data_17468 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A ; _BMRB_accession_number 17468 _BMRB_flat_file_name bmr17468.str _Entry_type original _Submission_date 2011-02-14 _Accession_date 2011-02-14 _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 Feuerstein Sophie . . 2 Willbold Dieter . . 3 Brutscher Bernhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 160 "13C chemical shifts" 511 "15N chemical shifts" 160 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-03-09 update BMRB 'update entry citation' 2011-05-03 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '1H, 13C, and 15N resonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21516467 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Feuerstein Sophie . . 2 Solyom Zsofia . . 3 Alada Amine . . 4 Hoffmann Silke . . 5 Willbold Dieter . . 6 Brutscher Bernhard . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 5 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 241 _Page_last 243 _Year 2011 _Details . loop_ _Keyword 'domain 2' HCV 'heteronuclear NMR' 'intrinsically disordered proteins' NS5A 'resonance assignment' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'NS5A fragment (191-369) monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'NS5A fragment (191-369) monomer' $NS5A_fragment_(191-369) stop_ _System_molecular_weight 20400 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NS5A_fragment_(191-369) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NS5A_fragment_(191-369) _Molecular_mass 20400 _Mol_thiol_state 'all free' loop_ _Biological_function 'viral RNA replication; signal transduction; virus persistence' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 188 _Mol_residue_sequence ; GPLGSLRGGEPEPDVTVLTS MLTDPSHITAETAKRRLARG SPPSLASSSASQLSAPSLKA TCTTHHDSPDADLIEANLLW RQEMGGNITRVESENKVVIL DSFEPLHADGDEREISVAAE ILRKSRKFPSALPIWARPDY NPPLLESWKDPDYVPPVVHG CPLPPTKAPPIPPPRRKRTV VLTESNVS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . GLY 2 . PRO 3 . LEU 4 . GLY 5 . SER 6 . LEU 7 . ARG 8 . GLY 9 . GLY 10 191 GLU 11 192 PRO 12 193 GLU 13 194 PRO 14 195 ASP 15 196 VAL 16 197 THR 17 198 VAL 18 199 LEU 19 200 THR 20 201 SER 21 202 MET 22 203 LEU 23 204 THR 24 205 ASP 25 206 PRO 26 207 SER 27 208 HIS 28 209 ILE 29 210 THR 30 211 ALA 31 212 GLU 32 213 THR 33 214 ALA 34 215 LYS 35 216 ARG 36 217 ARG 37 218 LEU 38 219 ALA 39 220 ARG 40 221 GLY 41 222 SER 42 223 PRO 43 224 PRO 44 225 SER 45 226 LEU 46 227 ALA 47 228 SER 48 229 SER 49 230 SER 50 231 ALA 51 232 SER 52 233 GLN 53 234 LEU 54 235 SER 55 236 ALA 56 237 PRO 57 238 SER 58 239 LEU 59 240 LYS 60 241 ALA 61 242 THR 62 243 CYS 63 244 THR 64 245 THR 65 246 HIS 66 247 HIS 67 248 ASP 68 249 SER 69 250 PRO 70 251 ASP 71 252 ALA 72 253 ASP 73 254 LEU 74 255 ILE 75 256 GLU 76 257 ALA 77 258 ASN 78 259 LEU 79 260 LEU 80 261 TRP 81 262 ARG 82 263 GLN 83 264 GLU 84 265 MET 85 266 GLY 86 267 GLY 87 268 ASN 88 269 ILE 89 270 THR 90 271 ARG 91 272 VAL 92 273 GLU 93 274 SER 94 275 GLU 95 276 ASN 96 277 LYS 97 278 VAL 98 279 VAL 99 280 ILE 100 281 LEU 101 282 ASP 102 283 SER 103 284 PHE 104 285 GLU 105 286 PRO 106 287 LEU 107 288 HIS 108 289 ALA 109 290 ASP 110 291 GLY 111 292 ASP 112 293 GLU 113 294 ARG 114 295 GLU 115 296 ILE 116 297 SER 117 298 VAL 118 299 ALA 119 300 ALA 120 301 GLU 121 302 ILE 122 303 LEU 123 304 ARG 124 305 LYS 125 306 SER 126 307 ARG 127 308 LYS 128 309 PHE 129 310 PRO 130 311 SER 131 312 ALA 132 313 LEU 133 314 PRO 134 315 ILE 135 316 TRP 136 317 ALA 137 318 ARG 138 319 PRO 139 320 ASP 140 321 TYR 141 322 ASN 142 323 PRO 143 324 PRO 144 325 LEU 145 326 LEU 146 327 GLU 147 328 SER 148 329 TRP 149 330 LYS 150 331 ASP 151 332 PRO 152 333 ASP 153 334 TYR 154 335 VAL 155 336 PRO 156 337 PRO 157 338 VAL 158 339 VAL 159 340 HIS 160 341 GLY 161 342 CYS 162 343 PRO 163 344 LEU 164 345 PRO 165 346 PRO 166 347 THR 167 348 LYS 168 349 ALA 169 350 PRO 170 351 PRO 171 352 ILE 172 353 PRO 173 354 PRO 174 355 PRO 175 356 ARG 176 357 ARG 177 358 LYS 178 359 ARG 179 360 THR 180 361 VAL 181 362 VAL 182 363 LEU 183 364 THR 184 365 GLU 185 366 SER 186 367 ASN 187 368 VAL 188 369 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-13 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 BMRB 26549 NS5A(191-447) 98.40 268 100.00 100.00 8.75e-128 DBJ BAA01583 "polyprotein precursor [Hepatitis C