data_6618 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shift assignments for peptide P6 ; _BMRB_accession_number 6618 _BMRB_flat_file_name bmr6618.str _Entry_type original _Submission_date 2005-05-03 _Accession_date 2005-05-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'structure was calculated from NMR data' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Martins Rafael M. . 2 Sforca Mauricio L. . 3 Amino Rogerio . . 4 Juliano Maria A. . 5 Juliano Luiz . . 6 Pertinhez Thelma A. . 7 Spisni Alberto . . 8 Schenkman Sergio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 161 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-08-07 original author . stop_ _Original_release_date 2006-08-07 save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _Citation_title ; Lytic Activity and Structural Differences of Amphipathic Peptides Derived from Trialysin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16460023 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Martins Rafael M. . 2 Sforca Mauricio L. . 3 Amino Rogerio . . 4 Juliano Maria A. . 5 Oyama Sergio . Jr. 6 Juliano Luiz . . 7 Pertinhez Thelma A. . 8 Spisni Alberto . . 9 Schenkman Sergio . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 45 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1765 _Page_last 1774 _Year 2006 _Details . loop_ _Keyword 'lytic peptide' NMR 'trialysin N-terminus' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'peptide P6' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'peptide P6' $trialysin_N-terminal_peptide_(F1-V32) stop_ _System_molecular_weight 3510.4 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'lytic peptide' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_trialysin_N-terminal_peptide_(F1-V32) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common P6 _Molecular_mass 3510.4 _Mol_thiol_state 'not present' loop_ _Biological_function antimicrobial anti-protozoan 'cytolytic peptide' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; FKIKPGKVLDKFGKIVGKVL KQLKKVSAVAKV ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 LYS 3 ILE 4 LYS 5 PRO 6 GLY 7 LYS 8 VAL 9 LEU 10 ASP 11 LYS 12 PHE 13 GLY 14 LYS 15 ILE 16 VAL 17 GLY 18 LYS 19 VAL 20 LEU 21 LYS 22 GLN 23 LEU 24 LYS 25 LYS 26 VAL 27 SER 28 ALA 29 VAL 30 ALA 31 LYS 32 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 BMRB 6616 trialysin_N-terminal_peptide_(G6-V32) 84.38 27 100.00 100.00 4.49e-06 BMRB 6619 trialysin_N-terminal_peptide_(F1-S27) 84.38 27 100.00 100.00 9.49e-07 GB AAL82380 "trialysin [Triatoma infestans]" 100.00 205 100.00 100.00 1.65e-09 GB ABR27919 "trialysin precursor allele [Triatoma infestans]" 100.00 260 100.00 100.00 2.51e-09 GB ABR27943 "trialysin allele [Triatoma infestans]" 100.00 260 100.00 100.00 2.46e-09 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Secretion _Gene_mnemonic _Details $trialysin_N-terminal_peptide_(F1-V32) 'Triatoma infestans' 30076 Eukaryota Metazoa Triatoma infestans 'salivary glands' salivary trialysin 'synthetic peptide based on the N-terminus of a salivary lytic protein from Triatoma infestans' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Organ _Vector_name $trialysin_N-terminal_peptide_(F1-V32) 'chemical synthesis' 'Triatoma infestans' Triatoma infestans . 'salivary secretion' . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1.2 mM P6 in TFE: H2O (30:70) (v/v) containing 5% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $trialysin_N-terminal_peptide_(F1-V32) 1.2 mM . TFE 30 '% (vol)' . D2O 5 '% (vol)' . H2O 65 '% (vol)' . stop_ save_ ############################ # Computer software used # ############################ save_NMRView5 _Saveframe_category software _Name NMRView5 _Version 5 loop_ _Vendor _Address _Electronic_address 'One Moon Scientific Inc.' . www.onemoonscientific.com stop_ loop_ _Task 'chemical shift assignment' 'spectrum analysis' stop_ _Details ; Johnson, B. A., and Blevins, R.A. (1994), Journal of Biomolecular NMR, 4:603-614. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_500MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H TOCSY' _Sample_label $sample_1 save_ save_1H_COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H COSY' _Sample_label $sample_1 save_ save_1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H NOESY' _Sample_label $sample_1 save_ save_1H_ROESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H ROESY' _Sample_label $sample_1 save_ save_1H_TOCSY _Saveframe_category NMR_applied_experiment _Experiment_name 1H_TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_1H_COSY _Saveframe_category NMR_applied_experiment _Experiment_name 1H_COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_1H_NOESY _Saveframe_category NMR_applied_experiment _Experiment_name 1H_NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_1H_ROESY _Saveframe_category NMR_applied_experiment _Experiment_name 1H_ROESY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_P6_conditions _Saveframe_category sample_conditions _Details '37 C' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4 0.2 pH temperature 310 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $citations $citations 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRView5 stop_ loop_ _Experiment_label '1H TOCSY' '1H COSY' '1H NOESY' '1H ROESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $P6_conditions _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'peptide P6' _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 PHE HA H 4.330 0.02 1 2 1 1 PHE HB2 H 3.570 0.02 2 3 1 1 PHE HB3 H 3.290 0.02 2 4 1 1 PHE HD1 H 7.301 0.02 3 5 1 1 PHE HE1 H 7.400 0.02 3 6 2 2 LYS H H 8.368 0.02 1 7 2 2 LYS HA H 4.446 0.02 1 8 2 2 LYS HB2 H 1.726 0.02 2 9 2 2 LYS HB3 H 1.818 0.02 2 10 2 2 LYS HG2 H 1.427 0.02 2 11 2 2 LYS HE2 H 2.992 0.02 2 12 3 3 ILE H H 7.869 0.02 1 13 3 3 ILE HA H 4.210 0.02 1 14 3 3 ILE HB H 1.820 0.02 1 15 3 3 ILE HG12 H 1.201 0.02 1 16 3 3 ILE HG13 H 1.518 0.02 1 17 3 3 ILE HD1 H 0.924 0.02 1 18 4 4 LYS H H 7.966 0.02 1 19 4 4 LYS HA H 4.714 0.02 1 20 4 4 LYS HB2 H 1.771 0.02 2 21 4 4 LYS HB3 H 1.891 0.02 2 22 4 4 LYS HG2 H 1.530 0.02 2 23 4 4 LYS HE2 H 3.039 0.02 2 24 5 5 PRO HA H 4.374 0.02 1 25 5 5 PRO HB2 H 2.114 0.02 2 26 5 5 PRO HB3 H 2.295 0.02 2 27 5 5 PRO HG2 H 2.007 0.02 2 28 5 5 PRO HD2 H 3.726 0.02 2 29 5 5 PRO HD3 H 3.874 0.02 2 30 6 6 GLY H H 8.237 0.02 1 31 6 6 GLY HA2 H 3.975 0.02 2 32 7 7 LYS H H 8.038 0.02 1 33 7 7 LYS HA H 4.305 0.02 1 34 7 7 LYS HB2 H 1.772 0.02 2 35 7 7 LYS HB3 H 1.936 0.02 2 36 7 7 LYS HG2 H 1.583 0.02 2 37 7 7 LYS HE2 H 3.062 0.02 2 38 8 8 VAL H H 7.740 0.02 1 39 8 8 VAL HA H 3.950 0.02 1 40 8 8 VAL HB H 2.192 0.02 1 41 8 8 VAL HG1 H 0.989 0.02 2 42 8 8 VAL HG2 H 1.038 0.02 2 43 9 9 LEU H H 7.952 0.02 1 44 9 9 LEU HA H 4.259 0.02 1 45 9 9 LEU HB2 H 1.684 0.02 2 46 9 9 LEU HD1 H 0.962 0.02 2 47 9 9 LEU HD2 H 0.915 0.02 2 48 10 10 ASP H H 8.085 0.02 1 49 10 10 ASP HA H 4.539 0.02 1 50 10 10 ASP HB2 H 2.888 0.02 2 51 10 10 ASP HB3 H 2.945 0.02 2 52 11 11 LYS H H 