data_6827 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure function relationships of the polyhistidine rich peptide LAH4 in micellar environment;pH dependent mode of antibiotic action and DNA transfection ; _BMRB_accession_number 6827 _BMRB_flat_file_name bmr6827.str _Entry_type original _Submission_date 2005-09-15 _Accession_date 2005-09-15 _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 Georgescu Julia . . 2 Bechinger Burkhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 113 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-11-03 original author . stop_ _Original_release_date 2009-11-03 save_ ############################# # Citation for this entry # ############################# save_lah4 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure-function relationships of the polyhistidine-rich peptide LAH4 in micellar environments; pH-dependent mode of antibiotic action and DNA transfection ; _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 Georgescu Julia . . 2 Bechinger Burkhard . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'amphipathic peptide' antibiotics carpet channel detergent DNA histidine micelles pore transfection stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'lah4 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'lah4 monomer' $lah4_polyhistidine_peptide_monomer stop_ _System_molecular_weight 2796 _System_physical_state unfolded _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'not available' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_lah4_polyhistidine_peptide_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common lah4 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 27 _Mol_residue_sequence ; KKALLALALHHLAHLALHLA LALKKAX ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 LYS 3 ALA 4 LEU 5 LEU 6 ALA 7 LEU 8 ALA 9 LEU 10 HIS 11 HIS 12 LEU 13 ALA 14 HIS 15 LEU 16 ALA 17 LEU 18 HIS 19 LEU 20 ALA 21 LEU 22 ALA 23 LEU 24 LYS 25 LYS 26 ALA 27 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-25 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 16332 lah4 96.15 26 100.00 100.00 9.37e-03 BMRB 16333 LAH4 96.15 26 100.00 100.00 9.37e-03 BMRB 6547 lah4 96.15 26 100.00 100.00 9.08e-03 BMRB 6886 lah4 96.15 26 100.00 100.00 9.37e-03 PDB 2KJN "Ph Dependent Structures Of Lah4 In Micellar Environmnet:mode Of Acting" 96.15 26 100.00 100.00 9.37e-03 PDB 2KJO "Ph Dependent Structures Of Lah4 In Micellar Environment: Mode Of Acting" 96.15 26 100.00 100.00 9.37e-03 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Aug 29 13:08:09 2011 ; 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 $lah4_polyhistidine_peptide_monomer unclassified . Unclassified 'Not applicable' unclassified unclassified 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 $lah4_polyhistidine_peptide_monomer 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type micelle _Details 50%TFE-PBS loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $lah4_polyhistidine_peptide_monomer 2 mM . TFE-PBS 50 % . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name ccnmr _Version . _Details 'ref: cieslar et al (1993) J.Magn.Res.B101, 97-101.