data_27050 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Trypanosoma brucei brucei Tryparedoxin oxidized ; _BMRB_accession_number 27050 _BMRB_flat_file_name bmr27050.str _Entry_type original _Submission_date 2017-03-18 _Accession_date 2017-03-18 _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 Wagner Annika . . 2 Diehl Erika A. . 3 Krauth-Siegel Luise . . 4 Hellmich Ute A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 129 "13C chemical shifts" 407 "15N chemical shifts" 129 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-03-14 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 27049 'Trypanosoma brucei brucei Tryparedoxin reduced' stop_ _Original_release_date 2017-03-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28573456 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wagner Annika . . 2 Diehl Erika . . 3 Krauth-Siegel 'R. Luise' . . 4 Hellmich Ute A. . stop_ _Journal_abbreviation 'Biomol NMR Assign' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 11 _Journal_issue 2 _Journal_ISSN 1874-270X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 193 _Page_last 196 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Tryparedoxin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Tpx monomer oxidized' $Tryparedoxin 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_Tryparedoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Tryparedoxin _Molecular_mass 16076.2 _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'Member of the thioredoxin family. Involved in regulation of oxidative stress in Trypanosoma brucei.' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 147 _Mol_residue_sequence ; GAMGSGLAKYLPGATNLLSK SGEVSLGSLVGKTVFLYFSA SWCPPCRGFTPVLAEFYEKH HVAKNFEVVLISWDENESDF HDYYGKMPWLALPFDQRSTV SELGKTFGVESIPTLITINA DTGAIIGTQARTRVIEDPDG ANFPWPN ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 MET 4 GLY 5 SER 6 GLY 7 LEU 8 ALA 9 LYS 10 TYR 11 LEU 12 PRO 13 GLY 14 ALA 15 THR 16 ASN 17 LEU 18 LEU 19 SER 20 LYS 21 SER 22 GLY 23 GLU 24 VAL 25 SER 26 LEU 27 GLY 28 SER 29 LEU 30 VAL 31 GLY 32 LYS 33 THR 34 VAL 35 PHE 36 LEU 37 TYR 38 PHE 39 SER 40 ALA 41 SER 42 TRP 43 CYS 44 PRO 45 PRO 46 CYS 47 ARG 48 GLY 49 PHE 50 THR 51 PRO 52 VAL 53 LEU 54 ALA 55 GLU 56 PHE 57 TYR 58 GLU 59 LYS 60 HIS 61 HIS 62 VAL 63 ALA 64 LYS 65 ASN 66 PHE 67 GLU 68 VAL 69 VAL 70 LEU 71 ILE 72 SER 73 TRP 74 ASP 75 GLU 76 ASN 77 GLU 78 SER 79 ASP 80 PHE 81 HIS 82 ASP 83 TYR 84 TYR 85 GLY 86 LYS 87 MET 88 PRO 89 TRP 90 LEU 91 ALA 92 LEU 93 PRO 94 PHE 95 ASP 96 GLN 97 ARG 98 SER 99 THR 100 VAL 101 SER 102 GLU 103 LEU 104 GLY 105 LYS 106 THR 107 PHE 108 GLY 109 VAL 110 GLU 111 SER 112 ILE 113 PRO 114 THR 115 LEU 116 ILE 117 THR 118 ILE 119 ASN 120 ALA 121 ASP 122 THR 123 GLY 124 ALA 125 ILE 126 ILE 127 GLY 128 THR 129 GLN 130 ALA 131 ARG 132 THR 133 ARG 134 VAL 135 ILE 136 GLU 137 ASP 138 PRO 139 ASP 140 GLY 141 ALA 142 ASN 143 PHE 144 PRO 145 TRP 146 PRO 147 ASN 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 $Tryparedoxin 'Trypanosoma brucei' 5691 Eukaryota . Trypanosoma brucei 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 $Tryparedoxin 'recombinant technology' . Escherichia coli BL21-Gold(DE3) pETtrx_1b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_U-15N-Tpx _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tryparedoxin 475 uM [U-15N] 'sodium chloride' 125 mM 'natural abundance' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ save_15N-Lys-Tpx _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tryparedoxin 153 uM [U-15N]-Lys 'sodium chloride' 125 mM 'natural abundance' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ save_15N-Arg-Tpx _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tryparedoxin 300 uM [U-15N]-Arg 'sodium chloride' 125 mM 'natural abundance' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ save_15N-Trp-Tpx _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tryparedoxin 338 uM [U-15N]-Trp 'sodium chloride' 125 mM 'natural abundance' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ save_U-13C-15N-Tpx _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tryparedoxin 348 uM '[U-13C; U-15N]' 'sodium chloride' 125 mM 'natural abundance' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ save_13C-15N-Pro-Tpx _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tryparedoxin 338 uM '[U-13C; U-15N]-Pro' 'sodium chloride' 125 mM 'natural abundance' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ save_15N-Cys-Tpx _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tryparedoxin 214 uM [U-15N]-Cys 'sodium chloride' 125 mM 'natural abundance' 'sodium phosphate' 25 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 'TopSpin 3.5pl5' loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _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 $U-15N-Tpx save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $U-13C-15N-Tpx save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $U-13C-15N-Tpx save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $U-13C-15N-Tpx save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $U-13C-15N-Tpx save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $15N-Lys-Tpx save_ save_2D_1H-15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $15N-Arg-Tpx save_ save_2D_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $15N-Trp-Tpx save_ save_2D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $15N-Cys-Tpx 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' 125 . mM 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 external indirect . . . 0.2514502 DSS H 1 'methyl protons' ppm 0 external direct . . . 1 DSS N 15 'methyl protons' ppm 0 external indirect . . . 0.1013 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 HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' stop_ loop_ _Sample_label $U-15N-Tpx $U-13C-15N-Tpx $15N-Lys-Tpx $15N-Arg-Tpx $15N-Trp-Tpx $15N-Cys-Tpx stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Tpx monomer oxidized' _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 5 5 SER C C 175.591 0.3 1 2 5 5 SER CA C 58.114 0.3 1 3 5 5 SER CB C 64.387 0.3 1 4 6 6 GLY H H 8.293 0.020 1 5 6 6 GLY C C 174.801 0.3 1 6 6 6 GLY CA C 46.409 0.3 1 7 6 6 GLY N N 112.610 0.3 1 8 7 7 LEU H H 8.263 0.020 1 9 7 7 LEU C C 177.712 0.3 1 10 7 7 LEU CA C 56.813 0.3 1 11 7 7 LEU CB C 42.277 0.3 1 12 7 7 LEU N N 120.468 0.3 1 13 8 8 ALA H H 7.748 0.020 1 14 8 8 ALA C C 178.367 0.3 1 15 8 8 ALA CA C 53.983 0.3 1 16 8 8 ALA CB C 17.872 0.3 1 17 8 8 ALA N N 119.670 0.3 1 18 9 9 LYS H H 7.248 0.020 1 19 9 9 LYS C C 177.105 0.3 1 20 9 9 LYS CA C 58.190 0.3 1 21 9 9 LYS CB C 31.949 0.3 1 22 9 9 LYS N N 116.228 0.3 1 23 10 10 TYR H H 7.326 0.020 1 24 10 10 TYR C C 174.190 0.3 1 25 10 10 TYR CA C 57.655 0.3 1 26 10 10 TYR CB C 39.676 0.3 1 27 10 10 TYR N N 115.332 0.3 1 28 11 11 LEU H H 7.490 0.020 1 29 11 11 LEU C C 173.114 0.3 1 30 11 11 LEU CA C 51.229 