data_27517 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for HTLV-1 HBZ 3-56 ; _BMRB_accession_number 27517 _BMRB_flat_file_name bmr27517.str _Entry_type original _Submission_date 2018-06-11 _Accession_date 2018-06-11 _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 Yang Ke . . 2 Stanfield 'Robyn L.' . . 3 Martinez-Yamout Maria . . 4 Dyson 'H. Jane' . . 5 Wilson 'Ian A.' . . 6 Wright 'Peter E.' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 52 "13C chemical shifts" 104 "15N chemical shifts" 52 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-09-26 original BMRB . stop_ _Original_release_date 2018-06-12 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural basis for cooperative regulation of KIX-mediated transcription pathways by the HTLV-1 HBZ activation domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30232260 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yang Ke . . 2 Stanfield Robyn L. . 3 Martinez-Yamout Maria A. . 4 Dyson 'H Jane' J. . 5 Wilson Ian A. . 6 Wright Peter E. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 115 _Journal_issue 40 _Journal_ISSN 1091-6490 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10040 _Page_last 10045 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HBZ activation domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HBZ activation domain' $HBZ_activation_domain stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HBZ_activation_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HBZ_activation_domain _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; GSHMASGLFRALPVSAPEDL LVEELVDGLLSLEEELKDKE EEKAVLDGLLSLEEESRG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 0 SER 3 1 HIS 4 2 MET 5 3 ALA 6 4 SER 7 5 GLY 8 6 LEU 9 7 PHE 10 8 ARG 11 9 ALA 12 10 LEU 13 11 PRO 14 12 VAL 15 13 SER 16 14 ALA 17 15 PRO 18 16 GLU 19 17 ASP 20 18 LEU 21 19 LEU 22 20 VAL 23 21 GLU 24 22 GLU 25 23 LEU 26 24 VAL 27 25 ASP 28 26 GLY 29 27 LEU 30 28 LEU 31 29 SER 32 30 LEU 33 31 GLU 34 32 GLU 35 33 GLU 36 34 LEU 37 35 LYS 38 36 ASP 39 37 LYS 40 38 GLU 41 39 GLU 42 40 GLU 43 41 LYS 44 42 ALA 45 43 VAL 46 44 LEU 47 45 ASP 48 46 GLY 49 47 LEU 50 48 LEU 51 49 SER 52 50 LEU 53 51 GLU 54 52 GLU 55 53 GLU 56 54 SER 57 55 ARG 58 56 GLY 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 _Strain $HBZ_activation_domain 'human T-cell leukemia virus' 11908 Viruses . . . 'type 1' 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 $HBZ_activation_domain 'recombinant technology' . Escherichia coli . pET21 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 TRIS 50 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' $HBZ_activation_domain 600 uM '[U-98% 13C; U-98% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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' 0.1 . M pH 6.80 . pH pressure 1 . atm temperature 301 . 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 external indirect . . . 0.251450201 DSS H 1 'methyl protons' ppm 0 external direct . . . 