data_27599 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shifts for super-stable p53 DNA-Binding Domain C5xS ; _BMRB_accession_number 27599 _BMRB_flat_file_name bmr27599.str _Entry_type original _Submission_date 2018-09-05 _Accession_date 2018-09-05 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Backbone chemical shift assignments for residues 88-312 of p53 (the DNA-binding domain) with mutations C124S/C182S/C229S/C275S/C277S and M133L/V203A/N239Y/N268D. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Krois Alexander S. . 2 Dyson Jane H. . 3 Wright Peter E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 176 "13C chemical shifts" 375 "15N chemical shifts" 176 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-11-25 update author 'update sample condition' 2019-01-04 update BMRB 'update entry citation' 2018-11-07 original author 'original release' stop_ _Original_release_date 2018-09-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30420502 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Krois Alexander S. . 2 Dyson Jane H. . 3 Wright Peter E. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 115 _Journal_issue 48 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first E11302 _Page_last E11310 _Year 2018 _Details . loop_ _Keyword idp intein p53 stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name p53(DBD) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label p53(DBD) $p53(DBD)_super-stable_C5xS stop_ _System_molecular_weight 26000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_p53(DBD)_super-stable_C5xS _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common p53(DBD)_super-stable_C5xS _Molecular_mass . _Mol_thiol_state 'free and other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 228 _Mol_residue_sequence ; GSHAPSWPLSSSVPSQKTYQ GSYGFRLGFLHSGTAKSVTS TYSPALNKLFCQLAKTCPVQ LWVDSTPPPGTRVRAMAIYK QSQHMTEVVRRCPHHERSSD SDGLAPPQHLIRVEGNLRAE YLDDRNTFRHSVVVPYEPPE VGSDSTTIHYNYMCYSSCMG GMNRRPILTIITLEDSSGNL LGRDSFEVRVSASPGRDRRT EEENLRKKGEPHHELPPGST KRALPNNT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 85 GLY 2 86 SER 3 87 HIS 4 88 ALA 5 89 PRO 6 90 SER 7 91 TRP 8 92 PRO 9 93 LEU 10 94 SER 11 95 SER 12 96 SER 13 97 VAL 14 98 PRO 15 99 SER 16 100 GLN 17 101 LYS 18 102 THR 19 103 TYR 20 104 GLN 21 105 GLY 22 106 SER 23 107 TYR 24 108 GLY 25 109 PHE 26 110 ARG 27 111 LEU 28 112 GLY 29 113 PHE 30 114 LEU 31 115 HIS 32 116 SER 33 117 GLY 34 118 THR 35 119 ALA 36 120 LYS 37 121 SER 38 122 VAL 39 123 THR 40 124 SER 41 125 THR 42 126 TYR 43 127 SER 44 128 PRO 45 129 ALA 46 130 LEU 47 131 ASN 48 132 LYS 49 133 LEU 50 134 PHE 51 135 CYS 52 136 GLN 53 137 LEU 54 138 ALA 55 139 LYS 56 140 THR 57 141 CYS 58 142 PRO 59 143 VAL 60 144 GLN 61 145 LEU 62 146 TRP 63 147 VAL 64 148 ASP 65 149 SER 66 150 THR 67 151 PRO 68 152 PRO 69 153 PRO 70 154 GLY 71 155 THR 72 156 ARG 73 157 VAL 74 158 ARG 75 159 ALA 76 160 MET 77 161 ALA 78 162 ILE 79 163 TYR 80 164 LYS 81 165 GLN 82 166 SER 83 167 GLN 84 168 HIS 85 169 MET 86 170 THR 87 171 GLU 88 172 VAL 89 173 VAL 90 174 ARG 91 175 ARG 92 176 CYS 93 177 PRO 94 178 HIS 95 179 HIS 96 180 GLU 97 181 ARG 98 182 SER 99 183 SER 100 184 ASP 101 185 SER 102 186 ASP 103 187 GLY 104 188 LEU 105 189 ALA 106 190 PRO 107 191 PRO 108 192 GLN 109 193 HIS 110 194 LEU 111 195 ILE 112 196 ARG 113 197 VAL 114 198 GLU 115 199 GLY 116 200 ASN 117 201 LEU 118 202 ARG 119 203 ALA 120 204 GLU 121 205 TYR 122 206 LEU 123 207 ASP 124 208 ASP 125 209 ARG 126 210 ASN 127 211 THR 128 212 PHE 129 213 ARG 130 214 HIS 131 215 SER 132 216 VAL 133 217 VAL 134 218 VAL 135 219 PRO 136 220 TYR 137 221 GLU 138 222 PRO 139 223 PRO 140 224 GLU 141 225 VAL 142 226 GLY 143 227 SER 144 228 ASP 145 229 SER 146 230 THR 147 231 THR 148 232 ILE 149 233 HIS 150 234 TYR 151 235 ASN 152 236 TYR 153 237 MET 