data_27049 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Trypanosoma brucei brucei Tryparedoxin reduced ; _BMRB_accession_number 27049 _BMRB_flat_file_name bmr27049.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 'R. 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" 132 "13C chemical shifts" 413 "15N chemical shifts" 132 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-03-14 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 27050 'Trypanosoma brucei brucei Tryparedoxin oxidized' 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 reduced' $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 free' 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' 56917 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' 'potassium phosphate' 25 mM 'natural abundance' TCEP 2 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 255 uM '[U-13C; U-15N]' 'sodium chloride' 125 mM 'natural abundance' 'potassium phosphate' 25 mM 'natural abundance' TCEP 2 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' 'potassium phosphate' 25 mM 'natural abundance' TCEP 2 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' 'potassium phosphate' 25 mM 'natural abundance' TCEP 2 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' 'potassium phosphate' 25 mM 'natural abundance' TCEP 2 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' 'potassium phosphate' 25 mM 'natural abundance' TCEP 2 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' 'potassium phosphate' 25 mM 'natural abundance' TCEP 2 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_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $13C-15N-Pro-Tpx save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $15N-Arg-Tpx save_ save_2D_1H-15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $15N-Trp-Tpx save_ save_2D_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $15N-Lys-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_ save_3D_HN(CO)CA_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $U-13C-15N-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 $13C-15N-Pro-Tpx $15N-Arg-Tpx $15N-Trp-Tpx $15N-Lys-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 reduced' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 ALA C C 177.785 0.3 1 2 3 3 MET H H 8.461 0.020 1 3 3 3 MET C C 176.611 0.3 1 4 3 3 MET CA C 55.496 0.3 1 5 3 3 MET N N 119.622 0.3 1 6 4 4 GLY H H 8.440 0.020 1 7 4 4 GLY C C 173.554 0.3 1 8 4 4 GLY CA C 45.126 0.3 1 9 4 4 GLY N N 110.098 0.3 1 10 5 5 SER H H 8.052 0.020 1 11 5 5 SER C C 175.642 0.3 1 12 5 5 SER CA C 58.145 0.3 1 13 5 5 SER CB C 64.251 0.3 1 14 5 5 SER N N 114.192 0.3 1 15 6 6 GLY H H 8.306 0.020 1 16 6 6 GLY C C 174.869 0.3 1 17 6 6 GLY CA C 46.443 0.3 1 18 6 6 GLY N N 112.717 0.3 1 19 7 7 LEU H H 8.268 0.020 1 20 7 7 LEU C C 177.712 0.3 1 21 7 7 LEU CA C 56.813 0.3 1 22 7 7 LEU CB C 42.277 0.3 1 23 7 7 LEU N N 120.402 0.3 1 24 8 8 ALA H H 7.748 0.020 1 25 8 8 ALA C C 178.316 0.3 1 26 8 8 ALA CA C 53.870 0.3 1 27 8 8 ALA CB C 17.872 0.3 1 28 8 8 ALA