data_27016 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the DHDD Region of GbnD4 KS14 from the Gladiolin Polyketide Synthase ; _BMRB_accession_number 27016 _BMRB_flat_file_name bmr27016.str _Entry_type original _Submission_date 2017-01-27 _Accession_date 2017-01-27 _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 Jenner Matthew . . 2 Kosol Simone . . 3 Lewandowski Jozef R. . 4 Challis Gregory L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 69 "13C chemical shifts" 230 "15N chemical shifts" 69 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-03-22 update BMRB 'update entry citation' 2017-12-12 original author 'original release' stop_ _Original_release_date 2017-01-30 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Mechanism of intersubunit ketosynthase-dehydratase interaction in polyketide synthases ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29309054 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jenner Matthew . . 2 Kosol Simone . . 3 Griffiths Daniel . . 4 Prasongpolchai Panward . . 5 Manzi Lucio . . 6 Barrow Andrew S. . 7 Moses John E. . 8 Oldham Neil J. . 9 Lewandowski Jozef R. . 10 Challis Gregory L. . stop_ _Journal_abbreviation 'Nat. Chem. Biol.' _Journal_name_full 'Nature chemical biology' _Journal_volume 14 _Journal_issue 3 _Journal_ISSN 1552-4469 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 270 _Page_last 275 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Gladiolin binding domain monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Protein DHDD' $DHDD stop_ _System_molecular_weight 9995.1 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DHDD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DHDD _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'Polyketide synthase module communication' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 91 _Mol_residue_sequence ; MKHHHHHHHHGGLVPRGSHG SDEGVPDALRADTVPRAGPV RYARRRYWIGEARSDALAPA APLEREPLPAEAMGAYFAIR RTDADDTVAAH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 GLY 12 GLY 13 LEU 14 VAL 15 PRO 16 ARG 17 GLY 18 SER 19 HIS 20 GLY 21 SER 22 ASP 23 GLU 24 GLY 25 VAL 26 PRO 27 ASP 28 ALA 29 LEU 30 ARG 31 ALA 32 ASP 33 THR 34 VAL 35 PRO 36 ARG 37 ALA 38 GLY 39 PRO 40 VAL 41 ARG 42 TYR 43 ALA 44 ARG 45 ARG 46 ARG 47 TYR 48 TRP 49 ILE 50 GLY 51 GLU 52 ALA 53 ARG 54 SER 55 ASP 56 ALA 57 LEU 58 ALA 59 PRO 60 ALA 61 ALA 62 PRO 63 LEU 64 GLU 65 ARG 66 GLU 67 PRO 68 LEU 69 PRO 70 ALA 71 GLU 72 ALA 73 MET 74 GLY 75 ALA 76 TYR 77 PHE 78 ALA 79 ILE 80 ARG 81 ARG 82 THR 83 ASP 84 ALA 85 ASP 86 ASP 87 THR 88 VAL 89 ALA 90 ALA 91 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 $DHDD 'Burkholderia gladioli' 28095 Bacteria . Burkholderia gladioli 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 $DHDD 'recombinant technology' . Escherichia coli . pet24a 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $DHDD 0.3 mM 0.1 0.5 '[U-99% 13C; U-99% 15N]' 'potassium phosphate' 50 mM . . 