data_28019 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for mouse Mdm2 (residues 282 to 432) ; _BMRB_accession_number 28019 _BMRB_flat_file_name bmr28019.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 ; Mouse Mdm2 fragment 282-432, C372A; contains a zinc-finger domain (~291-331) 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" 129 "13C chemical shifts" 408 "15N chemical shifts" 129 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-10-25 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 28011 '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 Mdm2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Mdm2 $Mdm2 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_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' 'Ribosomal proteins binding' 'p53 binding' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 151 _Mol_residue_sequence ; GESDTDSFEGDPEISLADYW KCTSCNEMNPPLPSHCKRCW TLRENWLPDDKGKDKVEISE KAKLENSAQAEEGLDVPDGK KLTENDAKEPAAEEDSEEKA EQTPLSQESDDYSQPSTSSS IVYSSQESVKELKEETQDKD ESVESSFSLNA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 282 GLY 2 283 GLU 3 284 SER 4 285 ASP 5 286 THR 6 287 ASP 7 288 SER 8 289 PHE 9 290 GLU 10 291 GLY 11 292 ASP 12 293 PRO 13 294 GLU 14 295 ILE 15 296 SER 16 297 LEU 17 298 ALA 18 299 ASP 19 300 TYR 20 301 TRP 21 302 LYS 22 303 CYS 23 304 THR 24 305 SER 25 306 CYS 26 307 ASN 27 308 GLU 28 309 MET 29 310 ASN 30 311 PRO 31 312 PRO 32 313 LEU 33 314 PRO 34 315 SER 35 316 HIS 36 317 CYS 37 318 LYS 38 319 ARG 39 320 CYS 40 321 TRP 41 322 THR 42 323 LEU 43 324 ARG 44 325 GLU 45 326 ASN 46 327 TRP 47 328 LEU 48 329 PRO 49 330 ASP 50 331 ASP 51 332 LYS 52 333 GLY 53 334 LYS 54 335 ASP 55 336 LYS 56 337 VAL 57 338 GLU 58 339 ILE 59 340 SER 60 341 GLU 61 342 LYS 62 343 ALA 63 344 LYS 64 345 LEU 65 346 GLU 66 347 ASN 67 348 SER 68 349 ALA 69 350 GLN 70 351 ALA 71 352 GLU 72 353 GLU 73 354 GLY 74 355 LEU 75 356 ASP 76 357 VAL 77 358 PRO 78 359 ASP 79 360 GLY 80 361 LYS 81 362 LYS 82 363 LEU 83 364 THR 84 365 GLU 85 366 ASN 86 367 ASP 87 368 ALA 88 369 LYS 89 370 GLU 90 371 PRO 91 372 ALA 92 373 ALA 93 374 GLU 94 375 GLU 95 376 ASP 96 377 SER 97 378 GLU 98 379 GLU 99 380 LYS 100 381 ALA 101 382 GLU 102 383 GLN 103 384 THR 104 385 PRO 105 386 LEU 106 387 SER 107 388 GLN 108 389 GLU 109 390 SER 110 391 ASP 111 392 ASP 112 393 TYR 113 394 SER 114 395 GLN 115 396 PRO 116 397 SER 117 398 THR 118 399 SER 119 400 SER 120 401 SER 121 402 ILE 122 403 VAL 123 404 TYR 124 405 SER 125 406 SER 126 407 GLN 127 408 GLU 128 409 SER 129 410 VAL 130 411 LYS 131 412 GLU 132 413 LEU 133 414 LYS 134 415 GLU 135 416 GLU 136 417 THR 137 418 GLN 138 419 ASP 139 420 LYS 140 421 ASP 141 422 GLU 142 423 SER 143 424 VAL 144 425 GLU 145 426 SER 146 427 SER 147 428 PHE 148 429 SER 149 430 LEU 150 431 ASN 151 432 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type 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_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Mdm2 Mouse 10090 Eukaryota Metazoa Mus musculus 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 500 uM '[U-99% 13C; U-99% 15N]' $entity_ZN 1 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_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_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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 6.85 . 