data_19528 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR solution structure of the DOUBLE GS-TAMAPIN MUTATION R6A R7A. ; _BMRB_accession_number 19528 _BMRB_flat_file_name bmr19528.str _Entry_type original _Submission_date 2013-09-24 _Accession_date 2013-09-24 _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" 174 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_ 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 'DOUBLE GS-TAMAPIN MUTATION R6A R7A' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DOUBLE GS-TAMAPIN MUTATION R6A R7A' $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 3442.085 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; SAFCNLAACELSCRSLGLLG KCIGEECKCVPY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 SER 2 3 ALA 3 4 PHE 4 5 CYS 5 6 ASN 6 7 LEU 7 8 ALA 8 9 ALA 9 10 CYS 10 11 GLU 11 12 LEU 12 13 SER 13 14 CYS 14 15 ARG 15 16 SER 16 17 LEU 17 18 GLY 18 19 LEU 19 20 LEU 20 21 GLY 21 22 LYS 22 23 CYS 23 24 ILE 24 25 GLY 25 26 GLU 26 27 GLU 27 28 CYS 28 29 LYS 29 30 CYS 30 31 VAL 31 32 PRO 32 33 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-07-28 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 2MEO "Nmr Solution Structure Of The Double Gs-tamapin Mutation R6a/r7a" 96.88 33 100.00 100.00 3.18e-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 $entity scorpions 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 3.0 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_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details '3mm Triple resonance probe.' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.5 0.1 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 'DOUBLE GS-TAMAPIN MUTATION R6A R7A' _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 1 SER H H 8.629 0.000 . 2 2 1 SER HA H 4.783 0.000 . 3 2 1 SER HB2 H 3.906 0.000 . 4 2 1 SER HB3 H 4.503 0.000 . 5 3 2 ALA H H 8.380 0.000 . 6 3 2 ALA HA H 4.390 0.000 . 7 3 2 ALA HB H 1.335 0.000 . 8 4 3 PHE H H 8.027 0.000 . 9 4 3 PHE HA H 4.666 0.000 . 10 4 3 PHE HB2 H 3.098 0.000 . 11 4 3 PHE HB3 H 2.991 0.000 . 12 4 3 PHE HD1 H 7.357 0.000 . 13 4 3 PHE HD2 H 7.357 0.000 . 14 4 3 PHE HE1 H 7.220 0.000 . 15 4 3 PHE HE2 H 7.220 0.000 . 16 5 4 CYS H H 8.143 0.000 . 17 5 4 CYS HA H 4.412 0.000 . 18 5 4 CYS HB2 H 2.685 0.000 . 19 5 4 CYS HB3 H 2.786 0.000 . 20 6 5 ASN H H 8.725 0.000 . 21 6 5 ASN HA H 4.830 0.000 . 22 6 5 ASN HB2 H 2.970 0.000 . 23 6 5 ASN HB3 H 2.788 0.000 . 24 6 5 ASN HD21 H 7.814 0.000 . 