data_16518 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments for oxidised Trypanosoma cruzi glutathione peroxidase ; _BMRB_accession_number 16518 _BMRB_flat_file_name bmr16518.str _Entry_type original _Submission_date 2009-09-24 _Accession_date 2009-09-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Related to X-ray structure submitted to PDB by the same authors: accession code 3E0U' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Driscoll Paul C. . 2 Harris Richard . . 3 Patel Shreenal H. . 4 Djordjevic Snezana . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 323 "13C chemical shifts" 473 "15N chemical shifts" 149 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-01-20 update BMRB 'complete entry citation' 2009-11-20 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural insights into the catalytic mechanism of Trypanosoma cruzi GPXI (glutathione peroxidase-like enzyme I).' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19886864 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Patel Shreenal . . 2 Hussain Syeed . . 3 Harris Richard . . 4 Sardiwal Sunita . . 5 Kelly John M. . 6 Wilkinson Shane R. . 7 Driscoll Paul C. . 8 Djordjevic Snezana . . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_name_full 'The Biochemical journal' _Journal_volume 425 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 513 _Page_last 522 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Tc GPXI monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TcGPXI $TcGPXI 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_TcGPXI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TcGPXI _Molecular_mass . _Mol_thiol_state 'disulfide bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 168 _Mol_residue_sequence ; GAKSIYEFQVNAADGKPYDL SQHKGHPLLIYNVASRCGYT KGGYETATTLYNKYKGQGFT VLAFPCNQFAGQEPGTALEV KEFACTRFKADFPIMAKIDV NGSGAKAHPLYEFMKATIPG LFGTKAIKWNFTSFLIDRHG VPVERFSPGASVEDIEKKLL PLLGGARI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 12 GLY 2 13 ALA 3 14 LYS 4 15 SER 5 16 ILE 6 17 TYR 7 18 GLU 8 19 PHE 9 20 GLN 10 21 VAL 11 22 ASN 12 23 ALA 13 24 ALA 14 25 ASP 15 26 GLY 16 27 LYS 17 28 PRO 18 29 TYR 19 30 ASP 20 31 LEU 21 32 SER 22 33 GLN 23 34 HIS 24 35 LYS 25 36 GLY 26 37 HIS 27 38 PRO 28 39 LEU 29 40 LEU 30 41 ILE 31 42 TYR 32 43 ASN 33 44 VAL 34 45 ALA 35 46 SER 36 47 ARG 37 48 CYS 38 49 GLY 39 50 TYR 40 51 THR 41 52 LYS 42 53 GLY 43 54 GLY 44 55 TYR 45 56 GLU 46 57 THR 47 58 ALA 48 59 THR 49 60 THR 50 61 LEU 51 62 TYR 52 63 ASN 53 64 LYS 54 65 TYR 55 66 LYS 56 67 GLY 57 68 GLN 58 69 GLY 59 70 PHE 60 71 THR 61 72 VAL 62 73 LEU 63 74 ALA 64 75 PHE 65 76 PRO 66 77 CYS 67 78 ASN 68 79 GLN 69 80 PHE 70 81 ALA 71 82 GLY 72 83 GLN 73 84 GLU 74 85 PRO 75 86 GLY 76 87 THR 77 88 ALA 78 89 LEU 79 90 GLU 80 91 VAL 81 92 LYS 82 93 GLU 83 94 PHE 84 95 ALA 85 96 CYS 86 97 THR 87 98 ARG 88 99 PHE 89 100 LYS 90 101 ALA 91 102 ASP 92 103 PHE 93 104 PRO 94 105 ILE 95 106 MET 96 107 ALA 97 108 LYS 98 109 ILE 99 110 ASP 100 111 VAL 101 112 ASN 102 113 GLY 103 114 SER 104 115 GLY 105 116 ALA 106 117 LYS 107 118 ALA 108 119 HIS 109 120 PRO 110 121 LEU 111 122 TYR 112 123 GLU 113 124 PHE 114 125 MET 115 126 LYS 116 127 ALA 117 128 THR 118 129 ILE 119 130 PRO 120 131 GLY 121 132 LEU 122 133 PHE 123 134 GLY 124 135 THR 125 136 LYS 126 137 ALA 127 138 ILE 128 139 LYS 129 140 TRP 130 141 ASN 131 142 PHE 132 143 THR 133 144 SER 134 145 PHE 135 146 LEU 136 147 ILE 137 148 ASP 138 149 ARG 139 150 HIS 140 151 GLY 141 152 VAL 142 153 PRO 143 154 VAL 144 155 GLU 145 156 ARG 146 157 PHE 147 158 SER 148 159 PRO 149 160 GLY 150 161 ALA 151 162 SER 152 163 VAL 153 164 GLU 154 165 ASP 155 166 ILE 156 167 GLU 157 168 LYS 158 169 LYS 159 170 LEU 160 171 LEU 161 172 PRO 162 173 LEU 163 174 LEU 164 175 GLY 165 176 GLY 166 177 ALA 167 178 ARG 168 179 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-05 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 3E0U "Crystal Structure Of T. Cruzi Gpx1" 100.00 166 98.81 98.81 9.21e-117 EMBL CAC85914 "glutathione peroxidase [Trypanosoma cruzi]" 98.81 177 98.80 98.80 1.52e-115 GB EAN90957 "trypanothione/tryparedoxin dependent peroxidase 2, putative [Trypanosoma cruzi]" 98.81 177 96.99 97.59 2.56e-113 GB ESS69943 "trypanothione/tryparedoxin dependent peroxidase 2 [Trypanosoma cruzi Dm28c]" 98.81 177 96.99 97.59 1.30e-113 REF XP_812808 "trypanothione/tryparedoxin dependent peroxidase 2 [Trypanosoma cruzi strain CL Brener]" 98.81 177 96.99 97.59 2.56e-113 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TcGPXI 'Trypanosoma cruzi' 5693 Eukaryota . Trypanosoma cruzi 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 $TcGPXI 'recombinant technology' . Escherichia coli . 