data_28003 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; FDX2 ; _BMRB_accession_number 28003 _BMRB_flat_file_name bmr28003.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 2' 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" 108 "13C chemical shifts" 221 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-08-22 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 28002 'Human Mitochondrial Ferredoxin FDX1' 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 FDX2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FDX2 $FDX2 '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_FDX2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FDX2 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 131 _Mol_residue_sequence ; AGEEDAGGPERPGDVVNVVF VDRSGQRIPVSGRVGDNVLH LAQRHGVDLEGACEASLACS TCHVYVSEDHLDLLPPPEER EDDMLDMAPLLQENSRLGCQ IVLTPELEGAEFTLPKITRN FYVDGHVPKPH ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLY 3 GLU 4 GLU 5 ASP 6 ALA 7 GLY 8 GLY 9 PRO 10 GLU 11 ARG 12 PRO 13 GLY 14 ASP 15 VAL 16 VAL 17 ASN 18 VAL 19 VAL 20 PHE 21 VAL 22 ASP 23 ARG 24 SER 25 GLY 26 GLN 27 ARG 28 ILE 29 PRO 30 VAL 31 SER 32 GLY 33 ARG 34 VAL 35 GLY 36 ASP 37 ASN 38 VAL 39 LEU 40 HIS 41 LEU 42 ALA 43 GLN 44 ARG 45 HIS 46 GLY 47 VAL 48 ASP 49 LEU 50 GLU 51 GLY 52 ALA 53 CYS 54 GLU 55 ALA 56 SER 57 LEU 58 ALA 59 CYS 60 SER 61 THR 62 CYS 63 HIS 64 VAL 65 TYR 66 VAL 67 SER 68 GLU 69 ASP 70 HIS 71 LEU 72 ASP 73 LEU 74 LEU 75 PRO 76 PRO 77 PRO 78 GLU 79 GLU 80 ARG 81 GLU 82 ASP 83 ASP 84 MET 85 LEU 86 ASP 87 MET 88 ALA 89 PRO 90 LEU 91 LEU 92 GLN 93 GLU 94 ASN 95 SER 96 ARG 97 LEU 98 GLY 99 CYS 100 GLN 101 ILE 102 VAL 103 LEU 104 THR 105 PRO 106 GLU 107 LEU 108 GLU 109 GLY 110 ALA 111 GLU 112 PHE 113 THR 114 LEU 115 PRO 116 LYS 117 ILE 118 THR 119 ARG 120 ASN 121 PHE 122 TYR 123 VAL 124 ASP 125 GLY 126 HIS 127 VAL 128 PRO 129 LYS 130 PRO 131 HIS 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 $FDX2 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 $FDX2 '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 $FDX2 0.8 mM '[U-100% 13C; U-100% 15N]' $entity_FES 0.8 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' HEPES 30 mM 'natural abundance' TCEP 1 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_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' 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_ save_PINE _Saveframe_category software _Name PINE _Version . loop_ _Vendor _Address _Electronic_address 'Bahrami, Markley, Assadi, and Eghbalnia' . . stop_ loop_ _Task 'chemical shift calculation' 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_HNCACB_3 _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 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 '2D 1H-15N HSQC' '3D CBCA(CO)NH' '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 FDX2 _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 GLY CA C 45.429 . 