data_4157 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Three-dimensional Solution Structure of Lactoferricin B, an Antimicrobial Peptide Derived from Bovine Lactoferrin ; _BMRB_accession_number 4157 _BMRB_flat_file_name bmr4157.str _Entry_type original _Submission_date 1998-07-02 _Accession_date 1998-07-02 _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 Hwang P. M. . 2 Zhou N. . . 3 Shan X. . . 4 Arrowsmith C. H. . 5 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" 166 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-02-03 original BMRB . stop_ _Original_release_date 1998-07-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Three-dimensional Solution Structure of Lactoferricin B, an Antimicrobial Peptide Derived from Bovine Lactoferrin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98190007 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hwang P. M. . 2 Zhou N. . . 3 Shan X. . . 4 Arrowsmith C. H. . 5 Vogel H. J. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 37 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4288 _Page_last 4298 _Year 1998 _Details . loop_ _Keyword 'antimicrobial peptide' 'proteolytic fragment' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title ; 1H, 13C and 15N chemical shift referencing in biomolecular NMR. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_lfcin _Saveframe_category molecular_system _Mol_system_name lactoferricin _Abbreviation_common lfcin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label lfcin $lfcin stop_ _System_molecular_weight 3122 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'antimicrobial peptide' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_lfcin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common lactoferricin _Abbreviation_common lfcin _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 25 _Mol_residue_sequence ; FKCRRWQWRMKKLGAPSITC VRRAF ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 LYS 3 CYS 4 ARG 5 ARG 6 TRP 7 GLN 8 TRP 9 ARG 10 MET 11 LYS 12 LYS 13 LEU 14 GLY 15 ALA 16 PRO 17 SER 18 ILE 19 THR 20 CYS 21 VAL 22 ARG 23 ARG 24 ALA 25 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $lfcin bovine 9913 Eucaryota Metazoa Bos taurus 'milk, exocrine' 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 $lfcin 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $lfcin 3 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label $sample_one save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_one save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 0.3 n/a pressure 1 . atm temperature 298 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 . 