data_27270 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments of NS5A-D2 from Hepatitis C virus (JFH-1) phosphorylated by Casein Kinase II ; _BMRB_accession_number 27270 _BMRB_flat_file_name bmr27270.str _Entry_type original _Submission_date 2017-10-03 _Accession_date 2017-10-03 _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 Hanoulle Xavier . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 80 "13C chemical shifts" 278 "15N chemical shifts" 80 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-06-22 update BMRB 'update entry citation' 2017-10-31 original author 'original release' stop_ _Original_release_date 2017-10-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29876401 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bessa Luiza M. . 2 Schneider Robert . . 3 Hanoulle Xavier . . stop_ _Journal_abbreviation 'Data Brief' _Journal_volume 17 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last 325 _Year 333 _Details 2018 loop_ _Keyword CK2 CKII HCV NMR NS5A stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name pNS5A-D2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label pNS5A-D2 $pNS5A-D2 stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_pNS5A-D2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common pNS5A-D2 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Involved in HCV RNA replication' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 103 _Mol_residue_sequence ; MNTYDVDMVDANLLMEGGVA QTEPESRVPVLDFLEPMAEE EXDLEPSIPSECMLPRSGFP RALPAWARPDYNPPLVESWR RPDYQPPTVAGCALPLQHHH HHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 247 MET 2 248 ASN 3 249 THR 4 250 TYR 5 251 ASP 6 252 VAL 7 253 ASP 8 254 MET 9 255 VAL 10 256 ASP 11 257 ALA 12 258 ASN 13 259 LEU 14 260 LEU 15 261 MET 16 262 GLU 17 263 GLY 18 264 GLY 19 265 VAL 20 266 ALA 21 267 GLN 22 268 THR 23 269 GLU 24 270 PRO 25 271 GLU 26 272 SER 27 273 ARG 28 274 VAL 29 275 PRO 30 276 VAL 31 277 LEU 32 278 ASP 33 279 PHE 34 280 LEU 35 281 GLU 36 282 PRO 37 283 MET 38 284 ALA 39 285 GLU 40 286 GLU 41 287 GLU 42 288 SEP 43 289 ASP 44 290 LEU 45 291 GLU 46 292 PRO 47 293 SER 48 294 ILE 49 295 PRO 50 296 SER 51 297 GLU 52 298 CYS 53 299 MET 54 300 LEU 55 301 PRO 56 302 ARG 57 303 SER 58 304 GLY 59 305 PHE 60 306 PRO 61 307 ARG 62 308 ALA 63 309 LEU 64 310 PRO 65 311 ALA 66 312 TRP 67 313 ALA 68 314 ARG 69 315 PRO 70 316 ASP 71 317 TYR 72 318 ASN 73 319 PRO 74 320 PRO 75 321 LEU 76 322 VAL 77 323 GLU 78 324 SER 79 325 TRP 80 326 ARG 81 327 ARG 82 328 PRO 83 329 ASP 84 330 TYR 85 331 GLN 86 332 PRO 87 333 PRO 88 334 THR 89 335 VAL 90 336 ALA 91 337 GLY 92 338 CYS 93 339 ALA 94 340 LEU 95 341 PRO 96 342 LEU 97 343 GLN 98 344 HIS 99 345 HIS 100 346 HIS 101 347 HIS 102 348 HIS 103 349 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value Swiss-Prot Q99IB8 POLG_HCVJF . . . . . GB AB047639 'Hepatitis C virus (isolate JFH-1) genomic