data_28002 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; FDX1 ; _BMRB_accession_number 28002 _BMRB_flat_file_name bmr28002.str _Entry_type original _Submission_date 2019-08-18 _Accession_date 2019-08-18 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Human Ferredoxin 1' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cai Kai . . 2 Markley John . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 103 "13C chemical shifts" 204 "15N chemical shifts" 103 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-08-22 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 28003 'Human Mitochondrial Ferredoxin FDX2' stop_ _Original_release_date 2019-08-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Human Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron-Sulfur Cluster Biosynthesis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28001042 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cai Kai . . 2 Tonelli Marco . . 3 Frederick Ronnie . . 4 Markley John . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 56 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 487 _Page_last 499 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name FDX1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FDX1 $FDX1 '2Fe-2S CLUSTER' $entity_FES 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_FDX1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FDX1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; SSSEDKITVHFINRDGETLT TKGKVGDSLLDVVVENNLDI DGFGACEGTLACSTCHLIFE DHIYEKLDAITDEENDMLDL AYGLTDRSRLGCQICLTKSM DNMTVRVPETVADARQSIDV GKTS ; loop_ _Residue_seq_code _Residue_label 1 SER 2 SER 3 SER 4 GLU 5 ASP 6 LYS 7 ILE 8 THR 9 VAL 10 HIS 11 PHE 12 ILE 13 ASN 14 ARG 15 ASP 16 GLY 17 GLU 18 THR 19 LEU 20 THR 21 THR 22 LYS 23 GLY 24 LYS 25 VAL 26 GLY 27 ASP 28 SER 29 LEU 30 LEU 31 ASP 32 VAL 33 VAL 34 VAL 35 GLU 36 ASN 37 ASN 38 LEU 39 ASP 40 ILE 41 ASP 42 GLY 43 PHE 44 GLY 45 ALA 46 CYS 47 GLU 48 GLY 49 THR 50 LEU 51 ALA 52 CYS 53 SER 54 THR 55 CYS 56 HIS 57 LEU 58 ILE 59 PHE 60 GLU 61 ASP 62 HIS 63 ILE 64 TYR 65 GLU 66 LYS 67 LEU 68 ASP 69 ALA 70 ILE 71 THR 72 ASP 73 GLU 74 GLU 75 ASN 76 ASP 77 MET 78 LEU 79 ASP 80 LEU 81 ALA 82 TYR 83 GLY 84 LEU 85 THR 86 ASP 87 ARG 88 SER 89 ARG 90 LEU 91 GLY 92 CYS 93 GLN 94 ILE 95 CYS 96 LEU 97 THR 98 LYS 99 SER 100 MET 101 ASP 102 ASN 103 MET 104 THR 105 VAL 106 ARG 107 VAL 108 PRO 109 GLU 110 THR 111 VAL 112 ALA 113 ASP 114 ALA 115 ARG 116 GLN 117 SER 118 ILE 119 ASP 120 VAL 121 GLY 122 LYS 123 THR 124 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_FES _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'FE2/S2 (INORGANIC) CLUSTER' _BMRB_code FES _PDB_code FES _Molecular_mass 175.820 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE1 FE1 FE . 