virus]" 95.21 3010 99.44 100.00 1.71e-111 DBJ BAA02756 "polyprotein precursor [Hepatitis C virus]" 95.21 3010 99.44 100.00 1.92e-111 GB AAC15722 "polyprotein [Hepatitis C virus subtype 1b]" 95.21 3010 99.44 100.00 1.34e-111 GB AAC15723 "polyprotein [Hepatitis C virus subtype 1b]" 95.21 3010 99.44 100.00 1.72e-111 GB AAC15724 "polyprotein [Hepatitis C virus subtype 1b]" 95.21 3010 99.44 100.00 1.88e-111 GB AAC15725 "polyprotein [Hepatitis C virus subtype 1b]" 95.21 3010 99.44 99.44 4.20e-111 GB AAC15726 "polyprotein, partial [Hepatitis C virus]" 95.21 2864 99.44 100.00 1.16e-111 SP O92972 "RecName: Full=Genome polyprotein; Contains: RecName: Full=Core protein p21; AltName: Full=Capsid protein C; AltName: Full=p21; " 95.21 3010 99.44 100.00 1.51e-111 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _ICTVdb_decimal_code _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic _Details $NS5A_fragment_(191-369) 'Hepatitis C virus subtype 1b' 00.026.0.03.001.01.002. 31647 virus . Hepacivirus 'Hepatitis C virus' HC-J4 'isolate HC-J4' 'virus host 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 $NS5A_fragment_(191-369) 'recombinant technology' . Escherichia coli 'BL21 DE3' pGEX-6P-2 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 $NS5A_fragment_(191-369) 130 uM '[U-98% 13C; U-98% 15N]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VNMRS _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_BEST-TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N BEST-TROSY' _Sample_label $sample_1 save_ save_2D_HADAMAC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HADAMAC' _Sample_label $sample_1 save_ save_3D_BEST-TROSY_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BEST-TROSY HNCO' _Sample_label $sample_1 save_ save_3D_BEST-TROSY_HNcoCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BEST-TROSY HNcoCA' _Sample_label $sample_1 save_ save_3D_BEST-TROSY_iHNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BEST-TROSY iHNCA' _Sample_label $sample_1 save_ save_3D_BEST-TROSY_HNcoCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BEST-TROSY HNcoCACB' _Sample_label $sample_1 save_ save_3D_BEST-TROSY_iHNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BEST-TROSY iHNCACB' _Sample_label $sample_1 save_ save_3D_BEST-TROSY_hNcocaNH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BEST-TROSY hNcocaNH' _Sample_label $sample_1 save_ save_3D_BEST-TROSY_hnCOcaNH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BEST-TROSY hnCOcaNH' _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' 20 . mM pH 6.5 . pH pressure 1 . atm temperature 278 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N BEST-TROSY' '2D HADAMAC' '3D BEST-TROSY HNCO' '3D BEST-TROSY HNcoCA' '3D BEST-TROSY iHNCA' '3D BEST-TROSY HNcoCACB' '3D BEST-TROSY iHNCACB' '3D BEST-TROSY hNcocaNH' '3D BEST-TROSY hnCOcaNH' 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 'NS5A fragment (191-369) monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 PRO C C 177.12 0.15 1 2 2 2 PRO CA C 62.99 0.15 1 3 2 2 PRO CB C 32.40 0.15 1 4 3 3 LEU H H 8.68 0.02 1 5 3 3 LEU C C 178.09 0.15 1 6 3 3 LEU CA C 55.45 0.15 1 7 3 3 LEU CB C 42.35 0.15 1 8 3 3 LEU N N 122.75 0.15 1 9 4 4 GLY H H 8.53 0.02 1 10 4 4 GLY C C 174.19 0.15 1 11 4 4 GLY CA C 45.34 0.15 1 12 4 4 GLY N N 110.23 0.15 1 13 5 5 SER H H 8.28 0.02 1 14 5 5 SER C C 174.72 0.15 1 15 5 5 SER CA C 58.32 0.15 1 16 5 5 SER CB C 64.07 0.15 1 17 5 5 SER N N 115.74 0.15 1 18 6 6 LEU H H 8.45 0.02 1 19 6 6 LEU C C 177.59 0.15 1 20 6 6 LEU CA C 55.31 0.15 1 21 6 6 LEU CB C 42.30 0.15 1 22 6 6 LEU N N 124.25 0.15 1 23 7 7 ARG H H 8.52 0.02 1 24 7 7 ARG C C 176.91 0.15 1 25 7 7 ARG CA C 56.19 0.15 1 26 7 7 ARG CB C 30.74 0.15 1 27 7 7 ARG N N 121.97 0.15 1 28 8 8 GLY H H 8.55 0.02 1 29 8 8 GLY C C 174.59 0.15 1 30 8 8 GLY CA C 45.37 0.15 1 31 8 8 GLY N N 110.58 0.15 1 32 9 9 GLY H H 8.37 0.02 1 33 9 9 GLY C C 173.91 0.15 1 34 9 9 GLY CA C 44.84 0.15 1 35 9 9 GLY N N 108.91 0.15 1 36 191 10 GLU H H 8.34 0.02 1 37 191 10 GLU CA C 54.41 0.15 1 38 191 10 GLU CB C 29.64 0.15 1 39 191 10 GLU N N 121.77 0.15 1 40 192 11 PRO C C 176.68 0.15 1 41 192 11 PRO CA C 62.77 0.15 1 42 192 11 PRO CB C 32.14 0.15 1 43 193 12 GLU H H 8.64 0.02 1 44 193 12 GLU CA C 54.34 0.15 1 45 193 12 GLU CB C 29.80 0.15 1 46 193 12 GLU N N 123.00 0.15 1 47 194 13 