data_27381 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment of human TRIM25 PRYSPRY domain ; _BMRB_accession_number 27381 _BMRB_flat_file_name bmr27381.str _Entry_type original _Submission_date 2018-01-23 _Accession_date 2018-01-23 _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 Haubrich Kevin . . 2 Hennig Janosch . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 175 "13C chemical shifts" 335 "15N chemical shifts" 175 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-05-22 original BMRB . stop_ _Original_release_date 2018-01-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29739942 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Koliopoulos Marios G. . 2 Lethier Mathilde . . 3 'van der Veen' Annemarthe . . 4 Haubrich Kevin . . 5 Hennig Janosch . . 6 Kowalinski Eva . . 7 Stevens Rebecca . . 8 Martin Stephen . . 9 'Reis e Sousa' Caetano . . 10 Cusack Stephen . . 11 Rittinger Katrin . . stop_ _Journal_abbreviation 'Nat. Commun.' _Journal_name_full 'Nature communications' _Journal_volume 9 _Journal_issue 1 _Journal_ISSN 2041-1723 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1820 _Page_last 1820 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'TRIM25 PRYSPRY' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PRYSPRY $TRIM25_PRYSPRY stop_ _System_molecular_weight 22.2 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TRIM25_PRYSPRY _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TRIM25_PRYSPRY _Molecular_mass 22.2 _Mol_thiol_state 'all free' loop_ _Biological_function 'substrate recognition' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 194 _Mol_residue_sequence ; GPKVLETFLAKSRPELLEYY IKVILDYNTAHNKVALSECY TVASVAEMPQNYRPHPQRFT YCSQVLGLHCYKKGIHYWEV ELQKNNFCGVGICYGSMNRQ GPESRLGRNSASWCVEWFNT KISAWHNNVEKTLPSTKATR VGVLLNCDHGFVIFFAVADK VHLMYKFRVDFTEALYPAFW VFSAGATLSICSPK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 0 PRO 3 1 LYS 4 2 VAL 5 3 LEU 6 4 GLU 7 5 THR 8 6 PHE 9 7 LEU 10 8 ALA 11 9 LYS 12 10 SER 13 11 ARG 14 12 PRO 15 13 GLU 16 14 LEU 17 15 LEU 18 16 GLU 19 17 TYR 20 18 TYR 21 19 ILE 22 20 LYS 23 21 VAL 24 22 ILE 25 23 LEU 26 24 ASP 27 25 TYR 28 26 ASN 29 27 THR 30 28 ALA 31 29 HIS 32 30 ASN 33 31 LYS 34 32 VAL 35 33 ALA 36 34 LEU 37 35 SER 38 36 GLU 39 37 CYS 40 38 TYR 41 39 THR 42 40 VAL 43 41 ALA 44 42 SER 45 43 VAL 46 44 ALA 47 45 GLU 48 46 MET 49 47 PRO 50 48 GLN 51 49 ASN 52 50 TYR 53 51 ARG 54 52 PRO 55 53 HIS 56 54 PRO 57 55 GLN 58 56 ARG 59 57 PHE 60 58 THR 61 59 TYR 62 60 CYS 63 61 SER 64 62 GLN 65 63 VAL 66 64 LEU 67 65 GLY 68 66 LEU 69 67 HIS 70 68 CYS 71 69 TYR 72 70 LYS 73 71 LYS 74 72 GLY 75 73 ILE 76 74 HIS 77 75 TYR 78 76 TRP 79 77 GLU 80 78 VAL 81 79 GLU 82 80 LEU 83 81 GLN 84 82 LYS 85 83 ASN 86 84 ASN 87 85 PHE 88 86 CYS 89 87 GLY 90 88 VAL 91 89 GLY 92 90 ILE 93 91 CYS 94 92 TYR 95 93 GLY 96 94 SER 97 95 MET 98 96 ASN 99 97 ARG 100 98 GLN 101 99 GLY 102 100 PRO 103 101 GLU 104 102 SER 105 103 ARG 106 104 LEU 107 105 GLY 108 106 ARG 109 107 ASN 110 108 SER 111 109 ALA 112 110 SER 113 111 TRP 114 112 CYS 115 113 VAL 116 114 GLU 117 115 TRP 118 116 PHE 119 117 ASN 120 118 THR 121 119 LYS 122 120 ILE 123 121 SER 124 122 ALA 125 123 TRP 126 124 HIS 127 125 ASN 128 126 ASN 129 127 VAL 130 128 GLU 131 129 LYS 132 130 THR 133 131 LEU 134 132 PRO 135 133 SER 136 134 THR 137 135 LYS 138 136 ALA 139 137 THR 140 138 ARG 141 139 VAL 142 140 GLY 143 141 VAL 144 142 LEU 145 143 LEU 146 144 ASN 147 145 CYS 148 146 ASP 149 147 HIS 150 148 GLY 151 149 PHE 152 150 