data_4541 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the Potassium Channel Scorpion Toxin HsTX1 ; _BMRB_accession_number 4541 _BMRB_flat_file_name bmr4541.str _Entry_type original _Submission_date 1999-08-20 _Accession_date 1999-12-06 _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 Savarin P. . . 2 Romi-Lebrun R. . . 3 Zinn-Justin S. . . 4 Lebrun B. . . 5 Nakajima T. . . 6 Gilquin B. . . 7 Menez A. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 211 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'Updating non-standard residue' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: Solution structure of the potassium channel inhibitor HsTX1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20095844 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Savarin Philippe . . 2 Romi-Lebrun Regine . . 3 Zinn-Justin Sophie . . 4 Lebrun Bruno . . 5 Nakajima Terumi . . 6 Gilquin Bernard . . 7 Menez Andre . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 8 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2672 _Page_last 2685 _Year 1999 _Details . loop_ _Keyword 'Molecular Modeling' NMR 'Scorpion Toxin' 'Structure Determination' stop_ save_ ################################## # Molecular system description # ################################## save_system_HsTX1 _Saveframe_category molecular_system _Mol_system_name 'Potassium Channel Scorpion Toxin HsTX1' _Abbreviation_common HsTX1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HsTX1 $HsTX1 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_HsTX1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HsTX1 _Abbreviation_common HsTX1 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; ASCRTPKDCADPCRKETGCP YGKCMNRKCKCNRCX ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 SER 3 CYS 4 ARG 5 THR 6 PRO 7 LYS 8 ASP 9 CYS 10 ALA 11 ASP 12 PRO 13 CYS 14 ARG 15 LYS 16 GLU 17 THR 18 GLY 19 CYS 20 PRO 21 TYR 22 GLY 23 LYS 24 CYS 25 MET 26 ASN 27 ARG 28 LYS 29 CYS 30 LYS 31 CYS 32 ASN 33 ARG 34 CYS 35 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1QUZ "Solution Structure Of The Potassium Channel Scorpion Toxin Hstx1" 97.14 35 100.00 100.00 1.37e-13 PDB 1Y2P "Solution Structure Of Hstx3p" 97.14 34 100.00 100.00 1.35e-13 GB AFB73768 "Kv1.3 potassium channel blocker precursor, partial [Heterometrus laoticus]" 97.14 35 97.06 100.00 4.41e-13 SP P59867 "RecName: Full=Potassium channel toxin alpha-KTx 6.3; AltName: Full=Neurotoxin HsTX1" 97.14 34 100.00 100.00 1.35e-13 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jul 15 10:45:47 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 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 HN1 ? ? SING N HN2 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $HsTX1 . 