data_5188 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of paralytic peptide of the silkworm, Bombyx mori ; _BMRB_accession_number 5188 _BMRB_flat_file_name bmr5188.str _Entry_type original _Submission_date 2001-10-23 _Accession_date 2001-10-23 _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 Miura Kazunori . . 2 Kamimura Manabu . . 3 Aizawa Tomoyasu . . 4 Kiuchi Makoto . . 5 Hayakawa Yoichi . . 6 Mizuguchi Mineyuki . . 7 Kawano Keiichi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 109 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-02-20 original BMRB . stop_ _Original_release_date 2001-10-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of Paralytic Peptide of Silkworm, Bombyx mori ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22423982 _PubMed_ID 12535689 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miura Kazunori . . 2 Kamimura Manabu . . 3 Aizawa Tomoyasu . . 4 Kiuchi Makoto . . 5 Hayakawa Yoichi . . 6 Mizuguchi Mineyuki . . 7 Kawano Keiichi . . stop_ _Journal_abbreviation Peptides _Journal_volume 23 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2111 _Page_last 2116 _Year 2002 _Details . loop_ _Keyword BmPP 'Bombyx mori' 'Solution structure' 'growth blocking peptide' 'nuclear magnetic resonance' 'paralytic peptide' stop_ save_ ################################## # Molecular system description # ################################## save_system_BmPP _Saveframe_category molecular_system _Mol_system_name 'paralytic peptide of Bombyx mori' _Abbreviation_common BmPP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BmPP $BmPP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BmPP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'paralytic peptide of Bombyx mori' _Abbreviation_common BmPP _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 23 _Mol_residue_sequence ; ENFVGGCATGFKRTADGRCK PTF ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 ASN 3 PHE 4 VAL 5 GLY 6 GLY 7 CYS 8 ALA 9 THR 10 GLY 11 PHE 12 LYS 13 ARG 14 THR 15 ALA 16 ASP 17 GLY 18 ARG 19 CYS 20 LYS 21 PRO 22 THR 23 PHE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 PDB 1IRR 'Solution Structure Of Paralytic Peptide Of The Silkworm, Bombyx Mori' 100.00 23 100.00 100.00 1.19e-04 DBJ BAB69463 'paralytic peptide [Bombyx mori]' 100.00 131 100.00 100.00 3.32e-05 REF NP_001036883 'paralytic peptide [Bombyx mori]' 100.00 131 100.00 100.00 3.32e-05 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BmPP Silkworm 7091 Eukaryota Metazoa Bombyx mori 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 $BmPP 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BmPP 4.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task 'raw spectral data processing' stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version 4.3.2 loop_ _Task 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 0.2 n/a temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H 1 'methyl protons' ppm 0.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label DQF-COSY NOESY TOCSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name BmPP _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 GLU HA H 3.99 0.03 1 2 . 