data_34268 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of the scorpion toxin AmmTx3 ; _BMRB_accession_number 34268 _BMRB_flat_file_name bmr34268.str _Entry_type original _Submission_date 2018-05-04 _Accession_date 2018-05-04 _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 Landon C. . . 2 Meudal H. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 205 "15N chemical shifts" 34 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-01-25 original BMRB . stop_ _Original_release_date 2019-01-22 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Synthesis by native chemical ligation and characterization of the scorpion toxin AmmTx3. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30529150 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zoukimian C. . . 2 Meudal H. . . 3 'De Waard' S. . . 4 Ouares K. A. . 5 Nicolas S. . . 6 Canepari M. . . 7 Beroud R. . . 8 Landon C. . . 9 'De Waard' M. . . 10 Boturyn D. . . stop_ _Journal_abbreviation 'Bioorg. Med. Chem.' _Journal_volume 27 _Journal_issue . _Journal_ASTM BMECEP _Journal_ISSN 1464-3391 _Journal_CSD 1200 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 247 _Page_last 253 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Potassium channel toxin alpha-KTx 15.3' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_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 3834.563 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; XIETNKKCQGGSCASVCRKV IGVAAGKCINGRCVCYP ; loop_ _Residue_seq_code _Residue_label 1 PCA 2 ILE 3 GLU 4 THR 5 ASN 6 LYS 7 LYS 8 CYS 9 GLN 10 GLY 11 GLY 12 SER 13 CYS 14 ALA 15 SER 16 VAL 17 CYS 18 ARG 19 LYS 20 VAL 21 ILE 22 GLY 23 VAL 24 ALA 25 ALA 26 GLY 27 LYS 28 CYS 29 ILE 30 ASN 31 GLY 32 ARG 33 CYS 34 VAL 35 CYS 36 TYR 37 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_PCA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common 'PYROGLUTAMIC ACID' _BMRB_code PCA _PDB_code PCA _Standard_residue_derivative . _Molecular_mass 129.114 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OE OE O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N CD ? ? SING N H ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? DOUB CD OE ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ 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 Scorpion 6860 Eukaryota Metazoa Androctonus mauritanicus 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 '1.2 mM AmmTx3, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1.2 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 collection processing stop_ _Details . save_ save_software_2 _Saveframe_category software _Name CcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 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 refinement 'structure calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceIII _Field_strength 700 _Details 'TCI cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_15N_Sofast_HMQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N Sofast HMQC' _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 . mM pH 4.5 . pH pressure 1 . atm temperature 298 . 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 DSS H 1 'methyl protons' ppm 0.000 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.000 internal indirect . . . 0.10132912 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 TOCSY' '2D 1H-1H NOESY' '15N Sofast HMQC' 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 entity_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 1 1 PCA N N 128.837 0 . 2 1 1 PCA HA H 4.099 0 . 3 1 1 PCA HB2 H 2.081 0 . 4 1 1 PCA HB3 H 1.835 0 . 5 1 1 PCA HG2 H 2.435 0 . 6 1 1 PCA HG3 H 2.385 0 . 7 2 2 ILE H H 8.795 0 . 8 2 2 ILE HA H 4.232 0 . 9 2 2 ILE HB H 1.535 0 . 10 2 2 ILE HG12 H 1.126 0 . 11 2 2 ILE HG13 H 1.360 0 . 12 2 2 ILE HG2 H 0.745 0 . 13 2 2 ILE HD1 H 0.759 0 . 14 2 2 ILE N N 125.802 0 . 15 3 3 GLU H H 8.857 0 . 16 3 3 GLU HA H 4.277 0 . 17 3 3 GLU HB2 H 2.063 0 . 18 3 3 GLU HB3 H 1.983 0 . 19 3 3 GLU HG2 H 2.319 0 . 20 3 3 GLU HG3 H 2.243 0 . 21 3 3 GLU N N 130.615 0 . 22 4 4 THR H H 7.817 0 . 23 4 4 THR HA H 4.565 0 . 24 4 4 THR HB H 4.197 0 . 25 4 4 THR HG1 H 5.724 0 . 26 4 4 THR HG2 H 1.133 0 . 27 4 4 THR N N 116.640 0 . 28 5 5 ASN HA H 4.634 0 . 29 5 5 ASN HB2 H 2.919 0 . 30 5 5 ASN HB3 H 2.920 0 . 31 5 5 ASN HD21 H 7.525 0 . 32 5 5 ASN HD22 H 6.858 0 . 33 6 6 LYS H H 8.229 0 . 34 6 6 LYS HA H 4.466 0 . 35 6 6 LYS HB2 H 1.700 0 . 36 6 6 LYS HB3 H 1.700 0 . 37 6 6 LYS HG2 H 1.401 0 . 38 6 6 LYS HG3 H 1.401 0 . 39 6 6 LYS HD2 H 1.596 0 . 40 6 6 LYS HD3 H 1.596 0 . 41 6 6 LYS HE2 H 2.938 0 . 42 6 6 LYS HE3 H 2.987 0 . 43 6 6 LYS N N 122.891 0 . 44 7 7 LYS H H 8.423 0 . 45 7 7 LYS HA H 4.574 0 . 46 7 7 LYS HB2 H 1.714 0 . 47 7 7 LYS HB3 H 1.882 0 . 48 7 7 LYS HG2 H 1.478 0 . 49 7 7 LYS HG3 H 1.478 0 . 50 7 7 LYS HD2 H 1.592 0 . 51 7 7 LYS HD3 H 1.592 0 . 52 7 7 LYS HE2 H 3.001 0 . 53 7 7 LYS HE3 H 3.001 0 . 54 7 7 LYS N N 125.323 0 . 55 8 8 CYS H H 7.671 0 . 56 8 8 CYS HA H 4.404 0 . 57 8 8 CYS HB2 H 2.916 0 . 58 8 8 CYS HB3 H 3.087 0 . 59 8 8 CYS N N 119.497 0 . 60 9 9 GLN H H 8.405 0 . 61 9 9 GLN HA H 4.544 0 . 62 9 9 GLN HB2 H 2.070 0 . 63 9 9 GLN HB3 H 1.935 0 . 