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, internal' 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 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 1 282 1 GLY CA C 43.37 0.1 1 2 283 2 GLU H H 8.89 0.01 1 3 283 2 GLU C C 176.92 0.1 1 4 283 2 GLU CA C 57.33 0.1 1 5 283 2 GLU CB C 30.19 0.1 1 6 283 2 GLU N N 120.51 0.05 1 7 284 3 SER H H 8.61 0.01 1 8 284 3 SER C C 174.41 0.1 1 9 284 3 SER CA C 58.26 0.1 1 10 284 3 SER CB C 63.70 0.1 1 11 284 3 SER N N 115.59 0.05 1 12 285 4 ASP H H 8.35 0.01 1 13 285 4 ASP C C 176.53 0.1 1 14 285 4 ASP CA C 54.65 0.1 1 15 285 4 ASP CB C 41.02 0.1 1 16 285 4 ASP N N 122.30 0.05 1 17 286 5 THR H H 8.19 0.01 1 18 286 5 THR C C 174.54 0.1 1 19 286 5 THR CA C 61.95 0.1 1 20 286 5 THR CB C 69.78 0.1 1 21 286 5 THR N N 113.53 0.05 1 22 287 6 ASP H H 8.40 0.01 1 23 287 6 ASP C C 176.19 0.1 1 24 287 6 ASP CA C 54.59 0.1 1 25 287 6 ASP CB C 41.15 0.1 1 26 287 6 ASP N N 122.94 0.05 1 27 288 7 SER H H 8.23 0.01 1 28 288 7 SER C C 174.12 0.1 1 29 288 7 SER CA C 58.25 0.1 1 30 288 7 SER CB C 63.80 0.1 1 31 288 7 SER N N 116.00 0.05 1 32 289 8 PHE H H 8.39 0.01 1 33 289 8 PHE C C 175.70 0.1 1 34 289 8 PHE CA C 57.76 0.1 1 35 289 8 PHE CB C 39.59 0.1 1 36 289 8 PHE N N 122.69 0.05 1 37 290 9 GLU H H 8.42 0.01 1 38 290 9 GLU C C 176.31 0.1 1 39 290 9 GLU CA C 56.46 0.1 1 40 290 9 GLU CB C 30.36 0.1 1 41 290 9 GLU N N 123.74 0.05 1 42 291 10 GLY H H 7.89 0.01 1 43 291 10 GLY C C 173.26 0.1 1 44 291 10 GLY CA C 44.78 0.1 1 45 291 10 GLY N N 109.71 0.05 1 46 292 11 ASP H H 8.37 0.01 1 47 292 11 ASP C C 174.89 0.1 1 48 292 11 ASP CA C 52.42 0.1 1 49 292 11 ASP CB C 40.99 0.1 1 50 292 11 ASP N N 122.01 0.05 1 51 293 12 PRO C C 177.17 0.1 1 52 293 12 PRO CA C 63.41 0.1 1 53 293 12 PRO CB C 32.11 0.1 1 54 294 13 GLU H H 8.58 0.01 1 55 294 13 GLU C C 176.79 0.1 1 56 294 13 GLU CA C 56.79 0.1 1 57 294 13 GLU CB C 29.89 0.1 1 58 294 13 GLU N N 120.45 0.05 1 59 295 14 ILE H H 8.07 0.01 1 60 295 14 ILE C C 176.20 0.1 1 61 295 14 ILE CA C 61.10 0.1 1 62 295 14 ILE CB C 38.72 0.1 1 63 295 14 ILE N N 121.79 0.05 1 64 296 15 SER H H 8.55 0.01 1 65 296 15 SER CA C 57.91 0.1 1 66 296 15 SER CB C 63.80 0.1 1 67 296 15 SER N N 119.87 0.05 1 68 297 16 LEU C C 178.22 0.1 1 69 297 16 LEU CA C 55.21 0.1 1 70 297 16 LEU CB C 41.21 0.1 1 71 298 17 ALA H H 8.02 0.01 1 72 298 17 ALA C C 177.93 0.1 1 73 298 17 ALA CA C 54.08 0.1 1 74 298 17 ALA CB C 18.82 0.1 1 75 298 17 ALA N N 122.88 0.05 1 76 299 18 ASP H H 8.43 0.01 1 77 299 18 ASP C C 175.92 0.1 1 78 299 18 ASP CA C 54.62 0.1 1 79 299 18 ASP CB C 40.85 0.1 1 80 299 18 ASP N N 115.45 0.05 1 81 300 19 TYR H H 7.88 0.01 1 82 300 19 TYR C C 175.83 0.1 1 83 300 19 TYR CA C 58.75 0.1 1 84 300 19 TYR CB C 38.89 0.1 1 85 300 19 TYR N N 122.05 0.05 1 86 301 20 TRP H H 9.25 0.01 1 87 301 20 TRP C C 173.74 0.1 1 88 301 20 TRP CA C 53.73 0.1 1 89 301 20 TRP CB C 31.60 0.1 1 90 301 20 TRP N N 119.38 