data_28020 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for human Mdm2 (residues 284 to 434) phosphorylated by DNA-PK ; _BMRB_accession_number 28020 _BMRB_flat_file_name bmr28020.str _Entry_type original _Submission_date 2019-09-24 _Accession_date 2019-09-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Human Mdm2 fragment 284-434, C362A-C374A; phosphorylated on T351, S386, S388, S395, S402, S407, T419 and S429 by DNA-PK (DNA-PKc+Ku70+Ku80+calf thymus DNA); 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" 133 "13C chemical shifts" 415 "15N chemical shifts" 133 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-10-25 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 28011 'non-modified human Mdm2(aa284-434)' stop_ _Original_release_date 2019-09-24 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 Bouguechtouli Chafiaa . . 4 Bermel Wolfgang . . 5 Ghouil Rania . . 6 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 DNA-damage Mdm2 NMR p53 phosphorylation stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name pMdm2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label pMdm2 $pMdm2 Zn2+ $entity_ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_pMdm2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common pMdm2 _Molecular_mass . _Mol_thiol_state 'all other bound' loop_ _Biological_function 'E3-ubiquitin ligase' 'p53 binding' 'ribosomal proteins binding' stop_ _Details 'The following residues are phosphorylated : T351, S386, S388, S395, S402, S407, T419, S429.' ############################## # 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 _Details $pMdm2 Mouse 10090 Eukaryota Metazoa Mus musculus 'The following residues are phosphorylated : T351, S386, S388, S395, S402, S407, T419, S429' 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 $pMdm2 'recombinant technology' . Escherichia coli . pET41 ; The following residues are phosphorylated : T351, S386, S388, S395, S402, S407, T419, S429. Phosphorylation was obtained upon reaction with purified, commercial DNA-PK ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'DNA-PK, ATP and Mg2+ were removed from the sample using size-exclusion chromatography.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $pMdm2 200 uM '[U-99% 13C; U-99% 15N]' $entity_ZN 1 mM 'natural abundance' HEPES 20 mM 'natural abundance' 'sodium chloride' 50 mM '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 . 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 'TCI cryoprobe, Avance NEO' 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_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 70 . mM pH 7.0 . 