data_25356 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Thiopurine methyltransferase *1 15-245 ; _BMRB_accession_number 25356 _BMRB_flat_file_name bmr25356.str _Entry_type original _Submission_date 2014-11-20 _Accession_date 2014-11-20 _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 Lundstrom Patrik . . 2 Niklasson Markus . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 157 "13C chemical shifts" 488 "15N chemical shifts" 157 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-08-19 update BMRB 'update entry citation' 2014-12-19 original author 'original release' stop_ _Original_release_date 2015-08-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Fast and accurate resonance assignment of small-to-large proteins by combining automated and manual approaches ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25569628 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Niklasson Markus . . 2 Ahlner Alexandra . . 3 Andresen Cecilia . . 4 Marsh Joseph . . 5 Lundstrom Patrik . . stop_ _Journal_abbreviation 'PLOS Comput. Biol.' _Journal_volume 11 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e1004022 _Page_last e1004022 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'TPMT *1 16-245' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TPMT *1 16-245' $TPMT_1_16-245 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_TPMT_1_16-245 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TPMT_1_16-245 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 249 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGST EVQKNQVLTLEEWQDKWVNG KTAFHQEQGHQLLKKHLDTF LKGKSGLRVFFPLCGKAVEM KWFADRGHSVVGVEISELGI QEFFTEQNLSYSEEPITEIP GTKVFKSSSGNISLYCCSIF DLPRTNIGKFDMIWDRGALV AINPGDRKCYADTMFSLLGK KFQYLLCVLSYDPTKHPGPP FYVPHAEIERLFGKICNIRC LEKVDAFEERHKSWGIDCLF EKLYLLTEK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 MET 2 -2 GLY 3 -1 SER 4 0 SER 5 1 HIS 6 2 HIS 7 3 HIS 8 4 HIS 9 5 HIS 10 6 HIS 11 7 SER 12 8 SER 13 9 GLY 14 10 LEU 15 11 VAL 16 12 PRO 17 13 ARG 18 14 GLY 19 15 SER 20 16 THR 21 17 GLU 22 18 VAL 23 19 GLN 24 20 LYS 25 21 ASN 26 22 GLN 27 23 VAL 28 24 LEU 29 25 THR 30 26 LEU 31 27 GLU 32 28 GLU 33 29 TRP 34 30 GLN 35 31 ASP 36 32 LYS 37 33 TRP 38 34 VAL 39 35 ASN 40 36 GLY 41 37 LYS 42 38 THR 43 39 ALA 44 40 PHE 45 41 HIS 46 42 GLN 47 43 GLU 48 44 GLN 49 45 GLY 50 46 HIS 51 47 GLN 52 48 LEU 53 49 LEU 54 50 LYS 55 51 LYS 56 52 HIS 57 53 LEU 58 54 ASP 59 55 THR 60 56 PHE 61 57 LEU 62 58 LYS 63 59 GLY 64 60 LYS 65 61 SER 66 62 GLY 67 63 LEU 68 64 ARG 69 65 VAL 70 66 PHE 71 67 PHE 72 68 PRO 73 69 LEU 74 70 CYS 75 71 GLY 76 72 LYS 77 73 ALA 78 74 VAL 79 75 GLU 80 76 MET 81 77 LYS 82 78 TRP 83 79 PHE 84 80 ALA 85 81 ASP 86 82 ARG 87 83 GLY 88 84 HIS 89 85 SER 90 86 VAL 91 87 VAL 92 88 GLY 93 89 VAL 94 90 GLU 95 91 ILE 96 92 SER 97 93 GLU 98 94 LEU 99 95 GLY 100 96 ILE 101 97 GLN 102 98 GLU 103 99 PHE 104 100 PHE 105 101 THR 106 102 GLU 107 103 GLN 108 104 ASN 109 105 LEU 110 106 SER 111 107 TYR 112 108 SER 113 109 GLU 114 110 GLU 115 111 PRO 116 112 ILE 117 113 THR 118 114 GLU 119 115 ILE 120 116 PRO 121 117 GLY 122 118 THR 123 119 LYS 124 120 VAL 125 121 PHE 126 122 LYS 127 123 SER 128 124 SER 129 125 SER 130 126 GLY 131 127 ASN 132 128 ILE 133 129 SER 134 130 LEU 135 131 TYR 136 132 CYS 137 133 CYS 138 134 SER 139 135 ILE 140 136 PHE 141 137 ASP 142 138 LEU 143 139 PRO 144 140 ARG 145 141 THR 146 142 ASN 147 143 ILE 148 144 GLY 149 145 LYS 150 146 PHE 151 147 ASP 152 148 MET 153 149 ILE 154 150 TRP 155 151 ASP 156 152 ARG 157 153 GLY 158 154 ALA 159 155 LEU 160 156 VAL 161 157 ALA 162 158 ILE 163 159 ASN 164 160 PRO 165 161 GLY 166 162 ASP 167 163 ARG 168 164 LYS 169 165 CYS 170 166 TYR 171 167 ALA 172 168 ASP 173 169 THR 174 170 MET 175 171 PHE 176 172 SER 177 173 LEU 178 174 LEU 179 175 GLY 180 176 LYS 181 177 LYS 182 178 PHE 183 179 GLN 184 180 TYR 185 181 LEU 186 182 LEU 187 183 CYS 188 184 VAL 189 185 LEU 190 186 SER 191 187 TYR 192 188 ASP 193 189 PRO 194 190 THR 195 191 LYS 196 192 HIS 197 193 PRO 198 194 GLY 199 195 PRO 200 196 PRO 201 197 PHE 202 198 TYR 203 199 VAL 204 200 PRO 205 201 HIS 206 202 ALA 207 203 GLU 208 204 ILE 209 205 GLU 210 206 ARG 211 207 LEU 212 208 PHE 213 209 GLY 214 210 LYS 215 211 ILE 216 212 CYS 217 213 ASN 218 214 ILE 219 215 ARG 220 216 CYS 221 217 LEU 222 218 GLU 223 219 LYS 224 220 VAL 225 221 ASP 226 222 ALA 227 223 PHE 228 224 GLU 229 225 GLU 230 226 ARG 231 227 