data_30218 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Ocellatin-LB2, solution structure in SDS micelle by NMR spectroscopy ; _BMRB_accession_number 30218 _BMRB_flat_file_name bmr30218.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" 111 "13C chemical shifts" 56 "15N chemical shifts" 6 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)' 30217 'Ocellatin LB1' 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-LB2 _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 2309.751 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 24 _Mol_residue_sequence ; GVVDILKGAAKDIAGHLASK VMNX ; 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 ASN 24 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-LB2, 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_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceIII _Field_strength 600 _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 4.133 . . 2 1 1 GLY HA3 H 4.047 . . 3 1 1 GLY CA C 43.746 . . 4 2 2 VAL H H 8.746 . . 5 2 2 VAL HA H 3.737 . . 6 2 2 VAL HB H 2.170 . . 7 2 2 VAL HG1 H 1.111 . . 8 2 2 VAL HG2 H 0.999 . . 9 2 2 VAL CA C 58.284 . . 10 2 2 VAL CB C 32.738 . . 11 2 2 VAL CG1 C 22.570 . . 12 2 2 VAL CG2 C 21.650 . . 13 2 2 VAL N N 120.851 . . 14 3 3 VAL H H 8.303 . . 15 3 3 VAL HA H 3.595 . . 16 3 3 VAL HB H 2.118 . . 17 3 3 VAL HG1 H 1.085 . . 18 3 3 VAL HG2 H 0.987 . . 19 3 3 VAL CA C 67.573 . . 20 3 3 VAL CB C 31.086 . . 21 3 3 VAL CG1 C 23.603 . . 22 3 3 VAL CG2 C 21.626 . . 23 4 4 ASP H H 7.594 . . 24 4 4 ASP HA H 4.356 . . 25 4 4 ASP HB2 H 2.859 . . 26 4 4 ASP HB3 H 2.817 . . 27 4 4 ASP N N 115.625 . . 28 5 5 ILE H H 7.683 . . 29 5 5 ILE HA H 3.891 . . 30 5 5 ILE HB H 2.073 . . 31 5 5 ILE HG12 H 1.714 . . 32 5 5 ILE HG13 H 1.292 . . 33 5 5 ILE HG2 H 0.940 . . 34 5 5 ILE HD1 H 0.871 . . 35 5 5 ILE CA C 60.813 . . 36 5 5 ILE CB C 37.888 . . 37 5 5 ILE CG1 C 28.939 . . 38 5 5 ILE CG2 C 17.890 . . 39 5 5 ILE CD1 C 13.107 . . 40 5 5 ILE N N 121.197 . . 41 6 6 LEU H H 8.191 . . 42 6 6 LEU HA H 4.046 . . 43 6 6 LEU HB2 H 1.948 . . 44 6 6 LEU HB3 H 1.522 . . 45 6 6 LEU HG H 1.923 . . 46 6 6 LEU HD1 H 0.880 . . 47 6 6 LEU HD2 H 0.842 . . 48 6 6 LEU CA C 58.166 . . 49 6 6 LEU CB C 41.932 . . 50 6 6 LEU CG C 26.901 . . 51 6 6 LEU CD1 C 25.922 . . 52 6 6 LEU CD2 C 23.122 . . 53 7 7 LYS H H 8.511 . . 54 7 7 LYS HA H 3.867 . . 55 7 7 LYS HB2 H 1.929 . . 56 7 7 LYS HG2 H 1.305 . . 57 7 7 LYS HD2 H 1.753 . . 58 7 7 LYS HE2 H 2.933 . . 59 7 7 LYS HE3 H 2.884 . . 60 7 7 LYS CB C 32.743 . . 61 7 7 LYS CD C 29.830 . . 62 7 7 LYS CE C 42.198 . . 63 7 7 LYS N N 117.901 . . 64 8 8 GLY H H 7.935 . . 65 8 8 GLY HA2 H 3.946 . . 66 8 8 GLY HA3 H 3.838 . . 67 9 9 ALA H H 8.389 . . 68 9 9 ALA HA H 4.232 . . 69 9 9 ALA HB H 1.524 . . 70 9 9 ALA CA C 54.993 . . 71 9 9 ALA CB C 18.566 . . 72 10 10 ALA H H 8.462 . . 73 10 10 ALA HA H 3.950 . . 74 10 10 ALA HB H 1.528 . . 75 10 10 ALA CA C 55.717 . . 