9 2 3 3 GLU H H 8.723 . 9 3 3 3 GLU CA C 57.598 . 9 4 3 3 GLU CB C 29.711 . 9 5 3 3 GLU N N 121.135 . 9 6 4 4 GLU H H 8.654 . 9 7 4 4 GLU CA C 56.965 . 9 8 4 4 GLU CB C 29.991 . 9 9 4 4 GLU N N 120.928 . 9 10 5 5 ASP H H 8.178 . 9 11 5 5 ASP CA C 51.018 . 9 12 5 5 ASP CB C 41.271 . 9 13 5 5 ASP N N 120.654 . 9 14 6 6 ALA H H 8.238 . 9 15 6 6 ALA CA C 52.821 . 9 16 6 6 ALA CB C 19.224 . 9 17 6 6 ALA N N 124.841 . 9 18 7 7 GLY H H 8.420 . 9 19 7 7 GLY CA C 45.293 . 9 20 7 7 GLY N N 107.983 . 9 21 8 8 GLY H H 8.063 . 9 22 8 8 GLY CA C 44.643 . 9 23 8 8 GLY N N 111.094 . 9 24 9 9 PRO CA C 63.184 . 9 25 9 9 PRO CB C 32.215 . 9 26 10 10 GLU H H 8.535 . 9 27 10 10 GLU CA C 56.653 . 9 28 10 10 GLU CB C 30.209 . 9 29 10 10 GLU N N 120.956 . 9 30 11 11 ARG H H 8.387 . 9 31 11 11 ARG N N 123.223 . 9 32 12 12 PRO CA C 63.353 . 9 33 12 12 PRO CB C 32.332 . 9 34 13 13 GLY H H 8.515 . 9 35 13 13 GLY CA C 45.160 . 9 36 13 13 GLY N N 108.248 . 9 37 14 14 ASP H H 8.240 . 9 38 14 14 ASP CA C 54.199 . 9 39 14 14 ASP CB C 41.015 . 9 40 14 14 ASP N N 119.688 . 9 41 15 15 VAL H H 7.858 . 9 42 15 15 VAL CA C 62.898 . 9 43 15 15 VAL CB C 32.987 . 9 44 15 15 VAL N N 120.972 . 9 45 16 16 VAL H H 8.075 . 9 46 16 16 VAL CA C 61.755 . 9 47 16 16 VAL CB C 34.732 . 9 48 16 16 VAL N N 127.586 . 9 49 17 17 ASN H H 9.408 . 9 50 17 17 ASN CA C 53.660 . 9 51 17 17 ASN CB C 39.169 . 9 52 17 17 ASN N N 127.727 . 9 53 18 18 VAL H H 8.735 . 9 54 18 18 VAL CA C 58.762 . 9 55 18 18 VAL CB C 35.740 . 9 56 18 18 VAL N N 114.186 . 9 57 19 19 VAL H H 8.673 . 9 58 19 19 VAL CA C 61.205 . 9 59 19 19 VAL CB C 36.345 . 9 60 19 19 VAL N N 121.462 . 9 61 20 20 PHE H H 8.586 . 9 62 20 20 PHE CA C 56.996 . 9 63 20 20 PHE CB C 42.545 . 9 64 20 20 PHE N N 123.421 . 9 65 21 21 VAL H H 9.007 . 9 66 21 21 VAL CA C 61.285 . 9 67 21 21 VAL CB C 31.705 . 9 68 21 21 VAL N N 124.266 . 9 69 22 22 ASP H H 8.752 . 9 70 22 22 ASP CA C 53.451 . 9 71 22 22 ASP CB C 40.495 . 9 72 22 22 ASP N N 125.104 . 9 73 23 23 ARG H H 8.612 . 9 74 23 23 ARG CA C 52.210 . 9 75 23 23 ARG CB C 29.425 . 9 76 23 23 ARG N N 116.339 . 9 77 24 24 SER H H 8.493 . 9 78 24 24 SER CA C 58.301 . 9 79 24 24 SER CB C 64.461 . 9 80 24 24 SER N N 114.678 . 9 81 25 25 GLY H H 8.257 . 9 82 25 25 GLY CA C 45.107 . 9 83 25 25 GLY N N 110.765 . 9 84 26 26 GLN H H 8.142 . 9 85 26 26 GLN CA C 46.896 . 9 86 26 26 GLN CB C 29.224 . 9 87 26 26 GLN N N 122.330 . 