PRO C C 176.38 0.15 1 48 194 13 PRO CA C 63.02 0.15 1 49 194 13 PRO CB C 32.22 0.15 1 50 195 14 ASP H H 8.55 0.02 1 51 195 14 ASP C C 176.62 0.15 1 52 195 14 ASP CA C 54.14 0.15 1 53 195 14 ASP CB C 41.18 0.15 1 54 195 14 ASP N N 121.11 0.15 1 55 196 15 VAL H H 8.29 0.02 1 56 196 15 VAL C C 176.57 0.15 1 57 196 15 VAL CA C 62.42 0.15 1 58 196 15 VAL CB C 32.61 0.15 1 59 196 15 VAL N N 120.91 0.15 1 60 197 16 THR H H 8.44 0.02 1 61 197 16 THR C C 174.76 0.15 1 62 197 16 THR CA C 62.77 0.15 1 63 197 16 THR CB C 69.79 0.15 1 64 197 16 THR N N 118.77 0.15 1 65 198 17 VAL H H 8.17 0.02 1 66 198 17 VAL C C 176.30 0.15 1 67 198 17 VAL CA C 62.63 0.15 1 68 198 17 VAL CB C 32.69 0.15 1 69 198 17 VAL N N 123.63 0.15 1 70 199 18 LEU H H 8.38 0.02 1 71 199 18 LEU C C 177.87 0.15 1 72 199 18 LEU CA C 55.37 0.15 1 73 199 18 LEU CB C 42.34 0.15 1 74 199 18 LEU N N 125.88 0.15 1 75 200 19 THR H H 8.19 0.02 1 76 200 19 THR C C 174.87 0.15 1 77 200 19 THR CA C 62.39 0.15 1 78 200 19 THR CB C 69.77 0.15 1 79 200 19 THR N N 114.92 0.15 1 80 201 20 SER H H 8.31 0.02 1 81 201 20 SER C C 174.67 0.15 1 82 201 20 SER CA C 58.66 0.15 1 83 201 20 SER CB C 63.75 0.15 1 84 201 20 SER N N 117.83 0.15 1 85 202 21 MET H H 8.37 0.02 1 86 202 21 MET C C 176.35 0.15 1 87 202 21 MET CA C 55.79 0.15 1 88 202 21 MET CB C 32.81 0.15 1 89 202 21 MET N N 122.08 0.15 1 90 203 22 LEU H H 8.19 0.02 1 91 203 22 LEU C C 177.52 0.15 1 92 203 22 LEU CA C 55.41 0.15 1 93 203 22 LEU CB C 42.31 0.15 1 94 203 22 LEU N N 122.20 0.15 1 95 204 23 THR H H 8.03 0.02 1 96 204 23 THR C C 173.88 0.15 1 97 204 23 THR CA C 61.59 0.15 1 98 204 23 THR CB C 69.94 0.15 1 99 204 23 THR N N 113.62 0.15 1 100 205 24 ASP H H 8.32 0.02 1 101 205 24 ASP CA C 52.05 0.15 1 102 205 24 ASP CB C 41.50 0.15 1 103 205 24 ASP N N 124.33 0.15 1 104 206 25 PRO C C 177.55 0.15 1 105 206 25 PRO CA C 64.05 0.15 1 106 206 25 PRO CB C 32.13 0.15 1 107 207 26 SER H H 8.53 0.02 1 108 207 26 SER C C 174.99 0.15 1 109 207 26 SER CA C 59.57 0.15 1 110 207 26 SER CB C 63.53 0.15 1 111 207 26 SER N N 114.81 0.15 1 112 208 27 HIS H H 8.15 0.02 1 113 208 27 HIS C C 175.06 0.15 1 114 208 27 HIS CA C 56.46 0.15 1 115 208 27 HIS CB C 29.76 0.15 1 116 208 27 HIS N N 121.13 0.15 1 117 209 28 ILE H H 8.05 0.02 1 118 209 28 ILE C C 176.98 0.15 1 119 209 28 ILE CA C 61.79 0.15 1 120 209 28 ILE CB C 38.64 0.15 1 121 209 28 ILE N N 122.33 0.15 1 122 210 29 THR H H 8.36 0.02 1 123 210 29 THR C C 175.06 0.15 1 124 210 29 THR CA C 62.65 0.15 1 125 210 29 THR CB C 69.98 0.15 1 126 210 29 THR N N 118.66 0.15 1 127 211 30 ALA H H 8.48 0.02 1 128 211 30 ALA C C 179.16 0.15 1 129 211 30 ALA CA C 53.81 0.15 1 130 211 30 ALA CB C 19.05 0.15 1 131 211 30 ALA N N 125.80 0.15 1 132 212 31 GLU H H 8.46 0.02 1 133 212 31 GLU C C 178.00 0.15 1 134 212 31 GLU CA C 57.97 0.15 1 135 212 31 GLU CB C 29.93 0.15 1 136 212 31 GLU N N 119.63 0.15 1 137 213 32 THR H H 8.17 0.02 1 138 213 32 THR C C 175.53 0.15 1 139 213 32 THR CA C 64.14 0.15 1 140 213 32 THR CB C 69.29 0.15 1 141 213 32 THR N N 116.36 0.15 1 142 214 33 ALA H H 8.24 0.02 1 143 214 33 ALA C C 179.03 0.15 1 144 214 33 ALA CA C 54.09 0.15 1 145 214 33 ALA CB C 18.85 0.15 1 146 214 33 ALA N N 125.08 0.15 1 147 215 34 LYS H H 8.08 0.02 1 148 215 34 LYS C C 178.03 0.15 1 149 215 34 LYS CA C 57.92 0.15 1 150 215 34 LYS CB C 32.99 0.15 1 151 215 34 LYS N N 119.23 0.15 1 152 216 35 ARG H H 8.10 0.02 1 153 216 35 ARG C C 177.43 0.15 1 154 216 35 ARG CA C 57.46 0.15 1 155 216 35 ARG CB C 30.65 0.15 1 156 216 35 ARG N N 120.94 0.15 1 157 217 36 ARG H H 8.22 0.02 1 158 217 36 ARG C C 177.34 0.15 1 159 217 36 ARG CA C 57.39 0.15 1 160 217 36 ARG CB C 30.59 0.15 1 161 217 36 ARG N N 121.05 0.15 1 162 218 37 LEU H H 8.12 0.02 1 163 218 37 LEU C C 177.74 0.15 1 164 218 37 LEU CA C 55.67 0.15 1 165 218 37 LEU CB C 42.38 0.15 1 166 218 37 LEU N N 122.19 0.15 1 167 219 38 ALA H H 8.10 0.02 1 168 219 38 ALA C C 178.03 0.15 1 169 219 38 ALA CA C 52.83 0.15 1 170 219 38 ALA CB C 19.14 0.15 1 171 219 38 ALA N N 123.77 0.15 1 172 220 39 ARG H H 8.20 0.02 1 173 220 39 ARG C C 177.02 0.15 1 174 220 39 ARG CA C 56.54 0.15 1 175 220 39 ARG CB C 30.88 0.15 1 176 220 39 ARG N N 119.77 0.15 1 177 221 40 GLY H H 8.35 0.02 1 178 221 40 GLY C C 173.76 0.15 1 179 221 40 GLY CA C 45.00 0.15 1 180 221 40 GLY N N 109.55 0.15 1 181 222 41 SER