VAL 153 151 ILE 154 152 PHE 155 153 PHE 156 154 ALA 157 155 VAL 158 156 ALA 159 157 ASP 160 158 LYS 161 159 VAL 162 160 HIS 163 161 LEU 164 162 MET 165 163 TYR 166 164 LYS 167 165 PHE 168 166 ARG 169 167 VAL 170 168 ASP 171 169 PHE 172 170 THR 173 171 GLU 174 172 ALA 175 173 LEU 176 174 TYR 177 175 PRO 178 176 ALA 179 177 PHE 180 178 TRP 181 179 VAL 182 180 PHE 183 181 SER 184 182 ALA 185 183 GLY 186 184 ALA 187 185 THR 188 186 LEU 189 187 SER 190 188 ILE 191 189 CYS 192 190 SER 193 191 PRO 194 192 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP Q14258 TRI25_HUMAN . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TRIM25_PRYSPRY Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $TRIM25_PRYSPRY 'recombinant technology' . Escherichia coli BL21(DE3) pETm22 'co-expressed with KJE, ClpB and GroELS' 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TRIM25_PRYSPRY 0.45 mM 0.3 0.6 '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 20 mM . . 'natural abundance' 'sodium chloride' 150 mM . . 'natural abundance' TCEP 0.2 mM . . 'natural abundance' 'sodium azide' 0.02 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Cara _Saveframe_category software _Name Cara _Version 1.8.4 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 8.7 loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _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 $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(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' 170 10 mM pH 6.5 0.2 pH pressure 1 . atm temperature 289 0.1 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 water C 13 protons ppm 4.773 internal direct . . . 1.0 water H 1 protons ppm 4.773 internal direct . . . 1.0 water N 15 protons ppm 4.77 internal direct . . . 1.0 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 $Cara $NMRPipe $TOPSPIN stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' '3D CBCA(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 PRYSPRY _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 1 3 LYS H H 8.538 0.020 1 2 1 3 LYS CA C 56.620 0.3 1 3 1 3 LYS CB C 31.875 0.3 1 4 1 3 LYS N N 122.425 0.3 1 5 2 4 VAL H H 7.994 0.020 1 6 2 4 VAL CA C 66.265 0.3 1 7 2 4 VAL CB C 31.680 0.3 1 8 2 4 VAL N N 122.007 0.3 1 9 3 5 LEU H H 8.125 0.020 1 10 3 5 LEU CA C 58.763 0.3 1 11 3 5 LEU CB C 40.497 0.3 1 12 3 5 LEU N N 122.288 0.3 1 13 4 6 GLU H H 8.095 0.020 1 14 4 6 GLU CA C 60.225 0.3 1 15 4 6 GLU CB C 28.562 0.3 1 16 4 6 GLU N N 117.161 0.3 1 17 5 7 THR H H 7.892 0.020 1 18 5 7 THR CA C 66.021 0.3 1 19 5 7 THR CB C 68.457 0.3 1 20 5 7 THR N N 114.988 0.3 1 21 6 8 PHE H H 7.970 0.020 1 22 6 8 PHE CA C 62.806 0.3 1 23 6 8 PHE CB C 39.717 0.3 1 24 6 8 PHE N N 120.724 0.3 1 25 7 9 LEU H H 8.040 0.020 1 26 7 9 LEU CA C 56.912 0.3 1 27 7 9 LEU CB C 41.276 0.3 1 28 7 9 LEU N N 116.897 0.3 1 29 8 10 ALA H H 6.895 0.020 1 30 8 10 ALA CA C 51.213 0.3 1 31 8 10 ALA CB C 19.405 0.3 1 32 8 10 ALA N N 118.338 0.3 1 33 9 11 LYS H H 6.980 0.020 1 34 9 11 LYS CA C 57.594 0.3 1 35 9 11 LYS CB C 33.677 0.3 1 36 9 11 LYS N N 119.957 0.3 1 37 10 12 SER H H 8.326 0.020 1 38 10 12 SER CA C 56.133 0.3 1 39 10 12 SER CB C 65.437 0.3 1 40 10 12 SER N N 115.344 0.3 1 41 11 13 ARG H H 9.150 0.020 1 42 11 13 ARG CA C 62.027 0.3 1 43 11 13 ARG CB C 26.906 0.3 1 44 11 13 ARG N N 120.544 0.3 1 45 13 15 GLU H H 6.781 0.020 1 46 13 15 GLU CA C 58.471 0.3 1 47 13 15 GLU CB C 30.413 0.3 1 48 13 15 GLU N N 114.100 0.3 1 49 14 16 LEU H H 7.994 0.020 1 50 14 16 LEU CA C 57.789 0.3 1 