9 88 27 27 ARG H H 8.153 . 9 89 27 27 ARG CA C 43.690 . 9 90 27 27 ARG CB C 31.247 . 9 91 27 27 ARG N N 121.789 . 9 92 28 28 ILE H H 9.429 . 9 93 28 28 ILE CA C 58.781 . 9 94 28 28 ILE CB C 40.010 . 9 95 28 28 ILE N N 125.881 . 9 96 29 29 PRO CA C 62.589 . 9 97 29 29 PRO CB C 32.103 . 9 98 30 30 VAL H H 8.927 . 9 99 30 30 VAL CA C 60.949 . 9 100 30 30 VAL CB C 36.359 . 9 101 30 30 VAL N N 122.442 . 9 102 31 31 SER H H 8.368 . 9 103 31 31 SER CA C 58.294 . 9 104 31 31 SER CB C 63.298 . 9 105 31 31 SER N N 120.750 . 9 106 32 32 GLY H H 8.587 . 9 107 32 32 GLY CA C 44.023 . 9 108 32 32 GLY N N 114.203 . 9 109 33 33 ARG H H 8.976 . 9 110 33 33 ARG CA C 53.131 . 9 111 33 33 ARG CB C 33.153 . 9 112 33 33 ARG N N 121.365 . 9 113 34 34 VAL H H 8.315 . 9 114 34 34 VAL CA C 65.260 . 9 115 34 34 VAL CB C 31.893 . 9 116 34 34 VAL N N 120.558 . 9 117 35 35 GLY H H 8.879 . 9 118 35 35 GLY CA C 44.754 . 9 119 35 35 GLY N N 116.071 . 9 120 36 36 ASP H H 8.381 . 9 121 36 36 ASP CA C 55.262 . 9 122 36 36 ASP CB C 41.813 . 9 123 36 36 ASP N N 121.694 . 9 124 37 37 ASN H H 8.750 . 9 125 37 37 ASN CA C 50.018 . 9 126 37 37 ASN CB C 41.546 . 9 127 37 37 ASN N N 121.066 . 9 128 38 38 VAL H H 8.527 . 9 129 38 38 VAL CA C 58.858 . 9 130 38 38 VAL CB C 30.858 . 9 131 38 38 VAL N N 125.531 . 9 132 39 39 LEU H H 7.582 . 9 133 39 39 LEU CA C 52.841 . 9 134 39 39 LEU CB C 42.257 . 9 135 39 39 LEU N N 120.613 . 9 136 40 40 HIS H H 8.309 . 9 137 40 40 HIS CA C 56.832 . 9 138 40 40 HIS CB C 30.327 . 9 139 40 40 HIS N N 121.723 . 9 140 41 41 LEU H H 8.387 . 9 141 41 41 LEU CA C 55.261 . 9 142 41 41 LEU CB C 42.466 . 9 143 41 41 LEU N N 122.103 . 9 144 42 42 ALA H H 8.277 . 9 145 42 42 ALA CA C 55.591 . 9 146 42 42 ALA CB C 18.016 . 9 147 42 42 ALA N N 120.573 . 9 148 43 43 GLN H H 7.928 . 9 149 43 43 GLN CA C 59.070 . 9 150 43 43 GLN CB C 27.868 . 9 151 43 43 GLN N N 115.535 . 9 152 44 44 ARG H H 8.260 . 9 153 44 44 ARG CA C 58.432 . 9 154 44 44 ARG CB C 30.420 . 9 155 44 44 ARG N N 119.844 . 9 156 45 45 HIS H H 7.426 . 9 157 45 45 HIS CA C 56.997 . 9 158 45 45 HIS CB C 29.999 . 9 159 45 45 HIS N N 115.848 . 9 160 46 46 GLY H H 7.643 . 9 161 46 46 GLY CA C 46.551 . 9 162 46 46 GLY N N 107.272 . 9 163 47 47 VAL H H 8.011 . 9 164 47 47 VAL CA C 62.021 . 9 165 47 47 VAL CB C 31.558 . 9 166 47 47 VAL N N 121.756 . 9 167 48 48 ASP H H 8.956 . 9 168 48 48 ASP CA C 54.368 . 9 169 48 48 ASP CB C 39.147 . 9 170 48 48 ASP N N 129.969 . 9 171 49 49 LEU H H 7.962 . 9 172 49 49 LEU CA C 50.860 . 9 173 49 49 LEU CB C 44.629 . 9 174 49 49 LEU N N 126.426 . 9 175 50 50 GLU H H 8.923 . 9 176 50 50 GLU CA C 56.537 . 9 177 50 50 GLU CB C 32.117 . 