154 238 CYS 155 239 TYR 156 240 SER 157 241 SER 158 242 CYS 159 243 MET 160 244 GLY 161 245 GLY 162 246 MET 163 247 ASN 164 248 ARG 165 249 ARG 166 250 PRO 167 251 ILE 168 252 LEU 169 253 THR 170 254 ILE 171 255 ILE 172 256 THR 173 257 LEU 174 258 GLU 175 259 ASP 176 260 SER 177 261 SER 178 262 GLY 179 263 ASN 180 264 LEU 181 265 LEU 182 266 GLY 183 267 ARG 184 268 ASP 185 269 SER 186 270 PHE 187 271 GLU 188 272 VAL 189 273 ARG 190 274 VAL 191 275 SER 192 276 ALA 193 277 SER 194 278 PRO 195 279 GLY 196 280 ARG 197 281 ASP 198 282 ARG 199 283 ARG 200 284 THR 201 285 GLU 202 286 GLU 203 287 GLU 204 288 ASN 205 289 LEU 206 290 ARG 207 291 LYS 208 292 LYS 209 293 GLY 210 294 GLU 211 295 PRO 212 296 HIS 213 297 HIS 214 298 GLU 215 299 LEU 216 300 PRO 217 301 PRO 218 302 GLY 219 303 SER 220 304 THR 221 305 LYS 222 306 ARG 223 307 ALA 224 308 LEU 225 309 PRO 226 310 ASN 227 311 ASN 228 312 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $p53(DBD)_super-stable_C5xS 'E. coli' 562 Bacteria . Escherichia coli 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 $p53(DBD)_super-stable_C5xS 'recombinant technology' . Escherichia coli . pET21 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '300 micromolar 15N, 13C, 2H labeled p53(88-312) super-stable and C5xS' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $p53(DBD)_super-stable_C5xS 300 uM '[U-100% 13C; U-100% 15N; U-80% 2H]' Tris 20 mM 'natural abundance' NaCl 150 mM 'natural abundance' DTT 2 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' collection 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details 'Cold-probe equipped' 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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '20mM Tris, pH 7.0, 150mM NaCl, 2mM DTT' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 170 . mM pH 7.0 . 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 'Referenced to external DSS sample.' loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 external direct . . . 1 DSS N 15 'methyl protons' ppm 0 external 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 $NMRView stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D HN(CO)CACB' '3D HNCA' 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 p53(DBD) _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 98 14 PRO CA C 61.754 0.1 1 2 98 14 PRO CB C 30.986 0.1 1 3 99 15 SER H H 8.362 0.01 1 4 99 15 SER CA C 57.877 0.1 1 5 99 15 SER CB C 63.239 0.1 1 6 99 15 SER N N 114.490 0.01 1 7 100 16 GLN H H 8.527 0.01 1 8 100 16 GLN CA C 53.835 0.1 1 9 100 16 GLN CB C 29.254 0.1 1 10 100 16 GLN N N 120.622 0.01 1 11 101 17 LYS H H 7.792 0.01 1 12 101 17 LYS CA C 56.704 0.1 1 13 101 17 LYS CB C 31.907 0.1 1 14 101 17 LYS N N 123.096 0.01 1 15 102 18 THR H H 8.814 0.01 1 16 102 18 THR CA C 64.311 0.1 1 17 102 18 THR CB C 68.435 0.1 1 18 102 18 THR N N 124.772 0.01 1 19 103 19 TYR H H 9.305 0.01 1 20 103 19 TYR CA C 55.923 0.1 1 21 103 19 TYR CB C 39.769 0.1 1 22 103 19 TYR N N 127.728 0.01 1 23 104 20 GLN H H 9.208 0.01 1 24 104 20 GLN CA C 57.902 0.1 1 25 104 20 GLN CB C 27.930 0.1 1 26 104 20 GLN N N 127.920 0.01 1 27 105 21 GLY H H 7.345 0.01 1 28 105 21 GLY CA C 44.762 0.1 1 29 105 21 GLY N N 104.645 0.01 1 30 106 22 SER H H 9.272 0.01 1 31 106 22 SER CA C 60.104 0.1 1 32 106 22 SER CB C 62.661 0.1 1 33 106 22 SER N N 116.639 0.01 1 34 107 23 TYR H H 8.672 0.01 1 35 107 23 TYR CA C 57.465 0.1 1 36 107 23 TYR CB C 34.863 0.1 1 37 107 23 TYR N N 117.224 0.01 1 38 108 24 GLY H H 7.439 0.01 1 39 108 24 GLY CA C 47.566 0.1 1 40 108 24 GLY N N 109.880 0.01 1 41 109 25 PHE H H 8.295 0.01 1 42 109 25 PHE CA C 57.217 0.1 1 43 109 25 PHE CB C 39.895 0.1 1 44 109 25 PHE N N 119.699 0.01 1 45 110 26 ARG H H 8.493 0.01 1 46 110 26 ARG CA C 54.743 0.1 1 47 110 26 ARG CB C 31.234 0.1 1 48 110 26 