data_30211 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Ocellatin-LB1 ; _BMRB_accession_number 30211 _BMRB_flat_file_name bmr30211.str _Entry_type original _Submission_date 2016-12-17 _Accession_date 2017-12-05 _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 Gusmao K. A.G. . 2 Santos D. M. . 3 'de Lima' M. E. . 4 Pilo-Veloso D. . . 5 Resende J. M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 109 "13C chemical shifts" 68 "15N chemical shifts" 20 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-12-08 original BMRB . stop_ _Original_release_date 2017-12-05 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR structures in different membrane environments of three ocellatin peptides isolated from Leptodactylus labyrinthicus ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gusmao K. A.G. . 2 Santos D. M. . 3 Verly R. M. . 4 'de Lima' M. E. . 5 Pilo-Veloso D. . . 6 Resende J. M. . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Ocellatin-K1 _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 2195.648 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 23 _Mol_residue_sequence ; GVVDILKGAAKDIAGHLASK VMX ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 VAL 3 VAL 4 ASP 5 ILE 6 LEU 7 LYS 8 GLY 9 ALA 10 ALA 11 LYS 12 ASP 13 ILE 14 ALA 15 GLY 16 HIS 17 LEU 18 ALA 19 SER 20 LYS 21 VAL 22 MET 23 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'AMINO GROUP' _BMRB_code NH2 _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N HN1 ? ? SING N HN2 ? ? 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_1 . . . . . . 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 _Details $entity_1 'chemical synthesis' . . . . . 'Skin secretions' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '2.0 mM Ocellatin-LB1, 20 mM potassium phosphate, 1 mM DSS, 60 % d2 TFE, 40 % H2O, trifluoroethanol/water' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling DSS 1 mM 'natural abundance' H2O 40 % 'natural abundance' $entity_1 2.0 mM 'natural abundance' TFE 60 % d2 'potassium phosphate' 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name Molmol _Version . loop_ _Vendor _Address _Electronic_address 'Koradi, Billeter and Wuthrich' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_software_3 _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson BA, Blevins RA.' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_software_4 _Saveframe_category software _Name 'Procheck 3.5.4' _Version . loop_ _Vendor _Address _Electronic_address 'Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_software_5 _Saveframe_category software _Name 'X-PLOR_NIH 2.17.0' _Version . loop_ _Vendor _Address _Electronic_address 'SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE' . . stop_ loop_ _Task refinement 'structure calculation' stop_ _Details . save_ save_software_6 _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceIII _Field_strength 600 _Details . 