0.05 1 91 302 21 LYS H H 8.94 0.01 1 92 302 21 LYS C C 176.60 0.1 1 93 302 21 LYS CA C 55.02 0.1 1 94 302 21 LYS CB C 34.46 0.1 1 95 302 21 LYS N N 123.95 0.05 1 96 303 22 CYS H H 9.05 0.01 1 97 303 22 CYS C C 178.12 0.1 1 98 303 22 CYS CA C 59.88 0.1 1 99 303 22 CYS CB C 31.42 0.1 1 100 303 22 CYS N N 131.75 0.05 1 101 304 23 THR H H 8.88 0.01 1 102 304 23 THR C C 175.38 0.1 1 103 304 23 THR CA C 63.90 0.1 1 104 304 23 THR CB C 68.84 0.1 1 105 304 23 THR N N 122.17 0.05 1 106 305 24 SER H H 9.26 0.01 1 107 305 24 SER C C 175.79 0.1 1 108 305 24 SER CA C 60.78 0.1 1 109 305 24 SER CB C 63.87 0.1 1 110 305 24 SER N N 120.55 0.05 1 111 306 25 CYS H H 8.75 0.01 1 112 306 25 CYS C C 176.79 0.1 1 113 306 25 CYS CA C 59.03 0.1 1 114 306 25 CYS CB C 32.68 0.1 1 115 306 25 CYS N N 120.32 0.05 1 116 307 26 ASN H H 7.79 0.01 1 117 307 26 ASN C C 173.18 0.1 1 118 307 26 ASN CA C 56.10 0.1 1 119 307 26 ASN CB C 37.75 0.1 1 120 307 26 ASN N N 117.15 0.05 1 121 308 27 GLU H H 8.72 0.01 1 122 308 27 GLU C C 175.85 0.1 1 123 308 27 GLU CA C 57.28 0.1 1 124 308 27 GLU CB C 31.58 0.1 1 125 308 27 GLU N N 124.56 0.05 1 126 309 28 MET H H 8.76 0.01 1 127 309 28 MET C C 176.29 0.1 1 128 309 28 MET CA C 52.93 0.1 1 129 309 28 MET CB C 30.76 0.1 1 130 309 28 MET N N 124.06 0.05 1 131 310 29 ASN H H 9.20 0.01 1 132 310 29 ASN C C 179.77 0.1 1 133 310 29 ASN CA C 51.10 0.1 1 134 310 29 ASN CB C 43.10 0.1 1 135 310 29 ASN N N 123.94 0.05 1 136 311 30 PRO CA C 62.50 0.1 1 137 314 33 PRO CA C 62.50 0.1 1 138 315 34 SER H H 8.73 0.01 1 139 315 34 SER C C 172.78 0.1 1 140 315 34 SER CA C 58.37 0.1 1 141 315 34 SER CB C 63.72 0.1 1 142 315 34 SER N N 114.48 0.05 1 143 316 35 HIS H H 7.57 0.01 1 144 316 35 HIS C C 173.74 0.1 1 145 316 35 HIS CA C 54.57 0.1 1 146 316 35 HIS CB C 31.76 0.1 1 147 316 35 HIS N N 117.11 0.05 1 148 317 36 CYS C C 177.12 0.1 1 149 317 36 CYS CA C 58.91 0.1 1 150 318 37 LYS H H 8.91 0.01 1 151 318 37 LYS C C 175.47 0.1 1 152 318 37 LYS CA C 57.86 0.1 1 153 318 37 LYS CB C 31.52 0.1 1 154 318 37 LYS N N 128.09 0.05 1 155 319 38 ARG H H 9.38 0.01 1 156 319 38 ARG C C 176.49 0.1 1 157 319 38 ARG CA C 57.78 0.1 1 158 319 38 ARG N N 124.87 0.05 1 159 321 40 TRP H H 7.88 0.01 1 160 321 40 TRP CA C 59.68 0.1 1 161 321 40 TRP CB C 27.46 0.1 1 162 321 40 TRP N N 120.91 0.05 1 163 326 45 ASN C C 174.25 0.1 1 164 326 45 ASN CA C 53.45 0.1 1 165 326 45 ASN CB C 38.89 0.1 1 166 327 46 TRP H H 8.06 0.01 1 167 327 46 TRP C C 175.36 0.1 1 168 327 46 TRP CA C 57.72 0.1 1 169 327 46 TRP CB C 29.88 0.1 1 170 327 46 TRP N N 121.78 0.05 1 171 328 47 LEU H H 7.91 0.01 1 172 328 47 LEU C C 174.25 0.1 1 173 328 47 LEU CA C 52.46 0.1 1 174 328 47 LEU CB C 42.51 0.1 1 175 328 47 LEU N N 126.38 0.05 1 176 329 48 PRO C C 176.73 0.1 1 177 329 48 PRO CA C 62.99 0.1 1 178 329 48 PRO CB C 31.92 0.1 1 179 330 49 ASP H H 8.42 0.01 1 180 330 49 ASP C C 176.16 0.1 1 181 330 49 ASP CA C 54.24 0.1 1 182 330 49 ASP CB C 41.13 0.1 1 183 330 49 ASP N N 120.41 0.05 1 184 331 50 ASP H H 8.32 0.01 1 185 331 50 ASP C C 176.82 0.1 1 186 331 50 ASP CA C 54.36 0.1 1 187 331 50 ASP CB C 41.02 0.1 1 188 331 50 