data_6370 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H assignment of APETx1 ; _BMRB_accession_number 6370 _BMRB_flat_file_name bmr6370.str _Entry_type original _Submission_date 2004-10-28 _Accession_date 2004-10-28 _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 Chagot B. . . 2 Diochot S. . . 3 Pimentel C. . . 4 Lazdunski M. . . 5 Darbon H. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 200 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-11-14 original BMRB . stop_ _Original_release_date 2004-10-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15726634 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chagot B. . . 2 Diochot S. . . 3 Pimentel C. . . 4 Lazdunski M. . . 5 Darbon H. . . stop_ _Journal_abbreviation Proteins _Journal_volume 59 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 380 _Page_last 386 _Year 2005 _Details . loop_ _Keyword APETx1 'Anthopleura elegantissima' HERG NMR 'potassium channel inhibitor' 'sea anemone toxin' 'structure determination' stop_ save_ ################################## # Molecular system description # ################################## save_system_APETx1 _Saveframe_category molecular_system _Mol_system_name 'Toxin APETx1' _Abbreviation_common APETx1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Toxin APETx1' $APETx1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_APETx1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Anthoplura elegantissima Toxin 1' _Abbreviation_common APETx1 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 42 _Mol_residue_sequence ; GTTCYCGKTIGIYWFGTKTC PSNRGYTGSCGYFLGICCYP VD ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 THR 3 THR 4 CYS 5 TYR 6 CYS 7 GLY 8 LYS 9 THR 10 ILE 11 GLY 12 ILE 13 TYR 14 TRP 15 PHE 16 GLY 17 THR 18 LYS 19 THR 20 CYS 21 PRO 22 SER 23 ASN 24 ARG 25 GLY 26 TYR 27 THR 28 GLY 29 SER 30 CYS 31 GLY 32 TYR 33 PHE 34 LEU 35 GLY 36 ILE 37 CYS 38 CYS 39 TYR 40 PRO 41 VAL 42 ASP stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1WQK 'Solution Structure Of Apetx1, A Specific Peptide Inhibitor Of Human Ether-A-Go-Go-Related Gene Potassium Channels From The Ven' 100.00 42 100.00 100.00 3.84e-15 SWISS-PROT P61541 'Toxin APETx1' 100.00 42 100.00 100.00 3.84e-15 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $APETx1 'Clonal anemone' 6110 Eukaryota Metazoa Anthopleura elegantissima 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 $APETx1 'purified from the natural source' . . . . . 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 $APETx1 . mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.1 loop_ _Task refinement stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version 1.2 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label $sample_1 save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3 . n/a temperature 280 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H2O H 1 protons ppm . internal indirect spherical internal parallel 1.0 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label COSY TOCSY NOESY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Toxin APETx1' _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 . 