data_12033 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; c-MYC 353-437 ; _BMRB_accession_number 12033 _BMRB_flat_file_name bmr12033.str _Entry_type original _Submission_date 2019-02-27 _Accession_date 2019-03-13 _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 Zinzalla Giovanna . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 54 "13C chemical shifts" 175 "15N chemical shifts" 54 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-07-23 original BMRB . stop_ _Original_release_date 2019-03-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Crystal Structures and Nuclear Magnetic Resonance Studies of the Apo Form of the c-MYC:MAX bHLHZip Complex Reveal a Helical Basic Region in the Absence of DNA. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31260268 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sammak Susan S . 2 Hamdani Najoua N . 3 Gorrec Fabrice F . 4 Allen 'Mark D' MD . 5 Freund 'Stefan M V' SMV . 6 Bycroft Mark M . 7 Zinzalla Giovanna G . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume . _Journal_issue . _Journal_ISSN 1520-4995 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name c-MYC _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label c-MYC $c-MYC stop_ _System_molecular_weight 12546 _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_c-MYC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common c-MYC _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MNVKRRTHNVLERQRRNELK RSFFALRDQIPELENNEKAP KVVILKKATAYILSVQAEEQ KLISEEDLLRKRREQLKHKL EQLRNS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 GLY 3 3 SER 4 4 SER 5 5 HIS 6 6 HIS 7 7 HIS 8 8 HIS 9 9 HIS 10 10 HIS 11 11 SER 12 12 SER 13 13 GLY 14 14 LEU 15 15 VAL 16 16 PRO 17 17 ARG 18 18 GLY 19 19 SER 20 20 HIS 21 21 MET 22 22 ASN 23 23 VAL 24 24 LYS 25 25 ARG 26 26 ARG 27 27 THR 28 28 HIS 29 29 ASN 30 30 VAL 31 31 LEU 32 32 GLU 33 33 ARG 34 34 GLN 35 35 ARG 36 36 ARG 37 37 ASN 38 38 GLU 39 39 LEU 40 40 LYS 41 41 ARG 42 42 SER 43 43 PHE 44 44 PHE 45 45 ALA 46 46 LEU 47 47 ARG 48 48 ASP 49 49 GLN 50 50 ILE 51 51 PRO 52 52 GLU 53 53 LEU 54 54 GLU 55 55 ASN 56 56 ASN 57 57 GLU 58 58 LYS 59 59 ALA 60 60 PRO 61 61 LYS 62 62 VAL 63 63 VAL 64 64 ILE 65 65 LEU 66 66 LYS 67 67 LYS 68 68 ALA 69 69 THR 70 70 ALA 71 71 TYR 72 72 ILE 73 73 LEU 74 74 SER 75 75 VAL 76 76 GLN 77 77 ALA 78 78 GLU 79 79 GLU 80 80 GLN 81 81 LYS 82 82 LEU 83 83 ILE 84 84 SER 85 85 GLU 86 86 GLU 87 87 ASP 88 88 LEU 89 89 LEU 90 90 ARG 91 91 LYS 92 92 ARG 93 93 ARG 94 94 GLU 95 95 GLN 96 96 LEU 97 97 LYS 98 98 HIS 99 99 LYS 100 100 LEU 101 101 GLU 102 102 GLN 103 103 LEU 104 104 ARG 105 105 ASN 106 106 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 $c-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 $c-MYC 'recombinant technology' . Escherichia coli . pRSETA 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 $c-MYC 80 uM '[U-99% 13C; U-99% 15N]' H2O 90 % 'natural abundance' D2O 10 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model ARX _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_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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_HNCA_5 _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' 150 . mM pH 7.0 . 