51 14 16 LEU CB C 39.035 0.3 1 52 14 16 LEU N N 123.204 0.3 1 53 15 17 LEU H H 7.940 0.020 1 54 15 17 LEU CA C 56.864 0.3 1 55 15 17 LEU CB C 41.422 0.3 1 56 15 17 LEU N N 115.034 0.3 1 57 16 18 GLU H H 7.070 0.020 1 58 16 18 GLU CA C 58.861 0.3 1 59 16 18 GLU CB C 28.660 0.3 1 60 16 18 GLU N N 120.331 0.3 1 61 17 19 TYR H H 7.719 0.020 1 62 17 19 TYR CA C 56.230 0.3 1 63 17 19 TYR CB C 37.282 0.3 1 64 17 19 TYR N N 116.874 0.3 1 65 18 20 TYR H H 7.648 0.020 1 66 18 20 TYR CA C 59.397 0.3 1 67 18 20 TYR CB C 39.766 0.3 1 68 18 20 TYR N N 122.929 0.3 1 69 19 21 ILE H H 8.213 0.020 1 70 19 21 ILE CA C 57.887 0.3 1 71 19 21 ILE CB C 42.445 0.3 1 72 19 21 ILE N N 126.921 0.3 1 73 20 22 LYS H H 7.965 0.020 1 74 20 22 LYS CA C 56.328 0.3 1 75 20 22 LYS CB C 32.557 0.3 1 76 20 22 LYS N N 123.484 0.3 1 77 21 23 VAL H H 8.095 0.020 1 78 21 23 VAL CA C 62.465 0.3 1 79 21 23 VAL CB C 32.849 0.3 1 80 21 23 VAL N N 131.404 0.3 1 81 22 24 ILE H H 8.566 0.020 1 82 22 24 ILE CA C 58.958 0.3 1 83 22 24 ILE CB C 40.984 0.3 1 84 22 24 ILE N N 125.386 0.3 1 85 23 25 LEU H H 8.826 0.020 1 86 23 25 LEU CA C 55.110 0.3 1 87 23 25 LEU CB C 42.348 0.3 1 88 23 25 LEU N N 123.478 0.3 1 89 24 26 ASP H H 8.758 0.020 1 90 24 26 ASP CA C 52.869 0.3 1 91 24 26 ASP CB C 41.909 0.3 1 92 24 26 ASP N N 117.943 0.3 1 93 25 27 TYR H H 7.915 0.020 1 94 25 27 TYR CA C 59.640 0.3 1 95 25 27 TYR CB C 38.061 0.3 1 96 25 27 TYR N N 128.174 0.3 1 97 27 29 THR H H 7.122 0.020 1 98 27 29 THR CA C 61.004 0.3 1 99 27 29 THR CB C 72.305 0.3 1 100 27 29 THR N N 134.296 0.3 1 101 28 30 ALA H H 6.094 0.020 1 102 28 30 ALA CA C 52.967 0.3 1 103 28 30 ALA CB C 18.528 0.3 1 104 28 30 ALA N N 122.628 0.3 1 105 29 31 HIS H H 7.908 0.020 1 106 29 31 HIS CA C 57.253 0.3 1 107 29 31 HIS CB C 34.310 0.3 1 108 29 31 HIS N N 121.920 0.3 1 109 30 32 ASN H H 7.825 0.020 1 110 30 32 ASN CA C 55.889 0.3 1 111 30 32 ASN CB C 38.840 0.3 1 112 30 32 ASN N N 121.488 0.3 1 113 31 33 LYS H H 8.472 0.020 1 114 31 33 LYS CA C 56.612 0.3 1 115 31 33 LYS N N 120.887 0.3 1 116 32 34 VAL H H 8.880 0.020 1 117 32 34 VAL CA C 61.900 0.3 1 118 32 34 VAL CB C 31.488 0.3 1 119 32 34 VAL N N 123.289 0.3 1 120 33 35 ALA H H 9.277 0.020 1 121 33 35 ALA CA C 50.921 0.3 1 122 33 35 ALA CB C 19.940 0.3 1 123 33 35 ALA N N 130.813 0.3 1 124 34 36 LEU H H 8.663 0.020 1 125 34 36 LEU CA C 52.575 0.3 1 126 34 36 LEU CB C 41.196 0.3 1 127 34 36 LEU N N 122.291 0.3 1 128 39 41 THR H H 7.672 0.020 1 129 39 41 THR CA C 61.835 0.3 1 130 39 41 THR CB C 71.320 0.3 1 131 39 41 THR N N 104.550 0.3 1 132 40 42 VAL H H 7.673 0.020 1 133 40 42 VAL CA C 61.004 0.3 1 134 40 42 VAL CB C 34.213 0.3 1 135 40 42 VAL N N 121.894 0.3 1 136 41 43 ALA H H 8.768 0.020 1 137 41 43 ALA CA C 49.070 0.3 1 138 41 43 ALA CB C 20.768 0.3 1 139 41 43 ALA N N 128.050 0.3 1 140 42 44 SER H H 8.885 0.020 1 141 42 44 SER CA C 56.036 0.3 1 142 42 44 SER CB C 66.021 0.3 1 143 42 44 SER N N 115.076 0.3 1 144 43 45 VAL H H 7.994 0.020 1 145 43 45 VAL CA C 63.245 0.3 1 146 43 45 VAL CB C 31.729 0.3 1 147 43 45 VAL N N 122.530 0.3 1 148 44 46 ALA H H 8.950 0.020 1 149 44 46 ALA CA C 50.726 0.3 1 150 44 46 ALA CB C 20.622 0.3 1 151 44 46 ALA N N 134.797 0.3 1 152 45 47 GLU H H 8.604 0.020 1 153 45 47 GLU CA C 58.130 0.3 1 154 45 47 GLU CB C 29.878 0.3 1 155 45 47 GLU N N 120.966 0.3 1 156 46 48 MET H H 7.637 0.020 1 157 46 48 MET CA C 51.554 0.3 1 158 46 48 MET CB C 32.849 0.3 1 159 46 48 MET N N 116.162 0.3 1 160 48 50 GLN H H 8.963 0.020 1 161 48 50 GLN CA C 54.108 