0.3 1 31 11 11 LEU CB C 42.507 0.3 1 32 11 11 LEU N N 117.671 0.3 1 33 13 13 GLY C C 174.084 0.3 1 34 13 13 GLY CA C 45.991 0.3 1 35 14 14 ALA H H 7.904 0.020 1 36 14 14 ALA C C 177.002 0.3 1 37 14 14 ALA CA C 51.821 0.3 1 38 14 14 ALA CB C 18.528 0.3 1 39 14 14 ALA N N 122.144 0.3 1 40 15 15 THR H H 7.999 0.020 1 41 15 15 THR C C 173.603 0.3 1 42 15 15 THR CA C 63.087 0.3 1 43 15 15 THR CB C 69.896 0.3 1 44 15 15 THR N N 114.440 0.3 1 45 16 16 ASN H H 8.132 0.020 1 46 16 16 ASN C C 174.264 0.3 1 47 16 16 ASN CA C 52.070 0.3 1 48 16 16 ASN CB C 40.747 0.3 1 49 16 16 ASN N N 121.458 0.3 1 50 17 17 LEU H H 8.940 0.020 1 51 17 17 LEU C C 176.658 0.3 1 52 17 17 LEU CA C 52.835 0.3 1 53 17 17 LEU CB C 43.718 0.3 1 54 17 17 LEU N N 117.852 0.3 1 55 18 18 LEU H H 9.088 0.020 1 56 18 18 LEU C C 175.584 0.3 1 57 18 18 LEU CA C 55.207 0.3 1 58 18 18 LEU CB C 42.890 0.3 1 59 18 18 LEU N N 119.201 0.3 1 60 19 19 SER H H 7.947 0.020 1 61 19 19 SER C C 175.462 0.3 1 62 19 19 SER CA C 56.584 0.3 1 63 19 19 SER CB C 68.519 0.3 1 64 19 19 SER N N 115.301 0.3 1 65 20 20 LYS H H 8.843 0.020 1 66 20 20 LYS C C 177.736 0.3 1 67 20 20 LYS CA C 56.890 0.3 1 68 20 20 LYS CB C 30.802 0.3 1 69 20 20 LYS N N 117.948 0.3 1 70 21 21 SER H H 8.182 0.020 1 71 21 21 SER C C 173.652 0.3 1 72 21 21 SER CA C 57.126 0.3 1 73 21 21 SER CB C 63.594 0.3 1 74 21 21 SER N N 112.234 0.3 1 75 22 22 GLY H H 7.459 0.020 1 76 22 22 GLY C C 173.334 0.3 1 77 22 22 GLY CA C 44.802 0.3 1 78 22 22 GLY N N 110.932 0.3 1 79 23 23 GLU H H 8.507 0.020 1 80 23 23 GLU C C 176.856 0.3 1 81 23 23 GLU CA C 56.354 0.3 1 82 23 23 GLU CB C 32.102 0.3 1 83 23 23 GLU N N 122.230 0.3 1 84 24 24 VAL H H 9.070 0.020 1 85 24 24 VAL C C 174.337 0.3 1 86 24 24 VAL CA C 59.568 0.3 1 87 24 24 VAL CB C 35.622 0.3 1 88 24 24 VAL N N 117.088 0.3 1 89 25 25 SER H H 8.569 0.020 1 90 25 25 SER C C 177.198 0.3 1 91 25 25 SER CA C 57.043 0.3 1 92 25 25 SER CB C 64.770 0.3 1 93 25 25 SER N N 117.778 0.3 1 94 26 26 LEU H H 8.867 0.020 1 95 26 26 LEU C C 179.717 0.3 1 96 26 26 LEU CA C 58.190 0.3 1 97 26 26 LEU CB C 40.977 0.3 1 98 26 26 LEU N N 124.853 0.3 1 99 27 27 GLY C C 175.679 0.3 1 100 27 27 GLY CA C 46.316 0.3 1 101 28 28 SER H H 7.738 0.020 1 102 28 28 SER C C 175.168 0.3 1 103 28 28 SER CA C 60.485 0.3 1 104 28 28 SER CB C 63.301 0.3 1 105 28 28 SER N N 115.946 0.3 1 106 29 29 LEU H H 7.498 0.020 1 107 29 29 LEU C C 174.215 0.3 1 108 29 29 LEU CA C 54.595 0.3 1 109 29 29 LEU CB C 40.594 0.3 1 110 29 29 LEU N N 121.522 0.3 1 111 30 30 VAL H H 6.740 0.020 1 112 30 30 VAL C C 177.028 0.3 1 113 30 30 VAL CA C 63.087 0.3 1 114 30 30 VAL CB C 31.873 0.3 1 115 30 30 VAL N N 115.882 0.3 1 116 31 31 GLY H H 9.869 0.020 1 117 31 31 GLY C C 174.728 0.3 1 118 31 31 GLY CA C 45.644 0.3 1 119 31 31 GLY N N 116.589 0.3 1 120 32 32 LYS H H 7.662 0.020 1 121 32 32 LYS C C 177.809 0.3 1 122 32 32 LYS CA C 56.278 0.3 1 123 32 32 LYS CB C 34.091 0.3 1 124 32 32 LYS N N 117.462 0.3 1 125 33 33 THR H H 7.709 0.020 1 126 33 33 THR C C 173.261 0.3 1 127 33 33 THR CA C 64.005 0.3 1 128 33 33 THR CB C 68.672 0.3 1 129 33 33 THR N N 118.292 0.3 1 130 34 34 VAL H H 9.328 0.020 1 131 34 34 VAL C C 173.774 0.3 1 132 34 34 VAL CA C 60.639 0.3 1 133 34 34 VAL CB C 34.780 0.3 1 134 34 34 VAL N N 126.892 0.3 1 135 35 35 PHE H H 9.073 0.020 1 136 35 35 PHE C C 175.560 0.3 1 137 35 35 PHE CA C 55.666 0.3 1 138 35 35 PHE CB C 40.747 0.3 1 139 35 35 PHE N N 124.289 0.3 1 140 36 36 LEU H H 9.460 0.020 