data_17661 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the long sarafotoxin srtx-i3 ; _BMRB_accession_number 17661 _BMRB_flat_file_name bmr17661.str _Entry_type original _Submission_date 2011-05-24 _Accession_date 2011-05-24 _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 Cordier Florence . . 2 Zorba Adelajda . . 3 Hajj Marianna . . 4 Ducancel Frederic . . 5 Servent Denis . . 6 Delepierre Muriel . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 146 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-05-09 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17662 'sarafotoxin srtx-m' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Pharmacological and structural characterization of long-sarafotoxins, a new family of endothelin-like peptides: Role of the C-terminus extension.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21889567 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mourier Gilles . . 2 Hajj Mariana . . 3 Cordier Florence . . 4 Zorba Adelajda . . 5 Gao XingHuang . . 6 Coskun Tolga . . 7 Herbet Amaury . . 8 Marcon Elodie . . 9 Beau Fabrice . . 10 Delepierre Muriel . . 11 Ducancel Frederic . . 12 Servent Denis . . stop_ _Journal_abbreviation Biochimie _Journal_name_full Biochimie _Journal_volume 94 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 461 _Page_last 470 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name srtx-i3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label srtx-i3 $srtx-i3 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_srtx-i3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common srtx-i3 _Molecular_mass 2967.403 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 25 _Mol_residue_sequence ; CSCTDMSDLECMNFCHKDVI WVNRN ; loop_ _Residue_seq_code _Residue_label 1 CYS 2 SER 3 CYS 4 THR 5 ASP 6 MET 7 SER 8 ASP 9 LEU 10 GLU 11 CYS 12 MET 13 ASN 14 PHE 15 CYS 16 HIS 17 LYS 18 ASP 19 VAL 20 ILE 21 TRP 22 VAL 23 ASN 24 ARG 25 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-23 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 2LDE "Solution Structure Of The Long Sarafotoxin Srtx-I3" 100.00 25 100.00 100.00 1.65e-08 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $srtx-i3 snake 512568 Eukaryota Metazoa Atractaspis irregularis 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 $srtx-i3 '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 $srtx-i3 3 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection 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_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' 'peak picking' 'chemical shift assignment' stop_ _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version . loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'structure solution' refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details 'Spectrometer equipped with a cryoprobe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _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_2D_1H-1H_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_25C _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 298 . K pH 4.5 . pH pressure 1 . atm 'ionic strength' 0 . M stop_ save_ save_sample_35C _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 308 . K pH 4.5 . pH pressure 1 . atm 'ionic strength' 0 . M 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 COSY' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_25C _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name srtx-i3 _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 1 CYS HA H 4.183 . 1 2 1 1 CYS HB2 H 3.321 . 2 3 1 1 CYS HB3 H 3.073 . 2 4 2 2 SER H H 8.942 . 1 5 2 2 SER HA H 4.734 . 1 6 2 2 SER HB2 H 3.821 . 2 7 2 2 SER HB3 H 3.821 . 2 8 3 3 CYS H H 8.728 . 1 9 3 3 CYS HA H 4.897 . 1 10 3 3 CYS HB2 H 3.370 . 2 11 3 3 CYS HB3 H 2.940 . 2 12 4 4 THR H H 8.058 . 