RNA, complete genome' . . . . . stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_SEP _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common PHOSPHOSERINE _BMRB_code SEP _PDB_code SEP _Standard_residue_derivative . _Molecular_mass 185.072 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? OG OG O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HXT HXT H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB OG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING OG P ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $pNS5A-D2 'Hepatitis C' 11103 Viruses . Hepacivirus 'Hepatitis C' JFH-1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $pNS5A-D2 'recombinant technology' . Escherichia coli BL21(DE3) pT7.7 'pNS5A-D2 corresponds to recombinant NS5A-D2 phosphorylated by CKII in vitro.' 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 $pNS5A-D2 250 uM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 30 mM 'natural abundance' THP 1 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_In_house_product_plane_algorithm _Saveframe_category software _Name In_house_product_plane_algorithm _Version . loop_ _Vendor _Address _Electronic_address 'in-house software' . . stop_ loop_ _Task 'chemical shift calculation' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceIII _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_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_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HN(CA)NNH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)NNH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.03 . M pH 6.3 . 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 'Referenced using TMSP' 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 TMSP C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 TMSP H 1 'methyl protons' ppm 0 internal direct . . . 1 TMSP N 15 'methyl protons' ppm 0 internal 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 'The first MET residue does not have assignments.' loop_ _Software_label $In_house_product_plane_algorithm stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D HN(CO)CACB' '3D HNCO' '3D HN(CA)CO' '3D HN(CA)NNH' 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 pNS5A-D2 _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 1 248 2 ASN C C 175.073 0.100 1 2 248 2 ASN CA C 53.229 0.500 1 3 248 2 ASN CB C 39.063 0.500 1 4 249 3 THR H H 8.238 0.007 1 5 249 3 THR C C 174.132 0.100 1 6 249 3 THR CA C 62.231 0.500 1 7 249 3 THR CB C 69.620 0.500 1 8 249 3 THR N N 114.659 0.100 1 9 250 4 TYR H H 8.102 0.007 1 10 250 4 TYR C C 175.388 0.100 1 11 250 4 TYR CA C 57.727 0.500 1 12 250 4 TYR CB C 38.652 0.500 1 13 250 4 TYR N N 121.086 0.100 1 14 251 5 ASP H H 8.199 0.007 1 15 251 5 ASP C C 176.267 0.100 1 16 251 5 ASP CA C 54.584 0.500 1 17 251 5 ASP CB C 41.251 0.500 1 18 251 5 ASP N N 122.049 0.100 1 19 252 6 VAL H H 