data_25941 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of retro-KR-12: A reversed sequence of a minimalized domain derived from human cathelicidin LL-37 ; _BMRB_accession_number 25941 _BMRB_flat_file_name bmr25941.str _Entry_type original _Submission_date 2016-01-05 _Accession_date 2016-01-05 _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 Gunasekera Sunithi . . 2 Goransson Ulf . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 85 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-01-12 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25926 KR-12 stop_ _Original_release_date 2016-01-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone-cyclized stable peptide-dimers derived from the human cathelicidin LL-37 mediate potent antimicrobial activity ; _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 Gunasekera Sunithi . . 2 Muhammad Taj . . 3 Stromstedt Adam A. . 4 Rosengren K. J. . 5 Goransson Ulf . . stop_ _Journal_abbreviation 'Not known' _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 . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name retro-KR-12 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $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 entity _Molecular_mass 1576.967 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 12 _Mol_residue_sequence ; RLFDKIRQVIRK ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 LEU 3 PHE 4 ASP 5 LYS 6 ILE 7 ARG 8 GLN 9 VAL 10 ILE 11 ARG 12 LYS 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 $entity . . . . . . 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 $entity 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM peptide dissolved in 600 microleters of H2O/D2O (9:1 v/v) atpH 4.5' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 1 mM 'natural abundance' H2O 90 '% v/v' 'natural abundance' D2O 10 '% v/v' 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '1 mM peptide dissolved in 600 microleters of D2O at pH 4.5' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 1 mM 'natural abundance' D2O 100 '% v/v' 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'G??ntert P.' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details 'BRUKER Avance HDIII equipped with a 5 mm TCI cryo probe.' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_2D_1H-1H_TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'H2O/D2O (9:1, v/v) at pH 4.5, 298K' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 . pH temperature 298 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details '1 mM peptide dissolved in 600 ul of D2O at pH 4.5' 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 water H 1 protons ppm 4.755 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '2D DQF-COSY' 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 entity _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 ARG HA H 4.093 0.001 . 2 1 1 ARG HB2 H 2.142 0.000 . 3 1 1 ARG HB3 H 1.954 0.000 . 4 1 1 ARG HG2 H 1.733 0.000 . 5 1 1 ARG HG3 H 1.733 0.000 . 6 1 1 ARG HD2 H 3.247 0.000 . 7 1 1 ARG HD3 H 3.247 0.000 . 8 2 2 LEU H H 8.634 0.001 . 9 2 2 LEU HA H 4.015 0.002 . 10 2 2 LEU HB2 H 1.597 0.000 . 11 2 2 LEU HB3 H 1.597 0.000 . 12 2 2 LEU HG H 1.417 0.000 . 13 2 2 LEU HD1 H 0.825 0.000 . 14 2 2 LEU HD2 H 0.760 0.000 . 15 3 3 PHE H H 8.273 0.001 . 16 3 3 PHE HA H 4.289 0.003 . 17 3 3 PHE HB2 H 3.233 0.000 . 18 3 3 PHE HB3 H 3.069 0.000 . 19 3 3 PHE HD1 H 7.155 0.003 . 20 3 3 PHE HD2 H 7.155 0.003 . 21 4 4 ASP H H 7.771 0.003 . 22 4 4 ASP HA H 4.313 0.001 . 23 4 4 ASP HB2 H 2.901 0.000 . 24 4 4 ASP HB3 H 2.796 0.000 . 25 5 5 LYS H H 7.831 0.003 . 26 5 5 LYS HA H 4.103 0.003 . 27 5 5 LYS HB2 H 1.805 0.000 . 28 5 5 LYS HB3 H 1.805 0.000 . 29 5 5 LYS HG2 H 1.619 0.000 . 30 5 5 LYS HG3 H 1.619 0.000 . 31 5 5 LYS HD2 H 1.385 0.000 . 32 5 5 LYS HD3 H 1.385 0.000 . 33 5 5 LYS HE2 H 2.913 0.000 . 34 5 5 LYS HE3 H 2.913 0.000 . 35 6 6 ILE H H 7.687 0.000 . 36 6 6 ILE HA H 3.676 0.001 . 37 6 6 ILE HB H 1.838 0.000 . 38 6 6 ILE HG12 H 1.627 0.000 . 39 6 6 ILE HG13 H 1.076 0.000 . 40 6 6 ILE HD1 H 0.820 0.000 . 41 7 7 ARG H H 7.912 0.001 . 42 7 7 ARG HA H 3.809 0.002 . 43 7 7 ARG HB2 H 1.798 0.000 . 44 7 7 ARG HB3 H 1.735 0.000 . 45 7 7 ARG HG2 H 1.659 0.000 . 46 7 7 ARG HG3 H 1.533 0.000 . 47 7 7 ARG HD2 H 3.103 0.001 . 48 7 7 ARG HD3 H 3.103 0.001 . 49 7 7 ARG HE H 7.092 0.001 . 50 8 8 GLN H H 7.489 0.001 . 51 8 8 GLN HA H 4.085 0.003 . 52 8 8 GLN HB2 H 2.427 0.000 . 53 8 8 GLN HB3 H 2.398 0.000 . 54 8 8 GLN HG3 H 2.133 0.000 . 55 9 9 VAL H H 7.530 0.000 . 56 9 9 VAL HA H 4.034 0.000 . 57 9 9 VAL HB H 2.203 0.000 . 58 9 9 VAL HG1 H 0.997 0.000 . 59 9 9 VAL HG2 H 0.920 0.000 . 60 10 10 ILE H H 7.399 0.002 . 61 10 10 ILE HA H 3.987 0.003 . 62 10 10 ILE HB H 1.892 0.000 . 63 10 10 ILE HG12 H 1.512 0.000 . 64 10 10 ILE HG13 H 1.240 0.000 . 65 10 10 ILE HG2 H 0.881 0.000 . 66 10 10 ILE HD1 H 0.771 0.000 . 67 11 11 ARG H H 7.831 0.001 . 68 11 11 ARG HA H 4.270 0.002 . 69 11 11 ARG HB2 H 1.873 0.000 . 70 11 11 ARG HB3 H 1.791 0.000 . 71 11 11 ARG HG2 H 1.617 0.000 . 72 11 11 ARG HG3 H 1.617 0.000 . 73 11 11 ARG HD2 H 3.161 0.000 . 74 11 11 ARG HD3 H 3.095 0.000 . 75 11 11 ARG HE H 7.025 0.002 . 76 12 12 LYS H H 7.761 0.002 . 77 12 12 LYS HA H 4.215 0.000 . 78 12 12 LYS HB2 H 1.846 0.000 . 79 12 12 LYS HB3 H 1.744 0.000 . 80 12 12 LYS HG2 H 1.634 0.000 . 81 12 12 LYS HG3 H 1.634 0.000 . 82 12 12 LYS HD2 H 1.409 0.000 . 83 12 12 LYS HD3 H 1.409 0.000 . 84 12 12 LYS HE2 H 2.957 0.000 . 85 12 12 LYS HE3 H 2.957 0.000 . stop_ save_