ARG N N 124.463 0.01 1 49 111 27 LEU H H 8.478 0.01 1 50 111 27 LEU CA C 52.350 0.1 1 51 111 27 LEU CB C 42.535 0.1 1 52 111 27 LEU N N 117.521 0.01 1 53 112 28 GLY H H 8.599 0.01 1 54 112 28 GLY CA C 43.689 0.1 1 55 112 28 GLY N N 107.141 0.01 1 56 113 29 PHE H H 7.945 0.01 1 57 113 29 PHE CA C 56.227 0.1 1 58 113 29 PHE CB C 41.875 0.1 1 59 113 29 PHE N N 115.574 0.01 1 60 114 30 LEU H H 8.925 0.01 1 61 114 30 LEU CA C 54.291 0.1 1 62 114 30 LEU CB C 41.601 0.1 1 63 114 30 LEU N N 122.661 0.01 1 64 117 33 GLY CA C 44.597 0.1 1 65 118 34 THR H H 8.313 0.01 1 66 118 34 THR CA C 60.352 0.1 1 67 118 34 THR CB C 69.178 0.1 1 68 118 34 THR N N 110.567 0.01 1 69 120 36 LYS CA C 62.361 0.1 1 70 120 36 LYS CB C 30.891 0.1 1 71 121 37 SER H H 8.199 0.01 1 72 121 37 SER CA C 57.306 0.1 1 73 121 37 SER CB C 63.429 0.1 1 74 121 37 SER N N 115.994 0.01 1 75 122 38 VAL H H 7.988 0.01 1 76 122 38 VAL CA C 61.861 0.1 1 77 122 38 VAL CB C 31.811 0.1 1 78 122 38 VAL N N 121.841 0.01 1 79 123 39 THR H H 8.691 0.01 1 80 123 39 THR CA C 62.674 0.1 1 81 123 39 THR CB C 68.848 0.1 1 82 123 39 THR N N 115.187 0.01 1 83 124 40 SER H H 7.507 0.01 1 84 124 40 SER CA C 57.712 0.1 1 85 124 40 SER CB C 64.971 0.1 1 86 124 40 SER N N 113.750 0.01 1 87 125 41 THR H H 9.507 0.01 1 88 125 41 THR CA C 59.774 0.1 1 89 125 41 THR CB C 68.188 0.1 1 90 125 41 THR N N 117.600 0.01 1 91 126 42 TYR H H 8.697 0.01 1 92 126 42 TYR CA C 55.650 0.1 1 93 126 42 TYR CB C 40.307 0.1 1 94 126 42 TYR N N 130.527 0.01 1 95 127 43 SER H H 8.473 0.01 1 96 127 43 SER CA C 52.928 0.1 1 97 127 43 SER CB C 64.228 0.1 1 98 127 43 SER N N 119.836 0.01 1 99 128 44 PRO CA C 63.898 0.1 1 100 128 44 PRO CB C 31.151 0.1 1 101 129 45 ALA H H 8.101 0.01 1 102 129 45 ALA CA C 54.248 0.1 1 103 129 45 ALA CB C 17.871 0.1 1 104 129 45 ALA N N 118.499 0.01 1 105 130 46 LEU H H 7.068 0.01 1 106 130 46 LEU CA C 53.175 0.1 1 107 130 46 LEU CB C 43.112 0.1 1 108 130 46 LEU N N 112.912 0.01 1 109 131 47 ASN H H 7.974 0.01 1 110 131 47 ASN CA C 53.190 0.1 1 111 131 47 ASN CB C 36.226 0.1 1 112 131 47 ASN N N 119.107 0.01 1 113 132 48 LYS H H 6.886 0.01 1 114 132 48 LYS CA C 53.670 0.1 1 115 132 48 LYS CB C 38.410 0.1 1 116 132 48 LYS N N 117.918 0.01 1 117 133 49 LEU H H 9.414 0.01 1 118 133 49 LEU CA C 53.391 0.1 1 119 133 49 LEU CB C 44.528 0.1 1 120 133 49 LEU N N 130.025 0.01 1 121 134 50 PHE H H 9.049 0.01 1 122 134 50 PHE CA C 55.567 0.1 1 123 134 50 PHE CB C 38.493 0.1 1 124 134 50 PHE N N 125.971 0.01 1 125 135 51 CYS H H 9.156 0.01 1 126 135 51 CYS CA C 54.578 0.1 1 127 135 51 CYS CB C 33.214 0.1 1 128 135 51 CYS N N 118.789 0.01 1 129 136 52 GLN H H 8.071 0.01 1 130 136 52 GLN CA C 54.165 0.1 1 131 136 52 GLN CB C 30.821 0.1 1 132 136 52 GLN N N 117.802 0.01 1 133 137 53 LEU H H 7.252 0.01 1 134 137 53 LEU CA C 55.897 0.1 1 135 137 53 LEU CB C 41.215 0.1 1 136 137 53 LEU N N 122.729 0.01 1 137 138 54 ALA H H 8.968 0.01 1 138 138 54 ALA CA C 54.000 0.1 1 139 138 54 ALA CB C 16.881 0.1 1 140 138 54 ALA N N 124.910 0.01 1 141 139 55 LYS H H 7.272 0.01 1 142 139 55 LYS CA C 53.258 0.1 1 143 139 55 LYS CB C 33.131 0.1 1 144 139 55 LYS N N 116.844 0.01 1 145 140 56 THR H H 8.153 0.01 1 146 140 56 THR CA C 65.136 0.1 1 147 140 56 THR CB C 68.600 0.1 1 148 140 56 THR N N 117.150 0.01 1 149 141 57 CYS H H 9.179 0.01 1 150 141 57 CYS CA C 55.650 0.1 1 151 141 57 CYS CB C 27.769 0.1 1 152 141 57 CYS N N 125.989 0.01 1 153 142 58 PRO CA C 61.424 0.1 1 154 142 58 PRO CB C 30.409 0.1 1 155 143 59 VAL H H 9.042 0.01 1 156 143 59 VAL CA C 61.424 0.1 1 157 143 59 VAL CB C 33.544 0.1 1 158 143 59 VAL N N 127.271 0.01 1 159 144 60 GLN H H 8.274 0.01 1 160 144 60 GLN CA C 53.079 0.1 1 161 144 60 GLN CB C 29.267 0.1 1 162 144 60 GLN N N 121.287 0.01 1 163 145 61 LEU H H 9.321 0.01 1 164 145 61 LEU CA C 53.093 0.1 1 165 145 