HIS 232 228 LYS 233 229 SER 234 230 TRP 235 231 GLY 236 232 ILE 237 233 ASP 238 234 CYS 239 235 LEU 240 236 PHE 241 237 GLU 242 238 LYS 243 239 LEU 244 240 TYR 245 241 LEU 246 242 LEU 247 243 THR 248 244 GLU 249 245 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 2BZG "Crystal Structure Of Thiopurine S-Methyltransferase" 93.17 232 98.71 98.71 4.43e-167 PDB 2H11 "Amino-Terminal Truncated Thiopurine S-Methyltransferase Complexed With S-Adenosyl-L-Homocysteine" 93.17 232 100.00 100.00 1.57e-170 DBJ BAA97037 "thiopurine S-methyltransferase [Homo sapiens]" 92.77 245 99.57 99.57 4.57e-169 DBJ BAJ20858 "thiopurine S-methyltransferase [synthetic construct]" 92.77 245 99.57 99.57 4.57e-169 GB AAB27277 "thiopurine methyltransferase [Homo sapiens]" 92.77 245 99.57 99.57 4.57e-169 GB AAB71625 "thiopurine methyltransferase [Homo sapiens]" 92.77 245 98.70 98.70 9.30e-167 GB AAB71626 "thiopurine methyltransferase [Homo sapiens]" 92.77 245 99.13 99.13 1.72e-168 GB AAB71627 "thiopurine methyltransferase [Homo sapiens]" 92.77 245 99.13 99.13 2.08e-167 GB AAB71629 "thiopurine methyltransferase [Homo sapiens]" 92.37 245 99.57 99.57 3.69e-168 REF NP_000358 "thiopurine S-methyltransferase [Homo sapiens]" 92.77 245 99.57 99.57 4.57e-169 REF NP_001030596 "thiopurine S-methyltransferase [Pan troglodytes]" 92.77 245 98.70 99.13 9.99e-168 REF XP_003823229 "PREDICTED: thiopurine S-methyltransferase isoform X1 [Pan paniscus]" 92.77 245 98.70 99.13 9.99e-168 REF XP_004043361 "PREDICTED: thiopurine S-methyltransferase [Gorilla gorilla gorilla]" 92.77 245 99.13 99.13 2.66e-168 REF XP_008975026 "PREDICTED: thiopurine S-methyltransferase isoform X1 [Pan paniscus]" 92.77 245 98.70 99.13 9.99e-168 SP P51580 "RecName: Full=Thiopurine S-methyltransferase; AltName: Full=Thiopurine methyltransferase" 92.77 245 99.57 99.57 4.57e-169 SP Q3BCR3 "RecName: Full=Thiopurine S-methyltransferase; AltName: Full=Thiopurine methyltransferase" 92.77 245 99.13 99.13 2.66e-168 SP Q3BCR8 "RecName: Full=Thiopurine S-methyltransferase; AltName: Full=Thiopurine methyltransferase" 92.77 245 98.70 99.13 9.99e-168 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TPMT_1_16-245 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 $TPMT_1_16-245 'recombinant technology' . Escherichia coli BL21(DE3) N.A. 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 $TPMT_1_16-245 0.5 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_COMPASS _Saveframe_category software _Name COMPASS _Version . loop_ _Vendor _Address _Electronic_address 'Niklasson, Ahlner, Andresen, Marsh, Lundstrom' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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' 95 . mM pH 7.3 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CB' '3D HN(COCA)CB' '3D HNCO' '3D HN(CA)CO' 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 'TPMT *1 16-245' _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 16 20 THR C C 174.620 0.000 1 2 16 20 THR CB C 69.573 0.000 1 3 17 21 GLU H H 8.332 0.003 1 4 17 21 GLU C C 176.534 0.031 1 5 17 21 GLU CA C 56.685 0.001 1 6 17 21 GLU CB C 30.197 0.055 1 7 17 21 GLU N N 124.278 0.020 1 8 18 22 VAL H H 8.074 0.003 1 9 18 22 VAL C C 176.306 0.022 1 10 18 22 VAL CA C 62.632 0.047 1 11 18 22 VAL CB C 32.524 0.069 1 12 18 22 VAL N N 122.380 0.020 1 13 19 23 GLN H H 8.324 0.011 1 14 19 23 GLN C C 176.076 0.015 1 15 19 23 GLN CA C 55.898 0.056 1 16 19 23 GLN CB C 29.303 0.017 1 17 19 23 GLN N N 124.828 0.141 1 18 20 24 LYS H H 8.285 0.008 1 19 20 24 LYS CA C 56.652 0.000 1 20 20 24 LYS CB C 33.216 0.000 1 21 20 24 LYS N N 123.465 0.132 1 22 21 25 ASN C C 175.293 0.043 1 23 21 25 ASN CA C 52.682 0.000 1 24 21 25 ASN CB C 38.712 0.000 1 25 22 26 GLN H H 7.554 0.006 1 26 22 26 GLN C C 175.494 0.003 1 27 22 26 GLN CA C 56.274 0.033 1 28 22 26 GLN CB C 30.035 0.044 1 29 22 26 GLN N N 121.021 0.091 1 30 23 27 VAL H H 8.196 0.007 1 31 23 27 VAL C C 175.099 0.012 1 32 23 27 VAL CA C 61.599 0.052 1 33 23 27 VAL N N 121.769 0.063 1 34 24 28 LEU H H 8.846 0.006 1 35 24 28 LEU C C 178.179 0.000 1 36 24 28 LEU CA C 55.264 0.108 1 37 24 28 LEU CB C 43.942 0.000 1 38 24 28 LEU N N 128.152 0.055 1 39 25 29 THR H H 8.848 0.010 1 40 25 29 THR C C 175.796 0.050 1 41 25 29 THR CA C 60.439 0.024 1 42 25 29 THR CB C 71.597 0.000 1 43 25 29 THR N N 115.052 0.060 1 44 26 30 LEU H H 8.692 0.003 1 45 26 30 LEU C C 180.251 0.000 1 46 26 30 LEU CA C 58.306 0.022 1 47 