data_27701 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Myc bHLH-LZ domain in presence of 3.2 M GdmCl ; _BMRB_accession_number 27701 _BMRB_flat_file_name bmr27701.str _Entry_type original _Submission_date 2018-11-24 _Accession_date 2018-11-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Panova Stanislava V. . 2 Cliff Matthew J. . 3 Macek Pavel . . 4 Blackledge Martin . . 5 Jensen Malene Ringkjobing . 6 Nissink 'J. Willem' M. . 7 Embrey Kevin J. . 8 Davies Rick . . 9 Waltho Jonathan P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 84 "13C chemical shifts" 255 "15N chemical shifts" 84 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-10-02 update BMRB 'update entry citation' 2019-08-15 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27702 'bHLHZip domain of Myc (in presence of 2.4 M GdmCl)' 27703 'bHLHZip domain of Myc (in presence of 1.6 M GdmCl)' 27704 'bHLHZip domain of Myc' stop_ _Original_release_date 2018-11-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31402220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Panova Stanislava V. . 2 Cliff Matthew J. . 3 Macek Pavel . . 4 Blackledge Martin . . 5 Jensen Malene Ringkjobing . 6 Nissink 'J. Willem' M. . 7 Embrey Kevin J. . 8 Davies Rick . . 9 Waltho Jonathan P. . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _Journal_volume 27 _Journal_issue 10 _Journal_ISSN 1878-4186 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1537 _Page_last 1546 _Year 2019 _Details . loop_ _Keyword IDP 'chemical denaturation' 'disordered protein' 'protein unfolding' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'bHLHZip domain of Myc' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'bHLHZip domain of Myc' $bHLHZip_domain_of_Myc stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_bHLHZip_domain_of_Myc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common bHLHZip_domain_of_Myc _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 87 _Mol_residue_sequence ; GSNVKRRTHNVLERQRRNEL KRSFFALRDQIPELENNEKA PKVVILKKATAYILSVQAEE QKLISEEDLLRKRREQLKHK LEQLRNS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 351 GLY 2 352 SER 3 353 ASN 4 354 VAL 5 355 LYS 6 356 ARG 7 357 ARG 8 358 THR 9 359 HIS 10 360 ASN 11 361 VAL 12 362 LEU 13 363 GLU 14 364 ARG 15 365 GLN 16 366 ARG 17 367 ARG 18 368 ASN 19 369 GLU 20 370 LEU 21 371 LYS 22 372 ARG 23 373 SER 24 374 PHE 25 375 PHE 26 376 ALA 27 377 LEU 28 378 ARG 29 379 ASP 30 380 GLN 31 381 ILE 32 382 PRO 33 383 GLU 34 384 LEU 35 385 GLU 36 386 ASN 37 387 ASN 38 388 GLU 39 389 LYS 40 390 ALA 41 391 PRO 42 392 LYS 43 393 VAL 44 