0.3 1 162 48 50 GLN CB C 29.345 0.3 1 163 48 50 GLN N N 120.774 0.3 1 164 49 51 ASN H H 8.008 0.020 1 165 49 51 ASN CA C 52.626 0.3 1 166 49 51 ASN CB C 36.746 0.3 1 167 49 51 ASN N N 118.164 0.3 1 168 50 52 TYR H H 7.533 0.020 1 169 50 52 TYR CA C 55.159 0.3 1 170 50 52 TYR CB C 37.769 0.3 1 171 50 52 TYR N N 119.368 0.3 1 172 51 53 ARG H H 8.824 0.020 1 173 51 53 ARG CA C 54.526 0.3 1 174 51 53 ARG CB C 29.390 0.3 1 175 51 53 ARG N N 123.961 0.3 1 176 53 55 HIS H H 8.176 0.020 1 177 53 55 HIS CA C 55.889 0.3 1 178 53 55 HIS CB C 34.456 0.3 1 179 53 55 HIS N N 124.042 0.3 1 180 55 57 GLN H H 10.658 0.020 1 181 55 57 GLN CA C 55.548 0.3 1 182 55 57 GLN CB C 28.270 0.3 1 183 55 57 GLN N N 118.240 0.3 1 184 56 58 ARG H H 7.648 0.020 1 185 56 58 ARG CA C 57.533 0.3 1 186 56 58 ARG CB C 30.124 0.3 1 187 56 58 ARG N N 121.208 0.3 1 188 57 59 PHE H H 8.106 0.020 1 189 57 59 PHE CA C 60.030 0.3 1 190 57 59 PHE CB C 38.889 0.3 1 191 57 59 PHE N N 124.348 0.3 1 192 58 60 THR H H 7.809 0.020 1 193 58 60 THR CA C 62.128 0.3 1 194 58 60 THR CB C 69.605 0.3 1 195 58 60 THR N N 109.316 0.3 1 196 59 61 TYR H H 9.311 0.020 1 197 59 61 TYR CA C 59.397 0.3 1 198 59 61 TYR CB C 42.153 0.3 1 199 59 61 TYR N N 125.382 0.3 1 200 61 63 SER H H 8.154 0.020 1 201 61 63 SER CA C 56.934 0.3 1 202 61 63 SER N N 114.965 0.3 1 203 62 64 GLN H H 7.747 0.020 1 204 62 64 GLN CA C 52.382 0.3 1 205 62 64 GLN CB C 32.362 0.3 1 206 62 64 GLN N N 122.988 0.3 1 207 63 65 VAL H H 8.125 0.020 1 208 63 65 VAL CA C 60.663 0.3 1 209 63 65 VAL CB C 33.872 0.3 1 210 63 65 VAL N N 113.916 0.3 1 211 64 66 LEU H H 8.734 0.020 1 212 64 66 LEU CA C 53.162 0.3 1 213 64 66 LEU CB C 45.076 0.3 1 214 64 66 LEU N N 124.399 0.3 1 215 65 67 GLY H H 8.506 0.020 1 216 65 67 GLY CA C 44.442 0.3 1 217 65 67 GLY N N 103.223 0.3 1 218 66 68 LEU H H 8.459 0.020 1 219 66 68 LEU CA C 57.174 0.3 1 220 66 68 LEU CB C 43.712 0.3 1 221 66 68 LEU N N 119.587 0.3 1 222 67 69 HIS H H 7.484 0.020 1 223 67 69 HIS CA C 54.233 0.3 1 224 67 69 HIS CB C 31.923 0.3 1 225 67 69 HIS N N 113.467 0.3 1 226 68 70 CYS H H 7.612 0.020 1 227 68 70 CYS CA C 51.846 0.3 1 228 68 70 CYS CB C 29.634 0.3 1 229 68 70 CYS N N 113.347 0.3 1 230 69 71 TYR H H 8.387 0.020 1 231 69 71 TYR CA C 56.474 0.3 1 232 69 71 TYR CB C 41.471 0.3 1 233 69 71 TYR N N 118.617 0.3 1 234 70 72 LYS H H 9.167 0.020 1 235 70 72 LYS CA C 55.159 0.3 1 236 70 72 LYS CB C 35.431 0.3 1 237 70 72 LYS N N 122.965 0.3 1 238 71 73 LYS H H 7.891 0.020 1 239 71 73 LYS CA C 54.672 0.3 1 240 71 73 LYS CB C 36.405 0.3 1 241 71 73 LYS N N 119.384 0.3 1 242 72 74 GLY H H 9.190 0.020 1 243 72 74 GLY CA C 44.978 0.3 1 244 72 74 GLY N N 113.436 0.3 1 245 73 75 ILE H H 7.503 0.020 1 246 73 75 ILE CA C 60.468 0.3 1 247 73 75 ILE CB C 39.863 0.3 1 248 73 75 ILE N N 118.587 0.3 1 249 74 76 HIS H H 8.600 0.020 1 250 74 76 HIS CA C 54.477 0.3 1 251 74 76 HIS CB C 33.921 0.3 1 252 74 76 HIS N N 123.032 0.3 1 253 75 77 TYR H H 8.098 0.020 1 254 75 77 TYR CA C 55.354 0.3 1 255 75 77 TYR CB C 44.394 0.3 1 256 75 77 TYR N N 125.211 0.3 1 257 76 78 TRP H H 7.604 0.020 1 258 76 78 TRP CA C 56.669 0.3 1 259 76 78 TRP CB C 31.826 0.3 1 260 76 78 TRP N N 122.364 0.3 1 261 77 79 GLU H H 8.417 0.020 1 262 77 79 GLU CA C 53.600 0.3 1 263 77 79 GLU CB C 34.651 0.3 1 264 77 79 GLU N N 115.447 0.3 1 265 78 80 VAL H H 9.315 0.020 1 266 78 80 VAL CA C 59.981 0.3 1 267 78 80 VAL CB C 35.625 0.3 1 268 78 80 VAL N N 120.179 0.3 1 269 79 81 GLU H H 9.459 0.020 1 270 79 81 GLU CA C 55.159 0.3 1 271 