ASP N N 121.35 0.05 1 189 332 51 LYS H H 8.38 0.01 1 190 332 51 LYS C C 177.57 0.1 1 191 332 51 LYS CA C 56.75 0.1 1 192 332 51 LYS CB C 32.45 0.1 1 193 332 51 LYS N N 121.62 0.05 1 194 333 52 GLY H H 8.55 0.01 1 195 333 52 GLY C C 174.60 0.1 1 196 333 52 GLY CA C 45.56 0.1 1 197 333 52 GLY N N 109.43 0.05 1 198 334 53 LYS H H 8.11 0.01 1 199 334 53 LYS C C 176.57 0.1 1 200 334 53 LYS CA C 56.52 0.1 1 201 334 53 LYS CB C 32.95 0.1 1 202 334 53 LYS N N 120.70 0.05 1 203 335 54 ASP H H 8.44 0.01 1 204 335 54 ASP C C 176.14 0.1 1 205 335 54 ASP CA C 54.59 0.1 1 206 335 54 ASP CB C 40.96 0.1 1 207 335 54 ASP N N 120.90 0.05 1 208 336 55 LYS H H 8.23 0.01 1 209 336 55 LYS CA C 56.39 0.1 1 210 336 55 LYS CB C 32.90 0.1 1 211 336 55 LYS N N 121.59 0.05 1 212 337 56 VAL H H 8.25 0.01 1 213 337 56 VAL C C 176.18 0.1 1 214 337 56 VAL CA C 62.54 0.1 1 215 337 56 VAL CB C 32.62 0.1 1 216 337 56 VAL N N 122.60 0.05 1 217 338 57 GLU H H 8.61 0.01 1 218 338 57 GLU C C 176.60 0.1 1 219 338 57 GLU CA C 56.45 0.1 1 220 338 57 GLU CB C 30.33 0.1 1 221 338 57 GLU N N 125.64 0.05 1 222 339 58 ILE H H 8.42 0.01 1 223 339 58 ILE C C 176.50 0.1 1 224 339 58 ILE CA C 61.44 0.1 1 225 339 58 ILE CB C 38.68 0.1 1 226 339 58 ILE N N 123.06 0.05 1 227 340 59 SER H H 8.48 0.01 1 228 340 59 SER C C 174.85 0.1 1 229 340 59 SER CA C 58.52 0.1 1 230 340 59 SER CB C 63.93 0.1 1 231 340 59 SER N N 120.21 0.05 1 232 341 60 GLU H H 8.59 0.01 1 233 341 60 GLU C C 177.12 0.1 1 234 341 60 GLU CA C 57.23 0.1 1 235 341 60 GLU CB C 30.00 0.1 1 236 341 60 GLU N N 123.45 0.05 1 237 342 61 LYS H H 8.33 0.01 1 238 342 61 LYS C C 176.96 0.1 1 239 342 61 LYS CA C 57.07 0.1 1 240 342 61 LYS CB C 32.91 0.1 1 241 342 61 LYS N N 122.04 0.05 1 242 343 62 ALA H H 8.26 0.01 1 243 343 62 ALA C C 178.32 0.1 1 244 343 62 ALA CA C 53.08 0.1 1 245 343 62 ALA CB C 18.85 0.1 1 246 343 62 ALA N N 124.46 0.05 1 247 344 63 LYS H H 8.23 0.01 1 248 344 63 LYS C C 177.17 0.1 1 249 344 63 LYS CA C 56.90 0.1 1 250 344 63 LYS CB C 32.86 0.1 1 251 344 63 LYS N N 120.49 0.05 1 252 345 64 LEU H H 8.23 0.01 1 253 345 64 LEU C C 177.88 0.1 1 254 345 64 LEU CA C 55.42 0.1 1 255 345 64 LEU CB C 42.14 0.1 1 256 345 64 LEU N N 123.08 0.05 1 257 346 65 GLU H H 8.44 0.01 1 258 346 65 GLU C C 176.55 0.1 1 259 346 65 GLU CA C 56.86 0.1 1 260 346 65 GLU CB C 30.15 0.1 1 261 346 65 GLU N N 121.55 0.05 1 262 347 66 ASN H H 8.50 0.01 1 263 347 66 ASN C C 175.54 0.1 1 264 347 66 ASN CA C 53.44 0.1 1 265 347 66 ASN CB C 38.87 0.1 1 266 347 66 ASN N N 119.53 0.05 1 267 348 67 SER H H 8.35 0.01 1 268 348 67 SER C C 174.51 0.1 1 269 348 67 SER CA C 58.76 0.1 1 270 348 67 SER CB C 63.72 0.1 1 271 348 67 SER N N 116.60 0.1 1 272 349 68 ALA H H 8.39 0.01 1 273 349 68 ALA C C 177.87 0.1 1 274 349 68 ALA CA C 52.77 0.1 1 275 349 68 ALA CB C 19.13 0.1 1 276 349 68 ALA N N 125.91 0.05 1 277 350 69 GLN H H 8.33 0.01 1 278 350 69 GLN C C 175.91 0.1 1 279 350 69 GLN CA C 55.83 0.1 1 280 350 69 GLN CB C 29.42 0.1 1 281 350 69 GLN N N 119.69 0.05 1 282 351 70 ALA H H 8.41 0.01 1 283 351 70 ALA C C 177.91 0.1 1 284 351 70 ALA CA C 52.68 0.1 1 285 351 70 ALA CB C 