26 30 LEU CB C 40.761 0.000 1 48 26 30 LEU N N 120.716 0.036 1 49 27 31 GLU H H 8.642 0.008 1 50 27 31 GLU C C 179.031 0.067 1 51 27 31 GLU CA C 60.462 0.033 1 52 27 31 GLU CB C 28.874 0.023 1 53 27 31 GLU N N 119.598 0.049 1 54 28 32 GLU H H 7.840 0.006 1 55 28 32 GLU C C 180.650 0.000 1 56 28 32 GLU CA C 59.697 0.000 1 57 28 32 GLU CB C 29.700 0.000 1 58 28 32 GLU N N 121.879 0.027 1 59 49 53 LEU C C 178.188 0.013 1 60 49 53 LEU CA C 58.161 0.000 1 61 49 53 LEU CB C 39.839 0.000 1 62 50 54 LYS H H 8.317 0.010 1 63 50 54 LYS C C 178.229 0.000 1 64 50 54 LYS CA C 60.045 0.061 1 65 50 54 LYS CB C 32.707 0.150 1 66 50 54 LYS N N 117.371 0.048 1 67 51 55 LYS H H 7.194 0.009 1 68 51 55 LYS C C 177.629 0.012 1 69 51 55 LYS CA C 58.827 0.044 1 70 51 55 LYS CB C 32.899 0.092 1 71 51 55 LYS N N 117.115 0.041 1 72 52 56 HIS H H 7.241 0.003 1 73 52 56 HIS C C 176.239 0.009 1 74 52 56 HIS CA C 57.481 0.055 1 75 52 56 HIS CB C 33.846 0.115 1 76 52 56 HIS N N 116.130 0.033 1 77 53 57 LEU H H 7.977 0.006 1 78 53 57 LEU C C 177.599 0.026 1 79 53 57 LEU CA C 59.807 0.028 1 80 53 57 LEU CB C 41.673 0.212 1 81 53 57 LEU N N 123.826 0.041 1 82 54 58 ASP H H 8.445 0.004 1 83 54 58 ASP C C 178.956 0.023 1 84 54 58 ASP CA C 57.539 0.059 1 85 54 58 ASP CB C 39.957 0.130 1 86 54 58 ASP N N 115.788 0.025 1 87 55 59 THR H H 7.723 0.006 1 88 55 59 THR C C 176.661 0.013 1 89 55 59 THR CA C 66.042 0.045 1 90 55 59 THR CB C 67.994 0.088 1 91 55 59 THR N N 117.319 0.038 1 92 56 60 PHE H H 7.672 0.006 1 93 56 60 PHE C C 177.241 0.009 1 94 56 60 PHE CA C 59.487 0.035 1 95 56 60 PHE CB C 38.867 0.123 1 96 56 60 PHE N N 119.971 0.043 1 97 57 61 LEU H H 7.762 0.004 1 98 57 61 LEU C C 177.354 0.000 1 99 57 61 LEU CA C 54.706 0.071 1 100 57 61 LEU CB C 42.210 0.084 1 101 57 61 LEU N N 115.211 0.026 1 102 58 62 LYS H H 7.432 0.007 1 103 58 62 LYS C C 178.129 0.000 1 104 58 62 LYS CA C 58.776 0.026 1 105 58 62 LYS CB C 31.944 0.000 1 106 58 62 LYS N N 123.535 0.024 1 107 59 63 GLY C C 174.213 0.000 1 108 59 63 GLY CA C 45.867 0.012 1 109 60 64 LYS H H 7.921 0.005 1 110 60 64 LYS C C 176.245 0.009 1 111 60 64 LYS CA C 54.465 0.052 1 112 60 64 LYS CB C 34.487 0.000 1 113 60 64 LYS N N 119.686 0.020 1 114 61 65 SER H H 8.559 0.006 1 115 61 65 SER C C 174.108 0.000 1 116 61 65 SER CA C 57.151 0.078 1 117 61 65 SER CB C 65.099 0.058 1 118 61 65 SER N N 116.258 0.045 1 119 62 66 GLY H H 8.531 0.008 1 120 62 66 GLY C C 176.007 0.011 1 121 62 66 GLY CA C 47.809 0.089 1 122 62 66 GLY N N 114.613 0.054 1 123 63 67 LEU H H 11.150 0.007 1 124 63 67 LEU C C 176.458 0.023 1 125 63 67 LEU CA C 55.181 0.072 1 126 63 67 LEU CB C 43.181 0.042 1 127 63 67 LEU N N 124.284 0.041 1 128 64 68 ARG H H 9.533 0.009 1 129 64 68 ARG C C 176.321 0.036 1 130 64 68 ARG CA C 56.281 0.014 1 131 64 68 ARG CB C 31.506 0.123 1 132 64 68 ARG N N 122.132 0.025 1 133 65 69 VAL H H 9.511 0.007 1 134 65 69 VAL C C 173.190 0.068 1 135 65 69 VAL CA C 60.851 0.068 1 136 65 69 VAL CB C 34.237 0.031 1 137 65 69 VAL N N 129.458 0.041 1 138 66 70 PHE H H 8.432 0.011 1 139 66 70 PHE C C 173.207 0.000 1 140 66 70 PHE CA C 54.368 0.129 1 141 66 70 PHE CB C 40.656 0.008 1 142 66 70 PHE N N 127.823 0.070 1 143 67 71 PHE H H 8.701 0.005 1 144 67 71 PHE CA C 53.098 0.000 1 145 67 71 PHE N N 128.941 0.064 1 146 72 76 LYS C C 175.895 0.000 1 147 72 76 LYS CA C 51.859 0.000 1 148 73 77 ALA H H 7.835 0.016 1 149 73 77 ALA C C 179.036 0.021 1 150 73 77 ALA CA C 54.351 0.024 1 151 73 77 ALA CB C 18.972 0.000 1 152 73 77 ALA N N 124.846 0.050 1 153 74 78 VAL H H 8.557 0.009 1 154 74 78 VAL C C 178.509 0.000 1 155 74 78 VAL CA C 63.745 0.114 1 156 74 78 VAL N N 120.715 0.053 1 157 75 79 GLU H H 9.275 0.014 1 158 75 79 GLU C C 178.056 0.052 1 159 75 79 GLU CA C 58.367 0.020 1 160 75 79 GLU N N 118.946 0.095 1 161 76 80 MET H H 7.150 0.007 1 162 76 80 MET C C 178.867 0.017 1 163 76 80 MET CA C 60.811 0.078 1 164 76 80 MET CB C 35.501 0.000 1 165 76 80 MET N N 117.665 0.059 1 166 77 81 LYS H H 7.262 0.008 1 167 77 81 LYS C C 177.103 0.015 1 168 77 81 LYS CA C 57.920 0.066 1 169 77 81 LYS CB C 33.857 0.002 1 170 77 81 LYS N N 117.850 0.053 1 171 78 82 TRP H H 7.189 0.008 1 172 78 82 TRP C C 180.141 0.027 1 173 78 82 TRP CA C 57.635 0.109 1 174 78 82 TRP CB C 28.816 0.000 1 175 78 82 TRP N N 118.162 0.026 1 176 79 83 PHE H H 7.374 0.006 1 177 79 83 PHE C C 178.246 0.014 1 178 79 83 PHE CA C 63.037 0.049 1 179 79 83 PHE CB C 40.501 