61 LEU CB C 41.050 0.1 1 166 145 61 LEU N N 119.628 0.01 1 167 146 62 TRP H H 8.999 0.01 1 168 146 62 TRP CA C 56.115 0.1 1 169 146 62 TRP CB C 29.216 0.1 1 170 146 62 TRP N N 126.657 0.01 1 171 147 63 VAL H H 8.118 0.01 1 172 147 63 VAL CA C 58.619 0.1 1 173 147 63 VAL CB C 33.956 0.1 1 174 147 63 VAL N N 110.572 0.01 1 175 148 64 ASP H H 9.114 0.01 1 176 148 64 ASP CA C 55.155 0.1 1 177 148 64 ASP CB C 41.215 0.1 1 178 148 64 ASP N N 121.690 0.01 1 179 149 65 SER H H 7.851 0.01 1 180 149 65 SER CA C 56.557 0.1 1 181 149 65 SER CB C 64.558 0.1 1 182 149 65 SER N N 113.390 0.01 1 183 150 66 THR H H 8.194 0.01 1 184 150 66 THR CA C 61.375 0.1 1 185 150 66 THR CB C 69.338 0.1 1 186 150 66 THR N N 117.350 0.01 1 187 153 69 PRO CA C 63.239 0.1 1 188 153 69 PRO CB C 30.515 0.1 1 189 154 70 GLY H H 8.821 0.01 1 190 154 70 GLY CA C 44.679 0.1 1 191 154 70 GLY N N 112.859 0.01 1 192 155 71 THR H H 7.609 0.01 1 193 155 71 THR CA C 64.228 0.1 1 194 155 71 THR CB C 67.940 0.1 1 195 155 71 THR N N 117.689 0.01 1 196 156 72 ARG H H 9.663 0.01 1 197 156 72 ARG CA C 54.687 0.1 1 198 156 72 ARG CB C 33.633 0.1 1 199 156 72 ARG N N 127.985 0.01 1 200 157 73 VAL H H 9.097 0.01 1 201 157 73 VAL CA C 60.269 0.1 1 202 157 73 VAL CB C 32.389 0.1 1 203 157 73 VAL N N 119.817 0.01 1 204 158 74 ARG H H 9.660 0.01 1 205 158 74 ARG CA C 54.084 0.1 1 206 158 74 ARG CB C 32.141 0.1 1 207 158 74 ARG N N 132.775 0.01 1 208 159 75 ALA H H 8.648 0.01 1 209 159 75 ALA CA C 50.099 0.1 1 210 159 75 ALA CB C 21.233 0.1 1 211 159 75 ALA N N 126.712 0.01 1 212 160 76 MET H H 8.127 0.01 1 213 160 76 MET CA C 54.000 0.1 1 214 160 76 MET CB C 37.833 0.1 1 215 160 76 MET N N 118.144 0.01 1 216 161 77 ALA H H 9.490 0.01 1 217 161 77 ALA CA C 49.133 0.1 1 218 161 77 ALA CB C 20.676 0.1 1 219 161 77 ALA N N 127.161 0.01 1 220 162 78 ILE H H 8.463 0.01 1 221 162 78 ILE CA C 58.867 0.1 1 222 162 78 ILE CB C 42.122 0.1 1 223 162 78 ILE N N 111.281 0.01 1 224 163 79 TYR H H 9.192 0.01 1 225 163 79 TYR CA C 60.479 0.1 1 226 163 79 TYR CB C 36.657 0.1 1 227 163 79 TYR N N 122.189 0.01 1 228 164 80 LYS H H 7.654 0.01 1 229 164 80 LYS CA C 57.300 0.1 1 230 164 80 LYS CB C 34.781 0.1 1 231 164 80 LYS N N 118.289 0.01 1 232 165 81 GLN H H 9.024 0.01 1 233 165 81 GLN CA C 55.320 0.1 1 234 165 81 GLN CB C 28.759 0.1 1 235 165 81 GLN N N 116.187 0.01 1 236 167 83 GLN CA C 57.465 0.1 1 237 167 83 GLN CB C 26.450 0.1 1 238 168 84 HIS H H 7.629 0.01 1 239 168 84 HIS CA C 54.578 0.1 1 240 168 84 HIS CB C 31.151 0.1 1 241 168 84 HIS N N 116.174 0.01 1 242 169 85 MET H H 7.452 0.01 1 243 169 85 MET CA C 60.269 0.1 1 244 169 85 MET CB C 32.636 0.1 1 245 169 85 MET N N 118.458 0.01 1 246 170 86 THR H H 8.452 0.01 1 247 170 86 THR CA C 62.826 0.1 1 248 170 86 THR CB C 68.270 0.1 1 249 170 86 THR N N 109.708 0.01 1 250 171 87 GLU H H 8.070 0.01 1 251 171 87 GLU CA C 55.726 0.1 1 252 171 87 GLU CB C 29.042 0.1 1 253 171 87 GLU N N 123.857 0.01 1 254 172 88 VAL H H 9.035 0.01 1 255 172 88 VAL CA C 63.666 0.1 1 256 172 88 VAL CB C 31.267 0.1 1 257 172 88 VAL N N 127.966 0.01 1 258 173 89 VAL H H 8.608 0.01 1 259 173 89 VAL CA C 62.989 0.1 1 260 173 89 VAL CB C 30.060 0.1 1 261 173 89 VAL N N 129.888 0.01 1 262 174 90 ARG H H 7.769 0.01 1 263 174 90 ARG CA C 53.918 0.1 1 264 174 90 ARG CB C 32.059 0.1 1 265 174 90 ARG N N 125.715 0.01 1 266 175 91 ARG H H 7.854 0.01 1 267 175 91 ARG CA C 56.145 0.1 1 268 175 91 ARG CB C 31.729 0.1 1 269 175 91 ARG N N 116.212 0.01 1 270 182 98 SER H H 7.827 0.01 1 271 182 98 SER CA C 57.217 0.1 1 272 182 98 SER CB C 63.156 0.1 1 273 182 98 SER N N 112.682 0.01 1 274 183 99 SER H H 7.946 0.01 1 275 183 99 SER CA C 57.877 0.1 1 276 183 99 SER CB C 63.074 0.1 1 277 183 99 SER N N 108.571 0.01 1 278 184 100 ASP H H 8.085 0.01 1 279 184 100 ASP CA C 52.845 0.1 1 280 184 100 ASP CB