19.132 0.132 . 74 21 21 ALA N N 123.304 0.000 . 75 22 22 ASN H H 8.642 0.000 . 76 22 22 ASN CA C 47.199 0.000 . 77 22 22 ASN CB C 36.650 0.000 . 78 22 22 ASN N N 119.343 0.000 . 79 23 23 PRO CA C 61.407 0.000 . 80 23 23 PRO CB C 28.027 0.000 . 81 24 24 TYR H H 7.299 0.000 . 82 24 24 TYR CA C 53.196 0.156 . 83 24 24 TYR CB C 33.553 0.167 . 84 24 24 TYR N N 110.914 0.000 . 85 25 25 ASP H H 7.724 0.000 . 86 25 25 ASP CA C 51.613 0.079 . 87 25 25 ASP CB C 38.246 0.064 . 88 25 25 ASP N N 123.203 0.000 . 89 26 26 SER H H 8.347 0.000 . 90 26 26 SER CA C 53.577 0.068 . 91 26 26 SER CB C 61.339 0.120 . 92 26 26 SER N N 115.078 0.000 . 93 27 27 VAL H H 8.744 0.000 . 94 27 27 VAL CA C 62.826 0.196 . 95 27 27 VAL CB C 27.757 0.200 . 96 27 27 VAL N N 122.898 0.000 . 97 28 28 LYS H H 8.811 0.000 . 98 28 28 LYS CA C 56.645 0.126 . 99 28 28 LYS CB C 28.714 0.123 . 100 28 28 LYS N N 121.375 0.000 . 101 29 29 LYS H H 7.804 0.000 . 102 29 29 LYS CA C 55.541 0.058 . 103 29 29 LYS CB C 28.283 0.162 . 104 29 29 LYS N N 119.343 0.000 . 105 30 30 ILE H H 7.397 0.000 . 106 30 30 ILE CA C 59.663 0.136 . 107 30 30 ILE CB C 31.541 0.128 . 108 30 30 ILE N N 117.617 0.000 . 109 31 31 LYS H H 7.944 0.000 . 110 31 31 LYS CA C 55.975 0.210 . 111 31 31 LYS CB C 29.767 0.142 . 112 31 31 LYS N N 118.835 0.000 . 113 32 32 GLU H H 8.309 0.000 . 114 32 32 GLU CA C 56.216 0.262 . 115 32 32 GLU CB C 24.594 0.000 . 116 32 32 GLU N N 121.781 0.000 . 117 33 33 HIS H H 7.677 0.000 . 118 33 33 HIS CA C 55.718 0.235 . 119 33 33 HIS CB C 24.642 0.094 . 120 33 33 HIS N N 122.289 0.000 . 121 34 34 VAL H H 8.411 0.000 . 122 34 34 VAL CA C 63.066 0.248 . 123 34 34 VAL CB C 27.514 0.052 . 124 34 34 VAL N N 121.161 0.000 . 125 35 35 ARG H H 8.963 0.000 . 126 35 35 ARG CA C 56.022 0.163 . 127 35 35 ARG CB C 26.221 0.075 . 128 35 35 ARG N N 125.843 0.000 . 129 36 36 SER H H 8.023 0.000 . 130 36 36 SER CA C 58.230 0.000 . 131 36 36 SER CB C 59.492 0.115 . 132 36 36 SER N N 116.601 0.000 . 133 37 37 LYS H H 7.098 0.000 . 134 37 37 LYS CA C 53.423 0.102 . 135 37 37 LYS CB C 30.429 0.146 . 136 37 37 LYS N N 117.414 0.000 . 137 38 38 THR H H 7.913 0.000 . 138 38 38 THR CA C 59.135 0.078 . 139 38 38 THR CB C 68.861 0.119 . 140 38 38 THR N N 107.257 0.000 . 141 39 39 LYS H H 8.473 0.000 . 142 39 39 LYS CA C 54.439 0.084 . 143 39 39 LYS CB C 26.125 0.073 . 144 39 39 LYS N N 115.992 0.000 . 145 40 40 VAL H H 7.896 0.000 . 146 40 40 VAL CA C 58.334 0.000 . 147 40 40 VAL CB C 29.520 0.000 . 148 40 40 VAL N N 125.841 0.000 . 149 41 41 PRO CA C 59.339 0.000 . 150 41 41 PRO CB C 29.155 0.000 . 151 42 42 VAL H H 8.463 0.000 . 