data_19519 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR solution structure of the GS-TAMAPIN MUTATION R6A. ; _BMRB_accession_number 19519 _BMRB_flat_file_name bmr19519.str _Entry_type original _Submission_date 2013-09-23 _Accession_date 2013-09-23 _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 'del Rio-Portilla' F. . . 2 Ramirez-Cordero B. . . 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 2014-06-25 update BMRB 'update entry citation' 2014-05-27 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19524 'GS-TAMAPIN MUTATION R7A' 19527 'GS-TAMAPIN MUTATION R13A' 19528 'DOUBLE GS-TAMAPIN MUTATION R6A R7A' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Cytotoxicity of recombinant tamapin and related toxin-like peptides on model cell lines.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24821061 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ramirez-Cordero Belen . . 2 Toledano Yanis . . 3 Cano-Sanchez Patricia . . 4 Hernandez-Lopez Rogelio . . 5 Flores-Solis David . . 6 Saucedo-Yanez Alma L. . 7 Chavez-Uribe Isabel . . 8 Brieba Luis G. . 9 'Del Rio-Portilla' Federico . . stop_ _Journal_abbreviation 'Chem. Res. Toxicol.' _Journal_name_full 'Chemical research in toxicology' _Journal_volume 27 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 960 _Page_last 967 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'GS-TAMAPIN MUTATION R6A' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'GS-TAMAPIN MUTATION R6A' $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 3528.202 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 33 _Mol_residue_sequence ; GSAFCNLARCELSCRSLGLL GKCIGEECKCVPY ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 ALA 4 PHE 5 CYS 6 ASN 7 LEU 8 ALA 9 ARG 10 CYS 11 GLU 12 LEU 13 SER 14 CYS 15 ARG 16 SER 17 LEU 18 GLY 19 LEU 20 LEU 21 GLY 22 LYS 23 CYS 24 ILE 25 GLY 26 GLU 27 GLU 28 CYS 29 LYS 30 CYS 31 VAL 32 PRO 33 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 BMRB 17227 GS-alfa-Ktx5.4_SCORPION_TOXIN 100.00 33 96.97 96.97 4.04e-12 PDB 2ME7 "Nmr Solution Structure Of The Gs-tamapin Mutation R6a" 96.97 33 100.00 100.00 7.53e-12 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 'Indian red scorpion' 34647 Eukaryota Metazoa Mesobuthus tamulus 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 $entity 'recombinant technology' . Escherichia coli . 'modified pEt32a' 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 $entity 3 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_AMBER _Saveframe_category software _Name AMBER _Version 99 loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.4 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'GS-TAMAPIN MUTATION R6A' _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 2 SER H H 8.633 0.000 . 2 2 2 SER HA H 4.519 0.000 . 3 2 2 SER HB2 H 3.847 0.000 . 4 2 2 SER HB3 H 3.847 0.000 . 