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 'Internal 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 HNCA' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name pMdm2 _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 43.34 0.1 1 2 285 2 GLU H H 8.90 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 30.13 0.1 1 6 285 2 GLU N N 120.50 0.5 1 7 286 3 SER H H 8.62 0.01 1 8 286 3 SER C C 174.44 0.1 1 9 286 3 SER CA C 58.16 0.1 1 10 286 3 SER CB C 63.69 0.1 1 11 286 3 SER N N 115.72 0.5 1 12 287 4 ASP H H 8.36 0.01 1 13 287 4 ASP C C 176.53 0.1 1 14 287 4 ASP CA C 54.70 0.1 1 15 287 4 ASP CB C 41.10 0.1 1 16 287 4 ASP N N 122.26 0.5 1 17 288 5 THR H H 8.19 0.01 1 18 288 5 THR C C 174.51 0.1 1 19 288 5 THR CA C 61.95 0.1 1 20 288 5 THR CB C 69.77 0.1 1 21 288 5 THR N N 113.57 0.5 1 22 289 6 ASP H H 8.39 0.01 1 23 289 6 ASP C C 176.11 0.1 1 24 289 6 ASP CA C 54.53 0.1 1 25 289 6 ASP CB C 41.25 0.1 1 26 289 6 ASP N N 122.95 0.5 1 27 290 7 SER H H 8.23 0.01 1 28 290 7 SER C C 174.09 0.1 1 29 290 7 SER CA C 58.22 0.1 1 30 290 7 SER CB C 63.81 0.1 1 31 290 7 SER N N 116.00 0.5 1 32 291 8 PHE H H 8.34 0.01 1 33 291 8 PHE C C 175.49 0.1 1 34 291 8 PHE CA C 57.81 0.1 1 35 291 8 PHE CB C 39.64 0.1 1 36 291 8 PHE N N 122.55 0.5 1 37 292 9 GLU H H 8.31 0.01 1 38 292 9 GLU C C 175.79 0.1 1 39 292 9 GLU CA C 56.16 0.1 1 40 292 9 GLU CB C 30.72 0.1 1 41 292 9 GLU N N 123.16 0.5 1 42 293 10 GLU H H 8.43 0.01 1 43 293 10 GLU C C 175.93 0.1 1 44 293 10 GLU CA C 56.22 0.1 1 45 293 10 GLU CB C 30.58 0.1 1 46 293 10 GLU N N 122.59 0.5 1 47 294 11 ASP H H 8.66 0.01 1 48 294 11 ASP C C 174.82 0.1 1 49 294 11 ASP CA C 52.33 0.1 1 50 294 11 ASP CB C 40.95 0.1 1 51 294 11 ASP N N 123.81 0.5 1 52 295 12 PRO C C 177.24 0.1 1 53 295 12 PRO CA C 63.44 0.1 1 54 295 12 PRO CB C 32.11 0.1 1 55 296 13 GLU H H 8.58 0.01 1 56 296 13 GLU C C 176.92 0.1 1 57 296 13 GLU CA C 56.86 0.1 1 58 296 13 GLU CB C 29.91 0.1 1 59 296 13 GLU N N 120.20 0.5 1 60 297 14 ILE H H 8.10 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 38.84 0.1 1 64 297 14 ILE N N 121.94 0.5 1 65 298 15 SER H H 8.53 0.01 1 66 298 15 SER C C 175.36 0.1 1 67 298 15 SER CA C 58.14 0.1 1 68 298 15 SER CB C 63.68 0.1 1 69 298 15 SER N N 119.69 0.5 1 70 299 16 LEU H H 8.40 0.01 1 71 299 16 LEU C C 178.18 0.1 1 72 299 16 LEU CB C 41.22 0.1 1 73 299 16 LEU N N 125.15 0.5 1 74 300 17 ALA H H 8.00 0.01 1 75 300 17 ALA C C 177.93 0.1 1 76 300 17 ALA CA C 54.06 0.1 1 77 300 17 ALA CB C 18.86 0.1 1 78 300 17 ALA N N 122.98 0.5 1 79 301 18 ASP H H 8.45 0.01 1 80 301 18 ASP N N 115.57 0.5 1 81 302 19 TYR H H 7.92 0.01 1 82 302 19 TYR C C 175.89 0.1 1 83 302 19 TYR CA C 58.78 0.1 1 84 302 19 TYR CB C 39.10 0.1 1 85 302 19 TYR N N 122.09 0.5 1 86 303 20 TRP H H 9.26 0.01 1 87 303 20 TRP C C 173.58 0.1 1 88 303 20 TRP CA C 53.76 0.1 1 89 303 20 TRP CB C 31.56 0.1 1 90 303 20 TRP N N 119.33 0.5 1 91 304 21 LYS H H 8.93 0.01 1 92 304 21 LYS C C 176.51 0.1 1 93 304 21 LYS CA C 55.11 0.1 1 94 304 21 LYS CB C 34.50 0.1 1 95 304 21 LYS N N 123.95 0.5 1 96 305 22 CYS H H 9.06 0.01 1 97 305 22 CYS C C 178.09 0.1 1 98 305 22 CYS CA C 59.83 0.1 1 99 305 22 CYS CB C 31.11 0.1 1 100 305 22 CYS N N 131.79 0.5 1 101 306 23 THR H H 8.87 0.01 1 102 306 23 THR C C 175.47 0.1 1 103 306 23 THR CA C 63.78 0.1 1 104 306 23 THR CB C 68.69 0.1 1 105 306 23 THR N N 122.22 0.5 1 106 307 24 SER H H 9.32 0.01 1 107 307 24 SER C C 175.55 0.1 1 108 307 24 SER CA C 61.22 0.1 1 109 307 24 SER CB C 63.87 0.1 1 110 307 24 SER N N 