data_28113 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; revmodN_ACC ; _BMRB_accession_number 28113 _BMRB_flat_file_name bmr28113.str _Entry_type original _Submission_date 2020-04-11 _Accession_date 2020-04-11 _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 Liu Sheng . . 2 Refaei 'Mary Anne' . . 3 Decker Aaron . . 4 Hinerman Jennifer M. . 5 Herr Andrew B. . 6 Liu Shuohui . . 7 Howell Michael . . 8 Musier-Forsyth Karin . . 9 Tsang Pearl . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 68 "13C chemical shifts" 198 "15N chemical shifts" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-08-24 update BMRB 'update entry citation' 2020-07-01 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 18696 revmodN stop_ _Original_release_date 2020-04-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Hairpin RNA-induced conformational change of a eukaryotic-specific lysyl-tRNA synthetase extension and role of adjacent anticodon-binding domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32611767 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Sheng . . 2 Refaei Maryanne . . 3 Liu Shuohui . . 4 Decker Aaron . . 5 Hinerman Jennifer M. . 6 Herr Andrew B. . 7 Howell Mike . . 8 Musier-Forsyth Karin . . 9 Tsang Pearl . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 295 _Journal_issue 34 _Journal_ISSN 1083-351X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 12071 _Page_last 12085 _Year 2020 _Details . loop_ _Keyword 'Lysyl-tRNA synthetase' 'N-terminal extension' 'RNA binding' 'intrinsic disorder' 'segmental protein labeling' 'sortase A ligation' tRNAlys stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name revmodN-ACC _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Lysyl tRNA acceptor stem' $tRNAlys_Acceptor_stem revmodN $revmodN_protein stop_ _System_molecular_weight 19537.1 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'LysRS N-terminal extension complexed with Lysyl tRNA acceptor stem' save_ ######################## # Monomeric polymers # ######################## save_tRNAlys_Acceptor_stem _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class RNA _Name_common tRNAlys_Acceptor_stem _Molecular_mass 11225.8 _Mol_thiol_state 'not present' loop_ _Biological_function 'Lysyl tRNA is aminoacylated for protein biosynthesis' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; GCCCGGACAGGGUUCAAGUC CCUGUUCGGGCGCCA ; loop_ _Residue_seq_code _Residue_label 1 G 2 C 3 C 4 C 5 G 6 G 7 A 8 C 9 A 10 G 11 G 12 G 13 U 14 U 15 C 16 A 17 A 18 G 19 U 20 C 21 C 22 C 23 U 24 G 25 U 26 U 27 C 28 G 29 G 30 G 31 C 32 G 33 C 34 C 35 A stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_revmodN_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common revmodN_protein _Molecular_mass 8311.3 _Mol_thiol_state 'not present' loop_ _Biological_function 'Non-specific RNA binding domain of