H H 8.29 0.02 1 182 222 41 SER CA C 56.67 0.15 1 183 222 41 SER CB C 63.27 0.15 1 184 222 41 SER N N 117.20 0.15 1 185 224 43 PRO C C 176.86 0.15 1 186 224 43 PRO CA C 63.04 0.15 1 187 224 43 PRO CB C 32.08 0.15 1 188 225 44 SER H H 8.50 0.02 1 189 225 44 SER C C 174.74 0.15 1 190 225 44 SER CA C 58.09 0.15 1 191 225 44 SER CB C 63.90 0.15 1 192 225 44 SER N N 116.20 0.15 1 193 226 45 LEU H H 8.46 0.02 1 194 226 45 LEU C C 177.44 0.15 1 195 226 45 LEU CA C 55.16 0.15 1 196 226 45 LEU CB C 42.44 0.15 1 197 226 45 LEU N N 124.86 0.15 1 198 227 46 ALA H H 8.39 0.02 1 199 227 46 ALA C C 178.03 0.15 1 200 227 46 ALA CA C 52.76 0.15 1 201 227 46 ALA CB C 19.40 0.15 1 202 227 46 ALA N N 124.97 0.15 1 203 228 47 SER H H 8.35 0.02 1 204 228 47 SER C C 174.94 0.15 1 205 228 47 SER CA C 58.41 0.15 1 206 228 47 SER CB C 63.85 0.15 1 207 228 47 SER N N 115.13 0.15 1 208 229 48 SER H H 8.45 0.02 1 209 229 48 SER C C 174.84 0.15 1 210 229 48 SER CA C 58.52 0.15 1 211 229 48 SER CB C 63.93 0.15 1 212 229 48 SER N N 118.16 0.15 1 213 230 49 SER H H 8.44 0.02 1 214 230 49 SER C C 174.64 0.15 1 215 230 49 SER CA C 58.65 0.15 1 216 230 49 SER CB C 63.87 0.15 1 217 230 49 SER N N 118.08 0.15 1 218 231 50 ALA H H 8.36 0.02 1 219 231 50 ALA C C 178.22 0.15 1 220 231 50 ALA CA C 53.02 0.15 1 221 231 50 ALA CB C 19.33 0.15 1 222 231 50 ALA N N 125.83 0.15 1 223 232 51 SER H H 8.30 0.02 1 224 232 51 SER C C 174.80 0.15 1 225 232 51 SER CA C 58.74 0.15 1 226 232 51 SER CB C 63.72 0.15 1 227 232 51 SER N N 114.81 0.15 1 228 233 52 GLN H H 8.36 0.02 1 229 233 52 GLN C C 176.05 0.15 1 230 233 52 GLN CA C 55.89 0.15 1 231 233 52 GLN CB C 29.48 0.15 1 232 233 52 GLN N N 122.16 0.15 1 233 234 53 LEU H H 8.26 0.02 1 234 234 53 LEU C C 177.45 0.15 1 235 234 53 LEU CA C 55.26 0.15 1 236 234 53 LEU CB C 42.46 0.15 1 237 234 53 LEU N N 122.88 0.15 1 238 235 54 SER H H 8.28 0.02 1 239 235 54 SER C C 173.67 0.15 1 240 235 54 SER CA C 58.05 0.15 1 241 235 54 SER CB C 64.02 0.15 1 242 235 54 SER N N 116.61 0.15 1 243 236 55 ALA H H 8.34 0.02 1 244 236 55 ALA CA C 50.76 0.15 1 245 236 55 ALA CB C 18.49 0.15 1 246 236 55 ALA N N 127.19 0.15 1 247 237 56 PRO C C 176.99 0.15 1 248 237 56 PRO CA C 63.17 0.15 1 249 237 56 PRO CB C 32.09 0.15 1 250 238 57 SER H H 8.48 0.02 1 251 238 57 SER C C 174.73 0.15 1 252 238 57 SER CA C 58.21 0.15 1 253 238 57 SER CB C 63.79 0.15 1 254 238 57 SER N N 116.16 0.15 1 255 239 58 LEU H H 8.42 0.02 1 256 239 58 LEU C C 177.38 0.15 1 257 239 58 LEU CA C 55.18 0.15 1 258 239 58 LEU CB C 42.39 0.15 1 259 239 58 LEU N N 124.86 0.15 1 260 240 59 LYS H H 8.32 0.02 1 261 240 59 LYS C C 176.32 0.15 1 262 240 59 LYS CA C 56.19 0.15 1 263 240 59 LYS CB C 33.17 0.15 1 264 240 59 LYS N N 122.52 0.15 1 265 241 60 ALA H H 8.43 0.02 1 266 241 60 ALA C C 177.98 0.15 1 267 241 60 ALA CA C 52.53 0.15 1 268 241 60 ALA CB C 19.63 0.15 1 269 241 60 ALA N N 125.80 0.15 1 270 242 61 THR H H 8.30 0.02 1 271 242 61 THR C C 174.44 0.15 1 272 242 61 THR CA C 61.88 0.15 1 273 242 61 THR CB C 70.02 0.15 1 274 242 61 THR N N 114.00 0.15 1 275 243 62 CYS H H 8.51 0.02 1 276 243 62 CYS C C 174.79 0.15 1 277 243 62 CYS CA C 58.37 0.15 1 278 243 62 CYS CB C 28.30 0.15 1 279 243 62 CYS N N 122.11 0.15 1 280 244 63 THR H H 8.51 0.02 1 281 244 63 THR C C 174.55 0.15 1 282 244 63 THR CA C 61.88 0.15 1 283 244 63 THR CB C 69.83 0.15 1 284 244 63 THR N N 117.48 0.15 1 285 245 64 THR H H 8.22 0.02 1 286 245 64 THR C C 174.02 0.15 1 287 245 64 THR CA C 61.75 0.15 1 288 245 64 THR CB C 69.98 0.15 1 289 245 64 THR N N 116.66 0.15 1 290 246 65 HIS H H 8.55 0.02 1 291 246 65 HIS C C 174.46 0.15 1 292 246 65 HIS CA C 55.82 0.15 1 293 246 65 HIS CB C 30.08 0.15 1 294 246 65 HIS N N 121.72 0.15 1 295 247 66 HIS H H 8.57 0.02 1 296 247 66 HIS C C 174.25 0.15 1 297 247 66 HIS CA C 55.63 0.15 1 298 247 66 HIS CB C 30.08 0.15 1 299 247 66 HIS N N 121.41 0.15 1 300 248 67 ASP H H 8.63 0.02 1 301 248 67 ASP C C 175.80 0.15 1 302 248 67 ASP CA C 54.38 0.15 1 303 248 67 ASP CB C 41.33 0.15 1 304 248 67 ASP N N 121.89 0.15 1 305 249 68 SER H H 8.38 0.02 1 306 249 68 SER CA C 56.27 0.15 1 307 249 68 SER CB C 63.54 0.15 1 308 249 68 SER N N 116.97 0.15 1 309 250 69 PRO C C 176.81 0.15 1 310 250 69 PRO CA C 63.49 0.15 1 311 250 69 PRO CB C 32.02 0.15 1 312 251 70 ASP H H 8.38 0.02 1 313 251 70 ASP C C 176.45 0.15 