79 81 GLU CB C 31.729 0.3 1 272 79 81 GLU N N 128.266 0.3 1 273 80 82 LEU H H 9.092 0.020 1 274 80 82 LEU CA C 54.185 0.3 1 275 80 82 LEU CB C 43.224 0.3 1 276 80 82 LEU N N 127.766 0.3 1 277 81 83 GLN H H 8.066 0.020 1 278 81 83 GLN CA C 55.695 0.3 1 279 81 83 GLN CB C 29.948 0.3 1 280 81 83 GLN N N 118.604 0.3 1 281 83 85 ASN H H 8.362 0.020 1 282 83 85 ASN CA C 53.632 0.3 1 283 83 85 ASN N N 116.473 0.3 1 284 84 86 ASN H H 7.907 0.020 1 285 84 86 ASN CA C 54.306 0.3 1 286 84 86 ASN CB C 37.525 0.3 1 287 84 86 ASN N N 117.826 0.3 1 288 86 88 CYS H H 8.876 0.020 1 289 86 88 CYS CA C 57.010 0.3 1 290 86 88 CYS CB C 29.975 0.3 1 291 86 88 CYS N N 116.823 0.3 1 292 87 89 GLY H H 10.147 0.020 1 293 87 89 GLY CA C 46.147 0.3 1 294 87 89 GLY N N 109.015 0.3 1 295 88 90 VAL H H 9.089 0.020 1 296 88 90 VAL CA C 61.296 0.3 1 297 88 90 VAL CB C 36.307 0.3 1 298 88 90 VAL N N 120.081 0.3 1 299 89 91 GLY H H 8.774 0.020 1 300 89 91 GLY CA C 46.537 0.3 1 301 89 91 GLY N N 110.600 0.3 1 302 90 92 ILE H H 9.311 0.020 1 303 90 92 ILE CA C 59.251 0.3 1 304 90 92 ILE CB C 44.588 0.3 1 305 90 92 ILE N N 116.992 0.3 1 306 91 93 CYS H H 9.403 0.020 1 307 91 93 CYS CA C 55.743 0.3 1 308 91 93 CYS CB C 35.090 0.3 1 309 91 93 CYS N N 115.239 0.3 1 310 92 94 TYR H H 8.725 0.020 1 311 92 94 TYR CA C 54.379 0.3 1 312 92 94 TYR CB C 38.694 0.3 1 313 92 94 TYR N N 120.115 0.3 1 314 93 95 GLY H H 9.547 0.020 1 315 93 95 GLY CA C 47.219 0.3 1 316 93 95 GLY N N 110.764 0.3 1 317 94 96 SER H H 7.602 0.020 1 318 94 96 SER CA C 58.282 0.3 1 319 94 96 SER CB C 62.125 0.3 1 320 94 96 SER N N 110.934 0.3 1 321 95 97 MET H H 7.382 0.020 1 322 95 97 MET CA C 57.253 0.3 1 323 95 97 MET CB C 33.239 0.3 1 324 95 97 MET N N 123.668 0.3 1 325 96 98 ASN H H 8.539 0.020 1 326 96 98 ASN CA C 54.574 0.3 1 327 96 98 ASN CB C 38.792 0.3 1 328 96 98 ASN N N 127.766 0.3 1 329 97 99 ARG H H 8.329 0.020 1 330 97 99 ARG CA C 53.259 0.3 1 331 97 99 ARG CB C 28.903 0.3 1 332 97 99 ARG N N 114.358 0.3 1 333 98 100 GLN H H 8.048 0.020 1 334 98 100 GLN CA C 54.379 0.3 1 335 98 100 GLN CB C 31.095 0.3 1 336 98 100 GLN N N 120.188 0.3 1 337 99 101 GLY H H 7.842 0.020 1 338 99 101 GLY CA C 44.929 0.3 1 339 99 101 GLY N N 105.034 0.3 1 340 101 103 GLU H H 9.101 0.020 1 341 101 103 GLU CA C 57.740 0.3 1 342 101 103 GLU CB C 27.929 0.3 1 343 101 103 GLU N N 116.672 0.3 1 344 102 104 SER H H 7.492 0.020 1 345 102 104 SER CA C 58.520 0.3 1 346 102 104 SER CB C 65.583 0.3 1 347 102 104 SER N N 113.852 0.3 1 348 103 105 ARG H H 6.586 0.020 1 349 103 105 ARG CA C 54.529 0.3 1 350 103 105 ARG CB C 29.101 0.3 1 351 103 105 ARG N N 122.793 0.3 1 352 104 106 LEU H H 8.566 0.020 1 353 104 106 LEU CA C 55.695 0.3 1 354 104 106 LEU CB C 42.737 0.3 1 355 104 106 LEU N N 126.980 0.3 1 356 105 107 GLY H H 9.137 0.020 1 357 105 107 GLY CA C 45.222 0.3 1 358 105 107 GLY N N 107.863 0.3 1 359 106 108 ARG H H 7.849 0.020 1 360 106 108 ARG CA C 54.185 0.3 1 361 106 108 ARG CB C 27.393 0.3 1 362 106 108 ARG N N 121.510 0.3 1 363 107 109 ASN H H 6.641 0.020 1 364 107 109 ASN CA C 51.505 0.3 1 365 107 109 ASN CB C 41.325 0.3 1 366 107 109 ASN N N 108.135 0.3 1 367 108 110 SER H H 8.837 0.020 1 368 108 110 SER CA C 59.202 0.3 1 369 108 110 SER CB C 62.709 0.3 1 370 108 110 SER N N 114.619 0.3 1 371 109 111 ALA H H 7.839 0.020 1 372 109 111 ALA CA C 50.288 0.3 1 373 109 111 ALA CB C 20.281 0.3 1 374 109 111 ALA N N 123.519 0.3 1 375 110 112 SER H H 6.439 0.020 1 376 110 112 SER CA C 57.549 0.3 1 377 110 112 SER CB C 66.950 