data_4760 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural and Functional Differences of Two Toxins from the Scorpion Pandinus Imperator ; _BMRB_accession_number 4760 _BMRB_flat_file_name bmr4760.str _Entry_type original _Submission_date 2000-06-12 _Accession_date 2000-06-12 _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 Klenk K. C. . 2 Tenenholz T. C. . 3 Matteson D. R. . 4 Rogowski R. S. . 5 Blaustein M. P. . 6 Weber D. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 213 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-06-27 original author . stop_ _Original_release_date 2000-06-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural and Functional Differences of Two Toxins from the Scorpion Pandinus Imperator ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20178341 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Klenk K. C. . 2 Tenenholz T. C. . 3 Matteson D. R. . 4 Rogowski R. S. . 5 Blaustein M. P. . 6 Weber D. J. . stop_ _Journal_abbreviation 'Proteins: Struct., Funct., Genet.' _Journal_volume 38 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 441 _Page_last 449 _Year 2000 _Details . loop_ _Keyword 'SCORPION TOXIN' 'POTASSIUM CHANNELS BLOCKERS' 'ALPHA-K TOXIN FAMILY' NEUROTOXIN 'NMR SOLUTION STRUCTURE' stop_ save_ ################################## # Molecular system description # ################################## save_system_PiTX-Kb _Saveframe_category molecular_system _Mol_system_name 'Pandinotoxin K-beta' _Abbreviation_common PiTX-Kb _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Pandinotoxin K-beta' $PiTX-Kb 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_PiTX-Kb _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Pandinotoxin K-beta' _Abbreviation_common PiTX-Kb _Molecular_mass 4068 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; TISCTNEKQCYPHCKKETGY PNAKCMNRKCKCFGR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 4 THR 2 5 ILE 3 6 SER 4 7 CYS 5 8 THR 6 9 ASN 7 10 GLU 8 11 LYS 9 12 GLN 10 13 CYS 11 14 TYR 12 15 PRO 13 16 HIS 14 17 CYS 15 18 LYS 16 19 LYS 17 20 GLU 18 21 THR 19 22 GLY 20 23 TYR 21 24 PRO 22 25 ASN 23 26 ALA 24 27 LYS 25 28 CYS 26 29 MET 27 30 ASN 28 31 ARG 29 32 LYS 30 33 CYS 31 34 LYS 32 35 CYS 33 36 PHE 34 37 GLY 35 38 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1C49 "Structural And Functional Differences Of Two Toxins From The Scorpion Pandinus Imperator" 100.00 35 100.00 100.00 8.26e-16 PDB 2PTA "Pandinus Toxin K-A (Pitx-Ka) From Pandinus Imperator, Nmr, 20 Structures" 100.00 35 97.14 97.14 7.68e-15 GB AAB52576 "toxin K-alpha [Pandinus