1 314 251 70 ASP CA C 54.58 0.15 1 315 251 70 ASP CB C 41.03 0.15 1 316 251 70 ASP N N 120.09 0.15 1 317 252 71 ALA H H 8.24 0.02 1 318 252 71 ALA C C 178.29 0.15 1 319 252 71 ALA CA C 53.63 0.15 1 320 252 71 ALA CB C 19.40 0.15 1 321 252 71 ALA N N 124.27 0.15 1 322 253 72 ASP H H 8.36 0.02 1 323 253 72 ASP C C 176.94 0.15 1 324 253 72 ASP CA C 55.16 0.15 1 325 253 72 ASP CB C 40.76 0.15 1 326 253 72 ASP N N 118.48 0.15 1 327 254 73 LEU H H 7.98 0.02 1 328 254 73 LEU C C 177.91 0.15 1 329 254 73 LEU CA C 55.92 0.15 1 330 254 73 LEU CB C 42.14 0.15 1 331 254 73 LEU N N 122.33 0.15 1 332 255 74 ILE H H 8.02 0.02 1 333 255 74 ILE C C 177.42 0.15 1 334 255 74 ILE CA C 62.38 0.15 1 335 255 74 ILE CB C 38.34 0.15 1 336 255 74 ILE N N 121.69 0.15 1 337 256 75 GLU H H 8.37 0.02 1 338 256 75 GLU C C 177.29 0.15 1 339 256 75 GLU CA C 57.84 0.15 1 340 256 75 GLU CB C 29.86 0.15 1 341 256 75 GLU N N 123.47 0.15 1 342 257 76 ALA H H 8.29 0.02 1 343 257 76 ALA C C 178.69 0.15 1 344 257 76 ALA CA C 53.74 0.15 1 345 257 76 ALA CB C 19.17 0.15 1 346 257 76 ALA N N 123.47 0.15 1 347 258 77 ASN H H 8.29 0.02 1 348 258 77 ASN C C 176.06 0.15 1 349 258 77 ASN CA C 54.13 0.15 1 350 258 77 ASN CB C 38.70 0.15 1 351 258 77 ASN N N 116.95 0.15 1 352 259 78 LEU H H 8.08 0.02 1 353 259 78 LEU C C 178.35 0.15 1 354 259 78 LEU CA C 56.52 0.15 1 355 259 78 LEU CB C 42.22 0.15 1 356 259 78 LEU N N 121.86 0.15 1 357 260 79 LEU H H 8.07 0.02 1 358 260 79 LEU C C 177.94 0.15 1 359 260 79 LEU CA C 56.25 0.15 1 360 260 79 LEU CB C 41.94 0.15 1 361 260 79 LEU N N 120.75 0.15 1 362 261 80 TRP H H 7.99 0.02 1 363 261 80 TRP C C 176.78 0.15 1 364 261 80 TRP CA C 58.42 0.15 1 365 261 80 TRP CB C 29.21 0.15 1 366 261 80 TRP N N 120.56 0.15 1 367 262 81 ARG H H 7.90 0.02 1 368 262 81 ARG C C 176.81 0.15 1 369 262 81 ARG CA C 56.93 0.15 1 370 262 81 ARG CB C 30.84 0.15 1 371 262 81 ARG N N 121.14 0.15 1 372 263 82 GLN H H 8.16 0.02 1 373 263 82 GLN C C 176.80 0.15 1 374 263 82 GLN CA C 56.87 0.15 1 375 263 82 GLN CB C 29.13 0.15 1 376 263 82 GLN N N 120.49 0.15 1 377 264 83 GLU H H 8.44 0.02 1 378 264 83 GLU C C 177.18 0.15 1 379 264 83 GLU CA C 57.11 0.15 1 380 264 83 GLU CB C 30.06 0.15 1 381 264 83 GLU N N 121.38 0.15 1 382 265 84 MET H H 8.32 0.02 1 383 265 84 MET C C 177.20 0.15 1 384 265 84 MET CA C 55.66 0.15 1 385 265 84 MET CB C 32.50 0.15 1 386 265 84 MET N N 120.12 0.15 1 387 266 85 GLY H H 8.30 0.02 1 388 266 85 GLY C C 174.67 0.15 1 389 266 85 GLY CA C 45.47 0.15 1 390 266 85 GLY N N 109.28 0.15 1 391 267 86 GLY H H 8.29 0.02 1 392 267 86 GLY C C 173.87 0.15 1 393 267 86 GLY CA C 45.18 0.15 1 394 267 86 GLY N N 108.38 0.15 1 395 268 87 ASN H H 8.41 0.02 1 396 268 87 ASN C C 175.13 0.15 1 397 268 87 ASN CA C 53.23 0.15 1 398 268 87 ASN CB C 38.97 0.15 1 399 268 87 ASN N N 118.70 0.15 1 400 269 88 ILE H H 8.20 0.02 1 401 269 88 ILE C C 176.41 0.15 1 402 269 88 ILE CA C 61.15 0.15 1 403 269 88 ILE CB C 38.89 0.15 1 404 269 88 ILE N N 121.22 0.15 1 405 270 89 THR H H 8.39 0.02 1 406 270 89 THR C C 174.15 0.15 1 407 270 89 THR CA C 62.11 0.15 1 408 270 89 THR CB C 69.96 0.15 1 409 270 89 THR N N 119.66 0.15 1 410 271 90 ARG H H 8.48 0.02 1 411 271 90 ARG C C 176.05 0.15 1 412 271 90 ARG CA C 56.01 0.15 1 413 271 90 ARG CB C 31.10 0.15 1 414 271 90 ARG N N 124.97 0.15 1 415 272 91 VAL H H 8.39 0.02 1 416 272 91 VAL C C 176.40 0.15 1 417 272 91 VAL CA C 62.43 0.15 1 418 272 91 VAL CB C 32.84 0.15 1 419 272 91 VAL N N 123.00 0.15 1 420 273 92 GLU H H 8.68 0.02 1 421 273 92 GLU C C 176.65 0.15 1 422 273 92 GLU CA C 56.66 0.15 1 423 273 92 GLU CB C 30.34 0.15 1 424 273 92 GLU N N 125.38 0.15 1 425 274 93 SER H H 8.45 0.02 1 426 274 93 SER C C 174.65 0.15 1 427 274 93 SER CA C 58.58 0.15 1 428 274 93 SER CB C 63.79 0.15 1 429 274 93 SER N N 116.91 0.15 1 430 275 94 GLU H H 8.53 0.02 1 431 275 94 GLU C C 176.17 0.15 1 432 275 94 GLU CA C 56.72 0.15 1 433 275 94 GLU CB C 30.41 0.15 1 434 275 94 GLU N N 122.72 0.15 1 435 276 95 ASN H H 8.48 0.02 1 436 276 95 ASN C C 174.86 0.15 1 437 276 95 ASN CA C 53.17 0.15 1 438 276 95 ASN CB C 38.87 0.15 1 439 276 95 ASN N N 119.80 0.15 1 440 277 96 LYS H H 8.32 0.02 1 441 277 96 LYS C C 176.27 0.15 1 442 277 96 LYS CA C 56.18 0.15 1 443 277 96 LYS CB C 33.18 0.15 1 444 277 96 LYS N N 122.42 0.15 1 445 278 97 VAL H H 8.28 0.02 1 446 278 97 VAL