'Rosetta (DE3)PLysS' 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 $TcGPXI 0.8 mM '[U-99% 13C; U-99% 15N]' phosphate 50 mM 'natural abundance' 'sodium chloride' 300 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HA(CA)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HA(CA)NH' _Sample_label $sample_1 save_ save_3D_HA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.350 . M pH 6.5 . pH pressure 1.0 . 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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_ _Software_label $ANSIG stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCA' '3D HN(CO)CA' '3D HA(CA)NH' '3D HA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name TcGPXI _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 14 3 LYS H H 8.904 . 1 2 14 3 LYS HA H 4.53 . . 3 14 3 LYS C C 175 . . 4 14 3 LYS CA C 56 . 1 5 14 3 LYS CB C 34.7 . 1 6 14 3 LYS N N 118.294 . 1 7 15 4 SER H H 7.287 . 1 8 15 4 SER HA H 4.72 . . 9 15 4 SER C C 173.4 . . 10 15 4 SER CA C 57.3 . 1 11 15 4 SER CB C 67.4 . 1 12 15 4 SER N N 113.297 . 1 13 16 5 ILE H H 9.22 . 1 14 16 5 ILE HA H 3.98 . . 15 16 5 ILE C C 174.4 . . 16 16 5 ILE CA C 64.4 . 1 17 16 5 ILE CB C 38.9 . 1 18 16 5 ILE N N 113.064 . 1 19 17 6 TYR H H 7.339 . 1 20 17 6 TYR HA H 4.45 . . 21 17 6 TYR C C 175.2 . . 22 17 6 TYR CA C 59.5 . 1 23 17 6 TYR CB C 36.6 . 1 24 17 6 TYR N N 115.294 . 1 25 18 7 GLU H H 6.897 . 1 26 18 7 GLU HA H 4.12 . . 27 18 7 GLU C C 173.8 . . 28 18 7 GLU CA C 56.6 . 1 29 18 7 GLU CB C 29.8 . 1 30 18 7 GLU N N 116.977 . 1 31 19 8 PHE H H 7.324 . 1 32 19 8 PHE HA H 4.66 . . 33 19 8 PHE C C 172.7 . . 34 19 8 PHE CA C 58.3 . 1 35 19 8 PHE CB C 41.7 . 1 36 19 8 PHE N N 117.788 . 1 37 20 9 GLN H H 8.917 . 1 38 20 9 GLN HA H 4.87 . . 39 20 9 GLN C C 174.7 . . 40 20 9 GLN CA C 55.7 . 1 41 20 9 GLN CB C 30.9 . 1 42 20 9 GLN N N 120.461 . 1 43 21 10 VAL H H 9.097 . 1 44 21 10 VAL HA H 4.97 . . 45 21 10 VAL C C 173.3 . . 46 21 10 VAL CA C 59.4 . 1 47 21 10 VAL CB C 36.8 . 1 48 21 10 VAL N N 117.534 . 1 49 22 11 ASN H H 8.698 . 1 50 22 11 ASN HA H 5.42 . . 51 22 11 ASN C C 174.9 . . 52 22 11 ASN CA C 52 . 1 53 22 11 ASN CB C 40 . 1 54 22 11 ASN N N 119.838 . 1 55 23 12 ALA H H 9.134 . 1 56 23 12 ALA HA H 4.76 . . 57 23 12 ALA C C 176.8 . . 58 23 12 ALA CA C 51.8 . 1 59 23 12 ALA CB C 20.6 . 1 60 23 12 ALA N N 124.419 . 1 61 24 13 ALA H H 7.949 . 1 62 24 13 ALA HA H 3.63 . . 63 24 13 ALA C C 177.2 . . 64 24 13 ALA CA C 55.9 . 1 65 24 13 ALA CB C 18.8 . 1 66 24 13 ALA N N 121.021 . 1 67 25 14 ASP H H 7.885 . 1 68 25 14 ASP HA H 4.44 . . 69 25 14 ASP C C 176.1 . . 70 25 14 ASP CA C 53.8 . 1 71 25 14 ASP CB C 39.8 . 1 72 25 14 ASP N N 114.68 . 1 73 26 15 GLY H H 8.483 . 1 74 26 15 GLY HA2 H 3.66 . . 75 26 15 GLY HA3 H 4.296 . 2 76 26 15 GLY C C 172.8 . . 77 26 15 GLY CA C 45.3 . 1 78 26 15 GLY N N 108.535 . 1 79 27 16 LYS H H 7.857 . 1 80 27 16 LYS HA H 4.66 . . 81 27 16 LYS C C 173 . . 82 27 16 LYS CA C 54.4 . 1 83 27 16 LYS CB C 31.8 . 1 84 27 16 LYS N N 121.636 . 1 85 28 17 PRO HA H 4.84 . . 86 28 17 PRO C C 175.6 . . 87 28 17 PRO CA C 64.3 . 1 88 28 17 PRO CB C 32.5 . 1 89 29 18 TYR H H 9.379 . 1 90 29 18 TYR HA H 4.66 . . 91 29 18 TYR C C 174.6 . . 92 29 18 TYR CA C 57.1 . 1 93 29 18 TYR CB C 41.5 . 1 94 29 18 TYR N N 126.497 . 1 95 30 19 ASP H H 8.302 . 1 96 30 19 ASP HA H 4.78 . . 97 30 19 ASP C C 175.3 . . 98 30 19 ASP CA C 52.7 . 1 99 30 19 ASP CB C 39.1 . 1 100 30 19 ASP N N 127.314 . 1 101 31 20 LEU H H 8.421 . 1 102 31 20 LEU HA H 4.33 . . 