imperator]" 100.00 47 97.14 97.14 2.90e-15 SP P55927 "RecName: Full=Potassium channel toxin alpha-KTx 7.1; AltName: Full=Pandinotoxin-alpha; AltName: Full=Potassium channel-blocking" 100.00 47 97.14 97.14 2.90e-15 SP P55928 "RecName: Full=Potassium channel toxin alpha-KTx 7.2; AltName: Full=Pandinotoxin-beta; AltName: Full=Potassium channel-blocking " 100.00 35 100.00 100.00 8.26e-16 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PiTX-Kb 'emperor scorpion' 55084 Eukaryota Metazoa Pandinus imperator 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 $PiTX-Kb 'recombinant technology' Bacteria Escherichia coli 'BL21 (DE3)' PSR9 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 $PiTX-Kb 4.36 mM . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.1 loop_ _Task 'REFINEMENT, STRUCTURE SOLUTION' stop_ _Details BRUNGER save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_ROESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label . save_ save_P.E.COSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name P.E.COSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name P.E.COSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.50 0.05 n/a temperature 310.00 0.05 K 'ionic strength' 1.44 . mM pressure 1 . atm 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 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 'Pandinotoxin K-beta' _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 THR HA H 4.13 0.02 1 2 . 1 THR HB H 3.93 0.02 1 3 . 1 THR HG2 H 1.28 0.02 1 4 . 2 ILE H H 8.54 0.02 1 5 . 2 ILE HA H 4.30 0.02 1 6 . 2 ILE HB H 1.62 0.02 1 7 . 2 ILE HG12 H 1.07 0.02 2 8 . 2 ILE HG13 H 0.81 0.02 2 9 . 2 ILE HG2 H 0.65 0.02 1 10 . 2 ILE HD1 H 0.61 0.02 1 11 . 3 SER H H 8.29 0.02 1 12 . 3 SER HA H 5.00 0.02 1 13 . 3 SER HB2 H 3.88 0.02 2 14 . 3 SER HB3 H 3.82 0.02 2 15 . 4 CYS H H 7.89 0.02 1 16 . 4 CYS HA H 4.85 0.02 1 17 . 4 CYS HB2 H 2.87 0.02 1 18 . 4 CYS HB3 H 3.33 0.02 1 19 . 5 THR H H 9.34 0.02 1 20 . 5 THR HA H 4.38 0.02 1 21 . 5 THR HB H 4.30 0.02 1 22 . 5 THR HG2 H 1.16 0.02 1 23 . 6 ASN H H 7.86 0.02 1 24 . 6 ASN HA H 4.79 0.02 1 25 . 6 ASN HB2 H 2.87 0.02 2 26 . 6 ASN HB3 H 2.75 0.02 2 27 . 6 ASN HD21 H 7.49 0.02 2 28 . 6 ASN HD22 H 6.77 0.02 2 29 . 7 GLU H H 9.02 0.02 1 30 . 7 GLU HA H 3.69 0.02 1 31 . 7 GLU HB2 H 2.13 0.02 1 32 . 7 GLU HB3 H 2.13 0.02 1 33 . 7 GLU HG2 H 2.34 0.02 2 34 . 7 GLU HG3 H 2.24 0.02 2 35 . 8 LYS H H 8.03 0.02 1 36 . 8 LYS HA H 2.65 0.02 1 37 . 8 LYS HB2 H 1.60 0.02 1 38 . 8 LYS HB3 H 1.66 0.02 1 39 . 8 LYS HG2 H 1.32 0.02 1 40 . 8 LYS HG3 H 1.32 0.02 1 41 . 8 LYS HD2 H 1.38 0.02 1 42 . 