data_28011 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for Mdm2 (residues 284 to 434) ; _BMRB_accession_number 28011 _BMRB_flat_file_name bmr28011.str _Entry_type original _Submission_date 2019-09-08 _Accession_date 2019-09-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Human Mdm2 fragment 284-434, C262A-C374A; contains a zinc-finger domain (293-333) showing two stable conformations (Prolines in trans or in cis) as reported previously in the litterature; we report here only the trans conformation assignment. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Theillet Francois-Xavier . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 139 "13C chemical shifts" 427 "15N chemical shifts" 139 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-10-15 original BMRB . stop_ _Original_release_date 2019-09-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Phosphorylation of Mdm2 by DNA-Damage Response Kinases in physiological conditions monitored using 13C-NMR ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Theillet Francois-Xavier . . 2 Alik Ania . . 3 Boucguechtouli Chafiaa . . 4 Julien Manon . . 5 Bermel Wolfgang . . 6 Kovacs Helena . . 7 Ghouil Rania . . 8 Zinn-Justin Sophie . . stop_ _Journal_abbreviation 'Not known' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword DNA-PK Mdm2 NMR p53 phosphorylation stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Mdm2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Mdm2 $Mdm2 ligand $entity_ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Binding ribosomal proteins' 'E3-ubiquitin ligase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Mdm2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Mdm2 _Molecular_mass . _Mol_thiol_state 'all other bound' loop_ _Biological_function 'E3-ubiquitin ligase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 151 _Mol_residue_sequence ; GESDTDSFEEDPEISLADYW KCTSCNEMNPPLPSHCNRCW ALRENWLPEDKGKDKGEISE KAKLENSTQAEEGFDVPDAK KTIVNDSRESAVEENDDKIT QASQSQESEDYSQPSTSSSI IYSSQEDVKEFEREETQDKE ESVESSLPLNA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 284 GLY 2 285 GLU 3 286 SER 4 287 ASP 5 288 THR 6 289 ASP 7 290 SER 8 291 PHE 9 292 GLU 10 293 GLU 11 294 ASP 12 295 PRO 13 296 GLU 14 297 ILE 15 298 SER 16 299 LEU 17 300 ALA 18 301 ASP 19 302 TYR 20 303 TRP 21 304 LYS 22 305 CYS 23 306 THR 24 307 SER 25 308 CYS 26 309 ASN 27 310 GLU 28 311 MET 29 312 ASN 30 313 PRO 31 314 PRO 32 315 LEU 33 316 PRO 34 317 SER 35 318 HIS 36 319 CYS 37 320 ASN 38 321 ARG 39 322 CYS 40 323 TRP 41 324 ALA 42 325 LEU 43 326 ARG 44 327 GLU 45 328 ASN 46 329 TRP 47 330 LEU 48 331 PRO 49 332 GLU 50 333 ASP 51 334 LYS 52 335 GLY 53 336 LYS 54 337 ASP 55 338 LYS 56 339 GLY 57 340 GLU 58 341 ILE 59 342 SER 60 343 GLU 61 344 LYS 62 345 ALA 63 346 LYS 64 347 LEU 65 348 GLU 66 349 ASN 67 350 SER 68 351 THR 69 352 GLN 70 353 ALA 71 354 GLU 72 355 GLU 73 356 GLY 74 357 PHE 75 358 ASP 76 359 VAL 77 360 PRO 78 361 ASP 79 362 ALA 80 363 LYS 81 364 LYS 82 365 THR 83 366 ILE 84 367 VAL 85 368 ASN 86 369 ASP 87 370 SER 88 371 ARG 89 372 GLU 90 373 SER 91 374 ALA 92 375 VAL 93 376 GLU 94 377 GLU 95 378 ASN 96 379 ASP 97 380 ASP 98 381 LYS 99 382 ILE 100 383 THR 101 384 GLN 102 385 ALA 103 386 SER 104 387 GLN 105 388 SER 106 389 GLN 107 390 GLU 108 391 SER 109 392 GLU 110 393 ASP 111 394 TYR 112 395 SER 113 396 GLN 114 397 PRO 115 398 SER 116 399 THR 117 400 SER 118 401 SER 119 402 SER 120 403 ILE 121 404 ILE 122 405 