120.85 0.5 1 111 308 25 CYS H H 8.80 0.01 1 112 308 25 CYS C C 176.58 0.1 1 113 308 25 CYS CA C 59.22 0.1 1 114 308 25 CYS CB C 32.84 0.1 1 115 308 25 CYS N N 121.05 0.5 1 116 309 26 ASN H H 7.83 0.01 1 117 309 26 ASN C C 173.37 0.1 1 118 309 26 ASN CA C 56.15 0.1 1 119 309 26 ASN CB C 37.73 0.1 1 120 309 26 ASN N N 117.12 0.5 1 121 310 27 GLU H H 8.68 0.01 1 122 310 27 GLU N N 124.22 0.5 1 123 311 28 MET C C 176.27 0.1 1 124 312 29 ASN H H 9.24 0.01 1 125 312 29 ASN CA C 51.17 0.1 1 126 312 29 ASN CB C 43.45 0.1 1 127 312 29 ASN N N 124.75 0.5 1 128 314 31 PRO C C 178.69 0.1 1 129 314 31 PRO CA C 65.34 0.1 1 130 315 32 LEU H H 8.14 0.01 1 131 315 32 LEU C C 175.09 0.1 1 132 315 32 LEU CA C 58.80 0.1 1 133 315 32 LEU CB C 40.26 0.1 1 134 315 32 LEU N N 117.75 0.5 1 135 316 33 PRO C C 176.57 0.1 1 136 317 34 SER H H 8.43 0.01 1 137 317 34 SER N N 114.15 0.5 1 138 318 35 HIS H H 7.56 0.01 1 139 318 35 HIS C C 173.66 0.1 1 140 318 35 HIS CA C 54.06 0.1 1 141 318 35 HIS CB C 31.71 0.1 1 142 318 35 HIS N N 117.15 0.5 1 143 319 36 CYS H H 9.00 0.01 1 144 319 36 CYS C C 177.35 0.1 1 145 319 36 CYS CA C 58.90 0.1 1 146 319 36 CYS CB C 31.09 0.1 1 147 319 36 CYS N N 124.19 0.5 1 148 320 37 ASN H H 9.06 0.01 1 149 320 37 ASN C C 174.88 0.1 1 150 320 37 ASN CA C 55.16 0.1 1 151 320 37 ASN CB C 38.82 0.1 1 152 320 37 ASN N N 127.85 0.5 1 153 321 38 ARG H H 9.37 0.01 1 154 321 38 ARG C C 176.87 0.1 1 155 321 38 ARG CA C 57.59 0.1 1 156 321 38 ARG CB C 31.24 0.1 1 157 321 38 ARG N N 122.26 0.5 1 158 322 39 CYS H H 8.56 0.01 1 159 322 39 CYS C C 176.58 0.1 1 160 322 39 CYS N N 119.19 0.5 1 161 323 40 TRP H H 7.85 0.01 1 162 323 40 TRP C C 175.11 0.1 1 163 323 40 TRP CA C 60.09 0.1 1 164 323 40 TRP CB C 28.28 0.1 1 165 323 40 TRP N N 121.32 0.5 1 166 324 41 ALA H H 9.08 0.01 1 167 324 41 ALA C C 178.57 0.1 1 168 324 41 ALA CA C 53.74 0.1 1 169 324 41 ALA CB C 20.45 0.1 1 170 324 41 ALA N N 126.75 0.5 1 171 325 42 LEU H H 8.61 0.01 1 172 325 42 LEU C C 177.22 0.1 1 173 325 42 LEU CA C 55.10 0.1 1 174 325 42 LEU CB C 42.91 0.1 1 175 325 42 LEU N N 123.69 0.5 1 176 326 43 ARG H H 8.01 0.01 1 177 326 43 ARG C C 175.93 0.1 1 178 326 43 ARG CA C 56.95 0.1 1 179 326 43 ARG CB C 30.17 0.1 1 180 326 43 ARG N N 125.30 0.5 1 181 327 44 GLU C C 176.93 0.1 1 182 328 45 ASN H H 8.49 0.01 1 183 328 45 ASN C C 176.93 0.1 1 184 328 45 ASN CA C 56.83 0.1 1 185 328 45 ASN CB C 38.68 0.1 1 186 328 45 ASN N N 118.86 0.5 1 187 329 46 TRP H H 8.07 0.01 1 188 329 46 TRP C C 175.33 0.1 1 189 329 46 TRP CA C 61.29 0.1 1 190 329 46 TRP CB C 29.93 0.1 1 191 329 46 TRP N N 121.75 0.5 1 192 330 47 LEU H H 8.00 0.01 1 193 330 47 LEU C C 174.41 0.1 1 194 330 47 LEU CA C 52.52 0.1 1 195 330 47 LEU CB C 42.14 0.1 1 196 330 47 LEU N N 126.19 0.5 1 197 331 48 PRO C C 177.18 0.1 1 198 331 48 PRO CA C 63.15 0.1 1 199 331 48 PRO CB C 32.15 0.1 1 200 332 49 GLU H H 8.62 0.01 1 201 332 49 GLU C C 176.33 0.1 1 202 332 49 GLU CA C 56.73 0.1 1 203 332 49 GLU CB C 30.32 0.1 1 204 332 49 GLU N N 120.90 0.5 1 205 333 50 ASP H H 8.47 0.01 1 206 333 50 ASP C C 176.59 0.1 1 207 333 