0.042 1 180 79 83 PHE N N 114.213 0.008 1 181 80 84 ALA H H 7.752 0.007 1 182 80 84 ALA C C 181.871 0.006 1 183 80 84 ALA CA C 54.999 0.029 1 184 80 84 ALA CB C 18.527 0.123 1 185 80 84 ALA N N 125.025 0.030 1 186 81 85 ASP H H 8.996 0.006 1 187 81 85 ASP C C 177.772 0.008 1 188 81 85 ASP CA C 56.714 0.087 1 189 81 85 ASP CB C 39.867 0.170 1 190 81 85 ASP N N 119.953 0.034 1 191 82 86 ARG H H 7.106 0.008 1 192 82 86 ARG C C 175.360 0.029 1 193 82 86 ARG CA C 55.566 0.113 1 194 82 86 ARG CB C 30.887 0.032 1 195 82 86 ARG N N 118.114 0.040 1 196 83 87 GLY H H 7.809 0.007 1 197 83 87 GLY C C 173.825 0.017 1 198 83 87 GLY CA C 45.889 0.051 1 199 83 87 GLY N N 107.177 0.031 1 200 84 88 HIS H H 7.317 0.008 1 201 84 88 HIS C C 174.349 0.008 1 202 84 88 HIS CA C 55.549 0.073 1 203 84 88 HIS CB C 32.045 0.086 1 204 84 88 HIS N N 121.539 0.023 1 205 85 89 SER H H 9.176 0.006 1 206 85 89 SER C C 173.186 0.037 1 207 85 89 SER CA C 58.284 0.051 1 208 85 89 SER CB C 64.592 0.068 1 209 85 89 SER N N 117.753 0.025 1 210 86 90 VAL H H 8.980 0.006 1 211 86 90 VAL C C 176.152 0.008 1 212 86 90 VAL CA C 61.656 0.048 1 213 86 90 VAL CB C 35.050 0.040 1 214 86 90 VAL N N 125.966 0.035 1 215 87 91 VAL H H 9.257 0.008 1 216 87 91 VAL C C 173.856 0.010 1 217 87 91 VAL CA C 60.086 0.036 1 218 87 91 VAL N N 131.094 0.029 1 219 88 92 GLY H H 8.840 0.005 1 220 88 92 GLY C C 171.780 0.000 1 221 88 92 GLY CA C 43.806 0.135 1 222 88 92 GLY N N 113.920 0.027 1 223 89 93 VAL H H 7.002 0.009 1 224 89 93 VAL C C 172.034 0.012 1 225 89 93 VAL CA C 59.078 0.127 1 226 89 93 VAL CB C 35.592 0.048 1 227 89 93 VAL N N 118.577 0.051 1 228 90 94 GLU H H 8.804 0.006 1 229 90 94 GLU C C 173.257 0.009 1 230 90 94 GLU CA C 55.017 0.026 1 231 90 94 GLU N N 133.289 0.048 1 232 91 95 ILE H H 7.178 0.011 1 233 91 95 ILE C C 174.552 0.000 1 234 91 95 ILE CA C 59.452 0.088 1 235 91 95 ILE N N 126.392 0.061 1 236 92 96 SER H H 9.245 0.008 1 237 92 96 SER C C 174.610 0.000 1 238 92 96 SER CA C 57.232 0.025 1 239 92 96 SER CB C 63.887 0.031 1 240 92 96 SER N N 123.274 0.075 1 241 93 97 GLU H H 8.595 0.009 1 242 93 97 GLU C C 177.394 0.014 1 243 93 97 GLU CA C 59.313 0.084 1 244 93 97 GLU CB C 29.864 0.089 1 245 93 97 GLU N N 132.532 0.059 1 246 94 98 LEU H H 7.012 0.012 1 247 94 98 LEU C C 178.580 0.020 1 248 94 98 LEU CA C 57.370 0.054 1 249 94 98 LEU CB C 42.014 0.009 1 250 94 98 LEU N N 119.866 0.057 1 251 95 99 GLY H H 7.135 0.009 1 252 95 99 GLY C C 173.937 0.000 1 253 95 99 GLY CA C 46.461 0.020 1 254 95 99 GLY N N 107.652 0.059 1 255 96 100 ILE H H 6.553 0.006 1 256 96 100 ILE C C 178.391 0.000 1 257 96 100 ILE CA C 65.479 0.160 1 258 96 100 ILE N N 119.641 0.060 1 259 97 101 GLN H H 7.877 0.011 1 260 97 101 GLN C C 179.613 0.125 1 261 97 101 GLN CA C 59.874 0.094 1 262 97 101 GLN CB C 29.258 0.000 1 263 97 101 GLN N N 118.563 0.025 1 264 98 102 GLU H H 8.391 0.008 1 265 98 102 GLU C C 177.866 0.021 1 266 98 102 GLU CA C 60.372 0.080 1 267 98 102 GLU CB C 29.993 0.055 1 268 98 102 GLU N N 121.542 0.187 1 269 99 103 PHE H H 7.733 0.009 1 270 99 103 PHE C C 176.650 0.016 1 271 99 103 PHE CA C 61.545 0.056 1 272 99 103 PHE CB C 37.252 0.000 1 273 99 103 PHE N N 120.738 0.053 1 274 100 104 PHE H H 7.287 0.008 1 275 100 104 PHE C C 178.346 0.005 1 276 100 104 PHE CA C 63.666 0.057 1 277 100 104 PHE CB C 38.564 0.046 1 278 100 104 PHE N N 116.504 0.055 1 279 101 105 THR H H 8.221 0.007 1 280 101 105 THR C C 178.383 0.000 1 281 101 105 THR CA C 66.585 0.027 1 282 101 105 THR CB C 68.808 0.111 1 283 101 105 THR N N 115.022 0.089 1 284 102 106 GLU H H 9.027 0.008 1 285 102 106 GLU C C 178.840 0.015 1 286 102 106 GLU CA C 59.572 0.080 1 287 102 106 GLU CB C 29.068 0.000 1 288 102 106 GLU N N 124.095 0.025 1 289 103 107 GLN H H 7.682 0.006 1 290 103 107 GLN C C 174.784 0.020 1 291 103 107 GLN CA C 53.557 0.073 1 292 103 107 GLN CB C 26.950 0.022 1 293 103 107 GLN N N 113.950 0.033 1 294 104 108 ASN H H 7.629 0.005 1 295 104 108 ASN C C 173.824 0.044 1 296 104 108 ASN CA C 54.014 0.043 1 297 104 108 ASN CB C 37.169 0.051 1 298 104 108 ASN N N 117.601 0.020 1 299 105 109 LEU H H 8.420 0.007 1 300 105 109 LEU C C 176.589 0.009 1 301 105 109 LEU CA C 53.344 0.040 1 302 105 109 LEU CB C 46.514 0.107 1 303 105 109 LEU N N 119.458 0.039 1 304 106 110 SER H H 8.323 0.007 1 305 106 110 SER C C 173.594 0.028 1 306 106 110 SER CA C 57.918 0.073 1 307 106 110 SER CB C 64.031 0.056 1 308 106 110 SER