data_27704 ####################### # 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 ; _BMRB_accession_number 27704 _BMRB_flat_file_name bmr27704.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" 46 "13C chemical shifts" 121 "15N chemical shifts" 46 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 27701 'bHLHZip domain of Myc (in presence of 3.2 M GdmCl)' 27702 'bHLHZip domain of Myc (in presence of 2.4 M GdmCl)' 27703 'bHLHZip domain of Myc (in precence of 1.6 M GdmCl)' 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 'disordered protein' 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 . 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' 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' 0.028 0.002 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 indirect . . . 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 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 8.843 0.003 1 2 352 2 SER C C 174.60265 0.6 1 3 352 2 SER CA C 58.533 0.6 1 4 352 2 SER CB C 64.074 0.6 1 5 352 2 SER N N 115.681 0.13 1 6 353 3 ASN H H 8.875 0.006 1 7 353 3 ASN C C 175.44689 0.6 1 8 353 3 ASN CA C 53.511 0.6 1 9 353 3 ASN CB C 38.718 0.6 1 10 353 3 ASN N N 121.815 0.09 1 11 354 4 VAL H H 8.273 0.006 1 12 354 4 VAL C C 176.43667 0.6 1 13 354 4 VAL CA C 62.975 0.6 1 14 354 4 VAL CB C 32.64 0.6 1 15 354 4 VAL N N 121.307 0.05 1 16 355 5 LYS H H 8.589 0.006 1 17 355 5 LYS C C 176.75382 0.6 1 18 355 5 LYS CA C 56.533 0.6 1 19 355 5 LYS CB C 32.909 0.6 1 20 355 5 LYS N N 126.201 0.1 1 21 356 6 ARG H H 8.576 0.007 1 22 356 6 ARG C C 176.56475 0.6 1 23 356 6 ARG CA C 56.391 0.6 1 24 356 6 ARG CB C 30.949 0.6 1 25 356 6 ARG N N 123.701 0.13 1 26 357 7 ARG H H 8.729 0.004 1 27 357 7 ARG C C 176.76638 0.6 1 28 357 7 ARG CA C 56.466 0.6 1 29 357 7 ARG CB C 30.974 0.6 1 30 357 7 ARG N N 123.68 0.08 1 31 358 8 THR H H 8.464 0.005 1 32 358 8 THR C C 174.58648 0.6 1 33 358 8 THR CA C 62.14 0.6 1 34 358 8 THR CB C 70.021 0.6 1 35 358 8 THR N N 116.177 0.05 1 36 359 9 HIS H H 8.671 0.053 1 37 359 9 HIS C C 175.17641 0.6 1 38 359 9 HIS CA C 56.472 0.6 1 39 359 9 HIS CB C 30.678 0.6 1 40 359 9 HIS N N 121.994 0.31 1 41 360 10 ASN H H 8.754 0.029 1 42 360 10 ASN C C 175.90861 0.6 1 43 360 10 ASN CA C 53.648 0.6 1 44 360 10 ASN CB C 38.794 0.6 1 45 360 10 ASN N N 121.108 0.15 1 46 361 11 VAL H H 8.386 0.007 1 47 361 11 VAL C C 177.17739 0.6 1 48 361 11 VAL CA C 64.545 0.6 1 49 361 11 VAL CB C 32.44 0.6 1 50 361 11 VAL N N 121.729 0.08 1 51 362 12 LEU H H 8.343 0.009 1 52 362 12 LEU C C 178.66324 0.6 1 53 362 12 LEU CA C 56.58 0.6 1 54 362 12 LEU CB C 41.933 0.6 1 55 362 12 LEU N N 