50 ASP CA C 54.37 0.1 1 208 333 50 ASP CB C 41.23 0.1 1 209 333 50 ASP N N 122.22 0.5 1 210 334 51 LYS H H 8.43 0.01 1 211 334 51 LYS C C 177.39 0.1 1 212 334 51 LYS CA C 56.70 0.1 1 213 334 51 LYS CB C 32.64 0.1 1 214 334 51 LYS N N 122.91 0.5 1 215 335 52 GLY H H 8.59 0.01 1 216 335 52 GLY C C 174.44 0.1 1 217 335 52 GLY CA C 45.42 0.1 1 218 335 52 GLY N N 109.53 0.5 1 219 336 53 LYS H H 8.12 0.01 1 220 336 53 LYS C C 176.57 0.1 1 221 336 53 LYS CA C 56.34 0.1 1 222 336 53 LYS CB C 32.94 0.1 1 223 336 53 LYS N N 120.74 0.5 1 224 337 54 ASP H H 8.50 0.01 1 225 337 54 ASP C C 176.53 0.1 1 226 337 54 ASP CA C 54.55 0.1 1 227 337 54 ASP CB C 41.19 0.1 1 228 337 54 ASP N N 121.45 0.5 1 229 338 55 LYS H H 8.45 0.01 1 230 338 55 LYS C C 177.32 0.1 1 231 338 55 LYS CA C 56.57 0.1 1 232 338 55 LYS CB C 32.70 0.1 1 233 338 55 LYS N N 122.25 0.5 1 234 339 56 GLY H H 8.52 0.01 1 235 339 56 GLY C C 174.14 0.1 1 236 339 56 GLY CA C 45.33 0.1 1 237 339 56 GLY N N 109.53 0.5 1 238 340 57 GLU H H 8.33 0.01 1 239 340 57 GLU C C 176.83 0.1 1 240 340 57 GLU CA C 56.49 0.1 1 241 340 57 GLU CB C 30.38 0.1 1 242 340 57 GLU N N 120.84 0.5 1 243 341 58 ILE H H 8.38 0.01 1 244 341 58 ILE C C 176.52 0.1 1 245 341 58 ILE CA C 61.39 0.1 1 246 341 58 ILE CB C 38.47 0.1 1 247 341 58 ILE N N 122.49 0.5 1 248 342 59 SER H H 8.49 0.01 1 249 342 59 SER C C 174.77 0.1 1 250 342 59 SER CA C 58.47 0.1 1 251 342 59 SER CB C 63.81 0.1 1 252 342 59 SER N N 120.28 0.5 1 253 343 60 GLU H H 8.57 0.01 1 254 343 60 GLU C C 176.84 0.1 1 255 343 60 GLU CA C 56.98 0.1 1 256 343 60 GLU CB C 30.08 0.1 1 257 343 60 GLU N N 123.50 0.5 1 258 344 61 LYS C C 176.76 0.1 1 259 344 61 LYS CA C 56.62 0.1 1 260 344 61 LYS CB C 32.89 0.1 1 261 345 62 ALA H H 8.31 0.01 1 262 345 62 ALA C C 178.05 0.1 1 263 345 62 ALA CA C 52.81 0.1 1 264 345 62 ALA CB C 19.06 0.1 1 265 345 62 ALA N N 124.88 0.5 1 266 346 63 LYS H H 8.27 0.01 1 267 346 63 LYS C C 176.86 0.1 1 268 346 63 LYS CA C 56.63 0.1 1 269 346 63 LYS CB C 32.93 0.1 1 270 346 63 LYS N N 120.79 0.5 1 271 347 64 LEU H H 8.30 0.01 1 272 347 64 LEU C C 177.61 0.1 1 273 347 64 LEU CA C 55.27 0.1 1 274 347 64 LEU CB C 42.22 0.1 1 275 347 64 LEU N N 123.52 0.5 1 276 348 65 GLU H H 8.45 0.01 1 277 348 65 GLU C C 176.23 0.1 1 278 348 65 GLU CA C 56.59 0.1 1 279 348 65 GLU CB C 30.24 0.1 1 280 348 65 GLU N N 121.47 0.5 1 281 349 66 ASN H H 8.56 0.01 1 282 349 66 ASN C C 175.08 0.1 1 283 349 66 ASN CA C 53.28 0.1 1 284 349 66 ASN CB C 38.90 0.1 1 285 349 66 ASN N N 119.46 0.5 1 286 350 67 SER H H 8.61 0.01 1 287 350 67 SER C C 174.69 0.1 1 288 350 67 SER CA C 58.50 0.1 1 289 350 67 SER CB C 64.13 0.1 1 290 350 67 SER N N 117.58 0.5 1 291 351 68 THR H H 9.18 0.01 1 292 351 68 THR C C 174.55 0.1 1 293 351 68 THR CA C 63.34 0.1 1 294 351 68 THR CB C 72.21 0.1 1 295 351 68 THR N N 120.11 0.5 1 296 352 69 GLN H H 8.65 0.01 1 297 352 69 GLN C C 175.58 0.1 1 298 352 69 GLN CA C 55.70 0.1 1 299 352 69 GLN CB C 29.36 0.1 1 300 352 69 GLN N N 124.50 0.5 1 301 353 70 ALA H H 8.41 0.01 1 302 353 70 ALA C C 177.84 0.1 1 303 353 70 ALA CA C 