data_25283 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of scoloptoxin SSD609 from Scolopendra mutilans ; _BMRB_accession_number 25283 _BMRB_flat_file_name bmr25283.str _Entry_type original _Submission_date 2014-10-14 _Accession_date 2014-10-14 _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 Wu Fangming . . 2 Sun Peibei . . 3 Wang Chenyang . . 4 He Yao . . 5 Zhang Longhua . . 6 Tian Changlin . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 217 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-09-04 original BMRB . stop_ _Original_release_date 2015-09-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A distinct three-helix centipede toxin SSD609 inhibits Iks channels by interacting with the KCNE1 auxiliary subunit ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26307551 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sun Peibei . . 2 Wu Fangming . . 3 Wen Ming . . 4 Yang Xingwang . . 5 Wang Chenyang . . 6 Li Yiming . . 7 He Shufang . . 8 Zhang Longhua . . 9 Zhang Yun . . 10 Tian Changlin . . stop_ _Journal_abbreviation 'Sci. Rep.' _Journal_volume 5 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 13399 _Page_last 13399 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'scoloptoxin SSD609 from Scolopendra mutilans' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SSD609 _Molecular_mass 5640.370 _Mol_thiol_state 'disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 47 _Mol_residue_sequence ; ADDKCEDSLRREIACTKCRD RVRTDDYFYECCTSESTFKK CQTMLHQ ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 ASP 4 LYS 5 CYS 6 GLU 7 ASP 8 SER 9 LEU 10 ARG 11 ARG 12 GLU 13 ILE 14 ALA 15 CYS 16 THR 17 LYS 18 CYS 19 ARG 20 ASP 21 ARG 22 VAL 23 ARG 24 THR 25 ASP 26 ASP 27 TYR 28 PHE 29 TYR 30 GLU 31 CYS 32 CYS 33 THR 34 SER 35 GLU 36 SER 37 THR 38 PHE 39 LYS 40 LYS 41 CYS 42 GLN 43 THR 44 MET 45 LEU 46 HIS 47 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 2MVT "Solution Structure Of Scoloptoxin Ssd609 From Scolopendra Mutilans" 100.00 47 100.00 100.00 8.77e-24 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 Centipedes 251420 Eukaryota Metazoa Scolopendra mutilans 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 'recombinant technology' . Escherichia coli . pET28 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 $entity 1 mM 'natural abundance' TRIS 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' 'calcium chloride' 5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _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-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _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' 0.115 . M pH 7.0 . pH pressure 1 . atm temperature 298 . 