9 178 50 50 GLU N N 126.998 . 9 179 51 51 GLY CA C 45.258 . 9 180 52 52 ALA H H 8.394 . 9 181 52 52 ALA CA C 52.991 . 9 182 52 52 ALA CB C 20.064 . 9 183 52 52 ALA N N 124.353 . 9 184 54 54 GLU H H 8.588 . 9 185 54 54 GLU CA C 30.217 . 9 186 54 54 GLU N N 120.507 . 9 187 57 57 LEU CA C 42.306 . 9 188 58 58 ALA H H 8.203 . 9 189 58 58 ALA N N 123.507 . 9 190 59 59 CYS CA C 58.863 . 9 191 59 59 CYS CB C 29.852 . 9 192 60 60 SER H H 8.443 . 9 193 60 60 SER CA C 63.386 . 9 194 60 60 SER N N 115.311 . 9 195 61 61 THR H H 8.162 . 9 196 61 61 THR CA C 61.689 . 9 197 61 61 THR CB C 70.125 . 9 198 61 61 THR N N 122.698 . 9 199 62 62 CYS H H 8.157 . 9 200 62 62 CYS CA C 45.943 . 9 201 62 62 CYS CB C 41.764 . 9 202 62 62 CYS N N 125.953 . 9 203 63 63 HIS H H 8.344 . 9 204 63 63 HIS CA C 42.544 . 9 205 63 63 HIS CB C 30.782 . 9 206 63 63 HIS N N 121.298 . 9 207 64 64 VAL H H 9.140 . 9 208 64 64 VAL CA C 59.135 . 9 209 64 64 VAL CB C 36.940 . 9 210 64 64 VAL N N 119.952 . 9 211 65 65 TYR H H 8.756 . 9 212 65 65 TYR CA C 53.611 . 9 213 65 65 TYR CB C 38.437 . 9 214 65 65 TYR N N 118.210 . 9 215 66 66 VAL H H 8.772 . 9 216 66 66 VAL CA C 61.888 . 9 217 66 66 VAL CB C 33.267 . 9 218 66 66 VAL N N 124.470 . 9 219 67 67 SER H H 8.202 . 9 220 67 67 SER CA C 58.749 . 9 221 67 67 SER CB C 60.440 . 9 222 67 67 SER N N 121.235 . 9 223 68 68 GLU H H 9.057 . 9 224 68 68 GLU CA C 60.935 . 9 225 68 68 GLU CB C 29.520 . 9 226 68 68 GLU N N 123.959 . 9 227 69 69 ASP H H 8.697 . 9 228 69 69 ASP CA C 56.153 . 9 229 69 69 ASP CB C 39.603 . 9 230 69 69 ASP N N 116.613 . 9 231 70 70 HIS H H 7.977 . 9 232 70 70 HIS CA C 58.434 . 9 233 70 70 HIS CB C 31.661 . 9 234 70 70 HIS N N 117.004 . 9 235 71 71 LEU H H 7.363 . 9 236 71 71 LEU CA C 58.660 . 9 237 71 71 LEU CB C 43.179 . 9 238 71 71 LEU N N 121.123 . 9 239 72 72 ASP H H 8.464 . 9 240 72 72 ASP CA C 55.339 . 9 241 72 72 ASP CB C 40.278 . 9 242 72 72 ASP N N 114.308 . 9 243 73 73 LEU H H 7.584 . 9 244 73 73 LEU CA C 54.371 . 9 245 73 73 LEU CB C 41.664 . 9 246 73 73 LEU N N 117.687 . 9 247 74 74 LEU H H 7.069 . 9 248 74 74 LEU CA C 52.583 . 9 249 74 74 LEU CB C 41.703 . 9 250 74 74 LEU N N 119.559 . 9 251 77 77 PRO CA C 63.191 . 9 252 77 77 PRO CB C 31.966 . 9 253 78 78 GLU H H 8.848 . 9 254 78 78 GLU CA C 55.804 . 9 255 78 78 GLU CB C 30.591 . 9 256 78 78 GLU N N 123.174 . 9 257 79 79 GLU H H 8.995 . 9 258 79 79 GLU CA C 60.534 . 9 259 79 79 GLU CB C 29.626 . 9 260 79 79 GLU N N 123.502 . 9 261 80 80 ARG H H 8.621 . 9 262 80 80 ARG CA C 58.863 . 9 263 80 80 ARG CB C 30.994 . 9 264 80 80 ARG N N 114.743 . 9 265 81 81 GLU H H 7.383 . 9 266 81 81 GLU CA C 59.238 . 