394 VAL 45 395 ILE 46 396 LEU 47 397 LYS 48 398 LYS 49 399 ALA 50 400 THR 51 401 ALA 52 402 TYR 53 403 ILE 54 404 LEU 55 405 SER 56 406 VAL 57 407 GLN 58 408 ALA 59 409 GLU 60 410 GLU 61 411 GLN 62 412 LYS 63 413 LEU 64 414 ILE 65 415 SER 66 416 GLU 67 417 GLU 68 418 ASP 69 419 LEU 70 420 LEU 71 421 ARG 72 422 LYS 73 423 ARG 74 424 ARG 75 425 GLU 76 426 GLN 77 427 LEU 78 428 LYS 79 429 HIS 80 430 LYS 81 431 LEU 82 432 GLU 83 433 GLN 84 434 LEU 85 435 ARG 86 436 ASN 87 437 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $bHLHZip_domain_of_Myc 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 $bHLHZip_domain_of_Myc 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '3.2 M GdmCl was added to achieve protein denaturation' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $bHLHZip_domain_of_Myc 1 mM '[U-13C; U-15N]' 'sodium phosphate' 20 mM 'natural abundance' TSP 1 mM 'natural abundance' GdmCl 3.2 M 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CCPNMR _Saveframe_category software _Name CCPNMR _Version 2.4.2 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_(H)N(CA)NNH_6 _Saveframe_category NMR_applied_experiment _Experiment_name (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' 3.2 0.05 M pH 6.5 0.1 pH pressure 1 . atm temperature 278 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio TSP C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 TSP H 1 'methyl protons' ppm 0 internal direct . . . 1 TSP N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CCPNMR stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D CBCA(CO)NH' (H)N(CA)NNH stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'bHLHZip domain of Myc' _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 1 352 2 SER H H 8.768 0.003 1 2 352 2 SER C C 174.405 0.6 1 3 352 2 SER CA C 58.59 0.6 1 4 352 2 SER CB C 64.264 0.6 1 5 352 2 SER N N 116.199 0.13 1 6 353 3 ASN H H 8.745 0.006 1 7 353 3 ASN C C 175.25 0.6 1 8 353 3 ASN CA C 53.534 0.6 1 9 353 3 ASN CB C 39.076 0.6 1 10 353 3 ASN N N 121.959 0.09 1 11 354 4 VAL H H 8.153 0.006 1 12 354 4 VAL C C 176.255 0.6 1 13 354 4 VAL CA C 62.722 0.6 1 14 354 4 VAL CB C 32.892 0.6 1 15 354 4 VAL N N 120.866 0.05 1 16 355 5 LYS H H 8.484 0.006 1 17 355 5 LYS C C 176.659 0.6 1 18 355 5 LYS CA C 56.4 0.6 1 19 355 5 LYS CB C 33.481 0.6 1 20 355 5 LYS N N 126.315 0.1 1 21 356 6 ARG H H 8.474 0.007 1 22 356 6 ARG C C 176.462 0.6 1 23 356 6 ARG CA C 56.299 0.6 1 24 356 6 ARG CB C 31.092 0.6 1 25 356 6 ARG N N 123.868 0.13 1 26 357 7 ARG H H 8.583 0.004 1 27 357 7 ARG C C 176.629 0.6 1 28 357 7 ARG CA C 56.315 0.6 1 29 