N N 119.732 0.3 1 29 9 9 LYS H H 7.245 0.020 1 30 9 9 LYS C C 177.054 0.3 1 31 9 9 LYS CA C 58.190 0.3 1 32 9 9 LYS CB C 31.949 0.3 1 33 9 9 LYS N N 116.263 0.3 1 34 10 10 TYR H H 7.336 0.020 1 35 10 10 TYR C C 174.220 0.3 1 36 10 10 TYR CA C 57.655 0.3 1 37 10 10 TYR CB C 39.676 0.3 1 38 10 10 TYR N N 115.315 0.3 1 39 11 11 LEU H H 7.516 0.020 1 40 11 11 LEU C C 173.114 0.3 1 41 11 11 LEU CA C 51.229 0.3 1 42 11 11 LEU CB C 42.507 0.3 1 43 11 11 LEU N N 117.669 0.3 1 44 12 12 PRO C C 177.983 0.3 1 45 12 12 PRO CA C 63.653 0.3 1 46 12 12 PRO CB C 31.294 0.3 1 47 13 13 GLY H H 8.716 0.020 1 48 13 13 GLY C C 174.092 0.3 1 49 13 13 GLY CA C 46.015 0.3 1 50 13 13 GLY N N 110.996 0.3 1 51 14 14 ALA H H 7.927 0.020 1 52 14 14 ALA C C 177.002 0.3 1 53 14 14 ALA CA C 51.821 0.3 1 54 14 14 ALA CB C 18.528 0.3 1 55 14 14 ALA N N 122.097 0.3 1 56 15 15 THR H H 7.971 0.020 1 57 15 15 THR C C 173.603 0.3 1 58 15 15 THR CA C 63.087 0.3 1 59 15 15 THR CB C 69.896 0.3 1 60 15 15 THR N N 114.457 0.3 1 61 16 16 ASN H H 8.154 0.020 1 62 16 16 ASN C C 174.264 0.3 1 63 16 16 ASN CA C 52.070 0.3 1 64 16 16 ASN CB C 40.747 0.3 1 65 16 16 ASN N N 121.608 0.3 1 66 17 17 LEU H H 8.941 0.020 1 67 17 17 LEU C C 176.318 0.3 1 68 17 17 LEU CA C 52.835 0.3 1 69 17 17 LEU CB C 43.718 0.3 1 70 17 17 LEU N N 118.025 0.3 1 71 18 18 LEU H H 9.108 0.020 1 72 18 18 LEU C C 175.584 0.3 1 73 18 18 LEU CA C 55.207 0.3 1 74 18 18 LEU CB C 42.890 0.3 1 75 18 18 LEU N N 119.217 0.3 1 76 19 19 SER H H 7.958 0.020 1 77 19 19 SER C C 175.462 0.3 1 78 19 19 SER CA C 56.584 0.3 1 79 19 19 SER CB C 68.519 0.3 1 80 19 19 SER N N 115.296 0.3 1 81 20 20 LYS H H 8.833 0.020 1 82 20 20 LYS C C 177.736 0.3 1 83 20 20 LYS CA C 56.890 0.3 1 84 20 20 LYS CB C 30.802 0.3 1 85 20 20 LYS N N 117.812 0.3 1 86 21 21 SER H H 8.181 0.020 1 87 21 21 SER C C 173.652 0.3 1 88 21 21 SER CA C 57.126 0.3 1 89 21 21 SER CB C 63.594 0.3 1 90 21 21 SER N N 112.135 0.3 1 91 22 22 GLY H H 7.465 0.020 1 92 22 22 GLY C C 173.334 0.3 1 93 22 22 GLY CA C 44.802 0.3 1 94 22 22 GLY N N 110.968 0.3 1 95 23 23 GLU H H 8.507 0.020 1 96 23 23 GLU C C 176.856 0.3 1 97 23 23 GLU CA C 56.354 0.3 1 98 23 23 GLU CB C 32.102 0.3 1 99 23 23 GLU N N 122.230 0.3 1 100 24 24 VAL H H 9.079 0.020 1 101 24 24 VAL C C 174.337 0.3 1 102 24 24 VAL CA C 59.568 0.3 1 103 24 24 VAL CB C 35.622 0.3 1 104 24 24 VAL N N 117.064 0.3 1 105 25 25 SER H H 8.574 0.020 1 106 25 25 SER C C 177.198 0.3 1 107 25 25 SER CA C 57.043 0.3 1 108 25 25 SER CB C 64.770 0.3 1 109 25 25 SER N N 117.864 0.3 1 110 26 26 LEU H H 8.880 0.020 1 111 26 26 LEU C C 179.717 0.3 1 112 26 26 LEU CA C 58.190 0.3 1 113 26 26 LEU CB C 40.977 0.3 1 114 26 26 LEU N N 124.769 0.3 1 115 27 27 GLY H H 8.537 0.020 1 116 27 27 GLY C C 175.679 0.3 1 117 27 27 GLY CA C 46.369 0.3 1 118 27 27 GLY N N 105.534 0.3 1 119 28 28 SER H H 7.738 0.020 1 120 28 28 SER C C 175.168 0.3 1 121 28 28 SER CA C 60.485 0.3 1 122 28 28 SER CB C 63.301 0.3 1 123 28 28 SER N N 115.946 0.3 1 124 29 29 LEU H H 7.513 0.020 1 125 29 29 LEU