52.56 0.1 1 304 353 70 ALA CB C 19.40 0.1 1 305 353 70 ALA N N 126.11 0.5 1 306 354 71 GLU H H 8.50 0.01 1 307 354 71 GLU C C 176.61 0.1 1 308 354 71 GLU CA C 56.51 0.1 1 309 354 71 GLU CB C 30.41 0.1 1 310 354 71 GLU N N 120.79 0.5 1 311 355 72 GLU H H 8.56 0.01 1 312 355 72 GLU C C 176.92 0.1 1 313 355 72 GLU CA C 56.83 0.1 1 314 355 72 GLU CB C 30.15 0.1 1 315 355 72 GLU N N 122.50 0.5 1 316 356 73 GLY H H 8.50 0.01 1 317 356 73 GLY C C 173.87 0.1 1 318 356 73 GLY CA C 45.12 0.1 1 319 356 73 GLY N N 110.01 0.5 1 320 357 74 PHE H H 8.12 0.01 1 321 357 74 PHE C C 175.40 0.1 1 322 357 74 PHE CA C 57.53 0.1 1 323 357 74 PHE CB C 39.68 0.1 1 324 357 74 PHE N N 119.65 0.5 1 325 358 75 ASP H H 8.49 0.01 1 326 358 75 ASP C C 175.58 0.1 1 327 358 75 ASP CA C 53.96 0.1 1 328 358 75 ASP CB C 41.27 0.1 1 329 358 75 ASP N N 121.99 0.5 1 330 359 76 VAL H H 8.15 0.01 1 331 359 76 VAL C C 174.68 0.1 1 332 359 76 VAL CA C 59.92 0.1 1 333 359 76 VAL CB C 32.57 0.1 1 334 359 76 VAL N N 122.01 0.5 1 335 360 77 PRO C C 176.90 0.1 1 336 360 77 PRO CA C 63.36 0.1 1 337 360 77 PRO CB C 32.25 0.1 1 338 361 78 ASP H H 8.52 0.01 1 339 361 78 ASP C C 176.48 0.1 1 340 361 78 ASP CA C 54.66 0.1 1 341 361 78 ASP CB C 41.10 0.1 1 342 361 78 ASP N N 120.56 0.5 1 343 362 79 ALA H H 8.38 0.01 1 344 362 79 ALA C C 178.15 0.1 1 345 362 79 ALA CA C 52.97 0.1 1 346 362 79 ALA CB C 19.15 0.1 1 347 362 79 ALA N N 124.93 0.5 1 348 363 80 LYS H H 8.37 0.01 1 349 363 80 LYS C C 176.83 0.1 1 350 363 80 LYS CA C 56.39 0.1 1 351 363 80 LYS CB C 32.62 0.1 1 352 363 80 LYS N N 119.53 0.5 1 353 364 81 LYS H H 8.22 0.01 1 354 364 81 LYS C C 176.72 0.1 1 355 364 81 LYS CA C 56.44 0.1 1 356 364 81 LYS CB C 32.97 0.1 1 357 364 81 LYS N N 122.38 0.5 1 358 365 82 THR H H 8.30 0.01 1 359 365 82 THR C C 174.25 0.1 1 360 365 82 THR CA C 62.18 0.1 1 361 365 82 THR CB C 69.73 0.1 1 362 365 82 THR N N 117.13 0.5 1 363 366 83 ILE H H 8.37 0.01 1 364 366 83 ILE C C 176.09 0.1 1 365 366 83 ILE CA C 60.93 0.1 1 366 366 83 ILE CB C 38.52 0.1 1 367 366 83 ILE N N 125.03 0.5 1 368 367 84 VAL H H 8.42 0.01 1 369 367 84 VAL C C 175.77 0.1 1 370 367 84 VAL CA C 62.26 0.1 1 371 367 84 VAL CB C 32.83 0.1 1 372 367 84 VAL N N 125.84 0.5 1 373 368 85 ASN H H 8.68 0.01 1 374 368 85 ASN C C 174.84 0.1 1 375 368 85 ASN CA C 53.23 0.1 1 376 368 85 ASN CB C 39.08 0.1 1 377 368 85 ASN N N 123.65 0.5 1 378 369 86 ASP H H 8.47 0.01 1 379 369 86 ASP C C 176.41 0.1 1 380 369 86 ASP CA C 54.23 0.1 1 381 369 86 ASP CB C 41.22 0.1 1 382 369 86 ASP N N 122.01 0.5 1 383 370 87 SER H H 8.41 0.01 1 384 370 87 SER C C 174.87 0.1 1 385 370 87 SER CA C 58.67 0.1 1 386 370 87 SER CB C 63.65 0.1 1 387 370 87 SER N N 117.00 0.5 1 388 371 88 ARG H H 8.46 0.01 1 389 371 88 ARG C C 176.66 0.1 1 390 371 88 ARG CA C 56.43 0.1 1 391 371 88 ARG CB C 30.65 0.1 1 392 371 88 ARG N N 122.96 0.5 1 393 372 89 GLU H H 8.51 0.01 1 394 372 89 GLU C C 176.64 0.1 1 395 372 89 GLU CA C 56.70 0.1 1 396 372 89 GLU CB C 30.15 0.1 1 397 372 89 GLU N N 121.63 0.5 1 398 373 90 SER H H 8.38 0.01 1 399 373 90 SER C C 174.12 0.1 1 400 373 