357 7 ARG CB C 31.051 0.6 1 30 357 7 ARG N N 123.757 0.08 1 31 358 8 THR H H 8.303 0.005 1 32 358 8 THR C C 174.426 0.6 1 33 358 8 THR CA C 61.943 0.6 1 34 358 8 THR CB C 70.164 0.6 1 35 358 8 THR N N 115.727 0.05 1 36 359 9 HIS H H 8.602 0.053 1 37 359 9 HIS C C 174.711 0.6 1 38 359 9 HIS CA C 56.088 0.6 1 39 359 9 HIS CB C 30.314 0.6 1 40 359 9 HIS N N 121.065 0.31 1 41 360 10 ASN H H 8.654 0.029 1 42 360 10 ASN C C 175.252 0.6 1 43 360 10 ASN CA C 53.514 0.6 1 44 360 10 ASN CB C 39.16 0.6 1 45 360 10 ASN N N 121.278 0.15 1 46 361 11 VAL H H 8.293 0.007 1 47 361 11 VAL C C 176.316 0.6 1 48 361 11 VAL CA C 62.902 0.6 1 49 361 11 VAL CB C 32.831 0.6 1 50 361 11 VAL N N 121.402 0.08 1 51 362 12 LEU H H 8.397 0.009 1 52 362 12 LEU C C 177.643 0.6 1 53 362 12 LEU CA C 55.517 0.6 1 54 362 12 LEU CB C 42.266 0.6 1 55 362 12 LEU N N 125.972 0.23 1 56 363 13 GLU H H 8.459 0.003 1 57 363 13 GLU C C 176.798 0.6 1 58 363 13 GLU CA C 57.111 0.6 1 59 363 13 GLU CB C 30.274 0.6 1 60 363 13 GLU N N 122.635 0.17 1 61 364 14 ARG H H 8.446 0.012 1 62 364 14 ARG C C 176.682 0.6 1 63 364 14 ARG CA C 56.898 0.6 1 64 364 14 ARG CB C 30.834 0.6 1 65 364 14 ARG N N 122.635 0.17 1 66 365 15 GLN H H 8.53 0.006 1 67 365 15 GLN C C 176.376 0.6 1 68 365 15 GLN CA C 56.271 0.6 1 69 365 15 GLN CB C 29.627 0.6 1 70 365 15 GLN N N 122.214 0.18 1 71 366 16 ARG H H 8.526 0.007 1 72 366 16 ARG C C 176.759 0.6 1 73 366 16 ARG CA C 56.61 0.6 1 74 366 16 ARG CB C 30.915 0.6 1 75 366 16 ARG N N 123.38 0.19 1 76 367 17 ARG H H 8.532 0.004 1 77 367 17 ARG C C 176.416 0.6 1 78 367 17 ARG CA C 56.853 0.6 1 79 367 17 ARG CB C 30.73 0.6 1 80 367 17 ARG N N 122.745 0.2 1 81 368 18 ASN H H 8.562 0.003 1 82 368 18 ASN C C 175.386 0.6 1 83 368 18 ASN CA C 53.649 0.6 1 84 368 18 ASN CB C 39.053 0.6 1 85 368 18 ASN N N 120.262 0.15 1 86 369 19 GLU H H 8.47 0.002 1 87 369 19 GLU C C 176.627 0.6 1 88 369 19 GLU CA C 56.93 0.6 1 89 369 19 GLU CB C 30.353 0.6 1 90 369 19 GLU N N 121.871 0.16 1 91 370 20 LEU H H 8.336 0.012 1 92 370 20 LEU C C 177.595 0.6 1 93 370 20 LEU CA C 55.53 0.6 1 94 370 20 LEU CB C 42.35 0.6 1 95 370 20 LEU N N 123.457 0.18 1 96 371 21 LYS H H 8.376 0.012 1 97 371 21 LYS C C 176.816 0.6 1 98 371 21 LYS CA C 56.61 0.6 1 99 371 21 LYS CB C 33.147 0.6 1 100 371 21 LYS N N 123.157 0.2 1 101 372 22 ARG H H 8.45 0.006 1 102 372 22 ARG C C 176.463 0.6 1 103 372 22 ARG CA C 56.449 0.6 1 104 372 22 ARG CB C 31.043 0.6 1 105 372 22 ARG N N 123.086 0.16 1 106 373 23 SER H H 8.41 0.004 1 107 373 23 SER C C 174.314 0.6 1 108 373 23 SER CA C 58.627 0.6 1 109 373 23 SER CB C 64.2 0.6 1 110 373 