LysRS' stop_ _Details . _Residue_count 76 _Mol_residue_sequence ; MAAVQAAEVKVDGSEPKLSK NELKRRLKAEKKVAEKEAKQ KELSEKQLSQATAAATNHTT DNGVLPETGGHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ALA 4 VAL 5 GLN 6 ALA 7 ALA 8 GLU 9 VAL 10 LYS 11 VAL 12 ASP 13 GLY 14 SER 15 GLU 16 PRO 17 LYS 18 LEU 19 SER 20 LYS 21 ASN 22 GLU 23 LEU 24 LYS 25 ARG 26 ARG 27 LEU 28 LYS 29 ALA 30 GLU 31 LYS 32 LYS 33 VAL 34 ALA 35 GLU 36 LYS 37 GLU 38 ALA 39 LYS 40 GLN 41 LYS 42 GLU 43 LEU 44 SER 45 GLU 46 LYS 47 GLN 48 LEU 49 SER 50 GLN 51 ALA 52 THR 53 ALA 54 ALA 55 ALA 56 THR 57 ASN 58 HIS 59 THR 60 THR 61 ASP 62 ASN 63 GLY 64 VAL 65 LEU 66 PRO 67 GLU 68 THR 69 GLY 70 GLY 71 HIS 72 HIS 73 HIS 74 HIS 75 HIS 76 HIS 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 _Details $revmodN_protein Human 9606 Eukaryota Metazoa Homo sapiens KARS 'The revmodN protein corresponds to residues 1-69 of the human LysRS enzyme.' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $revmodN_protein 'recombinant technology' . Escherichia coli BL21 DE3 pet30a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'pH 6.0 and 0.02% sodium azide for sample preservation' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $revmodN_protein 200 uM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 15 mM 'natural abundance' 'potassium chloride' 35 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _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' 0.07 0.01 M pH 6.0 . pH pressure 1 . atm temperature 298 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 'DSS was internal' 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' '2D 1H-13C HSQC' '3D HNCA' '3D HN(CO)CA' '3D HNCO' '3D HNCACB' '3D CBCA(CO)NH' '3D H(CCO)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 revmodN _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 2 ALA C C 176.945 . . 2 2 2 ALA CA C 52.416 . . 3 2 2 ALA CB C 19.344 . . 4 3 3 ALA H H 8.415 . . 5 3 3 ALA C C 177.733 . . 6 3 3 ALA CA C 52.445 . . 7 3 3 ALA CB C 19.293 . . 8 3 3 ALA N N 125.064 . . 9 4 4 VAL H H 8.143 . . 10 4 4 VAL C C 176.176 . . 11 4 4 VAL CA C 62.29 . . 12 4 4 VAL CB C 32.932 . . 13 4 4 VAL N N 120.484 . . 14 5 5 GLN H H 8.448 . . 15 5 5 GLN C C 175.552 . . 16 5 5 GLN CA C 55.668 . . 17 5 5 GLN CB C 29.632 . . 18 5 5 GLN N N 125.327 . . 19 6 6 ALA H H 8.384 . . 20 6 6 ALA C C 177.353 . . 21 6 6 ALA CA C 52.56 . . 22 6 6 ALA CB C 19.349 . . 23 6 6 ALA N N 126.945 . . 24 7 7 ALA H H 8.269 . . 25 7 7 ALA C C 177.676 . . 26 7 7 ALA CA C 52.505 . . 27 7 7 ALA CB C 19.388 . . 28 7 7 ALA N N 123.982 . . 29 8 8 GLU H H 8.329 . . 30 8 8 GLU C C 176.302 . . 31 8 8 GLU CA C 56.463 . . 32 8 8 GLU CB C 30.452 . . 33 8 8 GLU N N 120.938 . . 34 9 9 VAL H H 8.17 . . 35 9 9 VAL C C 175.849 . . 36 9 9 VAL CA C 62.33 . . 37 9 9 VAL CB C 32.782 . . 38 9 9 VAL N N 123.136 . . 39 10 10 LYS H H 8.447 . . 40 10 10 LYS C C 176.454 . . 