TYR 123 406 SER 124 407 SER 125 408 GLN 126 409 GLU 127 410 ASP 128 411 VAL 129 412 LYS 130 413 GLU 131 414 PHE 132 415 GLU 133 416 ARG 134 417 GLU 135 418 GLU 136 419 THR 137 420 GLN 138 421 ASP 139 422 LYS 140 423 GLU 141 424 GLU 142 425 SER 143 426 VAL 144 427 GLU 145 428 SER 146 429 SER 147 430 LEU 148 431 PRO 149 432 LEU 150 433 ASN 151 434 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'ZINC ION' _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Mdm2 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Mdm2 'recombinant technology' . Escherichia coli 'BL21 (DE3) Star' pET41 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 $Mdm2 700 uM '[U-100% 13C; U-100% 15N]' $entity_ZN 1 mM 'natural abundance' DSS 1 mM 'natural abundance' HEPES 20 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' H2O 55 M 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 4.0.4 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_ccpnmr_analysis _Saveframe_category software _Name ccpnmr_analysis _Version 2.4.2 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_(H)N(CA)NNH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)N(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' 70 . mM pH 6.6 . pH pressure 1 . atm temperature 283 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 'reference : DSS' loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCACB' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Mdm2 _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 1 284 1 GLY CA C 43.33 0.1 1 2 285 2 GLU H H 8.89 0.01 1 3 285 2 GLU C C 176.92 0.1 1 4 285 2 GLU CA C 57.27 0.1 1 5 285 2 GLU CB C 30.14 0.1 1 6 285 2 GLU N N 120.48 0.05 1 7 286 3 SER H H 8.61 0.01 1 8 286 3 SER C C 174.41 0.1 1 9 286 3 SER CA C 58.45 0.1 1 10 286 3 SER CB C 63.75 0.1 1 11 286 3 SER N N 115.62 0.05 1 12 287 4 ASP H H 8.36 0.01 1 13 287 4 ASP C C 176.52 0.1 1 14 287 4 ASP CA C 54.65 0.1 1 15 287 4 ASP CB C 41.06 0.1 1 16 287 4 ASP N N 122.27 0.05 1 17 288 5 THR H H 8.19 0.01 1 18 288 5 THR C C 174.48 0.1 1 19 288 5 THR CA C 61.96 0.1 1 20 288 5 THR CB C 69.85 0.1 1 21 288 5 THR N N 113.50 0.05 1 22 289 6 ASP H H 8.39 0.01 1 23 289 6 ASP C C 176.10 0.1 1 24 289 6 ASP CA C 54.62 0.1 1 25 289 6 ASP CB C 41.19 0.1 1 26 289 6 ASP N N 122.91 0.05 1 27 290 7 SER H H 8.22 0.01 1 28 290 7 SER C C 174.05 0.1 1 29 290 7 SER CA C 58.25 0.1 1 30 290 7 SER CB C 63.90 0.1 1 31 290 7 SER N N 115.99 0.05 1 32 291 8 PHE H H 8.35 0.01 1 33 291 8 PHE C C 175.46 0.1 1 34 291 8 PHE CA C 57.76 0.1 1 35 291 8 PHE CB C 39.68 0.1 1 36 291 8 PHE N N 122.56 0.05 1 37 292 9 GLU H H 8.32 0.01 1 38 292 9 GLU C C 175.75 0.1 1 39 292 9 GLU CA C 56.01 0.1 1 40 292 9 GLU CB C 30.67 0.1 1 41 292 9 GLU N N 123.16 0.05 1 42 293 10 GLU H H 8.44 0.01 1 43 293 10 GLU C C 175.91 0.1 1 44 293 10 GLU CA C 56.22 0.1 1 45 293 10 GLU CB C 30.60 0.1 1 46 293 10 GLU N N 122.59 0.05 1 47 294 11 ASP H H 8.66 0.01 1 48 294 11 ASP C C 174.78 0.1 1 49 294 11 ASP CA C 52.34 0.1 1 50 294 11 ASP CB C 40.93 0.1 1 51 294 11 ASP N N 123.84 0.05 1 52 295 12 PRO C C 177.23 0.1 1 53 295 12 PRO CA C 63.43 0.1 1 54 295 12 PRO CB C 32.35 0.1 1 55 296 13 GLU H H 8.57 0.01 1 56 296 13 GLU C C 176.91 0.1 1 57 296 13 GLU CA C 56.85 0.1 1 58 296 13 GLU CB C 29.91 0.1 1 59 296 13 GLU N N 120.19 0.05 1 60 297 14 ILE H H 8.08 0.01 1 61 297 14 ILE C C 176.37 0.1 1 62 297 14 ILE CA C 61.24 0.1 1 63 297 14 ILE CB C 38.72 0.1 1 64 297 14 ILE N N 121.88 0.05 1 65 298 15 SER H H 