23 SER N N 117.677 0.16 1 111 374 24 PHE H H 8.389 0.012 1 112 374 24 PHE C C 175.623 0.6 1 113 374 24 PHE CA C 58.749 0.6 1 114 374 24 PHE CB C 39.933 0.6 1 115 374 24 PHE N N 123.352 0.19 1 116 375 25 PHE H H 8.176 0.001 1 117 375 25 PHE C C 175.415 0.6 1 118 375 25 PHE CA C 57.661 0.6 1 119 375 25 PHE CB C 39.897 0.6 1 120 375 25 PHE N N 121.61 0.11 1 121 376 26 ALA H H 8.274 0.007 1 122 376 26 ALA C C 177.689 0.6 1 123 376 26 ALA CA C 52.706 0.6 1 124 376 26 ALA CB C 19.653 0.6 1 125 376 26 ALA N N 125.79 0.12 1 126 377 27 LEU H H 8.274 0.004 1 127 377 27 LEU C C 177.859 0.6 1 128 377 27 LEU CA C 55.707 0.6 1 129 377 27 LEU CB C 42.341 0.6 1 130 377 27 LEU N N 122.215 0.17 1 131 378 28 ARG H H 8.367 0.009 1 132 378 28 ARG C C 176.276 0.6 1 133 378 28 ARG CA C 56.444 0.6 1 134 378 28 ARG CB C 30.929 0.6 1 135 378 28 ARG N N 121.538 0.14 1 136 379 29 ASP H H 8.431 0.006 1 137 379 29 ASP C C 176.095 0.6 1 138 379 29 ASP CA C 54.782 0.6 1 139 379 29 ASP CB C 41.324 0.6 1 140 379 29 ASP N N 121.497 0.17 1 141 380 30 GLN H H 8.339 0.01 1 142 380 30 GLN C C 175.769 0.6 1 143 380 30 GLN CA C 56.023 0.6 1 144 380 30 GLN CB C 29.76 0.6 1 145 380 30 GLN N N 120.695 0.14 1 146 381 31 ILE H H 8.367 0.006 1 147 381 31 ILE C C 174.532 0.6 1 148 381 31 ILE CA C 59.136 0.6 1 149 381 31 ILE CB C 37.826 0.6 1 150 381 31 ILE N N 124.357 0.03 1 151 382 32 PRO C C 177.028 0.6 1 152 382 32 PRO CA C 63.543 0.6 1 153 382 32 PRO CB C 32.47 0.6 1 154 383 33 GLU H H 8.637 0.005 1 155 383 33 GLU C C 176.7 0.6 1 156 383 33 GLU CA C 56.908 0.6 1 157 383 33 GLU CB C 30.271 0.6 1 158 383 33 GLU N N 122.168 0.13 1 159 384 34 LEU H H 8.392 0.004 1 160 384 34 LEU C C 177.548 0.6 1 161 384 34 LEU CA C 55.476 0.6 1 162 384 34 LEU CB C 42.383 0.6 1 163 384 34 LEU N N 123.53 0.1 1 164 385 35 GLU H H 8.562 0 1 165 385 35 GLU C C 176.359 0.6 1 166 385 35 GLU CA C 56.626 0.6 1 167 385 35 GLU CB C 30.507 0.6 1 168 385 35 GLU N N 122.115 0.09 1 169 386 36 ASN H H 8.601 0.004 1 170 386 36 ASN C C 175.155 0.6 1 171 386 36 ASN CA C 53.52 0.6 1 172 386 36 ASN CB C 39.055 0.6 1 173 386 36 ASN N N 120.299 0.09 1 174 387 37 ASN H H 8.579 0.006 1 175 387 37 ASN C C 175.35 0.6 1 176 387 37 ASN CA C 53.36 0.6 1 177 387 37 ASN CB C 39.184 0.6 1 178 387 37 ASN N N 120.054 0.08 1 179 388 38 GLU H H 8.434 0.001 1 180 388 38 GLU C C 176.552 0.6 1 181 388 38 GLU CA C 56.875 0.6 1 182 388 38 GLU CB C 30.323 0.6 1 183 388 38 GLU N N 121.502 0.11 1 184 389 39 LYS H H 8.399 0.003 1 185 389 39 LYS C C 176.177 0.6 1 186 389 39 LYS CA C 56.316 0.6 1 187 389 39 LYS CB C 33.224 0.6 1 188 389 39 LYS N N 122.757 