103 31 20 LEU C C 176.8 . . 104 31 20 LEU CA C 58.1 . 1 105 31 20 LEU CB C 43.7 . 1 106 31 20 LEU N N 130.09 . 1 107 32 21 SER H H 8.33 . 1 108 32 21 SER HA H 3.86 . . 109 32 21 SER C C 174.7 . . 110 32 21 SER CA C 61.8 . 1 111 32 21 SER CB C 62.9 . 1 112 32 21 SER N N 110.802 . 1 113 33 22 GLN H H 7.141 . 1 114 33 22 GLN HA H 4.18 . . 115 33 22 GLN C C 174.9 . . 116 33 22 GLN CA C 57.7 . 1 117 33 22 GLN CB C 29.1 . 1 118 33 22 GLN N N 122.072 . 1 119 34 23 HIS H H 7.742 . 1 120 34 23 HIS HA H 4.72 . . 121 34 23 HIS C C 172.8 . . 122 34 23 HIS CA C 56 . 1 123 34 23 HIS CB C 29.4 . 1 124 34 23 HIS N N 118.82 . 1 125 35 24 LYS H H 7.019 . 1 126 35 24 LYS HA H 3.87 . . 127 35 24 LYS C C 176.3 . . 128 35 24 LYS CA C 58.8 . 1 129 35 24 LYS CB C 32.4 . 1 130 35 24 LYS N N 119.932 . 1 131 36 25 GLY H H 7.946 . 1 132 36 25 GLY HA2 H 3.54 . . 133 36 25 GLY C C 172.4 . . 134 36 25 GLY CA C 44.9 . 1 135 36 25 GLY N N 113.127 . 1 136 37 26 HIS H H 8.292 . 1 137 37 26 HIS HA H 5.18 . . 138 37 26 HIS C C 170.1 . . 139 37 26 HIS CA C 53.1 . 1 140 37 26 HIS CB C 31.3 . 1 141 37 26 HIS N N 119.133 . 1 142 38 27 PRO HA H 4.99 . . 143 38 27 PRO C C 173.6 . . 144 38 27 PRO CA C 62.7 . 1 145 38 27 PRO CB C 33.6 . 1 146 39 28 LEU H H 8.386 . 1 147 39 28 LEU HA H 4.95 . . 148 39 28 LEU C C 173.4 . . 149 39 28 LEU CA C 55.6 . 1 150 39 28 LEU CB C 45.5 . 1 151 39 28 LEU N N 113.753 . 1 152 40 29 LEU H H 7.656 . 1 153 40 29 LEU HA H 5.53 . . 154 40 29 LEU C C 174 . . 155 40 29 LEU CA C 53.6 . 1 156 40 29 LEU CB C 48.5 . 1 157 40 29 LEU N N 121.451 . 1 158 41 30 ILE H H 8.897 . 1 159 41 30 ILE HA H 4.97 . . 160 41 30 ILE C C 175.3 . . 161 41 30 ILE CA C 61.5 . 1 162 41 30 ILE CB C 40.6 . 1 163 41 30 ILE N N 122.179 . 1 164 42 31 TYR H H 9.162 . 1 165 42 31 TYR HA H 5.44 . . 166 42 31 TYR C C 174.3 . . 167 42 31 TYR CA C 57.7 . 1 168 42 31 TYR CB C 43.5 . 1 169 42 31 TYR N N 126.72 . 1 170 43 32 ASN H H 8.003 . 1 171 43 32 ASN HA H 5.91 . . 172 43 32 ASN C C 173.9 . . 173 43 32 ASN CA C 52.1 . 1 174 43 32 ASN CB C 39 . 1 175 43 32 ASN N N 116.472 . 1 176 44 33 VAL H H 8.539 . 1 177 44 33 VAL HA H 4.08 . . 178 44 33 VAL C C 173.7 . . 179 44 33 VAL CA C 58.4 . 1 180 44 33 VAL CB C 35 . 1 181 44 33 VAL N N 115.892 . 1 182 45 34 ALA H H 7.363 . 1 183 45 34 ALA HA H 4.62 . . 184 45 34 ALA C C 176.3 . . 185 45 34 ALA CA C 52.4 . 1 186 45 34 ALA CB C 20.3 . 1 187 45 34 ALA N N 124.209 . 1 188 46 35 SER H H 8.268 . 1 189 46 35 SER HA H 4.39 . . 190 46 35 SER CA C 59.4 . 1 191 46 35 SER CB C 63.7 . 1 192 46 35 SER N N 115.306 . 1 193 47 36 ARG H H 8.075 . 1 194 47 36 ARG HA H 4.6 . . 195 47 36 ARG C C 174.8 . . 196 47 36 ARG CA C 56 . 1 197 47 36 ARG CB C 32.1 . 1 198 47 36 ARG N N 121.76 . 1 199 48 37 CYS HA H 4.62 . . 200 48 37 CYS C C 173.7 . . 201 48 37 CYS CA C 56.4 . 1 202 48 37 CYS CB C 42 . 1 203 49 38 GLY H H 8.405 . 1 204 49 38 GLY HA2 H 3.95 . . 205 49 38 GLY C C 172.6 . . 206 49 38 GLY CA C 45.8 . 1 207 49 38 GLY N N 109.639 . 1 208 50 39 TYR H H 8.086 . 1 209 50 39 TYR HA H 4.58 . . 210 50 39 TYR C C 174.6 . . 211 50 39 TYR CA C 58.4 . 1 212 50 39 TYR CB C 39.3 . 1 213 50 39 TYR N N 120.128 . 1 214 51 40 THR H H 7.819 . 1 215 51 40 THR HA H 4.24 . . 216 51 40 THR C C 173 . . 217 51 40 THR CA C 61.6 . 1 218 51 40 THR CB C 70 . 1 219 51 40 THR N N 115.46 . 1 220 52 41 LYS H H 7.919 . 1 221 52 41 LYS HA H 4.26 . . 222 52 41 LYS C C 176.1 . . 223 52 41 LYS CA C 56.9 . 1 224 52 41 LYS CB C 33.1 . 1 225 52 41 LYS N N 122.787 . 1 226 53 42 GLY H H 8.635 . 1 227 53 42 GLY HA2 H 3.76 . . 228 53 42 GLY HA3 H 3.99 . 2 229 53 42 GLY C C 174.3 . . 230 53 42 GLY CA C 46.3 . 1 231 53 42 GLY N N 110.604 . 1 232 54 43 GLY H H 8.1 . 1 233 54 43 GLY HA2 H 3.12 . . 234 54 43 GLY HA3 H 3.7 . 2 235 54 43 GLY C C 173 . . 236 54 43 GLY CA C 46.7 . 1 237 54 43 GLY N N 110.767 . 1 238 55 44 TYR H H 7.632 . 1 239 55 44 TYR HA H 3.93 . . 240 55 44 TYR C C 176.9 . . 241 55 44 TYR CA C 61.4 . 1 242 55 44 TYR CB C 42.8 . 1 243 55 44 TYR N N 119.06 . 1 244 56 45 GLU H H 8.151 . 1 245 56 45 GLU HA H 3.98 . . 246 56 45 GLU C C 177.9 . . 247 56 45 GLU CA C 60.2 . 1 248 56 45 GLU CB C 29.4 . 