5 3 3 ALA H H 8.380 0.001 . 6 3 3 ALA HA H 4.404 0.002 . 7 3 3 ALA HB H 1.344 0.000 . 8 4 4 PHE H H 8.061 0.000 . 9 4 4 PHE HA H 4.673 0.000 . 10 4 4 PHE HB2 H 3.110 0.000 . 11 4 4 PHE HB3 H 3.001 0.000 . 12 4 4 PHE HD1 H 7.379 0.000 . 13 4 4 PHE HD2 H 7.379 0.000 . 14 4 4 PHE HE1 H 7.238 0.000 . 15 4 4 PHE HE2 H 7.238 0.000 . 16 5 5 CYS H H 8.165 0.000 . 17 5 5 CYS HA H 4.419 0.001 . 18 5 5 CYS HB2 H 2.808 0.000 . 19 5 5 CYS HB3 H 2.701 0.000 . 20 6 6 ASN H H 8.697 0.002 . 21 6 6 ASN HA H 4.827 0.000 . 22 6 6 ASN HB2 H 2.899 0.000 . 23 6 6 ASN HB3 H 2.796 0.000 . 24 6 6 ASN HD21 H 7.841 0.002 . 25 6 6 ASN HD22 H 7.099 0.002 . 26 7 7 LEU H H 8.841 0.000 . 27 7 7 LEU HA H 3.985 0.001 . 28 7 7 LEU HB2 H 1.815 0.000 . 29 7 7 LEU HB3 H 1.561 0.002 . 30 7 7 LEU HG H 1.502 0.005 . 31 7 7 LEU HD1 H 0.961 0.000 . 32 8 8 ALA H H 8.350 0.002 . 33 8 8 ALA HA H 4.143 0.003 . 34 8 8 ALA HB H 1.515 0.001 . 35 9 9 ARG H H 8.000 0.000 . 36 9 9 ARG HA H 4.086 0.000 . 37 9 9 ARG HB2 H 1.941 0.004 . 38 9 9 ARG HB3 H 1.880 0.001 . 39 9 9 ARG HG2 H 1.713 0.000 . 40 9 9 ARG HG3 H 1.796 0.000 . 41 9 9 ARG HD2 H 3.247 0.000 . 42 9 9 ARG HD3 H 3.247 0.000 . 43 9 9 ARG HE H 7.286 0.000 . 44 10 10 CYS H H 8.723 0.000 . 45 10 10 CYS HA H 4.652 0.000 . 46 10 10 CYS HB2 H 3.228 0.000 . 47 10 10 CYS HB3 H 2.797 0.000 . 48 11 11 GLU H H 9.141 0.000 . 49 11 11 GLU HA H 3.837 0.000 . 50 11 11 GLU HB2 H 2.349 0.000 . 51 11 11 GLU HB3 H 2.100 0.001 . 52 11 11 GLU HG2 H 2.663 0.000 . 53 11 11 GLU HG3 H 2.592 0.000 . 54 12 12 LEU H H 7.836 0.002 . 55 12 12 LEU HA H 4.138 0.001 . 56 12 12 LEU HB2 H 1.866 0.000 . 57 12 12 LEU HB3 H 1.804 0.000 . 58 12 12 LEU HG H 1.702 0.000 . 59 12 12 LEU HD1 H 0.960 0.002 . 60 13 13 SER H H 8.436 0.001 . 61 13 13 SER HA H 4.297 0.000 . 62 13 13 SER HB2 H 4.045 0.002 . 63 13 13 SER HB3 H 4.045 0.002 . 64 14 14 CYS H H 8.286 0.000 . 65 14 14 CYS HA H 4.522 0.000 . 66 14 14 CYS HB2 H 2.408 0.000 . 67 14 14 CYS HB3 H 2.408 0.000 . 68 15 15 ARG H H 8.371 0.000 . 69 15 15 ARG HA H 4.483 0.000 . 70 15 15 ARG HB2 H 2.258 0.000 . 71 15 15 ARG HB3 H 2.097 0.000 . 72 15 15 ARG HG2 H 1.877 0.000 . 73 15 15 ARG HG3 H 1.877 0.000 . 74 15 15 ARG HD2 H 3.304 0.001 . 75 15 15 ARG HD3 H 3.304 0.001 . 76 15 15 ARG HE H 7.255 0.002 . 77 16 16 SER H H 7.742 0.001 . 78 16 16 SER HA H 4.401 0.001 . 79 16 16 SER HB2 H 4.092 0.002 . 80 16 16 SER HB3 H 4.092 0.002 . 81 17 17 LEU H H 7.414 0.000 . 82 17 17 LEU HA H 4.577 0.000 . 83 17 17 LEU HB2 H 1.862 0.000 . 84 17 17 LEU HB3 H 1.862 0.000 . 85 17 17 LEU HG H 1.773 0.001 . 86 17 17 LEU HD1 H 1.011 0.000 . 87 17 17 LEU HD2 H 0.896 0.002 . 88 18 18 GLY H H 8.171 0.000 . 89 18 18 GLY HA2 H 3.997 0.000 . 90 18 18 GLY HA3 H 4.171 0.000 . 91 19 19 LEU H H 7.458 0.000 . 92 19 19 LEU HA H 4.674 0.000 . 93 19 19 LEU HB2 H 1.448 0.001 . 94 19 19 LEU HB3 H 1.448 0.001 . 95 19 19 LEU HG H 1.284 0.002 . 