6888 Eukaryota . Scorpionidae . 'scorpion name is Heterometrus spinnifer' 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 $HsTX1 'chemical synthesis' . . . . . 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 $HsTX1 3 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HsTX1 3 mM . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97 loop_ _Task 'data analysis' stop_ _Details . save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.1 loop_ _Task 'structure calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment_1 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_applied_experiment _Sample_label . save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name NMR_applied_experiment _BMRB_pulse_sequence_accession_number . _Details ; DQF-COSY 2D NOESY OFF-RESONANCE ROESY (35) TOCSY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.0 0.1 n/a pressure 1 . atm temperature 308 0.5 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_citation_label _Correction_value_citation_label TSP H 1 'methyl protons' ppm 0.00 internal direct spherical internal parallel $entry_citation $entry_citation 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_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name HsTX1 _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 ALA HA H 4.170 0.02 . 2 . 1 ALA HB H 1.49 0.02 . 3 . 2 SER H H 8.780 0.02 . 4 . 2 SER HA H 5.090 0.02 . 5 . 2 SER HB2 H 3.930 0.02 . 6 . 2 SER HB3 H 3.960 0.02 . 7 . 3 CYS H H 7.870 0.02 . 8 . 3 CYS HA H 4.760 0.02 . 9 . 3 CYS HB2 H 3.235 0.02 . 10 . 3 CYS HB3 H 3.050 0.02 . 11 . 4 ARG H H 9.610 0.02 . 12 . 4 ARG HA H 4.495 0.02 . 13 . 4 ARG HB2 H 1.920 0.02 . 14 . 4 ARG HB3 H 1.950 0.02 . 15 . 4 ARG HG2 H 1.680 0.02 . 16 . 4 ARG HG3 H 1.680 0.02 . 17 . 4 ARG HD2 H 3.240 0.02 . 18 . 4 ARG HD3 H 3.240 0.02 . 19 . 4 ARG HE H 7.310 0.02 . 20 . 5 THR H H 8.160 0.02 . 21 . 5 THR HA H 4.995 0.02 . 22 . 5 THR HB H 4.610 0.02 . 23 . 5 THR HG2 H 1.230 0.02 . 24 . 6 PRO HA H 4.01 0.02 . 25 . 6 PRO HB2 H 2.75 0.02 . 26 . 6 PRO HB3 H 2.04 0.02 . 27 . 6 PRO HG2 H 2.30 0.02 . 28 . 6 PRO HG3 H 2.30 0.02 . 29 . 6 PRO HD2 H 4.01 0.02 . 30 . 6 PRO HD3 H 4.01 0.02 . 31 . 7 LYS H H 7.830 0.02 . 32 . 7 LYS HA H 4.125 0.02 . 33 . 7 LYS HB2 H 1.825 0.02 . 34 . 7 LYS HB3 H 1.825 0.02 . 35 . 7 LYS HG2 H 1.520 0.02 . 36 . 7 LYS HG3 H 1.520 0.02 . 37 . 7 LYS HD2 H 1.705 0.02 . 38 . 7 LYS HD3 H 1.705 0.02 . 39 . 7 LYS HE2 H 3.000 0.02 . 40 . 7 LYS HE3 H 3.000 0.02 . 41 . 7 LYS HZ H 7.510 0.02 . 42 . 8 ASP H H 7.600 0.02 . 43 . 