data_30217 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Ocellatin-LB1, solution structure in SDS micelle by NMR spectroscopy ; _BMRB_accession_number 30217 _BMRB_flat_file_name bmr30217.str _Entry_type original _Submission_date 2016-12-19 _Accession_date 2016-12-19 _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 'dos Santos' D. M. . 3 Santos V. M. . 4 Pilo-Veloso D. . . 5 'de Lima' M. E. . 6 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" 106 "13C chemical shifts" 59 "15N chemical shifts" 18 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-03-24 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 30211 'Ocellatin LB1' 30212 'Ocellatin LB2' 30213 'Ocellatin F1' 30214 'Ocellatin LB1' 30215 Ocellatin-LB2 30216 'Ocellatin K1 (26)' 30218 'Ocellatin LB2' 30219 'Ocellatin F1' stop_ _Original_release_date 2017-03-22 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 'dos Santos' D. M. . 3 Santos V. M. . 4 Pilo-Veloso D. . . 5 'de Lima' M. E. . 6 Resende J. M. . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD 0353 _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-LB1 _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 'frogs and toads' 326590 Eukaryota Metazoa Leptodactylus labyrinthicus 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 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '2 mM Ocellatin-LB1, 1 mM DSS, 400 mM d-25 SDS, 5 % 99.75 D2O, 95% H2O/5% D2O.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling D2O 5 % '[U-99.75 2H]' DSS 1 mM 'natural abundance' $entity_1 2 mM 'natural abundance' SDS 400 mM d-25 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, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_software_3 _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ save_software_4 _Saveframe_category software _Name Procheck _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' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'geometry optimization' 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 800 _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_ 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_HMQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HMQC' _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 4 . pH pressure 1 . atm temperature 303.15 . 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 protons' ppm 0.000 internal indirect . . . 0.25144953 DSS 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' '2D 1H-13C HSQC' '2D 1H-15N HMQC' 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 4.130 . . 2 1 1 GLY HA3 H 4.036 . . 3 1 1 GLY CA C 43.455 . . 4 2 2 VAL H H 8.741 . . 5 2 2 VAL HA H 3.751 . . 6 2 2 VAL HB H 2.171 . . 7 2 2 VAL HG1 H 1.105 . . 8 2 2 VAL HG2 H 0.999 . . 9 2 2 VAL CA C 66.078 . . 10 2 2 VAL CB C 31.817 . . 11 2 2 VAL CG1 C 23.385 . . 12 2 2 VAL CG2 C 21.362 . . 13 2 2 VAL N N 120.745 . . 14 3 3 VAL H H 8.241 . . 15 3 3 VAL HA H 3.590 . . 16 3 3 VAL HB H 2.128 . . 17 3 3 VAL HG1 H 1.087 . . 18 3 3 VAL HG2 H 0.985 . . 19 3 3 VAL CB C 30.823 . . 20 3 3 VAL CG1 C 23.180 . . 21 3 3 VAL CG2 C 21.478 . . 22 3 3 VAL N N 118.916 . . 23 4 4 ASP H H 7.714 . . 24 4 4 ASP HA H 4.389 . . 25 4 4 ASP HB2 H 2.916 . . 26 4 4 ASP CB C 38.624 . . 27 4 4 ASP N N 117.393 . . 28 5 5 ILE H H 7.696 . . 29 5 5 ILE HA H 3.900 . . 30 5 5 ILE HB H 2.069 . . 31 5 5 ILE HG12 H 1.707 . . 32 5 5 ILE HG13 H 1.291 . . 33 5 5 ILE HG2 H 0.943 . . 34 5 5 ILE HD1 H 0.878 . . 35 5 5 ILE CA C 63.962 . . 36 5 5 ILE CB C 37.651 . . 37 5 5 ILE CG1 C 28.564 . . 38 5 5 ILE CG2 C 17.434 . . 39 5 5 ILE CD1 C 12.858 . . 40 5 5 ILE N N 121.165 . . 41 6 6 LEU H H 8.177 . . 42 6 6 LEU HA H 4.046 . . 43 6 6 LEU HB2 H 1.956 . . 44 6 6 LEU HB3 H 1.517 . . 45 6 6 LEU HG H 1.912 . . 46 6 6 LEU HD1 H 0.879 . . 47 6 6 LEU HD2 H 0.838 . . 48 6 6 LEU CA C 57.880 . . 49 6 6 LEU CB C 41.565 . . 50 6 6 LEU CG C 26.552 . . 