96 19 19 LEU HD1 H 0.748 0.002 . 97 20 20 LEU H H 8.655 0.000 . 98 20 20 LEU HA H 4.340 0.000 . 99 20 20 LEU HB2 H 1.468 0.000 . 100 20 20 LEU HB3 H 1.468 0.000 . 101 20 20 LEU HG H 1.255 0.007 . 102 20 20 LEU HD1 H 0.856 0.002 . 103 20 20 LEU HD2 H 0.749 0.002 . 104 21 21 GLY H H 8.043 0.000 . 105 21 21 GLY HA2 H 2.990 0.003 . 106 21 21 GLY HA3 H 5.208 0.002 . 107 22 22 LYS H H 8.871 0.001 . 108 22 22 LYS HA H 4.396 0.001 . 109 22 22 LYS HB2 H 1.672 0.000 . 110 22 22 LYS HB3 H 1.672 0.000 . 111 22 22 LYS HG2 H 1.295 0.000 . 112 22 22 LYS HG3 H 1.295 0.000 . 113 22 22 LYS HD2 H 1.553 0.001 . 114 22 22 LYS HD3 H 1.553 0.001 . 115 22 22 LYS HE2 H 2.850 0.000 . 116 22 22 LYS HE3 H 2.850 0.000 . 117 23 23 CYS H H 8.266 0.000 . 118 23 23 CYS HA H 5.312 0.000 . 119 23 23 CYS HB2 H 2.955 0.000 . 120 23 23 CYS HB3 H 2.845 0.000 . 121 24 24 ILE H H 9.056 0.000 . 122 24 24 ILE HA H 4.281 0.002 . 123 24 24 ILE HB H 1.815 0.000 . 124 24 24 ILE HG12 H 1.413 0.000 . 125 24 24 ILE HG13 H 1.116 0.000 . 126 24 24 ILE HG2 H 0.887 0.000 . 127 24 24 ILE HD1 H 0.803 0.002 . 128 25 25 GLY H H 9.027 0.000 . 129 25 25 GLY HA2 H 3.728 0.000 . 130 25 25 GLY HA3 H 3.954 0.000 . 131 26 26 GLU H H 8.852 0.001 . 132 26 26 GLU HA H 4.175 0.000 . 133 26 26 GLU HB2 H 1.974 0.000 . 134 26 26 GLU HB3 H 1.974 0.000 . 135 26 26 GLU HG2 H 2.263 0.001 . 136 26 26 GLU HG3 H 2.433 0.001 . 137 27 27 GLU H H 7.744 0.000 . 138 27 27 GLU HA H 4.541 0.002 . 139 27 27 GLU HB2 H 2.080 0.000 . 140 27 27 GLU HB3 H 2.012 0.002 . 141 27 27 GLU HG2 H 2.372 0.002 . 142 27 27 GLU HG3 H 2.429 0.003 . 143 28 28 CYS H H 8.695 0.000 . 144 28 28 CYS HA H 5.060 0.000 . 145 28 28 CYS HB2 H 3.072 0.000 . 146 28 28 CYS HB3 H 2.702 0.000 . 147 29 29 LYS H H 9.518 0.001 . 148 29 29 LYS HA H 4.687 0.000 . 149 29 29 LYS HB2 H 1.740 0.001 . 150 29 29 LYS HB3 H 1.639 0.003 . 151 29 29 LYS HG2 H 1.344 0.000 . 152 29 29 LYS HG3 H 1.344 0.000 . 153 29 29 LYS HD2 H 1.449 0.000 . 154 29 29 LYS HD3 H 1.449 0.000 . 155 29 29 LYS HE2 H 2.951 0.000 . 156 29 29 LYS HE3 H 2.951 0.000 . 157 30 30 CYS H H 8.543 0.001 . 158 30 30 CYS HA H 5.711 0.000 . 159 30 30 CYS HB2 H 2.954 0.000 . 160 30 30 CYS HB3 H 2.670 0.001 . 161 31 31 VAL H H 9.530 0.000 . 162 31 31 VAL HA H 4.954 0.001 . 163 31 31 VAL HB H 2.298 0.000 . 164 31 31 VAL HG1 H 0.858 0.000 . 165 31 31 VAL HG2 H 0.749 0.002 . 166 32 32 PRO HA H 4.562 0.000 . 167 32 32 PRO HB2 H 2.333 0.000 . 168 32 32 PRO HB3 H 2.049 0.002 . 169 32 32 PRO HG2 H 1.947 0.000 . 170 32 32 PRO HG3 H 1.947 0.000 . 171 32 32 PRO HD2 H 3.823 0.001 . 172 32 32 PRO HD3 H 3.652 0.000 . 173 33 33 TYR H H 8.275 0.000 . 174 33 33 TYR HA H 4.251 0.003 . 175 33 33 TYR HB2 H 3.108 0.000 . 176 33 33 TYR HB3 H 2.924 0.000 . 177 33 33 TYR HD1 H 7.237 0.000 . 178 33 33 TYR HD2 H 7.237 0.000 . 179 33 33 TYR HE1 H 6.738 0.000 . 180 33 33 TYR HE2 H 6.738 0.000 . stop_ save_