N N 118.717 0.051 1 309 107 111 TYR H H 7.824 0.002 1 310 107 111 TYR C C 173.976 0.003 1 311 107 111 TYR CA C 55.877 0.036 1 312 107 111 TYR CB C 40.430 0.133 1 313 107 111 TYR N N 118.224 0.022 1 314 108 112 SER H H 8.803 0.007 1 315 108 112 SER C C 172.513 0.007 1 316 108 112 SER CA C 56.398 0.055 1 317 108 112 SER CB C 66.231 0.028 1 318 108 112 SER N N 115.215 0.039 1 319 109 113 GLU H H 8.422 0.003 1 320 109 113 GLU C C 175.428 0.017 1 321 109 113 GLU CA C 54.235 0.042 1 322 109 113 GLU CB C 33.317 0.048 1 323 109 113 GLU N N 121.419 0.036 1 324 110 114 GLU H H 8.517 0.007 1 325 110 114 GLU C C 172.544 0.000 1 326 110 114 GLU CA C 53.175 0.008 1 327 110 114 GLU CB C 32.564 0.000 1 328 110 114 GLU N N 122.688 0.029 1 329 111 115 PRO C C 176.957 0.031 1 330 111 115 PRO CA C 62.622 0.017 1 331 111 115 PRO CB C 32.791 0.000 1 332 112 116 ILE H H 7.497 0.009 1 333 112 116 ILE C C 177.577 0.025 1 334 112 116 ILE CA C 60.723 0.074 1 335 112 116 ILE CB C 36.023 0.001 1 336 112 116 ILE N N 123.131 0.029 1 337 113 117 THR H H 8.624 0.003 1 338 113 117 THR C C 176.603 0.000 1 339 113 117 THR CA C 66.303 0.078 1 340 113 117 THR CB C 68.257 0.009 1 341 113 117 THR N N 124.622 0.047 1 342 114 118 GLU H H 9.115 0.007 1 343 114 118 GLU C C 175.740 0.015 1 344 114 118 GLU CA C 58.984 0.063 1 345 114 118 GLU CB C 30.072 0.162 1 346 114 118 GLU N N 117.678 0.045 1 347 115 119 ILE H H 6.914 0.006 1 348 115 119 ILE C C 171.933 0.000 1 349 115 119 ILE CA C 58.342 0.000 1 350 115 119 ILE CB C 37.709 0.000 1 351 115 119 ILE N N 116.815 0.033 1 352 116 120 PRO C C 177.618 0.000 1 353 116 120 PRO CA C 64.737 0.000 1 354 117 121 GLY H H 8.563 0.006 1 355 117 121 GLY C C 174.722 0.000 1 356 117 121 GLY CA C 45.377 0.037 1 357 117 121 GLY N N 112.493 0.021 1 358 118 122 THR H H 7.742 0.008 1 359 118 122 THR C C 175.337 0.024 1 360 118 122 THR CA C 61.714 0.085 1 361 118 122 THR CB C 70.984 0.157 1 362 118 122 THR N N 111.999 0.053 1 363 119 123 LYS H H 7.722 0.004 1 364 119 123 LYS C C 173.005 0.006 1 365 119 123 LYS CA C 55.363 0.035 1 366 119 123 LYS CB C 37.506 0.033 1 367 119 123 LYS N N 119.316 0.042 1 368 120 124 VAL H H 8.944 0.007 1 369 120 124 VAL C C 172.235 0.030 1 370 120 124 VAL CA C 58.526 0.053 1 371 120 124 VAL CB C 35.119 0.147 1 372 120 124 VAL N N 119.133 0.042 1 373 121 125 PHE H H 8.883 0.008 1 374 121 125 PHE C C 175.211 0.049 1 375 121 125 PHE CA C 55.920 0.094 1 376 121 125 PHE CB C 41.878 0.095 1 377 121 125 PHE N N 128.185 0.038 1 378 122 126 LYS H H 8.689 0.010 1 379 122 126 LYS C C 176.942 0.069 1 380 122 126 LYS CA C 54.435 0.049 1 381 122 126 LYS CB C 36.036 0.000 1 382 122 126 LYS N N 122.896 0.031 1 383 123 127 SER H H 9.106 0.005 1 384 123 127 SER CA C 57.979 0.000 1 385 123 127 SER N N 118.739 0.115 1 386 125 129 SER C C 175.759 0.000 1 387 125 129 SER CA C 58.718 0.010 1 388 125 129 SER CB C 64.098 0.000 1 389 126 130 GLY H H 8.058 0.009 1 390 126 130 GLY C C 173.942 0.000 1 391 126 130 GLY CA C 45.579 0.052 1 392 126 130 GLY N N 111.329 0.038 1 393 127 131 ASN H H 7.859 0.008 1 394 127 131 ASN C C 173.493 0.020 1 395 127 131 ASN CA C 53.815 0.075 1 396 127 131 ASN CB C 38.273 0.004 1 397 127 131 ASN N N 116.991 0.019 1 398 128 132 ILE H H 7.459 0.007 1 399 128 132 ILE C C 175.596 0.000 1 400 128 132 ILE CA C 61.679 0.066 1 401 128 132 ILE CB C 42.739 0.000 1 402 128 132 ILE N N 119.304 0.037 1 403 129 133 SER H H 8.505 0.002 1 404 129 133 SER C C 171.908 0.006 1 405 129 133 SER CA C 57.464 0.049 1 406 129 133 SER CB C 65.695 0.000 1 407 129 133 SER N N 124.078 0.153 1 408 130 134 LEU H H 9.627 0.005 1 409 130 134 LEU C C 175.114 0.000 1 410 130 134 LEU CA C 53.117 0.097 1 411 130 134 LEU CB C 42.337 0.127 1 412 130 134 LEU N N 125.241 0.009 1 413 131 135 TYR H H 9.303 0.009 1 414 131 135 TYR C C 173.641 0.014 1 415 131 135 TYR CA C 59.446 0.062 1 416 131 135 TYR CB C 39.511 0.000 1 417 131 135 TYR N N 127.568 0.016 1 418 132 136 CYS H H 9.059 0.008 1 419 132 136 CYS C C 173.866 0.000 1 420 132 136 CYS CA C 56.059 0.043 1 421 132 136 CYS CB C 26.305 0.000 1 422 132 136 CYS N N 128.526 0.023 1 423 133 137 CYS H H 7.561 0.009 1 424 133 137 CYS C C 170.798 0.000 1 425 133 137 CYS CA C 55.520 0.047 1 426 133 137 CYS CB C 28.869 0.048 1 427 133 137 CYS N N 119.787 0.048 1 428 134 138 SER H H 9.115 0.005 1 429 134 138 SER C C 179.822 0.000 1 430 134 138 SER CA C 55.203 0.051 1 431 134 138 SER CB C 63.922 0.030 1 432 134 