1 13 4 4 THR HA H 4.104 . 1 14 4 4 THR HB H 3.958 . 1 15 4 4 THR HG2 H 1.135 . 1 16 5 5 ASP H H 8.871 . 1 17 5 5 ASP HA H 4.494 . 1 18 5 5 ASP HB2 H 3.073 . 2 19 5 5 ASP HB3 H 2.805 . 2 20 6 6 MET H H 7.903 . 1 21 6 6 MET HA H 4.630 . 1 22 6 6 MET HB2 H 2.066 . 2 23 6 6 MET HB3 H 1.765 . 2 24 6 6 MET HG2 H 2.438 . 2 25 6 6 MET HG3 H 2.322 . 2 26 6 6 MET HE H 1.690 . 1 27 7 7 SER H H 8.179 . 1 28 7 7 SER HA H 4.471 . 1 29 7 7 SER HB2 H 4.235 . 2 30 7 7 SER HB3 H 3.973 . 2 31 8 8 ASP H H 8.809 . 1 32 8 8 ASP HA H 4.385 . 1 33 8 8 ASP HB2 H 2.884 . 2 34 8 8 ASP HB3 H 2.837 . 2 35 9 9 LEU H H 8.331 . 1 36 9 9 LEU HA H 4.048 . 1 37 9 9 LEU HB2 H 1.625 . 2 38 9 9 LEU HB3 H 1.625 . 2 39 9 9 LEU HG H 1.537 . 1 40 9 9 LEU HD1 H 0.853 . 4 41 9 9 LEU HD2 H 0.904 . 4 42 10 10 GLU H H 7.757 . 1 43 10 10 GLU HA H 4.069 . 1 44 10 10 GLU HB2 H 2.149 . 2 45 10 10 GLU HB3 H 2.071 . 2 46 10 10 GLU HG2 H 2.537 . 2 47 10 10 GLU HG3 H 2.537 . 2 48 11 11 CYS H H 8.510 . 1 49 11 11 CYS HA H 4.585 . 1 50 11 11 CYS HB2 H 3.108 . 2 51 11 11 CYS HB3 H 3.108 . 2 52 12 12 MET H H 8.203 . 1 53 12 12 MET HA H 4.097 . 1 54 12 12 MET HB2 H 2.150 . 2 55 12 12 MET HB3 H 2.081 . 2 56 12 12 MET HG2 H 2.615 . 2 57 12 12 MET HG3 H 2.534 . 2 58 12 12 MET HE H 2.002 . 1 59 13 13 ASN H H 7.819 . 1 60 13 13 ASN HA H 4.469 . 1 61 13 13 ASN HB2 H 2.752 . 2 62 13 13 ASN HB3 H 2.752 . 2 63 13 13 ASN HD21 H 6.857 . 2 64 13 13 ASN HD22 H 7.428 . 2 65 14 14 PHE H H 8.408 . 1 66 14 14 PHE HA H 4.375 . 1 67 14 14 PHE HB2 H 3.210 . 2 68 14 14 PHE HB3 H 3.158 . 2 69 14 14 PHE HD1 H 7.277 . 2 70 14 14 PHE HD2 H 7.277 . 2 71 14 14 PHE HE1 H 7.308 . 2 72 14 14 PHE HE2 H 7.308 . 2 73 14 14 PHE HZ H 7.384 . 1 74 15 15 CYS H H 8.416 . 1 75 15 15 CYS HA H 4.631 . 1 76 15 15 CYS HB2 H 3.125 . 2 77 15 15 CYS HB3 H 2.807 . 2 78 16 16 HIS H H 7.847 . 1 79 16 16 HIS HA H 4.628 . 1 80 16 16 HIS HB2 H 3.305 . 2 81 16 16 HIS HB3 H 3.305 . 2 82 16 16 HIS HD2 H 7.198 . 2 83 16 16 HIS HE1 H 8.536 . 2 84 17 17 LYS H H 7.969 . 1 85 17 17 LYS HA H 4.268 . 1 86 17 17 LYS HB2 H 1.788 . 2 87 17 17 LYS HB3 H 1.726 . 2 88 17 17 LYS HG2 H 1.341 . 2 89 17 17 LYS HG3 H 1.341 . 2 90 17 17 LYS HD2 H 1.618 . 2 91 17 17 LYS HD3 H 1.618 . 2 92 17 17 LYS HE2 H 2.922 . 2 93 17 17 LYS HE3 H 2.922 . 2 94 17 17 LYS HZ H 7.489 . 1 95 18 18 ASP H H 8.353 . 1 96 18 18 ASP HA H 4.650 . 1 97 18 18 ASP HB2 H 2.874 . 2 98 18 18 ASP HB3 H 2.743 . 2 99 19 19 VAL H H 7.901 . 1 100 19 19 VAL HA H 4.029 . 1 101 19 19 VAL HB H 1.920 . 1 102 19 19 VAL HG1 H 0.710 . 4 103 19 19 VAL HG2 H 0.805 . 4 104 20 20 ILE H H 8.032 . 1 105 20 20 ILE HA H 4.108 . 1 106 20 20 ILE HB H 1.754 . 1 107 20 20 ILE HG12 H 1.361 . 9 108 20 20 ILE HG13 H 1.089 . 9 109 20 20 ILE HG2 H 0.770 . 4 110 20 20 ILE HD1 H 0.770 . 1 111 21 21 TRP H H 8.230 . 1 112 21 21 TRP HA H 4.657 . 1 113 21 21 TRP HB2 H 3.213 . 2 114 21 21 TRP HB3 H 3.136 . 2 115 21 21 TRP HD1 H 7.162 . 1 116 21 21 TRP HE1 H 10.033 . 2 117 21 21 TRP HE3 H 7.564 . 2 118 21 21 TRP HZ2 H 7.429 . 2 119 21 21 TRP HZ3 H 7.090 . 2 120 21 21 TRP HH2 H 7.174 . 1 121 22 22 VAL H H 7.795 . 1 122 22 22 VAL HA H 3.958 . 1 123 22 22 VAL HB H 1.885 . 1 124 22 22 VAL HG1 H 0.801 . 4 125 22 22 VAL HG2 H 0.801 . 2 126 23 23 ASN H H 8.308 . 1 127 23 23 ASN HA H 4.510 . 1 128 23 23 ASN HB2 H 2.768 . 2 129 23 23 ASN HB3 H 2.620 . 2 130 23 23 ASN HD21 H 6.891 . 2 131 23 23 ASN HD22 H 7.549 . 2 132 24 24 ARG H H 8.214 . 1 133 24 24 ARG HA H 4.282 . 1 134 24 24 ARG HB2 H 1.821 . 2 135 24 24 ARG HB3 H 1.667 . 2 136 24 24 ARG HG2 H 1.533 . 2 137 24 24 ARG HG3 H 1.533 . 2 138 24 24 ARG HD2 H 3.068 . 2 139 24 24 ARG HD3 H 3.068 . 2 140 24 24 ARG HE H 7.069 . 1 141 25 25 ASN H H 8.279 . 1 142 25 25 ASN HA H 4.649 . 1 143 25 25 ASN HB2 H 2.816 . 2 144 25 25 ASN HB3 H 2.750 . 2 145 25 25 ASN HD21 H 6.846 . 2 146 25 25 ASN HD22 H 7.537 . 2 stop_ save_