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 DSS C 13 'methyl protons' ppm 0 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 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 CBCA(CO)NH' '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 c-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 3 3 SER CA C 58.595 . 1 2 3 3 SER CB C 64.135 . 1 3 4 4 SER H H 8.454 . 1 4 4 4 SER CA C 58.805 . 1 5 4 4 SER CB C 63.965 . 1 6 4 4 SER N N 117.538 . 1 7 11 11 SER C C 175.043 . 1 8 11 11 SER CA C 58.741 . 1 9 11 11 SER CB C 64.001 . 1 10 12 12 SER H H 8.396 . 1 11 12 12 SER C C 175.333 . 1 12 12 12 SER CA C 59.053 . 1 13 12 12 SER CB C 64.053 . 1 14 12 12 SER N N 117.94 . 1 15 13 13 GLY H H 8.257 . 1 16 13 13 GLY C C 174.166 . 1 17 13 13 GLY CA C 45.489 . 1 18 13 13 GLY N N 110.254 . 1 19 14 14 LEU H H 7.924 . 1 20 14 14 LEU C C 177.586 . 1 21 14 14 LEU CA C 55.33 . 1 22 14 14 LEU CB C 42.555 . 1 23 14 14 LEU N N 121.015 . 1 24 15 15 VAL H H 8.033 . 1 25 15 15 VAL CA C 60.139 . 1 26 15 15 VAL CB C 32.842 . 1 27 15 15 VAL N N 122.799 . 1 28 16 16 PRO C C 177.213 . 1 29 16 16 PRO CA C 63.331 . 1 30 16 16 PRO CB C 32.404 . 1 31 17 17 ARG H H 8.418 . 1 32 17 17 ARG C C 177.407 . 1 33 17 17 ARG CA C 56.739 . 1 34 17 17 ARG CB C 31.106 . 1 35 17 17 ARG N N 121.924 . 1 36 18 18 GLY H H 8.401 . 1 37 18 18 GLY C C 174.578 . 1 38 18 18 GLY CA C 45.513 . 1 39 18 18 GLY N N 110.1 . 1 40 19 19 SER H H 8.129 . 1 41 19 19 SER CA C 58.901 . 1 42 19 19 SER CB C 64.044 . 1 43 19 19 SER N N 115.309 . 1 44 20 20 HIS C C 175.67 . 1 45 20 20 HIS CA C 56.678 . 1 46 20 20 HIS CB C 30.53 . 1 47 21 21 MET H H 8.053 . 1 48 21 21 MET CA C 55.825 . 1 49 21 21 MET CB C 32.825 . 1 50 21 21 MET N N 120.476 . 1 51 22 22 ASN H H 8.364 . 1 52 22 22 ASN C C 175.497 . 1 53 22 22 ASN CA C 53.54 . 1 54 22 22 ASN CB C 38.911 . 1 55 22 22 ASN N N 119.823 . 1 56 23 23 VAL H H 7.927 . 1 57 23 23 VAL C C 176.559 . 1 58 23 23 VAL CA C 62.929 . 1 59 23 23 VAL CB C 32.945 . 1 60 23 23 VAL N N 120.385 . 1 61 24 24 LYS H H 8.247 . 1 62 24 24 LYS C C 176.935 . 1 63 24 24 LYS CA C 56.796 . 1 64 24 24 LYS CB C 33.04 . 1 65 24 24 LYS N N 124.8 . 1 66 25 25 ARG H H 8.21 . 1 67 25 25 ARG C C 176.643 . 1 68 25 25 ARG CA C 56.425 . 1 69 25 25 ARG CB C 31.071 . 1 70 25 25 ARG N N 122.515 . 1 71 26 26 ARG H H 8.351 . 1 72 26 26 ARG C C 176.87 . 1 73 26 26 ARG CA C 56.596 . 1 74 26 26 ARG CB C 31.08 . 1 75 26 26 ARG N N 122.66 . 1 76 27 27 THR H H 8.106 . 1 77 27 27 THR C C 176.709 . 1 78 27 27 THR CA C 62.3 . 1 79 27 27 THR CB C 70.13 . 1 80 27 27 THR N N 115.135 . 1 81 28 28 HIS H H 8.266 . 1 82 28 28 HIS C C 175.318 . 1 83 28 28 HIS CA C 56.625 . 1 84 28 28 HIS CB C 31.063 . 