64 9 9 GLN HG2 H 2.267 0 . 65 9 9 GLN HG3 H 2.267 0 . 66 9 9 GLN HE21 H 6.823 0 . 67 9 9 GLN HE22 H 7.501 0 . 68 9 9 GLN N N 123.171 0 . 69 10 10 GLY H H 8.715 0 . 70 10 10 GLY HA2 H 3.985 0 . 71 10 10 GLY HA3 H 3.845 0 . 72 11 11 GLY H H 8.350 0 . 73 11 11 GLY HA2 H 4.105 0 . 74 11 11 GLY HA3 H 3.922 0 . 75 11 11 GLY N N 110.045 0 . 76 12 12 SER H H 7.994 0 . 77 12 12 SER HA H 4.664 0 . 78 12 12 SER HB2 H 4.031 0 . 79 12 12 SER HB3 H 3.958 0 . 80 12 12 SER N N 116.577 0 . 81 13 13 CYS H H 9.132 0 . 82 13 13 CYS HA H 4.841 0 . 83 13 13 CYS HB2 H 2.410 0 . 84 13 13 CYS HB3 H 3.188 0 . 85 13 13 CYS N N 125.334 0 . 86 14 14 ALA H H 8.114 0 . 87 14 14 ALA HA H 3.926 0 . 88 14 14 ALA HB H 1.448 0 . 89 14 14 ALA N N 128.914 0 . 90 15 15 SER H H 8.301 0 . 91 15 15 SER HA H 4.133 0 . 92 15 15 SER HB2 H 3.902 0 . 93 15 15 SER HB3 H 3.902 0 . 94 15 15 SER N N 115.081 0 . 95 16 16 VAL H H 7.429 0 . 96 16 16 VAL HA H 3.666 0 . 97 16 16 VAL HB H 2.040 0 . 98 16 16 VAL HG1 H 0.783 0 . 99 16 16 VAL HG2 H 1.064 0 . 100 16 16 VAL N N 125.439 0 . 101 17 17 CYS H H 8.457 0 . 102 17 17 CYS HA H 4.436 0 . 103 17 17 CYS HB2 H 2.792 0 . 104 17 17 CYS HB3 H 3.025 0 . 105 17 17 CYS N N 120.118 0 . 106 18 18 ARG H H 8.211 0 . 107 18 18 ARG HA H 3.594 0 . 108 18 18 ARG HB2 H 1.773 0 . 109 18 18 ARG HB3 H 1.858 0 . 110 18 18 ARG HG2 H 1.533 0 . 111 18 18 ARG HG3 H 1.533 0 . 112 18 18 ARG HD2 H 3.114 0 . 113 18 18 ARG HD3 H 3.114 0 . 114 18 18 ARG HE H 7.241 0 . 115 18 18 ARG N N 125.438 0 . 116 19 19 LYS H H 7.401 0 . 117 19 19 LYS HA H 4.126 0 . 118 19 19 LYS HB2 H 1.943 0 . 119 19 19 LYS HB3 H 1.982 0 . 120 19 19 LYS HG2 H 1.440 0 . 121 19 19 LYS HG3 H 1.524 0 . 122 19 19 LYS HD2 H 1.674 0 . 123 19 19 LYS HD3 H 1.674 0 . 124 19 19 LYS HE2 H 2.960 0 . 125 19 19 LYS HE3 H 2.962 0 . 126 19 19 LYS N N 120.543 0 . 127 20 20 VAL H H 8.119 0 . 128 20 20 VAL HA H 3.954 0 . 129 20 20 VAL HB H 2.048 0 . 130 20 20 VAL HG1 H 0.959 0 . 131 20 20 VAL HG2 H 1.054 0 . 132 20 20 VAL N N 120.387 0 . 133 21 21 ILE H H 8.382 0 . 134 21 21 ILE HA H 4.717 0 . 135 21 21 ILE HB H 2.175 0 . 136 21 21 ILE HG12 H 1.408 0 . 137 21 21 ILE HG13 H 1.225 0 . 138 21 21 ILE HG2 H 0.904 0 . 139 21 21 ILE HD1 H 0.786 0 . 140 21 21 ILE N N 115.521 0 . 141 22 22 GLY H H 7.591 0 . 142 22 22 GLY HA2 H 4.295 0 . 143 22 22 GLY HA3 H 4.006 0 . 144 22 22 GLY N N 113.405 0 . 145 23 23 VAL H H 7.037 0 . 146 23 23 VAL HA H 4.370 0 . 147 23 23 VAL HB H 1.989 0 . 148 23 23 VAL HG1 H 0.853 0 . 149 23 23 VAL HG2 H 0.925 0 . 150 23 23 VAL N N 119.832 0 . 151 24 24 ALA H H 8.471 0 . 152 24 24 ALA HA H 4.481 0 . 