138 SER N N 110.772 0.023 1 433 135 139 ILE H H 10.200 0.008 1 434 135 139 ILE C C 174.304 0.000 1 435 135 139 ILE CA C 63.781 0.069 1 436 135 139 ILE CB C 37.622 0.000 1 437 135 139 ILE N N 131.668 0.034 1 438 136 140 PHE H H 7.136 0.007 1 439 136 140 PHE C C 176.476 0.032 1 440 136 140 PHE CA C 59.756 0.042 1 441 136 140 PHE CB C 37.936 0.125 1 442 136 140 PHE N N 116.650 0.029 1 443 137 141 ASP H H 7.624 0.012 1 444 137 141 ASP C C 175.763 0.040 1 445 137 141 ASP CA C 54.969 0.052 1 446 137 141 ASP CB C 42.823 0.021 1 447 137 141 ASP N N 117.108 0.062 1 448 138 142 LEU H H 7.073 0.009 1 449 138 142 LEU C C 174.370 0.000 1 450 138 142 LEU CA C 58.495 0.000 1 451 138 142 LEU CB C 41.000 0.000 1 452 138 142 LEU N N 120.874 0.044 1 453 139 143 PRO C C 176.776 0.000 1 454 139 143 PRO CA C 65.077 0.000 1 455 140 144 ARG H H 7.781 0.008 1 456 140 144 ARG C C 177.126 0.000 1 457 140 144 ARG CA C 57.605 0.062 1 458 140 144 ARG CB C 31.103 0.150 1 459 140 144 ARG N N 115.182 0.028 1 460 141 145 THR H H 7.873 0.007 1 461 141 145 THR C C 172.982 0.009 1 462 141 145 THR CA C 59.980 0.081 1 463 141 145 THR CB C 70.959 0.006 1 464 141 145 THR N N 111.770 0.042 1 465 142 146 ASN H H 7.958 0.008 1 466 142 146 ASN C C 175.757 0.006 1 467 142 146 ASN CA C 52.692 0.107 1 468 142 146 ASN CB C 37.564 0.070 1 469 142 146 ASN N N 120.289 0.085 1 470 143 147 ILE H H 7.850 0.005 1 471 143 147 ILE C C 175.223 0.039 1 472 143 147 ILE CA C 60.315 0.130 1 473 143 147 ILE CB C 39.510 0.140 1 474 143 147 ILE N N 121.071 0.033 1 475 144 148 GLY H H 8.045 0.004 1 476 144 148 GLY C C 172.080 0.033 1 477 144 148 GLY CA C 45.191 0.082 1 478 144 148 GLY N N 111.107 0.057 1 479 145 149 LYS H H 7.783 0.005 1 480 145 149 LYS C C 177.803 0.010 1 481 145 149 LYS CA C 53.111 0.106 1 482 145 149 LYS CB C 35.798 0.158 1 483 145 149 LYS N N 116.673 0.071 1 484 146 150 PHE H H 8.451 0.009 1 485 146 150 PHE C C 174.364 0.000 1 486 146 150 PHE CA C 59.177 0.029 1 487 146 150 PHE CB C 41.884 0.139 1 488 146 150 PHE N N 118.610 0.017 1 489 147 151 ASP H H 8.777 0.008 1 490 147 151 ASP C C 176.571 0.000 1 491 147 151 ASP CA C 55.984 0.026 1 492 147 151 ASP CB C 45.514 0.000 1 493 147 151 ASP N N 119.343 0.007 1 494 148 152 MET H H 7.981 0.007 1 495 148 152 MET C C 172.663 0.004 1 496 148 152 MET CA C 53.781 0.056 1 497 148 152 MET CB C 37.529 0.090 1 498 148 152 MET N N 118.523 0.059 1 499 149 153 ILE H H 8.138 0.009 1 500 149 153 ILE C C 174.273 0.013 1 501 149 153 ILE CA C 58.180 0.097 1 502 149 153 ILE CB C 41.107 0.000 1 503 149 153 ILE N N 125.637 0.070 1 504 150 154 TRP H H 7.608 0.006 1 505 150 154 TRP C C 172.153 0.015 1 506 150 154 TRP CA C 55.233 0.147 1 507 150 154 TRP CB C 30.241 0.052 1 508 150 154 TRP N N 126.433 0.061 1 509 151 155 ASP H H 8.231 0.005 1 510 151 155 ASP CA C 52.098 0.067 1 511 151 155 ASP CB C 45.214 0.000 1 512 151 155 ASP N N 130.741 0.040 1 513 156 160 VAL C C 173.659 0.000 1 514 156 160 VAL CA C 62.533 0.034 1 515 157 161 ALA H H 8.024 0.007 1 516 157 161 ALA C C 176.504 0.020 1 517 157 161 ALA CA C 52.836 0.197 1 518 157 161 ALA CB C 19.008 0.000 1 519 157 161 ALA N N 125.602 0.047 1 520 158 162 ILE H H 10.251 0.003 1 521 158 162 ILE C C 179.053 0.000 1 522 158 162 ILE N N 126.646 0.078 1 523 160 164 PRO C C 178.346 0.000 1 524 160 164 PRO CA C 56.379 0.000 1 525 160 164 PRO CB C 38.498 0.000 1 526 161 165 GLY H H 8.215 0.003 1 527 161 165 GLY CA C 45.349 0.051 1 528 161 165 GLY N N 115.031 0.073 1 529 162 166 ASP H H 7.945 0.005 1 530 162 166 ASP C C 175.772 0.000 1 531 162 166 ASP CA C 55.125 0.028 1 532 162 166 ASP CB C 42.522 0.011 1 533 162 166 ASP N N 122.288 0.003 1 534 163 167 ARG H H 7.990 0.004 1 535 163 167 ARG CA C 59.776 0.054 1 536 163 167 ARG CB C 32.640 0.000 1 537 163 167 ARG N N 123.221 0.049 1 538 164 168 LYS C C 177.499 0.006 1 539 164 168 LYS CA C 59.913 0.064 1 540 164 168 LYS CB C 31.221 0.000 1 541 165 169 CYS H H 7.959 0.003 1 542 165 169 CYS C C 178.752 0.012 1 543 165 169 CYS CA C 62.131 0.042 1 544 165 169 CYS CB C 26.339 0.081 1 545 165 169 CYS N N 120.043 0.079 1 546 166 170 TYR H H 8.716 0.008 1 547 166 170 TYR C C 175.888 0.029 1 548 166 170 TYR CA C 62.767 0.088 1 549 166 170 TYR CB C 38.903 0.266 1 550 166 170 TYR N N 124.186 0.072 1 551 167 171 ALA H H 8.495 0.005 1 552 167 171 ALA C C 177.517 0.012 1 553 167 171 ALA CA C 55.898 0.038 1 554 167 171 ALA CB C 17.966 0.000 1 555 167 171 ALA N N 124.460 0.037 