0 . ? FE2 FE2 FE . 0 . ? S1 S1 S . 0 . ? S2 S2 S . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING FE1 S1 ? ? SING FE1 S2 ? ? SING FE2 S1 ? ? SING FE2 S2 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FDX1 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 $FDX1 'recombinant technology' . Escherichia coli . pET-SUMO 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 $FDX1 0.8 mM '[U-100% 13C; U-100% 15N]' 'sodium chloride' 150 mM 'natural abundance' TCEP 3 mM 'natural abundance' HEPES 30 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_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _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_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 0.15 . M pH 7.5 . pH pressure 1 . atm temperature 25 . 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 HNCA' '3D HNCACB' 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 FDX1 _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 4 4 GLU CA C 56.626 . 9 2 4 4 GLU CB C 30.276 . 9 3 5 5 ASP H H 8.273 . 9 4 5 5 ASP CA C 54.464 . 9 5 5 5 ASP CB C 41.066 . 9 6 5 5 ASP N N 121.031 . 9 7 6 6 LYS H H 7.972 . 9 8 6 6 LYS CA C 55.365 . 9 9 6 6 LYS CB C 35.427 . 9 10 6 6 LYS N N 119.717 . 9 11 7 7 ILE H H 8.966 . 9 12 7 7 ILE CA C 58.988 . 9 13 7 7 ILE CB C 40.682 . 9 14 7 7 ILE N N 118.638 . 9 15 8 8 THR H H 8.874 . 9 16 8 8 THR CA C 63.240 . 9 17 8 8 THR CB C 69.119 . 9 18 8 8 THR N N 121.819 . 9 19 9 9 VAL H H 8.504 . 9 20 9 9 VAL CA C 61.037 . 9 21 9 9 VAL CB C 35.476 . 9 22 9 9 VAL N N 124.760 . 9 23 10 10 HIS H H 8.606 . 9 24 10 10 HIS CA C 54.253 . 9 25 10 10 HIS CB C 31.504 . 9 26 10 10 HIS N N 125.651 . 9 27 11 11 PHE H H 9.576 . 9 28 11 11 PHE CA C 55.705 . 9 29 11 11 PHE CB C 41.667 . 9 30 11 11 PHE N N 122.505 . 9 31 12 12 ILE H H 9.029 . 9 32 12 12 ILE CA C 60.400 . 9 33 12 12 ILE CB C 37.017 . 9 34 12 12 ILE N N 122.951 . 9 35 13 13 ASN H H 8.912 . 9 36 13 13 ASN CA C 51.289 . 9 37 13 13 ASN CB C 38.855 . 9 38 13 13 ASN N N 125.062 . 9 39 14 14 ARG H H 8.590 . 9 40 14 14 ARG CA C 59.233 . 9 41 14 14 ARG CB C 29.644 . 9 42 14 14 ARG N N 119.017 . 9 43 15 15 ASP H H 7.687 . 9 44 15 15 ASP CA C 53.583 . 9 45 15 15 ASP CB C 40.768 . 9 46 15 15 ASP N N 116.124 . 9 47 16 16 GLY H H 8.180 . 9 48 16 16 GLY CA C 45.232 . 9 49 16 16 GLY N N 108.341 . 9 50 17 17 GLU H H 7.970 . 9 51 17 17 GLU CA C 57.005 . 9 52 17 17 GLU CB C 30.382 . 9 53 17 17 GLU N N 122.346 . 9 54 18 18 THR H H 8.657 . 9 55 18 18 THR CA C 63.008 . 9 56 18 18 THR CB C 69.167 . 9 57 18 18 THR N N 119.233 . 