8.53 0.01 1 66 298 15 SER C C 175.35 0.1 1 67 298 15 SER CA C 58.35 0.1 1 68 298 15 SER CB C 63.62 0.1 1 69 298 15 SER N N 119.61 0.05 1 70 299 16 LEU H H 8.38 0.01 1 71 299 16 LEU C C 178.18 0.1 1 72 299 16 LEU CA C 55.24 0.1 1 73 299 16 LEU CB C 41.23 0.1 1 74 299 16 LEU N N 125.17 0.05 1 75 300 17 ALA H H 7.99 0.01 1 76 300 17 ALA C C 177.92 0.1 1 77 300 17 ALA CA C 54.05 0.1 1 78 300 17 ALA CB C 18.88 0.1 1 79 300 17 ALA N N 122.94 0.05 1 80 301 18 ASP H H 8.45 0.01 1 81 301 18 ASP C C 175.92 0.1 1 82 301 18 ASP CA C 52.39 0.1 1 83 301 18 ASP CB C 40.47 0.1 1 84 301 18 ASP N N 115.55 0.05 1 85 302 19 TYR H H 7.91 0.01 1 86 302 19 TYR C C 175.91 0.1 1 87 302 19 TYR CA C 58.69 0.1 1 88 302 19 TYR CB C 39.06 0.1 1 89 302 19 TYR N N 122.08 0.05 1 90 303 20 TRP H H 9.29 0.01 1 91 303 20 TRP C C 173.60 0.1 1 92 303 20 TRP CA C 53.73 0.1 1 93 303 20 TRP CB C 31.54 0.1 1 94 303 20 TRP N N 119.31 0.05 1 95 304 21 LYS H H 8.93 0.01 1 96 304 21 LYS C C 176.51 0.1 1 97 304 21 LYS CA C 55.12 0.1 1 98 304 21 LYS CB C 34.41 0.1 1 99 304 21 LYS N N 124.00 0.05 1 100 305 22 CYS H H 9.06 0.01 1 101 305 22 CYS C C 178.09 0.1 1 102 305 22 CYS CA C 59.91 0.1 1 103 305 22 CYS CB C 31.35 0.1 1 104 305 22 CYS N N 131.79 0.05 1 105 306 23 THR H H 8.84 0.01 1 106 306 23 THR C C 175.46 0.1 1 107 306 23 THR CA C 63.91 0.1 1 108 306 23 THR CB C 68.94 0.1 1 109 306 23 THR N N 122.19 0.05 1 110 307 24 SER H H 9.31 0.01 1 111 307 24 SER C C 175.55 0.1 1 112 307 24 SER CA C 61.21 0.1 1 113 307 24 SER CB C 63.86 0.1 1 114 307 24 SER N N 120.84 0.05 1 115 308 25 CYS H H 8.79 0.01 1 116 308 25 CYS C C 176.60 0.1 1 117 308 25 CYS CA C 59.21 0.1 1 118 308 25 CYS CB C 32.83 0.1 1 119 308 25 CYS N N 121.04 0.05 1 120 309 26 ASN H H 7.82 0.01 1 121 309 26 ASN C C 173.36 0.1 1 122 309 26 ASN CA C 56.20 0.1 1 123 309 26 ASN CB C 37.72 0.1 1 124 309 26 ASN N N 117.10 0.05 1 125 310 27 GLU H H 8.67 0.01 1 126 310 27 GLU N N 124.21 0.05 1 127 311 28 MET C C 176.24 0.1 1 128 312 29 ASN H H 9.24 0.01 1 129 312 29 ASN CA C 51.31 0.1 1 130 312 29 ASN CB C 43.16 0.1 1 131 312 29 ASN N N 124.76 0.05 1 132 314 31 PRO C C 178.69 0.1 1 133 314 31 PRO CA C 65.33 0.1 1 134 315 32 LEU H H 8.13 0.01 1 135 315 32 LEU C C 175.06 0.1 1 136 315 32 LEU CA C 58.91 0.1 1 137 315 32 LEU CB C 39.94 0.1 1 138 315 32 LEU N N 117.75 0.05 1 139 316 33 PRO C C 176.56 0.1 1 140 317 34 SER H H 8.41 0.01 1 141 317 34 SER C C 173.14 0.1 1 142 317 34 SER CA C 58.29 0.1 1 143 317 34 SER CB C 63.63 0.1 1 144 317 34 SER N N 114.10 0.05 1 145 318 35 HIS H H 7.58 0.01 1 146 318 35 HIS C C 173.50 0.1 1 147 318 35 HIS CA C 54.06 0.1 1 148 318 35 HIS CB C 30.85 0.1 1 149 318 35 HIS N N 116.58 0.05 1 150 319 36 CYS H H 9.06 0.01 1 151 319 36 CYS C C 177.40 0.1 1 152 319 36 CYS CA C 58.90 0.1 1 153 319 36 CYS CB C 31.11 0.1 1 154 319 36 CYS N N 124.39 0.05 1 155 320 37 ASN H H 9.16 0.01 1 156 320 37 ASN C C 175.07 0.1 1 157 320 37 ASN CA C 55.33 0.1 1 158 320 37 ASN CB C 39.11 0.1 1 159 320 37 ASN N N 128.07 0.05 1 160 321 38 ARG H H 9.41 0.01 1 161 321 38 ARG C C 176.87 0.1 1 162 321 38 ARG CA C 57.77 0.1 1 163 321 38 ARG CB C 31.16 0.1 1 164 321 38 ARG N N 122.48 0.05 1 165 322 39 CYS H H 8.58 0.01 1 166 322 39 CYS C C 176.57 0.1 1 167 322 39 CYS N N 119.30 0.05 1 168 323 40 TRP H H 7.84 0.01 1 169 323 40 TRP C C 175.23 0.1 1 170 323 40 TRP CA C 60.08 0.1 1 171 323 40 TRP CB C 28.27 0.1 1 172 323 40 TRP N N 121.31 0.05 1 173 324 41 ALA H H 9.16 0.01 1 174 324 41 ALA C C 