8 ASP HA H 4.490 0.02 . 44 . 8 ASP HB2 H 2.985 0.02 . 45 . 8 ASP HB3 H 2.985 0.02 . 46 . 9 CYS H H 7.737 0.02 . 47 . 9 CYS HA H 4.705 0.02 . 48 . 9 CYS HB2 H 3.280 0.02 . 49 . 9 CYS HB3 H 2.665 0.02 . 50 . 10 ALA H H 7.230 0.02 . 51 . 10 ALA HA H 3.845 0.02 . 52 . 10 ALA HB H 1.440 0.02 . 53 . 11 ASP H H 8.720 0.02 . 54 . 11 ASP HA H 4.640 0.02 . 55 . 11 ASP HB3 H 2.650 0.02 . 56 . 11 ASP HB2 H 2.740 0.02 . 57 . 12 PRO HA H 4.26 0.02 . 58 . 12 PRO HB2 H 2.26 0.02 . 59 . 12 PRO HB3 H 1.73 0.02 . 60 . 12 PRO HG2 H 2.25 0.02 . 61 . 12 PRO HG3 H 2.10 0.02 . 62 . 12 PRO HD2 H 3.65 0.02 . 63 . 12 PRO HD3 H 3.65 0.02 . 64 . 13 CYS H H 8.050 0.02 . 65 . 13 CYS HA H 4.880 0.02 . 66 . 13 CYS HB3 H 2.855 0.02 . 67 . 13 CYS HB2 H 3.375 0.02 . 68 . 14 ARG H H 8.365 0.02 . 69 . 14 ARG HA H 3.360 0.02 . 70 . 14 ARG HB2 H 2.000 0.02 . 71 . 14 ARG HB3 H 1.825 0.02 . 72 . 14 ARG HG2 H 1.460 0.02 . 73 . 14 ARG HG3 H 1.460 0.02 . 74 . 14 ARG HD2 H 3.190 0.02 . 75 . 14 ARG HD3 H 3.190 0.02 . 76 . 14 ARG HE H 7.290 0.02 . 77 . 15 LYS H H 7.545 0.02 . 78 . 15 LYS HA H 4.040 0.02 . 79 . 15 LYS HB2 H 1.965 0.02 . 80 . 15 LYS HB3 H 1.905 0.02 . 81 . 15 LYS HG2 H 1.530 0.02 . 82 . 15 LYS HG3 H 1.420 0.02 . 83 . 15 LYS HD2 H 1.660 0.02 . 84 . 15 LYS HD3 H 1.660 0.02 . 85 . 15 LYS HE2 H 2.970 0.02 . 86 . 15 LYS HE3 H 2.970 0.02 . 87 . 16 GLU H H 8.105 0.02 . 88 . 16 GLU HA H 4.225 0.02 . 89 . 16 GLU HB2 H 2.485 0.02 . 90 . 16 GLU HB3 H 2.485 0.02 . 91 . 16 GLU HG2 H 2.250 0.02 . 92 . 16 GLU HG3 H 2.250 0.02 . 93 . 17 THR H H 8.833 0.02 . 94 . 17 THR HA H 4.740 0.02 . 95 . 17 THR HB H 4.515 0.02 . 96 . 17 THR HG2 H 1.135 0.02 . 97 . 18 GLY H H 7.750 0.02 . 98 . 18 GLY HA3 H 4.465 0.02 . 99 . 18 GLY HA2 H 4.030 0.02 . 100 . 19 CYS H H 7.990 0.02 . 101 . 19 CYS HA H 5.195 0.02 . 102 . 19 CYS HB2 H 3.215 0.02 . 103 . 19 CYS HB3 H 3.030 0.02 . 104 . 20 PRO HA H 4.74 0.02 . 105 . 20 PRO HB2 H 1.51 0.02 . 106 . 20 PRO HB3 H 2.09 0.02 . 107 . 20 PRO HG2 H 1.86 0.02 . 108 . 20 PRO HG3 H 1.24 0.02 . 109 . 20 PRO HD2 H 3.54 0.02 . 110 . 20 PRO HD3 H 3.54 0.02 . 111 . 21 TYR H H 7.550 0.02 . 112 . 21 TYR HA H 4.745 0.02 . 113 . 21 TYR HB2 H 3.000 0.02 . 114 . 21 TYR HB3 H 2.680 0.02 . 115 . 21 TYR HD1 H 7.060 0.02 . 116 . 21 TYR HD2 H 7.060 0.02 . 117 . 21 TYR HE1 H 6.800 0.02 . 118 . 21 TYR HE2 H 6.800 0.02 . 119 . 22 GLY H H 8.290 0.02 . 120 . 22 GLY HA3 H 4.555 0.02 . 121 . 22 GLY HA2 H 3.810 0.02 . 122 . 23 LYS H H 8.205 0.02 . 123 . 23 LYS HA H 4.465 0.02 . 124 . 23 LYS HB2 H 1.800 0.02 . 125 . 23 LYS HB3 H 1.635 0.02 . 126 . 23 LYS HG2 H 1.450 0.02 . 127 . 23 LYS HG3 H 1.450 0.02 . 128 . 23 LYS HD2 H 1.715 0.02 . 129 . 