19.24 0.1 1 286 351 70 ALA N N 125.70 0.05 1 287 352 71 GLU H H 8.49 0.01 1 288 352 71 GLU C C 176.63 0.1 1 289 352 71 GLU CA C 56.55 0.1 1 290 352 71 GLU CB C 30.24 0.1 1 291 352 71 GLU N N 120.49 0.05 1 292 353 72 GLU H H 8.51 0.01 1 293 353 72 GLU C C 177.09 0.1 1 294 353 72 GLU CA C 56.84 0.1 1 295 353 72 GLU CB C 30.27 0.1 1 296 353 72 GLU N N 122.35 0.05 1 297 354 73 GLY H H 8.57 0.01 1 298 354 73 GLY C C 174.18 0.1 1 299 354 73 GLY CA C 45.43 0.1 1 300 354 73 GLY N N 110.03 0.05 1 301 355 74 LEU H H 8.12 0.01 1 302 355 74 LEU C C 177.15 0.1 1 303 355 74 LEU CA C 55.00 0.1 1 304 355 74 LEU CB C 42.51 0.1 1 305 355 74 LEU N N 121.29 0.05 1 306 356 75 ASP H H 8.51 0.01 1 307 356 75 ASP C C 175.74 0.1 1 308 356 75 ASP CA C 54.23 0.1 1 309 356 75 ASP CB C 40.95 0.1 1 310 356 75 ASP N N 121.45 0.05 1 311 357 76 VAL H H 8.14 0.01 1 312 357 76 VAL C C 174.65 0.1 1 313 357 76 VAL CA C 54.23 0.1 1 314 357 76 VAL CB C 32.63 0.1 1 315 357 76 VAL N N 121.94 0.05 1 316 358 77 PRO C C 176.91 0.1 1 317 358 77 PRO CA C 63.42 0.1 1 318 358 77 PRO CB C 32.11 0.1 1 319 359 78 ASP H H 8.53 0.01 1 320 359 78 ASP C C 177.10 0.1 1 321 359 78 ASP CA C 54.52 0.1 1 322 359 78 ASP CB C 41.22 0.1 1 323 359 78 ASP N N 120.70 0.05 1 324 360 79 GLY H H 8.45 0.01 1 325 360 79 GLY C C 174.48 0.1 1 326 360 79 GLY CA C 45.62 0.1 1 327 360 79 GLY N N 109.76 0.05 1 328 361 80 LYS H H 8.22 0.01 1 329 361 80 LYS C C 176.70 0.1 1 330 361 80 LYS CA C 56.46 0.1 1 331 361 80 LYS CB C 32.83 0.1 1 332 361 80 LYS N N 120.98 0.05 1 333 362 81 LYS H H 8.37 0.01 1 334 362 81 LYS C C 176.73 0.1 1 335 362 81 LYS CA C 56.29 0.1 1 336 362 81 LYS CB C 32.90 0.1 1 337 362 81 LYS N N 122.87 0.05 1 338 363 82 LEU H H 8.47 0.01 1 339 363 82 LEU C C 177.72 0.1 1 340 363 82 LEU CA C 55.37 0.1 1 341 363 82 LEU CB C 42.18 0.1 1 342 363 82 LEU N N 124.06 0.05 1 343 364 83 THR H H 8.25 0.01 1 344 364 83 THR C C 174.73 0.1 1 345 364 83 THR CA C 61.69 0.1 1 346 364 83 THR CB C 70.00 0.1 1 347 364 83 THR N N 114.53 0.05 1 348 365 84 GLU H H 8.55 0.01 1 349 365 84 GLU C C 176.35 0.1 1 350 365 84 GLU CA C 56.78 0.1 1 351 365 84 GLU CB C 30.19 0.1 1 352 365 84 GLU N N 123.01 0.05 1 353 366 85 ASN H H 8.54 0.01 1 354 366 85 ASN C C 175.04 0.1 1 355 366 85 ASN CA C 53.49 0.1 1 356 366 85 ASN CB C 39.01 0.1 1 357 366 85 ASN N N 119.51 0.05 1 358 367 86 ASP H H 8.35 0.01 1 359 367 86 ASP C C 175.92 0.1 1 360 367 86 ASP CA C 54.44 0.1 1 361 367 86 ASP CB C 41.07 0.1 1 362 367 86 ASP N N 121.22 0.05 1 363 368 87 ALA H H 8.23 0.01 1 364 368 87 ALA C C 177.55 0.1 1 365 368 87 ALA CA C 52.44 0.1 1 366 368 87 ALA CB C 19.12 0.1 1 367 368 87 ALA N N 124.28 0.05 1 368 369 88 LYS H H 8.33 0.01 1 369 369 88 LYS C C 176.51 0.1 1 370 369 88 LYS CA C 55.86 0.1 1 371 369 88 LYS CB C 33.12 0.1 1 372 369 88 LYS N N 121.08 0.05 1 373 370 89 GLU H H 8.54 0.01 1 374 370 89 GLU C C 174.51 0.1 1 375 370 89 GLU CA C 54.42 0.1 1 376 370 89 GLU CB C 29.47 0.1 1 377 370 89 GLU N N 124.11 0.05 1 378 371 90 PRO C C 176.58 0.1 1 379 371 90 PRO CA C 63.04 0.1 1 380 371 90 PRO CB C 32.14 0.1 1 381 372 91 ALA H H 8.52 0.01 1 382 372 91 ALA C C 177.49 0.1 1 