178.57 0.1 1 175 324 41 ALA CA C 53.80 0.1 1 176 324 41 ALA CB C 20.40 0.1 1 177 324 41 ALA N N 127.35 0.05 1 178 325 42 LEU H H 8.60 0.01 1 179 325 42 LEU C C 177.21 0.1 1 180 325 42 LEU CA C 55.09 0.1 1 181 325 42 LEU CB C 42.90 0.1 1 182 325 42 LEU N N 123.68 0.05 1 183 326 43 ARG H H 7.97 0.01 1 184 326 43 ARG C C 175.91 0.1 1 185 326 43 ARG CA C 56.89 0.1 1 186 326 43 ARG CB C 29.96 0.1 1 187 326 43 ARG N N 125.29 0.05 1 188 327 44 GLU C C 175.91 0.1 1 189 328 45 ASN H H 8.49 0.01 1 190 328 45 ASN C C 176.92 0.1 1 191 328 45 ASN CA C 56.75 0.1 1 192 328 45 ASN CB C 38.67 0.1 1 193 328 45 ASN N N 118.78 0.05 1 194 329 46 TRP H H 8.05 0.01 1 195 329 46 TRP C C 175.32 0.1 1 196 329 46 TRP CA C 61.25 0.1 1 197 329 46 TRP CB C 29.92 0.1 1 198 329 46 TRP N N 121.71 0.05 1 199 330 47 LEU H H 7.99 0.01 1 200 330 47 LEU C C 174.38 0.1 1 201 330 47 LEU CA C 52.44 0.1 1 202 330 47 LEU CB C 42.25 0.1 1 203 330 47 LEU N N 126.19 0.05 1 204 331 48 PRO C C 177.17 0.1 1 205 331 48 PRO CA C 63.09 0.1 1 206 331 48 PRO CB C 31.94 0.1 1 207 332 49 GLU H H 8.61 0.01 1 208 332 49 GLU C C 176.32 0.1 1 209 332 49 GLU CA C 56.76 0.1 1 210 332 49 GLU CB C 30.19 0.1 1 211 332 49 GLU N N 120.87 0.05 1 212 333 50 ASP H H 8.47 0.01 1 213 333 50 ASP C C 176.58 0.1 1 214 333 50 ASP CA C 54.36 0.1 1 215 333 50 ASP CB C 41.22 0.1 1 216 333 50 ASP N N 122.19 0.05 1 217 334 51 LYS H H 8.42 0.01 1 218 334 51 LYS C C 177.39 0.1 1 219 334 51 LYS CA C 56.75 0.1 1 220 334 51 LYS CB C 32.50 0.1 1 221 334 51 LYS N N 122.90 0.05 1 222 335 52 GLY H H 8.59 0.01 1 223 335 52 GLY C C 174.48 0.1 1 224 335 52 GLY CA C 45.47 0.1 1 225 335 52 GLY N N 109.51 0.05 1 226 336 53 LYS H H 8.11 0.01 1 227 336 53 LYS C C 176.61 0.1 1 228 336 53 LYS CA C 56.56 0.1 1 229 336 53 LYS CB C 33.01 0.1 1 230 336 53 LYS N N 120.74 0.05 1 231 337 54 ASP H H 8.50 0.01 1 232 337 54 ASP C C 176.50 0.1 1 233 337 54 ASP CA C 54.61 0.1 1 234 337 54 ASP CB C 41.19 0.1 1 235 337 54 ASP N N 121.44 0.05 1 236 338 55 LYS H H 8.45 0.01 1 237 338 55 LYS C C 177.33 0.1 1 238 338 55 LYS CA C 56.66 0.1 1 239 338 55 LYS CB C 32.57 0.1 1 240 338 55 LYS N N 122.24 0.05 1 241 339 56 GLY H H 8.51 0.01 1 242 339 56 GLY C C 174.18 0.1 1 243 339 56 GLY CA C 45.34 0.1 1 244 339 56 GLY N N 109.51 0.05 1 245 340 57 GLU H H 8.33 0.01 1 246 340 57 GLU C C 176.85 0.1 1 247 340 57 GLU CA C 56.65 0.1 1 248 340 57 GLU CB C 30.33 0.1 1 249 340 57 GLU N N 120.85 0.05 1 250 341 58 ILE H H 8.38 0.01 1 251 341 58 ILE C C 176.56 0.1 1 252 341 58 ILE CA C 61.73 0.1 1 253 341 58 ILE CB C 38.69 0.1 1 254 341 58 ILE N N 122.49 0.05 1 255 342 59 SER H H 8.48 0.01 1 256 342 59 SER C C 174.85 0.1 1 257 342 59 SER CA C 58.56 0.1 1 258 342 59 SER CB C 63.87 0.1 1 259 342 59 SER N N 120.23 0.05 1 260 343 60 GLU H H 8.58 0.01 1 261 343 60 GLU C C 177.09 0.1 1 262 343 60 GLU CA C 57.22 0.1 1 263 343 60 GLU CB C 30.06 0.1 1 264 343 60 GLU N N 123.37 0.05 1 265 344 61 LYS H H 8.34 0.01 1 266 344 61 LYS C C 176.93 0.1 1 267 344 61 LYS CA C 57.14 0.1 1 268 344 61 LYS CB C 32.84 0.1 1 269 344 61 LYS N N 122.03 0.05 1 270 345 62 ALA H H 8.27 0.01 1 271 345 62 ALA C C 178.27 0.1 1 272 345 62 ALA CA C 52.99 0.1 1 273 345 62 ALA CB C 18.98 0.1 1 274 345 62 ALA N N 124.53 0.05 1 275 346 63 LYS H H 8.25 0.01 1 276 346 63 LYS C C 177.10 0.1 1 277 346 63 LYS CA C 57.00 0.1 1 278 346 63 LYS CB C 32.87 0.1 1 279 346 63 LYS N N 120.53 0.05 1 280 347 64 LEU H H 8.25 0.01 1 281 347 64 LEU C C 177.84 0.1 1 282 347 64 LEU CA