9 58 19 19 LEU H H 10.020 . 9 59 19 19 LEU CA C 53.420 . 9 60 19 19 LEU CB C 42.719 . 9 61 19 19 LEU N N 131.274 . 9 62 20 20 THR H H 8.813 . 9 63 20 20 THR CA C 63.955 . 9 64 20 20 THR CB C 70.082 . 9 65 20 20 THR N N 122.991 . 9 66 21 21 THR H H 8.840 . 9 67 21 21 THR CA C 60.177 . 9 68 21 21 THR CB C 70.553 . 9 69 21 21 THR N N 122.608 . 9 70 22 22 LYS H H 7.989 . 9 71 22 22 LYS CA C 53.929 . 9 72 22 22 LYS CB C 35.899 . 9 73 22 22 LYS N N 118.364 . 9 74 23 23 GLY H H 8.879 . 9 75 23 23 GLY CA C 43.931 . 9 76 23 23 GLY N N 107.554 . 9 77 24 24 LYS H H 8.799 . 9 78 24 24 LYS CA C 55.046 . 9 79 24 24 LYS CB C 33.342 . 9 80 24 24 LYS N N 121.470 . 9 81 25 25 VAL H H 8.374 . 9 82 25 25 VAL CA C 65.639 . 9 83 25 25 VAL CB C 31.485 . 9 84 25 25 VAL N N 122.229 . 9 85 26 26 GLY H H 8.843 . 9 86 26 26 GLY CA C 45.134 . 9 87 26 26 GLY N N 116.747 . 9 88 27 27 ASP H H 8.181 . 9 89 27 27 ASP CA C 54.750 . 9 90 27 27 ASP CB C 41.575 . 9 91 27 27 ASP N N 123.140 . 9 92 28 28 SER H H 9.748 . 9 93 28 28 SER CA C 58.388 . 9 94 28 28 SER CB C 65.970 . 9 95 28 28 SER N N 118.357 . 9 96 29 29 LEU H H 8.229 . 9 97 29 29 LEU CA C 58.011 . 9 98 29 29 LEU CB C 40.720 . 9 99 29 29 LEU N N 119.346 . 9 100 30 30 LEU H H 7.287 . 9 101 30 30 LEU CA C 54.874 . 9 102 30 30 LEU CB C 42.495 . 9 103 30 30 LEU N N 116.890 . 9 104 31 31 ASP H H 8.102 . 9 105 31 31 ASP CA C 58.168 . 9 106 31 31 ASP CB C 41.139 . 9 107 31 31 ASP N N 124.823 . 9 108 32 32 VAL H H 7.791 . 9 109 32 32 VAL CA C 66.199 . 9 110 32 32 VAL CB C 32.092 . 9 111 32 32 VAL N N 117.223 . 9 112 33 33 VAL H H 7.490 . 9 113 33 33 VAL CA C 67.223 . 9 114 33 33 VAL CB C 32.182 . 9 115 33 33 VAL N N 121.589 . 9 116 34 34 VAL H H 8.403 . 9 117 34 34 VAL CA C 66.280 . 9 118 34 34 VAL CB C 32.467 . 9 119 34 34 VAL N N 118.737 . 9 120 35 35 GLU H H 9.146 . 9 121 35 35 GLU CA C 59.303 . 9 122 35 35 GLU CB C 29.456 . 9 123 35 35 GLU N N 120.451 . 9 124 36 36 ASN H H 7.201 . 9 125 36 36 ASN CA C 53.480 . 9 126 36 36 ASN CB C 39.558 . 9 127 36 36 ASN N N 111.526 . 9 128 37 37 ASN H H 7.867 . 9 129 37 37 ASN CA C 54.031 . 9 130 37 37 ASN CB C 37.345 . 9 131 37 37 ASN N N 117.548 . 9 132 38 38 LEU H H 7.778 . 9 133 38 38 LEU CA C 55.518 . 9 134 38 38 LEU CB C 42.045 . 9 135 38 38 LEU N N 115.451 . 9 136 39 39 ASP H H 8.565 . 9 137 39 39 ASP CA C 53.704 . 9 138 39 39 ASP CB C 39.829 . 9 139 39 39 ASP N N 122.820 . 9 140 40 40 ILE H H 7.602 . 9 141 40 40 ILE CA C 60.065 . 9 142 40 40 ILE CB C 38.417 . 9 143 40 40 ILE N N 123.851 . 9 144 41 41 ASP H H 8.543 . 9 145 41 41 ASP CA C 56.796 . 9 146 41 41 ASP CB C 41.859 . 9 147 41 41 ASP N N 127.546 . 9 148 42 42 GLY H H 9.001 . 