1 249 56 45 GLU N N 122.01 . 1 250 57 46 THR H H 8.173 . 1 251 57 46 THR HA H 3.66 . . 252 57 46 THR C C 174 . . 253 57 46 THR CA C 66.7 . 1 254 57 46 THR CB C 68.8 . 1 255 57 46 THR N N 120.002 . 1 256 58 47 ALA H H 7.986 . 1 257 58 47 ALA HA H 3.82 . . 258 58 47 ALA C C 178.2 . . 259 58 47 ALA CA C 55.9 . 1 260 58 47 ALA CB C 19.3 . 1 261 58 47 ALA N N 122.892 . 1 262 59 48 THR H H 8.134 . 1 263 59 48 THR HA H 3.98 . . 264 59 48 THR C C 175.5 . . 265 59 48 THR CA C 67.7 . 1 266 59 48 THR CB C 69.3 . 1 267 59 48 THR N N 112.625 . 1 268 60 49 THR H H 8.508 . 1 269 60 49 THR HA H 3.98 . . 270 60 49 THR C C 176 . . 271 60 49 THR CA C 67.3 . 1 272 60 49 THR CB C 68.6 . 1 273 60 49 THR N N 120.03 . 1 274 61 50 LEU H H 8.296 . 1 275 61 50 LEU HA H 3.92 . . 276 61 50 LEU C C 177.1 . . 277 61 50 LEU CA C 58.6 . 1 278 61 50 LEU CB C 42.8 . 1 279 61 50 LEU N N 120.67 . 1 280 62 51 TYR H H 8.7 . 1 281 62 51 TYR HA H 4.29 . . 282 62 51 TYR C C 175.4 . . 283 62 51 TYR CA C 62.6 . 1 284 62 51 TYR CB C 39 . 1 285 62 51 TYR N N 118.329 . 1 286 63 52 ASN H H 8.418 . 1 287 63 52 ASN HA H 4.16 . . 288 63 52 ASN C C 176.6 . . 289 63 52 ASN CA C 56.6 . 1 290 63 52 ASN CB C 38.8 . 1 291 63 52 ASN N N 114.339 . 1 292 64 53 LYS H H 8.017 . 1 293 64 53 LYS HA H 3.83 . . 294 64 53 LYS C C 177.8 . . 295 64 53 LYS CA C 59.8 . 1 296 64 53 LYS CB C 34.3 . 1 297 64 53 LYS N N 119.123 . 1 298 65 54 TYR H H 7.54 . . 299 65 54 TYR HA H 4.92 . . 300 65 54 TYR C C 176.7 . . 301 65 54 TYR CA C 59.0 . . 302 65 54 TYR CB C 39.3 . . 303 65 54 TYR N N 111.763 . . 304 66 55 LYS H H 8.574 . 1 305 66 55 LYS HA H 4.88 . . 306 66 55 LYS C C 179 . . 307 66 55 LYS CA C 59.3 . 1 308 66 55 LYS CB C 30.1 . 1 309 66 55 LYS N N 123.834 . 1 310 67 56 GLY H H 8.897 . 1 311 67 56 GLY HA2 H 3.85 . . 312 67 56 GLY HA3 H 4.03 . 2 313 67 56 GLY C C 174.2 . . 314 67 56 GLY CA C 46.3 . 1 315 67 56 GLY N N 110.469 . 1 316 68 57 GLN H H 7.907 . 1 317 68 57 GLN HA H 4.64 . . 318 68 57 GLN C C 174.8 . . 319 68 57 GLN CA C 55.6 . 1 320 68 57 GLN CB C 30.7 . 1 321 68 57 GLN N N 117.648 . 1 322 69 58 GLY H H 7.859 . 1 323 69 58 GLY HA2 H 3.45 . . 324 69 58 GLY HA3 H 3.6 . 2 325 69 58 GLY C C 171.7 . . 326 69 58 GLY CA C 45.1 . 1 327 69 58 GLY N N 107.382 . 1 328 70 59 PHE H H 6.81 . 1 329 70 59 PHE HA H 4.98 . . 330 70 59 PHE C C 173.2 . . 331 70 59 PHE CA C 57.4 . 1 332 70 59 PHE CB C 41.9 . 1 333 70 59 PHE N N 118.774 . 1 334 71 60 THR H H 6.232 . 1 335 71 60 THR HA H 4.45 . . 336 71 60 THR C C 169.2 . . 337 71 60 THR CA C 60.9 . 1 338 71 60 THR CB C 70.6 . 1 339 71 60 THR N N 118.86 . 1 340 72 61 VAL H H 6.826 . 1 341 72 61 VAL HA H 4.66 . . 342 72 61 VAL C C 172.1 . . 343 72 61 VAL CA C 59.9 . 1 344 72 61 VAL CB C 35.3 . 1 345 72 61 VAL N N 121.862 . 1 346 73 62 LEU H H 8.167 . 1 347 73 62 LEU HA H 4.87 . . 348 73 62 LEU C C 174.8 . . 349 73 62 LEU CA C 52.9 . 1 350 73 62 LEU CB C 45.5 . 1 351 73 62 LEU N N 120.203 . 1 352 74 63 ALA H H 7.904 . 1 353 74 63 ALA HA H 5.35 . . 354 74 63 ALA C C 173.9 . . 355 74 63 ALA CA C 49.7 . 1 356 74 63 ALA CB C 22.7 . 1 357 74 63 ALA N N 122.185 . 1 358 75 64 PHE H H 9.434 . 1 359 75 64 PHE HA H 4.6 . . 360 75 64 PHE C C 172.4 . . 361 75 64 PHE CA C 55.1 . 1 362 75 64 PHE CB C 39.9 . 1 363 75 64 PHE N N 122.783 . 1 364 76 65 PRO HA H 4.58 . . 365 76 65 PRO C C 174.3 . . 366 76 65 PRO CA C 62 . 1 367 76 65 PRO CB C 32.3 . 1 368 77 66 CYS H H 8.442 . 1 369 77 66 CYS HA H 4.63 . . 370 77 66 CYS C C 174.1 . . 371 77 66 CYS CA C 58.1 . 1 372 77 66 CYS CB C 29.9 . 1 373 77 66 CYS N N 119.213 . 1 374 78 67 ASN HA H 5.19 . . 375 78 67 ASN C C 175.9 . . 376 78 67 ASN CA C 53.1 . 1 377 78 67 ASN CB C 39.6 . 1 378 79 68 GLN H H 7.696 . 1 379 79 68 GLN HA H 3.86 . . 380 79 68 GLN C C 173.8 . . 381 79 68 GLN CA C 59 . 1 382 79 68 GLN CB C 29.9 . 1 383 79 68 GLN N N 116.784 . 1 384 80 69 PHE H H 8.147 . 1 385 80 69 PHE HA H 4.74 . . 386 80 69 PHE C C 174.5 . . 387 80 69 PHE CA C 56.5 . 1 388 80 69 PHE CB C 38 . 1 389 80 69 PHE N N 118.396 . 1 390 81 70 ALA H H 7.669 . 1 391 81 70 ALA HA H 4.37 . . 392 81 70 ALA C C 177.5 . . 393 81 70 ALA CA C 53.4 . 