C 55.42 0.1 1 283 347 64 LEU CB C 42.27 0.1 1 284 347 64 LEU N N 123.14 0.05 1 285 348 65 GLU H H 8.45 0.01 1 286 348 65 GLU C C 176.43 0.1 1 287 348 65 GLU CA C 56.87 0.1 1 288 348 65 GLU CB C 30.03 0.1 1 289 348 65 GLU N N 121.59 0.05 1 290 349 66 ASN H H 8.49 0.01 1 291 349 66 ASN C C 175.45 0.1 1 292 349 66 ASN CA C 53.50 0.1 1 293 349 66 ASN CB C 38.90 0.1 1 294 349 66 ASN N N 119.38 0.05 1 295 350 67 SER H H 8.38 0.01 1 296 350 67 SER C C 174.99 0.1 1 297 350 67 SER CA C 58.89 0.1 1 298 350 67 SER CB C 63.94 0.1 1 299 350 67 SER N N 116.39 0.05 1 300 351 68 THR H H 8.32 0.01 1 301 351 68 THR C C 174.61 0.1 1 302 351 68 THR CA C 62.21 0.1 1 303 351 68 THR CB C 69.76 0.1 1 304 351 68 THR N N 116.23 0.05 1 305 352 69 GLN H H 8.43 0.01 1 306 352 69 GLN C C 175.71 0.1 1 307 352 69 GLN CA C 56.06 0.1 1 308 352 69 GLN CB C 29.42 0.1 1 309 352 69 GLN N N 123.02 0.05 1 310 353 70 ALA H H 8.45 0.01 1 311 353 70 ALA C C 177.86 0.1 1 312 353 70 ALA CA C 52.61 0.1 1 313 353 70 ALA CB C 19.30 0.1 1 314 353 70 ALA N N 125.85 0.05 1 315 354 71 GLU H H 8.49 0.01 1 316 354 71 GLU C C 176.62 0.1 1 317 354 71 GLU CA C 56.44 0.1 1 318 354 71 GLU CB C 30.30 0.1 1 319 354 71 GLU N N 120.55 0.05 1 320 355 72 GLU H H 8.52 0.01 1 321 355 72 GLU C C 176.91 0.1 1 322 355 72 GLU CA C 56.92 0.1 1 323 355 72 GLU CB C 30.27 0.1 1 324 355 72 GLU N N 122.23 0.05 1 325 356 73 GLY H H 8.49 0.01 1 326 356 73 GLY C C 173.91 0.1 1 327 356 73 GLY CA C 45.21 0.1 1 328 356 73 GLY N N 109.93 0.05 1 329 357 74 PHE H H 8.10 0.01 1 330 357 74 PHE C C 175.39 0.1 1 331 357 74 PHE CA C 57.64 0.1 1 332 357 74 PHE CB C 39.76 0.1 1 333 357 74 PHE N N 119.59 0.05 1 334 358 75 ASP H H 8.49 0.01 1 335 358 75 ASP C C 175.57 0.1 1 336 358 75 ASP CA C 54.16 0.1 1 337 358 75 ASP CB C 41.12 0.1 1 338 358 75 ASP N N 121.96 0.05 1 339 359 76 VAL H H 8.15 0.01 1 340 359 76 VAL C C 174.67 0.1 1 341 359 76 VAL CA C 59.97 0.1 1 342 359 76 VAL CB C 32.47 0.1 1 343 359 76 VAL N N 122.01 0.05 1 344 360 77 PRO C C 176.85 0.1 1 345 360 77 PRO CA C 63.49 0.1 1 346 360 77 PRO CB C 32.09 0.1 1 347 361 78 ASP H H 8.52 0.01 1 348 361 78 ASP C C 176.49 0.1 1 349 361 78 ASP CA C 54.61 0.1 1 350 361 78 ASP CB C 41.07 0.1 1 351 361 78 ASP N N 120.60 0.05 1 352 362 79 ALA H H 8.38 0.01 1 353 362 79 ALA C C 178.14 0.1 1 354 362 79 ALA CA C 52.94 0.1 1 355 362 79 ALA CB C 19.14 0.1 1 356 362 79 ALA N N 125.01 0.05 1 357 363 80 LYS H H 8.36 0.01 1 358 363 80 LYS C C 176.83 0.1 1 359 363 80 LYS CA C 56.43 0.1 1 360 363 80 LYS CB C 32.61 0.1 1 361 363 80 LYS N N 119.50 0.05 1 362 364 81 LYS H H 8.22 0.01 1 363 364 81 LYS C C 176.72 0.1 1 364 364 81 LYS CA C 56.41 0.1 1 365 364 81 LYS CB C 33.12 0.1 1 366 364 81 LYS N N 122.35 0.05 1 367 365 82 THR H H 8.29 0.01 1 368 365 82 THR C C 174.24 0.1 1 369 365 82 THR CA C 62.29 0.1 1 370 365 82 THR CB C 69.81 0.1 1 371 365 82 THR N N 117.12 0.05 1 372 366 83 ILE H H 8.37 0.01 1 373 366 83 ILE C C 176.08 0.1 1 374 366 83 ILE CA C 61.18 0.1 1 375 366 83 ILE CB C 38.65 0.1 1 376 366 83 ILE N N 125.05 0.05 1 377 367 84 VAL H H 8.42 0.01 1 378 367 84 VAL C C 175.77 0.1 1 379 367 84 VAL CA C 62.29 0.1 1 380 367 84 VAL CB C 32.77 0.1 1 381 367 84 VAL N N 125.85 0.05 1 382 368 85 ASN H H 8.68 0.01 1 383 368 85 ASN C C 174.83 0.1 1 384 368 85 ASN CA C 53.23 0.1 1 385 368 85 ASN CB C 39.06 0.1 1 386 368 85 ASN N N 123.66 0.05 1 387 369 86 ASP H H 8.47 0.01 1 388 369 86 ASP C C 176.41 0.1 1 389 369 86 ASP CA C 54.32 0.1 1 390 369 86 ASP