1 DSS N 15 'methyl protons' ppm 0 external 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 $NMRView stop_ loop_ _Experiment_label '3D HNCACB' '3D CBCA(CO)NH' 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 'HBZ activation domain' _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 5 ALA H H 8.371 . . 2 3 5 ALA CA C 52.675 . . 3 3 5 ALA CB C 19.233 . . 4 3 5 ALA N N 125.566 . . 5 4 6 SER H H 8.258 . . 6 4 6 SER CA C 58.572 . . 7 4 6 SER CB C 64.021 . . 8 4 6 SER N N 114.868 . . 9 5 7 GLY H H 8.381 . . 10 5 7 GLY CA C 45.509 . . 11 5 7 GLY N N 110.508 . . 12 6 8 LEU H H 7.942 . . 13 6 8 LEU CA C 55.288 . . 14 6 8 LEU CB C 42.382 . . 15 6 8 LEU N N 121.266 . . 16 7 9 PHE H H 8.165 . . 17 7 9 PHE CA C 57.825 . . 18 7 9 PHE CB C 39.462 . . 19 7 9 PHE N N 120.552 . . 20 8 10 ARG H H 8.025 . . 21 8 10 ARG CA C 55.661 . . 22 8 10 ARG CB C 31.027 . . 23 8 10 ARG N N 123.044 . . 24 9 11 ALA H H 8.191 . . 25 9 11 ALA CA C 52.227 . . 26 9 11 ALA CB C 19.233 . . 27 9 11 ALA N N 125.480 . . 28 10 12 LEU H H 8.117 . . 29 10 12 LEU CA C 52.973 . . 30 10 12 LEU CB C 41.776 . . 31 10 12 LEU N N 122.733 . . 32 11 13 PRO CA C 63.051 . . 33 11 13 PRO CB C 31.920 . . 34 12 14 VAL H H 8.137 . . 35 12 14 VAL CA C 62.230 . . 36 12 14 VAL CB C 32.893 . . 37 12 14 VAL N N 119.679 . . 38 13 15 SER H H 8.304 . . 39 13 15 SER CA C 58.273 . . 40 13 15 SER CB C 64.021 . . 41 13 15 SER N N 119.217 . . 42 14 16 ALA H H 8.325 . . 43 14 16 ALA CA C 50.510 . . 44 14 16 ALA CB C 18.411 . . 45 14 16 ALA N N 127.067 . . 46 15 17 PRO CA C 63.797 . . 47 15 17 PRO CB C 31.923 . . 48 16 18 GLU H H 8.689 . . 49 16 18 GLU CA C 57.303 . . 50 16 18 GLU CB C 29.758 . . 51 16 18 GLU N N 119.403 . . 52 17 19 ASP H H 8.151 . . 53 17 19 ASP CA C 54.541 . . 54 17 19 ASP CB C 40.955 . . 55 17 19 ASP N N 120.346 . . 56 18 20 LEU H H 7.884 . . 57 18 20 LEU CA C 55.288 . . 58 18 20 LEU CB C 42.421 . . 59 18 20 LEU N N 121.596 . . 60 19 21 LEU H H 8.133 . . 61 19 21 LEU CA C 55.287 . . 62 19 21 LEU CB C 42.149 . . 63 19 21 LEU N N 123.194 . . 64 20 22 VAL H H 8.011 . . 65 20 22 VAL CA C 62.437 . . 66 20 22 VAL CB C 32.799 . . 67 20 22 VAL N N 121.417 . . 68 21 23 GLU H H 8.439 . . 69 21 23 GLU CA C 56.855 . . 70 21 23 GLU CB C 30.579 . . 71 21 23 GLU N N 124.513 . . 72 22 24 GLU H H 8.364 . . 73 22 24 GLU CA C 56.640 . . 74 22 24 GLU CB C 30.403 . . 75 22 24 GLU N N 122.019 . . 76 23 25 LEU H H 8.252 . . 77 23 25 LEU CA C 55.138 . . 78 23 25 LEU CB C 42.224 . . 79 23 25 LEU N N 123.828 . . 80 24 26 VAL H H 8.122 . . 81 24 26 VAL CA C 62.398 . . 82 24 26 VAL CB C 32.760 . . 83 24 26 VAL N N 121.354 . . 84 25 27 ASP H H 8.376 . . 85 25 27 ASP CA C 54.690 . . 86 25 27 ASP CB C 41.254 . . 87 25 27 ASP N N 123.832 . . 88 26 28 GLY H H 8.285 . . 89 26 28 GLY CA C 45.658 . . 90 26 28 GLY N N 109.312 . . 91 27 29 LEU H H 8.054 . . 92 27 29 LEU CA C 55.481 . . 93 27 29 LEU CB C 42.266 . . 94 27 29 LEU N N 121.400 . . 95 28 30 LEU H H 8.147 . . 96 28 30 LEU CA C 55.362 . . 97 28 30 LEU CB C 42.373 . . 98 28 30 LEU N N 122.486 . . 99 29 31 SER H H 8.252 . . 100 29 31 SER CA C 58.272 . . 101 29 31 SER CB C 63.750 . . 102 29 31 SER N N 116.761 . . 103 30 32 LEU H H 8.271 . . 104 30 32 LEU CA C 55.586 . . 