7.980 0.007 1 20 252 6 VAL C C 175.890 0.100 1 21 252 6 VAL CA C 62.674 0.500 1 22 252 6 VAL CB C 32.738 0.500 1 23 252 6 VAL N N 119.328 0.100 1 24 253 7 ASP H H 8.355 0.007 1 25 253 7 ASP C C 176.269 0.100 1 26 253 7 ASP CA C 54.815 0.500 1 27 253 7 ASP CB C 41.046 0.500 1 28 253 7 ASP N N 122.486 0.100 1 29 254 8 MET H H 8.147 0.007 1 30 254 8 MET C C 176.196 0.100 1 31 254 8 MET CA C 55.505 0.500 1 32 254 8 MET CB C 32.726 0.500 1 33 254 8 MET N N 120.754 0.100 1 34 255 9 VAL H H 8.087 0.007 1 35 255 9 VAL C C 175.936 0.100 1 36 255 9 VAL CA C 62.866 0.500 1 37 255 9 VAL CB C 32.627 0.500 1 38 255 9 VAL N N 121.519 0.100 1 39 256 10 ASP H H 8.361 0.007 1 40 256 10 ASP C C 176.487 0.100 1 41 256 10 ASP CA C 54.629 0.500 1 42 256 10 ASP CB C 41.112 0.500 1 43 256 10 ASP N N 123.881 0.100 1 44 257 11 ALA H H 8.333 0.007 1 45 257 11 ALA C C 178.260 0.100 1 46 257 11 ALA CA C 53.560 0.500 1 47 257 11 ALA CB C 18.955 0.500 1 48 257 11 ALA N N 125.424 0.100 1 49 258 12 ASN H H 8.470 0.007 1 50 258 12 ASN C C 175.730 0.100 1 51 258 12 ASN CA C 53.943 0.500 1 52 258 12 ASN CB C 38.494 0.500 1 53 258 12 ASN N N 116.472 0.100 1 54 259 13 LEU H H 7.922 0.007 1 55 259 13 LEU C C 177.596 0.100 1 56 259 13 LEU CA C 55.891 0.500 1 57 259 13 LEU CB C 42.111 0.500 1 58 259 13 LEU N N 121.286 0.100 1 59 260 14 LEU H H 7.979 0.007 1 60 260 14 LEU C C 177.430 0.100 1 61 260 14 LEU CA C 55.162 0.500 1 62 260 14 LEU CB C 41.949 0.500 1 63 260 14 LEU N N 121.433 0.100 1 64 261 15 MET H H 8.135 0.007 1 65 261 15 MET C C 176.446 0.100 1 66 261 15 MET CA C 55.564 0.500 1 67 261 15 MET CB C 32.770 0.500 1 68 261 15 MET N N 120.462 0.100 1 69 262 16 GLU H H 8.400 0.007 1 70 262 16 GLU C C 177.102 0.100 1 71 262 16 GLU CA C 56.991 0.500 1 72 262 16 GLU CB C 30.157 0.500 1 73 262 16 GLU N N 122.077 0.100 1 74 263 17 GLY H H 8.483 0.007 1 75 263 17 GLY C C 174.758 0.100 1 76 263 17 GLY CA C 45.384 0.500 1 77 263 17 GLY N N 110.224 0.100 1 78 264 18 GLY H H 8.260 0.007 1 79 264 18 GLY C C 173.968 0.100 1 80 264 18 GLY CA C 44.978 0.500 1 81 264 18 GLY N N 108.609 0.100 1 82 265 19 VAL H H 7.979 0.007 1 83 265 19 VAL C C 175.916 0.100 1 84 265 19 VAL CA C 62.091 0.500 1 85 265 19 VAL CB C 32.905 0.500 1 86 265 19 VAL N N 119.035 0.100 1 87 266 20 ALA H H 8.443 0.007 1 88 266 20 ALA C C 177.596 0.100 1 89 266 20 ALA CA C 52.340 0.500 1 90 266 20 ALA CB C 19.122 0.500 1 91 266 20 ALA N N 127.968 0.100 1 92 267 21 GLN H H 8.429 0.007 1 93 267 21 GLN C C 176.066 0.100 1 94 267 21 GLN CA C 55.838 0.500 1 95 267 21 GLN CB C 29.510 0.500 1 96 267 21 GLN N N 120.307 0.100 1 97 268 22 THR H H 8.212 0.007 1 98 268 22 THR C C 174.355 0.100 1 99 268 22 THR CA C 61.825 0.500 1 100 268 22 THR CB C 70.000 0.500 1 101 268 22 THR N N 115.748 0.100 1 102 269 23 GLU H H 8.486 0.007 1 103 269 23 GLU C C 174.682 0.100 1 104 269 23 GLU CA C 54.594 0.500 1 105 269 23 GLU CB C 29.570 0.500 