data_30508 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure of vil14a ; _BMRB_accession_number 30508 _BMRB_flat_file_name bmr30508.str _Entry_type original _Submission_date 2018-08-16 _Accession_date 2018-08-16 _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 Dovell S. . . 2 Mari F. . . 3 Moller C. . . 4 Melaun C. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 126 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-08-31 original BMRB . stop_ _Original_release_date 2018-08-27 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Definition of the R-superfamily of conotoxins: Structural convergence of helix-loop-helix peptidic scaffolds. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30040981 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Moller C. . . 2 Dovell S. . . 3 Melaun C. . . 4 Mari F. . . stop_ _Journal_abbreviation Peptides _Journal_volume 107 _Journal_issue . _Journal_ISSN 1873-5169 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 75 _Page_last 82 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Kappa-conotoxin vil14a' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 2879.409 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 27 _Mol_residue_sequence ; GGLGRCIYNCMNSGGGLSFI QCKTMCY ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 GLY 3 LEU 4 GLY 5 ARG 6 CYS 7 ILE 8 TYR 9 ASN 10 CYS 11 MET 12 ASN 13 SER 14 GLY 15 GLY 16 GLY 17 LEU 18 SER 19 PHE 20 ILE 21 GLN 22 CYS 23 LYS 24 THR 25 MET 26 CYS 27 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 "Villepin's cone" 257347 Eukaryota Metazoa Conus villepinii 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_1 . . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM NA peptide, 0.11 mM TSP, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM 'natural abundance' TSP 0.11 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name 'X-PLOR NIH' _Version 2.19 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement 'structure calculation' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name VNMR _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'water solution' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.6 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 TSP H 1 'methyl protons' ppm 0.000 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_assigned_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-1H TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name entity_1 _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 GLY H H 8.67 . 1 2 2 2 GLY HA3 H 4.06 . . 3 3 3 LEU H H 8.49 . 1 4 3 3 LEU HA H 4.31 . 1 5 3 3 LEU HB3 H 1.65 . . 6 3 3 LEU HG H 0.88 . 1 7 4 4 GLY H H 8.52 . 1 8 4 4 GLY HA2 H 3.84 . . 9 4 4 GLY HA3 H 4.00 . . 10 5 5 ARG H H 8.21 . 1 11 5 5 ARG HA H 4.21 . 1 12 5 5 ARG HB3 H 1.86 . . 13 5 5 ARG HG3 H 1.67 . . 14 5 5 ARG HD3 H 3.19 . . 15 5 5 ARG HE H 7.20 . 1 16 6 6 CYS H H 8.14 . 1 17 6 6 CYS HA H 4.23 . 1 18 6 6 CYS HB2 H 3.18 . . 