124.039 0.23 1 56 363 13 GLU H H 8.371 0.003 1 57 363 13 GLU C C 177.86016 0.6 1 58 363 13 GLU CA C 57.793 0.6 1 59 363 13 GLU CB C 29.821 0.6 1 60 363 13 GLU N N 121.543 0.17 1 61 364 14 ARG H H 8.354 0.012 1 62 364 14 ARG C C 177.61246 0.6 1 63 364 14 ARG CA C 57.534 0.6 1 64 364 14 ARG CB C 30.441 0.6 1 65 364 14 ARG N N 121.448 0.17 1 66 365 15 GLN H H 8.399 0.006 1 67 365 15 GLN C C 177.48099 0.6 1 68 365 15 GLN CA C 57.574 0.6 1 69 365 15 GLN CB C 29.007 0.6 1 70 365 15 GLN N N 120.616 0.18 1 71 366 16 ARG H H 8.435 0.007 1 72 366 16 ARG C C 177.91643 0.6 1 73 366 16 ARG CA C 57.751 0.6 1 74 366 16 ARG CB C 30.595 0.6 1 75 366 16 ARG N N 121.957 0.19 1 76 367 17 ARG H H 8.455 0.004 1 77 367 17 ARG C C 177.70453 0.6 1 78 367 17 ARG CA C 57.805 0.6 1 79 367 17 ARG CB C 30.463 0.6 1 80 367 17 ARG N N 121.175 0.2 1 81 368 18 ASN H H 8.535 0.003 1 82 368 18 ASN C C 176.55993 0.6 1 83 368 18 ASN CA C 54.412 0.6 1 84 368 18 ASN CB C 38.541 0.6 1 85 368 18 ASN N N 119.475 0.15 1 86 369 19 GLU H H 8.412 0.002 1 87 369 19 GLU C C 177.65002 0.6 1 88 369 19 GLU CA C 57.762 0.6 1 89 369 19 GLU CB C 29.961 0.6 1 90 369 19 GLU N N 121.449 0.16 1 91 370 20 LEU H H 8.208 0.012 1 92 370 20 LEU C C 178.39113 0.6 1 93 370 20 LEU CA C 56.447 0.6 1 94 370 20 LEU CB C 42.175 0.6 1 95 370 20 LEU N N 122.231 0.18 1 96 371 21 LYS H H 8.202 0.012 1 97 371 21 LYS C C 177.31837 0.6 1 98 371 21 LYS CA C 57.604 0.6 1 99 371 21 LYS CB C 32.651 0.6 1 100 371 21 LYS N N 121.381 0.2 1 101 372 22 ARG H H 8.314 0.006 1 102 372 22 ARG C C 177.22675 0.6 1 103 372 22 ARG CA C 56.766 0.6 1 104 372 22 ARG CB C 30.73 0.6 1 105 372 22 ARG N N 121.502 0.16 1 106 373 23 SER H H 8.379 0.004 1 107 373 23 SER C C 174.70092 0.6 1 108 373 23 SER CA C 59.06 0.6 1 109 373 23 SER CB C 63.78 0.6 1 110 373 23 SER N N 116.688 0.16 1 111 374 24 PHE H H 8.285 0.012 1 112 374 24 PHE C C 176.06906 0.6 1 113 374 24 PHE CA C 59.031 0.6 1 114 374 24 PHE CB C 39.676 0.6 1 115 374 24 PHE N N 122.48 0.19 1 116 375 25 PHE H H 8.197 0.001 1 117 375 25 PHE C C 175.70356 0.6 1 118 375 25 PHE CA C 58.252 0.6 1 119 375 25 PHE CB C 39.589 0.6 1 120 375 25 PHE N N 120.994 0.11 1 121 376 26 ALA H H 8.211 0.007 1 122 376 26 ALA C C 178.02266 0.6 1 123 376 26 ALA CA C 53.043 0.6 1 124 376 26 ALA CB C 19.243 0.6 1 125 376 26 ALA N N 124.936 0.12 1 126 377 27 LEU H H 8.2 0.004 1 127 377 27 LEU C C 178.05736 0.6 1 128 377 27 LEU CA C 55.727 0.6 1 129 377 27 LEU CB C 42.242 0.6 1 130 377 27 LEU N N 120.972 0.17 1 131 378 28 ARG H H 8.292 0.009 1 132 378 28 ARG C C 176.43802 0.6 1 133 378 28 ARG CA C 56.594 0.6 1 134 378 28 ARG CB C 30.748 0.6 1 135 378 28 ARG N N 