153 24 24 ALA HB H 1.277 0 . 154 24 24 ALA N N 129.419 0 . 155 25 25 ALA H H 7.526 0 . 156 25 25 ALA HA H 4.576 0 . 157 25 25 ALA HB H 1.424 0 . 158 25 25 ALA N N 126.706 0 . 159 26 26 GLY H H 8.164 0 . 160 26 26 GLY HA2 H 4.205 0 . 161 26 26 GLY HA3 H 4.822 0 . 162 26 26 GLY N N 111.718 0 . 163 27 27 LYS H H 9.215 0 . 164 27 27 LYS HA H 4.599 0 . 165 27 27 LYS HB2 H 1.806 0 . 166 27 27 LYS HB3 H 1.805 0 . 167 27 27 LYS HG2 H 1.398 0 . 168 27 27 LYS HG3 H 1.398 0 . 169 27 27 LYS HD2 H 1.658 0 . 170 27 27 LYS HD3 H 1.658 0 . 171 27 27 LYS HE2 H 2.836 0 . 172 27 27 LYS HE3 H 2.836 0 . 173 27 27 LYS N N 122.629 0 . 174 28 28 CYS H H 8.822 0 . 175 28 28 CYS HA H 4.791 0 . 176 28 28 CYS HB2 H 2.757 0 . 177 28 28 CYS HB3 H 3.086 0 . 178 28 28 CYS N N 127.113 0 . 179 29 29 ILE H H 9.134 0 . 180 29 29 ILE HA H 4.353 0 . 181 29 29 ILE HB H 1.806 0 . 182 29 29 ILE HG12 H 1.476 0 . 183 29 29 ILE HG13 H 1.066 0 . 184 29 29 ILE HG2 H 0.869 0 . 185 29 29 ILE HD1 H 0.864 0 . 186 29 29 ILE N N 125.334 0 . 187 30 30 ASN H H 9.496 0 . 188 30 30 ASN HA H 4.353 0 . 189 30 30 ASN HB2 H 3.086 0 . 190 30 30 ASN HB3 H 2.753 0 . 191 30 30 ASN HD21 H 7.639 0 . 192 30 30 ASN HD22 H 6.903 0 . 193 30 30 ASN N N 130.123 0 . 194 31 31 GLY H H 8.276 0 . 195 31 31 GLY HA2 H 3.665 0 . 196 31 31 GLY HA3 H 4.098 0 . 197 31 31 GLY N N 105.326 0 . 198 32 32 ARG H H 7.821 0 . 199 32 32 ARG HA H 5.178 0 . 200 32 32 ARG HB2 H 1.718 0 . 201 32 32 ARG HB3 H 1.718 0 . 202 32 32 ARG HG2 H 1.498 0 . 203 32 32 ARG HG3 H 1.606 0 . 204 32 32 ARG HD2 H 3.148 0 . 205 32 32 ARG HD3 H 3.064 0 . 206 32 32 ARG HE H 7.348 0 . 207 32 32 ARG N N 123.465 0 . 208 33 33 CYS H H 8.413 0 . 209 33 33 CYS HA H 5.175 0 . 210 33 33 CYS HB2 H 2.680 0 . 211 33 33 CYS HB3 H 2.541 0 . 212 33 33 CYS N N 120.046 0 . 213 34 34 VAL H H 9.252 0 . 214 34 34 VAL HA H 4.720 0 . 215 34 34 VAL HB H 1.987 0 . 216 34 34 VAL HG1 H 0.963 0 . 217 34 34 VAL HG2 H 0.630 0 . 218 34 34 VAL N N 131.211 0 . 219 35 35 CYS H H 8.806 0 . 220 35 35 CYS HA H 5.481 0 . 221 35 35 CYS HB2 H 2.217 0 . 222 35 35 CYS HB3 H 3.117 0 . 223 35 35 CYS N N 125.327 0 . 224 36 36 TYR H H 8.323 0 . 225 36 36 TYR HA H 5.027 0 . 226 36 36 TYR HB2 H 3.014 0 . 227 36 36 TYR HB3 H 2.605 0 . 228 36 36 TYR HD1 H 6.999 0 . 229 36 36 TYR HD2 H 6.999 0 . 230 36 36 TYR HE1 H 6.605 0 . 231 36 36 TYR HE2 H 6.605 0 . 232 36 36 TYR N N 125.372 0 . 233 37 37 PRO HA H 4.213 0 . 234 37 37 PRO HB2 H 1.988 0 . 235 37 37 PRO HB3 H 2.137 0 . 236 37 37 PRO HG2 H 1.882 0 . 237 37 37 PRO HG3 H 1.994 0 . 238 37 37 PRO HD2 H 3.889 0 . 239 37 37 PRO HD3 H 3.427 0 . stop_ save_