383 372 91 ALA CA C 52.12 0.1 1 384 372 91 ALA CB C 19.35 0.1 1 385 372 91 ALA N N 124.99 0.05 1 386 373 92 ALA H H 8.47 0.01 1 387 373 92 ALA C C 177.95 0.1 1 388 373 92 ALA CA C 52.36 0.1 1 389 373 92 ALA CB C 19.30 0.1 1 390 373 92 ALA N N 124.43 0.05 1 391 374 93 GLU H H 8.56 0.01 1 392 374 93 GLU C C 176.69 0.1 1 393 374 93 GLU CA C 56.48 0.1 1 394 374 93 GLU CB C 30.36 0.1 1 395 374 93 GLU N N 120.88 0.05 1 396 375 94 GLU H H 8.60 0.01 1 397 375 94 GLU C C 176.25 0.1 1 398 375 94 GLU CA C 56.54 0.1 1 399 375 94 GLU CB C 30.37 0.1 1 400 375 94 GLU N N 122.29 0.05 1 401 376 95 ASP C C 176.36 0.1 1 402 376 95 ASP CA C 54.33 0.1 1 403 376 95 ASP CB C 41.04 0.1 1 404 377 96 SER H H 8.39 0.01 1 405 377 96 SER C C 174.82 0.1 1 406 377 96 SER CA C 58.49 0.1 1 407 377 96 SER CB C 63.99 0.1 1 408 377 96 SER N N 116.83 0.05 1 409 378 97 GLU H H 8.54 0.01 1 410 378 97 GLU C C 176.62 0.1 1 411 378 97 GLU CA C 56.75 0.1 1 412 378 97 GLU CB C 30.30 0.1 1 413 378 97 GLU N N 123.15 0.05 1 414 379 98 GLU H H 8.50 0.01 1 415 379 98 GLU C C 176.53 0.1 1 416 379 98 GLU CA C 56.68 0.1 1 417 379 98 GLU CB C 29.99 0.1 1 418 379 98 GLU N N 122.61 0.05 1 419 380 99 LYS H H 8.45 0.01 1 420 380 99 LYS C C 176.38 0.1 1 421 380 99 LYS CA C 55.97 0.1 1 422 380 99 LYS CB C 33.07 0.1 1 423 380 99 LYS N N 123.58 0.05 1 424 381 100 ALA H H 8.44 0.01 1 425 381 100 ALA C C 177.88 0.1 1 426 381 100 ALA CA C 52.45 0.1 1 427 381 100 ALA CB C 19.21 0.1 1 428 381 100 ALA N N 125.90 0.05 1 429 382 101 GLU H H 8.52 0.01 1 430 382 101 GLU CA C 56.46 0.1 1 431 382 101 GLU CB C 30.33 0.1 1 432 382 101 GLU N N 120.85 0.05 1 433 383 102 GLN H H 8.57 0.01 1 434 383 102 GLN C C 175.96 0.1 1 435 383 102 GLN CA C 55.49 0.1 1 436 383 102 GLN CB C 29.59 0.1 1 437 383 102 GLN N N 122.31 0.05 1 438 384 103 THR H H 8.47 0.01 1 439 384 103 THR C C 172.83 0.1 1 440 384 103 THR CA C 60.18 0.1 1 441 384 103 THR CB C 69.52 0.1 1 442 384 103 THR N N 119.68 0.05 1 443 385 104 PRO C C 176.94 0.1 1 444 385 104 PRO CA C 63.12 0.1 1 445 385 104 PRO CB C 32.33 0.1 1 446 386 105 LEU H H 8.50 0.01 1 447 386 105 LEU C C 177.70 0.1 1 448 386 105 LEU CA C 55.30 0.1 1 449 386 105 LEU CB C 42.34 0.1 1 450 386 105 LEU N N 123.05 0.05 1 451 387 106 SER H H 8.44 0.01 1 452 387 106 SER C C 174.53 0.1 1 453 387 106 SER CA C 58.24 0.1 1 454 387 106 SER CB C 63.70 0.1 1 455 387 106 SER N N 117.11 0.05 1 456 388 107 GLN H H 8.57 0.01 1 457 388 107 GLN N N 122.58 0.05 1 458 389 108 GLU C C 176.58 0.1 1 459 390 109 SER H H 8.43 0.01 1 460 390 109 SER C C 174.42 0.1 1 461 390 109 SER CA C 58.28 0.1 1 462 390 109 SER CB C 63.99 0.1 1 463 390 109 SER N N 116.63 0.05 1 464 391 110 ASP H H 8.47 0.01 1 465 391 110 ASP C C 175.88 0.1 1 466 391 110 ASP CA C 54.47 0.1 1 467 391 110 ASP CB C 41.10 0.1 1 468 391 110 ASP N N 122.92 0.05 1 469 392 111 ASP H H 8.27 0.01 1 470 392 111 ASP C C 176.18 0.1 1 471 392 111 ASP CA C 54.25 0.1 1 472 392 111 ASP CB C 40.89 0.1 1 473 392 111 ASP N N 120.16 0.05 1 474 393 112 TYR H H 8.23 0.01 1 475 393 112 TYR C C 176.01 0.1 1 476 393 112 TYR CA C 58.17 0.1 1 477 393 112 TYR CB C 38.30 0.1 1 478 393 112 TYR N N 