152 42 42 VAL CA C 62.875 0.151 . 153 42 42 VAL CB C 27.777 0.032 . 154 42 42 VAL N N 119.750 0.000 . 155 43 43 GLN H H 8.918 0.000 . 156 43 43 GLN CA C 54.275 0.202 . 157 43 43 GLN CB C 23.990 0.101 . 158 43 43 GLN N N 116.906 0.000 . 159 44 44 ASP H H 7.586 0.000 . 160 44 44 ASP CA C 50.630 0.130 . 161 44 44 ASP CB C 37.732 0.020 . 162 44 44 ASP N N 120.359 0.000 . 163 45 45 GLN H H 7.100 0.003 . 164 45 45 GLN CA C 52.133 0.129 . 165 45 45 GLN CB C 28.560 0.063 . 166 45 45 GLN N N 117.426 0.012 . 167 46 46 VAL H H 9.194 0.000 . 168 46 46 VAL CA C 58.695 0.109 . 169 46 46 VAL CB C 30.324 0.135 . 170 46 46 VAL N N 125.640 0.000 . 171 47 47 LEU H H 8.736 0.000 . 172 47 47 LEU CA C 49.167 0.112 . 173 47 47 LEU CB C 42.050 0.000 . 174 47 47 LEU N N 126.046 0.000 . 175 48 48 LEU H H 9.177 0.000 . 176 48 48 LEU CA C 51.001 0.000 . 177 48 48 LEU CB C 41.476 0.000 . 178 48 48 LEU N N 121.501 0.000 . 179 49 49 LEU H H 8.573 0.000 . 180 49 49 LEU CA C 49.853 0.000 . 181 49 49 LEU CB C 40.558 0.000 . 182 49 49 LEU N N 124.015 0.000 . 183 51 51 SER CA C 54.637 0.000 . 184 51 51 SER CB C 60.185 0.000 . 185 52 52 LYS H H 8.053 0.000 . 186 52 52 LYS CA C 52.188 0.090 . 187 52 52 LYS CB C 29.861 0.049 . 188 52 52 LYS N N 124.320 0.000 . 189 53 53 ILE H H 8.465 0.000 . 190 53 53 ILE CA C 58.753 0.167 . 191 53 53 ILE CB C 35.133 0.149 . 192 53 53 ILE N N 126.148 0.000 . 193 54 54 LEU H H 8.618 0.000 . 194 54 54 LEU CA C 50.605 0.011 . 195 54 54 LEU CB C 38.727 0.169 . 196 54 54 LEU N N 127.976 0.000 . 197 55 55 LYS H H 8.148 0.000 . 198 55 55 LYS CA C 50.324 0.000 . 199 55 55 LYS CB C 29.227 0.000 . 200 55 55 LYS N N 124.015 0.000 . 201 56 56 PRO CA C 61.407 0.000 . 202 56 56 PRO CB C 29.061 0.000 . 203 57 57 ARG H H 8.325 0.000 . 204 57 57 ARG CA C 53.339 0.111 . 205 57 57 ARG CB C 26.174 0.122 . 206 57 57 ARG N N 112.843 0.000 . 207 58 58 ARG H H 7.613 0.000 . 208 58 58 ARG CA C 51.566 0.126 . 209 58 58 ARG CB C 28.809 0.125 . 210 58 58 ARG N N 119.546 0.000 . 211 59 59 SER H H 8.560 0.000 . 212 59 59 SER CA C 53.145 0.012 . 213 59 59 SER CB C 61.963 0.180 . 214 59 59 SER N N 114.062 0.000 . 215 60 60 LEU H H 8.657 0.000 . 216 60 60 LEU CA C 55.591 0.202 . 217 60 60 LEU CB C 36.953 0.087 . 218 60 60 LEU N N 123.174 0.000 . 219 61 61 SER H H 8.726 0.000 . 220 61 61 SER CA C 57.458 0.094 . 221 61 61 SER CB C 59.136 0.174 . 222 61 61 SER N N 113.351 0.000 . 223 62 62 SER H H 8.081 0.000 . 224 62 62 SER CA C 57.697 0.051 . 225 62 62 SER CB C 59.471 0.132 . 226 62 62 SER N N 118.937 0.000 . 227 63 63 TYR H H 7.797 0.000 . 228 63 63 TYR CA C 56.452 0.122 . 229 63 63 TYR CB C 35.040 0.243 . 