data_6389 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Acting on the Number of Molecular Contacts between Maurotoxin and Kv1.2 Channel Impacts Ligand Affinity ; _BMRB_accession_number 6389 _BMRB_flat_file_name bmr6389.str _Entry_type original _Submission_date 2004-11-15 _Accession_date 2004-11-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Solution structure of a butantoxin-maurotoxin chimera.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McBarek Sarrah . . 2 Chagot Benjamin . . 3 Andreotti Nicolas . . 4 Visan Violeta . . 5 Mansuelle Pascal . . 6 Grissmer Stephan . . 7 Marrakchi Mohamed . . 8 'El Ayeb' Mohamed . . 9 Sampieri Francois . . 10 Darbon Herve . . 11 Fajloun Ziad . . 12 'De Waard' Michel . . 13 Sabatier Jean-Marc . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 180 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-08-22 original BMRB . stop_ _Original_release_date 2004-11-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Increasing the Molecular Contacts between Maurotoxin and Kv1.2 Channel Augments Ligand Affinity ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15971207 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 M'Barek Sarrah . . 2 Chagot Benjamin . . 3 Andreotti Nicolas . . 4 Visan Violeta . . 5 Mansuelle Pascal . . 6 Grissmer Stephan . . 7 Marrakchi Mohamed . . 8 'El Ayeb' Mohamed . . 9 Sampieri Francois . . 10 Darbon Herve . . 11 Fajloun Ziad . . 12 'De Waard' Michel . . 13 Sabatier Jean-Marc . . stop_ _Journal_abbreviation Proteins _Journal_volume 60 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 401 _Page_last 411 _Year 2005 _Details . loop_ _Keyword Butantoxin 'K+ channels' Maurotoxin 'Scorpion toxin' 'molecular contacts' 'toxin affinity' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_BuTX-MTX _Saveframe_category molecular_system _Mol_system_name BuTX-MTX _Abbreviation_common BuTX-MTX _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BuTX-MTX $BuTX-MTX stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function toxin stop_ _Database_query_date . _Details 'Butantoxin maurotoxin chimera.' save_ ######################## # Monomeric polymers # ######################## save_BuTX-MTX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common BuTX-MTX _Abbreviation_common BuTX-MTX _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 41 _Mol_residue_sequence ; WCSTCLDLACTGSKDCYAPC RKQTGCPNAKCINKSCKCYG C ; loop_ _Residue_seq_code _Residue_label 1 TRP 2 CYS 3 SER 4 THR 5 CYS 6 LEU 7 ASP 8 LEU 9 ALA 10 CYS 11 THR 12 GLY 13 SER 14 LYS 15 ASP 16 CYS 17 TYR 18 ALA 19 PRO 20 CYS 21 ARG 22 LYS 23 GLN 24 THR 25 GLY 26 CYS 27 PRO 28 ASN 29 ALA 30 LYS 31 CYS 32 ILE 33 ASN 34 LYS 35 SER 36 CYS 37 LYS 38 CYS 39 TYR 40 GLY 41 CYS stop_ _Sequence_homology_query_date 2010-09-19 _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 1WT7 'Solution Structure Of Butx-Mtx: A Butantoxin-Maurotoxin Chimera' 100.00 41 100.00 100.00 1.75e-14 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BuTX-MTX scorpion 6887 Eukaryota Metazoa Tityus serrulatus 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 $BuTX-MTX '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 $BuTX-MTX . mM . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name xwinnmr _Version 2.1 loop_ _Vendor _Address _Electronic_address BRUKER . . 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_1H_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H COSY' _Sample_label $sample_1 save_ save_1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H TOCSY' _Sample_label $sample_1 save_ save_1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H NOESY' _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 0 pH temperature 290 0 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 water H 1 protons ppm 4.7 internal direct . . . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H COSY' '1H TOCSY' '1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name BuTX-MTX _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 TRP HA H 4.193 0.000 . 2 . 1 TRP HB2 H 3.220 0.000 . 3 . 1 TRP HD1 H 7.155 0.004 . 4 . 1 TRP HE1 H 10.135 0.000 . 5 . 2 CYS H H 8.230 0.051 . 6 . 2 CYS HA H 4.377 0.000 . 7 . 2 CYS HB2 H 2.975 0.000 . 8 . 2 CYS HB3 H 3.234 0.000 . 9 . 3 SER H H 8.692 0.000 . 10 . 3 SER HA H 3.937 0.001 . 11 . 3 SER HB2 H 3.613 0.002 . 12 . 3 SER HB3 H 3.800 0.001 . 13 . 4 THR H H 7.454 0.000 . 14 . 4 THR HA H 4.342 0.001 . 15 . 4 THR HB H 4.344 0.000 . 16 . 4 THR HG2 H 0.993 0.000 . 17 . 5 CYS H H 7.379 0.002 . 18 . 5 CYS HA H 4.494 0.002 . 19 . 5 CYS HB2 H 3.056 0.000 . 20 . 6 LEU H H 8.021 0.261 . 21 . 6 LEU HA H 4.162 0.000 . 22 . 6 LEU HB2 H 1.398 0.000 . 23 . 6 LEU HD1 H 0.687 0.000 . 24 . 6 LEU HD2 H 1.293 0.000 . 25 . 7 ASP H H 8.354 0.000 . 26 . 7 ASP HA H 4.472 0.000 . 27 . 7 ASP HB2 H 2.517 0.000 . 28 . 7 ASP HB3 H 2.714 0.000 . 29 . 8 LEU H H 8.041 0.000 . 30 . 8 LEU HA H 4.252 0.002 . 31 . 8 LEU HB2 H 1.313 0.000 . 32 . 8 LEU HD1 H 0.712 0.000 . 33 . 8 LEU HD2 H 1.410 0.000 . 34 . 9 ALA H H 8.025 0.001 . 35 . 9 ALA HA H 4.641 0.002 . 36 . 9 ALA HB H 1.251 0.001 . 37 . 10 CYS H H 7.710 0.002 . 38 . 10 CYS HA H 4.705 0.001 . 39 . 10 CYS HB2 H 2.826 0.002 . 40 . 10 CYS HB3 H 3.138 0.002 . 41 . 11 THR H H 9.004 0.002 . 42 . 11 THR HA H 4.275 0.001 . 43 . 11 THR HB H 4.086 0.001 . 44 . 11 THR HG2 H 1.033 0.002 . 45 . 12 GLY H H 7.716 0.000 . 46 . 12 GLY HA2 H 3.791 0.002 . 47 . 12 GLY HA3 H 4.309 0.002 . 48 . 13 SER H H 8.975 0.000 . 49 . 13 SER HA H 3.594 0.084 . 50 . 13 SER HB2 H 3.761 0.000 . 51 . 14 LYS H H 7.684 1.837 . 52 . 14 LYS HA H 2.827 0.004 . 53 . 14 LYS HB2 H 1.498 0.001 . 54 . 14 LYS HB3 H 1.580 0.002 . 55 . 14 LYS HG2 H 1.159 0.002 . 56 . 15 ASP H H 7.232 0.001 . 57 . 15 ASP HA H 4.191 0.000 . 58 . 15 ASP HB2 H 2.656 0.002 . 59 . 15 ASP HB3 H 2.789 0.002 . 60 . 16 CYS H H 7.661 0.001 . 61 . 16 CYS HA H 4.393 0.000 . 62 . 16 CYS HB2 H 2.530 0.000 . 63 . 16 CYS HB3 H 2.850 0.000 . 64 . 17 TYR H H 6.730 0.000 . 65 . 17 TYR HA H 4.817 0.000 . 66 . 17 TYR HB2 H 2.874 0.000 . 67 . 17 TYR HB3 H 3.068 0.001 . 68 . 17 TYR HD1 H 7.082 0.000 . 69 . 17 TYR HE1 H 6.683 0.000 . 70 . 18 ALA H H 8.980 0.001 . 71 . 18 ALA HA H 4.247 0.000 . 72 . 18 ALA HB H 1.336 0.003 . 73 . 19 PRO HA H 4.212 0.000 . 74 . 19 PRO HB2 H 1.610 0.000 . 75 . 19 PRO HB3 H 2.127 0.000 . 76 . 19 PRO HG2 H 1.977 0.000 . 77 . 19 PRO HG3 H 2.101 0.000 . 78 . 19 PRO HD2 H 3.507 0.001 . 79 . 20 CYS H H 8.116 0.001 . 80 . 20 CYS HA H 4.493 0.000 . 