7.824 0.02 1 53 11 11 LYS HA H 4.165 0.02 1 54 11 11 LYS HB2 H 1.679 0.02 2 55 11 11 LYS HB3 H 1.866 0.02 2 56 11 11 LYS HG2 H 1.350 0.02 2 57 11 11 LYS HE2 H 2.996 0.02 2 58 12 12 PHE H H 8.239 0.02 1 59 12 12 PHE HA H 4.487 0.02 1 60 12 12 PHE HB2 H 3.157 0.02 2 61 12 12 PHE HB3 H 3.228 0.02 2 62 12 12 PHE HD1 H 7.235 0.02 3 63 12 12 PHE HE1 H 7.297 0.02 3 64 13 13 GLY H H 8.442 0.02 1 65 13 13 GLY HA2 H 3.786 0.02 2 66 13 13 GLY HA3 H 4.004 0.02 2 67 14 14 LYS H H 7.841 0.02 1 68 14 14 LYS HA H 4.211 0.02 1 69 14 14 LYS HB2 H 1.753 0.02 2 70 14 14 LYS HB3 H 2.031 0.02 2 71 14 14 LYS HG2 H 1.518 0.02 2 72 14 14 LYS HD2 H 1.940 0.02 2 73 14 14 LYS HE2 H 3.038 0.02 2 74 15 15 ILE H H 7.711 0.02 1 75 15 15 ILE HA H 3.930 0.02 1 76 15 15 ILE HB H 2.031 0.02 1 77 15 15 ILE HG12 H 1.236 0.02 1 78 15 15 ILE HG13 H 1.714 0.02 1 79 15 15 ILE HD1 H 0.944 0.02 1 80 16 16 VAL H H 8.086 0.02 1 81 16 16 VAL HA H 3.584 0.02 1 82 16 16 VAL HB H 1.931 0.02 1 83 16 16 VAL HG1 H 0.849 0.02 2 84 16 16 VAL HG2 H 0.888 0.02 2 85 17 17 GLY H H 8.045 0.02 1 86 17 17 GLY HA2 H 3.812 0.02 2 87 17 17 GLY HA3 H 3.885 0.02 2 88 18 18 LYS H H 7.553 0.02 1 89 18 18 LYS HA H 4.142 0.02 1 90 18 18 LYS HB2 H 1.752 0.02 2 91 18 18 LYS HB3 H 2.061 0.02 2 92 18 18 LYS HG2 H 1.506 0.02 2 93 18 18 LYS HE2 H 3.039 0.02 2 94 19 19 VAL H H 8.027 0.02 1 95 19 19 VAL HA H 3.681 0.02 1 96 19 19 VAL HB H 2.265 0.02 1 97 19 19 VAL HG1 H 0.960 0.02 2 98 19 19 VAL HG2 H 1.057 0.02 2 99 20 20 LEU H H 8.555 0.02 1 100 20 20 LEU HA H 4.083 0.02 1 101 20 20 LEU HB2 H 1.898 0.02 2 102 20 20 LEU HG H 1.538 0.02 1 103 20 20 LEU HD1 H 0.884 0.02 2 104 21 21 LYS H H 7.710 0.02 1 105 21 21 LYS HA H 4.024 0.02 1 106 21 21 LYS HB2 H 1.750 0.02 2 107 21 21 LYS HB3 H 1.980 0.02 2 108 21 21 LYS HG2 H 1.480 0.02 2 109 21 21 LYS HE2 H 3.034 0.02 2 110 22 22 GLN H H 7.903 0.02 1 111 22 22 GLN HA H 4.245 0.02 1 112 22 22 GLN HB2 H 2.320 0.02 2 113 22 22 GLN HB3 H 2.267 0.02 2 114 22 22 GLN HG2 H 2.575 0.02 2 115 23 23 LEU H H 8.598 0.02 1 116 23 23 LEU HA H 4.165 0.02 1 117 23 23 LEU HB2 H 1.913 0.02 2 118 23 23 LEU HG H 1.608 0.02 1 119 23 23 LEU HD1 H 0.894 0.02 2 120 23 23 LEU HD2 H 0.870 0.02 2 121 24 24 LYS H H 8.182 0.02 1 122 24 24 LYS HA H 4.060 0.02 1 123 24 24 LYS HB2 H 1.730 0.02 2 124 24 24 LYS HB3 H 1.991 0.02 2 125 24 24 LYS HG2 H 1.538 0.02 2 126 25 25 LYS H H 7.710 0.02 1 127 25 25 LYS HA H 4.189 0.02 1 128 25 25 LYS HB2 H 1.634 0.02 2 129 25 25 LYS HB3 H 2.047 0.02 2 130 25 25 LYS HG2 H 1.500 0.02 2 131 25 25 LYS HE2 H 3.034 0.02 2 132 26 26 VAL H H 8.174 0.02 1 133 26 26 VAL HA H 3.907 0.02 1 134 26 26 VAL HB H 2.241 0.02 1 135 26 26 VAL HG1 H 1.007 0.02 2 136 26 26 VAL HG2 H 1.102 0.02 2 137 27 27 SER H H 8.113 0.02 1 138 27 27 SER HA H 4.284 0.02 1 139 27 27 SER HB2 H 3.989 0.02 2 140 27 27 SER HB3 H 4.033 0.02 2 141 28 28 ALA H H 7.705 0.02 1 142 28 28 ALA HA H 4.329 0.02 1 143 28 28 ALA HB H 1.557 0.02 1 144 29 29 VAL H H 7.758 0.02 1 145 29 29 VAL HA H 4.046 0.02 1 146 29 29 VAL HB H 2.232 0.02 1 147 29 29 VAL HG1 H 1.002 0.02 2 148 29 29 VAL HG2 H 1.060 0.02 2 149 30 30 ALA H H 8.051 0.02 1 150 30 30 ALA HA H 4.294 0.02 1 151 30 30 ALA HB H 1.463 0.02 1 152 31 31 LYS H H 7.805 0.02 1 153 31 31 LYS HA H 4.328 0.02 1 154 31 31 LYS HB2 H 1.772 0.02 2 155 31 31 LYS HB3 H 1.936 0.02 2 156 31 31 LYS HG2 H 1.583 0.02 2 157 31 31 LYS HE2 H 3.049 0.02 2 158 32 32 VAL H H 7.742 0.02 1 159 32 32 VAL HA H 4.141 0.02 1 160 32 32 VAL HB H 2.160 0.02 1 161 32 32 VAL HG2 H 1.008 0.02 2 stop_ save_