data_4755 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of HpTx2, a toxin from heteropoda venatoria spider that blocks Kv4.2 potassium channel ; _BMRB_accession_number 4755 _BMRB_flat_file_name bmr4755.str _Entry_type original _Submission_date 2000-06-08 _Accession_date 2000-06-08 _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 Bernard Cedric . . 2 Legros Christian . . 3 Ferrat Gilles . . 4 Bischoff Ulrike . . 5 Marquardt Annette . . 6 Pongs Olaf . . 7 Darbon Herve . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 144 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-15 original author . stop_ _Original_release_date 2001-02-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of hpTX2, a Toxin from Heteropoda venatoria Spider that blocks Kv4.2 Potassium Channel ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21025439 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bernard Cedric . . 2 Legros Christian . . 3 Ferrat Gilles . . 4 Bischoff Ulrike . . 5 Marquardt Annette . . 6 Pongs Olaf . . 7 Darbon Herve . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein Science' _Journal_volume 9 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2059 _Page_last 2067 _Year 2000 _Details . loop_ _Keyword heteropodatoxin NMR 'spider toxin' 'structure determination' 'voltage-dependant potassium channel' stop_ save_ ################################## # Molecular system description # ################################## save_system_HpTx2 _Saveframe_category molecular_system _Mol_system_name 'heteropoda toxin 2' _Abbreviation_common HpTx2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HpTx2 $HpTx2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HpTx2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HpTx2 _Abbreviation_common HpTx2 _Molecular_mass 3412.7 _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 30 _Mol_residue_sequence ; DDCGKLFSGCDTNADCCEGY VCRLWCKLDW ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 ASP 3 CYS 4 GLY 5 LYS 6 LEU 7 PHE 8 SER 9 GLY 10 CYS 11 ASP 12 THR 13 ASN 14 ALA 15 ASP 16 CYS 17 CYS 18 GLU 19 GLY 20 TYR 21 VAL 22 CYS 23 ARG 24 LEU 25 TRP 26 CYS 27 LYS 28 LEU 29 ASP 30 TRP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1EMX "Solution Structure Of Hptx2, A Toxin From Heteropoda Venatoria Spider Venom That Blocks Kv4.2 Potassium Channel" 100.00 30 100.00 100.00 1.17e-11 SP P58426 "RecName: Full=Kappa-sparatoxin-Hv1b; Short=Kappa-SPRTX-Hv1b; AltName: Full=Heteropodatoxin-2; Short=HpTX2; AltName: Full=Toxin " 100.00 30 100.00 100.00 1.17e-11 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HpTx2 'Giant crab spider' 152925 . . Heteropoda venatoria 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 $HpTx2 . . . . . . 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 $HpTx2 1.5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.5 . n/a temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 . H 1 . ppm 0 . . . . . $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_assignment_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name HpTx2 _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 ASP HA H 4.62 . 1 2 . 1 ASP HB2 H 3.13 . 1 3 . 1 ASP HB3 H 2.86 . 1 4 . 2 ASP H H 9.13 . 1 5 . 2 ASP HA H 4.90 . 1 6 . 2 ASP HB2 H 2.97 . 2 7 . 3 CYS H H 8.04 . 1 8 . 3 CYS HA H 5.08 . 1 9 . 3 CYS HB2 H 3.12 . 1 10 . 3 CYS HB3 H 2.88 . 1 11 . 4 GLY H H 8.62 . 1 12 . 4 GLY HA2 H 4.11 . 1 13 . 4 GLY HA3 H 3.95 . 1 14 . 5 LYS H H 7.81 . 