data_15827 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of antimicrobial peptide MSI-594, derived from Magainin-2 and Malittin, in the presence of LPS. ; _BMRB_accession_number 15827 _BMRB_flat_file_name bmr15827.str _Entry_type original _Submission_date 2008-06-26 _Accession_date 2008-06-26 _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 Bhunia Anirban . . 2 Bhattacharjya Surajit . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 110 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-27 update BMRB 'update entity/assembly name' 2009-06-15 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19180607 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhunia Anirban . . 2 Ramamoorthy Ayyalusamy . . 3 Bhattacharjya Surajit . . stop_ _Journal_abbreviation Chemistry _Journal_volume 15 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2036 _Page_last 2040 _Year 2009 _Details . loop_ _Keyword 'antimicrobial peptide' LPS MSI-594 NMR trNOE stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name MSI-594 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MSI-594 $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MSI-594 _Molecular_mass 2447.125 _Mol_thiol_state 'not present' loop_ _Biological_function 'Antimicrobial peptide' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 24 _Mol_residue_sequence ; GIGKFLKKAKKGIGAVLKVL TTGL ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ILE 3 GLY 4 LYS 5 PHE 6 LEU 7 LYS 8 LYS 9 ALA 10 LYS 11 LYS 12 GLY 13 ILE 14 GLY 15 ALA 16 VAL 17 LEU 18 LYS 19 VAL 20 LEU 21 THR 22 THR 23 GLY 24 LEU 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 PDB 2K98 "Helical Hairpin Structure Of Potent Antimicrobial Peptide Msi-594 In The Presence Of Lipopolysaccharide Micelle" 100.00 24 100.00 100.00 1.96e-04 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 . . . . F-moc "solid phase peptide synthesis" stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity 'chemical synthesis' . solid "phase peptide synthesis" . 'Solid phase peptide synthesis' 'Standard F-moc solid phase peptide 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 $entity 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Guntert, Braun and Wuthrich' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details 'equipped with cryo-probe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_transferred_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H transferred 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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 . pH temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $DYANA stop_ loop_ _Experiment_label '2D 1H-1H transferred NOESY' '2D 1H-1H TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name MSI-594 _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 3.78 0.020 2 2 1 1 GLY HA3 H 3.78 0.020 2 3 2 2 ILE H H 8.54 0.020 1 4 2 2 ILE HA H 4.27 0.020 1 5 2 2 ILE HB H 1.90 0.020 1 6 2 2 ILE HD1 H 0.95 0.020 1 7 2 2 ILE HG12 H 1.47 0.020 2 8 2 2 ILE HG2 H 1.22 0.020 1 9 3 3 GLY H H 8.48 0.020 1 10 3 3 GLY HA2 H 3.95 0.020 2 11 3 3 