0.1 1 189 390 40 ALA H H 8.45 0.002 1 190 390 40 ALA C C 175.902 0.6 1 191 390 40 ALA CA C 50.42 0.6 1 192 390 40 ALA CB C 18.397 0.6 1 193 390 40 ALA N N 127.115 0.09 1 194 391 41 PRO C C 176.909 0.6 1 195 391 41 PRO CA C 63.061 0.6 1 196 391 41 PRO CB C 32.385 0.6 1 197 392 42 LYS H H 8.549 0.001 1 198 392 42 LYS C C 176.749 0.6 1 199 392 42 LYS CA C 56.921 0.6 1 200 392 42 LYS CB C 33.227 0.6 1 201 392 42 LYS N N 123.272 0.14 1 202 393 43 VAL H H 8.311 0.007 1 203 393 43 VAL C C 175.921 0.6 1 204 393 43 VAL CA C 62.672 0.6 1 205 393 43 VAL CB C 32.824 0.6 1 206 393 43 VAL N N 123.3 0.03 1 207 394 44 VAL H H 8.372 0.016 1 208 394 44 VAL C C 175.806 0.6 1 209 394 44 VAL CA C 62.642 0.6 1 210 394 44 VAL CB C 33.16 0.6 1 211 394 44 VAL N N 126.516 0.03 1 212 395 45 ILE H H 8.421 0.011 1 213 395 45 ILE C C 176.105 0.6 1 214 395 45 ILE CA C 60.734 0.6 1 215 395 45 ILE CB C 38.465 0.6 1 216 395 45 ILE N N 127.416 0.04 1 217 396 46 LEU H H 8.481 0.008 1 218 396 46 LEU C C 177.251 0.6 1 219 396 46 LEU CA C 54.988 0.6 1 220 396 46 LEU CB C 42.343 0.6 1 221 396 46 LEU N N 128.47 0.08 1 222 397 47 LYS H H 8.431 0.005 1 223 397 47 LYS C C 176.662 0.6 1 224 397 47 LYS CA C 56.493 0.6 1 225 397 47 LYS CB C 32.977 0.6 1 226 397 47 LYS N N 123.833 0.07 1 227 398 48 LYS H H 8.466 0.007 1 228 398 48 LYS C C 176.619 0.6 1 229 398 48 LYS CA C 56.665 0.6 1 230 398 48 LYS CB C 33.181 0.6 1 231 398 48 LYS N N 123.881 0.05 1 232 399 49 ALA H H 8.547 0.004 1 233 399 49 ALA C C 178.054 0.6 1 234 399 49 ALA CA C 52.94 0.6 1 235 399 49 ALA CB C 19.497 0.6 1 236 399 49 ALA N N 126.338 0.09 1 237 400 50 THR H H 8.131 0.002 1 238 400 50 THR C C 174.463 0.6 1 239 400 50 THR CA C 62.374 0.6 1 240 400 50 THR CB C 70.165 0.6 1 241 400 50 THR N N 114.024 0.06 1 242 401 51 ALA H H 8.391 0.004 1 243 401 51 ALA C C 177.605 0.6 1 244 401 51 ALA CA C 53.06 0.6 1 245 401 51 ALA CB C 19.401 0.6 1 246 401 51 ALA N N 126.547 0.1 1 247 402 52 TYR H H 8.215 0.006 1 248 402 52 TYR C C 176.002 0.6 1 249 402 52 TYR CA C 58.715 0.6 1 250 402 52 TYR CB C 39.004 0.6 1 251 402 52 TYR N N 120.576 0.11 1 252 403 53 ILE H H 8.128 0.005 1 253 403 53 ILE C C 176.22 0.6 1 254 403 53 ILE CA C 61.479 0.6 1 255 403 53 ILE CB C 38.692 0.6 1 256 403 53 ILE N N 123.529 0.08 1 257 404 54 LEU H H 8.321 0.002 1 258 404 54 LEU C C 177.616 0.6 1 259 404 54 LEU CA C 55.584 0.6 1 260 404 54 LEU CB C 42.369 0.6 1 261 404 54 LEU N N 126.367 0.17 1 262 405 55 SER H H 8.36 0.002 1 263 405 55 SER C C 174.901 0.6 1 264 405 55 SER CA C 58.776 0.6 1 265 405 55 SER CB C 64.134 0.6 1 266 405 55 SER N N 117.992 0.11 1 267 406 