C C 174.182 0.3 1 126 29 29 LEU CA C 54.595 0.3 1 127 29 29 LEU CB C 40.594 0.3 1 128 29 29 LEU N N 121.518 0.3 1 129 30 30 VAL H H 6.748 0.020 1 130 30 30 VAL C C 177.028 0.3 1 131 30 30 VAL CA C 63.087 0.3 1 132 30 30 VAL CB C 31.873 0.3 1 133 30 30 VAL N N 115.800 0.3 1 134 31 31 GLY H H 9.872 0.020 1 135 31 31 GLY C C 174.728 0.3 1 136 31 31 GLY CA C 45.644 0.3 1 137 31 31 GLY N N 116.577 0.3 1 138 32 32 LYS H H 7.666 0.020 1 139 32 32 LYS C C 177.809 0.3 1 140 32 32 LYS CA C 56.278 0.3 1 141 32 32 LYS CB C 34.091 0.3 1 142 32 32 LYS N N 117.436 0.3 1 143 33 33 THR H H 7.711 0.020 1 144 33 33 THR C C 173.339 0.3 1 145 33 33 THR CA C 64.005 0.3 1 146 33 33 THR CB C 68.672 0.3 1 147 33 33 THR N N 118.272 0.3 1 148 34 34 VAL H H 9.333 0.020 1 149 34 34 VAL C C 173.774 0.3 1 150 34 34 VAL CA C 60.639 0.3 1 151 34 34 VAL CB C 34.780 0.3 1 152 34 34 VAL N N 126.968 0.3 1 153 35 35 PHE H H 9.073 0.020 1 154 35 35 PHE C C 175.560 0.3 1 155 35 35 PHE CA C 55.666 0.3 1 156 35 35 PHE CB C 40.747 0.3 1 157 35 35 PHE N N 124.289 0.3 1 158 36 36 LEU H H 9.463 0.020 1 159 36 36 LEU C C 174.875 0.3 1 160 36 36 LEU CA C 53.709 0.3 1 161 36 36 LEU CB C 41.818 0.3 1 162 36 36 LEU N N 123.987 0.3 1 163 37 37 TYR H H 8.863 0.020 1 164 37 37 TYR C C 172.600 0.3 1 165 37 37 TYR CA C 52.963 0.3 1 166 37 37 TYR CB C 38.872 0.3 1 167 37 37 TYR N N 125.697 0.3 1 168 38 38 PHE H H 9.014 0.020 1 169 38 38 PHE C C 174.092 0.3 1 170 38 38 PHE CA C 56.149 0.3 1 171 38 38 PHE CB C 39.217 0.3 1 172 38 38 PHE N N 129.958 0.3 1 173 39 39 SER H H 7.325 0.020 1 174 39 39 SER C C 172.258 0.3 1 175 39 39 SER CA C 55.538 0.3 1 176 39 39 SER CB C 65.999 0.3 1 177 39 39 SER N N 113.552 0.3 1 178 40 40 ALA C C 175.676 0.3 1 179 40 40 ALA CA C 51.653 0.3 1 180 40 40 ALA CB C 22.927 0.3 1 181 41 41 SER H H 9.410 0.020 1 182 41 41 SER C C 175.959 0.3 1 183 41 41 SER CA C 60.215 0.3 1 184 41 41 SER CB C 63.157 0.3 1 185 41 41 SER N N 117.807 0.3 1 186 42 42 TRP H H 6.348 0.020 1 187 42 42 TRP C C 174.948 0.3 1 188 42 42 TRP CA C 54.169 0.3 1 189 42 42 TRP CB C 29.501 0.3 1 190 42 42 TRP N N 115.293 0.3 1 191 43 43 CYS H H 6.503 0.020 1 192 43 43 CYS C C 173.799 0.3 1 193 43 43 CYS CA C 55.372 0.3 1 194 43 43 CYS CB C 27.705 0.3 1 195 43 43 CYS N N 125.194 0.3 1 196 45 45 PRO C C 180.915 0.3 1 197 45 45 PRO CA C 66.629 0.3 1 198 46 46 CYS H H 7.930 0.020 1 199 46 46 CYS C C 176.978 0.3 1 200 46 46 CYS CA C 53.574 0.3 1 201 46 46 CYS CB C 29.364 0.3 1 202 46 46 CYS N N 120.595 0.3 1 203 47 47 ARG H H 7.847 0.020 1 204 47 47 ARG C C 179.912 0.3 1 205 47 47 ARG CA C 59.269 0.3 1 206 47 47 ARG CB C 29.953 0.3 1 207 47 47 ARG N N 118.566 0.3 1 208 48 48 GLY H H 7.823 0.020 1 209 48 48 GLY C C 174.765 0.3 1 210 48 48 GLY CA C 45.861 0.3 1 211 48 48 GLY N N 102.260 0.3 1 212 49 49 PHE H H 7.934 0.020 1 213 49 49 PHE C C 176.991 0.3 1 214 49 49 PHE CA C 59.721 0.3 1 215 49 49 PHE CB C 40.594 0.3 1 216 49 49 PHE N N 122.087 0.3 1 217 50 50 THR H H 8.862 0.020 1 218 50 50 THR C C 177.736 0.3 1 219 50 50 THR CA C 69.437 0.3 