9 149 42 42 GLY CA C 46.198 . 9 150 42 42 GLY N N 113.790 . 9 151 43 43 PHE H H 7.667 . 9 152 43 43 PHE CA C 59.069 . 9 153 43 43 PHE CB C 41.242 . 9 154 43 43 PHE N N 120.938 . 9 155 44 44 GLY H H 8.512 . 9 156 44 44 GLY CA C 58.711 . 9 157 44 44 GLY N N 114.030 . 9 158 56 56 HIS CA C 54.977 . 9 159 56 56 HIS CB C 30.393 . 9 160 57 57 LEU H H 9.404 . 9 161 57 57 LEU CA C 53.628 . 9 162 57 57 LEU CB C 49.478 . 9 163 57 57 LEU N N 128.360 . 9 164 58 58 ILE H H 8.561 . 9 165 58 58 ILE CA C 61.364 . 9 166 58 58 ILE CB C 40.168 . 9 167 58 58 ILE N N 119.839 . 9 168 59 59 PHE H H 8.724 . 9 169 59 59 PHE CA C 58.472 . 9 170 59 59 PHE CB C 43.266 . 9 171 59 59 PHE N N 127.481 . 9 172 60 60 GLU H H 9.049 . 9 173 60 60 GLU CA C 56.847 . 9 174 60 60 GLU CB C 32.258 . 9 175 60 60 GLU N N 118.839 . 9 176 61 61 ASP H H 9.278 . 9 177 61 61 ASP CA C 59.131 . 9 178 61 61 ASP N N 123.700 . 9 179 62 62 HIS CA C 58.655 . 9 180 62 62 HIS CB C 29.466 . 9 181 63 63 ILE H H 6.336 . 9 182 63 63 ILE CA C 59.925 . 9 183 63 63 ILE CB C 36.520 . 9 184 63 63 ILE N N 119.973 . 9 185 64 64 TYR H H 8.666 . 9 186 64 64 TYR CA C 61.774 . 9 187 64 64 TYR CB C 39.578 . 9 188 64 64 TYR N N 119.920 . 9 189 65 65 GLU H H 7.809 . 9 190 65 65 GLU CA C 58.162 . 9 191 65 65 GLU CB C 29.999 . 9 192 65 65 GLU N N 113.284 . 9 193 66 66 LYS H H 7.277 . 9 194 66 66 LYS CA C 54.946 . 9 195 66 66 LYS CB C 33.258 . 9 196 66 66 LYS N N 116.069 . 9 197 67 67 LEU H H 6.826 . 9 198 67 67 LEU CA C 48.513 . 9 199 67 67 LEU CB C 46.719 . 9 200 67 67 LEU N N 119.710 . 9 201 68 68 ASP H H 8.855 . 9 202 68 68 ASP CA C 54.688 . 9 203 68 68 ASP CB C 41.559 . 9 204 68 68 ASP N N 121.976 . 9 205 69 69 ALA H H 8.169 . 9 206 69 69 ALA CA C 52.641 . 9 207 69 69 ALA CB C 18.769 . 9 208 69 69 ALA N N 122.032 . 9 209 70 70 ILE H H 8.351 . 9 210 70 70 ILE CA C 63.119 . 9 211 70 70 ILE CB C 39.277 . 9 212 70 70 ILE N N 123.975 . 9 213 71 71 THR H H 8.102 . 9 214 71 71 THR CA C 61.123 . 9 215 71 71 THR CB C 72.148 . 9 216 71 71 THR N N 119.076 . 9 217 72 72 ASP H H 8.980 . 9 218 72 72 ASP CA C 57.913 . 9 219 72 72 ASP CB C 40.556 . 9 220 72 72 ASP N N 122.566 . 9 221 73 73 GLU H H 8.975 . 9 222 73 73 GLU CA C 60.646 . 9 223 73 73 GLU CB C 29.270 . 9 224 73 73 GLU N N 117.334 . 9 225 74 74 GLU H H 7.531 . 9 226 74 74 GLU CA C 59.330 . 9 227 74 74 GLU CB C 29.186 . 9 228 74 74 GLU N N 119.621 . 9 229 75 75 ASN H H 8.589 . 9 230 75 75 ASN CA C 57.095 . 9 231 75 75 ASN CB C 39.169 . 9 232 75 75 ASN N N 119.789 . 9 233 76 76 ASP H H 8.287 . 9 234 76 76 ASP CA C 57.614 . 9 235 76 76 ASP CB C 40.719 . 9 236 76 76 ASP N N 117.243 . 9 237 77 77 MET H H 7.054 . 