'natural abundance' 'sodium chloride' 200 mM . . 'natural abundance' DSS 50 uM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_CcpNMR _Saveframe_category software _Name CcpNMR _Version 2.4.1 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 _Field_strength 700 _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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.28 . M pH 6.8 . pH pressure 1 . atm temperature 280 . 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 HNCA' '3D HNCO' '3D HNCACB' '3D HN(CO)CA' '3D HN(CA)CO' '3D CBCA(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 'Protein DHDD' _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 LYS C C 175.581 . 1 2 2 2 LYS CA C 55.999 . 1 3 2 2 LYS CB C 32.740 . 1 4 3 3 HIS H H 8.401 . 1 5 3 3 HIS C C 174.236 . 1 6 3 3 HIS CA C 55.551 . 1 7 3 3 HIS CB C 29.774 . 1 8 3 3 HIS N N 120.949 . 1 9 4 4 HIS H H 8.491 . 1 10 4 4 HIS N N 121.040 . 1 11 10 10 HIS C C 175.260 . 1 12 10 10 HIS CA C 55.927 . 1 13 10 10 HIS CB C 29.636 . 1 14 11 11 GLY H H 8.399 . 1 15 11 11 GLY C C 174.284 . 1 16 11 11 GLY CA C 45.279 . 1 17 11 11 GLY N N 110.626 . 1 18 12 12 GLY H H 8.169 . 1 19 12 12 GLY C C 173.680 . 1 20 12 12 GLY CA C 44.769 . 1 21 12 12 GLY N N 108.788 . 1 22 13 13 LEU H H 8.011 . 1 23 13 13 LEU C C 177.063 . 1 24 13 13 LEU CA C 55.011 . 1 25 13 13 LEU CB C 46.425 . 1 26 13 13 LEU N N 121.446 . 1 27 14 14 VAL H H 8.018 . 1 28 14 14 VAL C C 174.098 . 1 29 14 14 VAL CA C 59.608 . 1 30 14 14 VAL CB C 32.335 . 1 31 14 14 VAL N N 123.044 . 1 32 15 15 PRO C C 176.652 . 1 33 15 15 PRO CA C 62.947 . 1 34 15 15 PRO CB C 31.720 . 1 35 16 16 ARG H H 8.377 . 1 36 16 16 ARG C C 176.888 . 1 37 16 16 ARG CA C 56.322 . 1 38 16 16 ARG CB C 30.622 . 1 39 16 16 ARG N N 122.221 . 1 40 17 17 GLY H H 8.369 . 1 41 17 17 GLY C C 173.955 . 1 42 17 17 GLY CA C 44.920 . 1 43 17 17 GLY N N 110.470 . 1 44 18 18 SER H H 8.071 . 1 45 18 18 SER C C 174.260 . 1 46 18 18 SER CA C 58.200 . 1 47 18 18 SER CB C 63.625 . 1 48 18 18 SER N N 115.505 . 1 49 19 19 HIS H H 8.425 . 1 50 19 19 HIS C C 175.085 . 1 51 19 19 HIS CA C 55.735 . 1 52 19 19 HIS CB C 29.337 . 1 53 19 19 HIS N N 120.625 . 1 54 20 20 GLY H H 8.313 . 1 55 20 20 GLY C C 174.019 . 1 56 20 20 GLY CA C 45.108 . 1 57 20 20 GLY N N 110.221 . 1 58 21 21 SER H H 8.159 . 1 59 21 21 SER C C 174.181 . 1 60 21 21 SER CA C 58.216 . 1 61 21 21 SER CB C 63.607 . 1 62 21 21 SER N N 115.787 . 1 63 22 22 ASP H H 8.297 . 1 64 22 22 ASP C C 176.023 . 1 65 22 22 ASP CA C 54.118 . 1 66 22 22 ASP CB C 40.624 . 1 67 22 22 ASP N N 122.087 . 1 68 23 23 GLU H H 8.137 . 1 69 23 23 GLU C C 176.711 . 1 70 23 23 GLU CA C 56.562 . 1 71 23 23 GLU CB C 29.857 . 1 72 23 23 GLU N N 120.780 . 1 73 24 24 GLY H H 8.241 . 1 74 24 24 GLY C C 173.529 . 1 75 24 24 GLY CA C 44.855 . 1 76 24 24 GLY N N 109.594 . 