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_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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 7 . pH pressure 1 . atm temperature 293.15 . 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 DSS C 13 'methyl carbons' ppm 0 internal direct . . . 1 DSS H 1 protons ppm 0 internal direct . . . 1 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 TOCSY' '2D 1H-1H NOESY' '2D 1H-13C HSQC' '2D 1H-15N HSQC' 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 1 1 GLY HA2 H 4.096 . . 2 1 1 GLY HA3 H 4.096 . . 3 1 1 GLY CA C 43.542 . . 4 2 2 VAL H H 8.122 . . 5 2 2 VAL HA H 3.858 . . 6 2 2 VAL HB H 2.106 . . 7 2 2 VAL HG1 H 1.111 . . 8 2 2 VAL HG2 H 1.032 . . 9 2 2 VAL CA C 66.290 . . 10 2 2 VAL CB C 32.058 . . 11 2 2 VAL CG1 C 21.106 . . 12 2 2 VAL CG2 C 20.058 . . 13 3 3 VAL H H 8.125 . . 14 3 3 VAL HA H 3.791 . . 15 3 3 VAL HB H 2.107 . . 16 3 3 VAL HG1 H 1.075 . . 17 3 3 VAL HG2 H 0.998 . . 18 3 3 VAL CA C 66.033 . . 19 3 3 VAL CB C 31.393 . . 20 3 3 VAL CG1 C 21.783 . . 21 3 3 VAL CG2 C 20.679 . . 22 3 3 VAL N N 117.872 . . 23 4 4 ASP H H 7.429 . . 24 4 4 ASP HA H 4.395 . . 25 4 4 ASP HB2 H 2.836 . . 26 4 4 ASP HB3 H 2.751 . . 27 4 4 ASP CA C 57.289 . . 28 4 4 ASP CB C 41.051 . . 29 4 4 ASP N N 117.326 . . 30 5 5 ILE H H 7.616 . . 31 5 5 ILE HA H 3.867 . . 32 5 5 ILE HB H 2.170 . . 33 5 5 ILE HG12 H 1.732 . . 34 5 5 ILE HG13 H 1.244 . . 35 5 5 ILE HG2 H 0.977 . . 36 5 5 ILE HD1 H 0.910 . . 37 5 5 ILE CA C 64.379 . . 38 5 5 ILE CB C 37.883 . . 39 5 5 ILE CG1 C 28.090 . . 40 5 5 ILE CG2 C 16.437 . . 41 5 5 ILE CD1 C 11.933 . . 42 5 5 ILE N N 120.417 . . 43 6 6 LEU H H 8.101 . . 44 6 6 LEU HA H 4.156 . . 45 6 6 LEU HB2 H 1.945 . . 46 6 6 LEU HB3 H 1.591 . . 47 6 6 LEU HG H 1.886 . . 48 6 6 LEU HD1 H 0.922 . . 49 6 6 LEU HD2 H 0.887 . . 50 6 6 LEU CA C 58.137 . . 51 6 6 LEU CB C 41.602 . . 52 6 6 LEU CG C 26.757 . . 53 6 6 LEU CD1 C 22.559 . . 54 6 6 LEU CD2 C 21.677 . . 55 6 6 LEU N N 120.320 . . 56 7 7 LYS H H 8.427 . . 57 7 7 LYS HA H 4.088 . . 58 7 7 LYS HB2 H 1.977 . . 59 7 7 LYS HB3 H 1.922 . . 60 7 7 LYS HG2 H 1.476 . . 61 7 7 LYS HD2 H 1.756 . . 62 7 7 LYS HD3 H 1.739 . . 63 7 7 LYS HE2 H 2.967 . . 64 7 7 LYS HE3 H 3.043 . . 65 7 7 LYS CA C 59.575 . . 66 7 7 LYS CB C 32.658 . . 67 7 7 LYS CG C 25.458 . . 68 7 7 LYS CD C 29.740 . . 69 7 7 LYS CE C 42.228 . . 70 7 7 LYS N N 117.764 . . 71 8 8 GLY H H 7.994 . . 72 8 8 GLY HA2 H 3.948 . . 73 8 8 GLY HA3 H 3.921 . . 74 8 8 GLY CA C 43.564 . . 75 8 8 GLY N N 106.507 . . 76 9 9 ALA H H 8.340 . . 77 9 9 ALA HA H 4.338 . . 78 9 9 ALA HB H 1.569 . . 79 9 9 ALA CA C 54.775 . . 80 9 9 ALA CB C 17.605 . . 81 9 9 ALA N N 125.043 . . 82 10 10 ALA H H 8.197 . . 83 10 10 ALA HA H 4.126 . . 84 10 10 ALA HB H 1.569 . . 85 10 10 ALA CA C 59.213 . . 86 10 10 ALA CB C 17.614 . . 87 10 10 ALA N N 119.743 . . 88 11 11 LYS H H 7.891 . . 89 11 11 LYS HA H 4.125 . . 90 11 11 LYS HB2 H 2.017 . . 91 11 11 LYS HB3 H 1.925 . . 92 11 11 LYS HG2 H 1.676 . . 93 11 11 LYS HD2 H 1.764 . . 94 11 11 LYS HE2 H 3.040 . . 95 11 11 LYS HE3 H 2.954 . . 96 11 11 LYS CA C 59.272 . . 