1 394 81 70 ALA CB C 19.7 . 1 395 81 70 ALA N N 124.451 . 1 396 82 71 GLY H H 8.558 . 1 397 82 71 GLY HA2 H 4.01 . . 398 82 71 GLY HA3 H 4.02 . 2 399 82 71 GLY C C 173.1 . . 400 82 71 GLY CA C 45.5 . 1 401 82 71 GLY N N 108.308 . 1 402 83 72 GLN H H 8.139 . 1 403 83 72 GLN HA H 4.41 . . 404 83 72 GLN C C 174.9 . . 405 83 72 GLN CA C 55.9 . 1 406 83 72 GLN CB C 30 . 1 407 83 72 GLN N N 119.316 . 1 408 84 73 GLU H H 8.42 . 1 409 84 73 GLU HA H 4.55 . . 410 84 73 GLU C C 173.7 . . 411 84 73 GLU CA C 54.7 . 1 412 84 73 GLU CB C 29.9 . 1 413 84 73 GLU N N 123.275 . 1 414 85 74 PRO HA H 4.39 . . 415 85 74 PRO C C 176.6 . . 416 85 74 PRO CA C 63.9 . 1 417 85 74 PRO CB C 32.3 . 1 418 86 75 GLY H H 8.545 . 1 419 86 75 GLY HA2 H 3.94 . . 420 86 75 GLY HA3 H 4.02 . 2 421 86 75 GLY C C 173.6 . . 422 86 75 GLY CA C 45.7 . 1 423 86 75 GLY N N 109.314 . 1 424 87 76 THR H H 7.852 . 1 425 87 76 THR HA H 4.35 . . 426 87 76 THR C C 173.5 . . 427 87 76 THR CA C 62 . 1 428 87 76 THR CB C 70.4 . 1 429 87 76 THR N N 112.813 . 1 430 88 77 ALA H H 8.315 . 1 431 88 77 ALA HA H 4.32 . . 432 88 77 ALA C C 176.7 . . 433 88 77 ALA CA C 52.9 . 1 434 88 77 ALA CB C 19.3 . 1 435 88 77 ALA N N 125.724 . 1 436 89 78 LEU H H 8.062 . 1 437 89 78 LEU HA H 4.28 . . 438 89 78 LEU C C 176.5 . . 439 89 78 LEU CA C 55.7 . 1 440 89 78 LEU CB C 42.6 . 1 441 89 78 LEU N N 120.516 . 1 442 90 79 GLU H H 8.247 . 1 443 90 79 GLU HA H 4.26 . . 444 90 79 GLU C C 175.5 . . 445 90 79 GLU CA C 57 . 1 446 90 79 GLU CB C 30.4 . 1 447 90 79 GLU N N 120.939 . 1 448 91 80 VAL H H 8.004 . 1 449 91 80 VAL HA H 4.06 . . 450 91 80 VAL C C 175.3 . . 451 91 80 VAL CA C 62.7 . 1 452 91 80 VAL CB C 32.8 . 1 453 91 80 VAL N N 120.771 . 1 454 92 81 LYS H H 8.227 . 1 455 92 81 LYS HA H 4.27 . . 456 92 81 LYS C C 175.6 . . 457 92 81 LYS CA C 56.8 . 1 458 92 81 LYS CB C 33.1 . 1 459 92 81 LYS N N 124.161 . 1 460 93 82 GLU H H 8.24 . 1 461 93 82 GLU HA H 4.2 . . 462 93 82 GLU C C 175.2 . . 463 93 82 GLU CA C 57.1 . 1 464 93 82 GLU CB C 30.4 . 1 465 93 82 GLU N N 120.702 . 1 466 94 83 PHE H H 8.026 . 1 467 94 83 PHE HA H 4.6 . . 468 94 83 PHE C C 174.4 . . 469 94 83 PHE CA C 57.7 . 1 470 94 83 PHE CB C 39.8 . 1 471 94 83 PHE N N 120.052 . 1 472 95 84 ALA H H 8.152 . 1 473 95 84 ALA HA H 4.31 . . 474 95 84 ALA C C 176.2 . . 475 95 84 ALA CA C 52.6 . 1 476 95 84 ALA CB C 19.4 . 1 477 95 84 ALA N N 124.535 . 1 478 96 85 CYS H H 8.295 . 1 479 96 85 CYS HA H 4.7 . . 480 96 85 CYS C C 170.1 . . 481 96 85 CYS CA C 56.3 . 1 482 96 85 CYS CB C 43.3 . 1 483 96 85 CYS N N 118.91 . 1 484 97 86 THR HA H 4.4 . . 485 97 86 THR C C 173.3 . . 486 97 86 THR CA C 62.4 . 1 487 97 86 THR CB C 70.2 . 1 488 98 87 ARG H H 8.181 . 1 489 98 87 ARG HA H 4.33 . . 490 98 87 ARG C C 174.8 . . 491 98 87 ARG CA C 56.3 . 1 492 98 87 ARG CB C 31.1 . 1 493 98 87 ARG N N 123.118 . 1 494 99 88 PHE H H 8.307 . 1 495 99 88 PHE HA H 4.22 . . 496 99 88 PHE C C 173.2 . . 497 99 88 PHE CA C 59.1 . 1 498 99 88 PHE CB C 39.8 . 1 499 99 88 PHE N N 123.603 . 1 500 100 89 LYS H H 7.524 . 1 501 100 89 LYS HA H 4.2 . . 502 100 89 LYS C C 172.9 . . 503 100 89 LYS CA C 55.2 . 1 504 100 89 LYS CB C 34.4 . 1 505 100 89 LYS N N 126.631 . 1 506 101 90 ALA H H 7.768 . 1 507 101 90 ALA HA H 4.07 . . 508 101 90 ALA C C 175.2 . . 509 101 90 ALA CA C 51.4 . 1 510 101 90 ALA CB C 21.3 . 1 511 101 90 ALA N N 124.323 . 1 512 102 91 ASP H H 8.458 . 1 513 102 91 ASP HA H 4.49 . . 514 102 91 ASP C C 174.1 . . 515 102 91 ASP CA C 55.1 . 1 516 102 91 ASP CB C 42 . 1 517 102 91 ASP N N 117.004 . 1 518 103 92 PHE H H 5.823 . 1 519 103 92 PHE HA H 4.48 . . 520 103 92 PHE C C 171.6 . . 521 103 92 PHE CA C 52.5 . 1 522 103 92 PHE CB C 36.7 . 1 523 103 92 PHE N N 115.653 . 1 524 104 93 PRO HA H 4.1 . . 525 104 93 PRO C C 173.8 . . 526 104 93 PRO CA C 65 . 1 527 104 93 PRO CB C 33.2 . 1 528 105 94 ILE H H 7.506 . 1 529 105 94 ILE HA H 4.62 . . 530 105 94 ILE C C 175.4 . . 531 105 94 ILE CA C 59.5 . 1 532 105 94 ILE CB C 39.2 . 1 533 105 94 ILE N N 121.314 . 1 534 106 95 MET H H 8.385 . 1 535 106 95 MET HA H 4.62 . . 536 106 95 MET C C 174.3 . . 537 106 95 MET CA C 53 . 