121.31 0.05 1 479 394 113 SER H H 8.16 0.01 1 480 394 113 SER C C 173.91 0.1 1 481 394 113 SER CA C 58.42 0.1 1 482 394 113 SER CB C 63.83 0.1 1 483 394 113 SER N N 117.96 0.05 1 484 395 114 GLN H H 8.32 0.01 1 485 395 114 GLN C C 173.97 0.1 1 486 395 114 GLN CA C 53.61 0.1 1 487 395 114 GLN CB C 28.80 0.1 1 488 395 114 GLN N N 123.00 0.05 1 489 396 115 PRO C C 177.13 0.1 1 490 396 115 PRO CA C 63.19 0.1 1 491 396 115 PRO CB C 32.16 0.1 1 492 397 116 SER H H 8.66 0.01 1 493 397 116 SER C C 175.23 0.1 1 494 397 116 SER CA C 58.35 0.1 1 495 397 116 SER CB C 63.79 0.1 1 496 397 116 SER N N 116.67 0.05 1 497 398 117 THR H H 8.36 0.01 1 498 398 117 THR C C 174.84 0.1 1 499 398 117 THR CA C 61.81 0.1 1 500 398 117 THR CB C 69.76 0.1 1 501 398 117 THR N N 115.85 0.05 1 502 399 118 SER H H 8.43 0.01 1 503 399 118 SER C C 174.72 0.1 1 504 399 118 SER CA C 58.46 0.1 1 505 399 118 SER CB C 63.71 0.1 1 506 399 118 SER N N 118.05 0.05 1 507 400 119 SER H H 8.46 0.01 1 508 400 119 SER C C 174.58 0.1 1 509 400 119 SER CA C 58.47 0.1 1 510 400 119 SER CB C 63.73 0.1 1 511 400 119 SER N N 118.08 0.05 1 512 401 120 SER H H 8.40 0.01 1 513 401 120 SER C C 174.27 0.1 1 514 401 120 SER CA C 58.48 0.1 1 515 401 120 SER CB C 63.86 0.1 1 516 401 120 SER N N 118.22 0.05 1 517 402 121 ILE H H 8.14 0.01 1 518 402 121 ILE C C 175.85 0.1 1 519 402 121 ILE CA C 61.27 0.1 1 520 402 121 ILE CB C 38.46 0.1 1 521 402 121 ILE N N 123.44 0.05 1 522 403 122 VAL H H 8.24 0.01 1 523 403 122 VAL C C 175.87 0.1 1 524 403 122 VAL CA C 62.06 0.1 1 525 403 122 VAL CB C 32.81 0.1 1 526 403 122 VAL N N 125.51 0.05 1 527 404 123 TYR H H 8.52 0.01 1 528 404 123 TYR C C 175.87 0.1 1 529 404 123 TYR CA C 58.10 0.1 1 530 404 123 TYR CB C 38.97 0.1 1 531 404 123 TYR N N 125.82 0.05 1 532 405 124 SER H H 8.35 0.01 1 533 405 124 SER C C 174.35 0.1 1 534 405 124 SER CA C 57.98 0.1 1 535 405 124 SER CB C 63.97 0.1 1 536 405 124 SER N N 118.37 0.05 1 537 406 125 SER H H 8.50 0.01 1 538 406 125 SER C C 174.79 0.1 1 539 406 125 SER CA C 58.53 0.1 1 540 406 125 SER CB C 63.61 0.1 1 541 406 125 SER N N 118.39 0.05 1 542 407 126 GLN H H 8.52 0.01 1 543 407 126 GLN C C 176.16 0.1 1 544 407 126 GLN CA C 56.03 0.1 1 545 407 126 GLN CB C 29.98 0.1 1 546 407 126 GLN N N 122.26 0.05 1 547 408 127 GLU H H 8.46 0.01 1 548 408 127 GLU C C 176.65 0.1 1 549 408 127 GLU CA C 56.79 0.1 1 550 408 127 GLU CB C 30.48 0.1 1 551 408 127 GLU N N 121.97 0.05 1 552 409 128 SER H H 8.43 0.01 1 553 409 128 SER C C 174.55 0.1 1 554 409 128 SER CA C 58.52 0.1 1 555 409 128 SER CB C 63.71 0.1 1 556 409 128 SER N N 117.37 0.05 1 557 410 129 VAL H H 8.25 0.01 1 558 410 129 VAL C C 176.24 0.1 1 559 410 129 VAL CA C 62.54 0.1 1 560 410 129 VAL CB C 32.55 0.1 1 561 410 129 VAL N N 122.51 0.05 1 562 411 130 LYS H H 8.43 0.01 1 563 411 130 LYS C C 176.42 0.1 1 564 411 130 LYS CA C 56.29 0.1 1 565 411 130 LYS CB C 32.74 0.1 1 566 411 130 LYS N N 125.85 0.05 1 567 412 131 GLU H H 8.50 0.01 1 568 412 131 GLU C C 176.17 0.1 1 569 412 131 GLU CA C 56.45 0.1 1 570 412 131 GLU CB C 30.34 0.1 1 571 412 131 GLU N N 122.83 0.05 1 572 413 132 LEU H H 8.42 0.01 1 