9 267 81 81 GLU CB C 28.294 . 9 268 81 81 GLU N N 118.900 . 9 269 82 82 ASP H H 7.585 . 9 270 82 82 ASP CA C 58.045 . 9 271 82 82 ASP CB C 40.664 . 9 272 82 82 ASP N N 120.205 . 9 273 83 83 ASP H H 8.162 . 9 274 83 83 ASP CA C 57.406 . 9 275 83 83 ASP CB C 40.675 . 9 276 83 83 ASP N N 118.270 . 9 277 84 84 MET H H 7.699 . 9 278 84 84 MET CA C 56.399 . 9 279 84 84 MET CB C 34.851 . 9 280 84 84 MET N N 117.809 . 9 281 85 85 LEU CA C 42.342 . 9 282 86 86 ASP H H 8.149 . 9 283 86 86 ASP CA C 51.042 . 9 284 86 86 ASP CB C 41.415 . 9 285 86 86 ASP N N 124.052 . 9 286 87 87 MET H H 7.655 . 9 287 87 87 MET CA C 51.719 . 9 288 87 87 MET CB C 33.173 . 9 289 87 87 MET N N 117.081 . 9 290 88 88 ALA H H 8.141 . 9 291 88 88 ALA CA C 50.952 . 9 292 88 88 ALA CB C 18.023 . 9 293 88 88 ALA N N 119.310 . 9 294 89 89 PRO CA C 62.489 . 9 295 89 89 PRO CB C 32.213 . 9 296 90 90 LEU H H 8.834 . 9 297 90 90 LEU CA C 54.818 . 9 298 90 90 LEU CB C 37.926 . 9 299 90 90 LEU N N 114.544 . 9 300 91 91 LEU H H 7.566 . 9 301 91 91 LEU CA C 56.740 . 9 302 91 91 LEU CB C 42.947 . 9 303 91 91 LEU N N 121.334 . 9 304 92 92 GLN H H 10.157 . 9 305 92 92 GLN CA C 54.320 . 9 306 92 92 GLN CB C 33.608 . 9 307 92 92 GLN N N 126.451 . 9 308 93 93 GLU H H 9.219 . 9 309 93 93 GLU CA C 59.307 . 9 310 93 93 GLU CB C 29.236 . 9 311 93 93 GLU N N 121.099 . 9 312 94 94 ASN H H 8.575 . 9 313 94 94 ASN CA C 51.740 . 9 314 94 94 ASN CB C 36.040 . 9 315 94 94 ASN N N 113.240 . 9 316 95 95 SER H H 7.559 . 9 317 95 95 SER CA C 61.996 . 9 318 95 95 SER CB C 64.534 . 9 319 95 95 SER N N 118.375 . 9 320 96 96 ARG H H 9.569 . 9 321 96 96 ARG CA C 52.344 . 9 322 96 96 ARG CB C 35.136 . 9 323 96 96 ARG N N 120.530 . 9 324 97 97 LEU H H 9.174 . 9 325 97 97 LEU N N 120.192 . 9 326 100 100 GLN CA C 29.478 . 9 327 101 101 ILE H H 8.217 . 9 328 101 101 ILE CA C 61.112 . 9 329 101 101 ILE CB C 38.670 . 9 330 101 101 ILE N N 122.854 . 9 331 102 102 VAL H H 8.298 . 9 332 102 102 VAL CA C 59.394 . 9 333 102 102 VAL CB C 33.924 . 9 334 102 102 VAL N N 125.693 . 9 335 103 103 LEU H H 8.931 . 9 336 103 103 LEU CA C 57.105 . 9 337 103 103 LEU CB C 41.334 . 9 338 103 103 LEU N N 121.236 . 9 339 104 104 THR H H 6.833 . 9 340 104 104 THR CA C 58.850 . 9 341 104 104 THR CB C 69.031 . 9 342 104 104 THR N N 113.279 . 9 343 105 105 PRO CA C 65.864 . 9 344 105 105 PRO CB C 31.855 . 9 345 106 106 GLU H H 8.755 . 9 346 106 106 GLU CA C 51.384 . 9 347 106 106 GLU CB C 28.813 . 9 348 106 106 GLU N N 114.732 . 9 349 107 107 LEU H H 7.881 . 9 350 107 107 LEU CA C 53.990 . 9 351 107 107 LEU CB C 41.393 . 9 352 107 107 LEU N N 117.420 . 9 353 108 108 GLU H H 6.981 . 9 354 108 108 GLU CA C 57.781 . 