9 238 77 77 MET CA C 50.355 . 9 239 77 77 MET CB C 34.403 . 9 240 77 77 MET N N 116.029 . 9 241 78 78 LEU H H 8.827 . 9 242 78 78 LEU CA C 51.206 . 9 243 78 78 LEU CB C 41.420 . 9 244 78 78 LEU N N 123.628 . 9 245 79 79 ASP H H 7.994 . 9 246 79 79 ASP CA C 56.906 . 9 247 79 79 ASP CB C 41.417 . 9 248 79 79 ASP N N 116.740 . 9 249 80 80 LEU H H 7.064 . 9 250 80 80 LEU CA C 51.071 . 9 251 80 80 LEU CB C 42.403 . 9 252 80 80 LEU N N 116.652 . 9 253 81 81 ALA H H 7.848 . 9 254 81 81 ALA CA C 52.367 . 9 255 81 81 ALA CB C 19.104 . 9 256 81 81 ALA N N 124.194 . 9 257 82 82 TYR H H 8.325 . 9 258 82 82 TYR CA C 58.278 . 9 259 82 82 TYR CB C 38.870 . 9 260 82 82 TYR N N 123.006 . 9 261 83 83 GLY H H 8.382 . 9 262 83 83 GLY CA C 46.466 . 9 263 83 83 GLY N N 112.978 . 9 264 84 84 LEU H H 7.245 . 9 265 84 84 LEU CA C 56.898 . 9 266 84 84 LEU CB C 42.756 . 9 267 84 84 LEU N N 118.487 . 9 268 85 85 THR H H 8.855 . 9 269 85 85 THR CA C 60.127 . 9 270 85 85 THR CB C 74.476 . 9 271 85 85 THR N N 117.610 . 9 272 86 86 ASP H H 8.513 . 9 273 86 86 ASP CA C 54.337 . 9 274 86 86 ASP CB C 39.704 . 9 275 86 86 ASP N N 117.877 . 9 276 87 87 ARG H H 8.316 . 9 277 87 87 ARG CA C 53.797 . 9 278 87 87 ARG CB C 30.011 . 9 279 87 87 ARG N N 119.587 . 9 280 88 88 SER H H 7.040 . 9 281 88 88 SER CA C 60.674 . 9 282 88 88 SER CB C 65.342 . 9 283 88 88 SER N N 120.042 . 9 284 89 89 ARG H H 9.382 . 9 285 89 89 ARG CA C 52.828 . 9 286 89 89 ARG CB C 34.088 . 9 287 89 89 ARG N N 118.277 . 9 288 90 90 LEU H H 9.252 . 9 289 90 90 LEU CA C 58.172 . 9 290 90 90 LEU CB C 39.439 . 9 291 90 90 LEU N N 120.535 . 9 292 91 91 GLY H H 8.449 . 9 293 91 91 GLY CA C 45.410 . 9 294 91 91 GLY N N 110.624 . 9 295 92 92 CYS H H 8.068 . 9 296 92 92 CYS CA C 56.323 . 9 297 92 92 CYS CB C 33.272 . 9 298 92 92 CYS N N 120.980 . 9 299 93 93 GLN H H 8.288 . 9 300 93 93 GLN CA C 54.174 . 9 301 93 93 GLN CB C 29.988 . 9 302 93 93 GLN N N 115.383 . 9 303 94 94 ILE H H 7.350 . 9 304 94 94 ILE C C 47.852 . 9 305 94 94 ILE N N 121.091 . 9 306 95 95 CYS H H 8.082 . 9 307 95 95 CYS CB C 43.155 . 9 308 95 95 CYS N N 123.728 . 9 309 96 96 LEU H H 8.981 . 9 310 96 96 LEU CA C 52.303 . 9 311 96 96 LEU CB C 42.355 . 9 312 96 96 LEU N N 120.849 . 9 313 97 97 THR H H 7.804 . 9 314 97 97 THR CA C 59.350 . 9 315 97 97 THR CB C 71.601 . 9 316 97 97 THR N N 113.626 . 9 317 98 98 LYS H H 9.163 . 9 318 98 98 LYS CB C 31.993 . 9 319 98 98 LYS N N 121.094 . 9 320 99 99 SER CA C 60.303 . 9 321 99 99 SER CB C 62.680 . 9 322 100 100 MET H H 7.675 . 9 323 100 100 MET CA C 56.750 . 9 324 100 100 MET CB C 32.374 . 9 325 100 100 MET N N 120.217 . 9 326 101 101 ASP H H 7.206 . 9 327 101 101 ASP CA C 57.008 . 