2 THR H H 8.663 0.000 . 2 . 2 THR HA H 4.241 0.000 . 3 . 2 THR HB H 4.022 0.005 . 4 . 2 THR HG2 H 0.973 0.002 . 5 . 3 THR H H 8.149 0.000 . 6 . 3 THR HA H 4.274 0.001 . 7 . 3 THR HB H 3.786 0.000 . 8 . 3 THR HG2 H 0.881 0.002 . 9 . 4 CYS H H 7.637 0.000 . 10 . 4 CYS HA H 4.162 0.000 . 11 . 4 CYS HB2 H 1.251 0.001 . 12 . 4 CYS HB3 H 2.048 0.000 . 13 . 5 TYR H H 6.738 0.000 . 14 . 5 TYR HA H 4.804 0.000 . 15 . 5 TYR HB2 H 2.350 0.001 . 16 . 5 TYR HB3 H 2.675 0.000 . 17 . 5 TYR HD1 H 6.556 0.003 . 18 . 5 TYR HE1 H 6.391 0.001 . 19 . 6 CYS H H 8.452 0.000 . 20 . 6 CYS HA H 4.722 0.000 . 21 . 6 CYS HB2 H 1.952 0.002 . 22 . 6 CYS HB3 H 3.023 0.001 . 23 . 7 GLY H H 8.799 0.000 . 24 . 7 GLY HA2 H 3.351 0.000 . 25 . 7 GLY HA3 H 3.766 0.000 . 26 . 8 LYS H H 8.666 0.000 . 27 . 8 LYS HA H 4.062 0.001 . 28 . 8 LYS HB2 H 1.445 0.000 . 29 . 8 LYS HB3 H 1.742 0.000 . 30 . 8 LYS HG2 H 1.133 0.000 . 31 . 8 LYS HG3 H 1.180 0.000 . 32 . 8 LYS HD2 H 1.366 0.000 . 33 . 8 LYS HE2 H 2.698 0.000 . 34 . 8 LYS HZ H 7.283 0.000 . 35 . 9 THR H H 7.820 0.000 . 36 . 9 THR HA H 3.766 0.005 . 37 . 9 THR HB H 3.365 0.000 . 38 . 9 THR HG2 H 0.274 0.001 . 39 . 10 ILE H H 8.091 0.000 . 40 . 10 ILE HA H 3.511 0.002 . 41 . 10 ILE HB H 1.304 0.000 . 42 . 10 ILE HG2 H 0.625 0.002 . 43 . 10 ILE HG12 H 0.800 0.005 . 44 . 10 ILE HD1 H 0.967 0.007 . 45 . 11 GLY H H 8.011 0.000 . 46 . 11 GLY HA2 H 3.185 0.002 . 47 . 11 GLY HA3 H 4.334 0.006 . 48 . 12 ILE H H 8.858 0.000 . 49 . 12 ILE HA H 4.476 0.001 . 50 . 12 ILE HB H 1.589 0.003 . 51 . 12 ILE HG2 H 0.966 0.003 . 52 . 12 ILE HG12 H 1.378 0.001 . 53 . 12 ILE HD1 H 0.571 0.006 . 54 . 13 TYR H H 8.065 0.001 . 55 . 13 TYR HA H 4.846 0.000 . 56 . 13 TYR HB2 H 2.105 0.000 . 57 . 13 TYR HB3 H 2.319 0.000 . 58 . 13 TYR HD1 H 6.740 0.000 . 59 . 13 TYR HE1 H 6.788 0.001 . 60 . 14 TRP H H 8.834 0.000 . 61 . 14 TRP HA H 4.038 0.000 . 62 . 14 TRP HB2 H 2.487 0.000 . 63 . 14 TRP HB3 H 2.748 0.000 . 64 . 14 TRP HD1 H 6.629 0.001 . 65 . 14 TRP HE3 H 7.561 0.000 . 66 . 14 TRP HE1 H 9.074 0.000 . 67 . 14 TRP HZ2 H 7.373 0.005 . 68 . 14 TRP HH2 H 6.429 0.001 . 69 . 15 PHE H H 7.993 0.000 . 70 . 15 PHE HA H 3.868 0.001 . 71 . 15 PHE HB2 H 2.476 0.000 . 72 . 15 PHE HB3 H 2.852 0.000 . 73 . 15 PHE HD1 H 7.014 0.001 . 74 . 15 PHE HE1 H 7.144 0.000 . 75 . 16 GLY H H 7.967 0.000 . 76 . 16 GLY HA2 H 3.032 0.000 . 77 . 16 GLY HA3 H 3.113 0.000 . 78 . 17 THR H H 6.859 0.002 . 79 . 17 THR HA H 4.383 0.001 . 80 . 17 THR HB H 3.759 0.000 . 81 . 17 THR HG2 H 0.750 0.003 . 82 . 18 LYS H H 8.044 0.000 . 83 . 18 LYS HA H 4.135 0.002 . 84 . 18 LYS HB2 H 1.386 0.005 . 85 . 18 LYS HB3 H 1.688 0.000 . 86 . 18 LYS HD2 H 1.069 0.000 . 87 . 18 LYS HD3 H 1.157 0.000 . 88 . 18 LYS HE2 H 2.672 0.000 . 89 . 18 LYS HZ H 7.330 0.000 . 90 . 19 THR H H 7.610 0.000 . 91 . 19 THR HA H 4.061 0.001 . 92 . 19 THR HB H 3.486 0.000 . 93 . 19 THR HG2 H 0.782 0.000 . 94 . 20 CYS H H 8.665 0.001 . 95 . 20 CYS HA H 3.713 0.003 . 96 . 20 CYS HB2 H 2.433 0.000 . 97 . 20 CYS HB3 H 2.531 0.000 . 98 . 21 PRO HA H 3.871 0.000 . 99 . 21 PRO HB2 H 1.132 0.003 . 100 . 21 PRO HB3 H 1.738 0.000 . 101 . 21 PRO HG2 H 0.045 0.001 . 102 . 21 PRO HG3 H 0.564 0.005 . 103 . 21 PRO HD2 H 2.308 0.003 . 