51 6 6 LEU CD1 C 25.594 . . 52 6 6 LEU CD2 C 22.849 . . 53 6 6 LEU N N 120.041 . . 54 7 7 LYS H H 8.492 . . 55 7 7 LYS HA H 3.873 . . 56 7 7 LYS HB2 H 1.926 . . 57 7 7 LYS HG2 H 1.320 . . 58 7 7 LYS HD2 H 1.744 . . 59 7 7 LYS HE2 H 2.940 . . 60 7 7 LYS HE3 H 2.905 . . 61 7 7 LYS CA C 60.616 . . 62 7 7 LYS CB C 32.372 . . 63 7 7 LYS CD C 29.527 . . 64 7 7 LYS CE C 41.900 . . 65 7 7 LYS N N 117.818 . . 66 8 8 GLY H H 7.933 . . 67 8 8 GLY HA2 H 3.944 . . 68 8 8 GLY HA3 H 3.836 . . 69 8 8 GLY N N 105.894 . . 70 9 9 ALA H H 8.397 . . 71 9 9 ALA HA H 4.223 . . 72 9 9 ALA HB H 1.523 . . 73 9 9 ALA CA C 54.668 . . 74 9 9 ALA CB C 18.413 . . 75 10 10 ALA H H 8.464 . . 76 10 10 ALA HA H 3.954 . . 77 10 10 ALA HB H 1.528 . . 78 10 10 ALA CA C 55.364 . . 79 10 10 ALA CB C 18.130 . . 80 10 10 ALA N N 119.916 . . 81 11 11 LYS H H 8.089 . . 82 11 11 LYS HA H 3.938 . . 83 11 11 LYS HB2 H 1.971 . . 84 11 11 LYS HB3 H 1.755 . . 85 11 11 LYS HG2 H 1.645 . . 86 11 11 LYS HG3 H 1.467 . . 87 11 11 LYS HD2 H 1.531 . . 88 11 11 LYS HD3 H 1.764 . . 89 11 11 LYS HE2 H 2.994 . . 90 11 11 LYS CA C 59.676 . . 91 11 11 LYS CB C 31.893 . . 92 11 11 LYS CG C 25.332 . . 93 11 11 LYS CD C 29.096 . . 94 11 11 LYS CE C 42.023 . . 95 11 11 LYS N N 116.536 . . 96 12 12 ASP H H 8.067 . . 97 12 12 ASP HA H 4.531 . . 98 12 12 ASP HB2 H 3.175 . . 99 12 12 ASP HB3 H 2.988 . . 100 12 12 ASP CB C 37.336 . . 101 12 12 ASP N N 119.199 . . 102 13 13 ILE H H 8.557 . . 103 13 13 ILE HA H 3.714 . . 104 13 13 ILE HB H 1.991 . . 105 13 13 ILE HG12 H 1.118 . . 106 13 13 ILE HG2 H 0.939 . . 107 13 13 ILE HD1 H 0.842 . . 108 13 13 ILE CA C 65.147 . . 109 13 13 ILE CB C 38.049 . . 110 13 13 ILE CG1 C 22.230 . . 111 13 13 ILE CD1 C 13.412 . . 112 13 13 ILE N N 121.281 . . 113 14 14 ALA H H 8.609 . . 114 14 14 ALA HA H 4.001 . . 115 14 14 ALA HB H 1.543 . . 116 14 14 ALA CA C 55.594 . . 117 14 14 ALA CB C 18.359 . . 118 14 14 ALA N N 122.382 . . 119 15 15 GLY H H 8.320 . . 120 15 15 GLY HA2 H 4.043 . . 121 15 15 GLY HA3 H 3.884 . . 122 16 16 HIS H H 7.961 . . 123 16 16 HIS HA H 4.510 . . 124 16 16 HIS HB2 H 3.380 . . 125 16 16 HIS HD2 H 7.350 . . 126 16 16 HIS CA C 58.333 . . 127 16 16 HIS CB C 28.170 . . 128 16 16 HIS N N 119.338 . . 129 17 17 LEU H H 8.395 . . 130 17 17 LEU HA H 4.154 . . 131 17 17 LEU HB2 H 1.891 . . 132 17 17 LEU HB3 H 1.601 . . 133 17 17 LEU HG H 1.862 . . 134 17 17 LEU HD1 H 0.910 . . 135 17 17 LEU CA C 57.350 . . 136 17 17 LEU CB C 41.882 . . 137 17 17 LEU CG C 26.862 . . 138 17 17 LEU CD1 C 23.526 . . 139 17 17 LEU N N 120.458 . . 140 18 18 ALA H H 8.541 . . 141 18 18 ALA HA H 4.001 . . 142 18 18 ALA HB H 1.523 . . 143 18 18 ALA CA C 55.255 . . 144 18 18 ALA CB C 17.909 . . 145 18 18 ALA N N 120.692 . . 146 19 19 SER H H 7.797 . . 147 19 19 SER HA H 4.218 . . 148 19 19 SER HB2 H 4.009 . . 149 19 19 SER HB3 H 3.947 . . 150 19 19 SER CA C 60.723 . . 151 19 19 SER CB C 62.905 . . 152 19 19 SER N N 111.031 . . 153 20 20 LYS H H 7.689 . . 154 20 20 LYS HA H 4.207 . . 155 20 20 LYS HB2 H 1.983 . . 156 20 20 LYS HB3 H 1.859 . . 157 20 20 LYS HG2 H 1.519 . . 158 20 20 LYS HG3 H 1.462 . . 159 20 20 LYS HD2 H 1.752 . . 160 20 20 LYS HE2 H 2.991 . . 161 20 20 LYS CB C 32.522 . . 162 20 20 LYS CG C 24.529 . . 163 20 20 LYS CE C 41.967 . . 164 21 21 VAL H H 7.810 . . 165 21 21 VAL HA H 4.015 . . 166 21 21 VAL HB H 2.150 . . 167 21 21 VAL HG1 H 1.024 . . 168 21 21 VAL HG2 H 0.978 . . 169 21 21 VAL CA C 63.811 . . 170 21 21 VAL CB C 32.430 . . 171 21 21 VAL CG1 C 21.286 . . 172 21 21 VAL CG2 C 21.625 . . 173 21 21 VAL N N 115.880 . . 174 22 22 MET H H 8.002 . . 175 22 22 MET HA H 4.415 . . 176 22 22 MET HB2 H 2.669 . . 177 22 22 MET HB3 H 2.561 . . 178 22 22 MET HG2 H 2.157 . . 179 22 22 MET HG3 H 2.050 . . 180 22 22 MET CA C 55.671 . . 181 22 22 MET CB C 32.363 . . 182 22 22 MET CG C 32.739 . . 183 22 22 MET N N 118.554 . . stop_ save_