19 6 6 CYS HB3 H 3.28 . . 20 7 7 ILE H H 8.52 . 1 21 7 7 ILE HA H 3.39 . 1 22 7 7 ILE HB H 1.90 . 1 23 7 7 ILE HG12 H 0.84 . . 24 7 7 ILE HG13 H 1.78 . . 25 7 7 ILE HG2 H 0.73 . 1 26 7 7 ILE HD1 H 0.60 . 1 27 8 8 TYR H H 8.33 . 1 28 8 8 TYR HA H 4.08 . 1 29 8 8 TYR HB2 H 3.03 . . 30 8 8 TYR HB3 H 3.14 . . 31 8 8 TYR HD1 H 7.14 . 2 32 8 8 TYR HE1 H 6.82 . 2 33 9 9 ASN H H 8.68 . 1 34 9 9 ASN HA H 4.38 . 1 35 9 9 ASN HB2 H 2.83 . . 36 9 9 ASN HB3 H 2.94 . . 37 9 9 ASN HD21 H 7.65 . . 38 9 9 ASN HD22 H 6.89 . . 39 10 10 CYS H H 8.31 . 1 40 10 10 CYS HA H 4.08 . 1 41 10 10 CYS HB2 H 3.09 . . 42 10 10 CYS HB3 H 3.22 . . 43 11 11 MET H H 8.80 . 1 44 11 11 MET HA H 4.21 . 1 45 11 11 MET HB3 H 2.00 . . 46 11 11 MET HG2 H 2.44 . . 47 11 11 MET HG3 H 2.75 . . 48 11 11 MET HE H 2.14 . 1 49 12 12 ASN H H 7.65 . 1 50 12 12 ASN HA H 4.58 . 1 51 12 12 ASN HB2 H 2.81 . . 52 12 12 ASN HB3 H 2.97 . . 53 12 12 ASN HD21 H 6.87 . . 54 12 12 ASN HD22 H 6.50 . . 55 13 13 SER H H 7.51 . 1 56 13 13 SER HA H 4.47 . 1 57 13 13 SER HB3 H 4.16 . . 58 14 14 GLY H H 8.40 . 1 59 14 14 GLY HA2 H 3.85 . . 60 14 14 GLY HA3 H 4.22 . . 61 15 15 GLY H H 8.33 . 1 62 15 15 GLY HA2 H 3.81 . . 63 15 15 GLY HA3 H 4.08 . . 64 16 16 GLY H H 8.49 . 1 65 16 16 GLY HA2 H 3.85 . . 66 16 16 GLY HA3 H 3.94 . . 67 17 17 LEU H H 7.76 . 1 68 17 17 LEU HA H 4.42 . 1 69 17 17 LEU HB2 H 1.51 . . 70 17 17 LEU HB3 H 1.67 . . 71 17 17 LEU HG H 1.44 . 1 72 17 17 LEU HD1 H 0.82 . . 73 17 17 LEU HD2 H 0.74 . . 74 18 18 SER H H 8.70 . 1 75 18 18 SER HA H 4.54 . 1 76 18 18 SER HB2 H 4.04 . . 77 18 18 SER HB3 H 4.41 . . 78 19 19 PHE H H 9.06 . 1 79 19 19 PHE HA H 4.33 . 1 80 19 19 PHE HB2 H 3.02 . . 81 19 19 PHE HB3 H 3.26 . . 82 19 19 PHE HD1 H 7.22 . . 83 19 19 PHE HE1 H 7.34 . . 84 20 20 ILE H H 8.19 . 1 85 20 20 ILE HA H 3.65 . 1 86 20 20 ILE HB H 1.88 . 1 87 20 20 ILE HG12 H 1.40 . . 88 20 20 ILE HG13 H 1.60 . . 89 20 20 ILE HG2 H 0.94 . 1 90 21 21 GLN H H 7.76 . 1 91 21 21 GLN HA H 4.02 . 1 92 21 21 GLN HB3 H 1.88 . . 93 21 21 GLN HG3 H 2.35 . . 94 21 21 GLN HE21 H 7.48 . . 95 21 21 GLN HE22 H 6.48 . . 96 22 22 CYS H H 8.52 . 1 97 22 22 CYS HA H 4.44 . 1 98 22 22 CYS HB2 H 2.66 . . 99 22 22 CYS HB3 H 2.88 . . 100 23 23 LYS H H 8.88 . 1 101 23 23 LYS HA H 3.56 . 1 102 23 23 LYS HB2 H 1.52 . . 103 23 23 LYS HB3 H 1.61 . . 104 23 23 LYS HG3 H 1.19 . . 105 23 23 LYS HD3 H 1.32 . . 106 23 23 LYS HE3 H 2.80 . . 107 24 24 THR H H 7.63 . 1 108 24 24 THR HA H 4.29 . 1 109 24 24 THR HB H 3.95 . 1 110 24 24 THR HG2 H 1.27 . 1 111 25 25 MET H H 7.66 . 1 112 25 25 MET HA H 4.24 . 1 113 25 25 MET HB3 H 2.21 . . 114 25 25 MET HG2 H 2.57 . . 115 25 25 MET HG3 H 2.64 . . 116 25 25 MET HE H 2.01 . 1 117 26 26 CYS H H 7.65 . 1 118 26 26 CYS HA H 4.37 . 1 119 26 26 CYS HB2 H 2.97 . . 120 26 26 CYS HB3 H 3.05 . . 121 27 27 TYR H H 7.65 . 1 122 27 27 TYR HA H 4.87 . 1 123 27 27 TYR HB2 H 2.35 . . 124 27 27 TYR HB3 H 2.81 . . 125 27 27 TYR HD1 H 7.17 . . 126 27 27 TYR HE1 H 6.79 . . stop_ save_