41 10 10 LYS CA C 55.957 . . 42 10 10 LYS CB C 33.174 . . 43 10 10 LYS N N 127.12 . . 44 11 11 VAL H H 8.337 . . 45 11 11 VAL C C 175.974 . . 46 11 11 VAL CA C 62.095 . . 47 11 11 VAL CB C 32.916 . . 48 11 11 VAL N N 122.994 . . 49 12 12 ASP H H 8.506 . . 50 12 12 ASP C C 176.794 . . 51 12 12 ASP CA C 54.419 . . 52 12 12 ASP CB C 41.348 . . 53 12 12 ASP N N 125.111 . . 54 13 13 GLY H H 8.459 . . 55 13 13 GLY C C 174.413 . . 56 13 13 GLY CA C 45.566 . . 57 13 13 GLY N N 110.867 . . 58 14 14 SER H H 8.241 . . 59 14 14 SER C C 174.262 . . 60 14 14 SER CA C 58.536 . . 61 14 14 SER CB C 64.035 . . 62 14 14 SER N N 116.424 . . 63 15 15 GLU H H 8.419 . . 64 15 15 GLU C C 174.45 . . 65 15 15 GLU CA C 54.658 . . 66 15 15 GLU CB C 29.627 . . 67 15 15 GLU N N 124.435 . . 68 16 16 PRO C C 176.692 . . 69 16 16 PRO CA C 63.224 . . 70 16 16 PRO CB C 32.13 . . 71 17 17 LYS H H 8.436 . . 72 17 17 LYS C C 176.452 . . 73 17 17 LYS CA C 56.037 . . 74 17 17 LYS CB C 32.95 . . 75 17 17 LYS N N 122.856 . . 76 18 18 LEU H H 8.239 . . 77 18 18 LEU C C 177.181 . . 78 18 18 LEU CA C 54.634 . . 79 18 18 LEU CB C 43.212 . . 80 18 18 LEU N N 125.097 . . 81 19 19 SER H H 8.671 . . 82 19 19 SER C C 174.68 . . 83 19 19 SER CA C 57.611 . . 84 19 19 SER N N 119.261 . . 85 20 20 LYS H H 8.878 . . 86 20 20 LYS C C 179.078 . . 87 20 20 LYS CA C 59.542 . . 88 20 20 LYS N N 123.477 . . 89 21 21 ASN H H 8.852 . . 90 21 21 ASN C C 177.544 . . 91 21 21 ASN CA C 55.629 . . 92 21 21 ASN N N 118.884 . . 93 22 22 GLU H H 8.091 . . 94 22 22 GLU C C 178.638 . . 95 22 22 GLU CA C 58.861 . . 96 22 22 GLU CB C 30.057 . . 97 22 22 GLU N N 122.875 . . 98 23 23 LEU H H 8.293 . . 99 23 23 LEU C C 179.029 . . 100 23 23 LEU CA C 57.995 . . 101 23 23 LEU N N 122.032 . . 102 24 24 LYS H H 8.029 . . 103 24 24 LYS C C 179.074 . . 104 24 24 LYS CA C 59.574 . . 105 24 24 LYS N N 119.833 . . 106 25 25 ARG H H 7.957 . . 107 25 25 ARG C C 179.246 . . 108 25 25 ARG CA C 59.526 . . 109 25 25 ARG N N 120.237 . . 110 26 26 ARG H H 8.223 . . 111 26 26 ARG C C 178.657 . . 112 26 26 ARG CA C 58.982 . . 113 26 26 ARG N N 121.607 . . 114 27 27 LEU H H 8.21 . . 115 27 27 LEU C C 179.689 . . 116 27 27 LEU CA C 57.524 . . 117 27 27 LEU N N 120.902 . . 118 28 28 LYS H H 7.991 . . 119 28 28 LYS C C 178.578 . . 120 28 28 LYS CA C 59.114 . . 121 28 28 LYS N N 120.59 . . 122 29 29 ALA H H 7.923 . . 123 29 29 ALA C C 180.094 . . 124 29 29 ALA CA C 54.7 . . 125 29 29 ALA N N 122.863 . . 126 30 30 GLU H H 8.15 . . 127 30 30 GLU C C 178.821 . . 128 30 30 GLU CA C 58.646 . . 129 30 30 GLU CB C 29.623 . . 130 30 30 GLU N N 119.262 . . 131 31 31 LYS H H 8.024 . . 132 31 31 LYS C C 178.149 . . 133 31 31 LYS CA C 58.515 . . 134 31 31 LYS N N 121.808 . . 135 32 32 LYS H H 7.927 . . 136 32 32 LYS C C 178.739 . . 137 32 32 LYS CA C 58.355 . . 138 32 32 LYS CB C 32.516 . . 139 32 32 LYS N N 120.702 . . 140 33 33 VAL H H 7.851 . . 