1 77 25 25 VAL H H 7.817 . 1 78 25 25 VAL C C 174.385 . 1 79 25 25 VAL CA C 59.704 . 1 80 25 25 VAL CB C 32.308 . 1 81 25 25 VAL N N 121.059 . 1 82 26 26 PRO C C 176.566 . 1 83 26 26 PRO CA C 63.054 . 1 84 26 26 PRO CB C 31.835 . 1 85 27 27 ASP H H 8.264 . 1 86 27 27 ASP C C 176.348 . 1 87 27 27 ASP CA C 54.648 . 1 88 27 27 ASP CB C 40.742 . 1 89 27 27 ASP N N 120.914 . 1 90 28 28 ALA H H 8.135 . 1 91 28 28 ALA C C 177.699 . 1 92 28 28 ALA CA C 52.777 . 1 93 28 28 ALA CB C 18.800 . 1 94 28 28 ALA N N 123.624 . 1 95 29 29 LEU H H 7.962 . 1 96 29 29 LEU C C 177.257 . 1 97 29 29 LEU CA C 54.725 . 1 98 29 29 LEU CB C 41.886 . 1 99 29 29 LEU N N 119.713 . 1 100 30 30 ARG H H 7.862 . 1 101 30 30 ARG C C 175.895 . 1 102 30 30 ARG CA C 55.872 . 1 103 30 30 ARG CB C 30.629 . 1 104 30 30 ARG N N 121.727 . 1 105 31 31 ALA H H 8.195 . 1 106 31 31 ALA C C 177.289 . 1 107 31 31 ALA CA C 52.237 . 1 108 31 31 ALA CB C 19.061 . 1 109 31 31 ALA N N 125.254 . 1 110 32 32 ASP H H 8.174 . 1 111 32 32 ASP C C 176.215 . 1 112 32 32 ASP CA C 54.032 . 1 113 32 32 ASP CB C 40.783 . 1 114 32 32 ASP N N 119.035 . 1 115 33 33 THR H H 7.838 . 1 116 33 33 THR C C 174.209 . 1 117 33 33 THR CA C 61.682 . 1 118 33 33 THR CB C 69.850 . 1 119 33 33 THR N N 113.898 . 1 120 34 34 VAL H H 7.921 . 1 121 34 34 VAL C C 174.074 . 1 122 34 34 VAL CA C 59.872 . 1 123 34 34 VAL CB C 32.341 . 1 124 34 34 VAL N N 124.354 . 1 125 35 35 PRO C C 176.512 . 1 126 35 35 PRO CA C 62.760 . 1 127 35 35 PRO CB C 31.756 . 1 128 36 36 ARG H H 8.286 . 1 129 36 36 ARG C C 175.870 . 1 130 36 36 ARG CA C 55.796 . 1 131 36 36 ARG CB C 30.612 . 1 132 36 36 ARG N N 122.063 . 1 133 37 37 ALA H H 8.232 . 1 134 37 37 ALA C C 177.453 . 1 135 37 37 ALA CA C 52.234 . 1 136 37 37 ALA CB C 19.511 . 1 137 37 37 ALA N N 125.514 . 1 138 38 38 GLY H H 8.042 . 1 139 38 38 GLY C C 171.337 . 1 140 38 38 GLY CA C 44.235 . 1 141 38 38 GLY N N 108.598 . 1 142 40 40 VAL C C 175.827 . 1 143 40 40 VAL CA C 62.318 . 1 144 40 40 VAL CB C 32.402 . 1 145 41 41 ARG H H 8.154 . 1 146 41 41 ARG C C 175.465 . 1 147 41 41 ARG CA C 55.606 . 1 148 41 41 ARG CB C 30.620 . 1 149 41 41 ARG N N 124.973 . 1 150 42 42 TYR H H 8.034 . 1 151 42 42 TYR C C 175.184 . 1 152 42 42 TYR CA C 57.372 . 1 153 42 42 TYR CB C 38.588 . 1 154 42 42 TYR N N 121.497 . 1 155 43 43 ALA H H 8.090 . 1 156 43 43 ALA C C 177.069 . 1 157 43 43 ALA CA C 52.445 . 1 158 43 43 ALA CB C 19.180 . 1 159 43 43 ALA N N 125.251 . 1 160 44 44 ARG H H 8.074 . 1 161 44 44 ARG C C 176.063 . 1 162 44 44 ARG CA C 55.983 . 1 163 44 44 ARG CB C 30.504 . 1 164 44 44 ARG N N 120.188 . 1 165 48 48 TRP C C 175.586 . 1 166 49 49 ILE H H 7.832 . 1 167 49 49 ILE C C 175.947 . 1 168 49 49 ILE CA C 61.261 . 1 169 49 49 ILE CB C 38.500 . 1 170 49 49 ILE N N 123.137 . 1 171 50 50 GLY H H 7.634 . 1 172 50 50 GLY C C 173.600 . 1 173 50 50 GLY CA C 44.746 . 1 174 50 50 GLY N N 112.070 . 