1 538 106 95 MET CB C 35.7 . 1 539 106 95 MET N N 125.613 . 1 540 107 96 ALA H H 7.551 . 1 541 107 96 ALA HA H 4.1 . . 542 107 96 ALA C C 175.8 . . 543 107 96 ALA CA C 52.8 . 1 544 107 96 ALA CB C 19 . 1 545 107 96 ALA N N 119.059 . 1 546 108 97 LYS H H 7.945 . 1 547 108 97 LYS HA H 4.53 . . 548 108 97 LYS C C 175.8 . . 549 108 97 LYS CA C 56.9 . 1 550 108 97 LYS CB C 32.8 . 1 551 108 97 LYS N N 119.452 . 1 552 109 98 ILE H H 8.405 . 1 553 109 98 ILE HA H 4.81 . . 554 109 98 ILE C C 175 . . 555 109 98 ILE CA C 60 . 1 556 109 98 ILE CB C 44 . 1 557 109 98 ILE N N 118.931 . 1 558 110 99 ASP H H 8.555 . 1 559 110 99 ASP HA H 4.85 . . 560 110 99 ASP C C 174.7 . . 561 110 99 ASP CA C 54.4 . 1 562 110 99 ASP CB C 41.1 . 1 563 110 99 ASP N N 119.796 . 1 564 111 100 VAL H H 7.919 . 1 565 111 100 VAL HA H 4.13 . . 566 111 100 VAL C C 173 . . 567 111 100 VAL CA C 60.7 . 1 568 111 100 VAL CB C 33.1 . 1 569 111 100 VAL N N 112.032 . 1 570 112 101 ASN H H 8.1 . 1 571 112 101 ASN HA H 4.82 . . 572 112 101 ASN C C 175.3 . . 573 112 101 ASN CA C 51.3 . 1 574 112 101 ASN CB C 43.4 . 1 575 112 101 ASN N N 117.852 . 1 576 113 103 SER HA H 4.1 . . 577 113 103 SER C C 174.5 . . 578 113 103 SER CA C 61.6 . 1 579 113 103 SER CB C 63.5 . 1 580 114 106 LYS H H 8.572 . 1 581 114 106 LYS HA H 4.54 . . 582 114 106 LYS C C 174.7 . . 583 114 106 LYS CA C 54.5 . 1 584 114 106 LYS CB C 31.5 . 1 585 114 106 LYS N N 120.293 . 1 586 115 107 ALA H H 7.127 . 1 587 115 107 ALA HA H 3.51 . . 588 115 107 ALA C C 176.3 . . 589 115 107 ALA CA C 52 . 1 590 115 107 ALA CB C 18.8 . 1 591 115 107 ALA N N 122.526 . 1 592 116 108 HIS H H 8.169 . 1 593 116 108 HIS HA H 4.44 . . 594 116 108 HIS C C 174.9 . . 595 116 108 HIS CA C 57 . 1 596 116 108 HIS CB C 33 . 1 597 116 108 HIS N N 124.463 . 1 598 117 109 PRO HA H 4.09 . . 599 117 109 PRO C C 177.2 . . 600 117 109 PRO CA C 65.7 . 1 601 117 109 PRO CB C 32.6 . 1 602 118 110 LEU H H 11.465 . 1 603 118 110 LEU HA H 2.7 . . 604 118 110 LEU C C 178.6 . . 605 118 110 LEU CA C 58.5 . 1 606 118 110 LEU CB C 42.3 . 1 607 118 110 LEU N N 124.24 . 1 608 119 111 TYR H H 7.41 . 1 609 119 111 TYR HA H 3.38 . . 610 119 111 TYR C C 177.1 . . 611 119 111 TYR CA C 64 . 1 612 119 111 TYR CB C 38.9 . 1 613 119 111 TYR N N 117.859 . 1 614 120 112 GLU H H 7.623 . 1 615 120 112 GLU HA H 4.25 . . 616 120 112 GLU C C 178.1 . . 617 120 112 GLU CA C 59.3 . 1 618 120 112 GLU CB C 29.1 . 1 619 120 112 GLU N N 118.005 . 1 620 121 113 PHE H H 7.47 . 1 621 121 113 PHE HA H 4.4 . . 622 121 113 PHE C C 177 . . 623 121 113 PHE CA C 60 . 1 624 121 113 PHE CB C 39.6 . 1 625 121 113 PHE N N 119.222 . 1 626 122 114 MET H H 7.803 . 1 627 122 114 MET HA H 2.78 . . 628 122 114 MET C C 175.6 . . 629 122 114 MET CA C 61.7 . 1 630 122 114 MET CB C 31.4 . 1 631 122 114 MET N N 122.023 . 1 632 123 115 LYS H H 8.345 . 1 633 123 115 LYS HA H 3.67 . . 634 123 115 LYS C C 175.7 . . 635 123 115 LYS CA C 59.2 . 1 636 123 115 LYS CB C 33.2 . 1 637 123 115 LYS N N 115.148 . 1 638 124 116 ALA H H 7.015 . 1 639 124 116 ALA HA H 3.88 . . 640 124 116 ALA C C 178.4 . . 641 124 116 ALA CA C 53.4 . 1 642 124 116 ALA CB C 18.8 . 1 643 124 116 ALA N N 113.864 . 1 644 125 117 THR H H 7.253 . 1 645 125 117 THR HA H 3.73 . . 646 125 117 THR C C 173.1 . . 647 125 117 THR CA C 66.7 . 1 648 125 117 THR CB C 68.5 . 1 649 125 117 THR N N 114.402 . 1 650 126 118 ILE H H 7.497 . 1 651 126 118 ILE HA H 4.5 . . 652 126 118 ILE C C 171.3 . . 653 126 118 ILE CA C 56.7 . 1 654 126 118 ILE CB C 37.4 . 1 655 126 118 ILE N N 118.115 . 1 656 127 119 PRO HA H 4.5 . . 657 127 119 PRO C C 175.2 . . 658 127 119 PRO CA C 63.2 . 1 659 127 119 PRO CB C 32.6 . 1 660 128 120 GLY H H 8.014 . 1 661 128 120 GLY HA2 H 3.85 . . 662 128 120 GLY HA3 H 4.01 . 2 663 128 120 GLY C C 172.8 . . 664 128 120 GLY CA C 44.2 . 1 665 128 120 GLY N N 105.966 . 1 666 129 121 LEU H H 8.131 . 1 667 129 121 LEU HA H 3.95 . . 668 129 121 LEU C C 177.6 . . 669 129 121 LEU CA C 56.6 . 1 670 129 121 LEU CB C 42.3 . 1 671 129 121 LEU N N 121.226 . 1 672 130 122 PHE H H 8.776 . 1 673 130 122 PHE HA H 4.49 . . 674 130 122 PHE C C 175.3 . . 