1 220 50 50 THR CB C 68.213 0.3 1 221 50 50 THR N N 117.529 0.3 1 222 51 51 PRO C C 179.060 0.3 1 223 51 51 PRO CA C 65.734 0.3 1 224 51 51 PRO CB C 30.995 0.3 1 225 52 52 VAL H H 6.856 0.020 1 226 52 52 VAL C C 179.179 0.3 1 227 52 52 VAL CA C 65.535 0.3 1 228 52 52 VAL CB C 31.519 0.3 1 229 52 52 VAL N N 120.666 0.3 1 230 53 53 LEU H H 7.511 0.020 1 231 53 53 LEU C C 178.671 0.3 1 232 53 53 LEU CA C 56.758 0.3 1 233 53 53 LEU CB C 40.135 0.3 1 234 53 53 LEU N N 122.295 0.3 1 235 54 54 ALA H H 9.095 0.020 1 236 54 54 ALA C C 178.812 0.3 1 237 54 54 ALA CA C 56.354 0.3 1 238 54 54 ALA CB C 17.184 0.3 1 239 54 54 ALA N N 121.927 0.3 1 240 55 55 GLU H H 7.706 0.020 1 241 55 55 GLU C C 178.027 0.3 1 242 55 55 GLU CA C 59.718 0.3 1 243 55 55 GLU CB C 29.348 0.3 1 244 55 55 GLU N N 120.181 0.3 1 245 56 56 PHE H H 7.643 0.020 1 246 56 56 PHE C C 177.369 0.3 1 247 56 56 PHE CA C 61.626 0.3 1 248 56 56 PHE CB C 39.676 0.3 1 249 56 56 PHE N N 120.657 0.3 1 250 57 57 TYR H H 9.477 0.020 1 251 57 57 TYR C C 178.372 0.3 1 252 57 57 TYR CA C 61.944 0.3 1 253 57 57 TYR CB C 40.174 0.3 1 254 57 57 TYR N N 119.324 0.3 1 255 58 58 GLU H H 9.200 0.020 1 256 58 58 GLU C C 179.179 0.3 1 257 58 58 GLU CA C 59.644 0.3 1 258 58 58 GLU CB C 29.272 0.3 1 259 58 58 GLU N N 121.720 0.3 1 260 59 59 LYS H H 7.736 0.020 1 261 59 59 LYS C C 179.279 0.3 1 262 59 59 LYS CA C 59.206 0.3 1 263 59 59 LYS CB C 32.778 0.3 1 264 59 59 LYS N N 116.052 0.3 1 265 60 60 HIS H H 7.612 0.020 1 266 60 60 HIS C C 176.684 0.3 1 267 60 60 HIS CA C 57.043 0.3 1 268 60 60 HIS CB C 34.002 0.3 1 269 60 60 HIS N N 111.369 0.3 1 270 61 61 HIS H H 8.587 0.020 1 271 61 61 HIS C C 175.024 0.3 1 272 61 61 HIS CA C 59.371 0.3 1 273 61 61 HIS CB C 25.293 0.3 1 274 61 61 HIS N N 118.090 0.3 1 275 62 62 VAL H H 6.837 0.020 1 276 62 62 VAL C C 179.032 0.3 1 277 62 62 VAL CA C 65.076 0.3 1 278 62 62 VAL CB C 30.802 0.3 1 279 62 62 VAL N N 118.674 0.3 1 280 63 63 ALA H H 8.344 0.020 1 281 63 63 ALA C C 179.790 0.3 1 282 63 63 ALA CA C 55.207 0.3 1 283 63 63 ALA CB C 18.791 0.3 1 284 63 63 ALA N N 123.822 0.3 1 285 64 64 LYS H H 8.242 0.020 1 286 64 64 LYS C C 174.802 0.3 1 287 64 64 LYS CA C 55.839 0.3 1 288 64 64 LYS CB C 31.108 0.3 1 289 64 64 LYS N N 112.045 0.3 1 290 65 65 ASN H H 7.185 0.020 1 291 65 65 ASN C C 173.041 0.3 1 292 65 65 ASN CA C 53.524 0.3 1 293 65 65 ASN CB C 37.764 0.3 1 294 65 65 ASN N N 119.322 0.3 1 295 66 66 PHE H H 8.362 0.020 1 296 66 66 PHE C C 173.051 0.3 1 297 66 66 PHE CA C 54.671 0.3 1 298 66 66 PHE CB C 43.884 0.3 1 299 66 66 PHE N N 113.156 0.3 1 300 67 67 GLU H H 8.936 0.020 1 301 67 67 GLU C C 174.266 0.3 1 302 67 67 GLU CA C 52.912 0.3 1 303 67 67 GLU CB C 36.111 0.3 1 304 67 67 GLU N N 119.047 0.3 1 305 68 68 VAL H H 9.351 0.020 1 306 68 68 VAL C C 172.999 0.3 1 307 68 68 VAL CA C 60.562 0.3 1 308 68 68 VAL CB C 34.015 0.3 1 309 68 68 VAL N N 125.411 0.3 1 310 69 69 VAL H H 8.770 0.020 1 311 69 69 VAL C C 174.875 0.3 1 312 69 69 VAL CA C 60.180 0.3 1 313 69 69 VAL CB C 34.168 0.3 1 314 69 69 VAL N