data_34569 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Transmembrane helix of tumor necrosis factor alpha in trifluorethanol, AGALLL mutant ; _BMRB_accession_number 34569 _BMRB_flat_file_name bmr34569.str _Entry_type original _Submission_date 2020-10-29 _Accession_date 2020-10-29 _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 Guschtschin-Schmidt N. . . 2 Muhle-Goll C. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 157 "13C chemical shifts" 99 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-12-01 original BMRB . stop_ _Original_release_date 2020-11-24 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Increased helical flexibility of the TNFalpha transmembrane domain enhances non-canonical shedding by SPPL2a ; _Citation_status published _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 Spitz C. . . 2 Schlosser C. . . 3 Guschtschin-Schmidt N. . . 4 Stelzer W. . . 5 Menig S. . . 6 Gotz A. . . 7 Haug-Kroper M. . . 8 Scharnagl C. . . 9 Langosch D. . . 10 Muhle-Goll C. . . 11 Fluhrer R. . . stop_ _Journal_abbreviation iScience _Journal_volume 23 _Journal_issue . _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 101775 _Page_last 101775 _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Tumor necrosis factor' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label unit_1 $entity_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 3841.764 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 33 _Mol_residue_sequence ; RRCLFLSLFSFLIVLLLTTL FCLLHFGVIGPQR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 28 ARG 2 29 ARG 3 30 CYS 4 31 LEU 5 32 PHE 6 33 LEU 7 34 SER 8 35 LEU 9 36 PHE 10 37 SER 11 38 PHE 12 39 LEU 13 40 ILE 14 41 VAL 15 42 LEU 16 43 LEU 17 44 LEU 18 45 THR 19 46 THR 20 47 LEU 21 48 PHE 22 49 CYS 23 50 LEU 24 51 LEU 25 52 HIS 26 53 PHE 27 54 GLY 28 55 VAL 29 56 ILE 30 57 GLY 31 58 PRO 32 59 GLN 33 60 ARG 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 $entity_1 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 $entity_1 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '0.5 mM TNFA_TM_AGALLL, trifluoroethanol/water' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name TopSpin _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_software_2 _Saveframe_category software _Name 'CcpNmr Analysis' _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name ARIA _Version . loop_ _Vendor _Address _Electronic_address "Linge, O'Donoghue and Nilges" . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details 'TXI cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _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 0.1 M pH 6.5 0.3 pH pressure 1 . atm temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 TFE C 13 'methylene carbons' ppm 61.5 internal direct . . . 