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label COSY stop_ loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name lfcin _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 PHE HA H 4.34 0.005 1 2 . 1 PHE HB2 H 3.20 0.005 1 3 . 1 PHE HB3 H 3.20 0.005 1 4 . 1 PHE HD1 H 7.35 0.005 1 5 . 1 PHE HD2 H 7.35 0.005 1 6 . 1 PHE HE1 H 7.22 0.005 1 7 . 1 PHE HE2 H 7.22 0.005 1 8 . 2 LYS H H 8.68 0.005 1 9 . 2 LYS HA H 4.43 0.005 1 10 . 2 LYS HB2 H 1.71 0.005 2 11 . 2 LYS HB3 H 1.76 0.005 2 12 . 3 CYS H H 8.79 0.005 1 13 . 3 CYS HA H 4.52 0.005 1 14 . 3 CYS HB2 H 2.70 0.005 1 15 . 3 CYS HB3 H 2.82 0.005 1 16 . 4 ARG H H 8.77 0.005 1 17 . 4 ARG HA H 4.37 0.005 1 18 . 4 ARG HB2 H 1.56 0.005 1 19 . 4 ARG HB3 H 1.56 0.005 1 20 . 4 ARG HG2 H 1.77 0.005 1 21 . 4 ARG HG3 H 1.77 0.005 1 22 . 4 ARG HD2 H 3.11 0.005 1 23 . 4 ARG HD3 H 3.11 0.005 1 24 . 4 ARG HE H 7.18 0.005 1 25 . 5 ARG H H 7.85 0.005 1 26 . 5 ARG HA H 4.40 0.005 1 27 . 5 ARG HB2 H 1.62 0.005 2 28 . 5 ARG HB3 H 1.68 0.005 2 29 . 5 ARG HG2 H 1.45 0.005 1 30 . 5 ARG HG3 H 1.45 0.005 1 31 . 5 ARG HD2 H 3.11 0.005 1 32 . 5 ARG HD3 H 3.11 0.005 1 33 . 5 ARG HE H 7.21 0.005 1 34 . 6 TRP H H 8.67 0.005 1 35 . 6 TRP HA H 5.01 0.005 1 36 . 6 TRP HB2 H 3.06 0.005 1 37 . 6 TRP HB3 H 3.06 0.005 1 38 . 6 TRP HD1 H 7.12 0.005 1 39 . 6 TRP HE1 H 10.10 0.005 1 40 . 6 TRP HE3 H 7.34 0.005 1 41 . 6 TRP HZ2 H 7.46 0.005 1 42 . 6 TRP HZ3 H 7.01 0.005 1 43 . 6 TRP HH2 H 7.21 0.005 1 44 . 7 GLN H H 8.81 0.005 1 45 . 7 GLN HA H 4.58 0.005 1 46 . 7 GLN HB2 H 1.86 0.005 2 47 . 7 GLN HB3 H 1.98 0.005 2 48 . 7 GLN HG2 H 2.20 0.005 1 49 . 7 GLN HG3 H 2.20 0.005 1 50 . 7 GLN HE21 H 6.90 0.005 2 51 . 7 GLN HE22 H 7.48 0.005 2 52 . 8 TRP H H 8.63 0.005 1 53 . 8 TRP HA H 4.87 0.005 1 54 . 8 TRP HB2 H 3.21 0.005 1 55 . 8 TRP HB3 H 3.21 0.005 1 56 . 8 TRP HD1 H 7.24 0.005 1 57 . 8 TRP HE1 H 10.17 0.005 1 58 . 8 TRP HE3 H 7.49 0.005 1 59 . 8 TRP HZ2 H 7.44 0.005 1 60 . 8 TRP HZ3 H 7.09 0.005 1 61 . 8 TRP HH2 H 7.21 0.005 1 62 . 9 ARG H H 8.61 0.005 1 63 . 9 ARG HA H 4.46 0.005 1 64 . 9 ARG HB2 H 1.70 0.005 2 65 . 9 ARG HB3 H 1.81 0.005 2 66 . 9 ARG HG2 H 1.50 0.005 1 67 . 9 ARG HG3 H 1.50 0.005 1 68 . 9 ARG HD2 H 3.14 0.005 1 69 . 9 ARG HD3 H 3.14 0.005 1 70 . 9 ARG HE H 7.15 0.005 1 71 . 10 MET H H 8.46 0.005 1 72 . 10 MET HA H 4.45 0.005 1 73 . 10 MET HB2 H 1.99 0.005 2 74 . 10 MET HB3 H 2.08 0.005 2 75 . 10 MET HG2 H 2.56 0.005 1 76 . 10 MET HG3 H 2.56 0.005 1 77 . 11 LYS H H 8.42 0.005 1 78 . 11 LYS HA H 4.36 0.005 1 79 . 11 LYS HB2 H 1.70 0.005 2 80 . 11 LYS HB3 H 1.82 0.005 2 81 . 11 LYS HG2 H 1.38 0.005 4 82 . 11 LYS HG3 H 1.38 0.005 4 83 . 