C 40.307 0.1 1 281 184 100 ASP N N 121.398 0.01 1 282 185 101 SER H H 8.343 0.01 1 283 185 101 SER CA C 58.418 0.1 1 284 185 101 SER CB C 63.368 0.1 1 285 185 101 SER N N 115.997 0.01 1 286 186 102 ASP H H 8.202 0.01 1 287 186 102 ASP CA C 53.258 0.1 1 288 186 102 ASP CB C 40.470 0.1 1 289 186 102 ASP N N 124.021 0.01 1 290 187 103 GLY H H 8.386 0.01 1 291 187 103 GLY CA C 44.844 0.1 1 292 187 103 GLY N N 108.967 0.01 1 293 188 104 LEU H H 8.253 0.01 1 294 188 104 LEU CA C 55.485 0.1 1 295 188 104 LEU CB C 43.112 0.1 1 296 188 104 LEU N N 121.997 0.01 1 297 189 105 ALA H H 8.766 0.01 1 298 189 105 ALA CA C 49.133 0.1 1 299 189 105 ALA CB C 17.294 0.1 1 300 189 105 ALA N N 124.032 0.01 1 301 191 107 PRO CA C 64.228 0.1 1 302 191 107 PRO CB C 32.966 0.1 1 303 192 108 GLN H H 8.497 0.01 1 304 192 108 GLN CA C 56.970 0.1 1 305 192 108 GLN CB C 27.687 0.1 1 306 192 108 GLN N N 113.043 0.01 1 307 193 109 HIS H H 7.272 0.01 1 308 193 109 HIS CA C 57.135 0.1 1 309 193 109 HIS CB C 30.821 0.1 1 310 193 109 HIS N N 118.030 0.01 1 311 194 110 LEU CA C 57.434 0.1 1 312 194 110 LEU CB C 41.385 0.1 1 313 195 111 ILE H H 7.782 0.01 1 314 195 111 ILE CA C 60.517 0.1 1 315 195 111 ILE CB C 37.585 0.1 1 316 195 111 ILE N N 115.299 0.01 1 317 196 112 ARG H H 8.725 0.01 1 318 196 112 ARG CA C 53.175 0.1 1 319 196 112 ARG CB C 33.626 0.1 1 320 196 112 ARG N N 121.452 0.01 1 321 197 113 VAL H H 7.712 0.01 1 322 197 113 VAL CA C 60.352 0.1 1 323 197 113 VAL CB C 32.636 0.1 1 324 197 113 VAL N N 118.143 0.01 1 325 198 114 GLU H H 8.612 0.01 1 326 198 114 GLU CA C 54.321 0.1 1 327 198 114 GLU CB C 30.473 0.1 1 328 198 114 GLU N N 129.110 0.01 1 329 199 115 GLY H H 8.819 0.01 1 330 199 115 GLY CA C 46.164 0.1 1 331 199 115 GLY N N 112.047 0.01 1 332 200 116 ASN H H 7.989 0.01 1 333 200 116 ASN CA C 51.938 0.1 1 334 200 116 ASN CB C 39.318 0.1 1 335 200 116 ASN N N 116.068 0.01 1 336 201 117 LEU H H 8.974 0.01 1 337 201 117 LEU CA C 55.941 0.1 1 338 201 117 LEU CB C 40.265 0.1 1 339 201 117 LEU N N 126.840 0.01 1 340 202 118 ARG H H 8.459 0.01 1 341 202 118 ARG CA C 54.776 0.1 1 342 202 118 ARG CB C 28.267 0.1 1 343 202 118 ARG N N 117.070 0.01 1 344 203 119 ALA H H 6.953 0.01 1 345 203 119 ALA CA C 51.938 0.1 1 346 203 119 ALA CB C 17.871 0.1 1 347 203 119 ALA N N 120.757 0.01 1 348 204 120 GLU H H 8.930 0.01 1 349 204 120 GLU CA C 54.248 0.1 1 350 204 120 GLU CB C 31.764 0.1 1 351 204 120 GLU N N 122.061 0.01 1 352 205 121 TYR H H 8.821 0.01 1 353 205 121 TYR CA C 57.712 0.1 1 354 205 121 TYR CB C 38.163 0.1 1 355 205 121 TYR N N 123.731 0.01 1 356 206 122 LEU H H 9.371 0.01 1 357 206 122 LEU CA C 53.835 0.1 1 358 206 122 LEU CB C 43.607 0.1 1 359 206 122 LEU N N 126.621 0.01 1 360 207 123 ASP H H 8.354 0.01 1 361 207 123 ASP CA C 51.955 0.1 1 362 207 123 ASP CB C 40.724 0.1 1 363 207 123 ASP N N 122.520 0.01 1 364 208 124 ASP H H 8.241 0.01 1 365 208 124 ASP CA C 55.131 0.1 1 366 208 124 ASP CB C 43.003 0.1 1 367 208 124 ASP N N 123.638 0.01 1 368 209 125 ARG H H 9.125 0.01 1 369 209 125 ARG CA C 57.417 0.1 1 370 209 125 ARG CB C 29.083 0.1 1 371 209 125 ARG N N 127.820 0.01 1 372 210 126 ASN H H 8.764 0.01 1 373 210 126 ASN CA C 54.248 0.1 1 374 210 126 ASN CB C 39.400 0.1 1 375 210 126 ASN N N 114.410 0.01 1 376 211 127 THR H H 8.727 0.01 1 377 211 127 THR CA C 61.259 0.1 1 378 211 127 THR CB C 69.920 0.1 1 379 211 127 THR N N 109.373 0.01 1 380 212 128 PHE H H 7.610 0.01 1 381 212 128 PHE CA C 57.300 0.1 1 382 212 128 PHE CB C 36.183 0.1 1 383 212 128 PHE N N 113.377 0.01 1 384 213 129 ARG H H 7.602 0.01 1 385 213 129 ARG CA C 55.897 0.1 1 386 213 129 ARG CB C 29.832 0.1 1 387 213 129 ARG N N 115.462 0.01 1 388 214 130 HIS H H 7.793 0.01 1 389 214 130 HIS CA C 52.069 0.1 1 390 214 130 HIS CB C 31.726 0.1 1 391 214 130 HIS N N 122.574 0.01 1 392 215 131 SER