8 LYS HD3 H 1.38 0.02 1 43 . 9 GLN H H 7.34 0.02 1 44 . 9 GLN HA H 4.02 0.02 1 45 . 9 GLN HB2 H 2.25 0.02 1 46 . 9 GLN HB3 H 2.12 0.02 1 47 . 9 GLN HG2 H 2.49 0.02 2 48 . 9 GLN HG3 H 2.41 0.02 2 49 . 9 GLN HE21 H 6.76 0.02 2 50 . 9 GLN HE22 H 7.44 0.02 2 51 . 10 CYS H H 7.73 0.02 1 52 . 10 CYS HA H 4.57 0.02 1 53 . 10 CYS HB2 H 3.00 0.02 1 54 . 10 CYS HB3 H 3.00 0.02 1 55 . 11 TYR H H 7.28 0.02 1 56 . 11 TYR HA H 5.10 0.02 1 57 . 11 TYR HB2 H 3.38 0.02 1 58 . 11 TYR HB3 H 3.20 0.02 1 59 . 11 TYR HD1 H 7.19 0.02 1 60 . 11 TYR HD2 H 7.19 0.02 1 61 . 11 TYR HE1 H 6.84 0.02 1 62 . 11 TYR HE2 H 6.84 0.02 1 63 . 12 PRO HA H 4.30 0.02 1 64 . 12 PRO HB2 H 2.34 0.02 2 65 . 12 PRO HB3 H 1.85 0.02 2 66 . 12 PRO HG2 H 2.06 0.02 1 67 . 12 PRO HG3 H 2.06 0.02 1 68 . 12 PRO HD2 H 3.86 0.02 2 69 . 12 PRO HD3 H 3.77 0.02 2 70 . 13 HIS H H 7.76 0.02 1 71 . 13 HIS HA H 4.39 0.02 1 72 . 13 HIS HB2 H 3.40 0.02 2 73 . 13 HIS HB3 H 3.27 0.02 2 74 . 13 HIS HD1 H 7.12 0.02 2 75 . 13 HIS HE2 H 8.68 0.02 2 76 . 14 CYS H H 8.69 0.02 1 77 . 14 CYS HA H 4.60 0.02 1 78 . 14 CYS HB2 H 2.90 0.02 1 79 . 14 CYS HB3 H 3.49 0.02 1 80 . 15 LYS H H 8.88 0.02 1 81 . 15 LYS HA H 3.58 0.02 1 82 . 15 LYS HB2 H 1.87 0.02 2 83 . 15 LYS HB3 H 1.45 0.02 2 84 . 15 LYS HG2 H 1.01 0.02 1 85 . 15 LYS HG3 H 1.01 0.02 1 86 . 15 LYS HD2 H 1.23 0.02 1 87 . 15 LYS HD3 H 1.23 0.02 1 88 . 15 LYS HE2 H 2.84 0.02 1 89 . 15 LYS HE3 H 2.84 0.02 1 90 . 16 LYS H H 7.61 0.02 1 91 . 16 LYS HA H 3.99 0.02 1 92 . 16 LYS HB2 H 1.93 0.02 2 93 . 16 LYS HB3 H 1.90 0.02 2 94 . 16 LYS HG2 H 1.48 0.02 2 95 . 16 LYS HG3 H 1.41 0.02 2 96 . 16 LYS HD2 H 1.68 0.02 1 97 . 16 LYS HD3 H 1.68 0.02 1 98 . 16 LYS HE2 H 2.97 0.02 1 99 . 16 LYS HE3 H 2.97 0.02 1 100 . 17 GLU H H 7.94 0.02 1 101 . 17 GLU HA H 4.19 0.02 1 102 . 17 GLU HB2 H 2.14 0.02 2 103 . 17 GLU HB3 H 1.97 0.02 2 104 . 17 GLU HG2 H 2.32 0.02 2 105 . 17 GLU HG3 H 2.25 0.02 2 106 . 18 THR H H 8.40 0.02 1 107 . 18 THR HA H 4.78 0.02 1 108 . 18 THR HB H 4.50 0.02 1 109 . 18 THR HG2 H 1.24 0.02 1 110 . 19 GLY H H 7.92 0.02 1 111 . 19 GLY HA2 H 3.56 0.02 2 112 . 19 GLY HA3 H 4.24 0.02 2 113 . 20 TYR H H 8.25 0.02 1 114 . 20 TYR HA H 4.80 0.02 1 115 . 20 TYR HB2 H 2.41 0.02 1 116 . 20 TYR HB3 H 3.02 0.02 1 117 . 20 TYR HD1 H 6.97 0.02 1 118 . 20 TYR HD2 H 6.97 0.02 1 119 . 20 TYR HE1 H 6.82 0.02 1 120 . 20 TYR HE2 H 6.82 0.02 1 121 . 21 PRO HA H 4.35 0.02 1 122 . 21 PRO HB2 H 1.86 0.02 2 123 . 21 PRO HB3 H 1.56 0.02 2 124 . 21 PRO HG2 H 1.91 0.02 2 125 . 21 PRO HG3 H 1.79 0.02 2 126 . 21 PRO HD2 H 3.45 0.02 2 127 . 21 PRO HD3 H 3.88 0.02 2 128 . 22 ASN H H 7.02 0.02 1 129 . 