1 141 36 36 LEU C C 174.875 0.3 1 142 36 36 LEU CA C 53.600 0.3 1 143 36 36 LEU CB C 41.818 0.3 1 144 36 36 LEU N N 123.871 0.3 1 145 37 37 TYR H H 8.857 0.020 1 146 37 37 TYR C C 172.600 0.3 1 147 37 37 TYR CA C 52.963 0.3 1 148 37 37 TYR CB C 38.758 0.3 1 149 37 37 TYR N N 125.395 0.3 1 150 38 38 PHE H H 8.987 0.020 1 151 38 38 PHE C C 174.312 0.3 1 152 38 38 PHE CA C 56.048 0.3 1 153 38 38 PHE CB C 39.217 0.3 1 154 38 38 PHE N N 129.705 0.3 1 155 39 39 SER H H 7.420 0.020 1 156 39 39 SER C C 171.378 0.3 1 157 39 39 SER CA C 56.737 0.3 1 158 39 39 SER CB C 65.382 0.3 1 159 39 39 SER N N 113.442 0.3 1 160 40 40 ALA H H 6.778 0.020 1 161 40 40 ALA C C 176.367 0.3 1 162 40 40 ALA CA C 51.764 0.3 1 163 40 40 ALA CB C 22.463 0.3 1 164 40 40 ALA N N 119.250 0.3 1 165 41 41 SER H H 9.854 0.020 1 166 41 41 SER C C 174.581 0.3 1 167 41 41 SER CA C 60.715 0.3 1 168 41 41 SER CB C 62.934 0.3 1 169 41 41 SER N N 119.803 0.3 1 170 42 42 TRP H H 6.364 0.020 1 171 42 42 TRP C C 174.948 0.3 1 172 42 42 TRP CA C 54.059 0.3 1 173 42 42 TRP CB C 29.501 0.3 1 174 42 42 TRP N N 115.953 0.3 1 175 43 43 CYS H H 6.414 0.020 1 176 43 43 CYS C C 172.650 0.3 1 177 43 43 CYS CA C 51.611 0.3 1 178 43 43 CYS CB C 44.726 0.3 1 179 43 43 CYS N N 123.313 0.3 1 180 45 45 PRO C C 179.936 0.3 1 181 45 45 PRO CA C 65.458 0.3 1 182 45 45 PRO CB C 30.266 0.3 1 183 46 46 CYS H H 8.342 0.020 1 184 46 46 CYS C C 175.706 0.3 1 185 46 46 CYS CA C 63.852 0.3 1 186 46 46 CYS CB C 33.020 0.3 1 187 46 46 CYS N N 115.571 0.3 1 188 47 47 ARG H H 8.018 0.020 1 189 47 47 ARG C C 179.448 0.3 1 190 47 47 ARG CA C 59.269 0.3 1 191 47 47 ARG CB C 29.953 0.3 1 192 47 47 ARG N N 120.145 0.3 1 193 48 48 GLY H H 7.583 0.020 1 194 48 48 GLY C C 174.801 0.3 1 195 48 48 GLY CA C 46.026 0.3 1 196 48 48 GLY N N 102.562 0.3 1 197 49 49 PHE H H 7.772 0.020 1 198 49 49 PHE C C 176.244 0.3 1 199 49 49 PHE CA C 59.721 0.3 1 200 49 49 PHE CB C 40.594 0.3 1 201 49 49 PHE N N 121.041 0.3 1 202 50 50 THR H H 8.587 0.020 1 203 50 50 THR CA C 69.437 0.3 1 204 50 50 THR CB C 68.213 0.3 1 205 50 50 THR N N 116.539 0.3 1 206 51 51 PRO C C 179.060 0.3 1 207 51 51 PRO CA C 65.734 0.3 1 208 51 51 PRO CB C 31.644 0.3 1 209 52 52 VAL H H 6.809 0.020 1 210 52 52 VAL C C 179.179 0.3 1 211 52 52 VAL CA C 65.535 0.3 1 212 52 52 VAL CB C 31.184 0.3 1 213 52 52 VAL N N 120.594 0.3 1 214 53 53 LEU H H 7.384 0.020 1 215 53 53 LEU C C 178.543 0.3 1 216 53 53 LEU CA C 56.660 0.3 1 217 53 53 LEU CB C 40.135 0.3 1 218 53 53 LEU N N 122.073 0.3 1 219 54 54 ALA H H 9.054 0.020 1 220 54 54 ALA C C 178.812 0.3 1 221 54 54 ALA CA C 56.354 0.3 1 222 54 54 ALA CB C 17.184 0.3 1 223 54 54 ALA N N 121.893 0.3 1 224 55 55 GLU H H 7.756 0.020 1 225 55 55 GLU C C 177.981 0.3 1 226 55 55 GLU CA C 59.644 0.3 1 227 55 55 GLU CB C 29.348 0.3 1 228 55 55 GLU N N 120.285 0.3 1 229 56 56 PHE H H 7.615 0.020 1 230 56 56 PHE C C 177.369 0.3 1 231 56 56 PHE CA C 61.557 0.3 1 232 56 56 PHE CB C 39.676 0.3 1 233 56 56 PHE N N 120.562 0.3 1 234 57 57 TYR H H 9.437 0.020 1 235 57 57 TYR C C 178.372 0.3 1 236 57 57 TYR CA C 61.863 0.3 1 237 57 57 TYR CB C 40.059 0.3 1 238 57 57 TYR N N 119.304 0.3 1 239 58 58 GLU H H 9.187 0.020 1 240 58 58 GLU C C 179.179 0.3 1 241 58 58 GLU CA C 59.644 0.3 1 242 58 58 GLU CB C 29.272 0.3 1 243 58 58 GLU N N 121.590 0.3 1 244 59 59 LYS H H 7.724 0.020 1 245 59 59 LYS C C 179.288 0.3 1 246 59 59 LYS CA C 59.148 0.3 1 247 59 59 LYS CB C 32.778 0.3 1 248 59 59 LYS N N 116.088 