56 VAL H H 8.257 0.001 1 268 406 56 VAL C C 176.683 0.6 1 269 406 56 VAL CA C 63.243 0.6 1 270 406 56 VAL CB C 32.609 0.6 1 271 406 56 VAL N N 122.308 0.03 1 272 407 57 GLN H H 8.46 0.004 1 273 407 57 GLN C C 176.274 0.6 1 274 407 57 GLN CA C 56.475 0.6 1 275 407 57 GLN CB C 29.47 0.6 1 276 407 57 GLN N N 123.479 0.13 1 277 408 58 ALA H H 8.366 0.005 1 278 408 58 ALA C C 178.27 0.6 1 279 408 58 ALA CA C 53.352 0.6 1 280 408 58 ALA CB C 19.369 0.6 1 281 408 58 ALA N N 125.314 0.11 1 282 409 59 GLU H H 8.447 0 1 283 409 59 GLU C C 177.035 0.6 1 284 409 59 GLU CA C 57.218 0.6 1 285 409 59 GLU CB C 30.305 0.6 1 286 409 59 GLU N N 120.474 0.1 1 287 410 60 GLU H H 8.478 0 1 288 410 60 GLU C C 176.847 0.6 1 289 410 60 GLU CA C 57.093 0.6 1 290 410 60 GLU CB C 30.46 0.6 1 291 410 60 GLU N N 121.836 0.12 1 292 411 61 GLN H H 8.442 0.007 1 293 411 61 GLN C C 176.216 0.6 1 294 411 61 GLN CA C 56.419 0.6 1 295 411 61 GLN CB C 29.653 0.6 1 296 411 61 GLN N N 121.65 0.18 1 297 412 62 LYS H H 8.394 0.01 1 298 412 62 LYS C C 176.687 0.6 1 299 412 62 LYS CA C 56.826 0.6 1 300 412 62 LYS CB C 33.152 0.6 1 301 412 62 LYS N N 123.362 0.14 1 302 413 63 LEU H H 8.374 0.01 1 303 413 63 LEU C C 177.497 0.6 1 304 413 63 LEU CA C 55.674 0.6 1 305 413 63 LEU CB C 42.308 0.6 1 306 413 63 LEU N N 124.199 0.23 1 307 414 64 ILE H H 8.292 0.009 1 308 414 64 ILE C C 176.383 0.6 1 309 414 64 ILE CA C 61.596 0.6 1 310 414 64 ILE CB C 38.799 0.6 1 311 414 64 ILE N N 123.053 0.15 1 312 415 65 SER H H 8.627 0.022 1 313 415 65 SER C C 175.054 0.6 1 314 415 65 SER CA C 58.75 0.6 1 315 415 65 SER CB C 64.372 0.6 1 316 415 65 SER N N 120.912 0.08 1 317 416 66 GLU H H 8.663 0.009 1 318 416 66 GLU C C 177.385 0.6 1 319 416 66 GLU CA C 57.345 0.6 1 320 416 66 GLU CB C 30.227 0.6 1 321 416 66 GLU N N 123.564 0.15 1 322 417 67 GLU H H 8.483 0.012 1 323 417 67 GLU C C 177.102 0.6 1 324 417 67 GLU CA C 57.796 0.6 1 325 417 67 GLU CB C 29.912 0.6 1 326 417 67 GLU N N 120.26 0.11 1 327 418 68 ASP H H 8.315 0.011 1 328 418 68 ASP C C 176.933 0.6 1 329 418 68 ASP CA C 55.442 0.6 1 330 418 68 ASP CB C 41.018 0.6 1 331 418 68 ASP N N 121.112 0.1 1 332 419 69 LEU H H 8.111 0.004 1 333 419 69 LEU C C 178.014 0.6 1 334 419 69 LEU CA C 56.249 0.6 1 335 419 69 LEU CB C 42.218 0.6 1 336 419 69 LEU N N 122.39 0.09 1 337 420 70 LEU H H 8.205 0.015 1 338 420 70 LEU C C 177.993 0.6 1 339 420 70 LEU CA C 56.061 0.6 1 340 420 70 LEU CB C 42.173 0.6 1 341 420 70 LEU N N 122.09 0.33 1 342 421 71 ARG H H 8.194 0.029 1 343 421 71 ARG C C 176.829 0.6 1 344 421 71 ARG CA C 57.132 0.6 1 345 421 71 ARG CB C 30.302 0.6 1 