1 85 28 28 HIS N N 121.524 . 1 86 29 29 ASN H H 8.374 . 1 87 29 29 ASN C C 175.915 . 1 88 29 29 ASN CA C 53.759 . 1 89 29 29 ASN CB C 38.996 . 1 90 29 29 ASN N N 120.22 . 1 91 30 30 VAL H H 8.067 . 1 92 30 30 VAL C C 177.156 . 1 93 30 30 VAL CA C 64.271 . 1 94 30 30 VAL CB C 32.567 . 1 95 30 30 VAL N N 120.968 . 1 96 31 31 LEU H H 8.051 . 1 97 31 31 LEU C C 178.636 . 1 98 31 31 LEU CA C 56.463 . 1 99 31 31 LEU CB C 42.125 . 1 100 31 31 LEU N N 123.32 . 1 101 32 32 GLU H H 8.098 . 1 102 32 32 GLU C C 177.80 . 1 103 32 32 GLU CA C 57.863 . 1 104 32 32 GLU CB C 30.074 . 1 105 32 32 GLU N N 120.842 . 1 106 33 33 ARG H H 8.056 . 1 107 33 33 ARG C C 177.61 . 1 108 33 33 ARG CA C 57.911 . 1 109 33 33 ARG CB C 30.77 . 1 110 33 33 ARG N N 120.652 . 1 111 34 34 GLN H H 8.101 . 1 112 34 34 GLN C C 177.385 . 1 113 34 34 GLN CA C 57.425 . 1 114 34 34 GLN CB C 29.105 . 1 115 34 34 GLN N N 119.848 . 1 116 35 35 ARG H H 8.143 . 1 117 35 35 ARG C C 177.407 . 1 118 35 35 ARG CA C 57.549 . 1 119 35 35 ARG CB C 30.796 . 1 120 35 35 ARG N N 121.222 . 1 121 36 36 ARG H H 8.143 . 1 122 36 36 ARG C C 177.538 . 1 123 36 36 ARG CA C 57.812 . 1 124 36 36 ARG CB C 30.788 . 1 125 36 36 ARG N N 121.222 . 1 126 37 37 ASN H H 8.237 . 1 127 37 37 ASN C C 176.434 . 1 128 37 37 ASN CA C 54.473 . 1 129 37 37 ASN CB C 38.549 . 1 130 37 37 ASN N N 118.78 . 1 131 38 38 GLU H H 8.143 . 1 132 38 38 GLU C C 177.556 . 1 133 38 38 GLU CA C 57.701 . 1 134 38 38 GLU CB C 30.126 . 1 135 38 38 GLU N N 120.73 . 1 136 39 39 LEU H H 7.929 . 1 137 39 39 LEU C C 178.29 . 1 138 39 39 LEU CA C 56.216 . 1 139 39 39 LEU CB C 42.383 . 1 140 39 39 LEU N N 121.534 . 1 141 40 40 LYS H H 7.929 . 1 142 40 40 LYS C C 177.264 . 1 143 40 40 LYS CA C 57.244 . 1 144 40 40 LYS CB C 32.928 . 1 145 40 40 LYS N N 120.732 . 1 146 41 41 ARG H H 8.036 . 1 147 41 41 ARG C C 177.12 . 1 148 41 41 ARG CA C 57.082 . 1 149 41 41 ARG CB C 31.003 . 1 150 41 41 ARG N N 120.821 . 1 151 42 42 SER H H 8.094 . 1 152 42 42 SER C C 174.691 . 1 153 42 42 SER CA C 58.964 . 1 154 42 42 SER CB C 63.881 . 1 155 42 42 SER N N 115.983 . 1 156 43 43 PHE H H 7.999 . 1 157 43 43 PHE C C 178.062 . 1 158 43 43 PHE CA C 58.918 . 1 159 43 43 PHE CB C 39.796 . 1 160 43 43 PHE N N 121.76 . 1 161 44 44 PHE H H 7.911 . 1 162 44 44 PHE C C 175.7 . 1 163 44 44 PHE CA C 58.259 . 1 164 44 44 PHE CB C 39.693 . 1 165 44 44 PHE N N 120.319 . 1 166 45 45 ALA H H 7.93 . 1 167 45 45 ALA C C 176.028 . 1 168 45 45 ALA CA C 53.016 . 1 169 45 45 ALA CB C 19.424 . 1 170 45 45 ALA N N 124.238 . 1 171 46 46 LEU H H 7.91 . 1 172 46 46 LEU C C 178.111 . 1 173 46 46 LEU CA C 55.801 . 1 174 46 46 LEU CB C 42.323 . 1 175 46 46 LEU N N 120.266 . 1 176 47 47 ARG H H 7.999 . 1 177 47 47 ARG C C 176.488 . 1 178 47 47 ARG CA C 56.739 . 1 179 47 47 ARG CB C 30.968 . 1 180 47 47 ARG N N 120.296 . 1 181 48 48 ASP H H 8.096 . 1 182 48 48 ASP C C 176.213 . 1 183 48 48 ASP CA C 54.882 . 1 184 48 48 ASP CB C 41.197 . 