CB C 41.19 0.1 1 391 369 86 ASP N N 121.98 0.05 1 392 370 87 SER H H 8.41 0.01 1 393 370 87 SER C C 174.86 0.1 1 394 370 87 SER CA C 58.70 0.1 1 395 370 87 SER CB C 63.70 0.1 1 396 370 87 SER N N 117.01 0.05 1 397 371 88 ARG H H 8.46 0.01 1 398 371 88 ARG C C 176.65 0.1 1 399 371 88 ARG CA C 56.35 0.1 1 400 371 88 ARG CB C 30.63 0.1 1 401 371 88 ARG N N 122.95 0.05 1 402 372 89 GLU H H 8.51 0.01 1 403 372 89 GLU C C 176.62 0.1 1 404 372 89 GLU CA C 56.78 0.1 1 405 372 89 GLU CB C 30.19 0.1 1 406 372 89 GLU N N 121.63 0.05 1 407 373 90 SER H H 8.38 0.01 1 408 373 90 SER C C 174.11 0.1 1 409 373 90 SER CA C 58.49 0.1 1 410 373 90 SER CB C 63.86 0.1 1 411 373 90 SER N N 116.90 0.05 1 412 374 91 ALA H H 8.43 0.01 1 413 374 91 ALA C C 177.70 0.1 1 414 374 91 ALA CA C 52.45 0.1 1 415 374 91 ALA CB C 19.35 0.1 1 416 374 91 ALA N N 126.54 0.05 1 417 375 92 VAL H H 8.23 0.01 1 418 375 92 VAL C C 176.31 0.1 1 419 375 92 VAL CA C 62.46 0.1 1 420 375 92 VAL CB C 32.86 0.1 1 421 375 92 VAL N N 120.02 0.05 1 422 376 93 GLU H H 8.60 0.01 1 423 376 93 GLU C C 176.41 0.1 1 424 376 93 GLU CA C 56.42 0.1 1 425 376 93 GLU CB C 30.35 0.1 1 426 376 93 GLU N N 125.21 0.05 1 427 377 94 GLU H H 8.58 0.01 1 428 377 94 GLU C C 176.15 0.1 1 429 377 94 GLU CA C 56.69 0.1 1 430 377 94 GLU CB C 30.26 0.1 1 431 377 94 GLU N N 122.83 0.05 1 432 378 95 ASN H H 8.60 0.01 1 433 378 95 ASN C C 175.02 0.1 1 434 378 95 ASN CA C 53.36 0.1 1 435 378 95 ASN CB C 39.33 0.1 1 436 378 95 ASN N N 120.12 0.05 1 437 379 96 ASP H H 8.48 0.01 1 438 379 96 ASP C C 176.27 0.1 1 439 379 96 ASP CA C 54.63 0.1 1 440 379 96 ASP CB C 41.09 0.1 1 441 379 96 ASP N N 121.63 0.05 1 442 380 97 ASP H H 8.43 0.01 1 443 380 97 ASP C C 176.63 0.1 1 444 380 97 ASP CA C 54.83 0.1 1 445 380 97 ASP CB C 40.79 0.1 1 446 380 97 ASP N N 121.28 0.05 1 447 381 98 LYS H H 8.26 0.01 1 448 381 98 LYS C C 177.20 0.1 1 449 381 98 LYS CA C 56.83 0.1 1 450 381 98 LYS CB C 32.48 0.1 1 451 381 98 LYS N N 120.66 0.05 1 452 382 99 ILE H H 8.16 0.01 1 453 382 99 ILE C C 177.03 0.1 1 454 382 99 ILE CA C 61.65 0.1 1 455 382 99 ILE CB C 38.39 0.1 1 456 382 99 ILE N N 121.58 0.05 1 457 383 100 THR H H 8.35 0.01 1 458 383 100 THR C C 174.83 0.1 1 459 383 100 THR CA C 62.58 0.1 1 460 383 100 THR CB C 69.65 0.1 1 461 383 100 THR N N 119.03 0.05 1 462 384 101 GLN H H 8.48 0.01 1 463 384 101 GLN C C 176.04 0.1 1 464 384 101 GLN CA C 56.04 0.1 1 465 384 101 GLN CB C 29.36 0.1 1 466 384 101 GLN N N 123.20 0.05 1 467 385 102 ALA H H 8.44 0.01 1 468 385 102 ALA C C 178.13 0.1 1 469 385 102 ALA CA C 52.86 0.1 1 470 385 102 ALA CB C 19.13 0.1 1 471 385 102 ALA N N 125.51 0.05 1 472 386 103 SER H H 8.39 0.01 1 473 386 103 SER C C 174.79 0.1 1 474 386 103 SER CA C 58.76 0.1 1 475 386 103 SER CB C 63.74 0.1 1 476 386 103 SER N N 115.30 0.05 1 477 387 104 GLN H H 8.47 0.01 1 478 387 104 GLN C C 176.15 0.1 1 479 387 104 GLN CA C 55.90 0.1 1 480 387 104 GLN CB C 29.46 0.1 1 481 387 104 GLN N N 122.32 0.05 1 482 388 105 SER H H 8.45 0.01 1 483 388 105 SER C C 174.64 0.1 1 484 388 105 SER CA C 58.68 0.1 1 485 388 105 SER CB C 63.79 0.1 1 486 388 105 SER N N 117.32 0.05 1 487 389 106 GLN H H 8.57 0.01 1 488 389 106 GLN C C 176.08 0.1 1 489 389 106 GLN CA C 56.03 0.1 1 490 389 106 GLN CB C 29.50 0.1 1 491 389 106 GLN N N 122.55 0.05 1 492 390 107 GLU H H 8.54 0.01 1 493 390 107 GLU C C 176.61 0.1 1 494 390 107 GLU CA C 56.78 0.1 1 495 390 107 GLU CB C 30.16 0.1 1 496 390 107 GLU N N 122.14 0.05 1 497 