25 6 5 ASN HD22 H 7.087 0.000 . 26 7 6 LEU H H 8.787 0.000 . 27 7 6 LEU HA H 3.977 0.000 . 28 7 6 LEU HB2 H 1.563 0.000 . 29 7 6 LEU HB3 H 1.806 0.000 . 30 7 6 LEU HG H 1.497 0.000 . 31 7 6 LEU HD1 H 0.950 0.000 . 32 8 7 ALA H H 8.354 0.000 . 33 8 7 ALA HA H 4.120 0.000 . 34 8 7 ALA HB H 1.498 0.000 . 35 9 8 ALA H H 7.884 0.000 . 36 9 8 ALA HA H 4.152 0.000 . 37 9 8 ALA HB H 1.496 0.001 . 38 10 9 CYS H H 8.672 0.000 . 39 10 9 CYS HA H 4.637 0.000 . 40 10 9 CYS HB2 H 3.239 0.000 . 41 10 9 CYS HB3 H 2.787 0.000 . 42 11 10 GLU H H 9.111 0.000 . 43 11 10 GLU HA H 3.825 0.000 . 44 11 10 GLU HB2 H 2.339 0.003 . 45 11 10 GLU HB3 H 2.090 0.000 . 46 11 10 GLU HG2 H 2.653 0.000 . 47 11 10 GLU HG3 H 2.586 0.001 . 48 12 11 LEU H H 7.868 0.000 . 49 12 11 LEU HA H 4.126 0.003 . 50 12 11 LEU HB2 H 1.820 0.006 . 51 12 11 LEU HB3 H 1.820 0.006 . 52 12 11 LEU HG H 1.761 0.000 . 53 12 11 LEU HD1 H 0.957 0.002 . 54 12 11 LEU HD2 H 0.957 0.002 . 55 13 12 SER H H 8.360 0.000 . 56 13 12 SER HA H 4.278 0.000 . 57 13 12 SER HB2 H 4.025 0.000 . 58 13 12 SER HB3 H 4.025 0.000 . 59 14 13 CYS H H 8.312 0.000 . 60 14 13 CYS HA H 4.495 0.000 . 61 14 13 CYS HB2 H 2.385 0.000 . 62 14 13 CYS HB3 H 2.385 0.000 . 63 15 14 ARG H H 8.345 0.000 . 64 15 14 ARG HA H 4.467 0.000 . 65 15 14 ARG HB2 H 2.251 0.000 . 66 15 14 ARG HB3 H 2.078 0.000 . 67 15 14 ARG HG2 H 1.859 0.000 . 68 15 14 ARG HG3 H 1.859 0.000 . 69 15 14 ARG HD2 H 3.286 0.000 . 70 15 14 ARG HD3 H 3.286 0.000 . 71 15 14 ARG HE H 7.235 0.000 . 72 16 15 SER H H 7.727 0.000 . 73 16 15 SER HA H 4.392 0.000 . 74 16 15 SER HB2 H 4.087 0.000 . 75 16 15 SER HB3 H 4.087 0.000 . 76 17 16 LEU H H 7.401 0.000 . 77 17 16 LEU HA H 4.570 0.000 . 78 17 16 LEU HB2 H 1.853 0.000 . 79 17 16 LEU HB3 H 1.853 0.000 . 80 17 16 LEU HG H 1.762 0.000 . 81 17 16 LEU HD1 H 1.000 0.004 . 82 17 16 LEU HD2 H 0.884 0.005 . 83 18 17 GLY H H 8.152 0.000 . 84 18 17 GLY HA2 H 4.150 0.000 . 85 18 17 GLY HA3 H 3.992 0.000 . 86 19 18 LEU H H 7.446 0.000 . 87 19 18 LEU HA H 4.652 0.000 . 88 19 18 LEU HB2 H 1.279 0.000 . 89 19 18 LEU HB3 H 1.279 0.000 . 90 19 18 LEU HG H 1.438 0.000 . 91 19 18 LEU HD1 H 0.738 0.000 . 92 20 19 LEU H H 8.641 0.000 . 93 20 19 LEU HA H 4.332 0.000 . 94 20 19 LEU HB2 H 1.456 0.007 . 95 20 19 LEU HB3 H 1.456 0.007 . 96 20 19 LEU HG H 1.252 0.005 . 97 20 19 LEU HD1 H 0.741 0.000 . 98 20 19 LEU HD2 H 0.853 0.000 . 99 21 20 GLY H H 8.018 0.000 . 100 21 20 GLY HA2 H 2.977 0.000 . 101 21 20 GLY HA3 H 5.198 0.000 . 