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 H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 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-1H TOCSY' '2D 1H-1H NOESY' 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 entity _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 ALA HA H 4.073 0.004 . 2 1 1 ALA HB H 1.505 0.005 . 3 2 2 ASP H H 8.670 0.021 . 4 2 2 ASP HA H 4.546 0.018 . 5 2 2 ASP HB2 H 2.562 0.019 . 6 2 2 ASP HB3 H 2.665 0.001 . 7 3 3 ASP H H 8.316 0.016 . 8 3 3 ASP HA H 4.203 0.020 . 9 3 3 ASP HB2 H 2.894 0.012 . 10 3 3 ASP HB3 H 2.430 0.014 . 11 4 4 LYS H H 8.295 0.022 . 12 4 4 LYS HA H 4.171 0.003 . 13 4 4 LYS HB2 H 1.831 0.007 . 14 4 4 LYS HB3 H 1.543 0.015 . 15 5 5 CYS H H 8.498 0.005 . 16 5 5 CYS HA H 3.810 0.011 . 17 5 5 CYS HB2 H 3.598 0.018 . 18 5 5 CYS HB3 H 3.298 0.016 . 19 6 6 GLU H H 7.303 0.015 . 20 6 6 GLU HA H 3.949 0.010 . 21 6 6 GLU HB2 H 1.960 0.004 . 22 6 6 GLU HB3 H 1.960 0.004 . 23 7 7 ASP H H 7.084 0.017 . 24 7 7 ASP HA H 4.683 0.004 . 25 7 7 ASP HB2 H 2.722 0.003 . 26 7 7 ASP HB3 H 2.523 0.015 . 27 8 8 SER H H 7.116 0.006 . 28 8 8 SER HA H 4.743 0.019 . 29 8 8 SER HB2 H 3.750 0.006 . 30 8 8 SER HB3 H 3.725 0.001 . 31 9 9 LEU H H 8.759 0.023 . 32 9 9 LEU HA H 4.294 0.016 . 33 9 9 LEU HB2 H 1.649 0.011 . 34 9 9 LEU HB3 H 1.681 0.000 . 35 9 9 LEU HD1 H 0.958 0.000 . 36 9 9 LEU HD2 H 0.909 0.000 . 37 10 10 ARG H H 8.297 0.018 . 38 10 10 ARG HA H 3.957 0.006 . 39 10 10 ARG HB2 H 1.778 0.017 . 40 10 10 ARG HB3 H 1.811 0.000 . 41 11 11 ARG H H 7.563 0.023 . 42 11 11 ARG HA H 3.837 0.005 . 43 11 11 ARG HB2 H 1.824 0.007 . 44 11 11 ARG HB3 H 1.343 0.009 . 45 12 12 GLU H H 8.225 0.022 . 46 12 12 GLU HA H 4.263 0.018 . 47 12 12 GLU HB2 H 2.513 0.005 . 48 12 12 GLU HB3 H 2.552 0.006 . 49 12 12 GLU HG2 H 1.701 0.002 . 50 12 12 GLU HG3 H 1.827 0.001 . 51 13 13 ILE H H 9.074 0.016 . 52 13 13 ILE HA H 3.745 0.008 . 53 13 13 ILE HB H 1.865 0.004 . 54 13 13 ILE HG12 H 1.185 0.020 . 55 13 13 ILE HG13 H 1.185 0.020 . 56 13 13 ILE HG2 H 0.959 0.001 . 57 13 13 ILE HD1 H 0.915 0.008 . 58 14 14 ALA H H 7.961 0.020 . 59 14 14 ALA HA H 4.124 0.010 . 60 14 14 ALA HB H 1.707 0.011 . 61 15 15 CYS H H 9.032 0.025 . 62 15 15 CYS HA H 5.043 0.013 . 63 15 15 CYS HB2 H 3.002 0.020 . 64 15 15 CYS HB3 H 2.904 0.014 . 65 16 16 THR H H 8.529 0.019 . 66 16 16 THR HA H 3.960 0.008 . 