1 TFE H 1 'methylene protons' ppm 3.88 internal direct . . . 1 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-1H TOCSY' '2D 1H-13C HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name unit_1 _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 28 1 ARG HA H 3.668 . . 2 28 1 ARG HB2 H 1.817 . . 3 28 1 ARG HB3 H 1.947 . . 4 28 1 ARG HG2 H 1.731 . . 5 28 1 ARG HD2 H 3.230 . . 6 28 1 ARG CA C 55.850 . . 7 28 1 ARG CB C 31.982 . . 8 28 1 ARG CG C 26.675 . . 9 28 1 ARG CD C 42.421 . . 10 29 2 ARG HA H 3.668 . . 11 29 2 ARG HB2 H 1.947 . . 12 29 2 ARG HB3 H 1.817 . . 13 29 2 ARG HG2 H 1.731 . . 14 29 2 ARG HD2 H 3.230 . . 15 29 2 ARG CA C 55.850 . . 16 29 2 ARG CB C 31.982 . . 17 29 2 ARG CG C 26.675 . . 18 29 2 ARG CD C 42.421 . . 19 30 3 CYS H H 8.327 . . 20 30 3 CYS HA H 4.405 . . 21 30 3 CYS HB2 H 3.039 . . 22 30 3 CYS HB3 H 2.973 . . 23 30 3 CYS CA C 59.010 . . 24 30 3 CYS CB C 26.190 . . 25 31 4 LEU H H 7.731 . . 26 31 4 LEU HA H 4.221 . . 27 31 4 LEU HB2 H 1.670 . . 28 31 4 LEU HB3 H 1.610 . . 29 31 4 LEU HD1 H 0.952 . . 30 31 4 LEU CA C 57.996 . . 31 31 4 LEU CB C 41.310 . . 32 31 4 LEU CD1 C 21.934 . . 33 32 5 PHE H H 7.729 . . 34 32 5 PHE HA H 4.338 . . 35 32 5 PHE HB2 H 3.169 . . 36 32 5 PHE CA C 60.195 . . 37 32 5 PHE CB C 38.028 . . 38 33 6 LEU H H 8.001 . . 39 33 6 LEU HA H 4.219 . . 40 33 6 LEU HB2 H 1.824 . . 41 33 6 LEU HG H 1.676 . . 42 33 6 LEU HD1 H 0.976 . . 43 33 6 LEU CA C 57.118 . . 44 33 6 LEU CB C 41.295 . . 45 33 6 LEU CG C 26.600 . . 46 33 6 LEU CD1 C 23.540 . . 47 34 7 SER H H 7.880 . . 48 34 7 SER HA H 4.275 . . 49 34 7 SER HB2 H 4.146 . . 50 34 7 SER HB3 H 3.981 . . 51 34 7 SER CA C 57.444 . . 52 34 7 SER CB C 62.406 . . 53 35 8 LEU H H 7.943 . . 54 35 8 LEU HA H 4.275 . . 55 35 8 LEU HB2 H 1.748 . . 56 35 8 LEU HB3 H 1.657 . . 57 35 8 LEU HD1 H 0.947 . . 58 35 8 LEU HD2 H 0.895 . . 59 35 8 LEU CA C 57.444 . . 60 35 8 LEU CB C 41.354 . . 61 35 8 LEU CD1 C 23.352 . . 62 35 8 LEU CD2 C 22.655 . . 63 36 9 PHE H H 8.380 . . 64 36 9 PHE HA H 4.344 . . 65 36 9 PHE HB2 H 3.091 . . 66 36 9 PHE HB3 H 3.030 . . 67 36 9 PHE CA C 60.196 . . 68 36 9 PHE CB C 38.300 . . 69 37 10 SER H H 7.984 . . 70 37 10 SER HA H 4.275 . . 71 37 10 SER HB2 H 3.983 . . 72 37 10 SER HB3 H 4.120 . . 73 37 10 SER CA C 57.193 . . 74 37 10 SER CB C 62.415 . . 75 38 11 PHE H H 7.682 . . 76 38 11 PHE HA H 4.371 . . 77 38 11 PHE HB2 H 3.282 . . 78 38 11 PHE CA C 60.053 . . 79 38 11 PHE CB C 38.443 . . 