0.3 1 249 60 60 HIS H H 7.611 0.020 1 250 60 60 HIS C C 176.684 0.3 1 251 60 60 HIS CA C 57.043 0.3 1 252 60 60 HIS CB C 33.938 0.3 1 253 60 60 HIS N N 111.481 0.3 1 254 61 61 HIS H H 8.543 0.020 1 255 61 61 HIS C C 175.144 0.3 1 256 61 61 HIS CA C 59.491 0.3 1 257 61 61 HIS CB C 25.293 0.3 1 258 61 61 HIS N N 118.471 0.3 1 259 62 62 VAL H H 6.778 0.020 1 260 62 62 VAL C C 179.032 0.3 1 261 62 62 VAL CA C 65.076 0.3 1 262 62 62 VAL CB C 30.802 0.3 1 263 62 62 VAL N N 118.704 0.3 1 264 63 63 ALA H H 8.328 0.020 1 265 63 63 ALA C C 179.790 0.3 1 266 63 63 ALA CA C 55.207 0.3 1 267 63 63 ALA CB C 18.791 0.3 1 268 63 63 ALA N N 123.786 0.3 1 269 64 64 LYS H H 8.272 0.020 1 270 64 64 LYS C C 174.802 0.3 1 271 64 64 LYS CA C 55.895 0.3 1 272 64 64 LYS CB C 31.108 0.3 1 273 64 64 LYS N N 112.169 0.3 1 274 65 65 ASN H H 7.185 0.020 1 275 65 65 ASN C C 173.041 0.3 1 276 65 65 ASN CA C 53.524 0.3 1 277 65 65 ASN CB C 37.764 0.3 1 278 65 65 ASN N N 119.322 0.3 1 279 66 66 PHE H H 8.374 0.020 1 280 66 66 PHE C C 173.051 0.3 1 281 66 66 PHE CA C 54.671 0.3 1 282 66 66 PHE CB C 43.884 0.3 1 283 66 66 PHE N N 113.270 0.3 1 284 67 67 GLU H H 8.902 0.020 1 285 67 67 GLU C C 174.312 0.3 1 286 67 67 GLU CA C 52.912 0.3 1 287 67 67 GLU CB C 36.111 0.3 1 288 67 67 GLU N N 118.841 0.3 1 289 68 68 VAL H H 9.353 0.020 1 290 68 68 VAL C C 172.919 0.3 1 291 68 68 VAL CA C 60.562 0.3 1 292 68 68 VAL CB C 34.015 0.3 1 293 68 68 VAL N N 125.306 0.3 1 294 69 69 VAL H H 8.770 0.020 1 295 69 69 VAL C C 174.875 0.3 1 296 69 69 VAL CA C 60.023 0.3 1 297 69 69 VAL CB C 34.168 0.3 1 298 69 69 VAL N N 124.833 0.3 1 299 70 70 LEU H H 9.210 0.020 1 300 70 70 LEU C C 173.481 0.3 1 301 70 70 LEU CA C 55.819 0.3 1 302 70 70 LEU CB C 43.349 0.3 1 303 70 70 LEU N N 129.105 0.3 1 304 71 71 ILE H H 8.845 0.020 1 305 71 71 ILE C C 174.215 0.3 1 306 71 71 ILE CA C 58.059 0.3 1 307 71 71 ILE CB C 35.239 0.3 1 308 71 71 ILE N N 131.140 0.3 1 309 72 72 SER H H 8.964 0.020 1 310 72 72 SER C C 177.394 0.3 1 311 72 72 SER CA C 58.267 0.3 1 312 72 72 SER CB C 64.999 0.3 1 313 72 72 SER N N 116.989 0.3 1 314 73 73 TRP H H 8.770 0.020 1 315 73 73 TRP C C 176.929 0.3 1 316 73 73 TRP CA C 55.298 0.3 1 317 73 73 TRP CB C 29.348 0.3 1 318 73 73 TRP N N 127.203 0.3 1 319 74 74 ASP H H 9.501 0.020 1 320 74 74 ASP C C 175.095 0.3 1 321 74 74 ASP CA C 58.190 0.3 1 322 74 74 ASP CB C 41.895 0.3 1 323 74 74 ASP N N 122.466 0.3 1 324 75 75 GLU H H 9.503 0.020 1 325 75 75 GLU C C 175.975 0.3 1 326 75 75 GLU CA C 56.966 0.3 1 327 75 75 GLU CB C 31.021 0.3 1 328 75 75 GLU N N 117.702 0.3 1 329 76 76 ASN H H 7.534 0.020 1 330 76 76 ASN C C 174.068 0.3 1 331 76 76 ASN CA C 51.917 0.3 1 332 76 76 ASN CB C 40.824 0.3 1 333 76 76 ASN N N 113.959 0.3 1 334 77 77 GLU H H 8.802 0.020 1 335 77 77 GLU C C 177.051 0.3 1 336 77 77 GLU CA C 59.207 0.3 1 337 77 77 GLU CB C 29.526 0.3 1 338 77 77 GLU N N 124.747 0.3 1 339 78 78 SER H H 8.163 0.020 1 340 78 78 SER C C 177.223 0.3 1 341 78 78 SER CA C 61.718 0.3 1 342 78 78 SER N N 115.436 0.3 1 343 79 79 ASP H H 8.090 0.020 1 344 79 79 ASP C C 178.421 0.3 1 345 79 79 ASP CA C 57.196 0.3 1 346 79 79 ASP CB C 40.059 0.3 1 347 79 79 ASP N N 122.448 0.3 1 348 80 80 PHE H H 7.740 0.020 1 349 80 80 PHE C C 176.709 0.3 1 350 80 80 PHE CA C 61.480 0.3 1 351 80 80 PHE CB C 38.835 0.3 1 352 80 80 PHE N N 119.080 0.3 1 353 81 81 HIS H H 8.392 0.020 1 354 81 81 HIS C C 179.399 0.3 1 355 81 81 HIS CA C 60.639 0.3 1 356 81 81 HIS CB C 30.266 