1 106 269 23 GLU N N 124.619 0.100 1 107 270 24 PRO C C 177.075 0.100 1 108 270 24 PRO CA C 63.460 0.500 1 109 270 24 PRO CB C 31.998 0.500 1 110 271 25 GLU H H 8.579 0.007 1 111 271 25 GLU C C 176.663 0.100 1 112 271 25 GLU CA C 56.940 0.500 1 113 271 25 GLU CB C 30.083 0.500 1 114 271 25 GLU N N 120.818 0.100 1 115 272 26 SER H H 8.333 0.007 1 116 272 26 SER C C 174.395 0.100 1 117 272 26 SER CA C 58.408 0.500 1 118 272 26 SER CB C 63.764 0.500 1 119 272 26 SER N N 116.881 0.100 1 120 273 27 ARG H H 8.373 0.007 1 121 273 27 ARG C C 176.016 0.100 1 122 273 27 ARG CA C 55.988 0.500 1 123 273 27 ARG CB C 30.808 0.500 1 124 273 27 ARG N N 123.518 0.100 1 125 274 28 VAL H H 8.177 0.007 1 126 274 28 VAL C C 174.471 0.100 1 127 274 28 VAL CA C 60.146 0.500 1 128 274 28 VAL CB C 32.450 0.500 1 129 274 28 VAL N N 123.187 0.100 1 130 275 29 PRO C C 176.542 0.100 1 131 275 29 PRO CA C 63.292 0.500 1 132 275 29 PRO CB C 32.075 0.500 1 133 276 30 VAL H H 8.211 0.007 1 134 276 30 VAL C C 176.130 0.100 1 135 276 30 VAL CA C 62.535 0.500 1 136 276 30 VAL CB C 32.387 0.500 1 137 276 30 VAL N N 121.006 0.100 1 138 277 31 LEU H H 8.305 0.007 1 139 277 31 LEU C C 176.699 0.100 1 140 277 31 LEU CA C 54.889 0.500 1 141 277 31 LEU CB C 42.456 0.500 1 142 277 31 LEU N N 126.370 0.100 1 143 278 32 ASP H H 8.173 0.007 1 144 278 32 ASP C C 175.566 0.100 1 145 278 32 ASP CA C 54.341 0.500 1 146 278 32 ASP CB C 41.194 0.500 1 147 278 32 ASP N N 121.016 0.100 1 148 279 33 PHE H H 8.034 0.007 1 149 279 33 PHE C C 175.077 0.100 1 150 279 33 PHE CA C 57.639 0.500 1 151 279 33 PHE CB C 39.461 0.500 1 152 279 33 PHE N N 119.820 0.100 1 153 280 34 LEU H H 8.060 0.007 1 154 280 34 LEU C C 176.492 0.100 1 155 280 34 LEU CA C 54.707 0.500 1 156 280 34 LEU CB C 42.652 0.500 1 157 280 34 LEU N N 124.378 0.100 1 158 281 35 GLU H H 8.238 0.007 1 159 281 35 GLU C C 174.382 0.100 1 160 281 35 GLU CA C 54.334 0.500 1 161 281 35 GLU CB C 29.636 0.500 1 162 281 35 GLU N N 123.578 0.100 1 163 282 36 PRO C C 176.899 0.100 1 164 282 36 PRO CA C 63.127 0.500 1 165 282 36 PRO CB C 32.026 0.500 1 166 283 37 MET H H 8.463 0.007 1 167 283 37 MET C C 175.920 0.100 1 168 283 37 MET CA C 55.245 0.500 1 169 283 37 MET CB C 33.196 0.500 1 170 283 37 MET N N 121.075 0.100 1 171 284 38 ALA H H 8.385 0.007 1 172 284 38 ALA C C 177.551 0.100 1 173 284 38 ALA CA C 52.349 0.500 1 174 284 38 ALA CB C 19.399 0.500 1 175 284 38 ALA N N 126.076 0.100 1 176 285 39 GLU H H 8.456 0.007 1 177 285 39 GLU C C 176.384 0.100 1 178 285 39 GLU CA C 56.396 0.500 1 179 285 39 GLU CB C 30.404 0.500 1 180 285 39 GLU N N 120.656 0.100 1 181 286 40 GLU H H 8.457 0.007 1 182 286 40 GLU C C 176.309 0.100 1 183 286 40 GLU CA C 56.237 0.500 1 184 286 40 GLU CB C 30.678 0.500 1 185 286 40 GLU N N 122.013 0.100 1 186 287 41 GLU H H 8.510 0.007 1 187 287 41 GLU C C 176.617 0.100 1 188 287 41 GLU CA C 56.857 0.500 1 189 287 41 