1 185 48 48 ASP N N 119.607 . 1 186 49 49 GLN H H 7.969 . 1 187 49 49 GLN C C 175.968 . 1 188 49 49 GLN CA C 55.816 . 1 189 49 49 GLN CB C 29.816 . 1 190 49 49 GLN N N 119.221 . 1 191 50 50 ILE H H 8.132 . 1 192 50 50 ILE C C 174.994 . 1 193 50 50 ILE CA C 59.263 . 1 194 50 50 ILE CB C 38.567 . 1 195 50 50 ILE N N 123.91 . 1 196 51 51 PRO C C 177.174 . 1 197 51 51 PRO CA C 63.554 . 1 198 51 51 PRO CB C 32.472 . 1 199 52 52 GLU H H 8.384 . 1 200 52 52 GLU C C 176.911 . 1 201 52 52 GLU CA C 56.901 . 1 202 52 52 GLU CB C 30.401 . 1 203 52 52 GLU N N 120.876 . 1 204 53 53 LEU H H 8.15 . 1 205 53 53 LEU C C 177.783 . 1 206 53 53 LEU CA C 55.435 . 1 207 53 53 LEU CB C 42.658 . 1 208 53 53 LEU N N 122.731 . 1 209 54 54 GLU H H 8.276 . 1 210 54 54 GLU C C 176.47 . 1 211 54 54 GLU CA C 56.835 . 1 212 54 54 GLU CB C 30.538 . 1 213 54 54 GLU N N 121.284 . 1 214 55 55 ASN H H 8.366 . 1 215 55 55 ASN C C 175.354 . 1 216 55 55 ASN CA C 53.587 . 1 217 55 55 ASN CB C 39.134 . 1 218 55 55 ASN N N 119.444 . 1 219 56 56 ASN H H 8.363 . 1 220 56 56 ASN C C 175.736 . 1 221 56 56 ASN CA C 53.654 . 1 222 56 56 ASN CB C 39.194 . 1 223 56 56 ASN N N 119.31 . 1 224 57 57 GLU H H 8.239 . 1 225 57 57 GLU C C 176.828 . 1 226 57 57 GLU CA C 57.234 . 1 227 57 57 GLU CB C 30.281 . 1 228 57 57 GLU N N 120.667 . 1 229 58 58 LYS H H 8.1 . 1 230 58 58 LYS C C 176.386 . 1 231 58 58 LYS CA C 56.235 . 1 232 58 58 LYS CB C 33.117 . 1 233 58 58 LYS N N 121.096 . 1 234 59 59 ALA H H 8.027 . 1 235 59 59 ALA C C 175.595 . 1 236 59 59 ALA CA C 50.807 . 1 237 59 59 ALA CB C 18.333 . 1 238 59 59 ALA N N 125.658 . 1 239 60 60 PRO C C 177.126 . 1 240 60 60 PRO CA C 63.09 . 1 241 60 60 PRO CB C 32.438 . 1 242 61 61 LYS H H 8.308 . 1 243 61 61 LYS C C 176.965 . 1 244 61 61 LYS CA C 56.625 . 1 245 61 61 LYS CB C 33.272 . 1 246 61 61 LYS N N 121.742 . 1 247 62 62 VAL H H 8.098 . 1 248 62 62 VAL C C 176.148 . 1 249 62 62 VAL CA C 62.681 . 1 250 62 62 VAL CB C 32.997 . 1 251 62 62 VAL N N 122.705 . 1 252 63 63 VAL H H 8.244 . 1 253 63 63 VAL C C 176.07 . 1 254 63 63 VAL CA C 62.591 . 1 255 63 63 VAL CB C 33.095 . 1 256 63 63 VAL N N 126.267 . 1 257 64 64 ILE H H 8.262 . 1 258 64 64 ILE C C 176.333 . 1 259 64 64 ILE CA C 60.939 . 1 260 64 64 ILE CB C 38.524 . 1 261 64 64 ILE N N 126.851 . 1 262 65 65 LEU H H 8.292 . 1 263 65 65 LEU C C 177.341 . 1 264 65 65 LEU CA C 55.168 . 1 265 65 65 LEU CB C 42.624 . 1 266 65 65 LEU N N 127.75 . 1 267 66 66 LYS H H 8.219 . 1 268 66 66 LYS CA C 56.616 . 1 269 66 66 LYS CB C 33.409 . 1 270 66 66 LYS N N 123.047 . 1 271 103 103 LEU C C 174.626 . 1 272 103 103 LEU CA C 55.354 . 1 273 103 103 LEU CB C 42.615 . 1 274 104 104 ARG H H 8.273 . 1 275 104 104 ARG CA C 56.815 . 1 276 104 104 ARG N N 121.308 . 1 277 105 105 ASN C C 174.626 . 1 278 105 105 ASN CA C 53.514 . 1 279 105 105 ASN CB C 39.383 . 1 280 106 106 SER H H 7.675 . 1 281 106 106 SER CA C 60.491 . 1 282 106 106 SER CB C 65.144 . 1 283 106 106 SER N N 120.82 . 1 stop_ save_