90 SER CA C 58.18 0.1 1 401 373 90 SER CB C 63.88 0.1 1 402 373 90 SER N N 116.91 0.5 1 403 374 91 ALA H H 8.43 0.01 1 404 374 91 ALA C C 177.69 0.1 1 405 374 91 ALA CA C 52.43 0.1 1 406 374 91 ALA CB C 19.41 0.1 1 407 374 91 ALA N N 126.57 0.5 1 408 375 92 VAL H H 8.23 0.01 1 409 375 92 VAL C C 176.29 0.1 1 410 375 92 VAL CA C 62.36 0.1 1 411 375 92 VAL CB C 32.83 0.1 1 412 375 92 VAL N N 120.02 0.5 1 413 376 93 GLU H H 8.60 0.01 1 414 376 93 GLU C C 176.56 0.1 1 415 376 93 GLU CA C 56.32 0.1 1 416 376 93 GLU CB C 30.38 0.1 1 417 376 93 GLU N N 125.23 0.5 1 418 377 94 GLU H H 8.59 0.01 1 419 377 94 GLU C C 176.16 0.1 1 420 377 94 GLU CA C 56.52 0.1 1 421 377 94 GLU CB C 30.27 0.1 1 422 377 94 GLU N N 122.87 0.5 1 423 378 95 ASN H H 8.62 0.01 1 424 378 95 ASN C C 175.02 0.1 1 425 378 95 ASN CA C 53.28 0.1 1 426 378 95 ASN CB C 39.34 0.1 1 427 378 95 ASN N N 120.18 0.5 1 428 379 96 ASP H H 8.49 0.01 1 429 379 96 ASP C C 176.15 0.1 1 430 379 96 ASP CA C 54.53 0.1 1 431 379 96 ASP CB C 41.19 0.1 1 432 379 96 ASP N N 121.63 0.5 1 433 380 97 ASP H H 8.41 0.01 1 434 380 97 ASP C C 176.43 0.1 1 435 380 97 ASP CA C 54.56 0.1 1 436 380 97 ASP CB C 40.86 0.1 1 437 380 97 ASP N N 121.12 0.5 1 438 381 98 LYS H H 8.24 0.01 1 439 381 98 LYS C C 177.21 0.1 1 440 381 98 LYS CA C 56.37 0.1 1 441 381 98 LYS CB C 32.49 0.1 1 442 381 98 LYS N N 120.94 0.5 1 443 382 99 ILE H H 8.20 0.01 1 444 382 99 ILE C C 176.72 0.1 1 445 382 99 ILE CA C 61.16 0.1 1 446 382 99 ILE CB C 38.46 0.1 1 447 382 99 ILE N N 121.94 0.5 1 448 383 100 THR H H 8.39 0.01 1 449 383 100 THR C C 174.24 0.1 1 450 383 100 THR CA C 62.00 0.1 1 451 383 100 THR CB C 69.74 0.1 1 452 383 100 THR N N 119.64 0.5 1 453 384 101 GLN H H 8.52 0.01 1 454 384 101 GLN C C 175.40 0.1 1 455 384 101 GLN CA C 55.35 0.1 1 456 384 101 GLN CB C 29.65 0.1 1 457 384 101 GLN N N 123.85 0.5 1 458 385 102 ALA H H 8.54 0.01 1 459 385 102 ALA C C 177.90 0.1 1 460 385 102 ALA CA C 52.87 0.1 1 461 385 102 ALA CB C 19.14 0.1 1 462 385 102 ALA N N 126.88 0.5 1 463 386 103 SER H H 8.83 0.01 1 464 386 103 SER C C 174.37 0.1 1 465 386 103 SER CA C 58.18 0.1 1 466 386 103 SER CB C 65.81 0.1 1 467 386 103 SER N N 116.88 0.5 1 468 387 104 GLN H H 8.50 0.01 1 469 387 104 GLN C C 176.02 0.1 1 470 387 104 GLN CA C 55.45 0.1 1 471 387 104 GLN CB C 29.90 0.1 1 472 387 104 GLN N N 122.11 0.5 1 473 388 105 SER H H 9.06 0.01 1 474 388 105 SER C C 174.44 0.1 1 475 388 105 SER CA C 58.15 0.1 1 476 388 105 SER CB C 65.72 0.1 1 477 388 105 SER N N 119.75 0.5 1 478 389 106 GLN H H 8.55 0.01 1 479 389 106 GLN C C 175.91 0.1 1 480 389 106 GLN CA C 55.50 0.1 1 481 389 106 GLN CB C 29.51 0.1 1 482 389 106 GLN N N 121.93 0.5 1 483 390 107 GLU H H 8.63 0.01 1 484 390 107 GLU C C 176.60 0.1 1 485 390 107 GLU CA C 56.51 0.1 1 486 390 107 GLU CB C 29.73 0.1 1 487 390 107 GLU N N 122.85 0.5 1 488 391 108 SER H H 8.52 0.01 1 489 391 108 SER C C 174.61 0.1 1 490 391 108 SER CA C 58.42 0.1 1 491 391 108 SER CB C 64.02 0.1 1 492 391 108 SER N N 117.53 0.5 1 493 392 109 GLU H H 8.61 0.01 1 494 392 109 GLU C C 175.86 0.1 1 495 392 