1 175 51 51 GLU H H 7.940 . 1 176 51 51 GLU C C 175.954 . 1 177 51 51 GLU CA C 56.125 . 1 178 51 51 GLU CB C 30.265 . 1 179 51 51 GLU N N 120.500 . 1 180 52 52 ALA C C 177.405 . 1 181 52 52 ALA CA C 52.298 . 1 182 52 52 ALA CB C 18.806 . 1 183 53 53 ARG H H 8.120 . 1 184 53 53 ARG C C 176.372 . 1 185 53 53 ARG CA C 55.870 . 1 186 53 53 ARG CB C 30.854 . 1 187 53 53 ARG N N 120.597 . 1 188 54 54 SER H H 8.221 . 1 189 54 54 SER C C 174.126 . 1 190 54 54 SER CA C 58.275 . 1 191 54 54 SER CB C 63.508 . 1 192 54 54 SER N N 116.994 . 1 193 55 55 ASP H H 8.159 . 1 194 55 55 ASP C C 175.741 . 1 195 55 55 ASP CA C 53.814 . 1 196 55 55 ASP CB C 40.592 . 1 197 55 55 ASP N N 122.086 . 1 198 56 56 ALA H H 7.906 . 1 199 56 56 ALA C C 177.429 . 1 200 56 56 ALA CA C 52.524 . 1 201 56 56 ALA CB C 18.983 . 1 202 56 56 ALA N N 123.379 . 1 203 57 57 LEU H H 7.932 . 1 204 57 57 LEU C C 176.562 . 1 205 57 57 LEU CA C 54.372 . 1 206 57 57 LEU CB C 41.974 . 1 207 57 57 LEU N N 120.174 . 1 208 58 58 ALA H H 7.924 . 1 209 58 58 ALA C C 174.978 . 1 210 58 58 ALA CA C 50.219 . 1 211 58 58 ALA CB C 17.682 . 1 212 58 58 ALA N N 125.892 . 1 213 59 59 PRO C C 176.310 . 1 214 59 59 PRO CA C 62.589 . 1 215 59 59 PRO CB C 32.020 . 1 216 60 60 ALA H H 8.215 . 1 217 60 60 ALA C C 176.843 . 1 218 60 60 ALA CA C 51.725 . 1 219 60 60 ALA CB C 19.065 . 1 220 60 60 ALA N N 124.534 . 1 221 61 61 ALA H H 8.095 . 1 222 61 61 ALA C C 175.215 . 1 223 61 61 ALA CA C 50.203 . 1 224 61 61 ALA CB C 17.703 . 1 225 61 61 ALA N N 124.686 . 1 226 62 62 PRO C C 176.618 . 1 227 62 62 PRO CA C 62.785 . 1 228 62 62 PRO CB C 31.769 . 1 229 63 63 LEU H H 8.194 . 1 230 63 63 LEU C C 177.332 . 1 231 63 63 LEU CA C 54.811 . 1 232 63 63 LEU CB C 42.094 . 1 233 63 63 LEU N N 122.248 . 1 234 64 64 GLU H H 8.214 . 1 235 64 64 GLU C C 175.835 . 1 236 64 64 GLU CA C 56.133 . 1 237 64 64 GLU CB C 30.071 . 1 238 64 64 GLU N N 121.772 . 1 239 65 65 ARG H H 8.107 . 1 240 65 65 ARG C C 175.623 . 1 241 65 65 ARG CA C 55.517 . 1 242 65 65 ARG CB C 30.915 . 1 243 65 65 ARG N N 121.826 . 1 244 66 66 GLU H H 8.310 . 1 245 66 66 GLU C C 174.080 . 1 246 66 66 GLU CA C 54.137 . 1 247 66 66 GLU CB C 29.374 . 1 248 66 66 GLU N N 123.802 . 1 249 67 67 PRO C C 176.436 . 1 250 67 67 PRO CA C 62.544 . 1 251 67 67 PRO CB C 31.821 . 1 252 68 68 LEU H H 8.243 . 1 253 68 68 LEU C C 175.243 . 1 254 68 68 LEU CA C 52.804 . 1 255 68 68 LEU CB C 41.249 . 1 256 68 68 LEU N N 123.854 . 1 257 69 69 PRO C C 176.785 . 1 258 69 69 PRO CA C 63.132 . 1 259 69 69 PRO CB C 31.764 . 1 260 70 70 ALA H H 8.248 . 1 261 70 70 ALA C C 178.286 . 1 262 70 70 ALA CA C 52.942 . 1 263 70 70 ALA CB C 18.670 . 1 264 70 70 ALA N N 123.288 . 1 265 71 71 GLU H H 8.202 . 1 266 71 71 GLU C C 176.323 . 1 267 71 71 GLU CA C 56.523 . 1 268 71 71 GLU CB C 30.013 . 1 269 71 71 GLU N N 118.656 . 1 270 72 72 ALA H H 7.952 . 1 271 72 72 ALA C C 177.685 . 