9 355 108 108 GLU CB C 29.008 . 9 356 108 108 GLU N N 119.653 . 9 357 109 109 GLY H H 9.476 . 9 358 109 109 GLY CA C 44.837 . 9 359 109 109 GLY N N 118.142 . 9 360 110 110 ALA H H 7.994 . 9 361 110 110 ALA CA C 52.618 . 9 362 110 110 ALA CB C 19.345 . 9 363 110 110 ALA N N 123.855 . 9 364 111 111 GLU H H 7.734 . 9 365 111 111 GLU CA C 48.756 . 9 366 111 111 GLU CB C 32.509 . 9 367 111 111 GLU N N 116.613 . 9 368 112 112 PHE H H 8.751 . 9 369 112 112 PHE CA C 55.211 . 9 370 112 112 PHE CB C 40.365 . 9 371 112 112 PHE N N 123.706 . 9 372 113 113 THR H H 9.553 . 9 373 113 113 THR CA C 62.298 . 9 374 113 113 THR CB C 70.150 . 9 375 113 113 THR N N 121.688 . 9 376 114 114 LEU H H 8.721 . 9 377 114 114 LEU CA C 53.698 . 9 378 114 114 LEU CB C 41.190 . 9 379 114 114 LEU N N 128.920 . 9 380 115 115 PRO CA C 63.564 . 9 381 115 115 PRO CB C 32.084 . 9 382 116 116 LYS H H 8.632 . 9 383 116 116 LYS CA C 58.439 . 9 384 116 116 LYS CB C 32.975 . 9 385 116 116 LYS N N 119.806 . 9 386 117 117 ILE H H 7.192 . 9 387 117 117 ILE CA C 59.970 . 9 388 117 117 ILE CB C 41.064 . 9 389 117 117 ILE N N 114.684 . 9 390 118 118 THR H H 8.294 . 9 391 118 118 THR CA C 61.727 . 9 392 118 118 THR CB C 67.918 . 9 393 118 118 THR N N 116.493 . 9 394 119 119 ARG H H 8.030 . 9 395 119 119 ARG CA C 57.537 . 9 396 119 119 ARG CB C 30.925 . 9 397 119 119 ARG N N 128.959 . 9 398 120 120 ASN H H 8.403 . 9 399 120 120 ASN CA C 41.527 . 9 400 120 120 ASN N N 121.164 . 9 401 121 121 PHE H H 7.784 . 9 402 121 121 PHE CA C 56.541 . 9 403 121 121 PHE CB C 40.229 . 9 404 121 121 PHE N N 115.362 . 9 405 122 122 TYR H H 8.062 . 9 406 122 122 TYR CA C 53.082 . 9 407 122 122 TYR CB C 39.003 . 9 408 122 122 TYR N N 122.279 . 9 409 123 123 VAL H H 7.955 . 9 410 123 123 VAL CA C 62.296 . 9 411 123 123 VAL CB C 33.008 . 9 412 123 123 VAL N N 121.920 . 9 413 124 124 ASP H H 8.288 . 9 414 124 124 ASP CA C 54.732 . 9 415 124 124 ASP CB C 41.214 . 9 416 124 124 ASP N N 123.174 . 9 417 125 125 GLY H H 8.226 . 9 418 125 125 GLY CA C 45.467 . 9 419 125 125 GLY N N 108.971 . 9 420 126 126 HIS H H 8.120 . 9 421 126 126 HIS CA C 49.744 . 9 422 126 126 HIS CB C 31.020 . 9 423 126 126 HIS N N 119.785 . 9 424 127 127 VAL H H 7.966 . 9 425 127 127 VAL CA C 59.697 . 9 426 127 127 VAL CB C 32.790 . 9 427 127 127 VAL N N 124.303 . 9 428 128 128 PRO CA C 47.679 . 9 429 128 128 PRO CB C 42.402 . 9 430 129 129 LYS H H 8.316 . 9 431 129 129 LYS N N 121.722 . 9 432 130 130 PRO CA C 63.488 . 9 433 130 130 PRO CB C 31.939 . 9 434 131 131 HIS H H 7.790 . 9 435 131 131 HIS CA C 57.552 . 9 436 131 131 HIS CB C 31.110 . 9 437 131 131 HIS N N 124.336 . 9 stop_ save_