675 130 122 PHE CA C 58.1 . 1 676 130 122 PHE CB C 37.4 . 1 677 130 122 PHE N N 117.998 . 1 678 131 123 GLY H H 8.226 . 1 679 131 123 GLY HA2 H 3.6 . . 680 131 123 GLY HA3 H 4.21 . 2 681 131 123 GLY C C 173.7 . . 682 131 123 GLY CA C 46 . 1 683 131 123 GLY N N 106.751 . 1 684 132 124 THR H H 7.393 . 1 685 132 124 THR HA H 4.35 . . 686 132 124 THR C C 174.1 . . 687 132 124 THR CA C 61.8 . 1 688 132 124 THR CB C 70 . 1 689 132 124 THR N N 114.558 . 1 690 133 125 LYS HA H 3.98 . . 691 133 125 LYS C C 176.8 . . 692 133 125 LYS CA C 59.6 . 1 693 133 125 LYS CB C 33.7 . 1 694 134 126 ALA H H 7.824 . 1 695 134 126 ALA HA H 4.02 . . 696 134 126 ALA C C 176.9 . . 697 134 126 ALA CA C 53.7 . 1 698 134 126 ALA CB C 19.3 . 1 699 134 126 ALA N N 120.279 . 1 700 135 127 ILE H H 8.548 . 1 701 135 127 ILE C C 176.9 . . 702 135 127 ILE CA C 59.9 . 1 703 135 127 ILE CB C 36.6 . 1 704 135 127 ILE N N 122.412 . 1 705 136 128 LYS H H 9.16 . 1 706 136 128 LYS HA H 3.97 . . 707 136 128 LYS C C 173.8 . . 708 136 128 LYS CA C 56.8 . 1 709 136 128 LYS CB C 33.4 . 1 710 136 128 LYS N N 127.141 . 1 711 137 129 TRP H H 6.163 . 1 712 137 129 TRP HA H 4.55 . . 713 137 129 TRP HE1 H 10.26 . 1 714 137 129 TRP C C 176.4 . . 715 137 129 TRP CA C 55.4 . 1 716 137 129 TRP CB C 34.1 . 1 717 137 129 TRP N N 112.468 . 1 718 137 129 TRP NE1 N 130.57 . 1 719 138 130 ASN H H 8.68 . 1 720 138 130 ASN HA H 4.14 . . 721 138 130 ASN C C 177.7 . . 722 138 130 ASN CA C 54.4 . 1 723 138 130 ASN CB C 39.8 . 1 724 138 130 ASN N N 120.899 . 1 725 139 131 PHE H H 8.574 . 1 726 139 131 PHE HA H 4.2 . . 727 139 131 PHE C C 175.4 . . 728 139 131 PHE CA C 62.2 . 1 729 139 131 PHE CB C 35.8 . 1 730 139 131 PHE N N 114.257 . 1 731 140 132 THR H H 7.204 . 1 732 140 132 THR HA H 4.37 . . 733 140 132 THR C C 172 . . 734 140 132 THR CA C 65.7 . 1 735 140 132 THR CB C 69.6 . 1 736 140 132 THR N N 116.523 . 1 737 141 133 SER H H 8.535 . 1 738 141 133 SER HA H 5.53 . . 739 141 133 SER C C 172.3 . . 740 141 133 SER CA C 56.7 . 1 741 141 133 SER CB C 66.2 . 1 742 141 133 SER N N 119.145 . 1 743 142 134 PHE H H 8.473 . 1 744 142 134 PHE HA H 5.37 . . 745 142 134 PHE C C 174.1 . . 746 142 134 PHE CA C 56.3 . 1 747 142 134 PHE CB C 44 . 1 748 142 134 PHE N N 115.492 . 1 749 143 135 LEU H H 8.653 . 1 750 143 135 LEU HA H 5.05 . . 751 143 135 LEU C C 172.5 . . 752 143 135 LEU CA C 54 . 1 753 143 135 LEU CB C 44.9 . 1 754 143 135 LEU N N 124.725 . 1 755 144 136 ILE H H 9.603 . 1 756 144 136 ILE HA H 4.57 . . 757 144 136 ILE C C 174.4 . . 758 144 136 ILE CA C 57.9 . 1 759 144 136 ILE CB C 37.6 . 1 760 144 136 ILE N N 130.29 . 1 761 145 137 ASP H H 8.491 . 1 762 145 137 ASP HA H 4.6 . . 763 145 137 ASP C C 177.6 . . 764 145 137 ASP CA C 53.1 . 1 765 145 137 ASP CB C 41.7 . 1 766 145 137 ASP N N 123.954 . 1 767 146 138 ARG H H 8.572 . 1 768 146 138 ARG HA H 3.75 . . 769 146 138 ARG C C 174.7 . . 770 146 138 ARG CA C 58.8 . 1 771 146 138 ARG CB C 30 . 1 772 146 138 ARG N N 113.845 . 1 773 147 139 HIS H H 8.539 . 1 774 147 139 HIS HA H 4.82 . . 775 147 139 HIS C C 175.1 . . 776 147 139 HIS CA C 55.5 . 1 777 147 139 HIS CB C 30.6 . 1 778 147 139 HIS N N 118.736 . 1 779 148 140 GLY H H 8.234 . 1 780 148 140 GLY HA2 H 3.42 . . 781 148 140 GLY HA3 H 4.34 . 2 782 148 140 GLY C C 172.2 . . 783 148 140 GLY CA C 47.2 . 1 784 148 140 GLY N N 107.003 . 1 785 149 141 VAL H H 8.851 . 1 786 149 141 VAL HA H 4.53 . . 787 149 141 VAL C C 173.5 . . 788 149 141 VAL CA C 60.6 . 1 789 149 141 VAL CB C 33.3 . 1 790 149 141 VAL N N 126.014 . 1 791 150 142 PRO HA H 4.94 . . 792 150 142 PRO C C 174.8 . . 793 150 142 PRO CA C 62.7 . 1 794 150 142 PRO CB C 31.5 . 1 795 151 143 VAL H H 9.331 . 1 796 151 143 VAL HA H 4.53 . . 797 151 143 VAL C C 174.9 . . 798 151 143 VAL CA C 61.6 . 1 799 151 143 VAL CB C 34.5 . 1 800 151 143 VAL N N 115.257 . 1 801 152 144 GLU H H 7.4 . 1 802 152 144 GLU HA H 4.54 . . 803 152 144 GLU C C 171.9 . . 804 152 144 GLU CA C 55.3 . 1 805 152 144 GLU CB C 34 . 1 806 152 144 GLU N N 117.626 . 1 807 153 145 ARG H H 8.841 . 1 808 153 145 ARG HA H 4.7 . . 809 153 145 ARG C C 173.5 . . 810 153 145 ARG CA C 54.2 . 