0.3 1 357 81 81 HIS N N 118.463 0.3 1 358 82 82 ASP H H 8.280 0.020 1 359 82 82 ASP C C 177.834 0.3 1 360 82 82 ASP CA C 57.272 0.3 1 361 82 82 ASP CB C 41.206 0.3 1 362 82 82 ASP N N 121.311 0.3 1 363 83 83 TYR H H 8.045 0.020 1 364 83 83 TYR C C 178.201 0.3 1 365 83 83 TYR CA C 58.956 0.3 1 366 83 83 TYR CB C 38.911 0.3 1 367 83 83 TYR N N 120.080 0.3 1 368 84 84 TYR H H 8.663 0.020 1 369 84 84 TYR C C 178.344 0.3 1 370 84 84 TYR CA C 58.649 0.3 1 371 84 84 TYR CB C 36.999 0.3 1 372 84 84 TYR N N 118.703 0.3 1 373 85 85 GLY H H 7.677 0.020 1 374 85 85 GLY C C 174.312 0.3 1 375 85 85 GLY CA C 46.256 0.3 1 376 85 85 GLY N N 105.361 0.3 1 377 86 86 LYS H H 6.846 0.020 1 378 86 86 LYS C C 176.049 0.3 1 379 86 86 LYS CA C 55.513 0.3 1 380 86 86 LYS CB C 32.179 0.3 1 381 86 86 LYS N N 117.089 0.3 1 382 87 87 MET H H 7.412 0.020 1 383 87 87 MET C C 174.875 0.3 1 384 87 87 MET CA C 52.376 0.3 1 385 87 87 MET CB C 31.643 0.3 1 386 87 87 MET N N 118.224 0.3 1 387 88 88 PRO C C 175.223 0.3 1 388 89 89 TRP H H 5.292 0.020 1 389 89 89 TRP C C 174.239 0.3 1 390 89 89 TRP CA C 55.530 0.3 1 391 89 89 TRP CB C 27.046 0.3 1 392 89 89 TRP N N 117.525 0.3 1 393 90 90 LEU H H 8.455 0.020 1 394 90 90 LEU C C 178.054 0.3 1 395 90 90 LEU CA C 55.054 0.3 1 396 90 90 LEU CB C 44.649 0.3 1 397 90 90 LEU N N 121.113 0.3 1 398 91 91 ALA H H 8.601 0.020 1 399 91 91 ALA C C 175.609 0.3 1 400 91 91 ALA CA C 51.763 0.3 1 401 91 91 ALA CB C 21.198 0.3 1 402 91 91 ALA N N 118.537 0.3 1 403 92 92 LEU H H 8.159 0.020 1 404 92 92 LEU C C 174.019 0.3 1 405 92 92 LEU CA C 52.479 0.3 1 406 92 92 LEU CB C 43.119 0.3 1 407 92 92 LEU N N 125.666 0.3 1 408 93 93 PRO C C 177.203 0.3 1 409 93 93 PRO CA C 63.775 0.3 1 410 93 93 PRO CB C 32.408 0.3 1 411 94 94 PHE H H 7.943 0.020 1 412 94 94 PHE C C 174.777 0.3 1 413 94 94 PHE CA C 61.560 0.3 1 414 94 94 PHE CB C 38.602 0.3 1 415 94 94 PHE N N 125.242 0.3 1 416 95 95 ASP H H 8.147 0.020 1 417 95 95 ASP C C 177.540 0.3 1 418 95 95 ASP CA C 54.977 0.3 1 419 95 95 ASP CB C 39.370 0.3 1 420 95 95 ASP N N 112.238 0.3 1 421 96 96 GLN H H 7.240 0.020 1 422 96 96 GLN C C 177.222 0.3 1 423 96 96 GLN CA C 53.830 0.3 1 424 96 96 GLN CB C 25.829 0.3 1 425 96 96 GLN N N 121.662 0.3 1 426 97 97 ARG H H 7.545 0.020 1 427 97 97 ARG C C 179.839 0.3 1 428 97 97 ARG CA C 58.573 0.3 1 429 97 97 ARG CB C 31.720 0.3 1 430 97 97 ARG N N 122.279 0.3 1 431 98 98 SER C C 176.958 0.3 1 432 98 98 SER CA C 65.793 0.3 1 433 98 98 SER CB C 68.612 0.3 1 434 99 99 THR H H 7.637 0.020 1 435 99 99 THR C C 175.399 0.3 1 436 99 99 THR CA C 65.992 0.3 1 437 99 99 THR CB C 68.436 0.3 1 438 99 99 THR N N 118.987 0.3 1 439 100 100 VAL H H 7.318 0.020 1 440 100 100 VAL C C 179.081 0.3 1 441 100 100 VAL CA C 67.983 0.3 1 442 100 100 VAL CB C 31.490 0.3 1 443 100 100 VAL N N 120.905 0.3 1 444 101 101 SER H H 7.615 0.020 1 445 101 101 SER C C 177.431 0.3 1 446 101 101 SER CA C 61.327 0.3 1 447 101 101 SER CB C 62.322 0.3 1 448 101 101 SER N N 115.265 0.3 1 449 102 102 GLU H H 8.131 0.020 1 450 102 102 GLU C C 179.448 0.3 1 451 102 102 GLU CA C 59.338 0.3 1 452 102 102 GLU CB C 29.348 0.3 1 453 102 102 GLU N N 122.518 0.3 1 454 103 103 LEU H H 8.857 0.020 1 455 103 103 LEU C C 179.358 0.3 1 456 103 103 LEU CA C 57.884 0.3 1 457 103 103 LEU CB C 43.119 0.3 1 458 103 103 LEU N N 120.811 0.3 1 459 104 104 GLY H H 8.100 0.020 1 460 104 104 GLY C C 176.440 0.3 1 461 104 104 GLY CA C 47.709 0.3 1 462 104 104 GLY N N 104.881 0.3 1 463 105 