1 556 168 172 ASP H H 8.192 0.005 1 557 168 172 ASP C C 180.079 0.004 1 558 168 172 ASP CA C 57.548 0.070 1 559 168 172 ASP CB C 40.100 0.026 1 560 168 172 ASP N N 116.748 0.028 1 561 169 173 THR H H 8.076 0.005 1 562 169 173 THR C C 176.748 0.000 1 563 169 173 THR CA C 67.651 0.097 1 564 169 173 THR N N 119.563 0.038 1 565 170 174 MET H H 8.289 0.007 1 566 170 174 MET C C 179.439 0.033 1 567 170 174 MET CA C 56.655 0.037 1 568 170 174 MET CB C 29.479 0.033 1 569 170 174 MET N N 122.765 0.038 1 570 171 175 PHE H H 8.426 0.006 1 571 171 175 PHE C C 179.231 0.023 1 572 171 175 PHE CA C 59.677 0.043 1 573 171 175 PHE CB C 37.678 0.065 1 574 171 175 PHE N N 117.432 0.044 1 575 172 176 SER H H 7.460 0.010 1 576 172 176 SER C C 173.897 0.025 1 577 172 176 SER CA C 60.930 0.065 1 578 172 176 SER CB C 63.486 0.052 1 579 172 176 SER N N 115.161 0.024 1 580 173 177 LEU H H 7.460 0.005 1 581 173 177 LEU C C 176.148 0.025 1 582 173 177 LEU CA C 54.584 0.026 1 583 173 177 LEU CB C 42.285 0.057 1 584 173 177 LEU N N 121.186 0.063 1 585 174 178 LEU H H 6.901 0.008 1 586 174 178 LEU C C 178.020 0.023 1 587 174 178 LEU CA C 55.230 0.082 1 588 174 178 LEU CB C 42.346 0.084 1 589 174 178 LEU N N 120.257 0.031 1 590 175 179 GLY H H 8.459 0.006 1 591 175 179 GLY C C 172.639 0.044 1 592 175 179 GLY CA C 43.912 0.050 1 593 175 179 GLY N N 110.228 0.056 1 594 176 180 LYS H H 8.143 0.004 1 595 176 180 LYS C C 177.508 0.009 1 596 176 180 LYS CA C 58.247 0.018 1 597 176 180 LYS CB C 32.736 0.073 1 598 176 180 LYS N N 118.944 0.036 1 599 177 181 LYS H H 8.036 0.009 1 600 177 181 LYS C C 175.909 0.000 1 601 177 181 LYS CA C 55.316 0.024 1 602 177 181 LYS CB C 32.940 0.000 1 603 177 181 LYS N N 116.938 0.067 1 604 178 182 PHE H H 7.659 0.003 1 605 178 182 PHE C C 174.419 0.041 1 606 178 182 PHE CA C 56.529 0.088 1 607 178 182 PHE CB C 40.854 0.094 1 608 178 182 PHE N N 117.672 0.093 1 609 179 183 GLN H H 7.886 0.009 1 610 179 183 GLN C C 172.695 0.028 1 611 179 183 GLN CA C 55.653 0.101 1 612 179 183 GLN CB C 32.431 0.050 1 613 179 183 GLN N N 116.458 0.037 1 614 180 184 TYR H H 9.658 0.013 1 615 180 184 TYR C C 173.638 0.000 1 616 180 184 TYR CA C 54.843 0.047 1 617 180 184 TYR CB C 39.608 0.140 1 618 180 184 TYR N N 129.878 0.041 1 619 181 185 LEU H H 8.975 0.009 1 620 181 185 LEU C C 173.150 0.000 1 621 181 185 LEU CA C 54.124 0.028 1 622 181 185 LEU CB C 42.861 0.018 1 623 181 185 LEU N N 131.205 0.039 1 624 182 186 LEU H H 8.802 0.006 1 625 182 186 LEU CA C 53.177 0.000 1 626 182 186 LEU CB C 46.067 0.000 1 627 182 186 LEU N N 126.823 0.011 1 628 183 187 CYS C C 175.694 0.000 1 629 183 187 CYS CA C 56.067 0.039 1 630 183 187 CYS CB C 29.446 0.000 1 631 184 188 VAL H H 8.100 0.004 1 632 184 188 VAL C C 175.971 0.014 1 633 184 188 VAL CA C 62.485 0.021 1 634 184 188 VAL CB C 32.472 0.031 1 635 184 188 VAL N N 122.622 0.091 1 636 185 189 LEU H H 8.246 0.008 1 637 185 189 LEU C C 177.383 0.000 1 638 185 189 LEU CA C 55.127 0.000 1 639 185 189 LEU CB C 42.536 0.000 1 640 185 189 LEU N N 126.892 0.097 1 641 186 190 SER C C 172.695 0.000 1 642 186 190 SER CA C 58.459 0.096 1 643 186 190 SER CB C 64.139 0.000 1 644 187 191 TYR H H 6.893 0.009 1 645 187 191 TYR C C 172.004 0.000 1 646 187 191 TYR CA C 55.767 0.056 1 647 187 191 TYR CB C 39.432 0.000 1 648 187 191 TYR N N 122.460 0.048 1 649 190 194 THR C C 176.170 0.000 1 650 190 194 THR CA C 63.568 0.107 1 651 191 195 LYS H H 7.632 0.005 1 652 191 195 LYS C C 175.050 0.000 1 653 191 195 LYS CA C 55.997 0.000 1 654 191 195 LYS CB C 34.566 0.000 1 655 191 195 LYS N N 120.498 0.043 1 656 201 205 HIS C C 177.256 0.000 1 657 201 205 HIS CA C 61.503 0.000 1 658 202 206 ALA H H 8.773 0.016 1 659 202 206 ALA C C 180.462 0.000 1 660 202 206 ALA CA C 54.893 0.029 1 661 202 206 ALA CB C 18.443 0.000 1 662 202 206 ALA N N 117.585 0.060 1 663 203 207 GLU H H 7.256 0.005 1 664 203 207 GLU C C 177.567 0.021 1 665 203 207 GLU CA C 57.519 0.146 1 666 203 207 GLU CB C 29.406 0.000 1 667 203 207 GLU N N 119.569 0.128 1 668 204 208 ILE H H 7.294 0.005 1 669 204 208 ILE C C 178.333 0.000 1 670 204 208 ILE CA C 65.724 0.034 1 671 204 208 ILE CB C 37.094 0.000 1 672 204 208 ILE N N 122.346 0.068 1 673 205 209 GLU H H 7.811 0.007 1 674 205 209 GLU C C 180.663 0.000 1 675 205 209 GLU CA C 59.965 0.122 1 676 205 209 GLU CB C 29.457 0.142 1 677 205 209 GLU N N 118.418 0.046 1 678 206 210 ARG H H 7.762 0.006 1 679 206 210 ARG C C 