0.3 1 378 110 112 SER N N 104.870 0.3 1 379 111 113 TRP H H 8.569 0.020 1 380 111 113 TRP CA C 58.081 0.3 1 381 111 113 TRP CB C 34.067 0.3 1 382 111 113 TRP N N 122.295 0.3 1 383 112 114 CYS H H 9.123 0.020 1 384 112 114 CYS CA C 56.474 0.3 1 385 112 114 CYS CB C 31.485 0.3 1 386 112 114 CYS N N 115.020 0.3 1 387 113 115 VAL H H 8.213 0.020 1 388 113 115 VAL CA C 60.423 0.3 1 389 113 115 VAL CB C 33.777 0.3 1 390 113 115 VAL N N 113.647 0.3 1 391 114 116 GLU H H 9.223 0.020 1 392 114 116 GLU CA C 55.548 0.3 1 393 114 116 GLU CB C 36.307 0.3 1 394 114 116 GLU N N 123.595 0.3 1 395 115 117 TRP H H 9.878 0.020 1 396 115 117 TRP CA C 58.715 0.3 1 397 115 117 TRP CB C 32.557 0.3 1 398 115 117 TRP N N 130.463 0.3 1 399 116 118 PHE H H 8.954 0.020 1 400 116 118 PHE CA C 57.137 0.3 1 401 116 118 PHE CB C 41.861 0.3 1 402 116 118 PHE N N 123.052 0.3 1 403 118 120 THR H H 8.182 0.020 1 404 118 120 THR CA C 64.073 0.3 1 405 118 120 THR N N 110.444 0.3 1 406 119 121 LYS H H 7.785 0.020 1 407 119 121 LYS CA C 55.743 0.3 1 408 119 121 LYS CB C 33.726 0.3 1 409 119 121 LYS N N 123.941 0.3 1 410 120 122 ILE H H 8.834 0.020 1 411 120 122 ILE CA C 60.225 0.3 1 412 120 122 ILE CB C 38.987 0.3 1 413 120 122 ILE N N 126.469 0.3 1 414 121 123 SER H H 8.800 0.020 1 415 121 123 SER CA C 56.377 0.3 1 416 121 123 SER CB C 67.093 0.3 1 417 121 123 SER N N 119.583 0.3 1 418 122 124 ALA H H 8.861 0.020 1 419 122 124 ALA CA C 49.752 0.3 1 420 122 124 ALA CB C 21.207 0.3 1 421 122 124 ALA N N 123.846 0.3 1 422 123 125 TRP H H 9.086 0.020 1 423 123 125 TRP CA C 56.766 0.3 1 424 123 125 TRP CB C 33.872 0.3 1 425 123 125 TRP N N 121.467 0.3 1 426 124 126 HIS H H 7.844 0.020 1 427 124 126 HIS CA C 57.059 0.3 1 428 124 126 HIS CB C 31.729 0.3 1 429 124 126 HIS N N 116.467 0.3 1 430 125 127 ASN H H 6.736 0.020 1 431 125 127 ASN CA C 52.723 0.3 1 432 125 127 ASN CB C 36.697 0.3 1 433 125 127 ASN N N 124.788 0.3 1 434 126 128 ASN H H 8.575 0.020 1 435 126 128 ASN CA C 54.720 0.3 1 436 126 128 ASN CB C 38.792 0.3 1 437 126 128 ASN N N 108.429 0.3 1 438 127 129 VAL H H 7.874 0.020 1 439 127 129 VAL CA C 62.319 0.3 1 440 127 129 VAL CB C 32.703 0.3 1 441 127 129 VAL N N 120.810 0.3 1 442 128 130 GLU H H 8.019 0.020 1 443 128 130 GLU CA C 54.233 0.3 1 444 128 130 GLU CB C 30.316 0.3 1 445 128 130 GLU N N 131.354 0.3 1 446 129 131 LYS H H 8.457 0.020 1 447 129 131 LYS CA C 53.210 0.3 1 448 129 131 LYS CB C 33.385 0.3 1 449 129 131 LYS N N 127.828 0.3 1 450 130 132 THR H H 8.478 0.020 1 451 130 132 THR CA C 63.342 0.3 1 452 130 132 THR CB C 68.847 0.3 1 453 130 132 THR N N 121.825 0.3 1 454 131 133 LEU H H 8.732 0.020 1 455 131 133 LEU CA C 51.993 0.3 1 456 131 133 LEU CB C 40.838 0.3 1 457 131 133 LEU N N 126.352 0.3 1 458 133 135 SER H H 8.227 0.020 1 459 133 135 SER CA C 59.104 0.3 1 460 133 135 SER CB C 63.294 0.3 1 461 133 135 SER N N 114.885 0.3 1 462 134 136 THR H H 7.421 0.020 1 463 134 136 THR CA C 59.884 0.3 1 464 134 136 THR CB C 69.383 0.3 1 465 134 136 THR N N 116.881 0.3 1 466 135 137 LYS H H 8.625 0.020 1 467 135 137 LYS CA C 55.938 0.3 1 468 135 137 LYS CB C 32.070 0.3 1 469 135 137 LYS N N 125.987 0.3 1 470 136 138 ALA H H 8.295 0.020 1 471 136 138 ALA CA C 53.259 0.3 1 472 136 138 ALA CB C 19.940 0.3 1 473 136 138 ALA N N 124.697 0.3 1 474 137 139 THR H H 8.770 0.020 1 475 137 139 THR CA C 60.420 0.3 1 476 137 139 THR CB C 68.165 0.3 1 477 137 139 THR N N 109.696 0.3 1 478 138 140 ARG H H 7.205 0.020 1 479 138 140 ARG CA C 54.185 0.3 1 480 138 140 ARG CB C 