141 33 33 VAL C C 177.502 . . 142 33 33 VAL CA C 65.19 . . 143 33 33 VAL N N 120.944 . . 144 34 34 ALA H H 8.023 . . 145 34 34 ALA C C 180.019 . . 146 34 34 ALA CA C 54.276 . . 147 34 34 ALA N N 124.746 . . 148 35 35 GLU H H 8.302 . . 149 35 35 GLU C C 178.184 . . 150 35 35 GLU CA C 58.354 . . 151 35 35 GLU CB C 29.686 . . 152 35 35 GLU N N 120.249 . . 153 36 36 LYS H H 8.047 . . 154 36 36 LYS C C 178.586 . . 155 36 36 LYS CA C 58.623 . . 156 36 36 LYS CB C 32.525 . . 157 36 36 LYS N N 121.786 . . 158 37 37 GLU H H 8.306 . . 159 37 37 GLU C C 178.104 . . 160 37 37 GLU CA C 58.301 . . 161 37 37 GLU CB C 29.727 . . 162 37 37 GLU N N 120.842 . . 163 38 38 ALA H H 8.118 . . 164 38 38 ALA C C 179.529 . . 165 38 38 ALA CA C 54.178 . . 166 38 38 ALA CB C 18.431 . . 167 38 38 ALA N N 123.915 . . 168 39 39 LYS H H 8.075 . . 169 39 39 LYS C C 178.06 . . 170 39 39 LYS CA C 57.736 . . 171 39 39 LYS CB C 32.519 . . 172 39 39 LYS N N 120.112 . . 173 40 40 GLN H H 8.135 . . 174 40 40 GLN C C 177.562 . . 175 40 40 GLN CA C 57.522 . . 176 40 40 GLN CB C 28.764 . . 177 40 40 GLN N N 120.413 . . 178 41 41 LYS H H 8.131 . . 179 41 41 LYS C C 177.675 . . 180 41 41 LYS CA C 58.113 . . 181 41 41 LYS CB C 32.814 . . 182 41 41 LYS N N 122.139 . . 183 42 42 GLU H H 8.135 . . 184 42 42 GLU C C 177.716 . . 185 42 42 GLU CA C 57.879 . . 186 42 42 GLU CB C 30.048 . . 187 42 42 GLU N N 121.161 . . 188 43 43 LEU H H 8.131 . . 189 43 43 LEU C C 178.458 . . 190 43 43 LEU CA C 56.418 . . 191 43 43 LEU CB C 42.16 . . 192 43 43 LEU N N 121.967 . . 193 44 44 SER H H 8.237 . . 194 44 44 SER C C 175.615 . . 195 44 44 SER CA C 59.711 . . 196 44 44 SER CB C 63.683 . . 197 44 44 SER N N 116.478 . . 198 45 45 GLU H H 8.275 . . 199 45 45 GLU C C 177.668 . . 200 45 45 GLU CA C 57.849 . . 201 45 45 GLU CB C 29.859 . . 202 45 45 GLU N N 122.59 . . 203 46 46 LYS H H 8.106 . . 204 46 46 LYS C C 177.428 . . 205 46 46 LYS CA C 57.48 . . 206 46 46 LYS CB C 32.769 . . 207 46 46 LYS N N 121.486 . . 208 47 47 GLN H H 8.182 . . 209 47 47 GLN C C 176.905 . . 210 47 47 GLN CA C 56.743 . . 211 47 47 GLN CB C 29.1 . . 212 47 47 GLN N N 120.694 . . 213 48 48 LEU H H 8.192 . . 214 48 48 LEU C C 178.052 . . 215 48 48 LEU CA C 55.973 . . 216 48 48 LEU CB C 42.282 . . 217 48 48 LEU N N 122.955 . . 218 49 49 SER H H 8.191 . . 219 49 49 SER C C 174.984 . . 220 49 49 SER CA C 58.962 . . 221 49 49 SER CB C 63.667 . . 222 49 49 SER N N 116.423 . . 223 50 50 GLN H H 8.256 . . 224 50 50 GLN C C 176.081 . . 225 50 50 GLN CA C 56.221 . . 226 50 50 GLN CB C 29.37 . . 227 50 50 GLN N N 122.436 . . 228 51 51 ALA H H 8.24 . . 229 51 51 ALA C C 178.24 . . 230 51 51 ALA CA C 53.106 . . 231 51 51 ALA CB C 19.2 . . 232 51 51 ALA N N 125.203 . . 233 52 52 THR H H 8.054 . . 234 52 52 THR C C 174.519 . . 235 52 52 THR CA C 62.109 . . 236 52 52 THR CB C 69.811 . . 237 52 52 THR N N 113.812 . . 