97 11 11 LYS CB C 32.178 . . 98 11 11 LYS CG C 24.787 . . 99 11 11 LYS CD C 29.431 . . 100 11 11 LYS CE C 42.028 . . 101 11 11 LYS N N 116.888 . . 102 12 12 ASP H H 8.044 . . 103 12 12 ASP HA H 4.635 . . 104 12 12 ASP HB2 H 2.928 . . 105 12 12 ASP HB3 H 2.835 . . 106 12 12 ASP CA C 56.926 . . 107 12 12 ASP CB C 40.785 . . 108 12 12 ASP N N 121.128 . . 109 13 13 ILE H H 8.480 . . 110 13 13 ILE HA H 3.834 . . 111 13 13 ILE HB H 1.987 . . 112 13 13 ILE HG12 H 1.834 . . 113 13 13 ILE HG13 H 1.162 . . 114 13 13 ILE HG2 H 0.999 . . 115 13 13 ILE HD1 H 0.901 . . 116 13 13 ILE CA C 65.266 . . 117 13 13 ILE CB C 38.296 . . 118 13 13 ILE CG1 C 28.916 . . 119 13 13 ILE CG2 C 16.434 . . 120 13 13 ILE CD1 C 12.137 . . 121 13 13 ILE N N 122.482 . . 122 14 14 ALA H H 8.403 . . 123 14 14 ALA HA H 4.124 . . 124 14 14 ALA HB H 1.569 . . 125 14 14 ALA CA C 55.372 . . 126 14 14 ALA CB C 17.614 . . 127 14 14 ALA N N 122.009 . . 128 15 15 GLY H H 8.263 . . 129 15 15 GLY HA2 H 3.976 . . 130 15 15 GLY HA3 H 3.897 . . 131 15 15 GLY CA C 46.760 . . 132 15 15 GLY N N 103.563 . . 133 16 16 HIS H H 8.151 . . 134 16 16 HIS HA H 4.426 . . 135 16 16 HIS HB2 H 3.350 . . 136 16 16 HIS HD2 H 7.059 . . 137 16 16 HIS CA C 59.841 . . 138 16 16 HIS CB C 29.267 . . 139 16 16 HIS N N 121.467 . . 140 17 17 LEU H H 8.618 . . 141 17 17 LEU HA H 4.131 . . 142 17 17 LEU HB2 H 1.933 . . 143 17 17 LEU HB3 H 1.650 . . 144 17 17 LEU HG H 1.878 . . 145 17 17 LEU HD1 H 0.945 . . 146 17 17 LEU HD2 H 0.924 . . 147 17 17 LEU CA C 55.374 . . 148 17 17 LEU CB C 41.680 . . 149 17 17 LEU CG C 26.744 . . 150 17 17 LEU CD1 C 24.153 . . 151 17 17 LEU CD2 C 24.592 . . 152 17 17 LEU N N 121.214 . . 153 18 18 ALA H H 8.535 . . 154 18 18 ALA HA H 4.098 . . 155 18 18 ALA HB H 1.547 . . 156 18 18 ALA CA C 59.579 . . 157 18 18 ALA CB C 17.634 . . 158 18 18 ALA N N 120.603 . . 159 19 19 SER H H 7.850 . . 160 19 19 SER HA H 4.233 . . 161 19 19 SER HB2 H 4.052 . . 162 19 19 SER CA C 61.191 . . 163 19 19 SER CB C 63.177 . . 164 19 19 SER N N 110.985 . . 165 20 20 LYS H H 7.772 . . 166 20 20 LYS HA H 4.287 . . 167 20 20 LYS HB2 H 2.020 . . 168 20 20 LYS HG2 H 1.534 . . 169 20 20 LYS HD2 H 1.761 . . 170 20 20 LYS HD3 H 1.693 . . 171 20 20 LYS HE2 H 3.028 . . 172 20 20 LYS HE3 H 2.946 . . 173 20 20 LYS CA C 57.625 . . 174 20 20 LYS CB C 32.273 . . 175 20 20 LYS CG C 24.427 . . 176 20 20 LYS CD C 28.420 . . 177 20 20 LYS CE C 42.026 . . 178 20 20 LYS N N 121.357 . . 179 21 21 VAL H H 7.962 . . 180 21 21 VAL HA H 3.975 . . 181 21 21 VAL HB H 2.207 . . 182 21 21 VAL HG1 H 1.059 . . 183 21 21 VAL HG2 H 1.007 . . 184 21 21 VAL CA C 64.619 . . 185 21 21 VAL CB C 32.452 . . 186 21 21 VAL CG1 C 20.787 . . 187 21 21 VAL N N 117.392 . . 188 22 22 MET H H 8.119 . . 189 22 22 MET HA H 4.431 . . 190 22 22 MET HB2 H 2.183 . . 191 22 22 MET HB3 H 2.131 . . 192 22 22 MET HG2 H 2.698 . . 193 22 22 MET HG3 H 2.600 . . 194 22 22 MET CA C 55.966 . . 195 22 22 MET CB C 32.742 . . 196 22 22 MET CG C 32.274 . . 197 22 22 MET N N 118.290 . . stop_ save_