33.336 0.3 1 481 138 140 ARG N N 121.078 0.3 1 482 139 141 VAL H H 9.110 0.020 1 483 139 141 VAL CA C 58.910 0.3 1 484 139 141 VAL CB C 35.772 0.3 1 485 139 141 VAL N N 125.697 0.3 1 486 140 142 GLY H H 9.828 0.020 1 487 140 142 GLY CA C 44.296 0.3 1 488 140 142 GLY N N 115.164 0.3 1 489 141 143 VAL H H 8.623 0.020 1 490 141 143 VAL CA C 60.744 0.3 1 491 141 143 VAL CB C 31.777 0.3 1 492 141 143 VAL N N 126.154 0.3 1 493 142 144 LEU H H 8.777 0.020 1 494 142 144 LEU CA C 50.336 0.3 1 495 142 144 LEU CB C 43.419 0.3 1 496 142 144 LEU N N 125.382 0.3 1 497 143 145 LEU H H 9.489 0.020 1 498 143 145 LEU CA C 53.015 0.3 1 499 143 145 LEU CB C 45.076 0.3 1 500 143 145 LEU N N 127.463 0.3 1 501 144 146 ASN H H 8.808 0.020 1 502 144 146 ASN CA C 50.726 0.3 1 503 144 146 ASN CB C 38.110 0.3 1 504 144 146 ASN N N 125.777 0.3 1 505 145 147 CYS H H 8.305 0.020 1 506 145 147 CYS CA C 61.686 0.3 1 507 145 147 CYS CB C 27.198 0.3 1 508 145 147 CYS N N 120.978 0.3 1 509 146 148 ASP H H 7.084 0.020 1 510 146 148 ASP CA C 56.571 0.3 1 511 146 148 ASP CB C 39.669 0.3 1 512 146 148 ASP N N 119.534 0.3 1 513 147 149 HIS H H 7.446 0.020 1 514 147 149 HIS CA C 56.477 0.3 1 515 147 149 HIS CB C 31.780 0.3 1 516 147 149 HIS N N 115.350 0.3 1 517 148 150 GLY H H 6.903 0.020 1 518 148 150 GLY CA C 48.680 0.3 1 519 148 150 GLY N N 108.178 0.3 1 520 149 151 PHE H H 8.147 0.020 1 521 149 151 PHE CA C 56.474 0.3 1 522 149 151 PHE CB C 40.789 0.3 1 523 149 151 PHE N N 113.899 0.3 1 524 150 152 VAL H H 8.813 0.020 1 525 150 152 VAL CA C 57.692 0.3 1 526 150 152 VAL CB C 35.285 0.3 1 527 150 152 VAL N N 117.693 0.3 1 528 151 153 ILE H H 9.197 0.020 1 529 151 153 ILE CA C 60.225 0.3 1 530 151 153 ILE CB C 41.471 0.3 1 531 151 153 ILE N N 126.679 0.3 1 532 152 154 PHE H H 8.613 0.020 1 533 152 154 PHE CA C 56.230 0.3 1 534 152 154 PHE CB C 41.081 0.3 1 535 152 154 PHE N N 121.979 0.3 1 536 153 155 PHE H H 10.293 0.020 1 537 153 155 PHE CA C 57.253 0.3 1 538 153 155 PHE CB C 42.202 0.3 1 539 153 155 PHE N N 123.694 0.3 1 540 154 156 ALA H H 9.751 0.020 1 541 154 156 ALA CA C 51.625 0.3 1 542 154 156 ALA CB C 19.453 0.3 1 543 154 156 ALA N N 125.642 0.3 1 544 155 157 VAL H H 8.691 0.020 1 545 155 157 VAL CA C 62.855 0.3 1 546 155 157 VAL CB C 32.508 0.3 1 547 155 157 VAL N N 124.196 0.3 1 548 156 158 ALA H H 7.807 0.020 1 549 156 158 ALA CA C 51.749 0.3 1 550 156 158 ALA CB C 18.576 0.3 1 551 156 158 ALA N N 133.098 0.3 1 552 157 159 ASP H H 8.828 0.020 1 553 157 159 ASP CA C 56.718 0.3 1 554 157 159 ASP CB C 39.522 0.3 1 555 157 159 ASP N N 122.871 0.3 1 556 158 160 LYS H H 7.632 0.020 1 557 158 160 LYS CA C 53.844 0.3 1 558 158 160 LYS CB C 35.479 0.3 1 559 158 160 LYS N N 116.011 0.3 1 560 159 161 VAL H H 7.835 0.020 1 561 159 161 VAL CA C 60.712 0.3 1 562 159 161 VAL CB C 32.995 0.3 1 563 159 161 VAL N N 114.868 0.3 1 564 160 162 HIS H H 9.011 0.020 1 565 160 162 HIS CA C 54.672 0.3 1 566 160 162 HIS CB C 32.849 0.3 1 567 160 162 HIS N N 120.503 0.3 1 568 161 163 LEU H H 9.238 0.020 1 569 161 163 LEU CA C 57.205 0.3 1 570 161 163 LEU CB C 42.153 0.3 1 571 161 163 LEU N N 127.508 0.3 1 572 162 164 MET H H 9.128 0.020 1 573 162 164 MET CA C 57.594 0.3 1 574 162 164 MET CB C 34.700 0.3 1 575 162 164 MET N N 123.837 0.3 1 576 163 165 TYR H H 7.986 0.020 1 577 163 165 TYR CA C 59.104 0.3 1 578 163 165 TYR CB C 42.689 0.3 1 579 163 165 TYR N N 115.510 0.3 1 580 164 166 LYS H H 6.561 0.020 1 581 164 166 LYS CA C 53.308 0.3 1 582 164 166 LYS CB C 35.772 0.3 1 583 164 166 LYS