391 108 SER H H 8.42 0.01 1 498 391 108 SER C C 174.69 0.1 1 499 391 108 SER CA C 58.49 0.1 1 500 391 108 SER CB C 63.96 0.1 1 501 391 108 SER N N 116.76 0.05 1 502 392 109 GLU H H 8.54 0.01 1 503 392 109 GLU C C 175.87 0.1 1 504 392 109 GLU CA C 56.81 0.1 1 505 392 109 GLU CB C 30.17 0.1 1 506 392 109 GLU N N 123.12 0.05 1 507 393 110 ASP H H 8.35 0.01 1 508 393 110 ASP C C 176.12 0.1 1 509 393 110 ASP CA C 54.07 0.1 1 510 393 110 ASP CB C 41.05 0.1 1 511 393 110 ASP N N 120.98 0.05 1 512 394 111 TYR H H 8.26 0.01 1 513 394 111 TYR C C 175.95 0.1 1 514 394 111 TYR CA C 58.17 0.1 1 515 394 111 TYR CB C 38.36 0.1 1 516 394 111 TYR N N 122.11 0.05 1 517 395 112 SER H H 8.23 0.01 1 518 395 112 SER C C 173.90 0.1 1 519 395 112 SER CA C 58.43 0.1 1 520 395 112 SER CB C 63.92 0.1 1 521 395 112 SER N N 118.08 0.05 1 522 396 113 GLN H H 8.31 0.01 1 523 396 113 GLN C C 173.98 0.1 1 524 396 113 GLN CA C 53.60 0.1 1 525 396 113 GLN CB C 28.85 0.1 1 526 396 113 GLN N N 123.01 0.05 1 527 397 114 PRO C C 177.13 0.1 1 528 397 114 PRO CA C 63.29 0.1 1 529 397 114 PRO CB C 32.26 0.1 1 530 398 115 SER H H 8.67 0.01 1 531 398 115 SER C C 175.23 0.1 1 532 398 115 SER CA C 58.45 0.1 1 533 398 115 SER CB C 63.85 0.1 1 534 398 115 SER N N 116.70 0.05 1 535 399 116 THR H H 8.36 0.01 1 536 399 116 THR C C 174.84 0.1 1 537 399 116 THR CA C 61.98 0.1 1 538 399 116 THR CB C 69.83 0.1 1 539 399 116 THR N N 115.89 0.05 1 540 400 117 SER H H 8.44 0.01 1 541 400 117 SER C C 174.73 0.1 1 542 400 117 SER CA C 58.60 0.1 1 543 400 117 SER CB C 63.86 0.1 1 544 400 117 SER N N 118.05 0.05 1 545 401 118 SER H H 8.47 0.01 1 546 401 118 SER C C 174.59 0.1 1 547 401 118 SER CA C 58.59 0.1 1 548 401 118 SER CB C 63.81 0.1 1 549 401 118 SER N N 118.14 0.05 1 550 402 119 SER H H 8.41 0.01 1 551 402 119 SER C C 174.24 0.1 1 552 402 119 SER CA C 58.65 0.1 1 553 402 119 SER CB C 63.86 0.1 1 554 402 119 SER N N 118.24 0.05 1 555 403 120 ILE H H 8.13 0.01 1 556 403 120 ILE C C 175.74 0.1 1 557 403 120 ILE CA C 61.36 0.1 1 558 403 120 ILE CB C 38.65 0.1 1 559 403 120 ILE N N 123.35 0.05 1 560 404 121 ILE H H 8.22 0.01 1 561 404 121 ILE C C 175.96 0.1 1 562 404 121 ILE CA C 60.77 0.1 1 563 404 121 ILE CB C 38.51 0.1 1 564 404 121 ILE N N 125.76 0.05 1 565 405 122 TYR H H 8.49 0.01 1 566 405 122 TYR C C 175.80 0.1 1 567 405 122 TYR CA C 58.07 0.1 1 568 405 122 TYR CB C 39.02 0.1 1 569 405 122 TYR N N 126.09 0.05 1 570 406 123 SER H H 8.35 0.01 1 571 406 123 SER C C 174.26 0.1 1 572 406 123 SER CA C 58.28 0.1 1 573 406 123 SER CB C 64.06 0.1 1 574 406 123 SER N N 118.40 0.05 1 575 407 124 SER H H 8.51 0.01 1 576 407 124 SER C C 174.73 0.1 1 577 407 124 SER CA C 58.51 0.1 1 578 407 124 SER CB C 63.81 0.1 1 579 407 124 SER N N 118.38 0.05 1 580 408 125 GLN H H 8.54 0.01 1 581 408 125 GLN N N 122.39 0.05 1 582 409 126 GLU C C 176.24 0.1 1 583 409 126 GLU CA C 56.78 0.1 1 584 409 126 GLU CB C 30.25 0.1 1 585 410 127 ASP H H 8.43 0.01 1 586 410 127 ASP C C 176.18 0.1 1 587 410 127 ASP CA C 54.45 0.1 1 588 410 127 ASP CB C 41.04 0.1 1 589 410 127 ASP N N 121.71 0.05 1 590 411 128 VAL H H 8.14 0.01 1 591 411 128 VAL C C 176.29 0.1 1 592 411 128 VAL CA C 62.57 0.1 1 593 411 128 VAL CB C 32.49 0.1 1 594 411 128 VAL N N 121.21 0.05 1 595 412 129 LYS H H 8.46 0.01 1 596 412 129 LYS C C 176.63 0.1 1 597 412 129 LYS CA C 56.12 0.1 1 598 412 129 LYS CB C 32.90 0.1 1 599 412 129 LYS N N 125.69 0.05 1 600 413 130 GLU H H 8.43 0.01 1 601 413 130 GLU C C 176.25 