22 ASN HA H 4.20 0.02 1 130 . 22 ASN HB2 H 2.71 0.02 2 131 . 22 ASN HB3 H 2.67 0.02 2 132 . 22 ASN HD21 H 7.74 0.02 2 133 . 22 ASN HD22 H 6.78 0.02 2 134 . 23 ALA H H 8.17 0.02 1 135 . 23 ALA HA H 5.38 0.02 1 136 . 23 ALA HB H 1.54 0.02 1 137 . 24 LYS H H 8.44 0.02 1 138 . 24 LYS HA H 4.64 0.02 1 139 . 24 LYS HB2 H 1.76 0.02 2 140 . 24 LYS HB3 H 1.66 0.02 2 141 . 24 LYS HG2 H 1.46 0.02 2 142 . 24 LYS HG3 H 1.39 0.02 2 143 . 24 LYS HD2 H 1.81 0.02 1 144 . 24 LYS HD3 H 1.81 0.02 1 145 . 25 CYS H H 9.07 0.02 1 146 . 25 CYS HA H 4.98 0.02 1 147 . 25 CYS HB2 H 2.85 0.02 2 148 . 25 CYS HB3 H 2.24 0.02 2 149 . 26 MET H H 8.78 0.02 1 150 . 26 MET HA H 4.75 0.02 1 151 . 26 MET HB2 H 2.06 0.02 2 152 . 26 MET HB3 H 1.80 0.02 2 153 . 26 MET HG2 H 2.44 0.02 1 154 . 26 MET HG3 H 2.44 0.02 1 155 . 27 ASN H H 9.46 0.02 1 156 . 27 ASN HA H 4.31 0.02 1 157 . 27 ASN HB2 H 2.71 0.02 2 158 . 27 ASN HB3 H 2.99 0.02 2 159 . 27 ASN HD21 H 7.51 0.02 2 160 . 27 ASN HD22 H 6.86 0.02 2 161 . 28 ARG H H 8.49 0.02 1 162 . 28 ARG HA H 4.07 0.02 1 163 . 28 ARG HB2 H 2.13 0.02 1 164 . 28 ARG HB3 H 2.24 0.02 1 165 . 28 ARG HG2 H 1.58 0.02 1 166 . 28 ARG HG3 H 1.58 0.02 1 167 . 28 ARG HD2 H 3.20 0.02 1 168 . 28 ARG HD3 H 3.20 0.02 1 169 . 28 ARG HE H 7.06 0.02 2 170 . 29 LYS H H 7.65 0.02 1 171 . 29 LYS HA H 5.02 0.02 1 172 . 29 LYS HB2 H 1.70 0.02 1 173 . 29 LYS HB3 H 1.70 0.02 1 174 . 29 LYS HG2 H 1.43 0.02 2 175 . 29 LYS HG3 H 1.34 0.02 2 176 . 29 LYS HD2 H 1.57 0.02 1 177 . 29 LYS HD3 H 1.57 0.02 1 178 . 30 CYS H H 8.53 0.02 1 179 . 30 CYS HA H 4.83 0.02 1 180 . 30 CYS HB2 H 2.80 0.02 1 181 . 30 CYS HB3 H 2.59 0.02 1 182 . 31 LYS H H 9.18 0.02 1 183 . 31 LYS HA H 4.58 0.02 1 184 . 31 LYS HB2 H 1.75 0.02 2 185 . 31 LYS HB3 H 1.66 0.02 2 186 . 31 LYS HG2 H 1.16 0.02 2 187 . 31 LYS HG3 H 1.09 0.02 2 188 . 31 LYS HD2 H 1.56 0.02 1 189 . 31 LYS HD3 H 1.56 0.02 1 190 . 32 CYS H H 8.79 0.02 1 191 . 32 CYS HA H 5.16 0.02 1 192 . 32 CYS HB2 H 3.69 0.02 1 193 . 32 CYS HB3 H 2.67 0.02 1 194 . 33 PHE H H 8.14 0.02 1 195 . 33 PHE HA H 4.54 0.02 1 196 . 33 PHE HB2 H 2.64 0.02 1 197 . 33 PHE HB3 H 3.17 0.02 1 198 . 33 PHE HD1 H 7.14 0.02 1 199 . 33 PHE HD2 H 7.14 0.02 1 200 . 33 PHE HE1 H 7.22 0.02 1 201 . 33 PHE HE2 H 7.22 0.02 1 202 . 34 GLY H H 9.48 0.02 1 203 . 34 GLY HA2 H 3.97 0.02 2 204 . 34 GLY HA3 H 3.66 0.02 2 205 . 35 ARG H H 7.58 0.02 1 206 . 35 ARG HA H 3.27 0.02 1 207 . 35 ARG HB2 H 1.46 0.02 2 208 . 35 ARG HB3 H 1.24 0.02 2 209 . 35 ARG HG2 H 1.32 0.02 1 210 . 35 ARG HG3 H 1.32 0.02 1 211 . 35 ARG HD2 H 3.00 0.02 1 212 . 35 ARG HD3 H 3.00 0.02 1 213 . 35 ARG HE H 7.01 0.02 2 stop_ save_