1 811 153 145 ARG CB C 34 . 1 812 153 145 ARG N N 126.558 . 1 813 154 146 PHE H H 9.583 . 1 814 154 146 PHE HA H 4.85 . . 815 154 146 PHE C C 174.7 . . 816 154 146 PHE CA C 57.2 . 1 817 154 146 PHE CB C 40.1 . 1 818 154 146 PHE N N 126.662 . 1 819 155 147 SER H H 8.8 . 1 820 155 147 SER HA H 4.75 . . 821 155 147 SER C C 173.2 . . 822 155 147 SER CA C 57.1 . 1 823 155 147 SER CB C 63.2 . 1 824 155 147 SER N N 118.597 . 1 825 156 148 PRO HA H 4.58 . . 826 156 148 PRO C C 175.2 . . 827 156 148 PRO CA C 64.7 . 1 828 156 148 PRO CB C 32 . 1 829 157 149 GLY H H 8.004 . 1 830 157 149 GLY HA2 H 3.58 . . 831 157 149 GLY HA3 H 4.03 . 2 832 157 149 GLY C C 173.2 . . 833 157 149 GLY CA C 44.8 . 1 834 157 149 GLY N N 106.482 . 1 835 158 150 ALA H H 7.294 . 1 836 158 150 ALA HA H 4.34 . . 837 158 150 ALA C C 176.1 . . 838 158 150 ALA CA C 53 . 1 839 158 150 ALA CB C 19.1 . 1 840 158 150 ALA N N 124.182 . 1 841 159 151 SER H H 9.08 . 1 842 159 151 SER HA H 4.53 . . 843 159 151 SER C C 173.7 . . 844 159 151 SER CA C 56.6 . 1 845 159 151 SER CB C 66.6 . 1 846 159 151 SER N N 120.128 . 1 847 160 152 VAL H H 8.518 . 1 848 160 152 VAL HA H 3.29 . . 849 160 152 VAL C C 176.4 . . 850 160 152 VAL CA C 67.3 . 1 851 160 152 VAL CB C 32.4 . 1 852 160 152 VAL N N 119.789 . 1 853 161 153 GLU H H 8.442 . 1 854 161 153 GLU HA H 4.13 . . 855 161 153 GLU C C 178 . . 856 161 153 GLU CA C 60.5 . 1 857 161 153 GLU CB C 29.4 . 1 858 161 153 GLU N N 117.697 . 1 859 162 154 ASP H H 8.029 . 1 860 162 154 ASP HA H 4.23 . . 861 162 154 ASP C C 177.8 . . 862 162 154 ASP CA C 57.6 . 1 863 162 154 ASP CB C 40.7 . 1 864 162 154 ASP N N 120.573 . 1 865 163 155 ILE H H 7.463 . 1 866 163 155 ILE HA H 3.33 . . 867 163 155 ILE C C 178.5 . . 868 163 155 ILE CA C 64.7 . 1 869 163 155 ILE CB C 37.6 . 1 870 163 155 ILE N N 119.167 . 1 871 164 156 GLU H H 9.105 . 1 872 164 156 GLU HA H 3.53 . . 873 164 156 GLU C C 176.4 . . 874 164 156 GLU CA C 60.9 . 1 875 164 156 GLU CB C 30.3 . 1 876 164 156 GLU N N 121.365 . 1 877 165 157 LYS H H 7.568 . 1 878 165 157 LYS HA H 3.98 . . 879 165 157 LYS C C 177.2 . . 880 165 157 LYS CA C 59.7 . 1 881 165 157 LYS CB C 33 . 1 882 165 157 LYS N N 115.643 . 1 883 166 158 LYS H H 7.06 . 1 884 166 158 LYS HA H 4.44 . . 885 166 158 LYS C C 176.2 . . 886 166 158 LYS CA C 55.3 . 1 887 166 158 LYS CB C 33.9 . 1 888 166 158 LYS N N 113.015 . 1 889 167 159 LEU H H 8.671 . 1 890 167 159 LEU HA H 4.08 . . 891 167 159 LEU C C 176.5 . . 892 167 159 LEU CA C 57.4 . 1 893 167 159 LEU CB C 44.1 . 1 894 167 159 LEU N N 120.778 . 1 895 168 160 LEU H H 8.539 . 1 896 168 160 LEU HA H 3.92 . . 897 168 160 LEU C C 176.9 . . 898 168 160 LEU CA C 60.4 . 1 899 168 160 LEU CB C 38.7 . 1 900 168 160 LEU N N 118.696 . 1 901 169 161 PRO HA H 4.36 . . 902 169 161 PRO C C 177.6 . . 903 169 161 PRO CA C 65.7 . 1 904 169 161 PRO CB C 31.8 . 1 905 170 162 LEU H H 7.325 . 1 906 170 162 LEU HA H 4.34 . . 907 170 162 LEU C C 177.9 . . 908 170 162 LEU CA C 55.9 . 1 909 170 162 LEU CB C 42.5 . 1 910 170 162 LEU N N 114.554 . 1 911 171 163 LEU H H 7.676 . 1 912 171 163 LEU HA H 4.28 . . 913 171 163 LEU C C 177 . . 914 171 163 LEU CA C 56 . 1 915 171 163 LEU CB C 42.8 . 1 916 171 163 LEU N N 119.103 . 1 917 172 164 GLY H H 7.929 . 1 918 172 164 GLY HA2 H 4.03 . . 919 172 164 GLY C C 173.6 . . 920 172 164 GLY CA C 45.7 . 1 921 172 164 GLY N N 106.547 . 1 922 173 165 GLY H H 8.111 . 1 923 173 165 GLY HA2 H 3.98 . . 924 173 165 GLY HA3 H 3.975 . 2 925 173 165 GLY C C 172.7 . . 926 173 165 GLY CA C 45.3 . 1 927 173 165 GLY N N 108.408 . 1 928 174 166 ALA H H 8.16 . 1 929 174 166 ALA HA H 4.35 . . 930 174 166 ALA C C 176.5 . . 931 174 166 ALA CA C 52.5 . 1 932 174 166 ALA CB C 19.8 . 1 933 174 166 ALA N N 123.386 . 1 934 175 167 ARG H H 8.328 . 1 935 175 167 ARG HA H 4.38 . . 936 175 167 ARG C C 174.4 . . 937 175 167 ARG CA C 56.2 . 1 938 175 167 ARG CB C 30.9 . 1 939 175 167 ARG N N 121.097 . 1 940 176 168 ILE H H 7.716 . 1 941 176 168 ILE HA H 4.09 . . 942 176 168 ILE C C 180.1 . . 943 176 168 ILE CA C 63 . 1 944 176 168 ILE CB C 39.9 . 1 945 176 168 ILE N N 126.502 . 1 stop_ save_