H H 9.283 0.01 1 393 215 131 SER CA C 58.537 0.1 1 394 215 131 SER CB C 65.961 0.1 1 395 215 131 SER N N 114.728 0.01 1 396 216 132 VAL H H 8.258 0.01 1 397 216 132 VAL CA C 57.547 0.1 1 398 216 132 VAL CB C 32.801 0.1 1 399 216 132 VAL N N 114.886 0.01 1 400 217 133 VAL H H 9.216 0.01 1 401 217 133 VAL CA C 58.731 0.1 1 402 217 133 VAL CB C 34.378 0.1 1 403 217 133 VAL N N 130.099 0.01 1 404 218 134 VAL H H 8.471 0.01 1 405 218 134 VAL CA C 56.882 0.1 1 406 218 134 VAL CB C 32.520 0.1 1 407 218 134 VAL N N 117.064 0.01 1 408 219 135 PRO CA C 62.414 0.1 1 409 219 135 PRO CB C 30.739 0.1 1 410 220 136 TYR H H 8.576 0.01 1 411 220 136 TYR CA C 58.867 0.1 1 412 220 136 TYR CB C 37.338 0.1 1 413 220 136 TYR N N 123.814 0.01 1 414 221 137 GLU H H 7.143 0.01 1 415 221 137 GLU CA C 51.608 0.1 1 416 221 137 GLU CB C 30.162 0.1 1 417 221 137 GLU N N 130.565 0.01 1 418 223 139 PRO CA C 62.068 0.1 1 419 223 139 PRO CB C 31.245 0.1 1 420 224 140 GLU H H 8.375 0.01 1 421 224 140 GLU CA C 55.362 0.1 1 422 224 140 GLU CB C 29.363 0.1 1 423 224 140 GLU N N 122.104 0.01 1 424 225 141 VAL H H 8.293 0.01 1 425 225 141 VAL CA C 64.256 0.1 1 426 225 141 VAL CB C 30.287 0.1 1 427 225 141 VAL N N 121.201 0.01 1 428 226 142 GLY H H 8.828 0.01 1 429 226 142 GLY CA C 44.597 0.1 1 430 226 142 GLY N N 115.722 0.01 1 431 227 143 SER H H 8.315 0.01 1 432 227 143 SER CA C 56.640 0.1 1 433 227 143 SER CB C 64.558 0.1 1 434 227 143 SER N N 116.208 0.01 1 435 228 144 ASP H H 8.226 0.01 1 436 228 144 ASP CA C 53.670 0.1 1 437 228 144 ASP CB C 41.957 0.1 1 438 228 144 ASP N N 119.661 0.01 1 439 229 145 SER H H 7.454 0.01 1 440 229 145 SER CA C 56.475 0.1 1 441 229 145 SER CB C 63.898 0.1 1 442 229 145 SER N N 111.117 0.01 1 443 230 146 THR H H 8.001 0.01 1 444 230 146 THR CA C 61.589 0.1 1 445 230 146 THR CB C 70.085 0.1 1 446 230 146 THR N N 117.960 0.01 1 447 231 147 THR H H 8.800 0.01 1 448 231 147 THR CA C 62.050 0.1 1 449 231 147 THR CB C 69.284 0.1 1 450 231 147 THR N N 123.487 0.01 1 451 232 148 ILE H H 9.076 0.01 1 452 232 148 ILE CA C 59.825 0.1 1 453 232 148 ILE CB C 39.269 0.1 1 454 232 148 ILE N N 129.101 0.01 1 455 233 149 HIS H H 8.319 0.01 1 456 233 149 HIS CA C 53.835 0.1 1 457 233 149 HIS CB C 29.997 0.1 1 458 233 149 HIS N N 124.194 0.01 1 459 234 150 TYR H H 8.342 0.01 1 460 234 150 TYR CA C 57.185 0.1 1 461 234 150 TYR CB C 41.010 0.1 1 462 234 150 TYR N N 122.086 0.01 1 463 235 151 ASN H H 9.144 0.01 1 464 235 151 ASN CA C 51.526 0.1 1 465 235 151 ASN CB C 43.524 0.1 1 466 235 151 ASN N N 117.543 0.01 1 467 236 152 TYR H H 9.904 0.01 1 468 236 152 TYR CA C 57.712 0.1 1 469 236 152 TYR CB C 40.637 0.1 1 470 236 152 TYR N N 120.703 0.01 1 471 237 153 MET H H 8.461 0.01 1 472 237 153 MET CA C 53.918 0.1 1 473 237 153 MET CB C 28.512 0.1 1 474 237 153 MET N N 116.198 0.01 1 475 238 154 CYS H H 7.192 0.01 1 476 238 154 CYS CA C 60.846 0.1 1 477 238 154 CYS CB C 34.781 0.1 1 478 238 154 CYS N N 119.729 0.01 1 479 239 155 TYR H H 8.376 0.01 1 480 239 155 TYR CA C 58.537 0.1 1 481 239 155 TYR CB C 38.080 0.1 1 482 239 155 TYR N N 117.161 0.01 1 483 244 160 GLY H H 8.922 0.01 1 484 244 160 GLY CA C 44.927 0.1 1 485 244 160 GLY N N 110.104 0.01 1 486 245 161 GLY H H 7.331 0.01 1 487 245 161 GLY CA C 43.442 0.1 1 488 245 161 GLY N N 108.134 0.01 1 489 246 162 MET CA C 59.444 0.1 1 490 246 162 MET CB C 32.554 0.1 1 491 247 163 ASN H H 8.675 0.01 1 492 247 163 ASN CA C 54.413 0.1 1 493 247 163 ASN CB C 36.678 0.1 1 494 247 163 ASN N N 117.606 0.01 1 495 248 164 ARG H H 9.405 0.01 1 496 248 164 ARG CA C 57.217 0.1 1 497 248 164 ARG CB C 26.367 0.1 1 498 248 164 ARG N N 107.590 0.01 1 499 249 165 ARG H H 7.812 0.01 1 500 249 165 ARG CA C 53.542 0.1 1 501 249 165 ARG CB C 30.210 0.1 1 502 249 165 ARG N N 123.022 0.01 1 503 250 166 PRO CA C 62.331 0.1 1 504 250 166 PRO