GLU CB C 30.701 0.500 1 190 287 41 GLU N N 122.616 0.100 1 191 288 42 SEP H H 8.824 0.007 1 192 288 42 SEP C C 173.898 0.100 1 193 288 42 SEP CA C 57.802 0.500 1 194 288 42 SEP CB C 66.178 0.500 1 195 288 42 SEP N N 118.058 0.100 1 196 289 43 ASP H H 8.497 0.007 1 197 289 43 ASP C C 175.890 0.100 1 198 289 43 ASP CA C 54.529 0.500 1 199 289 43 ASP CB C 40.998 0.500 1 200 289 43 ASP N N 122.244 0.100 1 201 290 44 LEU H H 8.115 0.007 1 202 290 44 LEU C C 177.319 0.100 1 203 290 44 LEU CA C 55.135 0.500 1 204 290 44 LEU CB C 42.661 0.500 1 205 290 44 LEU N N 122.332 0.100 1 206 291 45 GLU H H 8.361 0.007 1 207 291 45 GLU C C 174.408 0.100 1 208 291 45 GLU CA C 54.417 0.500 1 209 291 45 GLU CB C 29.581 0.500 1 210 291 45 GLU N N 123.039 0.100 1 211 292 46 PRO C C 176.959 0.100 1 212 292 46 PRO CA C 63.033 0.500 1 213 292 46 PRO CB C 32.094 0.500 1 214 293 47 SER H H 8.453 0.007 1 215 293 47 SER C C 174.252 0.100 1 216 293 47 SER CA C 58.480 0.500 1 217 293 47 SER CB C 63.988 0.500 1 218 293 47 SER N N 116.463 0.100 1 219 294 48 ILE H H 8.129 0.007 1 220 294 48 ILE C C 174.604 0.100 1 221 294 48 ILE CA C 59.133 0.500 1 222 294 48 ILE CB C 38.773 0.500 1 223 294 48 ILE N N 123.748 0.100 1 224 295 49 PRO C C 177.221 0.100 1 225 295 49 PRO CA C 63.577 0.500 1 226 295 49 PRO CB C 32.093 0.500 1 227 296 50 SER H H 8.387 0.007 1 228 296 50 SER C C 175.238 0.100 1 229 296 50 SER CA C 59.055 0.500 1 230 296 50 SER CB C 63.777 0.500 1 231 296 50 SER N N 116.203 0.100 1 232 297 51 GLU H H 8.634 0.007 1 233 297 51 GLU C C 176.594 0.100 1 234 297 51 GLU CA C 57.287 0.500 1 235 297 51 GLU CB C 29.769 0.500 1 236 297 51 GLU N N 122.080 0.100 1 237 298 52 CYS H H 8.211 0.007 1 238 298 52 CYS C C 174.477 0.100 1 239 298 52 CYS CA C 58.955 0.500 1 240 298 52 CYS CB C 27.879 0.500 1 241 298 52 CYS N N 118.843 0.100 1 242 299 53 MET H H 8.277 0.007 1 243 299 53 MET C C 175.801 0.100 1 244 299 53 MET CA C 55.371 0.500 1 245 299 53 MET CB C 32.583 0.500 1 246 299 53 MET N N 122.245 0.100 1 247 300 54 LEU H H 8.101 0.007 1 248 300 54 LEU C C 175.038 0.100 1 249 300 54 LEU CA C 53.206 0.500 1 250 300 54 LEU CB C 41.753 0.500 1 251 300 54 LEU N N 124.251 0.100 1 252 301 55 PRO C C 177.076 0.100 1 253 301 55 PRO CA C 63.219 0.500 1 254 301 55 PRO CB C 32.002 0.500 1 255 302 56 ARG H H 8.512 0.007 1 256 302 56 ARG C C 176.588 0.100 1 257 302 56 ARG CA C 56.270 0.500 1 258 302 56 ARG CB C 30.663 0.500 1 259 302 56 ARG N N 121.404 0.100 1 260 303 57 SER H H 8.334 0.007 1 261 303 57 SER C C 174.879 0.100 1 262 303 57 SER CA C 58.794 0.500 1 263 303 57 SER CB C 63.919 0.500 1 264 303 57 SER N N 116.288 0.100 1 265 304 58 GLY H H 8.374 0.007 1 266 304 58 GLY C C 173.394 0.100 1 267 304 58 GLY CA C 44.998 0.500 1 268 304 58 GLY N N 110.342 0.100 1 269 305 59 PHE H H 8.030 0.007 1 270 305 59 PHE C C 173.386 0.100 1 271 305 59 PHE CA C 55.866 0.500 1 272 305 59 PHE CB C 