67 16 16 THR HB H 4.546 0.007 . 68 16 16 THR HG2 H 1.207 0.002 . 69 17 17 LYS H H 8.074 0.014 . 70 17 17 LYS HA H 4.166 0.007 . 71 17 17 LYS HB2 H 2.207 0.013 . 72 17 17 LYS HB3 H 1.836 0.009 . 73 17 17 LYS HG2 H 0.978 0.005 . 74 17 17 LYS HG3 H 0.716 0.005 . 75 17 17 LYS HD2 H 1.756 0.009 . 76 17 17 LYS HD3 H 1.487 0.014 . 77 18 18 CYS H H 9.312 0.015 . 78 18 18 CYS HA H 3.785 0.006 . 79 18 18 CYS HB2 H 4.080 0.017 . 80 18 18 CYS HB3 H 3.232 0.011 . 81 19 19 ARG H H 8.724 0.015 . 82 19 19 ARG HA H 3.832 0.009 . 83 19 19 ARG HB2 H 2.421 0.006 . 84 19 19 ARG HB3 H 2.349 0.004 . 85 19 19 ARG HG2 H 1.884 0.012 . 86 19 19 ARG HG3 H 1.884 0.012 . 87 20 20 ASP H H 7.612 0.011 . 88 20 20 ASP HA H 4.485 0.002 . 89 20 20 ASP HB2 H 2.805 0.018 . 90 20 20 ASP HB3 H 2.853 0.000 . 91 21 21 ARG H H 7.375 0.004 . 92 21 21 ARG HA H 4.304 0.004 . 93 21 21 ARG HB2 H 1.864 0.003 . 94 21 21 ARG HB3 H 1.699 0.003 . 95 22 22 VAL H H 7.818 0.019 . 96 22 22 VAL HA H 3.789 0.012 . 97 22 22 VAL HB H 1.246 0.013 . 98 22 22 VAL HG1 H 0.806 0.015 . 99 22 22 VAL HG2 H 0.467 0.005 . 100 23 23 ARG H H 8.440 0.017 . 101 23 23 ARG HA H 4.068 0.017 . 102 23 23 ARG HB2 H 1.508 0.006 . 103 23 23 ARG HB3 H 1.361 0.016 . 104 23 23 ARG HG2 H 1.952 0.000 . 105 23 23 ARG HG3 H 1.868 0.000 . 106 23 23 ARG HD2 H 3.157 0.003 . 107 23 23 ARG HD3 H 3.157 0.003 . 108 24 24 THR H H 7.101 0.009 . 109 24 24 THR HA H 4.593 0.007 . 110 24 24 THR HB H 4.408 0.019 . 111 25 25 ASP H H 8.938 0.022 . 112 25 25 ASP HA H 4.448 0.008 . 113 25 25 ASP HB2 H 2.683 0.004 . 114 25 25 ASP HB3 H 2.683 0.004 . 115 26 26 ASP H H 8.846 0.017 . 116 26 26 ASP HA H 4.795 0.015 . 117 26 26 ASP HB2 H 2.972 0.007 . 118 26 26 ASP HB3 H 2.764 0.005 . 119 27 27 TYR H H 7.545 0.012 . 120 27 27 TYR HA H 3.757 0.011 . 121 27 27 TYR HB2 H 3.376 0.010 . 122 27 27 TYR HB3 H 2.720 0.008 . 123 28 28 PHE H H 9.120 0.021 . 124 28 28 PHE HA H 3.884 0.010 . 125 28 28 PHE HB2 H 3.123 0.009 . 126 28 28 PHE HB3 H 3.087 0.006 . 127 28 28 PHE HD1 H 6.827 0.001 . 128 28 28 PHE HD2 H 6.827 0.001 . 129 28 28 PHE HE1 H 6.773 0.001 . 130 28 28 PHE HE2 H 6.773 0.001 . 131 29 29 TYR H H 8.282 0.016 . 132 29 29 TYR HA H 3.820 0.014 . 133 29 29 TYR HB2 H 3.131 0.007 . 134 29 29 TYR HB3 H 2.851 0.011 . 135 30 30 GLU H H 7.690 0.004 . 136 30 30 GLU HA H 3.571 0.016 . 137 30 30 GLU HB2 H 1.979 0.013 . 138 30 30 GLU HB3 H 2.003 0.000 . 139 30 30 GLU HG2 H 2.500 0.012 . 140 30 30 GLU HG3 H 2.292 0.000 . 141 31 31 CYS H H 8.820 0.019 . 142 31 31 CYS HA H 3.594 0.010 . 