CB C 32.801 0.1 1 505 251 167 ILE H H 7.026 0.01 1 506 251 167 ILE CA C 58.372 0.1 1 507 251 167 ILE CB C 42.370 0.1 1 508 251 167 ILE N N 111.753 0.01 1 509 252 168 LEU H H 9.280 0.01 1 510 252 168 LEU CA C 52.680 0.1 1 511 252 168 LEU CB C 43.937 0.1 1 512 252 168 LEU N N 118.172 0.01 1 513 253 169 THR H H 8.923 0.01 1 514 253 169 THR CA C 61.589 0.1 1 515 253 169 THR CB C 69.260 0.1 1 516 253 169 THR N N 114.238 0.01 1 517 254 170 ILE H H 9.307 0.01 1 518 254 170 ILE CA C 59.692 0.1 1 519 254 170 ILE CB C 38.658 0.1 1 520 254 170 ILE N N 126.255 0.01 1 521 255 171 ILE H H 9.229 0.01 1 522 255 171 ILE CA C 57.609 0.1 1 523 255 171 ILE CB C 36.547 0.1 1 524 255 171 ILE N N 130.108 0.01 1 525 256 172 THR H H 9.393 0.01 1 526 256 172 THR CA C 57.547 0.1 1 527 256 172 THR CB C 69.343 0.1 1 528 256 172 THR N N 115.429 0.01 1 529 257 173 LEU H H 8.128 0.01 1 530 257 173 LEU CA C 51.938 0.1 1 531 257 173 LEU CB C 42.122 0.1 1 532 257 173 LEU N N 124.600 0.01 1 533 258 174 GLU H H 9.236 0.01 1 534 258 174 GLU CA C 53.340 0.1 1 535 258 174 GLU CB C 33.873 0.1 1 536 258 174 GLU N N 125.760 0.01 1 537 259 175 ASP H H 8.397 0.01 1 538 259 175 ASP CA C 52.112 0.1 1 539 259 175 ASP CB C 40.694 0.1 1 540 259 175 ASP N N 119.197 0.01 1 541 260 176 SER H H 8.565 0.01 1 542 260 176 SER CA C 60.764 0.1 1 543 260 176 SER CB C 62.711 0.1 1 544 260 176 SER N N 112.787 0.01 1 545 261 177 SER H H 8.085 0.01 1 546 261 177 SER CA C 58.042 0.1 1 547 261 177 SER CB C 63.742 0.1 1 548 261 177 SER N N 116.630 0.01 1 549 262 178 GLY H H 8.025 0.01 1 550 262 178 GLY CA C 44.349 0.1 1 551 262 178 GLY N N 108.733 0.01 1 552 263 179 ASN H H 8.710 0.01 1 553 263 179 ASN CA C 53.093 0.1 1 554 263 179 ASN CB C 37.503 0.1 1 555 263 179 ASN N N 120.371 0.01 1 556 264 180 LEU H H 8.553 0.01 1 557 264 180 LEU CA C 55.827 0.1 1 558 264 180 LEU CB C 41.352 0.1 1 559 264 180 LEU N N 123.130 0.01 1 560 265 181 LEU H H 9.640 0.01 1 561 265 181 LEU CA C 54.248 0.1 1 562 265 181 LEU CB C 42.699 0.1 1 563 265 181 LEU N N 123.917 0.01 1 564 266 182 GLY H H 7.926 0.01 1 565 266 182 GLY CA C 45.092 0.1 1 566 266 182 GLY N N 106.312 0.01 1 567 267 183 ARG H H 10.232 0.01 1 568 267 183 ARG CA C 56.145 0.1 1 569 267 183 ARG CB C 34.038 0.1 1 570 267 183 ARG N N 124.455 0.01 1 571 268 184 ASP H H 9.606 0.01 1 572 268 184 ASP CA C 53.122 0.1 1 573 268 184 ASP CB C 43.515 0.1 1 574 268 184 ASP N N 128.332 0.01 1 575 269 185 SER H H 9.716 0.01 1 576 269 185 SER CA C 57.547 0.1 1 577 269 185 SER CB C 66.950 0.1 1 578 269 185 SER N N 113.658 0.01 1 579 270 186 PHE H H 8.036 0.01 1 580 270 186 PHE CA C 55.732 0.1 1 581 270 186 PHE CB C 39.153 0.1 1 582 270 186 PHE N N 112.525 0.01 1 583 271 187 GLU H H 8.647 0.01 1 584 271 187 GLU CA C 55.127 0.1 1 585 271 187 GLU CB C 29.605 0.1 1 586 271 187 GLU N N 122.825 0.01 1 587 272 188 VAL H H 7.974 0.01 1 588 272 188 VAL CA C 59.965 0.1 1 589 272 188 VAL CB C 34.934 0.1 1 590 272 188 VAL N N 122.434 0.01 1 591 273 189 ARG H H 8.470 0.01 1 592 273 189 ARG CA C 54.743 0.1 1 593 273 189 ARG CB C 32.801 0.1 1 594 273 189 ARG N N 126.063 0.01 1 595 274 190 VAL H H 8.812 0.01 1 596 274 190 VAL CA C 58.949 0.1 1 597 274 190 VAL CB C 31.481 0.1 1 598 274 190 VAL N N 129.357 0.01 1 599 275 191 SER H H 10.061 0.01 1 600 275 191 SER CA C 56.722 0.1 1 601 275 191 SER CB C 66.126 0.1 1 602 275 191 SER N N 125.724 0.01 1 603 276 192 ALA H H 8.561 0.01 1 604 276 192 ALA CA C 52.680 0.1 1 605 276 192 ALA CB C 18.036 0.1 1 606 276 192 ALA N N 118.780 0.01 1 607 277 193 SER H H 8.070 0.01 1 608 277 193 SER CA C 54.165 0.1 1 609 277 193 SER CB C 63.651 0.1 1 610 277 193 SER N N 110.441 0.01 1 611 278 194 PRO CA C 64.971 0.1 1 612 278 194 PRO CB C 30.739 0.1 1 613 279 195 GLY H H 8.337 0.01 1 614 279 195 GLY CA C 46.494 0.1 1 615 279 195 GLY N N 105.220 0.01 1 616 280 196 