109 GLU CA C 56.36 0.1 1 496 392 109 GLU CB C 30.14 0.1 1 497 392 109 GLU N N 123.23 0.5 1 498 393 110 ASP H H 8.35 0.01 1 499 393 110 ASP C C 175.62 0.1 1 500 393 110 ASP CA C 54.02 0.1 1 501 393 110 ASP CB C 41.09 0.1 1 502 393 110 ASP N N 121.39 0.5 1 503 394 111 TYR H H 8.10 0.01 1 504 394 111 TYR C C 175.88 0.1 1 505 394 111 TYR CA C 57.53 0.1 1 506 394 111 TYR CB C 39.10 0.1 1 507 394 111 TYR N N 121.06 0.5 1 508 395 112 SER H H 8.77 0.01 1 509 395 112 SER C C 173.92 0.1 1 510 395 112 SER CA C 57.40 0.1 1 511 395 112 SER CB C 65.83 0.1 1 512 395 112 SER N N 119.19 0.5 1 513 396 113 GLN H H 8.44 0.01 1 514 396 113 GLN C C 173.99 0.1 1 515 396 113 GLN CA C 53.52 0.1 1 516 396 113 GLN CB C 29.01 0.1 1 517 396 113 GLN N N 123.34 0.5 1 518 397 114 PRO C C 177.13 0.1 1 519 397 114 PRO CA C 63.06 0.1 1 520 397 114 PRO CB C 32.27 0.1 1 521 398 115 SER H H 8.67 0.01 1 522 398 115 SER C C 175.23 0.1 1 523 398 115 SER CA C 58.46 0.1 1 524 398 115 SER CB C 63.86 0.1 1 525 398 115 SER N N 116.77 0.5 1 526 399 116 THR H H 8.37 0.01 1 527 399 116 THR C C 174.85 0.1 1 528 399 116 THR CA C 61.99 0.1 1 529 399 116 THR CB C 69.84 0.1 1 530 399 116 THR N N 115.95 0.5 1 531 400 117 SER H H 8.45 0.01 1 532 400 117 SER C C 174.71 0.1 1 533 400 117 SER CA C 58.61 0.1 1 534 400 117 SER CB C 63.87 0.1 1 535 400 117 SER N N 118.05 0.5 1 536 401 118 SER H H 8.63 0.01 1 537 401 118 SER C C 174.66 0.1 1 538 401 118 SER CA C 58.28 0.1 1 539 401 118 SER CB C 63.93 0.1 1 540 401 118 SER N N 118.81 0.5 1 541 402 119 SER H H 8.96 0.01 1 542 402 119 SER C C 174.12 0.1 1 543 402 119 SER CA C 58.09 0.1 1 544 402 119 SER CB C 65.52 0.1 1 545 402 119 SER N N 119.83 0.5 1 546 403 120 ILE H H 8.16 0.01 1 547 403 120 ILE C C 175.65 0.1 1 548 403 120 ILE CA C 61.21 0.1 1 549 403 120 ILE CB C 38.69 0.1 1 550 403 120 ILE N N 123.49 0.5 1 551 404 121 ILE H H 8.26 0.01 1 552 404 121 ILE C C 175.78 0.1 1 553 404 121 ILE CA C 60.52 0.1 1 554 404 121 ILE CB C 38.62 0.1 1 555 404 121 ILE N N 126.43 0.5 1 556 405 122 TYR H H 8.58 0.01 1 557 405 122 TYR C C 175.53 0.1 1 558 405 122 TYR CA C 58.05 0.1 1 559 405 122 TYR CB C 39.06 0.1 1 560 405 122 TYR N N 126.88 0.5 1 561 406 123 SER H H 8.28 0.01 1 562 406 123 SER C C 174.40 0.1 1 563 406 123 SER CA C 57.55 0.1 1 564 406 123 SER CB C 64.28 0.1 1 565 406 123 SER N N 119.05 0.5 1 566 407 124 SER H H 9.33 0.01 1 567 407 124 SER C C 174.78 0.1 1 568 407 124 SER CA C 58.46 0.1 1 569 407 124 SER CB C 65.58 0.1 1 570 407 124 SER N N 121.15 0.5 1 571 408 125 GLN H H 8.33 0.01 1 572 408 125 GLN C C 175.88 0.1 1 573 408 125 GLN CA C 55.66 0.1 1 574 408 125 GLN N N 121.41 0.5 1 575 409 126 GLU C C 175.92 0.1 1 576 409 126 GLU CA C 56.48 0.1 1 577 409 126 GLU CB C 30.46 0.1 1 578 410 127 ASP H H 8.30 0.01 1 579 410 127 ASP C C 176.12 0.1 1 580 410 127 ASP CA C 54.26 0.1 1 581 410 127 ASP CB C 41.13 0.1 1 582 410 127 ASP N N 121.95 0.5 1 583 411 128 VAL H H 8.19 0.01 1 584 411 128 VAL C C 176.31 0.1 1 585 411 128 VAL CA C 62.54 0.1 1 586 411 128 VAL CB C 32.52 0.1 1 587 411 128 VAL N N 121.39 0.5 1 588 412 129 LYS H H 8.48 