346 421 71 ARG N N 121.85 0.31 1 347 422 72 LYS H H 8.355 0.028 1 348 422 72 LYS C C 177.203 0.6 1 349 422 72 LYS CA C 57.109 0.6 1 350 422 72 LYS CB C 33.21 0.6 1 351 422 72 LYS N N 122.857 0.37 1 352 423 73 ARG H H 8.437 0.025 1 353 423 73 ARG C C 176.962 0.6 1 354 423 73 ARG CA C 57.315 0.6 1 355 423 73 ARG CB C 30.848 0.6 1 356 423 73 ARG N N 122.801 0.35 1 357 424 74 ARG H H 8.473 0.023 1 358 424 74 ARG C C 176.901 0.6 1 359 424 74 ARG CA C 56.93 0.6 1 360 424 74 ARG CB C 30.785 0.6 1 361 424 74 ARG N N 122.814 0.35 1 362 425 75 GLU H H 8.534 0.02 1 363 425 75 GLU C C 176.751 0.6 1 364 425 75 GLU CA C 57.201 0.6 1 365 425 75 GLU CB C 30.279 0.6 1 366 425 75 GLU N N 122.614 0.31 1 367 426 76 GLN H H 8.512 0.026 1 368 426 76 GLN C C 176.277 0.6 1 369 426 76 GLN CA C 56.29 0.6 1 370 426 76 GLN CB C 29.632 0.6 1 371 426 76 GLN N N 122.146 0.38 1 372 427 77 LEU H H 8.355 0.023 1 373 427 77 LEU C C 177.599 0.6 1 374 427 77 LEU CA C 55.698 0.6 1 375 427 77 LEU CB C 42.352 0.6 1 376 427 77 LEU N N 124.128 0.31 1 377 428 78 LYS H H 8.377 0.025 1 378 428 78 LYS C C 176.769 0.6 1 379 428 78 LYS CA C 57.083 0.6 1 380 428 78 LYS CB C 33.164 0.6 1 381 428 78 LYS N N 122.368 0.25 1 382 429 79 HIS H H 8.501 0.074 1 383 429 79 HIS C C 175.266 0.6 1 384 429 79 HIS CA C 56.139 0.6 1 385 429 79 HIS CB C 30.026 0.6 1 386 429 79 HIS N N 120.118 0.03 1 387 430 80 LYS H H 8.487 0.052 1 388 430 80 LYS C C 176.843 0.6 1 389 430 80 LYS CA C 56.781 0.6 1 390 430 80 LYS CB C 33.205 0.6 1 391 430 80 LYS N N 123.676 0.32 1 392 431 81 LEU H H 8.478 0.006 1 393 431 81 LEU C C 177.769 0.6 1 394 431 81 LEU CA C 55.772 0.6 1 395 431 81 LEU CB C 42.288 0.6 1 396 431 81 LEU N N 124.066 0.33 1 397 432 82 GLU H H 8.538 0.016 1 398 432 82 GLU C C 176.651 0.6 1 399 432 82 GLU CA C 57.104 0.6 1 400 432 82 GLU CB C 30.28 0.6 1 401 432 82 GLU N N 122.765 0.27 1 402 433 83 GLN H H 8.503 0.014 1 403 433 83 GLN C C 176.202 0.6 1 404 433 83 GLN CA C 56.236 0.6 1 405 433 83 GLN CB C 29.663 0.6 1 406 433 83 GLN N N 122.085 0.18 1 407 434 84 LEU H H 8.439 0.017 1 408 434 84 LEU C C 177.699 0.6 1 409 434 84 LEU CA C 55.616 0.6 1 410 434 84 LEU CB C 42.337 0.6 1 411 434 84 LEU N N 124.486 0.27 1 412 435 85 ARG H H 8.475 0.014 1 413 435 85 ARG C C 176.362 0.6 1 414 435 85 ARG CA C 56.498 0.6 1 415 435 85 ARG CB C 31.026 0.6 1 416 435 85 ARG N N 122.107 0.17 1 417 436 86 ASN H H 8.578 0.01 1 418 436 86 ASN C C 174.588 0.6 1 419 436 86 ASN CA C 53.44 0.6 1 420 436 86 ASN CB C 39.297 0.6 1 421 436 86 ASN N N 120.647 0.16 1 422 437 87 SER H H 8.024 0.006 1 423 437 87 SER N N 121.662 0.1 1 stop_ save_