105 30 32 LEU CB C 42.373 . . 106 30 32 LEU N N 124.454 . . 107 31 33 GLU H H 8.335 . . 108 31 33 GLU CA C 57.218 . . 109 31 33 GLU CB C 30.126 . . 110 31 33 GLU N N 120.848 . . 111 32 34 GLU H H 8.438 . . 112 32 34 GLU CA C 56.988 . . 113 32 34 GLU CB C 30.210 . . 114 32 34 GLU N N 121.973 . . 115 33 35 GLU H H 8.345 . . 116 33 35 GLU CA C 57.066 . . 117 33 35 GLU CB C 30.326 . . 118 33 35 GLU N N 121.708 . . 119 34 36 LEU H H 8.211 . . 120 34 36 LEU CA C 55.437 . . 121 34 36 LEU CB C 42.075 . . 122 34 36 LEU N N 122.883 . . 123 35 37 LYS H H 8.118 . . 124 35 37 LYS CA C 56.602 . . 125 35 37 LYS CB C 33.108 . . 126 35 37 LYS N N 122.090 . . 127 36 38 ASP H H 8.307 . . 128 36 38 ASP CA C 54.631 . . 129 36 38 ASP CB C 41.068 . . 130 36 38 ASP N N 121.114 . . 131 37 39 LYS H H 8.184 . . 132 37 39 LYS CA C 56.563 . . 133 37 39 LYS CB C 32.953 . . 134 37 39 LYS N N 121.308 . . 135 38 40 GLU H H 8.427 . . 136 38 40 GLU CA C 56.988 . . 137 38 40 GLU CB C 30.094 . . 138 38 40 GLU N N 122.218 . . 139 39 41 GLU H H 8.379 . . 140 39 41 GLU CA C 57.027 . . 141 39 41 GLU CB C 30.171 . . 142 39 41 GLU N N 122.218 . . 143 40 42 GLU H H 8.401 . . 144 40 42 GLU CA C 56.988 . . 145 40 42 GLU CB C 30.364 . . 146 40 42 GLU N N 121.753 . . 147 41 43 LYS H H 8.235 . . 148 41 43 LYS CA C 56.706 . . 149 41 43 LYS CB C 32.968 . . 150 41 43 LYS N N 122.598 . . 151 42 44 ALA H H 8.239 . . 152 42 44 ALA CA C 52.899 . . 153 42 44 ALA CB C 19.009 . . 154 42 44 ALA N N 124.807 . . 155 43 45 VAL H H 8.060 . . 156 43 45 VAL CA C 62.827 . . 157 43 45 VAL CB C 32.595 . . 158 43 45 VAL N N 119.756 . . 159 44 46 LEU H H 8.239 . . 160 44 46 LEU CA C 55.437 . . 161 44 46 LEU CB C 42.149 . . 162 44 46 LEU N N 125.460 . . 163 45 47 ASP H H 8.252 . . 164 45 47 ASP CA C 54.914 . . 165 45 47 ASP CB C 41.179 . . 166 45 47 ASP N N 120.927 . . 167 46 48 GLY H H 8.249 . . 168 46 48 GLY CA C 45.733 . . 169 46 48 GLY N N 108.942 . . 170 47 49 LEU H H 8.018 . . 171 47 49 LEU CA C 55.558 . . 172 47 49 LEU CB C 42.189 . . 173 47 49 LEU N N 121.420 . . 174 48 50 LEU H H 8.123 . . 175 48 50 LEU CA C 55.398 . . 176 48 50 LEU CB C 42.368 . . 177 48 50 LEU N N 122.233 . . 178 49 51 SER H H 8.219 . . 179 49 51 SER CA C 58.273 . . 180 49 51 SER CB C 63.797 . . 181 49 51 SER N N 116.548 . . 182 50 52 LEU H H 8.250 . . 183 50 52 LEU CA C 55.536 . . 184 50 52 LEU CB C 42.277 . . 185 50 52 LEU N N 123.704 . . 186 51 53 GLU H H 8.329 . . 187 51 53 GLU CA C 57.025 . . 188 51 53 GLU CB C 30.118 . . 189 51 53 GLU N N 121.149 . . 190 52 54 GLU H H 8.280 . . 191 52 54 GLU CA C 57.104 . . 192 52 54 GLU CB C 30.326 . . 193 52 54 GLU N N 121.342 . . 194 53 55 GLU H H 8.333 . . 195 53 55 GLU CA C 56.950 . . 196 53 55 GLU CB C 30.364 . . 197 53 55 GLU N N 121.588 . . 198 54 56 SER H H 8.317 . . 199 54 56 SER CA C 58.497 . . 200 54 56 SER CB C 63.648 . . 201 54 56 SER N N 116.735 . . 202 55 57 ARG H H 8.322 . . 203 55 57 ARG CA C 56.109 . . 204 55 57 ARG CB C 30.952 . . 205 55 57 ARG N N 123.704 . . 206 56 58 GLY H H 8.010 . . 207 56 58 GLY CA C 46.180 . . 208 56 58 GLY N N 115.920 . . stop_ save_