238 53 53 ALA H H 8.209 . . 239 53 53 ALA C C 177.436 . . 240 53 53 ALA CA C 52.692 . . 241 53 53 ALA CB C 19.311 . . 242 53 53 ALA N N 127.086 . . 243 54 54 ALA H H 8.23 . . 244 54 54 ALA C C 177.854 . . 245 54 54 ALA CA C 52.722 . . 246 54 54 ALA CB C 19.117 . . 247 54 54 ALA N N 124.18 . . 248 55 55 ALA H H 8.172 . . 249 55 55 ALA C C 178.116 . . 250 55 55 ALA CA C 52.731 . . 251 55 55 ALA CB C 19.264 . . 252 55 55 ALA N N 123.47 . . 253 56 56 THR H H 8.041 . . 254 56 56 THR C C 174.284 . . 255 56 56 THR CA C 61.872 . . 256 56 56 THR CB C 69.826 . . 257 56 56 THR N N 113.145 . . 258 57 57 ASN H H 8.33 . . 259 57 57 ASN C C 174.871 . . 260 57 57 ASN CA C 53.24 . . 261 57 57 ASN CB C 38.896 . . 262 57 57 ASN N N 121.29 . . 263 58 58 HIS H H 8.483 . . 264 58 58 HIS C C 174.682 . . 265 58 58 HIS CA C 55.55 . . 266 58 58 HIS CB C 29.251 . . 267 58 58 HIS N N 119.997 . . 268 59 59 THR H H 8.32 . . 269 59 59 THR C C 174.834 . . 270 59 59 THR CA C 62.342 . . 271 59 59 THR CB C 69.845 . . 272 59 59 THR N N 116.331 . . 273 60 60 THR H H 8.182 . . 274 60 60 THR C C 174.124 . . 275 60 60 THR CA C 61.567 . . 276 60 60 THR CB C 69.86 . . 277 60 60 THR N N 115.681 . . 278 61 61 ASP H H 8.064 . . 279 61 61 ASP C C 175.998 . . 280 61 61 ASP CA C 54.243 . . 281 61 61 ASP CB C 41.213 . . 282 61 61 ASP N N 126.586 . . 283 62 62 ASN H H 7.995 . . 284 62 62 ASN C C 176.126 . . 285 62 62 ASN CA C 54.899 . . 286 62 62 ASN CB C 41.088 . . 287 62 62 ASN N N 124.603 . . 288 63 63 GLY H H 8.378 . . 289 63 63 GLY C C 174.026 . . 290 63 63 GLY CA C 45.578 . . 291 63 63 GLY N N 109.705 . . 292 64 64 VAL H H 8.082 . . 293 64 64 VAL C C 176.18 . . 294 64 64 VAL CA C 62.125 . . 295 64 64 VAL CB C 32.915 . . 296 64 64 VAL N N 120.102 . . 297 65 65 LEU H H 8.412 . . 298 65 65 LEU C C 175.242 . . 299 65 65 LEU CA C 52.982 . . 300 65 65 LEU CB C 41.757 . . 301 65 65 LEU N N 128.549 . . 302 66 66 PRO C C 176.975 . . 303 66 66 PRO CA C 63.073 . . 304 66 66 PRO CB C 32.152 . . 305 67 67 GLU H H 8.547 . . 306 67 67 GLU C C 176.913 . . 307 67 67 GLU CA C 56.609 . . 308 67 67 GLU CB C 30.228 . . 309 67 67 GLU N N 121.892 . . 310 68 68 THR H H 8.229 . . 311 68 68 THR C C 175.253 . . 312 68 68 THR CA C 61.83 . . 313 68 68 THR CB C 69.988 . . 314 68 68 THR N N 115.433 . . 315 69 69 GLY H H 8.477 . . 316 69 69 GLY C C 174.591 . . 317 69 69 GLY CA C 45.428 . . 318 69 69 GLY N N 111.786 . . 319 70 70 GLY H H 8.304 . . 320 70 70 GLY C C 173.919 . . 321 70 70 GLY CA C 45.191 . . 322 70 70 GLY N N 109.075 . . 323 71 71 HIS H H 8.421 . . 324 71 71 HIS CA C 55.36 . . 325 71 71 HIS CB C 29.2 . . 326 71 71 HIS N N 118.597 . . 327 75 75 HIS C C 173.688 . . 328 75 75 HIS CA C 55.592 . . 329 75 75 HIS CB C 29.409 . . 330 76 76 HIS H H 8.363 . . 331 76 76 HIS C C 178.915 . . 332 76 76 HIS CA C 57.032 . . 333 76 76 HIS CB C 29.751 . . 334 76 76 HIS N N 125.918 . . stop_ save_