230 63 63 TYR N N 120.968 0.000 . 231 64 64 GLY H H 8.101 0.000 . 232 64 64 GLY CA C 42.655 0.148 . 233 64 64 GLY N N 108.070 0.000 . 234 65 65 ILE H H 7.168 0.000 . 235 65 65 ILE CA C 57.507 0.143 . 236 65 65 ILE CB C 34.079 0.128 . 237 65 65 ILE N N 117.820 0.000 . 238 66 66 ASP H H 8.893 0.000 . 239 66 66 ASP CA C 52.000 0.278 . 240 66 66 ASP CB C 38.033 0.000 . 241 66 66 ASP N N 122.898 0.000 . 242 67 67 LYS H H 8.314 0.000 . 243 67 67 LYS CA C 53.244 0.205 . 244 67 67 LYS CB C 29.003 0.224 . 245 67 67 LYS N N 118.260 0.000 . 246 68 68 GLU H H 8.574 0.000 . 247 68 68 GLU CA C 53.938 0.000 . 248 68 68 GLU CB C 26.561 0.321 . 249 68 68 GLU N N 120.257 0.000 . 250 69 69 LYS H H 8.344 0.000 . 251 69 69 LYS CA C 53.525 0.000 . 252 69 69 LYS CB C 29.542 0.000 . 253 69 69 LYS N N 118.328 0.000 . 254 70 70 THR H H 7.728 0.000 . 255 70 70 THR CA C 57.460 0.190 . 256 70 70 THR CB C 67.808 0.195 . 257 70 70 THR N N 114.671 0.000 . 258 71 71 ILE H H 8.531 0.000 . 259 71 71 ILE CA C 55.830 0.159 . 260 71 71 ILE CB C 37.961 0.155 . 261 71 71 ILE N N 121.781 0.000 . 262 72 72 HIS H H 8.517 0.000 . 263 72 72 HIS CA C 52.474 0.000 . 264 72 72 HIS CB C 36.380 11.587 . 265 72 72 HIS N N 124.523 0.000 . 266 73 73 LEU H H 9.380 0.000 . 267 73 73 LEU CA C 49.348 0.000 . 268 73 73 LEU CB C 41.650 0.177 . 269 73 73 LEU N N 122.695 0.000 . 270 74 74 THR H H 9.188 0.000 . 271 74 74 THR CA C 58.275 0.253 . 272 74 74 THR CB C 67.759 0.146 . 273 74 74 THR N N 118.734 0.000 . 274 75 75 LEU H H 8.884 0.000 . 275 75 75 LEU CA C 50.130 0.194 . 276 75 75 LEU CB C 41.267 0.170 . 277 75 75 LEU N N 126.757 0.000 . 278 76 76 LYS H H 9.530 0.000 . 279 76 76 LYS CA C 51.231 0.167 . 280 76 76 LYS CB C 31.781 0.181 . 281 76 76 LYS N N 128.789 0.000 . 282 77 77 VAL H H 8.639 0.000 . 283 77 77 VAL CA C 58.001 0.000 . 284 77 77 VAL CB C 29.910 0.097 . 285 77 77 VAL N N 122.187 0.000 . 286 78 78 VAL H H 8.817 0.000 . 287 78 78 VAL CA C 58.230 0.000 . 288 78 78 VAL CB C 30.189 0.000 . 289 78 78 VAL N N 127.976 0.000 . 290 79 79 LYS H H 8.968 0.000 . 291 79 79 LYS CA C 51.804 0.000 . 292 79 79 LYS CB C 29.227 0.000 . 293 79 79 LYS N N 130.312 0.000 . 294 80 80 PRO CA C 59.607 0.000 . 295 80 80 PRO CB C 28.591 0.000 . 296 81 81 SER H H 8.374 0.000 . 297 81 81 SER CA C 54.770 0.133 . 298 81 81 SER CB C 60.506 0.133 . 299 81 81 SER N N 115.449 0.000 . 300 82 82 ASP H H 8.399 0.000 . 301 82 82 ASP CA C 51.137 0.021 . 302 82 82 ASP CB C 37.783 0.093 . 303 82 82 ASP N N 123.000 0.000 . 304 83 83 GLU H H 7.880 0.000 . 305 83 83 GLU CA C 54.673 0.000 . 306 83 83 GLU CB C 27.706 0.000 . 307 83 83 GLU N N 125.640 0.000 . stop_ save_