104 . 21 PRO HD3 H 2.513 0.002 . 105 . 22 SER H H 8.158 0.000 . 106 . 22 SER HA H 4.016 0.000 . 107 . 22 SER HB2 H 3.572 0.001 . 108 . 23 ASN H H 8.624 0.000 . 109 . 23 ASN HA H 4.195 0.001 . 110 . 23 ASN HB2 H 2.595 0.003 . 111 . 23 ASN HB3 H 2.671 0.004 . 112 . 23 ASN HD21 H 6.926 0.000 . 113 . 23 ASN HD22 H 6.430 0.000 . 114 . 24 ARG H H 8.458 0.001 . 115 . 24 ARG HA H 4.112 0.000 . 116 . 24 ARG HB2 H 1.116 0.001 . 117 . 24 ARG HB3 H 1.204 0.001 . 118 . 24 ARG HG2 H 0.378 0.000 . 119 . 24 ARG HD2 H 2.767 0.001 . 120 . 24 ARG HD3 H 2.972 0.001 . 121 . 24 ARG HE H 7.231 0.000 . 122 . 25 GLY H H 8.172 0.004 . 123 . 25 GLY HA2 H 3.243 0.000 . 124 . 25 GLY HA3 H 3.644 0.000 . 125 . 26 TYR H H 7.284 0.000 . 126 . 26 TYR HA H 4.489 0.000 . 127 . 26 TYR HB2 H 2.450 0.000 . 128 . 26 TYR HB3 H 2.875 0.000 . 129 . 26 TYR HD1 H 6.918 0.000 . 130 . 27 THR H H 9.558 0.000 . 131 . 27 THR HA H 4.284 0.000 . 132 . 27 THR HG2 H 0.950 0.000 . 133 . 28 GLY H H 7.456 0.000 . 134 . 28 GLY HA2 H 3.020 0.000 . 135 . 28 GLY HA3 H 3.855 0.002 . 136 . 29 SER H H 7.762 0.000 . 137 . 29 SER HA H 5.200 0.000 . 138 . 29 SER HB2 H 3.355 0.001 . 139 . 29 SER HB3 H 3.820 0.001 . 140 . 30 CYS H H 8.695 0.000 . 141 . 30 CYS HA H 4.891 0.000 . 142 . 30 CYS HB2 H 3.157 0.000 . 143 . 30 CYS HB3 H 3.235 0.000 . 144 . 31 GLY H H 8.673 0.000 . 145 . 31 GLY HA2 H 3.608 0.000 . 146 . 31 GLY HA3 H 3.935 0.000 . 147 . 32 TYR H H 7.732 0.000 . 148 . 32 TYR HA H 4.241 0.000 . 149 . 32 TYR HB2 H 2.512 0.000 . 150 . 32 TYR HB3 H 2.691 0.000 . 151 . 32 TYR HD1 H 6.872 0.002 . 152 . 32 TYR HE1 H 6.507 0.001 . 153 . 33 PHE H H 8.414 0.000 . 154 . 33 PHE HA H 3.904 0.000 . 155 . 33 PHE HB2 H 2.581 0.000 . 156 . 33 PHE HB3 H 2.719 0.001 . 157 . 33 PHE HD1 H 6.661 0.000 . 158 . 33 PHE HE1 H 7.022 0.000 . 159 . 34 LEU H H 7.828 0.000 . 160 . 34 LEU HB2 H 1.594 0.000 . 161 . 34 LEU HD1 H 0.488 0.000 . 162 . 34 LEU HD2 H 0.640 0.000 . 163 . 35 GLY H H 8.480 0.000 . 164 . 35 GLY HA2 H 4.152 0.000 . 165 . 35 GLY HA3 H 4.232 0.000 . 166 . 36 ILE H H 8.535 0.000 . 167 . 36 ILE HA H 4.864 0.000 . 168 . 36 ILE HB H 1.492 0.002 . 169 . 36 ILE HG2 H 0.600 0.004 . 170 . 36 ILE HG12 H 0.846 0.004 . 171 . 36 ILE HG13 H 1.189 0.002 . 172 . 36 ILE HD1 H 0.323 0.002 . 173 . 37 CYS H H 9.007 0.000 . 174 . 37 CYS HA H 5.038 0.000 . 175 . 37 CYS HB2 H 2.014 0.000 . 176 . 37 CYS HB3 H 3.242 0.000 . 177 . 38 CYS H H 8.571 0.001 . 178 . 38 CYS HA H 4.408 0.002 . 179 . 38 CYS HB2 H 1.063 0.000 . 180 . 38 CYS HB3 H 1.869 0.003 . 181 . 39 TYR H H 7.716 0.000 . 182 . 39 TYR HA H 4.777 0.001 . 183 . 39 TYR HB2 H 2.288 0.000 . 184 . 39 TYR HB3 H 2.830 0.002 . 185 . 39 TYR HD1 H 6.312 0.001 . 186 . 39 TYR HE1 H 6.363 0.001 . 187 . 40 PRO HA H 4.930 0.003 . 188 . 40 PRO HB2 H 2.069 0.000 . 189 . 40 PRO HB3 H 2.399 0.000 . 190 . 40 PRO HG2 H 1.722 0.000 . 191 . 40 PRO HG3 H 1.831 0.001 . 192 . 40 PRO HD2 H 3.934 0.000 . 193 . 41 VAL H H 8.266 0.000 . 194 . 41 VAL HA H 3.812 0.001 . 195 . 41 VAL HB H 1.850 0.000 . 196 . 41 VAL HG1 H 0.707 0.001 . 197 . 41 VAL HG2 H 0.760 0.000 . 198 . 42 ASP H H 8.034 0.000 . 199 . 42 ASP HA H 4.377 0.000 . 200 . 42 ASP HB2 H 2.610 0.000 . stop_ save_