39.084 0.500 1 273 305 59 PHE N N 120.683 0.100 1 274 306 60 PRO C C 176.643 0.100 1 275 306 60 PRO CA C 63.373 0.500 1 276 306 60 PRO CB C 31.936 0.500 1 277 307 61 ARG H H 8.336 0.007 1 278 307 61 ARG C C 175.873 0.100 1 279 307 61 ARG CA C 56.147 0.500 1 280 307 61 ARG CB C 30.916 0.500 1 281 307 61 ARG N N 121.180 0.100 1 282 308 62 ALA H H 8.279 0.007 1 283 308 62 ALA C C 177.136 0.100 1 284 308 62 ALA CA C 52.024 0.500 1 285 308 62 ALA CB C 19.274 0.500 1 286 308 62 ALA N N 124.778 0.100 1 287 309 63 LEU H H 8.101 0.007 1 288 309 63 LEU C C 175.091 0.100 1 289 309 63 LEU CA C 52.711 0.500 1 290 309 63 LEU CB C 42.093 0.500 1 291 309 63 LEU N N 122.961 0.100 1 292 310 64 PRO C C 177.162 0.100 1 293 310 64 PRO CA C 62.770 0.500 1 294 310 64 PRO CB C 31.699 0.500 1 295 311 65 ALA H H 8.456 0.007 1 296 311 65 ALA C C 178.064 0.100 1 297 311 65 ALA CA C 54.083 0.500 1 298 311 65 ALA CB C 18.689 0.500 1 299 311 65 ALA N N 123.295 0.100 1 300 312 66 TRP H H 7.168 0.007 1 301 312 66 TRP C C 175.881 0.100 1 302 312 66 TRP CA C 56.321 0.500 1 303 312 66 TRP CB C 28.575 0.500 1 304 312 66 TRP N N 113.893 0.100 1 305 313 67 ALA H H 7.454 0.007 1 306 313 67 ALA C C 176.734 0.100 1 307 313 67 ALA CA C 51.923 0.500 1 308 313 67 ALA CB C 19.302 0.500 1 309 313 67 ALA N N 124.466 0.100 1 310 314 68 ARG H H 7.760 0.007 1 311 314 68 ARG C C 174.853 0.100 1 312 314 68 ARG CA C 54.293 0.500 1 313 314 68 ARG CB C 30.419 0.500 1 314 314 68 ARG N N 120.408 0.100 1 315 315 69 PRO C C 176.474 0.100 1 316 315 69 PRO CA C 63.968 0.500 1 317 315 69 PRO CB C 31.814 0.500 1 318 316 70 ASP H H 8.307 0.007 1 319 316 70 ASP C C 175.610 0.100 1 320 316 70 ASP CA C 53.797 0.500 1 321 316 70 ASP CB C 40.389 0.500 1 322 316 70 ASP N N 117.733 0.100 1 323 317 71 TYR H H 7.816 0.007 1 324 317 71 TYR C C 174.817 0.100 1 325 317 71 TYR CA C 58.099 0.500 1 326 317 71 TYR CB C 38.974 0.500 1 327 317 71 TYR N N 120.686 0.100 1 328 318 72 ASN H H 8.184 0.007 1 329 318 72 ASN C C 171.551 0.100 1 330 318 72 ASN CA C 50.718 0.500 1 331 318 72 ASN CB C 39.409 0.500 1 332 318 72 ASN N N 123.880 0.100 1 333 320 74 PRO C C 176.784 0.100 1 334 320 74 PRO CA C 62.993 0.500 1 335 320 74 PRO CB C 31.858 0.500 1 336 321 75 LEU H H 8.243 0.007 1 337 321 75 LEU C C 177.388 0.100 1 338 321 75 LEU CA C 55.250 0.500 1 339 321 75 LEU CB C 42.090 0.500 1 340 321 75 LEU N N 122.157 0.100 1 341 322 76 VAL H H 8.021 0.007 1 342 322 76 VAL C C 176.074 0.100 1 343 322 76 VAL CA C 62.388 0.500 1 344 322 76 VAL CB C 32.761 0.500 1 345 322 76 VAL N N 120.923 0.100 1 346 323 77 GLU H H 8.565 0.007 1 347 323 77 GLU C C 176.991 0.100 1 348 323 77 GLU CA C 56.696 0.500 1 349 323 77 GLU CB C 29.706 0.500 1 350 323 77 GLU N N 124.466 0.100 1 351 324 78 SER H H 8.334 0.007 1 352 324 78 SER C C 174.417 0.100 1 353 324 78 SER CA C 59.430 0.500 1 354 324 78 SER CB C 63.604 0.500 1 355 324 78 SER N N 116.888 0.100 