102 22 21 LYS H H 8.862 0.000 . 103 22 21 LYS HA H 4.385 0.000 . 104 22 21 LYS HB2 H 1.664 0.000 . 105 22 21 LYS HB3 H 1.664 0.000 . 106 22 21 LYS HG2 H 1.284 0.000 . 107 22 21 LYS HG3 H 1.284 0.000 . 108 22 21 LYS HD2 H 1.541 0.000 . 109 22 21 LYS HD3 H 1.541 0.000 . 110 22 21 LYS HE2 H 2.849 0.003 . 111 22 21 LYS HE3 H 2.849 0.003 . 112 23 22 CYS H H 8.240 0.000 . 113 23 22 CYS HA H 5.290 0.000 . 114 23 22 CYS HB2 H 2.935 0.000 . 115 23 22 CYS HB3 H 2.837 0.000 . 116 24 23 ILE H H 9.040 0.000 . 117 24 23 ILE HA H 4.264 0.000 . 118 24 23 ILE HB H 1.805 0.000 . 119 24 23 ILE HG12 H 1.402 0.000 . 120 24 23 ILE HG13 H 1.113 0.000 . 121 24 23 ILE HG2 H 0.873 0.000 . 122 24 23 ILE HD1 H 0.793 0.001 . 123 25 24 GLY H H 9.016 0.000 . 124 25 24 GLY HA2 H 3.719 0.000 . 125 25 24 GLY HA3 H 3.935 0.000 . 126 26 25 GLU H H 8.831 0.000 . 127 26 25 GLU HA H 4.159 0.000 . 128 26 25 GLU HB2 H 1.963 0.000 . 129 26 25 GLU HB3 H 1.963 0.000 . 130 26 25 GLU HG2 H 2.249 0.000 . 131 26 25 GLU HG3 H 2.419 0.000 . 132 27 26 GLU H H 7.699 0.000 . 133 27 26 GLU HA H 4.530 0.004 . 134 27 26 GLU HB2 H 2.050 0.000 . 135 27 26 GLU HB3 H 1.997 0.001 . 136 27 26 GLU HG2 H 2.345 0.005 . 137 27 26 GLU HG3 H 2.414 0.001 . 138 28 27 CYS H H 8.701 0.000 . 139 28 27 CYS HA H 5.035 0.000 . 140 28 27 CYS HB2 H 3.078 0.000 . 141 28 27 CYS HB3 H 2.689 0.000 . 142 29 28 LYS H H 9.492 0.000 . 143 29 28 LYS HA H 4.675 0.000 . 144 29 28 LYS HB2 H 1.730 0.000 . 145 29 28 LYS HB3 H 1.633 0.000 . 146 29 28 LYS HG2 H 1.324 0.001 . 147 29 28 LYS HG3 H 1.324 0.001 . 148 29 28 LYS HD2 H 1.418 0.008 . 149 29 28 LYS HD3 H 1.418 0.008 . 150 29 28 LYS HE2 H 2.930 0.006 . 151 29 28 LYS HE3 H 2.930 0.006 . 152 30 29 CYS H H 8.519 0.000 . 153 30 29 CYS HA H 5.708 0.000 . 154 30 29 CYS HB2 H 2.936 0.000 . 155 30 29 CYS HB3 H 2.651 0.000 . 156 31 30 VAL H H 9.511 0.000 . 157 31 30 VAL HA H 4.934 0.000 . 158 31 30 VAL HB H 2.289 0.004 . 159 31 30 VAL HG1 H 0.848 0.000 . 160 31 30 VAL HG2 H 0.741 0.003 . 161 32 31 PRO HB2 H 2.312 0.000 . 162 32 31 PRO HB3 H 2.024 0.000 . 163 32 31 PRO HG2 H 1.932 0.001 . 164 32 31 PRO HG3 H 1.932 0.001 . 165 32 31 PRO HD2 H 3.635 0.000 . 166 32 31 PRO HD3 H 3.800 0.000 . 167 33 32 TYR H H 8.163 0.000 . 168 33 32 TYR HA H 4.216 0.000 . 169 33 32 TYR HB2 H 2.906 0.000 . 170 33 32 TYR HB3 H 3.098 0.000 . 171 33 32 TYR HD1 H 7.217 0.000 . 172 33 32 TYR HD2 H 7.217 0.000 . 173 33 32 TYR HE1 H 6.732 0.004 . 174 33 32 TYR HE2 H 6.732 0.004 . stop_ save_