80 39 12 LEU H H 8.048 . . 81 39 12 LEU HA H 3.955 . . 82 39 12 LEU HB2 H 1.859 . . 83 39 12 LEU HG H 1.640 . . 84 39 12 LEU HD1 H 0.933 . . 85 39 12 LEU CA C 57.545 . . 86 39 12 LEU CB C 40.910 . . 87 39 12 LEU CG C 26.450 . . 88 39 12 LEU CD1 C 22.798 . . 89 40 13 ILE H H 7.908 . . 90 40 13 ILE HA H 3.777 . . 91 40 13 ILE HB H 1.936 . . 92 40 13 ILE HG12 H 1.468 . . 93 40 13 ILE HG13 H 1.151 . . 94 40 13 ILE HG2 H 0.904 . . 95 40 13 ILE HD1 H 0.751 . . 96 40 13 ILE CA C 64.867 . . 97 40 13 ILE CB C 36.420 . . 98 40 13 ILE CG1 C 27.704 . . 99 40 13 ILE CG2 C 16.343 . . 100 40 13 ILE CD1 C 10.519 . . 101 41 14 VAL H H 7.629 . . 102 41 14 VAL HA H 3.626 . . 103 41 14 VAL HB H 2.206 . . 104 41 14 VAL HG1 H 1.099 . . 105 41 14 VAL HG2 H 0.915 . . 106 41 14 VAL CA C 66.570 . . 107 41 14 VAL CB C 30.755 . . 108 41 14 VAL CG1 C 21.679 . . 109 41 14 VAL CG2 C 19.942 . . 110 42 15 LEU H H 8.321 . . 111 42 15 LEU HA H 3.970 . . 112 42 15 LEU HB2 H 1.630 . . 113 42 15 LEU HB3 H 1.493 . . 114 42 15 LEU HD1 H 0.817 . . 115 42 15 LEU CA C 58.025 . . 116 42 15 LEU CB C 40.899 . . 117 42 15 LEU CD1 C 22.932 . . 118 43 16 LEU H H 8.620 . . 119 43 16 LEU HA H 4.074 . . 120 43 16 LEU HB2 H 1.752 . . 121 43 16 LEU HB3 H 1.861 . . 122 43 16 LEU HD1 H 0.913 . . 123 43 16 LEU CA C 58.337 . . 124 43 16 LEU CB C 41.036 . . 125 43 16 LEU CD1 C 22.100 . . 126 44 17 LEU H H 8.881 . . 127 44 17 LEU HA H 4.112 . . 128 44 17 LEU HB2 H 1.945 . . 129 44 17 LEU HG H 1.492 . . 130 44 17 LEU HD1 H 0.882 . . 131 44 17 LEU CA C 57.864 . . 132 44 17 LEU CB C 41.033 . . 133 44 17 LEU CG C 26.022 . . 134 44 17 LEU CD1 C 22.394 . . 135 45 18 THR H H 8.496 . . 136 45 18 THR HA H 3.992 . . 137 45 18 THR HB H 4.335 . . 138 45 18 THR HG1 H 5.339 . . 139 45 18 THR HG2 H 1.307 . . 140 45 18 THR CA C 66.640 . . 141 45 18 THR CB C 68.499 . . 142 45 18 THR CG2 C 19.859 . . 143 46 19 THR H H 8.189 . . 144 46 19 THR HA H 3.924 . . 145 46 19 THR HB H 4.536 . . 146 46 19 THR HG1 H 5.453 . . 147 46 19 THR HG2 H 1.282 . . 148 46 19 THR CA C 67.491 . . 149 46 19 THR CB C 68.089 . . 150 46 19 THR CG2 C 19.329 . . 151 47 20 LEU H H 8.501 . . 152 47 20 LEU HA H 4.105 . . 153 47 20 LEU HB2 H 1.882 . . 154 47 20 LEU HB3 H 1.827 . . 155 47 20 LEU HG H 1.739 . . 156 47 20 LEU HD1 H 0.897 . . 157 47 20 LEU CA C 61.579 . . 158 47 20 LEU CB C 41.077 . . 159 47 20 LEU CG C 26.346 . . 160 47 20 LEU CD1 C 22.934 . . 161 48 21 PHE H H 8.561 . . 162 48 21 PHE HA H 4.159 . . 163 48 21 PHE HB2 H 3.480 . . 164 48 21 PHE HB3 H 3.373 . . 165 48 21 PHE CA C 61.913 . . 166 48 21 PHE CB C 38.236 . . 167 49 22 CYS H H 8.510 . . 168 49 22 CYS HA H 4.179 . . 