573 413 132 LEU C C 177.11 0.1 1 574 413 132 LEU CA C 55.08 0.1 1 575 413 132 LEU CB C 42.17 0.1 1 576 413 132 LEU N N 124.57 0.05 1 577 414 133 LYS H H 8.46 0.01 1 578 414 133 LYS C C 176.34 0.1 1 579 414 133 LYS CA C 56.04 0.1 1 580 414 133 LYS CB C 33.21 0.1 1 581 414 133 LYS N N 123.52 0.05 1 582 415 134 GLU H H 8.59 0.01 1 583 415 134 GLU C C 176.51 0.1 1 584 415 134 GLU CA C 56.50 0.1 1 585 415 134 GLU CB C 30.41 0.1 1 586 415 134 GLU N N 123.15 0.05 1 587 416 135 GLU H H 8.66 0.01 1 588 416 135 GLU C C 176.70 0.1 1 589 416 135 GLU CA C 56.43 0.1 1 590 416 135 GLU CB C 30.32 0.1 1 591 416 135 GLU N N 122.93 0.05 1 592 417 136 THR H H 8.38 0.01 1 593 417 136 THR C C 174.48 0.1 1 594 417 136 THR CA C 61.84 0.1 1 595 417 136 THR CB C 69.79 0.1 1 596 417 136 THR N N 116.07 0.05 1 597 418 137 GLN H H 8.56 0.01 1 598 418 137 GLN CA C 55.66 0.1 1 599 418 137 GLN CB C 29.75 0.1 1 600 418 137 GLN N N 123.09 0.05 1 601 419 138 ASP H H 8.55 0.01 1 602 419 138 ASP C C 176.18 0.1 1 603 419 138 ASP CA C 54.55 0.1 1 604 419 138 ASP CB C 41.01 0.1 1 605 419 138 ASP N N 122.46 0.05 1 606 420 139 LYS H H 8.39 0.01 1 607 420 139 LYS CA C 56.18 0.1 1 608 420 139 LYS CB C 33.14 0.1 1 609 420 139 LYS N N 121.96 0.05 1 610 421 140 ASP C C 176.45 0.1 1 611 421 140 ASP CA C 55.70 0.1 1 612 421 140 ASP CB C 41.13 0.1 1 613 422 141 GLU H H 8.57 0.01 1 614 422 141 GLU C C 176.67 0.1 1 615 422 141 GLU CA C 56.60 0.1 1 616 422 141 GLU CB C 30.12 0.1 1 617 422 141 GLU N N 122.72 0.05 1 618 423 142 SER H H 8.54 0.01 1 619 423 142 SER C C 174.81 0.1 1 620 423 142 SER CA C 58.79 0.1 1 621 423 142 SER CB C 63.76 0.1 1 622 423 142 SER N N 117.39 0.05 1 623 424 143 VAL H H 8.16 0.01 1 624 424 143 VAL C C 176.53 0.1 1 625 424 143 VAL CA C 62.41 0.1 1 626 424 143 VAL CB C 32.73 0.1 1 627 424 143 VAL N N 121.89 0.05 1 628 425 144 GLU H H 8.56 0.01 1 629 425 144 GLU C C 176.84 0.1 1 630 425 144 GLU CA C 56.85 0.1 1 631 425 144 GLU CB C 30.07 0.1 1 632 425 144 GLU N N 124.60 0.05 1 633 426 145 SER H H 8.47 0.01 1 634 426 145 SER C C 174.82 0.1 1 635 426 145 SER CA C 58.53 0.1 1 636 426 145 SER CB C 63.79 0.1 1 637 426 145 SER N N 117.40 0.05 1 638 427 146 SER H H 8.39 0.01 1 639 427 146 SER C C 174.34 0.1 1 640 427 146 SER CA C 58.69 0.1 1 641 427 146 SER CB C 63.63 0.1 1 642 427 146 SER N N 117.99 0.05 1 643 428 147 PHE H H 8.21 0.01 1 644 428 147 PHE C C 175.80 0.1 1 645 428 147 PHE CA C 57.98 0.1 1 646 428 147 PHE CB C 39.55 0.1 1 647 428 147 PHE N N 122.11 0.05 1 648 429 148 SER H H 8.20 0.01 1 649 429 148 SER C C 174.24 0.1 1 650 429 148 SER CA C 58.05 0.1 1 651 429 148 SER CB C 63.84 0.1 1 652 429 148 SER N N 117.51 0.05 1 653 430 149 LEU H H 8.33 0.01 1 654 430 149 LEU C C 177.12 0.1 1 655 430 149 LEU CA C 55.36 0.1 1 656 430 149 LEU CB C 42.25 0.1 1 657 430 149 LEU N N 124.36 0.05 1 658 431 150 ASN H H 8.43 0.01 1 659 431 150 ASN C C 173.80 0.1 1 660 431 150 ASN CA C 53.17 0.1 1 661 431 150 ASN CB C 38.99 0.1 1 662 431 150 ASN N N 119.51 0.05 1 663 432 151 ALA H H 7.90 0.01 1 664 432 151 ALA CA C 53.95 0.1 1 665 432 151 ALA CB C 20.08 0.1 1 666 432 151 ALA N N 129.75 0.05 1 stop_ save_