105 LYS H H 7.576 0.020 1 464 105 105 LYS C C 179.546 0.3 1 465 105 105 LYS CA C 58.879 0.3 1 466 105 105 LYS CB C 32.179 0.3 1 467 105 105 LYS N N 120.836 0.3 1 468 106 106 THR H H 8.595 0.020 1 469 106 106 THR C C 175.609 0.3 1 470 106 106 THR CA C 66.571 0.3 1 471 106 106 THR CB C 68.714 0.3 1 472 106 106 THR N N 118.597 0.3 1 473 107 107 PHE H H 7.748 0.020 1 474 107 107 PHE C C 174.973 0.3 1 475 107 107 PHE CA C 57.502 0.3 1 476 107 107 PHE CB C 39.447 0.3 1 477 107 107 PHE N N 114.507 0.3 1 478 108 108 GLY H H 7.556 0.020 1 479 108 108 GLY C C 175.048 0.3 1 480 108 108 GLY CA C 47.327 0.3 1 481 108 108 GLY N N 111.482 0.3 1 482 109 109 VAL H H 8.382 0.020 1 483 109 109 VAL C C 175.066 0.3 1 484 109 109 VAL CA C 63.240 0.3 1 485 109 109 VAL CB C 30.725 0.3 1 486 109 109 VAL N N 120.017 0.3 1 487 110 110 GLU H H 8.447 0.020 1 488 110 110 GLU C C 175.853 0.3 1 489 110 110 GLU CA C 55.902 0.3 1 490 110 110 GLU CB C 31.342 0.3 1 491 110 110 GLU N N 126.448 0.3 1 492 111 111 SER H H 7.678 0.020 1 493 111 111 SER C C 171.378 0.3 1 494 111 111 SER CA C 56.431 0.3 1 495 111 111 SER CB C 65.229 0.3 1 496 111 111 SER N N 112.926 0.3 1 497 112 112 ILE H H 7.897 0.020 1 498 112 112 ILE C C 172.063 0.3 1 499 112 112 ILE CA C 58.190 0.3 1 500 112 112 ILE CB C 40.365 0.3 1 501 112 112 ILE N N 113.613 0.3 1 502 113 113 PRO C C 175.749 0.3 1 503 113 113 PRO CA C 61.327 0.3 1 504 113 113 PRO CB C 36.387 0.3 1 505 114 114 THR H H 8.069 0.020 1 506 114 114 THR C C 171.769 0.3 1 507 114 114 THR CA C 63.087 0.3 1 508 114 114 THR CB C 73.262 0.3 1 509 114 114 THR N N 116.711 0.3 1 510 115 115 LEU H H 8.836 0.020 1 511 115 115 LEU C C 175.242 0.3 1 512 115 115 LEU CA C 53.371 0.3 1 513 115 115 LEU CB C 46.485 0.3 1 514 115 115 LEU N N 127.321 0.3 1 515 116 116 ILE H H 8.867 0.020 1 516 116 116 ILE C C 174.215 0.3 1 517 116 116 ILE CA C 58.610 0.3 1 518 116 116 ILE CB C 38.709 0.3 1 519 116 116 ILE N N 125.295 0.3 1 520 117 117 THR H H 8.492 0.020 1 521 117 117 THR C C 173.701 0.3 1 522 117 117 THR CA C 61.710 0.3 1 523 117 117 THR CB C 67.983 0.3 1 524 117 117 THR N N 125.075 0.3 1 525 118 118 ILE H H 9.387 0.020 1 526 118 118 ILE C C 174.679 0.3 1 527 118 118 ILE CA C 58.803 0.3 1 528 118 118 ILE CB C 42.430 0.3 1 529 118 118 ILE N N 126.121 0.3 1 530 119 119 ASN H H 8.625 0.020 1 531 119 119 ASN C C 175.682 0.3 1 532 119 119 ASN CA C 53.218 0.3 1 533 119 119 ASN CB C 39.753 0.3 1 534 119 119 ASN N N 124.605 0.3 1 535 120 120 ALA H H 8.006 0.020 1 536 120 120 ALA C C 177.467 0.3 1 537 120 120 ALA CA C 55.742 0.3 1 538 120 120 ALA CB C 19.938 0.3 1 539 120 120 ALA N N 128.677 0.3 1 540 121 121 ASP H H 8.413 0.020 1 541 121 121 ASP C C 178.494 0.3 1 542 121 121 ASP CA C 56.737 0.3 1 543 121 121 ASP CB C 40.671 0.3 1 544 121 121 ASP N N 115.265 0.3 1 545 122 122 THR H H 7.936 0.020 1 546 122 122 THR C C 177.247 0.3 1 547 122 122 THR CA C 61.480 0.3 1 548 122 122 THR CB C 70.737 0.3 1 549 122 122 THR N N 107.148 0.3 1 550 123 123 GLY H H 8.695 0.020 1 551 123 123 GLY C C 172.332 0.3 1 552 123 123 GLY CA C 45.414 0.3 1 553 123 123 GLY N N 112.033 0.3 1 554 124 124 ALA H H 7.924 0.020 1 555 124 124 ALA C C 176.513 0.3 1 556 124 124 ALA CA C 52.759 0.3 1 557 124 124 ALA CB C 19.097 0.3 1 558 124 124 ALA N N 122.847 0.3 1 559 125 125 ILE H H 8.590 0.020 1 560 125 125 ILE C C 176.953 0.3 1 561 125 125 ILE CA C 61.133 0.3 1 562 125 125 ILE CB C 37.214 0.3 1 563 125 125 ILE N N 121.382 0.3 1 564 126 126 ILE H H 8.759 