1 272 72 72 ALA CA C 52.499 . 1 273 72 72 ALA CB C 18.881 . 1 274 72 72 ALA N N 124.281 . 1 275 73 73 MET H H 8.026 . 1 276 73 73 MET C C 176.735 . 1 277 73 73 MET CA C 55.573 . 1 278 73 73 MET CB C 32.369 . 1 279 73 73 MET N N 118.805 . 1 280 74 74 GLY H H 8.124 . 1 281 74 74 GLY C C 173.798 . 1 282 74 74 GLY CA C 45.237 . 1 283 74 74 GLY N N 109.354 . 1 284 75 75 ALA H H 7.895 . 1 285 75 75 ALA C C 177.396 . 1 286 75 75 ALA CA C 52.477 . 1 287 75 75 ALA CB C 18.904 . 1 288 75 75 ALA N N 123.469 . 1 289 76 76 TYR H H 7.870 . 1 290 76 76 TYR C C 175.265 . 1 291 76 76 TYR CA C 58.220 . 1 292 76 76 TYR CB C 38.548 . 1 293 76 76 TYR N N 118.844 . 1 294 77 77 PHE H H 7.697 . 1 295 77 77 PHE C C 174.613 . 1 296 77 77 PHE CA C 57.621 . 1 297 77 77 PHE CB C 39.607 . 1 298 77 77 PHE N N 121.280 . 1 299 78 78 ALA H H 7.814 . 1 300 78 78 ALA C C 177.046 . 1 301 78 78 ALA CA C 52.121 . 1 302 78 78 ALA CB C 19.207 . 1 303 78 78 ALA N N 124.831 . 1 304 79 79 ILE H H 7.794 . 1 305 79 79 ILE C C 175.868 . 1 306 79 79 ILE CA C 61.143 . 1 307 79 79 ILE CB C 38.561 . 1 308 79 79 ILE N N 119.990 . 1 309 80 80 ARG H H 8.175 . 1 310 80 80 ARG C C 175.818 . 1 311 80 80 ARG CA C 55.505 . 1 312 80 80 ARG CB C 30.629 . 1 313 80 80 ARG N N 125.855 . 1 314 81 81 ARG H H 8.347 . 1 315 81 81 ARG C C 176.510 . 1 316 81 81 ARG CA C 55.951 . 1 317 81 81 ARG CB C 30.921 . 1 318 81 81 ARG N N 123.879 . 1 319 82 82 THR H H 8.204 . 1 320 82 82 THR C C 174.201 . 1 321 82 82 THR CA C 61.549 . 1 322 82 82 THR CB C 69.791 . 1 323 82 82 THR N N 114.944 . 1 324 83 83 ASP H H 8.204 . 1 325 83 83 ASP C C 175.862 . 1 326 83 83 ASP CA C 54.142 . 1 327 83 83 ASP CB C 40.720 . 1 328 83 83 ASP N N 122.053 . 1 329 84 84 ALA H H 7.945 . 1 330 84 84 ALA C C 177.360 . 1 331 84 84 ALA CA C 52.552 . 1 332 84 84 ALA CB C 18.986 . 1 333 84 84 ALA N N 123.396 . 1 334 85 85 ASP H H 8.054 . 1 335 85 85 ASP C C 175.933 . 1 336 85 85 ASP CA C 54.213 . 1 337 85 85 ASP CB C 40.526 . 1 338 85 85 ASP N N 119.191 . 1 339 86 86 ASP H H 8.057 . 1 340 86 86 ASP C C 176.387 . 1 341 86 86 ASP CA C 54.134 . 1 342 86 86 ASP CB C 40.683 . 1 343 86 86 ASP N N 121.057 . 1 344 87 87 THR H H 7.961 . 1 345 87 87 THR C C 174.542 . 1 346 87 87 THR CA C 62.669 . 1 347 87 87 THR CB C 69.439 . 1 348 87 87 THR N N 114.328 . 1 349 88 88 VAL H H 7.876 . 1 350 88 88 VAL C C 175.549 . 1 351 88 88 VAL CA C 62.156 . 1 352 88 88 VAL CB C 32.390 . 1 353 88 88 VAL N N 122.864 . 1 354 89 89 ALA H H 8.163 . 1 355 89 89 ALA C C 176.925 . 1 356 89 89 ALA CA C 51.996 . 1 357 89 89 ALA CB C 18.945 . 1 358 89 89 ALA N N 128.062 . 1 359 90 90 ALA H H 8.096 . 1 360 90 90 ALA C C 176.553 . 1 361 90 90 ALA CA C 52.205 . 1 362 90 90 ALA CB C 19.031 . 1 363 90 90 ALA N N 124.142 . 1 364 91 91 HIS H H 7.802 . 1 365 91 91 HIS C C 178.765 . 1 366 91 91 HIS CA C 56.609 . 1 367 91 91 HIS CB C 29.846 . 1 368 91 91 HIS N N 122.683 . 1 stop_ save_