C C 175.88 0.15 1 447 278 97 VAL CA C 62.46 0.15 1 448 278 97 VAL CB C 32.76 0.15 1 449 278 97 VAL N N 123.14 0.15 1 450 279 98 VAL H H 8.43 0.02 1 451 279 98 VAL C C 175.64 0.15 1 452 279 98 VAL CA C 62.19 0.15 1 453 279 98 VAL CB C 33.07 0.15 1 454 279 98 VAL N N 126.77 0.15 1 455 280 99 ILE H H 8.51 0.02 1 456 280 99 ILE C C 176.05 0.15 1 457 280 99 ILE CA C 60.48 0.15 1 458 280 99 ILE CB C 38.41 0.15 1 459 280 99 ILE N N 127.56 0.15 1 460 281 100 LEU H H 8.53 0.02 1 461 281 100 LEU C C 176.88 0.15 1 462 281 100 LEU CA C 54.78 0.15 1 463 281 100 LEU CB C 42.63 0.15 1 464 281 100 LEU N N 128.19 0.15 1 465 282 101 ASP H H 8.42 0.02 1 466 282 101 ASP C C 175.96 0.15 1 467 282 101 ASP CA C 54.31 0.15 1 468 282 101 ASP CB C 41.38 0.15 1 469 282 101 ASP N N 121.89 0.15 1 470 283 102 SER H H 8.21 0.02 1 471 283 102 SER C C 173.96 0.15 1 472 283 102 SER CA C 58.09 0.15 1 473 283 102 SER CB C 63.91 0.15 1 474 283 102 SER N N 115.84 0.15 1 475 284 103 PHE H H 8.33 0.02 1 476 284 103 PHE C C 175.18 0.15 1 477 284 103 PHE CA C 57.57 0.15 1 478 284 103 PHE CB C 39.77 0.15 1 479 284 103 PHE N N 122.24 0.15 1 480 285 104 GLU H H 8.25 0.02 1 481 285 104 GLU CA C 53.84 0.15 1 482 285 104 GLU CB C 30.18 0.15 1 483 285 104 GLU N N 124.77 0.15 1 484 286 105 PRO C C 176.67 0.15 1 485 286 105 PRO CA C 62.85 0.15 1 486 286 105 PRO CB C 32.22 0.15 1 487 287 106 LEU H H 8.44 0.02 1 488 287 106 LEU C C 177.28 0.15 1 489 287 106 LEU CA C 55.17 0.15 1 490 287 106 LEU CB C 42.38 0.15 1 491 287 106 LEU N N 122.02 0.15 1 492 288 107 HIS H H 8.56 0.02 1 493 288 107 HIS C C 174.21 0.15 1 494 288 107 HIS CA C 55.11 0.15 1 495 288 107 HIS CB C 29.73 0.15 1 496 288 107 HIS N N 119.98 0.15 1 497 289 108 ALA H H 8.57 0.02 1 498 289 108 ALA C C 177.27 0.15 1 499 289 108 ALA CA C 52.27 0.15 1 500 289 108 ALA CB C 19.80 0.15 1 501 289 108 ALA N N 126.55 0.15 1 502 290 109 ASP H H 8.57 0.02 1 503 290 109 ASP C C 176.82 0.15 1 504 290 109 ASP CA C 54.64 0.15 1 505 290 109 ASP CB C 41.33 0.15 1 506 290 109 ASP N N 120.31 0.15 1 507 291 110 GLY H H 8.47 0.02 1 508 291 110 GLY C C 174.03 0.15 1 509 291 110 GLY CA C 45.35 0.15 1 510 291 110 GLY N N 109.64 0.15 1 511 292 111 ASP H H 8.30 0.02 1 512 292 111 ASP C C 176.60 0.15 1 513 292 111 ASP CA C 54.37 0.15 1 514 292 111 ASP CB C 41.35 0.15 1 515 292 111 ASP N N 120.83 0.15 1 516 293 112 GLU H H 8.64 0.02 1 517 293 112 GLU C C 177.15 0.15 1 518 293 112 GLU CA C 57.44 0.15 1 519 293 112 GLU CB C 29.84 0.15 1 520 293 112 GLU N N 121.84 0.15 1 521 294 113 ARG H H 8.35 0.02 1 522 294 113 ARG C C 176.90 0.15 1 523 294 113 ARG CA C 57.03 0.15 1 524 294 113 ARG CB C 30.53 0.15 1 525 294 113 ARG N N 121.38 0.15 1 526 295 114 GLU H H 8.38 0.02 1 527 295 114 GLU C C 177.37 0.15 1 528 295 114 GLU CA C 57.30 0.15 1 529 295 114 GLU CB C 30.12 0.15 1 530 295 114 GLU N N 121.05 0.15 1 531 296 115 ILE H H 8.25 0.02 1 532 296 115 ILE C C 177.01 0.15 1 533 296 115 ILE CA C 62.19 0.15 1 534 296 115 ILE CB C 38.52 0.15 1 535 296 115 ILE N N 121.80 0.15 1 536 297 116 SER H H 8.32 0.02 1 537 297 116 SER C C 175.53 0.15 1 538 297 116 SER CA C 59.06 0.15 1 539 297 116 SER CB C 63.66 0.15 1 540 297 116 SER N N 119.36 0.15 1 541 298 117 VAL H H 8.33 0.02 1 542 298 117 VAL C C 177.47 0.15 1 543 298 117 VAL CA C 64.48 0.15 1 544 298 117 VAL CB C 32.42 0.15 1 545 298 117 VAL N N 123.47 0.15 1 546 299 118 ALA H H 8.26 0.02 1 547 299 118 ALA C C 179.52 0.15 1 548 299 118 ALA CA C 54.21 0.15 1 549 299 118 ALA CB C 18.64 0.15 1 550 299 118 ALA N N 124.05 0.15 1 551 300 119 ALA H H 8.23 0.02 1 552 300 119 ALA C C 179.73 0.15 1 553 300 119 ALA CA C 54.25 0.15 1 554 300 119 ALA CB C 18.75 0.15 1 555 300 119 ALA N N 121.75 0.15 1 556 301 120 GLU H H 8.20 0.02 1 557 301 120 GLU C C 178.07 0.15 1 558 301 120 GLU CA C 58.16 0.15 1 559 301 120 GLU CB C 29.54 0.15 1 560 301 120 GLU N N 120.45 0.15 1 561 302 121 ILE H H 8.00 0.02 1 562 302 121 ILE C C 178.52 0.15 1 563 302 121 ILE CA C 63.85 0.15 1 564 302 121 ILE CB C 38.38 0.15 1 565 302 121 ILE N N 120.97 0.15 1 566 303 122 LEU H H 7.88 0.02 1 567 303 122 LEU CA C 56.87 0.15 1 568 303 122 LEU N N 122.17 0.15 1 569 304 123 ARG C C 178.15 0.15 1 570 304 123 ARG CA C 58.45 0.15 1 571 304 123 ARG CB C 30.68 0.15 1 572 305 124 LYS H H 8.14 0.02 1 573 305 124 LYS C C 177.48 0.15 1 574 305 124 LYS CA C 57.82 0.15 1 575 305 124 