169 49 22 CYS HB2 H 3.383 . . 170 49 22 CYS HB3 H 2.970 . . 171 49 22 CYS CA C 63.936 . . 172 49 22 CYS CB C 25.818 . . 173 50 23 LEU H H 8.709 . . 174 50 23 LEU HA H 4.104 . . 175 50 23 LEU HB2 H 1.983 . . 176 50 23 LEU HB3 H 1.893 . . 177 50 23 LEU HG H 1.608 . . 178 50 23 LEU HD1 H 0.888 . . 179 50 23 LEU CA C 56.558 . . 180 50 23 LEU CB C 41.311 . . 181 50 23 LEU CG C 26.462 . . 182 50 23 LEU CD1 C 21.835 . . 183 51 24 LEU H H 8.430 . . 184 51 24 LEU HA H 4.101 . . 185 51 24 LEU HB2 H 1.701 . . 186 51 24 LEU HB3 H 1.749 . . 187 51 24 LEU HG H 1.287 . . 188 51 24 LEU HD1 H 0.838 . . 189 51 24 LEU HD2 H 0.802 . . 190 51 24 LEU CA C 58.047 . . 191 51 24 LEU CB C 41.371 . . 192 51 24 LEU CG C 30.903 . . 193 51 24 LEU CD1 C 23.669 . . 194 51 24 LEU CD2 C 21.468 . . 195 52 25 HIS H H 7.818 . . 196 52 25 HIS HA H 4.244 . . 197 52 25 HIS HB2 H 2.848 . . 198 52 25 HIS HB3 H 2.544 . . 199 52 25 HIS CA C 58.102 . . 200 52 25 HIS CB C 27.636 . . 201 53 26 PHE H H 8.259 . . 202 53 26 PHE HA H 4.672 . . 203 53 26 PHE HB2 H 3.188 . . 204 53 26 PHE HB3 H 3.319 . . 205 53 26 PHE CB C 38.542 . . 206 54 27 GLY H H 7.995 . . 207 54 27 GLY HA2 H 3.971 . . 208 54 27 GLY CA C 45.223 . . 209 55 28 VAL H H 7.605 . . 210 55 28 VAL HA H 4.098 . . 211 55 28 VAL HB H 2.176 . . 212 55 28 VAL HG1 H 0.974 . . 213 55 28 VAL CA C 62.656 . . 214 55 28 VAL CB C 32.033 . . 215 55 28 VAL CG1 C 19.506 . . 216 56 29 ILE H H 7.510 . . 217 56 29 ILE HA H 4.259 . . 218 56 29 ILE HB H 1.913 . . 219 56 29 ILE HG12 H 1.514 . . 220 56 29 ILE HG13 H 1.169 . . 221 56 29 ILE HG2 H 0.947 . . 222 56 29 ILE HD1 H 0.885 . . 223 56 29 ILE CA C 60.681 . . 224 56 29 ILE CB C 38.520 . . 225 56 29 ILE CG1 C 26.404 . . 226 56 29 ILE CG2 C 16.341 . . 227 56 29 ILE CD1 C 11.746 . . 228 57 30 GLY H H 7.679 . . 229 57 30 GLY HA2 H 4.105 . . 230 57 30 GLY HA3 H 3.990 . . 231 57 30 GLY CA C 43.837 . . 232 58 31 PRO HA H 4.405 . . 233 58 31 PRO HB2 H 1.996 . . 234 58 31 PRO HB3 H 2.194 . . 235 58 31 PRO HD2 H 3.628 . . 236 58 31 PRO HD3 H 3.495 . . 237 58 31 PRO CA C 62.747 . . 238 58 31 PRO CB C 31.033 . . 239 58 31 PRO CD C 48.757 . . 240 59 32 GLN H H 8.016 . . 241 59 32 GLN HA H 4.312 . . 242 59 32 GLN HB2 H 2.165 . . 243 59 32 GLN HB3 H 2.005 . . 244 59 32 GLN HG2 H 2.377 . . 245 59 32 GLN CA C 55.419 . . 246 59 32 GLN CB C 28.690 . . 247 60 33 ARG H H 7.593 . . 248 60 33 ARG HA H 4.247 . . 249 60 33 ARG HB2 H 1.893 . . 250 60 33 ARG HB3 H 1.744 . . 251 60 33 ARG HG2 H 1.637 . . 252 60 33 ARG HD2 H 3.203 . . 253 60 33 ARG CA C 56.381 . . 254 60 33 ARG CB C 31.008 . . 255 60 33 ARG CG C 26.134 . . 256 60 33 ARG CD C 42.700 . . stop_ save_