0.01 1 589 412 129 LYS C C 176.57 0.1 1 590 412 129 LYS CA C 55.97 0.1 1 591 412 129 LYS CB C 32.91 0.1 1 592 412 129 LYS N N 125.81 0.5 1 593 413 130 GLU H H 8.44 0.01 1 594 413 130 GLU C C 176.24 0.1 1 595 413 130 GLU CA C 56.84 0.1 1 596 413 130 GLU CB C 30.22 0.1 1 597 413 130 GLU N N 122.29 0.5 1 598 414 131 PHE H H 8.26 0.01 1 599 414 131 PHE C C 175.61 0.1 1 600 414 131 PHE CA C 57.80 0.1 1 601 414 131 PHE CB C 39.60 0.1 1 602 414 131 PHE N N 120.58 0.5 1 603 415 132 GLU H H 8.36 0.01 1 604 415 132 GLU C C 176.01 0.1 1 605 415 132 GLU CA C 56.36 0.1 1 606 415 132 GLU CB C 30.55 0.1 1 607 415 132 GLU N N 122.87 0.5 1 608 418 135 GLU C C 176.55 0.1 1 609 418 135 GLU CA C 56.40 0.1 1 610 418 135 GLU CB C 30.49 0.1 1 611 419 136 THR H H 9.23 0.01 1 612 419 136 THR C C 174.41 0.1 1 613 419 136 THR CA C 63.05 0.1 1 614 419 136 THR CB C 72.28 0.1 1 615 419 136 THR N N 120.82 0.5 1 616 420 137 GLN H H 8.77 0.01 1 617 420 137 GLN CA C 55.67 0.1 1 618 420 137 GLN CB C 29.85 0.1 1 619 420 137 GLN N N 125.20 0.5 1 620 421 138 ASP H H 8.39 0.01 1 621 421 138 ASP C C 176.16 0.1 1 622 421 138 ASP CA C 54.54 0.1 1 623 421 138 ASP CB C 41.08 0.1 1 624 421 138 ASP N N 121.99 0.5 1 625 422 139 LYS H H 8.39 0.01 1 626 422 139 LYS C C 176.59 0.1 1 627 422 139 LYS CA C 56.06 0.1 1 628 422 139 LYS CB C 33.24 0.1 1 629 422 139 LYS N N 121.99 0.5 1 630 423 140 GLU H H 8.58 0.01 1 631 423 140 GLU CA C 56.45 0.1 1 632 423 140 GLU CB C 30.13 0.1 1 633 423 140 GLU N N 122.85 0.5 1 634 424 141 GLU C C 176.49 0.1 1 635 424 141 GLU CA C 56.33 0.1 1 636 424 141 GLU CB C 30.44 0.1 1 637 425 142 SER H H 8.55 0.01 1 638 425 142 SER C C 174.67 0.1 1 639 425 142 SER CA C 58.20 0.1 1 640 425 142 SER CB C 63.81 0.1 1 641 425 142 SER N N 117.92 0.5 1 642 426 143 VAL C C 176.17 0.1 1 643 426 143 VAL CA C 62.09 0.1 1 644 426 143 VAL CB C 32.79 0.1 1 645 427 144 GLU H H 8.61 0.01 1 646 427 144 GLU C C 176.30 0.1 1 647 427 144 GLU CA C 56.34 0.1 1 648 427 144 GLU CB C 30.43 0.1 1 649 427 144 GLU N N 125.35 0.5 1 650 428 145 SER H H 8.50 0.01 1 651 428 145 SER C C 174.45 0.1 1 652 428 145 SER CA C 58.20 0.1 1 653 428 145 SER CB C 64.08 0.1 1 654 428 145 SER N N 117.96 0.5 1 655 429 146 SER H H 9.11 0.01 1 656 429 146 SER C C 174.15 0.1 1 657 429 146 SER CA C 57.81 0.1 1 658 429 146 SER CB C 65.76 0.1 1 659 429 146 SER N N 120.05 0.5 1 660 430 147 LEU H H 8.40 0.01 1 661 430 147 LEU C C 175.18 0.1 1 662 430 147 LEU CA C 53.22 0.1 1 663 430 147 LEU CB C 41.78 0.1 1 664 430 147 LEU N N 125.60 0.5 1 665 431 148 PRO C C 176.85 0.1 1 666 431 148 PRO CA C 62.79 0.1 1 667 431 148 PRO CB C 32.10 0.1 1 668 432 149 LEU H H 8.48 0.01 1 669 432 149 LEU C C 177.36 0.1 1 670 432 149 LEU CA C 55.34 0.1 1 671 432 149 LEU CB C 42.48 0.1 1 672 432 149 LEU N N 122.73 0.5 1 673 433 150 ASN H H 8.52 0.01 1 674 433 150 ASN C C 173.79 0.1 1 675 433 150 ASN CA C 53.18 0.1 1 676 433 150 ASN CB C 38.90 0.1 1 677 433 150 ASN N N 119.64 0.5 1 678 434 151 ALA H H 7.94 0.01 1 679 434 151 ALA CA C 53.91 0.1 1 680 434 151 ALA CB C 20.19 0.1 1 681 434 151 ALA N N 129.69 0.5 1 stop_ save_