LYS CB C 33.21 0.15 1 576 305 124 LYS N N 119.44 0.15 1 577 306 125 SER H H 8.04 0.02 1 578 306 125 SER C C 174.70 0.15 1 579 306 125 SER CA C 59.20 0.15 1 580 306 125 SER CB C 63.73 0.15 1 581 306 125 SER N N 115.27 0.15 1 582 307 126 ARG H H 7.96 0.02 1 583 307 126 ARG C C 175.99 0.15 1 584 307 126 ARG CA C 56.39 0.15 1 585 307 126 ARG CB C 30.73 0.15 1 586 307 126 ARG N N 122.05 0.15 1 587 308 127 LYS H H 8.09 0.02 1 588 308 127 LYS C C 175.88 0.15 1 589 308 127 LYS CA C 56.12 0.15 1 590 308 127 LYS CB C 33.10 0.15 1 591 308 127 LYS N N 121.38 0.15 1 592 309 128 PHE H H 8.27 0.02 1 593 309 128 PHE CA C 55.45 0.15 1 594 309 128 PHE CB C 39.22 0.15 1 595 309 128 PHE N N 121.50 0.15 1 596 310 129 PRO C C 176.92 0.15 1 597 310 129 PRO CA C 63.20 0.15 1 598 310 129 PRO CB C 32.12 0.15 1 599 311 130 SER H H 8.47 0.02 1 600 311 130 SER C C 174.21 0.15 1 601 311 130 SER CA C 58.50 0.15 1 602 311 130 SER CB C 63.96 0.15 1 603 311 130 SER N N 116.55 0.15 1 604 312 131 ALA H H 8.41 0.02 1 605 312 131 ALA C C 177.38 0.15 1 606 312 131 ALA CA C 52.10 0.15 1 607 312 131 ALA CB C 19.71 0.15 1 608 312 131 ALA N N 125.75 0.15 1 609 313 132 LEU H H 8.17 0.02 1 610 313 132 LEU CA C 52.81 0.15 1 611 313 132 LEU CB C 41.93 0.15 1 612 313 132 LEU N N 123.00 0.15 1 613 314 133 PRO C C 177.28 0.15 1 614 314 133 PRO CA C 62.40 0.15 1 615 314 133 PRO CB C 31.82 0.15 1 616 315 134 ILE H H 8.32 0.02 1 617 315 134 ILE CA C 62.76 0.15 1 618 315 134 ILE CB C 38.68 0.15 1 619 315 134 ILE N N 120.45 0.15 1 620 316 135 TRP C C 175.70 0.15 1 621 316 135 TRP CA C 56.26 0.15 1 622 316 135 TRP CB C 29.15 0.15 1 623 317 136 ALA H H 7.57 0.02 1 624 317 136 ALA C C 176.59 0.15 1 625 317 136 ALA CA C 51.56 0.15 1 626 317 136 ALA CB C 19.85 0.15 1 627 317 136 ALA N N 125.09 0.15 1 628 318 137 ARG H H 7.74 0.02 1 629 318 137 ARG CA C 54.42 0.15 1 630 318 137 ARG CB C 31.49 0.15 1 631 318 137 ARG N N 120.86 0.15 1 632 319 138 PRO C C 176.42 0.15 1 633 319 138 PRO CA C 63.73 0.15 1 634 319 138 PRO CB C 32.09 0.15 1 635 320 139 ASP H H 8.35 0.02 1 636 320 139 ASP C C 175.52 0.15 1 637 320 139 ASP CA C 53.77 0.15 1 638 320 139 ASP CB C 40.55 0.15 1 639 320 139 ASP N N 117.91 0.15 1 640 321 140 TYR H H 7.87 0.02 1 641 321 140 TYR C C 174.81 0.15 1 642 321 140 TYR CA C 58.06 0.15 1 643 321 140 TYR CB C 39.08 0.15 1 644 321 140 TYR N N 120.97 0.15 1 645 322 141 ASN H H 8.27 0.02 1 646 322 141 ASN CA C 50.55 0.15 1 647 322 141 ASN CB C 39.57 0.15 1 648 322 141 ASN N N 124.52 0.15 1 649 324 143 PRO C C 176.67 0.15 1 650 324 143 PRO CA C 62.69 0.15 1 651 324 143 PRO CB C 32.15 0.15 1 652 325 144 LEU H H 8.37 0.02 1 653 325 144 LEU C C 177.32 0.15 1 654 325 144 LEU CA C 55.08 0.15 1 655 325 144 LEU CB C 42.40 0.15 1 656 325 144 LEU N N 122.61 0.15 1 657 326 145 LEU H H 8.30 0.02 1 658 326 145 LEU C C 177.28 0.15 1 659 326 145 LEU CA C 54.98 0.15 1 660 326 145 LEU CB C 42.51 0.15 1 661 326 145 LEU N N 123.66 0.15 1 662 327 146 GLU H H 8.52 0.02 1 663 327 146 GLU C C 176.71 0.15 1 664 327 146 GLU CA C 56.42 0.15 1 665 327 146 GLU CB C 30.07 0.15 1 666 327 146 GLU N N 122.09 0.15 1 667 328 147 SER H H 8.31 0.02 1 668 328 147 SER C C 174.24 0.15 1 669 328 147 SER CA C 58.92 0.15 1 670 328 147 SER CB C 63.52 0.15 1 671 328 147 SER N N 117.17 0.15 1 672 329 148 TRP H H 7.93 0.02 1 673 329 148 TRP C C 175.72 0.15 1 674 329 148 TRP CA C 57.62 0.15 1 675 329 148 TRP CB C 29.06 0.15 1 676 329 148 TRP N N 121.97 0.15 1 677 330 149 LYS H H 7.55 0.02 1 678 330 149 LYS C C 175.04 0.15 1 679 330 149 LYS CA C 55.37 0.15 1 680 330 149 LYS CB C 33.53 0.15 1 681 330 149 LYS N N 123.38 0.15 1 682 331 150 ASP H H 8.00 0.02 1 683 331 150 ASP CA C 52.10 0.15 1 684 331 150 ASP CB C 41.40 0.15 1 685 331 150 ASP N N 123.27 0.15 1 686 332 151 PRO C C 176.87 0.15 1 687 332 151 PRO CA C 63.84 0.15 1 688 332 151 PRO CB C 32.15 0.15 1 689 333 152 ASP H H 8.41 0.02 1 690 333 152 ASP C C 175.69 0.15 1 691 333 152 ASP CA C 54.14 0.15 1 692 333 152 ASP CB C 41.07 0.15 1 693 333 152 ASP N N 118.27 0.15 1 694 334 153 TYR H H 7.74 0.02 1 695 334 153 TYR C C 174.84 0.15 1 696 334 153 TYR CA C 58.72 0.15 1 697 334 153 TYR CB C 39.07 0.15 1 698 334 153 TYR N N 121.58 0.15 1 699 335 154 VAL H H 7.80 0.02 1 700 335 154 VAL CA C 58.79 0.15 1 701 335 154 VAL CB C 33.87 0.15 1 702 335 154 VAL N N 129.52 0.15 1 703 337 156 PRO C C 176.65 