ARG H H 7.677 0.01 1 617 280 196 ARG CA C 58.207 0.1 1 618 280 196 ARG CB C 29.089 0.1 1 619 280 196 ARG N N 123.073 0.01 1 620 281 197 ASP H H 8.265 0.01 1 621 281 197 ASP CA C 57.112 0.1 1 622 281 197 ASP CB C 38.597 0.1 1 623 281 197 ASP N N 121.161 0.01 1 624 282 198 ARG H H 7.799 0.01 1 625 282 198 ARG CA C 58.537 0.1 1 626 282 198 ARG CB C 27.522 0.1 1 627 282 198 ARG N N 121.058 0.01 1 628 283 199 ARG H H 7.367 0.01 1 629 283 199 ARG CA C 58.784 0.1 1 630 283 199 ARG CB C 28.594 0.1 1 631 283 199 ARG N N 117.299 0.01 1 632 284 200 THR H H 8.335 0.01 1 633 284 200 THR CA C 65.850 0.1 1 634 284 200 THR CB C 68.342 0.1 1 635 284 200 THR N N 115.743 0.01 1 636 285 201 GLU H H 8.184 0.01 1 637 285 201 GLU CA C 60.599 0.1 1 638 285 201 GLU CB C 28.512 0.1 1 639 285 201 GLU N N 120.872 0.01 1 640 286 202 GLU H H 8.652 0.01 1 641 286 202 GLU CA C 59.362 0.1 1 642 286 202 GLU CB C 28.017 0.1 1 643 286 202 GLU N N 119.642 0.01 1 644 287 203 GLU H H 8.326 0.01 1 645 287 203 GLU CA C 58.550 0.1 1 646 287 203 GLU CB C 28.092 0.1 1 647 287 203 GLU N N 121.025 0.01 1 648 288 204 ASN H H 7.949 0.01 1 649 288 204 ASN CA C 54.825 0.1 1 650 288 204 ASN CB C 37.585 0.1 1 651 288 204 ASN N N 117.099 0.01 1 652 289 205 LEU H H 7.527 0.01 1 653 289 205 LEU CA C 56.640 0.1 1 654 289 205 LEU CB C 40.802 0.1 1 655 289 205 LEU N N 120.219 0.01 1 656 290 206 ARG H H 7.735 0.01 1 657 290 206 ARG CA C 57.186 0.1 1 658 290 206 ARG CB C 29.136 0.1 1 659 290 206 ARG N N 118.822 0.01 1 660 291 207 LYS H H 7.954 0.01 1 661 291 207 LYS CA C 56.906 0.1 1 662 291 207 LYS CB C 31.648 0.1 1 663 291 207 LYS N N 119.348 0.01 1 664 292 208 LYS H H 7.963 0.01 1 665 292 208 LYS CA C 56.805 0.1 1 666 292 208 LYS CB C 31.564 0.1 1 667 292 208 LYS N N 120.385 0.01 1 668 293 209 GLY H H 8.101 0.01 1 669 293 209 GLY CA C 44.597 0.1 1 670 293 209 GLY N N 108.297 0.01 1 671 294 210 GLU H H 8.050 0.01 1 672 294 210 GLU CA C 53.726 0.1 1 673 294 210 GLU CB C 28.842 0.1 1 674 294 210 GLU N N 121.553 0.01 1 675 295 211 PRO CA C 64.340 0.1 1 676 295 211 PRO CB C 31.602 0.1 1 677 296 212 HIS H H 9.073 0.01 1 678 296 212 HIS CA C 56.814 0.1 1 679 296 212 HIS CB C 29.485 0.1 1 680 296 212 HIS N N 129.266 0.01 1 681 297 213 HIS CA C 55.197 0.1 1 682 297 213 HIS CB C 29.808 0.1 1 683 298 214 GLU H H 8.480 0.01 1 684 298 214 GLU CA C 55.668 0.1 1 685 298 214 GLU CB C 29.584 0.1 1 686 298 214 GLU N N 122.334 0.01 1 687 299 215 LEU H H 8.375 0.01 1 688 299 215 LEU CA C 52.433 0.1 1 689 299 215 LEU CB C 40.472 0.1 1 690 299 215 LEU N N 124.772 0.01 1 691 302 218 GLY H H 8.554 0.01 1 692 302 218 GLY CA C 44.679 0.1 1 693 302 218 GLY N N 109.464 0.01 1 694 303 219 SER H H 8.084 0.01 1 695 303 219 SER CA C 58.289 0.1 1 696 303 219 SER CB C 63.734 0.1 1 697 303 219 SER N N 115.305 0.01 1 698 304 220 THR CA C 61.469 0.1 1 699 304 220 THR CB C 69.118 0.1 1 700 305 221 LYS H H 8.266 0.01 1 701 305 221 LYS CA C 55.787 0.1 1 702 305 221 LYS CB C 31.857 0.1 1 703 305 221 LYS N N 123.624 0.01 1 704 306 222 ARG H H 8.264 0.01 1 705 306 222 ARG CA C 55.476 0.1 1 706 306 222 ARG CB C 29.899 0.1 1 707 306 222 ARG N N 122.521 0.01 1 708 307 223 ALA H H 8.316 0.01 1 709 307 223 ALA CA C 51.608 0.1 1 710 307 223 ALA CB C 18.284 0.1 1 711 307 223 ALA N N 125.669 0.01 1 712 308 224 LEU H H 8.239 0.01 1 713 308 224 LEU CA C 52.470 0.1 1 714 308 224 LEU CB C 40.513 0.1 1 715 308 224 LEU N N 122.977 0.01 1 716 309 225 PRO CA C 62.661 0.1 1 717 309 225 PRO CB C 31.069 0.1 1 718 310 226 ASN H H 8.474 0.01 1 719 310 226 ASN CA C 52.845 0.1 1 720 310 226 ASN CB C 38.245 0.1 1 721 310 226 ASN N N 118.266 0.01 1 722 311 227 ASN CA C 53.074 0.1 1 723 311 227 ASN CB C 38.388 0.1 1 724 312 228 THR H H 7.751 0.01 1 725 312 228 THR CA C 62.840 0.1 1 726 312 228 THR CB C 70.183 0.1 1 727 312 228 THR N N 118.782 0.01 1 stop_ save_