178.706 0.045 1 680 206 210 ARG CA C 59.862 0.015 1 681 206 210 ARG CB C 31.011 0.110 1 682 206 210 ARG N N 121.757 0.059 1 683 207 211 LEU H H 8.060 0.007 1 684 207 211 LEU C C 178.623 0.000 1 685 207 211 LEU CA C 56.722 0.128 1 686 207 211 LEU CB C 43.540 0.000 1 687 207 211 LEU N N 117.775 0.104 1 688 208 212 PHE H H 8.210 0.015 1 689 208 212 PHE C C 177.715 0.010 1 690 208 212 PHE CA C 58.775 0.039 1 691 208 212 PHE CB C 40.870 0.000 1 692 208 212 PHE N N 112.462 0.111 1 693 209 213 GLY H H 8.404 0.008 1 694 209 213 GLY C C 174.343 0.000 1 695 209 213 GLY CA C 47.416 0.055 1 696 209 213 GLY N N 109.951 0.048 1 697 210 214 LYS C C 177.815 0.000 1 698 210 214 LYS CA C 58.447 0.049 1 699 210 214 LYS CB C 32.314 0.000 1 700 211 215 ILE H H 6.897 0.006 1 701 211 215 ILE C C 175.409 0.000 1 702 211 215 ILE CA C 60.336 0.055 1 703 211 215 ILE CB C 39.912 0.075 1 704 211 215 ILE N N 113.832 0.049 1 705 212 216 CYS H H 8.058 0.005 1 706 212 216 CYS C C 175.620 0.011 1 707 212 216 CYS CA C 57.419 0.052 1 708 212 216 CYS CB C 30.589 0.094 1 709 212 216 CYS N N 117.095 0.062 1 710 213 217 ASN H H 8.946 0.009 1 711 213 217 ASN C C 175.123 0.030 1 712 213 217 ASN CA C 53.424 0.097 1 713 213 217 ASN CB C 39.689 0.004 1 714 213 217 ASN N N 121.711 0.068 1 715 214 218 ILE H H 8.609 0.005 1 716 214 218 ILE C C 175.143 0.000 1 717 214 218 ILE CA C 61.743 0.122 1 718 214 218 ILE CB C 40.839 0.082 1 719 214 218 ILE N N 124.337 0.022 1 720 215 219 ARG H H 8.382 0.009 1 721 215 219 ARG C C 173.936 0.000 1 722 215 219 ARG CA C 54.715 0.085 1 723 215 219 ARG CB C 34.268 0.000 1 724 215 219 ARG N N 127.837 0.056 1 725 216 220 CYS C C 174.721 0.000 1 726 216 220 CYS CA C 59.117 0.119 1 727 216 220 CYS CB C 26.431 0.000 1 728 217 221 LEU H H 9.461 0.013 1 729 217 221 LEU C C 177.452 0.000 1 730 217 221 LEU CA C 56.681 0.008 1 731 217 221 LEU CB C 43.783 0.000 1 732 217 221 LEU N N 131.425 0.053 1 733 218 222 GLU H H 7.399 0.007 1 734 218 222 GLU C C 173.221 0.010 1 735 218 222 GLU CA C 55.807 0.086 1 736 218 222 GLU CB C 34.544 0.008 1 737 218 222 GLU N N 116.127 0.045 1 738 219 223 LYS H H 8.448 0.007 1 739 219 223 LYS C C 175.275 0.022 1 740 219 223 LYS CA C 55.432 0.094 1 741 219 223 LYS CB C 35.198 0.000 1 742 219 223 LYS N N 124.432 0.055 1 743 220 224 VAL H H 9.338 0.010 1 744 220 224 VAL C C 174.660 0.000 1 745 220 224 VAL CA C 59.189 0.052 1 746 220 224 VAL N N 121.692 0.060 1 747 221 225 ASP H H 8.692 0.005 1 748 221 225 ASP CA C 55.048 0.173 1 749 221 225 ASP CB C 40.443 0.000 1 750 221 225 ASP N N 124.693 0.047 1 751 222 226 ALA H H 7.217 0.008 1 752 222 226 ALA CB C 19.478 0.000 1 753 222 226 ALA N N 119.353 0.063 1 754 228 232 LYS C C 177.041 0.023 1 755 228 232 LYS CA C 54.382 0.066 1 756 228 232 LYS CB C 35.671 0.000 1 757 229 233 SER H H 9.176 0.006 1 758 229 233 SER C C 176.899 0.000 1 759 229 233 SER CA C 58.170 0.103 1 760 229 233 SER CB C 64.492 0.001 1 761 229 233 SER N N 119.132 0.033 1 762 230 234 TRP H H 8.913 0.003 1 763 230 234 TRP CA C 61.346 0.000 1 764 230 234 TRP N N 122.311 0.024 1 765 238 242 LYS C C 174.327 0.027 1 766 238 242 LYS CA C 54.623 0.028 1 767 238 242 LYS CB C 36.281 0.000 1 768 239 243 LEU H H 8.224 0.008 1 769 239 243 LEU C C 174.440 0.000 1 770 239 243 LEU CA C 53.245 0.041 1 771 239 243 LEU CB C 44.698 0.011 1 772 239 243 LEU N N 123.672 0.039 1 773 240 244 TYR H H 10.203 0.008 1 774 240 244 TYR C C 173.717 0.000 1 775 240 244 TYR CA C 57.210 0.046 1 776 240 244 TYR CB C 42.286 0.000 1 777 240 244 TYR N N 128.044 0.048 1 778 241 245 LEU H H 9.138 0.012 1 779 241 245 LEU C C 174.710 0.000 1 780 241 245 LEU CA C 53.748 0.061 1 781 241 245 LEU CB C 45.290 0.107 1 782 241 245 LEU N N 120.886 0.039 1 783 242 246 LEU H H 9.896 0.006 1 784 242 246 LEU C C 175.746 0.140 1 785 242 246 LEU CA C 54.053 0.064 1 786 242 246 LEU CB C 42.650 0.000 1 787 242 246 LEU N N 134.694 0.045 1 788 243 247 THR H H 8.201 0.006 1 789 243 247 THR C C 173.572 0.007 1 790 243 247 THR CA C 59.340 0.066 1 791 243 247 THR CB C 72.865 0.079 1 792 243 247 THR N N 112.680 0.047 1 793 244 248 GLU H H 8.378 0.005 1 794 244 248 GLU C C 175.635 0.011 1 795 244 248 GLU CA C 57.431 0.039 1 796 244 248 GLU CB C 28.911 0.026 1 797 244 248 GLU N N 122.528 0.042 1 798 245 249 LYS H H 7.668 0.004 1 799 245 249 LYS C C 182.067 0.000 1 800 245 249 LYS CA C 58.561 0.004 1 801 245 249 LYS CB C 33.997 0.000 1 802 245 249 LYS N N 127.875 0.021 1 stop_ save_