9 328 101 101 ASP CB C 41.125 . 9 329 101 101 ASP N N 117.875 . 9 330 102 102 ASN H H 9.975 . 9 331 102 102 ASN CA C 55.757 . 9 332 102 102 ASN CB C 37.996 . 9 333 102 102 ASN N N 122.417 . 9 334 103 103 MET H H 8.402 . 9 335 103 103 MET CA C 56.566 . 9 336 103 103 MET CB C 31.436 . 9 337 103 103 MET N N 118.039 . 9 338 104 104 THR H H 8.634 . 9 339 104 104 THR CA C 63.934 . 9 340 104 104 THR CB C 70.476 . 9 341 104 104 THR N N 117.013 . 9 342 105 105 VAL H H 9.124 . 9 343 105 105 VAL CA C 58.341 . 9 344 105 105 VAL CB C 34.325 . 9 345 105 105 VAL N N 122.496 . 9 346 106 106 ARG H H 8.403 . 9 347 106 106 ARG CA C 54.621 . 9 348 106 106 ARG CB C 33.568 . 9 349 106 106 ARG N N 120.888 . 9 350 107 107 VAL H H 8.396 . 9 351 107 107 VAL CA C 59.654 . 9 352 107 107 VAL CB C 32.210 . 9 353 107 107 VAL N N 124.384 . 9 354 108 108 PRO CA C 62.862 . 9 355 108 108 PRO CB C 32.330 . 9 356 109 109 GLU H H 8.649 . 9 357 109 109 GLU CA C 57.262 . 9 358 109 109 GLU CB C 30.794 . 9 359 109 109 GLU N N 120.791 . 9 360 110 110 THR H H 8.324 . 9 361 110 110 THR CA C 61.136 . 9 362 110 110 THR CB C 70.309 . 9 363 110 110 THR N N 113.644 . 9 364 111 111 VAL H H 7.859 . 9 365 111 111 VAL CA C 61.885 . 9 366 111 111 VAL CB C 32.987 . 9 367 111 111 VAL N N 120.992 . 9 368 112 112 ALA H H 8.170 . 9 369 112 112 ALA CA C 52.678 . 9 370 112 112 ALA CB C 19.296 . 9 371 112 112 ALA N N 127.087 . 9 372 113 113 ASP H H 8.152 . 9 373 113 113 ASP CA C 51.091 . 9 374 113 113 ASP CB C 41.389 . 9 375 113 113 ASP N N 119.705 . 9 376 114 114 ALA H H 8.239 . 9 377 114 114 ALA CA C 52.932 . 9 378 114 114 ALA CB C 19.074 . 9 379 114 114 ALA N N 125.127 . 9 380 115 115 ARG H H 8.290 . 9 381 115 115 ARG CA C 43.603 . 9 382 115 115 ARG CB C 30.504 . 9 383 115 115 ARG N N 119.454 . 9 384 116 116 GLN H H 9.422 . 9 385 116 116 GLN N N 128.199 . 9 386 117 117 SER H H 7.965 . 9 387 117 117 SER CA C 60.172 . 9 388 117 117 SER CB C 63.717 . 9 389 117 117 SER N N 123.295 . 9 390 118 118 ILE H H 8.094 . 9 391 118 118 ILE CA C 61.317 . 9 392 118 118 ILE CB C 39.050 . 9 393 118 118 ILE N N 121.961 . 9 394 119 119 ASP H H 8.367 . 9 395 119 119 ASP CA C 54.325 . 9 396 119 119 ASP CB C 41.248 . 9 397 119 119 ASP N N 124.277 . 9 398 120 120 VAL H H 8.019 . 9 399 120 120 VAL CA C 57.581 . 9 400 120 120 VAL CB C 32.609 . 9 401 120 120 VAL N N 120.253 . 9 402 121 121 GLY H H 8.425 . 9 403 121 121 GLY CA C 45.391 . 9 404 121 121 GLY N N 116.244 . 9 405 123 123 THR CA C 61.777 . 9 406 123 123 THR CB C 69.966 . 9 407 124 124 SER H H 7.966 . 9 408 124 124 SER CA C 60.044 . 9 409 124 124 SER CB C 64.837 . 9 410 124 124 SER N N 123.358 . 9 stop_ save_