data_6462 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The structure of a lactoferricinB derivative bound to micelles (LfcinB4-14) ; _BMRB_accession_number 6462 _BMRB_flat_file_name bmr6462.str _Entry_type original _Submission_date 2004-01-19 _Accession_date 2004-01-19 _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 Nguyen L. T. . 2 Schibli D. J. . 3 Vogel H. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 75 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-09-08 original author . stop_ _Original_release_date 2005-09-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural studies and model membrane interactions of two peptides derived from bovine lactoferricin. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15635665 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nguyen L. T. . 2 Schibli D. J. . 3 Vogel H. J. . stop_ _Journal_abbreviation 'J. Pept. Sci.' _Journal_volume 11 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 379 _Page_last 389 _Year 2004 _Details . loop_ _Keyword Micelle-bound Peptide stop_ save_ ################################## # Molecular system description # ################################## save_system _Saveframe_category molecular_system _Mol_system_name Lactotransferrin _Abbreviation_common Lactotransferrin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Lactotransferrin $Lactotransferrin stop_ _System_molecular_weight . _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Lactotransferrin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Lactotransferrin _Abbreviation_common Lactotransferrin _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 11 _Mol_residue_sequence RRWQWRMKKLG loop_ _Residue_seq_code _Residue_label 1 ARG 2 ARG 3 TRP 4 GLN 5 TRP 6 ARG 7 MET 8 LYS 9 LYS 10 LEU 11 GLY stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2005-09-15 save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Lactotransferrin Bovine 9913 Eukaryota Metazoa Bos taurus 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 $Lactotransferrin '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 $Lactotransferrin 3 mM . SDS 180 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . _Details . save_ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.4 . pH pressure 1 . atm temperature 310 . 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 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Lactotransferrin _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 ARG HA H 4.061 . . 2 . 1 ARG HB3 H 1.968 . . 3 . 1 ARG HB2 H 1.794 . . 4 . 1 ARG HG2 H 1.672 . . 5 . 1 ARG HD2 H 3.131 . . 6 . 1 ARG HE H 7.147 . . 7 . 2 ARG H H 8.471 . . 8 . 2 ARG HA H 4.112 . . 9 . 2 ARG HB3 H 1.534 . . 10 . 2 ARG HB2 H 1.58 . . 11 . 2 ARG HG3 H 1.222 . . 12 . 2 ARG HG2 H 1.349 . . 13 . 2 ARG HD3 H 2.941 . . 14 . 2 ARG HD2 H 2.903 . . 15 . 2 ARG HE H 6.86 . . 16 . 3 TRP H H 7.58 . . 17 . 3 TRP HA H 4.734 . . 18 . 3 TRP HB2 H 3.117 . . 19 . 3 TRP HD1 H 7.147 . . 20 . 3 TRP HE1 H 9.692 . . 21 . 3 TRP HZ2 H 7.383 . . 22 . 3 TRP HH2 H 7.041 . . 23 . 3 TRP HZ3 H 7.027 . . 24 . 3 TRP HE3 H 7.582 . . 25 . 4 GLN H H 7.914 . . 26 . 4 GLN HA H 4.33 . . 27 . 4 GLN HB2 H 1.886 . . 28 . 4 GLN HG3 H 2.206 . . 29 . 4 GLN HG2 H 2.049 . . 30 . 4 GLN HE21 H 6.7 . . 31 . 4 GLN HE22 H 7.353 . . 32 . 5 TRP H H 7.653 . . 33 . 5 TRP HA H 4.444 . . 34 . 5 TRP HB2 H 3.243 . . 35 . 5 TRP HD1 H 7.262 . . 36 . 5 TRP HE1 H 9.768 . . 37 . 5 TRP HZ2 H 7.362 . . 38 . 5 TRP HH2 H 7.028 . . 39 . 5 TRP HZ3 H 6.99 . . 40 . 5 TRP HE3 H 7.477 . . 41 . 6 ARG H H 7.749 . . 42 . 6 ARG HA H 4.139 . . 43 . 6 ARG HB3 H 1.767 . . 44 . 6 ARG HB2 H 1.631 . . 45 . 6 ARG HG2 H 1.426 . . 46 . 6 ARG HD2 H 3.112 . . 47 . 6 ARG HE H 7.051 . . 48 . 7 MET H H 7.742 . . 49 . 7 MET HA H 4.246 . . 50 . 7 MET HB3 H 2.067 . . 51 . 7 MET HB2 H 2.008 . . 52 . 7 MET HG3 H 2.592 . . 53 . 7 MET HG2 H 2.521 . . 54 . 8 LYS H H 7.907 . . 55 . 8 LYS HA H 4.218 . . 56 . 8 LYS HB2 H 1.834 . . 57 . 8 LYS HG2 H 1.434 . . 58 . 8 LYS HD2 H 1.684 . . 59 . 8 LYS HE2 H 2.994 . . 60 . 8 LYS HZ H 7.421 . . 61 . 9 LYS H H 7.925 . . 62 . 9 LYS HA H 4.26 . . 63 . 9 LYS HB2 H 1.75 . . 64 . 9 LYS HG2 H 1.422 . . 65 . 9 LYS HD2 H 1.679 . . 66 . 9 LYS HE2 H 2.994 . . 67 . 9 LYS HZ H 7.421 . . 68 . 10 LEU H H 7.83 . . 69 . 10 LEU HA H 4.364 . . 70 . 10 LEU HB2 H 1.681 . . 71 . 10 LEU HG H 1.616 . . 72 . 10 LEU HD1 H 0.942 . . 73 . 10 LEU HD2 H 0.878 . . 74 . 11 GLY H H 7.842 . . 75 . 11 GLY HA2 H 3.833 . . stop_ save_