N 124.833 0.3 1 315 70 70 LEU H H 9.215 0.020 1 316 70 70 LEU C C 173.481 0.3 1 317 70 70 LEU CA C 55.991 0.3 1 318 70 70 LEU CB C 43.349 0.3 1 319 70 70 LEU N N 129.154 0.3 1 320 71 71 ILE H H 8.946 0.020 1 321 71 71 ILE C C 174.312 0.3 1 322 71 71 ILE CA C 58.059 0.3 1 323 71 71 ILE CB C 34.957 0.3 1 324 71 71 ILE N N 131.232 0.3 1 325 72 72 SER H H 8.918 0.020 1 326 72 72 SER C C 177.500 0.3 1 327 72 72 SER CA C 59.150 0.3 1 328 72 72 SER CB C 64.999 0.3 1 329 72 72 SER N N 116.921 0.3 1 330 73 73 TRP H H 8.744 0.020 1 331 73 73 TRP C C 177.198 0.3 1 332 73 73 TRP CA C 55.697 0.3 1 333 73 73 TRP CB C 29.348 0.3 1 334 73 73 TRP N N 127.684 0.3 1 335 74 74 ASP H H 9.451 0.020 1 336 74 74 ASP C C 174.802 0.3 1 337 74 74 ASP CA C 58.190 0.3 1 338 74 74 ASP CB C 41.895 0.3 1 339 74 74 ASP N N 122.545 0.3 1 340 75 75 GLU H H 9.456 0.020 1 341 75 75 GLU C C 176.047 0.3 1 342 75 75 GLU CA C 56.966 0.3 1 343 75 75 GLU CB C 31.220 0.3 1 344 75 75 GLU N N 116.987 0.3 1 345 76 76 ASN H H 7.526 0.020 1 346 76 76 ASN C C 174.068 0.3 1 347 76 76 ASN CA C 51.917 0.3 1 348 76 76 ASN CB C 40.824 0.3 1 349 76 76 ASN N N 113.591 0.3 1 350 77 77 GLU H H 8.806 0.020 1 351 77 77 GLU C C 177.051 0.3 1 352 77 77 GLU CA C 59.046 0.3 1 353 77 77 GLU CB C 29.481 0.3 1 354 77 77 GLU N N 124.310 0.3 1 355 78 78 SER H H 8.190 0.020 1 356 78 78 SER C C 177.223 0.3 1 357 78 78 SER CA C 61.718 0.3 1 358 78 78 SER N N 115.491 0.3 1 359 79 79 ASP H H 8.057 0.020 1 360 79 79 ASP C C 178.592 0.3 1 361 79 79 ASP CA C 57.196 0.3 1 362 79 79 ASP CB C 40.059 0.3 1 363 79 79 ASP N N 122.412 0.3 1 364 80 80 PHE H H 7.649 0.020 1 365 80 80 PHE C C 176.353 0.3 1 366 80 80 PHE CA C 61.480 0.3 1 367 80 80 PHE CB C 38.835 0.3 1 368 80 80 PHE N N 119.354 0.3 1 369 81 81 HIS H H 8.479 0.020 1 370 81 81 HIS C C 179.399 0.3 1 371 81 81 HIS CA C 60.525 0.3 1 372 81 81 HIS CB C 29.996 0.3 1 373 81 81 HIS N N 118.495 0.3 1 374 82 82 ASP H H 8.210 0.020 1 375 82 82 ASP C C 177.721 0.3 1 376 82 82 ASP CA C 57.272 0.3 1 377 82 82 ASP CB C 41.206 0.3 1 378 82 82 ASP N N 120.978 0.3 1 379 83 83 TYR H H 8.034 0.020 1 380 83 83 TYR C C 178.201 0.3 1 381 83 83 TYR CA C 58.598 0.3 1 382 83 83 TYR CB C 39.272 0.3 1 383 83 83 TYR N N 120.544 0.3 1 384 84 84 TYR H H 8.835 0.020 1 385 84 84 TYR C C 178.567 0.3 1 386 84 84 TYR CA C 58.649 0.3 1 387 84 84 TYR CB C 36.999 0.3 1 388 84 84 TYR N N 118.906 0.3 1 389 85 85 GLY H H 7.643 0.020 1 390 85 85 GLY C C 174.312 0.3 1 391 85 85 GLY CA C 46.256 0.3 1 392 85 85 GLY N N 105.464 0.3 1 393 86 86 LYS H H 6.888 0.020 1 394 86 86 LYS C C 176.049 0.3 1 395 86 86 LYS CA C 55.513 0.3 1 396 86 86 LYS CB C 32.179 0.3 1 397 86 86 LYS N N 117.178 0.3 1 398 87 87 MET H H 7.423 0.020 1 399 87 87 MET C C 174.875 0.3 1 400 87 87 MET CA C 52.376 0.3 1 401 87 87 MET CB C 31.643 0.3 1 402 87 87 MET N N 118.270 0.3 1 403 89 89 TRP C C 174.207 0.3 1 404 89 89 TRP CA C 55.487 0.3 1 405 89 89 TRP CB C 27.130 0.3 1 406 90 90 LEU H H 8.479 0.020 1 407 90 90 LEU C C 178.054 0.3 1 408 90 90 LEU CA C 55.054 0.3 1 