1 356 325 79 TRP H H 7.690 0.007 1 357 325 79 TRP C C 175.902 0.100 1 358 325 79 TRP CA C 57.141 0.500 1 359 325 79 TRP CB C 28.871 0.500 1 360 325 79 TRP N N 120.716 0.100 1 361 326 80 ARG H H 7.570 0.007 1 362 326 80 ARG C C 175.491 0.100 1 363 326 80 ARG CA C 55.899 0.500 1 364 326 80 ARG CB C 30.746 0.500 1 365 326 80 ARG N N 122.109 0.100 1 366 327 81 ARG H H 8.067 0.007 1 367 327 81 ARG C C 174.831 0.100 1 368 327 81 ARG CA C 54.231 0.500 1 369 327 81 ARG CB C 30.210 0.500 1 370 327 81 ARG N N 123.032 0.100 1 371 328 82 PRO C C 176.555 0.100 1 372 328 82 PRO CA C 63.834 0.500 1 373 328 82 PRO CB C 31.847 0.500 1 374 329 83 ASP H H 8.348 0.007 1 375 329 83 ASP C C 175.750 0.100 1 376 329 83 ASP CA C 53.980 0.500 1 377 329 83 ASP CB C 40.553 0.500 1 378 329 83 ASP N N 118.233 0.100 1 379 330 84 TYR H H 7.870 0.007 1 380 330 84 TYR C C 174.913 0.100 1 381 330 84 TYR CA C 58.397 0.500 1 382 330 84 TYR CB C 38.965 0.500 1 383 330 84 TYR N N 120.606 0.100 1 384 331 85 GLN H H 7.899 0.007 1 385 331 85 GLN C C 172.367 0.100 1 386 331 85 GLN CA C 52.434 0.500 1 387 331 85 GLN CB C 29.658 0.500 1 388 331 85 GLN N N 125.622 0.100 1 389 333 87 PRO C C 176.990 0.100 1 390 333 87 PRO CA C 63.155 0.500 1 391 333 87 PRO CB C 31.990 0.500 1 392 334 88 THR H H 8.185 0.007 1 393 334 88 THR C C 174.599 0.100 1 394 334 88 THR CA C 61.808 0.500 1 395 334 88 THR CB C 69.951 0.500 1 396 334 88 THR N N 114.414 0.100 1 397 335 89 VAL H H 8.157 0.007 1 398 335 89 VAL C C 175.777 0.100 1 399 335 89 VAL CA C 62.161 0.500 1 400 335 89 VAL CB C 32.886 0.500 1 401 335 89 VAL N N 122.559 0.100 1 402 336 90 ALA H H 8.442 0.007 1 403 336 90 ALA C C 178.220 0.100 1 404 336 90 ALA CA C 52.737 0.500 1 405 336 90 ALA CB C 19.106 0.500 1 406 336 90 ALA N N 127.954 0.100 1 407 337 91 GLY H H 8.402 0.007 1 408 337 91 GLY C C 174.077 0.100 1 409 337 91 GLY CA C 45.287 0.500 1 410 337 91 GLY N N 108.307 0.100 1 411 338 92 CYS H H 8.115 0.007 1 412 338 92 CYS C C 174.049 0.100 1 413 338 92 CYS CA C 58.315 0.500 1 414 338 92 CYS CB C 28.258 0.500 1 415 338 92 CYS N N 118.691 0.100 1 416 339 93 ALA H H 8.429 0.007 1 417 339 93 ALA C C 177.255 0.100 1 418 339 93 ALA CA C 52.292 0.500 1 419 339 93 ALA CB C 19.211 0.500 1 420 339 93 ALA N N 126.675 0.100 1 421 340 94 LEU H H 8.183 0.007 1 422 340 94 LEU C C 175.287 0.100 1 423 340 94 LEU CA C 53.197 0.500 1 424 340 94 LEU CB C 41.829 0.500 1 425 340 94 LEU N N 122.938 0.100 1 426 341 95 PRO C C 176.805 0.100 1 427 341 95 PRO CA C 63.114 0.500 1 428 341 95 PRO CB C 31.823 0.500 1 429 342 96 LEU H H 8.266 0.007 1 430 342 96 LEU C C 177.422 0.100 1 431 342 96 LEU CA C 55.292 0.500 1 432 342 96 LEU CB C 42.240 0.500 1 433 342 96 LEU N N 121.942 0.100 1 434 343 97 GLN H H 8.320 0.007 1 435 343 97 GLN C C 175.572 0.100 1 436 343 97 GLN CA C 55.945 0.500 1 437 343 97 GLN CB C 29.374 0.500 1 438 343 97 GLN N N 120.532 0.100 1 stop_ save_