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_DRX_500MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_ROESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label $sample_1 save_ save_COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details 50%TFE-PBS loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 0.2 pH temperature 317 3 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 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D TOCSY' NOESY ROESY COSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'lah4 monomer' _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 3 3 ALA HA H 4.332 0.02 1 2 3 3 ALA HB H 1.571 0.02 1 3 4 4 LEU H H 7.553 0.02 1 4 4 4 LEU HA H 4.371 0.02 1 5 4 4 LEU HB2 H 1.903 0.02 2 6 4 4 LEU HB3 H 1.858 0.02 2 7 4 4 LEU HD1 H 1.134 0.02 1 8 4 4 LEU HD2 H 1.059 0.02 1 9 5 5 LEU H H 7.729 0.02 1 10 5 5 LEU HA H 4.303 0.02 1 11 5 5 LEU HB2 H 2.049 0.02 2 12 5 5 LEU HB3 H 1.896 0.02 2 13 5 5 LEU HG H 1.792 0.02 1 14 5 5 LEU HD1 H 1.106 0.02 1 15 5 5 LEU HD2 H 1.056 0.02 1 16 6 6 ALA H H 8.009 0.02 9 17 6 6 ALA HA H 4.231 0.02 9 18 6 6 ALA HB H 1.654 0.02 1 19 7 7 LEU H H 7.889 0.02 1 20 7 7 LEU HA H 4.311 0.02 9 21 7 7 LEU HB2 H 2.032 0.02 2 22 7 7 LEU HG H 1.908 0.02 1 23 7 7 LEU HD1 H 1.088 0.02 1 24 7 7 LEU HD2 H 1.038 0.02 1 25 8 8 ALA H H 8.353 0.02 9 26 8 8 ALA HA H 4.320 0.02 9 27 8 8 ALA HB H 1.725 0.02 1 28 9 9 LEU H H 8.592 0.02 9 29 9 9 LEU HA H 4.318 0.02 9 30 9 9 LEU HB2 H 1.976 0.02 2 31 9 9 LEU HG H 1.802 0.02 1 32 9 9 LEU HD1 H 1.043 0.02 2 33 10 10 HIS H H 8.253 0.02 9 34 10 10 HIS HA H 4.457 0.02 1 35 10 10 HIS HB2 H 3.464 0.02 2 36 10 10 HIS HD2 H 7.009 0.02 1 37 10 10 HIS HE1 H 7.878 0.02 9 38 11 11 HIS H H 8.460 0.02 9 39 11 11 HIS HA H 4.560 0.02 1 40 11 11 HIS HB2 H 3.474 0.02 2 41 11 11 HIS HD2 H 7.104 0.02 1 42 11 11 HIS HE1 H 7.840 0.02 1 43 12 12 LEU H H 8.677 0.02 1 44 12 12 LEU HA H 4.267 0.02 1 45 12 12 LEU HB2 H 2.042 0.02 2 46 12 12 LEU HG H 1.865 0.02 1 47 12 12 LEU HD1 H 1.081 0.02 2 48 13 13 ALA H H 8.456 0.02 9 49 13 13 ALA HA H 4.217 0.02 1 50 13 13 ALA HB H 1.608 0.02 1 51 14 14 HIS H H 7.976 0.02 9 52 14 14 HIS HA H 4.429 0.02 1 53 14 14 HIS HB2 H 3.405 0.02 1 54 14 14 HIS HB3 H 3.351 0.02 1 55 14 14 HIS HD2 H 7.085 0.02 1 56 14 14 HIS HE1 H 7.808 0.02 1 57 15 15 LEU H H 8.343 0.02 9 58 15 15 LEU HA H 4.277 0.02 9 59 15 15 LEU HB2 H 1.945 0.02 2 60 15 15 LEU HG H 1.824 0.02 1 61 15 15 LEU HD1 H 1.040 0.02 2 62 16 16 ALA H H 8.597 0.02 1 63 16 16 ALA HA H 4.179 0.02 1 64 16 16 ALA HB H 1.651 0.02 1 65 17 17 LEU H H 7.996 0.02 9 66 17 17 LEU HA H 4.275 0.02 9 67 17 17 LEU HB2 H 1.874 0.02 2 68 17 17 LEU HG H 1.791 0.02 1 69 17 17 LEU HD1 H 0.998 0.02 2 70 18 18 HIS H H 8.107 0.02 1 71 18 18 HIS HA H 4.315 0.02 9 72 18 18 HIS HB2 H 3.409 0.02 1 73 18 18 HIS HB3 H 3.356 0.02 1 74 18 18 HIS HD2 H 7.050 0.02 1 75 18 18 HIS HE1 H 7.831 0.02 1 76 19 19 LEU H H 8.585 0.02 9 77 19 19 LEU HA H 4.269 0.02 9 78 19 19 LEU HB2 H 2.043 0.02 2 79 19 19 LEU HG H 1.721 0.02 1 80 19 19 LEU HD1 H 1.045 0.02 2 81 20 20 ALA H H 8.269 0.02 9 82 20 20 ALA HA H 4.182 0.02 9 83 20 20 ALA HB H 1.676 0.02 9 84 21 21 LEU H H 8.258 0.02 9 85 21 21 LEU HA H 4.217 0.02 9 86 21 21 LEU HB2 H 2.021 0.02 2 87 21 21 LEU HG H 1.646 0.02 9 88 21 21 LEU HD1 H 0.997 0.02 2 89 22 22 ALA H H 7.874 0.02 1 90 22 22 ALA HA H 4.291 0.02 9 91 22 22 ALA HB H 1.660 0.02 1 92 23 23 LEU H H 8.426 0.02 1 93 23 23 LEU HA H 4.294 0.02 1 94 23 23 LEU HB2 H 2.042 0.02 2 95 23 23 LEU HG H 1.694 0.02 1 96 23 23 LEU HD1 H 1.022 0.02 2 97 24 24 LYS H H 8.067 0.02 1 98 24 24 LYS HA H 4.284 0.02 1 99 24 24 LYS HB2 H 2.150 0.02 1 100 24 24 LYS HG2 H 1.709 0.02 1 101 24 24 LYS HG3 H 1.665 0.02 1 102 24 24 LYS HD2 H 1.866 0.02 2 103 24 24 LYS HE2 H 3.151 0.02 2 104 25 25 LYS H H 8.124 0.02 1 105 25 25 LYS HA H 4.332 0.02 1 106 25 25 LYS HB2 H 2.075 0.02 2 107 25 25 LYS HG2 H 1.716 0.02 1 108 25 25 LYS HG3 H 1.653 0.02 1 109 25 25 LYS HD2 H 1.861 0.02 2 110 25 25 LYS HE2 H 3.148 0.02 2 111 26 26 ALA H H 7.974 0.02 9 112 26 26 ALA HA H 4.388 0.02 9 113 26 26 ALA HB H 1.632 0.02 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 28 76 '29,77' '32,32,32,80,80,80' stop_ save_