409 90 90 LEU CB C 44.649 0.3 1 410 90 90 LEU N N 121.213 0.3 1 411 91 91 ALA H H 8.617 0.020 1 412 91 91 ALA C C 175.609 0.3 1 413 91 91 ALA CA C 51.763 0.3 1 414 91 91 ALA CB C 21.198 0.3 1 415 91 91 ALA N N 118.588 0.3 1 416 92 92 LEU H H 8.205 0.020 1 417 92 92 LEU C C 174.019 0.3 1 418 92 92 LEU CA C 52.479 0.3 1 419 92 92 LEU CB C 43.119 0.3 1 420 92 92 LEU N N 125.673 0.3 1 421 93 93 PRO C C 177.333 0.3 1 422 93 93 PRO CA C 63.834 0.3 1 423 93 93 PRO CB C 32.191 0.3 1 424 94 94 PHE H H 7.959 0.020 1 425 94 94 PHE C C 174.679 0.3 1 426 94 94 PHE CA C 61.648 0.3 1 427 94 94 PHE CB C 38.692 0.3 1 428 94 94 PHE N N 125.435 0.3 1 429 95 95 ASP H H 8.164 0.020 1 430 95 95 ASP C C 177.626 0.3 1 431 95 95 ASP CA C 54.977 0.3 1 432 95 95 ASP CB C 39.370 0.3 1 433 95 95 ASP N N 112.036 0.3 1 434 96 96 GLN H H 7.235 0.020 1 435 96 96 GLN C C 177.341 0.3 1 436 96 96 GLN CA C 53.830 0.3 1 437 96 96 GLN CB C 25.725 0.3 1 438 96 96 GLN N N 121.902 0.3 1 439 97 97 ARG H H 7.609 0.020 1 440 97 97 ARG C C 179.978 0.3 1 441 97 97 ARG CA C 58.573 0.3 1 442 97 97 ARG CB C 31.720 0.3 1 443 97 97 ARG N N 122.422 0.3 1 444 98 98 SER C C 176.958 0.3 1 445 98 98 SER CA C 61.552 0.3 1 446 99 99 THR H H 7.618 0.020 1 447 99 99 THR C C 175.388 0.3 1 448 99 99 THR CA C 66.011 0.3 1 449 99 99 THR CB C 68.436 0.3 1 450 99 99 THR N N 119.012 0.3 1 451 100 100 VAL H H 7.289 0.020 1 452 100 100 VAL C C 179.081 0.3 1 453 100 100 VAL CA C 67.983 0.3 1 454 100 100 VAL CB C 31.490 0.3 1 455 100 100 VAL N N 120.760 0.3 1 456 101 101 SER H H 7.599 0.020 1 457 101 101 SER C C 177.431 0.3 1 458 101 101 SER CA C 61.403 0.3 1 459 101 101 SER CB C 62.322 0.3 1 460 101 101 SER N N 115.385 0.3 1 461 102 102 GLU H H 8.149 0.020 1 462 102 102 GLU C C 179.448 0.3 1 463 102 102 GLU CA C 59.364 0.3 1 464 102 102 GLU CB C 29.348 0.3 1 465 102 102 GLU N N 122.455 0.3 1 466 103 103 LEU H H 8.879 0.020 1 467 103 103 LEU C C 179.358 0.3 1 468 103 103 LEU CA C 57.946 0.3 1 469 103 103 LEU CB C 43.119 0.3 1 470 103 103 LEU N N 120.749 0.3 1 471 104 104 GLY H H 8.127 0.020 1 472 104 104 GLY C C 176.440 0.3 1 473 104 104 GLY CA C 47.709 0.3 1 474 104 104 GLY N N 104.959 0.3 1 475 105 105 LYS H H 7.592 0.020 1 476 105 105 LYS C C 179.546 0.3 1 477 105 105 LYS CA C 58.879 0.3 1 478 105 105 LYS CB C 32.179 0.3 1 479 105 105 LYS N N 120.779 0.3 1 480 106 106 THR H H 8.575 0.020 1 481 106 106 THR C C 175.609 0.3 1 482 106 106 THR CA C 66.571 0.3 1 483 106 106 THR CB C 68.714 0.3 1 484 106 106 THR N N 118.617 0.3 1 485 107 107 PHE H H 7.755 0.020 1 486 107 107 PHE C C 174.973 0.3 1 487 107 107 PHE CA C 57.502 0.3 1 488 107 107 PHE CB C 39.447 0.3 1 489 107 107 PHE N N 114.505 0.3 1 490 108 108 GLY H H 7.564 0.020 1 491 108 108 GLY C C 175.070 0.3 1 492 108 108 GLY CA C 47.327 0.3 1 493 108 108 GLY N N 111.543 0.3 1 494 109 109 VAL H H 8.375 0.020 1 495 109 109 VAL C C 175.168 0.3 1 496 109 109 VAL CA C 63.388 0.3 1 497 109 109 VAL CB C 30.725 0.3 1 498 109 109 VAL N N 119.970 0.3 1 499 110 110 GLU H H 8.470 0.020 1 500 110 110 GLU