81 . 20 CYS HB2 H 2.884 0.000 . 82 . 20 CYS HB3 H 3.338 0.000 . 83 . 21 ARG H H 8.646 0.000 . 84 . 21 ARG HA H 3.428 0.002 . 85 . 21 ARG HB2 H 1.387 0.001 . 86 . 21 ARG HB3 H 1.795 0.000 . 87 . 21 ARG HG2 H 1.034 0.000 . 88 . 21 ARG HG3 H 1.247 0.000 . 89 . 21 ARG HD2 H 2.990 0.000 . 90 . 21 ARG HE H 7.211 0.000 . 91 . 22 LYS H H 7.841 0.044 . 92 . 22 LYS HA H 3.849 0.000 . 93 . 22 LYS HB2 H 1.748 0.003 . 94 . 22 LYS HB3 H 1.850 0.001 . 95 . 23 GLN H H 7.747 0.040 . 96 . 23 GLN HA H 4.046 0.000 . 97 . 23 GLN HB2 H 2.044 0.000 . 98 . 23 GLN HG2 H 2.195 0.005 . 99 . 23 GLN HG3 H 2.310 0.000 . 100 . 24 THR H H 8.189 0.035 . 101 . 24 THR HA H 4.580 0.000 . 102 . 24 THR HB H 4.229 0.000 . 103 . 24 THR HG2 H 0.988 0.000 . 104 . 25 GLY H H 8.089 0.001 . 105 . 25 GLY HA2 H 3.601 0.002 . 106 . 25 GLY HA3 H 4.560 0.001 . 107 . 26 CYS H H 8.149 0.001 . 108 . 26 CYS HA H 4.916 0.001 . 109 . 26 CYS HB2 H 1.941 0.001 . 110 . 26 CYS HB3 H 3.570 0.000 . 111 . 27 PRO HA H 4.381 0.003 . 112 . 27 PRO HB2 H 1.757 0.001 . 113 . 27 PRO HG2 H 1.596 0.001 . 114 . 27 PRO HD2 H 3.180 0.000 . 115 . 27 PRO HD3 H 3.628 0.001 . 116 . 28 ASN H H 7.071 0.001 . 117 . 28 ASN HA H 4.179 0.002 . 118 . 28 ASN HB2 H 2.622 0.000 . 119 . 28 ASN HB3 H 2.673 0.000 . 120 . 29 ALA H H 8.105 0.001 . 121 . 29 ALA HA H 5.234 0.002 . 122 . 29 ALA HB H 1.311 0.000 . 123 . 30 LYS H H 8.223 0.001 . 124 . 30 LYS HA H 4.526 0.000 . 125 . 30 LYS HB2 H 1.583 0.000 . 126 . 30 LYS HB3 H 1.683 0.001 . 127 . 30 LYS HG2 H 1.255 0.000 . 128 . 30 LYS HD2 H 1.431 0.000 . 129 . 31 CYS HB2 H 2.171 0.004 . 130 . 31 CYS HB3 H 2.649 0.002 . 131 . 32 ILE H H 8.676 0.000 . 132 . 32 ILE HA H 4.129 0.000 . 133 . 32 ILE HB H 1.554 0.000 . 134 . 32 ILE HG2 H 1.235 0.000 . 135 . 32 ILE HG12 H 0.799 0.000 . 136 . 32 ILE HD1 H 0.698 0.000 . 137 . 33 ASN H H 9.318 0.000 . 138 . 33 ASN HA H 4.165 0.000 . 139 . 33 ASN HB2 H 2.579 0.000 . 140 . 33 ASN HB3 H 2.893 0.000 . 141 . 34 LYS H H 8.356 0.000 . 142 . 34 LYS HA H 3.764 0.000 . 143 . 34 LYS HB2 H 2.003 0.000 . 144 . 34 LYS HB3 H 2.091 0.000 . 145 . 34 LYS HG2 H 1.209 0.000 . 146 . 34 LYS HE2 H 2.842 0.000 . 147 . 34 LYS HZ H 7.379 0.000 . 148 . 35 SER H H 7.666 0.003 . 149 . 35 SER HA H 5.162 0.002 . 150 . 35 SER HB2 H 3.521 0.000 . 151 . 35 SER HB3 H 3.617 0.000 . 152 . 36 CYS H H 8.697 0.000 . 153 . 36 CYS HA H 4.513 0.001 . 154 . 36 CYS HB2 H 2.365 0.000 . 155 . 36 CYS HB3 H 2.659 0.000 . 156 . 37 LYS H H 8.955 0.000 . 157 . 37 LYS HA H 4.375 0.000 . 158 . 37 LYS HB2 H 1.455 0.000 . 159 . 37 LYS HB3 H 1.552 0.000 . 160 . 37 LYS HD2 H 1.305 0.000 . 161 . 37 LYS HE2 H 2.490 0.000 . 162 . 37 LYS HE3 H 2.642 0.000 . 163 . 37 LYS HZ H 7.323 0.000 . 164 . 38 CYS H H 8.639 0.001 . 165 . 38 CYS HA H 4.680 0.290 . 166 . 38 CYS HB2 H 2.492 0.065 . 167 . 38 CYS HB3 H 3.330 0.329 . 168 . 39 TYR H H 8.104 0.000 . 169 . 39 TYR HA H 4.316 0.000 . 170 . 39 TYR HB2 H 2.291 0.001 . 171 . 39 TYR HB3 H 3.071 0.000 . 172 . 39 TYR HD1 H 6.815 0.002 . 173 . 39 TYR HE1 H 7.573 0.001 . 174 . 40 GLY H H 9.415 0.002 . 175 . 40 GLY HA2 H 3.696 0.000 . 176 . 40 GLY HA3 H 4.096 0.000 . 177 . 41 CYS H H 8.746 0.000 . 178 . 41 CYS HA H 4.362 0.000 . 179 . 41 CYS HB2 H 2.675 0.000 . 180 . 41 CYS HB3 H 3.047 0.000 . stop_ save_