GLY HA3 H 3.88 0.020 2 12 4 4 LYS H H 8.16 0.020 1 13 4 4 LYS HA H 4.33 0.020 1 14 4 4 LYS HB2 H 1.64 0.020 2 15 4 4 LYS HB3 H 1.64 0.020 2 16 4 4 LYS HE3 H 3.00 0.020 2 17 4 4 LYS HG3 H 1.46 0.020 2 18 5 5 PHE H H 8.26 0.020 1 19 5 5 PHE HA H 4.64 0.020 1 20 5 5 PHE HB2 H 3.14 0.020 2 21 5 5 PHE HB3 H 3.00 0.020 2 22 5 5 PHE HD1 H 7.24 0.020 1 23 5 5 PHE HE1 H 7.35 0.020 1 24 5 5 PHE HZ H 7.31 0.020 1 25 6 6 LEU H H 8.13 0.020 1 26 6 6 LEU HA H 4.35 0.020 1 27 6 6 LEU HB3 H 1.56 0.020 2 28 6 6 LEU HD1 H 0.92 0.020 2 29 6 6 LEU HD2 H 0.92 0.020 2 30 7 7 LYS H H 8.32 0.020 1 31 7 7 LYS HA H 4.33 0.020 1 32 7 7 LYS HB2 H 1.75 0.020 2 33 7 7 LYS HB3 H 1.75 0.020 2 34 7 7 LYS HE3 H 2.99 0.020 2 35 8 8 LYS H H 8.27 0.020 1 36 8 8 LYS HA H 4.25 0.020 1 37 8 8 LYS HB2 H 1.71 0.020 2 38 8 8 LYS HB3 H 1.71 0.020 2 39 8 8 LYS HE3 H 3.00 0.020 2 40 8 8 LYS HG3 H 1.56 0.020 2 41 9 9 ALA H H 8.36 0.020 1 42 9 9 ALA HA H 4.32 0.020 1 43 9 9 ALA HB H 1.37 0.020 1 44 10 10 LYS H H 8.27 0.020 1 45 10 10 LYS HA H 4.26 0.020 1 46 10 10 LYS HB2 H 1.80 0.020 2 47 10 10 LYS HB3 H 1.80 0.020 2 48 10 10 LYS HG3 H 1.61 0.020 2 49 11 11 LYS H H 8.33 0.020 1 50 11 11 LYS HA H 4.32 0.020 1 51 11 11 LYS HB2 H 1.73 0.020 2 52 11 11 LYS HB3 H 1.73 0.020 2 53 11 11 LYS HE3 H 3.00 0.020 2 54 12 12 GLY H H 8.49 0.020 1 55 12 12 GLY HA2 H 4.02 0.020 2 56 12 12 GLY HA3 H 4.02 0.020 2 57 13 13 ILE H H 8.11 0.020 1 58 13 13 ILE HA H 4.22 0.020 1 59 13 13 ILE HB H 1.90 0.020 1 60 13 13 ILE HD1 H 0.93 0.020 1 61 13 13 ILE HG12 H 1.46 0.020 2 62 13 13 ILE HG2 H 1.21 0.020 1 63 14 14 GLY H H 8.51 0.020 1 64 14 14 GLY HA2 H 3.94 0.020 2 65 14 14 GLY HA3 H 3.94 0.020 2 66 15 15 ALA H H 8.13 0.020 1 67 15 15 ALA HA H 4.33 0.020 1 68 15 15 ALA HB H 1.36 0.020 1 69 16 16 VAL H H 8.17 0.020 1 70 16 16 VAL HA H 4.07 0.020 1 71 16 16 VAL HB H 2.05 0.020 1 72 16 16 VAL HG1 H 0.92 0.020 2 73 16 16 VAL HG2 H 0.92 0.020 2 74 17 17 LEU H H 8.33 0.020 1 75 17 17 LEU HA H 4.31 0.020 1 76 17 17 LEU HB3 H 1.60 0.020 2 77 17 17 LEU HD1 H 0.88 0.020 2 78 17 17 LEU HD2 H 0.88 0.020 2 79 18 18 LYS H H 8.39 0.020 1 80 18 18 LYS HA H 4.30 0.020 1 81 18 18 LYS HB2 H 1.76 0.020 2 82 18 18 LYS HB3 H 1.76 0.020 2 83 18 18 LYS HE3 H 3.00 0.020 2 84 18 18 LYS HG3 H 1.45 0.020 2 85 19 19 VAL H H 8.20 0.020 1 86 19 19 VAL HA H 4.09 0.020 1 87 19 19 VAL HB H 2.04 0.020 1 88 19 19 VAL HG1 H 0.93 0.020 2 89 19 19 VAL HG2 H 0.93 0.020 2 90 20 20 LEU H H 8.47 0.020 1 91 20 20 LEU HA H 4.48 0.020 1 92 20 20 LEU HB3 H 1.65 0.020 2 93 20 20 LEU HD1 H 0.90 0.020 2 94 20 20 LEU HD2 H 0.90 0.020 2 95 21 21 THR H H 8.20 0.020 1 96 21 21 THR HA H 4.43 0.020 1 97 21 21 THR HB H 4.26 0.020 1 98 21 21 THR HG2 H 1.21 0.020 1 99 22 22 THR H H 8.14 0.020 1 100 22 22 THR HA H 4.36 0.020 1 101 22 22 THR HB H 4.25 0.020 1 102 22 22 THR HG2 H 1.21 0.020 1 103 23 23 GLY H H 8.46 0.020 1 104 23 23 GLY HA2 H 3.94 0.020 2 105 23 23 GLY HA3 H 3.94 0.020 2 106 24 24 LEU H H 8.15 0.020 1 107 24 24 LEU HA H 4.31 0.020 1 108 24 24 LEU HB3 H 1.64 0.020 2 109 24 24 LEU HD1 H 0.93 0.020 2 110 24 24 LEU HD2 H 0.93 0.020 2 stop_ save_