143 31 31 CYS HB2 H 2.957 0.014 . 144 31 31 CYS HB3 H 2.339 0.011 . 145 32 32 CYS H H 8.097 0.015 . 146 32 32 CYS HA H 3.855 0.011 . 147 32 32 CYS HB2 H 3.086 0.009 . 148 32 32 CYS HB3 H 2.511 0.007 . 149 33 33 THR H H 7.165 0.006 . 150 33 33 THR HA H 4.551 0.002 . 151 33 33 THR HB H 3.802 0.002 . 152 34 34 SER H H 8.339 0.008 . 153 34 34 SER HA H 4.902 0.005 . 154 34 34 SER HB2 H 4.003 0.011 . 155 34 34 SER HB3 H 3.839 0.005 . 156 35 35 GLU H H 9.263 0.020 . 157 35 35 GLU HA H 4.172 0.008 . 158 35 35 GLU HB2 H 2.140 0.002 . 159 35 35 GLU HB3 H 2.484 0.007 . 160 35 35 GLU HG2 H 2.491 0.001 . 161 35 35 GLU HG3 H 2.140 0.001 . 162 36 36 SER H H 8.468 0.015 . 163 36 36 SER HA H 3.859 0.007 . 164 36 36 SER HB2 H 4.176 0.000 . 165 36 36 SER HB3 H 4.176 0.000 . 166 37 37 THR H H 7.770 0.018 . 167 37 37 THR HA H 3.899 0.012 . 168 37 37 THR HB H 3.604 0.010 . 169 37 37 THR HG2 H 0.945 0.022 . 170 38 38 PHE H H 8.408 0.018 . 171 38 38 PHE HA H 4.614 0.008 . 172 38 38 PHE HB2 H 3.803 0.010 . 173 38 38 PHE HB3 H 2.941 0.011 . 174 39 39 LYS H H 8.595 0.012 . 175 39 39 LYS HA H 3.789 0.010 . 176 39 39 LYS HB2 H 1.869 0.006 . 177 39 39 LYS HB3 H 1.610 0.013 . 178 40 40 LYS H H 7.505 0.020 . 179 40 40 LYS HA H 4.050 0.009 . 180 40 40 LYS HB2 H 1.972 0.012 . 181 40 40 LYS HB3 H 1.655 0.010 . 182 41 41 CYS H H 8.204 0.019 . 183 41 41 CYS HA H 4.676 0.005 . 184 41 41 CYS HB2 H 3.858 0.014 . 185 41 41 CYS HB3 H 3.238 0.017 . 186 42 42 GLN H H 8.267 0.019 . 187 42 42 GLN HA H 3.727 0.015 . 188 42 42 GLN HB2 H 1.931 0.012 . 189 42 42 GLN HB3 H 1.811 0.012 . 190 42 42 GLN HG2 H 1.608 0.005 . 191 42 42 GLN HG3 H 1.608 0.005 . 192 43 43 THR H H 7.858 0.015 . 193 43 43 THR HA H 4.210 0.010 . 194 43 43 THR HB H 3.937 0.011 . 195 43 43 THR HG2 H 1.213 0.001 . 196 44 44 MET H H 8.002 0.020 . 197 44 44 MET HA H 4.160 0.008 . 198 44 44 MET HB2 H 2.381 0.011 . 199 44 44 MET HB3 H 2.231 0.013 . 200 44 44 MET HG2 H 2.808 0.001 . 201 44 44 MET HG3 H 2.808 0.001 . 202 45 45 LEU H H 7.721 0.021 . 203 45 45 LEU HA H 4.179 0.008 . 204 45 45 LEU HB2 H 1.687 0.007 . 205 45 45 LEU HB3 H 1.503 0.006 . 206 45 45 LEU HG H 1.924 0.006 . 207 45 45 LEU HD1 H 0.983 0.002 . 208 45 45 LEU HD2 H 0.714 0.003 . 209 46 46 HIS H H 7.709 0.004 . 210 46 46 HIS HA H 4.526 0.014 . 211 46 46 HIS HB2 H 3.362 0.017 . 212 46 46 HIS HB3 H 3.278 0.011 . 213 47 47 GLN H H 7.889 0.006 . 214 47 47 GLN HB2 H 2.108 0.003 . 215 47 47 GLN HB3 H 1.893 0.012 . 216 47 47 GLN HG2 H 2.325 0.010 . 217 47 47 GLN HG3 H 2.325 0.010 . stop_ save_