1 15 . 5 LYS HA H 3.68 . 1 16 . 5 LYS HB2 H 1.76 . 1 17 . 5 LYS HB3 H 1.70 . 1 18 . 5 LYS HG2 H 1.58 . 2 19 . 5 LYS HD2 H 1.01 . 2 20 . 5 LYS HE2 H 3.03 . 2 21 . 5 LYS HZ H 7.53 . 1 22 . 6 LEU H H 7.18 . 1 23 . 6 LEU HA H 3.73 . 1 24 . 6 LEU HB2 H 1.36 . 2 25 . 6 LEU HG H 1.26 . 1 26 . 6 LEU HD1 H 0.82 . 2 27 . 6 LEU HD2 H 0.64 . 2 28 . 7 PHE H H 8.55 . 1 29 . 7 PHE HA H 4.01 . 1 30 . 7 PHE HB2 H 3.37 . 1 31 . 7 PHE HB3 H 3.12 . 1 32 . 7 PHE HD1 H 6.60 . 3 33 . 7 PHE HE1 H 7.21 . 3 34 . 8 SER H H 8.44 . 1 35 . 8 SER HA H 4.46 . 1 36 . 8 SER HB2 H 3.90 . 1 37 . 8 SER HB3 H 3.81 . 1 38 . 9 GLY H H 8.86 . 1 39 . 9 GLY HA2 H 4.27 . 1 40 . 9 GLY HA3 H 3.82 . 1 41 . 10 CYS H H 8.07 . 1 42 . 10 CYS HA H 4.89 . 1 43 . 10 CYS HB2 H 3.19 . 2 44 . 11 ASP H H 8.90 . 1 45 . 11 ASP HA H 4.83 . 1 46 . 11 ASP HB2 H 2.91 . 1 47 . 11 ASP HB3 H 2.82 . 1 48 . 12 THR H H 8.02 . 1 49 . 12 THR HA H 4.64 . 1 50 . 12 THR HB H 4.45 . 1 51 . 12 THR HG2 H 1.17 . 1 52 . 13 ASN H H 9.08 . 1 53 . 13 ASN HA H 4.17 . 1 54 . 13 ASN HB2 H 3.07 . 1 55 . 13 ASN HB3 H 2.90 . 1 56 . 13 ASN HD21 H 7.74 . 1 57 . 13 ASN HD22 H 7.11 . 1 58 . 14 ALA H H 7.97 . 1 59 . 14 ALA HA H 4.25 . 1 60 . 14 ALA HB H 1.38 . 1 61 . 15 ASP H H 7.66 . 1 62 . 15 ASP HA H 4.65 . 1 63 . 15 ASP HB2 H 3.12 . 1 64 . 15 ASP HB3 H 2.96 . 1 65 . 16 CYS H H 8.04 . 1 66 . 16 CYS HA H 5.08 . 1 67 . 16 CYS HB2 H 3.21 . 1 68 . 16 CYS HB3 H 2.69 . 1 69 . 17 CYS H H 9.51 . 1 70 . 17 CYS HA H 4.57 . 1 71 . 17 CYS HB2 H 3.41 . 1 72 . 17 CYS HB3 H 2.38 . 1 73 . 18 GLU H H 8.35 . 1 74 . 18 GLU HA H 4.15 . 1 75 . 18 GLU HB2 H 2.10 . 1 76 . 18 GLU HB3 H 1.20 . 1 77 . 18 GLU HG2 H 2.51 . 2 78 . 19 GLY H H 8.82 . 1 79 . 19 GLY HA2 H 4.14 . 1 80 . 19 GLY HA3 H 3.42 . 1 81 . 20 TYR H H 8.10 . 1 82 . 20 TYR HA H 5.18 . 1 83 . 20 TYR HB2 H 3.30 . 1 84 . 20 TYR HB3 H 2.71 . 1 85 . 20 TYR HD1 H 7.06 . 3 86 . 20 TYR HE1 H 6.70 . 3 87 . 21 VAL H H 9.28 . 1 88 . 21 VAL HA H 4.39 . 1 89 . 21 VAL HB H 1.93 . 1 90 . 21 VAL HG1 H 0.77 . 2 91 . 21 VAL HG2 H 0.67 . 2 92 . 22 CYS H H 8.81 . 1 93 . 22 CYS HA H 4.72 . 1 94 . 22 CYS HB2 H 2.75 . 2 95 . 23 ARG H H 8.10 . 1 96 . 23 ARG HA H 4.41 . 1 97 . 23 ARG HB2 H 1.87 . 2 98 . 23 ARG HG2 H 1.59 . 1 99 . 23 ARG HG3 H 1.48 . 1 100 . 23 ARG HD2 H 3.20 . 1 101 . 23 ARG HD3 H 2.99 . 1 102 . 23 ARG HH11 H 7.18 . 2 103 . 24 LEU H H 8.15 . 1 104 . 24 LEU HA H 3.81 . 1 105 . 24 LEU HB2 H 1.97 . 2 106 . 24 LEU HG H 1.30 . 1 107 . 24 LEU HD1 H 0.82 . 2 108 . 25 TRP H H 8.02 . 1 109 . 25 TRP HA H 5.32 . 1 110 . 25 TRP HB2 H 3.26 . 1 111 . 25 TRP HB3 H 2.76 . 1 112 . 25 TRP HD1 H 7.06 . 3 113 . 25 TRP HE1 H 10.35 . 1 114 . 25 TRP HE3 H 7.66 . 1 115 . 25 TRP HZ2 H 7.47 . 1 116 . 25 TRP HH2 H 7.20 . 1 117 . 26 CYS H H 9.01 . 1 118 . 26 CYS HA H 5.00 . 1 119 . 26 CYS HB2 H 3.21 . 1 120 . 26 CYS HB3 H 2.76 . 1 121 . 27 LYS H H 9.61 . 1 122 . 27 LYS HA H 4.75 . 1 123 . 27 LYS HB2 H 1.85 . 2 124 . 27 LYS HG3 H 1.70 . 2 125 . 27 LYS HD2 H 1.42 . 2 126 . 27 LYS HE2 H 2.77 . 2 127 . 28 LEU H H 8.22 . 1 128 . 28 LEU HA H 3.92 . 1 129 . 28 LEU HB2 H 1.37 . 2 130 . 28 LEU HG H 1.24 . 1 131 . 28 LEU HD1 H 0.66 . 2 132 . 28 LEU HD2 H 0.52 . 2 133 . 29 ASP H H 8.26 . 1 134 . 29 ASP HA H 4.52 . 1 135 . 29 ASP HB2 H 2.64 . 1 136 . 29 ASP HB3 H 2.52 . 1 137 . 30 TRP H H 7.58 . 1 138 . 30 TRP HA H 4.59 . 1 139 . 30 TRP HB2 H 3.25 . 2 140 . 30 TRP HD1 H 7.17 . 3 141 . 30 TRP HE1 H 10.06 . 1 142 . 30 TRP HE3 H 7.57 . 1 143 . 30 TRP HZ2 H 6.88 . 1 144 . 30 TRP HH2 H 7.29 . 1 stop_ save_