0.1 1 602 413 130 GLU CA C 56.83 0.1 1 603 413 130 GLU CB C 30.21 0.1 1 604 413 130 GLU N N 122.29 0.05 1 605 414 131 PHE H H 8.26 0.01 1 606 414 131 PHE C C 175.65 0.1 1 607 414 131 PHE CA C 57.79 0.1 1 608 414 131 PHE CB C 39.61 0.1 1 609 414 131 PHE N N 120.53 0.05 1 610 415 132 GLU H H 8.36 0.01 1 611 415 132 GLU C C 176.01 0.1 1 612 415 132 GLU CA C 56.39 0.1 1 613 415 132 GLU CB C 30.28 0.1 1 614 415 132 GLU N N 122.76 0.05 1 615 416 133 ARG H H 8.36 0.01 1 616 416 133 ARG C C 176.24 0.1 1 617 416 133 ARG CA C 56.24 0.1 1 618 416 133 ARG CB C 30.96 0.1 1 619 416 133 ARG N N 122.57 0.05 1 620 417 134 GLU H H 8.63 0.01 1 621 417 134 GLU C C 176.58 0.1 1 622 417 134 GLU CA C 56.56 0.1 1 623 417 134 GLU CB C 30.30 0.1 1 624 417 134 GLU N N 123.07 0.05 1 625 418 135 GLU H H 8.67 0.01 1 626 418 135 GLU C C 176.75 0.1 1 627 418 135 GLU CA C 56.61 0.1 1 628 418 135 GLU CB C 30.26 0.1 1 629 418 135 GLU N N 122.92 0.05 1 630 419 136 THR H H 8.37 0.01 1 631 419 136 THR C C 174.57 0.1 1 632 419 136 THR CA C 62.05 0.1 1 633 419 136 THR CB C 69.84 0.1 1 634 419 136 THR N N 115.97 0.05 1 635 420 137 GLN H H 8.54 0.01 1 636 420 137 GLN C C 175.70 0.1 1 637 420 137 GLN CB C 29.63 0.1 1 638 420 137 GLN N N 123.04 0.05 1 639 421 138 ASP H H 8.54 0.01 1 640 421 138 ASP C C 176.15 0.1 1 641 421 138 ASP CA C 54.66 0.1 1 642 421 138 ASP CB C 41.01 0.1 1 643 421 138 ASP N N 122.32 0.05 1 644 422 139 LYS H H 8.38 0.01 1 645 422 139 LYS C C 176.58 0.1 1 646 422 139 LYS CA C 56.17 0.1 1 647 422 139 LYS CB C 33.18 0.1 1 648 422 139 LYS N N 121.97 0.05 1 649 423 140 GLU H H 8.57 0.01 1 650 423 140 GLU C C 176.08 0.1 1 651 423 140 GLU CA C 56.34 0.1 1 652 423 140 GLU CB C 30.10 0.1 1 653 423 140 GLU N N 122.71 0.05 1 654 424 141 GLU H H 8.45 0.01 1 655 424 141 GLU C C 176.48 0.1 1 656 424 141 GLU CA C 56.42 0.1 1 657 424 141 GLU CB C 30.41 0.1 1 658 424 141 GLU N N 121.66 0.05 1 659 425 142 SER H H 8.55 0.01 1 660 425 142 SER C C 174.66 0.1 1 661 425 142 SER CA C 58.18 0.1 1 662 425 142 SER CB C 63.83 0.1 1 663 425 142 SER N N 117.90 0.05 1 664 426 143 VAL H H 8.38 0.01 1 665 426 143 VAL C C 176.49 0.1 1 666 426 143 VAL CA C 62.40 0.1 1 667 426 143 VAL CB C 32.80 0.1 1 668 426 143 VAL N N 122.46 0.05 1 669 427 144 GLU H H 8.63 0.01 1 670 427 144 GLU C C 176.67 0.1 1 671 427 144 GLU CA C 56.79 0.1 1 672 427 144 GLU CB C 30.13 0.1 1 673 427 144 GLU N N 124.88 0.05 1 674 428 145 SER H H 8.49 0.01 1 675 428 145 SER C C 174.56 0.1 1 676 428 145 SER CA C 58.51 0.1 1 677 428 145 SER CB C 63.86 0.1 1 678 428 145 SER N N 117.47 0.05 1 679 429 146 SER H H 8.44 0.01 1 680 429 146 SER C C 174.13 0.1 1 681 429 146 SER CA C 58.33 0.1 1 682 429 146 SER CB C 63.89 0.1 1 683 429 146 SER N N 118.41 0.05 1 684 430 147 LEU H H 8.27 0.01 1 685 430 147 LEU C C 175.25 0.1 1 686 430 147 LEU CA C 53.33 0.1 1 687 430 147 LEU CB C 41.60 0.1 1 688 430 147 LEU N N 125.34 0.05 1 689 431 148 PRO C C 176.85 0.1 1 690 431 148 PRO CA C 62.97 0.1 1 691 431 148 PRO CB C 31.94 0.1 1 692 432 149 LEU H H 8.47 0.01 1 693 432 149 LEU C C 177.35 0.1 1 694 432 149 LEU CA C 55.36 0.1 1 695 432 149 LEU CB C 42.45 0.1 1 696 432 149 LEU N N 122.60 0.05 1 697 433 150 ASN H H 8.51 0.01 1 698 433 150 ASN C C 173.80 0.1 1 699 433 150 ASN CA C 53.17 0.1 1 700 433 150 ASN CB C 38.97 0.1 1 701 433 150 ASN N N 119.63 0.05 1 702 434 151 ALA H H 7.94 0.01 1 703 434 151 ALA CA C 53.88 0.1 1 704 434 151 ALA CB C 20.19 0.1 1 705 434 151 ALA N N 129.65 0.05 1 stop_ save_