23 LYS HD3 H 1.715 0.02 . 130 . 23 LYS HE2 H 3.020 0.02 . 131 . 23 LYS HE3 H 3.020 0.02 . 132 . 24 CYS H H 8.675 0.02 . 133 . 24 CYS HA H 4.965 0.02 . 134 . 24 CYS HB2 H 2.775 0.02 . 135 . 24 CYS HB3 H 2.145 0.02 . 136 . 25 MET H H 8.722 0.02 . 137 . 25 MET HA H 4.740 0.02 . 138 . 25 MET HB2 H 2.055 0.02 . 139 . 25 MET HB3 H 1.845 0.02 . 140 . 25 MET HG2 H 2.430 0.02 . 141 . 25 MET HG3 H 2.430 0.02 . 142 . 26 ASN H H 9.415 0.02 . 143 . 26 ASN HA H 4.320 0.02 . 144 . 26 ASN HB2 H 3.010 0.02 . 145 . 26 ASN HB3 H 2.715 0.02 . 146 . 26 ASN HD21 H 7.170 0.02 . 147 . 26 ASN HD22 H 7.600 0.02 . 148 . 27 ARG H H 8.470 0.02 . 149 . 27 ARG HA H 3.970 0.02 . 150 . 27 ARG HB2 H 2.270 0.02 . 151 . 27 ARG HB3 H 2.195 0.02 . 152 . 27 ARG HG2 H 1.630 0.02 . 153 . 27 ARG HG3 H 1.630 0.02 . 154 . 27 ARG HD2 H 3.290 0.02 . 155 . 27 ARG HD3 H 3.290 0.02 . 156 . 27 ARG HE H 7.110 0.02 . 157 . 27 ARG HH21 H 7.110 0.02 . 158 . 27 ARG HH22 H 7.110 0.02 . 159 . 28 LYS H H 7.726 0.02 . 160 . 28 LYS HA H 5.045 0.02 . 161 . 28 LYS HB2 H 1.790 0.02 . 162 . 28 LYS HB3 H 1.715 0.02 . 163 . 28 LYS HG2 H 1.435 0.02 . 164 . 28 LYS HG3 H 1.435 0.02 . 165 . 28 LYS HD2 H 1.710 0.02 . 166 . 28 LYS HD3 H 1.710 0.02 . 167 . 28 LYS HE2 H 3.019 0.02 . 168 . 28 LYS HE3 H 3.019 0.02 . 169 . 29 CYS H H 8.245 0.02 . 170 . 29 CYS HA H 4.975 0.02 . 171 . 29 CYS HB2 H 2.910 0.02 . 172 . 29 CYS HB3 H 2.500 0.02 . 173 . 30 LYS H H 9.445 0.02 . 174 . 30 LYS HA H 4.660 0.02 . 175 . 30 LYS HB2 H 1.850 0.02 . 176 . 30 LYS HB3 H 1.720 0.02 . 177 . 30 LYS HG2 H 1.415 0.02 . 178 . 30 LYS HG3 H 1.415 0.02 . 179 . 30 LYS HD2 H 1.720 0.02 . 180 . 30 LYS HD3 H 1.720 0.02 . 181 . 30 LYS HE2 H 3.010 0.02 . 182 . 30 LYS HE3 H 3.010 0.02 . 183 . 31 CYS H H 9.190 0.02 . 184 . 31 CYS HA H 4.955 0.02 . 185 . 31 CYS HB3 H 2.630 0.02 . 186 . 31 CYS HB2 H 3.350 0.02 . 187 . 32 ASN H H 8.750 0.02 . 188 . 32 ASN HA H 4.810 0.02 . 189 . 32 ASN HB2 H 2.870 0.02 . 190 . 32 ASN HB3 H 2.660 0.02 . 191 . 32 ASN HD21 H 7.530 0.02 . 192 . 32 ASN HD22 H 6.870 0.02 . 193 . 33 ARG H H 8.440 0.02 . 194 . 33 ARG HA H 4.465 0.02 . 195 . 33 ARG HB2 H 1.895 0.02 . 196 . 33 ARG HB3 H 1.760 0.02 . 197 . 33 ARG HG2 H 1.640 0.02 . 198 . 33 ARG HG3 H 1.640 0.02 . 199 . 33 ARG HD2 H 3.240 0.02 . 200 . 33 ARG HD3 H 3.240 0.02 . 201 . 33 ARG HE H 7.240 0.02 . 202 . 33 ARG HH11 H 6.912 0.02 . 203 . 33 ARG HH12 H 6.912 0.02 . 204 . 33 ARG HH21 H 6.682 0.02 . 205 . 33 ARG HH22 H 6.682 0.02 . 206 . 34 CYS H H 8.600 0.02 . 207 . 34 CYS HA H 4.825 0.02 . 208 . 34 CYS HB3 H 3.250 0.02 . 209 . 34 CYS HB2 H 3.315 0.02 . 210 . 35 NH2 HN1 H 6.97 0.02 . 211 . 35 NH2 HN2 H 7.92 0.02 . stop_ save_