120.958 0.14 1 136 379 29 ASP H H 8.373 0.006 1 137 379 29 ASP C C 176.14165 0.6 1 138 379 29 ASP CA C 54.893 0.6 1 139 379 29 ASP CB C 41.114 0.6 1 140 379 29 ASP N N 120.249 0.17 1 141 380 30 GLN H H 8.247 0.01 1 142 380 30 GLN C C 175.8988 0.6 1 143 380 30 GLN CA C 55.745 0.6 1 144 380 30 GLN CB C 29.602 0.6 1 145 380 30 GLN N N 119.899 0.14 1 146 381 31 ILE H H 8.419 0.006 1 147 381 31 ILE N N 124.623 0.03 1 148 382 32 PRO C C 177.07646 0.6 1 149 382 32 PRO CA C 63.539 0.6 1 150 382 32 PRO CB C 32.258 0.6 1 151 383 33 GLU H H 8.666 0.005 1 152 383 33 GLU C C 176.83846 0.6 1 153 383 33 GLU CA C 56.702 0.6 1 154 383 33 GLU CB C 30.255 0.6 1 155 383 33 GLU N N 121.543 0.13 1 156 384 34 LEU H H 8.437 0.004 1 157 384 34 LEU C C 177.68932 0.6 1 158 384 34 LEU CA C 55.315 0.6 1 159 384 34 LEU CB C 42.464 0.6 1 160 384 34 LEU N N 123.39 0.1 1 161 385 35 GLU H H 8.555 0 1 162 385 35 GLU C C 176.37306 0.6 1 163 385 35 GLU CA C 56.603 0.6 1 164 385 35 GLU CB C 30.379 0.6 1 165 385 35 GLU N N 121.956 0.09 1 166 386 36 ASN H H 8.65 0.004 1 167 386 36 ASN C C 175.26626 0.6 1 168 386 36 ASN CA C 53.518 0.6 1 169 386 36 ASN CB C 38.883 0.6 1 170 386 36 ASN N N 120.158 0.09 1 171 387 37 ASN H H 8.645 0.006 1 172 387 37 ASN C C 175.65019 0.6 1 173 387 37 ASN CA C 53.632 0.6 1 174 387 37 ASN CB C 39.024 0.6 1 175 387 37 ASN N N 119.98 0.08 1 176 388 38 GLU H H 8.523 0.001 1 177 388 38 GLU C C 176.73516 0.6 1 178 388 38 GLU CA C 57.22 0.6 1 179 388 38 GLU CB C 30.126 0.6 1 180 388 38 GLU N N 121.292 0.11 1 181 389 39 LYS H H 8.385 0.003 1 182 389 39 LYS C C 176.30093 0.6 1 183 389 39 LYS CA C 56.239 0.6 1 184 389 39 LYS CB C 32.998 0.6 1 185 389 39 LYS N N 121.728 0.1 1 186 390 40 ALA H H 8.271 0.002 1 187 390 40 ALA N N 126.118 0.09 1 188 391 41 PRO C C 177.04625 0.6 1 189 391 41 PRO CA C 63.055 0.6 1 190 391 41 PRO CB C 32.25 0.6 1 191 392 42 LYS H H 8.606 0.001 1 192 392 42 LYS C C 176.75861 0.6 1 193 392 42 LYS CA C 56.49 0.6 1 194 392 42 LYS CB C 33.036 0.6 1 195 392 42 LYS N N 122.314 0.14 1 196 393 43 VAL H H 8.375 0.007 1 197 393 43 VAL C C 176.11038 0.6 1 198 393 43 VAL N N 123.234 0.03 1 199 394 44 VAL H H 8.512 0.016 1 200 394 44 VAL C C 176.02354 0.6 1 201 394 44 VAL N N 126.863 0.03 1 202 395 45 ILE C C 176.4094 0.6 1 203 396 46 LEU H H 8.579 0.008 1 204 396 46 LEU C C 177.54207 0.6 1 205 396 46 LEU N N 128.223 0.08 1 206 397 47 LYS H H 8.517 0.005 1 207 397 47 LYS N N 123.57 0.07 1 208 399 49 ALA H H 8.61 0.004 1 209 399 49 ALA N N 126.189 0.09 1 210 415 65 SER H H 8.715 0.022 1 211 415 65 SER N N 120.024 0.08 1 212 422 72 LYS H H 8.149 0.028 1 213 422 72 LYS N N 120.13 0.37 1 stop_ save_