11 LYS HD2 H 1.44 0.005 4 84 . 11 LYS HD3 H 1.44 0.005 4 85 . 12 LYS H H 8.30 0.005 1 86 . 12 LYS HA H 4.21 0.005 1 87 . 12 LYS HB2 H 1.80 0.005 1 88 . 12 LYS HB3 H 1.80 0.005 1 89 . 12 LYS HG2 H 1.41 0.005 4 90 . 12 LYS HG3 H 1.41 0.005 4 91 . 12 LYS HD2 H 1.71 0.005 4 92 . 12 LYS HD3 H 1.71 0.005 4 93 . 12 LYS HE2 H 3.14 0.005 1 94 . 12 LYS HE3 H 3.14 0.005 1 95 . 12 LYS HZ H 7.15 0.005 2 96 . 13 LEU H H 8.19 0.005 1 97 . 13 LEU HA H 4.33 0.005 1 98 . 13 LEU HB2 H 1.68 0.005 1 99 . 13 LEU HB3 H 1.68 0.005 1 100 . 13 LEU HG H 1.61 0.005 1 101 . 13 LEU HD1 H 0.91 0.005 4 102 . 13 LEU HD2 H 0.91 0.005 4 103 . 14 GLY H H 8.34 0.005 1 104 . 14 GLY HA2 H 3.91 0.005 1 105 . 14 GLY HA3 H 4.06 0.005 1 106 . 15 ALA H H 8.11 0.005 1 107 . 15 ALA HA H 4.65 0.005 1 108 . 15 ALA HB H 1.37 0.005 1 109 . 16 PRO HA H 4.60 0.005 1 110 . 16 PRO HB2 H 1.88 0.005 1 111 . 16 PRO HB3 H 2.25 0.005 1 112 . 16 PRO HG2 H 2.00 0.005 1 113 . 16 PRO HG3 H 2.00 0.005 1 114 . 16 PRO HD2 H 3.64 0.005 1 115 . 16 PRO HD3 H 3.78 0.005 1 116 . 17 SER H H 8.49 0.005 1 117 . 17 SER HA H 4.69 0.005 1 118 . 17 SER HB2 H 3.83 0.005 1 119 . 17 SER HB3 H 3.83 0.005 1 120 . 18 ILE H H 8.34 0.005 1 121 . 18 ILE HA H 4.48 0.005 1 122 . 18 ILE HB H 1.38 0.005 1 123 . 18 ILE HG12 H 0.77 0.005 1 124 . 18 ILE HG13 H 1.05 0.005 1 125 . 18 ILE HG2 H 0.62 0.005 1 126 . 18 ILE HD1 H 0.42 0.005 1 127 . 19 THR H H 8.56 0.005 1 128 . 19 THR HA H 4.68 0.005 1 129 . 19 THR HB H 4.07 0.005 1 130 . 19 THR HG2 H 1.16 0.005 1 131 . 20 CYS H H 8.90 0.005 1 132 . 20 CYS HA H 4.49 0.005 1 133 . 20 CYS HB2 H 3.04 0.005 1 134 . 20 CYS HB3 H 2.50 0.005 1 135 . 21 VAL H H 8.44 0.005 1 136 . 21 VAL HA H 4.49 0.005 1 137 . 21 VAL HB H 2.09 0.005 1 138 . 21 VAL HG1 H 0.89 0.005 2 139 . 21 VAL HG2 H 0.81 0.005 2 140 . 22 ARG H H 7.96 0.005 1 141 . 22 ARG HA H 4.39 0.005 1 142 . 22 ARG HB2 H 1.68 0.005 1 143 . 22 ARG HB3 H 1.68 0.005 1 144 . 22 ARG HG2 H 1.49 0.005 2 145 . 22 ARG HG3 H 1.57 0.005 2 146 . 22 ARG HD2 H 3.09 0.005 1 147 . 22 ARG HD3 H 3.09 0.005 1 148 . 22 ARG HE H 7.11 0.005 1 149 . 23 ARG H H 8.55 0.005 1 150 . 23 ARG HA H 4.35 0.005 1 151 . 23 ARG HB2 H 1.63 0.005 2 152 . 23 ARG HB3 H 1.68 0.005 2 153 . 23 ARG HG2 H 1.40 0.005 2 154 . 23 ARG HG3 H 1.46 0.005 2 155 . 23 ARG HD2 H 2.92 0.005 1 156 . 23 ARG HD3 H 2.92 0.005 1 157 . 23 ARG HE H 6.95 0.005 1 158 . 24 ALA H H 8.28 0.005 1 159 . 24 ALA HA H 4.28 0.005 1 160 . 24 ALA HB H 1.29 0.005 1 161 . 25 PHE H H 7.67 0.005 1 162 . 25 PHE HA H 4.38 0.005 1 163 . 25 PHE HB2 H 3.14 0.005 1 164 . 25 PHE HB3 H 2.97 0.005 1 165 . 25 PHE HD1 H 7.22 0.005 1 166 . 25 PHE HD2 H 7.22 0.005 1 stop_ save_