0.15 1 704 337 156 PRO CA C 62.56 0.15 1 705 337 156 PRO CB C 32.16 0.15 1 706 338 157 VAL H H 8.30 0.02 1 707 338 157 VAL C C 176.06 0.15 1 708 338 157 VAL CA C 62.29 0.15 1 709 338 157 VAL CB C 32.91 0.15 1 710 338 157 VAL N N 121.58 0.15 1 711 339 158 VAL H H 8.39 0.02 1 712 339 158 VAL C C 175.78 0.15 1 713 339 158 VAL CA C 61.95 0.15 1 714 339 158 VAL CB C 33.02 0.15 1 715 339 158 VAL N N 125.88 0.15 1 716 340 159 HIS H H 8.70 0.02 1 717 340 159 HIS C C 175.43 0.15 1 718 340 159 HIS CA C 55.92 0.15 1 719 340 159 HIS CB C 30.34 0.15 1 720 340 159 HIS N N 124.69 0.15 1 721 341 160 GLY H H 8.63 0.02 1 722 341 160 GLY C C 173.49 0.15 1 723 341 160 GLY CA C 44.98 0.15 1 724 341 160 GLY N N 110.97 0.15 1 725 342 161 CYS H H 8.32 0.02 1 726 342 161 CYS CA C 56.46 0.15 1 727 342 161 CYS CB C 27.75 0.15 1 728 342 161 CYS N N 120.74 0.15 1 729 343 162 PRO C C 176.53 0.15 1 730 343 162 PRO CA C 62.97 0.15 1 731 343 162 PRO CB C 32.15 0.15 1 732 344 163 LEU H H 8.45 0.02 1 733 344 163 LEU CA C 52.95 0.15 1 734 344 163 LEU CB C 41.63 0.15 1 735 344 163 LEU N N 124.16 0.15 1 736 346 165 PRO C C 177.10 0.15 1 737 346 165 PRO CA C 62.80 0.15 1 738 346 165 PRO CB C 32.06 0.15 1 739 347 166 THR H H 8.36 0.02 1 740 347 166 THR C C 174.37 0.15 1 741 347 166 THR CA C 61.95 0.15 1 742 347 166 THR CB C 70.06 0.15 1 743 347 166 THR N N 115.55 0.15 1 744 348 167 LYS H H 8.43 0.02 1 745 348 167 LYS C C 175.71 0.15 1 746 348 167 LYS CA C 55.87 0.15 1 747 348 167 LYS CB C 33.40 0.15 1 748 348 167 LYS N N 124.61 0.15 1 749 349 168 ALA H H 8.48 0.02 1 750 349 168 ALA CA C 50.45 0.15 1 751 349 168 ALA CB C 19.27 0.15 1 752 349 168 ALA N N 127.87 0.15 1 753 351 170 PRO C C 176.61 0.15 1 754 351 170 PRO CA C 62.59 0.15 1 755 351 170 PRO CB C 32.04 0.15 1 756 352 171 ILE H H 8.37 0.02 1 757 352 171 ILE CA C 58.57 0.15 1 758 352 171 ILE CB C 38.82 0.15 1 759 352 171 ILE N N 123.12 0.15 1 760 355 174 PRO C C 176.82 0.15 1 761 355 174 PRO CA C 62.71 0.15 1 762 355 174 PRO CB C 32.13 0.15 1 763 356 175 ARG H H 8.55 0.02 1 764 356 175 ARG C C 176.41 0.15 1 765 356 175 ARG CA C 55.98 0.15 1 766 356 175 ARG CB C 31.06 0.15 1 767 356 175 ARG N N 121.99 0.15 1 768 357 176 ARG H H 8.57 0.02 1 769 357 176 ARG C C 176.18 0.15 1 770 357 176 ARG CA C 55.91 0.15 1 771 357 176 ARG CB C 31.16 0.15 1 772 357 176 ARG N N 123.52 0.15 1 773 358 177 LYS H H 8.60 0.02 1 774 358 177 LYS C C 176.47 0.15 1 775 358 177 LYS CA C 56.29 0.15 1 776 358 177 LYS CB C 33.30 0.15 1 777 358 177 LYS N N 124.31 0.15 1 778 359 178 ARG H H 8.66 0.02 1 779 359 178 ARG C C 176.39 0.15 1 780 359 178 ARG CA C 56.04 0.15 1 781 359 178 ARG CB C 31.10 0.15 1 782 359 178 ARG N N 123.91 0.15 1 783 360 179 THR H H 8.48 0.02 1 784 360 179 THR C C 174.20 0.15 1 785 360 179 THR CA C 62.18 0.15 1 786 360 179 THR CB C 69.89 0.15 1 787 360 179 THR N N 118.23 0.15 1 788 361 180 VAL H H 8.38 0.02 1 789 361 180 VAL C C 175.65 0.15 1 790 361 180 VAL CA C 62.23 0.15 1 791 361 180 VAL CB C 33.09 0.15 1 792 361 180 VAL N N 124.63 0.15 1 793 362 181 VAL H H 8.45 0.02 1 794 362 181 VAL C C 176.01 0.15 1 795 362 181 VAL CA C 62.18 0.15 1 796 362 181 VAL CB C 32.85 0.15 1 797 362 181 VAL N N 126.30 0.15 1 798 363 182 LEU H H 8.61 0.02 1 799 363 182 LEU C C 177.35 0.15 1 800 363 182 LEU CA C 55.03 0.15 1 801 363 182 LEU CB C 42.44 0.15 1 802 363 182 LEU N N 127.74 0.15 1 803 364 183 THR H H 8.23 0.02 1 804 364 183 THR C C 174.44 0.15 1 805 364 183 THR CA C 61.71 0.15 1 806 364 183 THR CB C 69.95 0.15 1 807 364 183 THR N N 115.55 0.15 1 808 365 184 GLU H H 8.53 0.02 1 809 365 184 GLU C C 176.33 0.15 1 810 365 184 GLU CA C 56.48 0.15 1 811 365 184 GLU CB C 30.53 0.15 1 812 365 184 GLU N N 123.47 0.15 1 813 366 185 SER H H 8.47 0.02 1 814 366 185 SER C C 174.14 0.15 1 815 366 185 SER CA C 58.28 0.15 1 816 366 185 SER CB C 63.96 0.15 1 817 366 185 SER N N 116.98 0.15 1 818 367 186 ASN H H 8.60 0.02 1 819 367 186 ASN C C 174.96 0.15 1 820 367 186 ASN CA C 53.29 0.15 1 821 367 186 ASN CB C 39.03 0.15 1 822 367 186 ASN N N 121.30 0.15 1 823 368 187 VAL H H 8.18 0.02 1 824 368 187 VAL C C 175.47 0.15 1 825 368 187 VAL CA C 62.19 0.15 1 826 368 187 VAL CB C 33.05 0.15 1 827 368 187 VAL N N 120.24 0.15 1 828 369 188 SER H H 8.09 0.02 1 829 369 188 SER CA C 60.05 0.15 1 830 369 188 SER CB C 64.95 0.15 1 831 369 188 SER N N 125.39 0.15 1 stop_ save_