76 10 10 ALA CB C 18.271 . . 77 11 11 LYS H H 8.092 . . 78 11 11 LYS HA H 3.939 . . 79 11 11 LYS HB2 H 1.970 . . 80 11 11 LYS HG2 H 1.646 . . 81 11 11 LYS HG3 H 1.471 . . 82 11 11 LYS HD2 H 1.760 . . 83 11 11 LYS HE2 H 2.995 . . 84 11 11 LYS CB C 32.193 . . 85 11 11 LYS CG C 25.621 . . 86 11 11 LYS CD C 29.298 . . 87 11 11 LYS CE C 42.369 . . 88 11 11 LYS N N 116.826 . . 89 12 12 ASP H H 8.058 . . 90 12 12 ASP HA H 4.527 . . 91 12 12 ASP HB2 H 3.167 . . 92 12 12 ASP HB3 H 2.977 . . 93 13 13 ILE H H 8.556 . . 94 13 13 ILE HA H 3.715 . . 95 13 13 ILE HB H 1.993 . . 96 13 13 ILE HG12 H 1.862 . . 97 13 13 ILE HG13 H 1.127 . . 98 13 13 ILE HG2 H 0.945 . . 99 13 13 ILE HD1 H 0.851 . . 100 13 13 ILE CA C 65.413 . . 101 13 13 ILE CB C 38.342 . . 102 13 13 ILE CG2 C 17.890 . . 103 13 13 ILE CD1 C 13.685 . . 104 13 13 ILE N N 119.304 . . 105 14 14 ALA H H 8.610 . . 106 14 14 ALA HA H 3.994 . . 107 14 14 ALA HB H 1.538 . . 108 14 14 ALA CA C 55.671 . . 109 14 14 ALA CB C 18.632 . . 110 15 15 GLY H H 8.323 . . 111 15 15 GLY HA2 H 4.049 . . 112 15 15 GLY HA3 H 3.878 . . 113 16 16 HIS H H 7.967 . . 114 16 16 HIS HA H 4.508 . . 115 16 16 HIS HB2 H 3.398 . . 116 16 16 HIS HD2 H 7.347 . . 117 16 16 HIS CB C 28.482 . . 118 17 17 LEU H H 8.420 . . 119 17 17 LEU HA H 4.146 . . 120 17 17 LEU HB2 H 1.909 . . 121 17 17 LEU HB3 H 1.599 . . 122 17 17 LEU HG H 1.862 . . 123 17 17 LEU HD1 H 0.948 . . 124 17 17 LEU HD2 H 0.918 . . 125 17 17 LEU CA C 57.668 . . 126 17 17 LEU CB C 42.139 . . 127 17 17 LEU CG C 27.138 . . 128 17 17 LEU CD1 C 25.538 . . 129 17 17 LEU CD2 C 23.793 . . 130 18 18 ALA H H 8.559 . . 131 18 18 ALA HA H 3.991 . . 132 18 18 ALA HB H 1.527 . . 133 18 18 ALA CA C 55.824 . . 134 18 18 ALA CB C 18.092 . . 135 19 19 SER H H 7.791 . . 136 19 19 SER HA H 4.197 . . 137 19 19 SER HB2 H 3.993 . . 138 19 19 SER HB3 H 3.958 . . 139 19 19 SER CA C 58.016 . . 140 19 19 SER CB C 63.170 . . 141 20 20 LYS H H 7.700 . . 142 20 20 LYS HA H 4.178 . . 143 20 20 LYS HB2 H 1.995 . . 144 20 20 LYS HG2 H 1.523 . . 145 20 20 LYS HG3 H 1.451 . . 146 20 20 LYS HE2 H 2.995 . . 147 20 20 LYS CA C 57.742 . . 148 20 20 LYS CB C 32.855 . . 149 20 20 LYS CG C 24.811 . . 150 20 20 LYS CE C 42.354 . . 151 21 21 VAL H H 7.817 . . 152 21 21 VAL HA H 3.940 . . 153 21 21 VAL HB H 2.169 . . 154 21 21 VAL HG1 H 1.040 . . 155 21 21 VAL HG2 H 0.977 . . 156 21 21 VAL CA C 58.035 . . 157 21 21 VAL CB C 32.104 . . 158 21 21 VAL CG1 C 21.717 . . 159 22 22 MET H H 8.112 . . 160 22 22 MET HA H 4.369 . . 161 22 22 MET HB2 H 2.680 . . 162 22 22 MET HB3 H 2.576 . . 163 22 22 MET HG2 H 2.161 . . 164 22 22 MET HG3 H 2.059 . . 165 22 22 MET CA C 58.035 . . 166 22 22 MET CB C 32.634 . . 167 22 22 MET CG C 33.027 . . 168 23 23 ASN H H 7.951 . . 169 23 23 ASN HA H 4.697 . . 170 23 23 ASN HB2 H 2.860 . . 171 23 23 ASN HB3 H 2.799 . . 172 23 23 ASN HD21 H 7.569 . . 173 23 23 ASN HD22 H 6.886 . . stop_ save_