C C 175.682 0.3 1 501 110 110 GLU CA C 55.790 0.3 1 502 110 110 GLU CB C 31.451 0.3 1 503 110 110 GLU N N 126.425 0.3 1 504 111 111 SER H H 7.671 0.020 1 505 111 111 SER C C 171.158 0.3 1 506 111 111 SER CA C 56.489 0.3 1 507 111 111 SER CB C 65.229 0.3 1 508 111 111 SER N N 113.267 0.3 1 509 112 112 ILE H H 7.881 0.020 1 510 112 112 ILE C C 171.647 0.3 1 511 112 112 ILE CA C 58.190 0.3 1 512 112 112 ILE CB C 40.365 0.3 1 513 112 112 ILE N N 114.322 0.3 1 514 113 113 PRO C C 176.640 0.3 1 515 113 113 PRO CA C 61.327 0.3 1 516 113 113 PRO CB C 36.387 0.3 1 517 114 114 THR H H 8.089 0.020 1 518 114 114 THR C C 172.011 0.3 1 519 114 114 THR CA C 63.302 0.3 1 520 114 114 THR CB C 73.478 0.3 1 521 114 114 THR N N 117.066 0.3 1 522 115 115 LEU H H 8.818 0.020 1 523 115 115 LEU C C 175.486 0.3 1 524 115 115 LEU CA C 53.295 0.3 1 525 115 115 LEU CB C 46.485 0.3 1 526 115 115 LEU N N 127.073 0.3 1 527 116 116 ILE H H 8.905 0.020 1 528 116 116 ILE C C 174.312 0.3 1 529 116 116 ILE CA C 58.454 0.3 1 530 116 116 ILE CB C 38.504 0.3 1 531 116 116 ILE N N 125.166 0.3 1 532 117 117 THR H H 8.508 0.020 1 533 117 117 THR C C 173.701 0.3 1 534 117 117 THR CA C 61.793 0.3 1 535 117 117 THR CB C 67.929 0.3 1 536 117 117 THR N N 125.193 0.3 1 537 118 118 ILE H H 9.402 0.020 1 538 118 118 ILE C C 174.679 0.3 1 539 118 118 ILE CA C 58.803 0.3 1 540 118 118 ILE CB C 42.300 0.3 1 541 118 118 ILE N N 126.347 0.3 1 542 119 119 ASN H H 8.625 0.020 1 543 119 119 ASN C C 175.682 0.3 1 544 119 119 ASN CA C 53.349 0.3 1 545 119 119 ASN CB C 39.753 0.3 1 546 119 119 ASN N N 124.605 0.3 1 547 120 120 ALA H H 8.006 0.020 1 548 120 120 ALA C C 177.467 0.3 1 549 120 120 ALA CA C 55.742 0.3 1 550 120 120 ALA CB C 19.938 0.3 1 551 120 120 ALA N N 128.677 0.3 1 552 121 121 ASP H H 8.413 0.020 1 553 121 121 ASP C C 178.494 0.3 1 554 121 121 ASP CA C 56.826 0.3 1 555 121 121 ASP CB C 40.671 0.3 1 556 121 121 ASP N N 115.265 0.3 1 557 122 122 THR H H 7.936 0.020 1 558 122 122 THR C C 177.247 0.3 1 559 122 122 THR CA C 61.480 0.3 1 560 122 122 THR CB C 70.737 0.3 1 561 122 122 THR N N 107.148 0.3 1 562 123 123 GLY H H 8.715 0.020 1 563 123 123 GLY C C 172.332 0.3 1 564 123 123 GLY CA C 45.414 0.3 1 565 123 123 GLY N N 112.089 0.3 1 566 124 124 ALA H H 7.924 0.020 1 567 124 124 ALA C C 176.513 0.3 1 568 124 124 ALA CA C 52.759 0.3 1 569 124 124 ALA CB C 19.097 0.3 1 570 124 124 ALA N N 122.847 0.3 1 571 125 125 ILE H H 8.590 0.020 1 572 125 125 ILE C C 176.953 0.3 1 573 125 125 ILE CA C 61.133 0.3 1 574 125 125 ILE CB C 37.214 0.3 1 575 125 125 ILE N N 121.382 0.3 1 576 126 126 ILE H H 8.779 0.020 1 577 126 126 ILE C C 176.195 0.3 1 578 126 126 ILE CA C 62.628 0.3 1 579 126 126 ILE CB C 39.141 0.3 1 580 126 126 ILE N N 131.873 0.3 1 581 127 127 GLY H H 7.470 0.020 1 582 127 127 GLY C C 172.038 0.3 1 583 127 127 GLY CA C 45.644 0.3 1 584 127 127 GLY N N 104.149 0.3 1 585 128 128 THR H H 8.711 0.020 1 586 128 128 THR C C 175.584 0.3 1 587 128 128 THR CA C 61.623 0.3 1 588 128 128 THR CB C 70.083 0.3 1 589 128 128 