N N 118.466 0.3 1 584 165 167 PHE H H 8.694 0.020 1 585 165 167 PHE CA C 56.961 0.3 1 586 165 167 PHE CB C 42.348 0.3 1 587 165 167 PHE N N 115.058 0.3 1 588 166 168 ARG H H 8.707 0.020 1 589 166 168 ARG CA C 54.915 0.3 1 590 166 168 ARG CB C 30.365 0.3 1 591 166 168 ARG N N 124.798 0.3 1 592 167 169 VAL H H 7.783 0.020 1 593 167 169 VAL CA C 60.614 0.3 1 594 167 169 VAL CB C 35.382 0.3 1 595 167 169 VAL N N 127.896 0.3 1 596 168 170 ASP H H 8.059 0.020 1 597 168 170 ASP CA C 51.993 0.3 1 598 168 170 ASP CB C 38.743 0.3 1 599 168 170 ASP N N 124.597 0.3 1 600 169 171 PHE H H 7.245 0.020 1 601 169 171 PHE CA C 58.520 0.3 1 602 169 171 PHE CB C 39.133 0.3 1 603 169 171 PHE N N 123.834 0.3 1 604 170 172 THR H H 8.660 0.020 1 605 170 172 THR CA C 62.173 0.3 1 606 170 172 THR CB C 69.090 0.3 1 607 170 172 THR N N 110.251 0.3 1 608 171 173 GLU H H 7.217 0.020 1 609 171 173 GLU CA C 54.038 0.3 1 610 171 173 GLU CB C 32.654 0.3 1 611 171 173 GLU N N 117.709 0.3 1 612 172 174 ALA H H 8.240 0.020 1 613 172 174 ALA CA C 52.480 0.3 1 614 172 174 ALA CB C 20.379 0.3 1 615 172 174 ALA N N 118.976 0.3 1 616 173 175 LEU H H 8.157 0.020 1 617 173 175 LEU CA C 52.483 0.3 1 618 173 175 LEU CB C 44.978 0.3 1 619 173 175 LEU N N 119.976 0.3 1 620 174 176 TYR H H 9.708 0.020 1 621 174 176 TYR CA C 55.646 0.3 1 622 174 176 TYR CB C 40.253 0.3 1 623 174 176 TYR N N 118.491 0.3 1 624 176 178 ALA H H 7.986 0.020 1 625 176 178 ALA CA C 51.067 0.3 1 626 176 178 ALA CB C 25.737 0.3 1 627 176 178 ALA N N 125.884 0.3 1 628 177 179 PHE H H 8.176 0.020 1 629 177 179 PHE CA C 56.669 0.3 1 630 177 179 PHE CB C 42.348 0.3 1 631 177 179 PHE N N 117.075 0.3 1 632 178 180 TRP H H 8.956 0.020 1 633 178 180 TRP CA C 56.523 0.3 1 634 178 180 TRP CB C 32.073 0.3 1 635 178 180 TRP N N 123.080 0.3 1 636 179 181 VAL H H 7.747 0.020 1 637 179 181 VAL CA C 60.176 0.3 1 638 179 181 VAL CB C 34.310 0.3 1 639 179 181 VAL N N 121.406 0.3 1 640 180 182 PHE H H 7.033 0.020 1 641 180 182 PHE CA C 58.422 0.3 1 642 180 182 PHE N N 121.742 0.3 1 643 181 183 SER H H 7.217 0.020 1 644 181 183 SER CA C 58.860 0.3 1 645 181 183 SER CB C 63.881 0.3 1 646 181 183 SER N N 115.919 0.3 1 647 182 184 ALA H H 8.062 0.020 1 648 182 184 ALA CA C 53.941 0.3 1 649 182 184 ALA CB C 17.943 0.3 1 650 182 184 ALA N N 123.325 0.3 1 651 183 185 GLY H H 8.566 0.020 1 652 183 185 GLY CA C 45.222 0.3 1 653 183 185 GLY N N 111.096 0.3 1 654 184 186 ALA H H 7.873 0.020 1 655 184 186 ALA CA C 53.356 0.3 1 656 184 186 ALA CB C 19.697 0.3 1 657 184 186 ALA N N 124.137 0.3 1 658 185 187 THR H H 7.807 0.020 1 659 185 187 THR CA C 60.614 0.3 1 660 185 187 THR CB C 72.403 0.3 1 661 185 187 THR N N 114.134 0.3 1 662 186 188 LEU H H 9.031 0.020 1 663 186 188 LEU CA C 53.649 0.3 1 664 186 188 LEU CB C 45.319 0.3 1 665 186 188 LEU N N 125.168 0.3 1 666 187 189 SER H H 8.512 0.020 1 667 187 189 SER CA C 55.938 0.3 1 668 187 189 SER CB C 64.609 0.3 1 669 187 189 SER N N 115.636 0.3 1 670 188 190 ILE H H 9.386 0.020 1 671 188 190 ILE CA C 60.907 0.3 1 672 188 190 ILE CB C 36.161 0.3 1 673 188 190 ILE N N 126.905 0.3 1 674 189 191 CYS H H 8.281 0.020 1 675 189 191 CYS CA C 59.104 0.3 1 676 189 191 CYS CB C 29.829 0.3 1 677 189 191 CYS N N 127.482 0.3 1 678 190 192 SER H H 8.963 0.020 1 679 190 192 SER CA C 56.523 0.3 1 680 190 192 SER CB C 63.342 0.3 1 681 190 192 SER N N 121.000 0.3 1 682 192 194 LYS H H 7.453 0.020 1 683 192 194 LYS CA C 57.448 0.3 1 684 192 194 LYS CB C 33.726 0.3 1 685 192 194 LYS N N 124.830 0.3 1 stop_ save_