1 GLU HB2 H 1.98 0.03 2 3 . 1 GLU HB3 H 2.25 0.03 2 4 . 2 ASN H H 8.80 0.03 1 5 . 2 ASN HA H 4.74 0.03 1 6 . 2 ASN HB2 H 2.68 0.03 2 7 . 2 ASN HB3 H 2.73 0.03 2 8 . 3 PHE H H 8.41 0.03 1 9 . 3 PHE HA H 4.68 0.03 1 10 . 3 PHE HB2 H 3.11 0.03 2 11 . 3 PHE HB3 H 2.99 0.03 2 12 . 4 VAL H H 8.23 0.03 1 13 . 4 VAL HA H 4.09 0.03 1 14 . 4 VAL HB H 2.05 0.03 1 15 . 4 VAL HG1 H 0.91 0.03 2 16 . 4 VAL HG2 H 0.90 0.03 2 17 . 5 GLY H H 8.23 0.03 1 18 . 5 GLY HA2 H 3.95 0.03 1 19 . 5 GLY HA3 H 3.95 0.03 1 20 . 6 GLY H H 8.21 0.03 1 21 . 6 GLY HA2 H 3.99 0.03 1 22 . 6 GLY HA3 H 3.99 0.03 1 23 . 7 CYS H H 8.25 0.03 1 24 . 7 CYS HA H 4.81 0.03 1 25 . 7 CYS HB2 H 3.08 0.03 2 26 . 7 CYS HB3 H 2.65 0.03 2 27 . 8 ALA H H 8.48 0.03 1 28 . 8 ALA HA H 4.25 0.03 1 29 . 8 ALA HB H 1.26 0.03 1 30 . 9 THR H H 8.17 0.03 1 31 . 9 THR HA H 4.07 0.03 1 32 . 9 THR HB H 4.10 0.03 1 33 . 9 THR HG2 H 1.29 0.03 1 34 . 10 GLY H H 8.92 0.03 1 35 . 10 GLY HA2 H 3.60 0.03 2 36 . 10 GLY HA3 H 4.25 0.03 2 37 . 11 PHE H H 8.38 0.03 1 38 . 11 PHE HA H 5.09 0.03 1 39 . 11 PHE HB2 H 2.55 0.03 2 40 . 11 PHE HB3 H 3.39 0.03 2 41 . 11 PHE HD1 H 6.86 0.03 1 42 . 11 PHE HD2 H 6.86 0.03 1 43 . 11 PHE HE1 H 7.36 0.03 1 44 . 11 PHE HE2 H 7.36 0.03 1 45 . 12 LYS H H 9.22 0.03 1 46 . 12 LYS HA H 4.64 0.03 1 47 . 12 LYS HB2 H 1.69 0.03 1 48 . 12 LYS HB3 H 1.69 0.03 1 49 . 12 LYS HG2 H 1.32 0.03 1 50 . 12 LYS HG3 H 1.32 0.03 1 51 . 12 LYS HD2 H 1.61 0.03 1 52 . 12 LYS HD3 H 1.61 0.03 1 53 . 13 ARG H H 8.61 0.03 1 54 . 13 ARG HA H 4.97 0.03 1 55 . 13 ARG HB2 H 1.80 0.03 1 56 . 13 ARG HB3 H 1.80 0.03 1 57 . 13 ARG HG2 H 1.60 0.03 1 58 . 13 ARG HG3 H 1.60 0.03 1 59 . 13 ARG HD2 H 3.08 0.03 1 60 . 13 ARG HD3 H 3.08 0.03 1 61 . 14 THR H H 8.93 0.03 1 62 . 14 THR HA H 4.61 0.03 1 63 . 14 THR HB H 4.62 0.03 1 64 . 14 THR HG2 H 1.24 0.03 1 65 . 15 ALA H H 8.85 0.03 1 66 . 15 ALA HA H 4.15 0.03 1 67 . 15 ALA HB H 1.49 0.03 1 68 . 16 ASP H H 8.09 0.03 1 69 . 16 ASP HA H 4.60 0.03 1 70 . 16 ASP HB2 H 2.65 0.03 2 71 . 16 ASP HB3 H 2.98 0.03 2 72 . 17 GLY H H 8.09 0.03 1 73 . 17 GLY HA2 H 3.56 0.03 2 74 . 17 GLY HA3 H 4.18 0.03 2 75 . 18 ARG H H 7.66 0.03 1 76 . 18 ARG HA H 4.49 0.03 1 77 . 18 ARG HB2 H 1.81 0.03 1 78 . 18 ARG HB3 H 1.81 0.03 1 79 . 18 ARG HG2 H 1.53 0.03 1 80 . 18 ARG HG3 H 1.53 0.03 1 81 . 18 ARG HD2 H 3.17 0.03 1 82 . 18 ARG HD3 H 3.17 0.03 1 83 . 19 CYS H H 8.58 0.03 1 84 . 19 CYS HA H 5.24 0.03 1 85 . 19 CYS HB2 H 2.78 0.03 2 86 . 19 CYS HB3 H 2.83 0.03 2 87 . 20 LYS H H 9.23 0.03 1 88 . 20 LYS HA H 5.07 0.03 1 89 . 20 LYS HB2 H 1.87 0.03 1 90 . 20 LYS HB3 H 1.87 0.03 1 91 . 20 LYS HG2 H 1.45 0.03 1 92 . 20 LYS HG3 H 1.45 0.03 1 93 . 20 LYS HD2 H 1.71 0.03 1 94 . 20 LYS HD3 H 1.71 0.03 1 95 . 21 PRO HA H 3.95 0.03 1 96 . 21 PRO HB2 H 1.54 0.03 2 97 . 21 PRO HB3 H 1.65 0.03 2 98 . 21 PRO HG2 H 1.85 0.03 2 99 . 21 PRO HG3 H 1.99 0.03 2 100 . 21 PRO HD2 H 3.70 0.03 2 101 . 21 PRO HD3 H 3.85 0.03 2 102 . 22 THR H H 7.94 0.03 1 103 . 22 THR HA H 4.05 0.03 1 104 . 22 THR HB H 4.11 0.03 1 105 . 22 THR HG2 H 0.98 0.03 1 106 . 23 PHE H H 7.36 0.03 1 107 . 23 PHE HA H 4.43 0.03 1 108 . 23 PHE HB2 H 2.99 0.03 2 109 . 23 PHE HB3 H 3.08 0.03 2 stop_ save_