THR N N 107.496 0.3 1 590 129 129 GLN H H 7.913 0.020 1 591 129 129 GLN C C 177.296 0.3 1 592 129 129 GLN CA C 54.671 0.3 1 593 129 129 GLN CB C 28.813 0.3 1 594 129 129 GLN N N 119.565 0.3 1 595 130 130 ALA H H 9.247 0.020 1 596 130 130 ALA C C 176.709 0.3 1 597 130 130 ALA CA C 55.513 0.3 1 598 130 130 ALA CB C 18.867 0.3 1 599 130 130 ALA N N 122.503 0.3 1 600 131 131 ARG H H 8.027 0.020 1 601 131 131 ARG C C 176.505 0.3 1 602 131 131 ARG CA C 59.185 0.3 1 603 131 131 ARG CB C 29.501 0.3 1 604 131 131 ARG N N 116.242 0.3 1 605 132 132 THR H H 6.988 0.020 1 606 132 132 THR C C 176.458 0.3 1 607 132 132 THR CA C 64.199 0.3 1 608 132 132 THR CB C 68.748 0.3 1 609 132 132 THR N N 109.372 0.3 1 610 133 133 ARG H H 7.136 0.020 1 611 133 133 ARG C C 177.320 0.3 1 612 133 133 ARG CA C 57.119 0.3 1 613 133 133 ARG CB C 27.512 0.3 1 614 133 133 ARG N N 120.022 0.3 1 615 134 134 VAL H H 7.462 0.020 1 616 134 134 VAL C C 176.073 0.3 1 617 134 134 VAL CA C 64.517 0.3 1 618 134 134 VAL CB C 31.184 0.3 1 619 134 134 VAL N N 116.051 0.3 1 620 135 135 ILE H H 6.261 0.020 1 621 135 135 ILE C C 177.687 0.3 1 622 135 135 ILE CA C 62.551 0.3 1 623 135 135 ILE CB C 37.381 0.3 1 624 135 135 ILE N N 116.135 0.3 1 625 136 136 GLU H H 7.014 0.020 1 626 136 136 GLU C C 175.996 0.3 1 627 136 136 GLU CA C 57.043 0.3 1 628 136 136 GLU CB C 30.572 0.3 1 629 136 136 GLU N N 116.706 0.3 1 630 137 137 ASP H H 7.910 0.020 1 631 137 137 ASP C C 173.163 0.3 1 632 137 137 ASP CA C 51.535 0.3 1 633 137 137 ASP CB C 41.206 0.3 1 634 137 137 ASP N N 118.416 0.3 1 635 138 138 PRO C C 178.254 0.3 1 636 138 138 PRO CA C 64.999 0.3 1 637 138 138 PRO CB C 31.796 0.3 1 638 139 139 ASP H H 8.543 0.020 1 639 139 139 ASP C C 176.513 0.3 1 640 139 139 ASP CA C 53.983 0.3 1 641 139 139 ASP CB C 40.824 0.3 1 642 139 139 ASP N N 115.127 0.3 1 643 140 140 GLY H H 8.801 0.020 1 644 140 140 GLY C C 175.633 0.3 1 645 140 140 GLY CA C 47.939 0.3 1 646 140 140 GLY N N 109.969 0.3 1 647 141 141 ALA H H 9.896 0.020 1 648 141 141 ALA C C 180.157 0.3 1 649 141 141 ALA CA C 55.436 0.3 1 650 141 141 ALA CB C 18.102 0.3 1 651 141 141 ALA N N 126.901 0.3 1 652 142 142 ASN H H 10.349 0.020 1 653 142 142 ASN C C 174.704 0.3 1 654 142 142 ASN CA C 51.581 0.3 1 655 142 142 ASN CB C 39.523 0.3 1 656 142 142 ASN N N 114.391 0.3 1 657 143 143 PHE H H 6.669 0.020 1 658 143 143 PHE C C 172.992 0.3 1 659 143 143 PHE CA C 55.895 0.3 1 660 143 143 PHE CB C 39.523 0.3 1 661 143 143 PHE N N 122.830 0.3 1 662 144 144 PRO C C 171.702 0.3 1 663 144 144 PRO CA C 63.699 0.3 1 664 144 144 PRO CB C 30.190 0.3 1 665 145 145 TRP H H 8.439 0.020 1 666 145 145 TRP C C 171.940 0.3 1 667 145 145 TRP CA C 57.808 0.3 1 668 145 145 TRP CB C 24.834 0.3 1 669 145 145 TRP N N 118.078 0.3 1 670 146 146 PRO C C 177.186 0.3 1 671 146 146 PRO CA C 63.087 0.3 1 672 146 146 PRO CB C 31.720 0.3 1 673 147 147 ASN H H 8.191 0.020 1 674 147 147 ASN C C 179.203 0.3 1 675 147 147 ASN CA C 55.589 0.3 1 676 147 147 ASN CB C 39.982 0.3 1 677 147 147 ASN N N 123.592 0.3 1 stop_ save_