0.020 1 565 126 126 ILE C C 176.195 0.3 1 566 126 126 ILE CA C 62.628 0.3 1 567 126 126 ILE CB C 39.141 0.3 1 568 126 126 ILE N N 131.889 0.3 1 569 127 127 GLY H H 7.490 0.020 1 570 127 127 GLY C C 172.038 0.3 1 571 127 127 GLY CA C 45.644 0.3 1 572 127 127 GLY N N 104.300 0.3 1 573 128 128 THR H H 8.711 0.020 1 574 128 128 THR C C 175.462 0.3 1 575 128 128 THR CA C 61.623 0.3 1 576 128 128 THR CB C 70.083 0.3 1 577 128 128 THR N N 107.496 0.3 1 578 129 129 GLN H H 7.959 0.020 1 579 129 129 GLN C C 177.174 0.3 1 580 129 129 GLN CA C 54.671 0.3 1 581 129 129 GLN CB C 28.813 0.3 1 582 129 129 GLN N N 119.735 0.3 1 583 130 130 ALA H H 9.167 0.020 1 584 130 130 ALA C C 176.709 0.3 1 585 130 130 ALA CA C 55.513 0.3 1 586 130 130 ALA CB C 18.867 0.3 1 587 130 130 ALA N N 122.462 0.3 1 588 131 131 ARG H H 8.076 0.020 1 589 131 131 ARG C C 176.367 0.3 1 590 131 131 ARG CA C 59.185 0.3 1 591 131 131 ARG CB C 29.501 0.3 1 592 131 131 ARG N N 116.295 0.3 1 593 132 132 THR H H 6.973 0.020 1 594 132 132 THR C C 176.367 0.3 1 595 132 132 THR CA C 64.081 0.3 1 596 132 132 THR CB C 68.748 0.3 1 597 132 132 THR N N 109.107 0.3 1 598 133 133 ARG H H 7.153 0.020 1 599 133 133 ARG C C 177.320 0.3 1 600 133 133 ARG CA C 57.119 0.3 1 601 133 133 ARG CB C 27.512 0.3 1 602 133 133 ARG N N 120.062 0.3 1 603 134 134 VAL H H 7.435 0.020 1 604 134 134 VAL C C 176.073 0.3 1 605 134 134 VAL CA C 64.387 0.3 1 606 134 134 VAL CB C 31.184 0.3 1 607 134 134 VAL N N 116.059 0.3 1 608 135 135 ILE H H 6.265 0.020 1 609 135 135 ILE C C 177.687 0.3 1 610 135 135 ILE CA C 62.551 0.3 1 611 135 135 ILE CB C 37.381 0.3 1 612 135 135 ILE N N 116.329 0.3 1 613 136 136 GLU H H 6.996 0.020 1 614 136 136 GLU C C 175.926 0.3 1 615 136 136 GLU CA C 57.043 0.3 1 616 136 136 GLU CB C 30.572 0.3 1 617 136 136 GLU N N 116.572 0.3 1 618 137 137 ASP H H 7.869 0.020 1 619 137 137 ASP C C 173.163 0.3 1 620 137 137 ASP CA C 51.535 0.3 1 621 137 137 ASP CB C 41.206 0.3 1 622 137 137 ASP N N 118.429 0.3 1 623 138 138 PRO C C 178.254 0.3 1 624 138 138 PRO CA C 64.999 0.3 1 625 138 138 PRO CB C 31.796 0.3 1 626 139 139 ASP H H 8.543 0.020 1 627 139 139 ASP C C 176.513 0.3 1 628 139 139 ASP CA C 53.983 0.3 1 629 139 139 ASP CB C 40.824 0.3 1 630 139 139 ASP N N 115.127 0.3 1 631 140 140 GLY H H 8.789 0.020 1 632 140 140 GLY C C 175.633 0.3 1 633 140 140 GLY CA C 47.939 0.3 1 634 140 140 GLY N N 109.934 0.3 1 635 141 141 ALA H H 9.900 0.020 1 636 141 141 ALA C C 180.157 0.3 1 637 141 141 ALA CA C 55.436 0.3 1 638 141 141 ALA CB C 18.102 0.3 1 639 141 141 ALA N N 126.943 0.3 1 640 142 142 ASN H H 10.349 0.020 1 641 142 142 ASN C C 174.704 0.3 1 642 142 142 ASN CA C 51.581 0.3 1 643 142 142 ASN CB C 39.523 0.3 1 644 142 142 ASN N N 114.391 0.3 1 645 143 143 PHE H H 6.669 0.020 1 646 143 143 PHE C C 172.992 0.3 1 647 143 143 PHE CA C 55.895 0.3 1 648 143 143 PHE CB C 39.523 0.3 1 649 143 143 PHE N N 122.830 0.3 1 650 144 144 PRO C C 171.702 0.3 1 651 144 144 PRO CA C 63.699 0.3 1 652 144 144 PRO CB C 30.190 0.3 1 653 145 145 TRP H H 8.429 0.020 1 654 145 145 TRP C C 171.940 0.3 1 655 145 145 TRP CA C 57.808 0.3 1 656 145 145 TRP CB C 24.834 0.3 1 657 145 145 TRP N N 118.062 0.3 1 658 146 146 PRO C C 177.186 0.3 1 659 146 146 PRO CA C 63.087 0.3 1 660 146 146 PRO CB C 31.720 0.3 1 661 147 147 ASN H H 8.175 0.020 1 662 147 147 ASN C C 179.203 0.3 1 663 147 147 ASN CA C 55.589 0.3 1 664 147 147 ASN CB C 39.982 0.3 1 665 147 147 ASN N N 123.554 0.3 1 stop_ save_