data_11554 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of anoplin double mutant R5F T8W in DPC micelles ; _BMRB_accession_number 11554 _BMRB_flat_file_name bmr11554.str _Entry_type original _Submission_date 2014-02-10 _Accession_date 2014-02-11 _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 Uggerhoej Lars E . 2 Poulsen Tanja J . 3 Wimmer Reinhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-12-01 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 11551 'Structure of antimicrobial peptide anoplin in DPC micelles' 11552 'Structure of anoplin mutant R5W in DPC micelles' 11553 'Structure of anoplin double mutant R5K T8W in DPC micelles' stop_ _Original_release_date 2014-12-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Rational Design of alpha-helical antimicrobial peptides: DOs and DON'Ts' _Citation_status submitted _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 Uggerhoej Lars E . 2 Poulsen Tanja J . 3 Munk Jens . . 4 Fredborg Marlene . . 5 Sondergaard Teis E . 6 Frimodt-Moeller Niels . . 7 Hansen Paul R . 8 Wimmer Reinhard . . stop_ _Journal_abbreviation ChemBioChem _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 anoplin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label anoplin $anoplin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'anoplin R5F T8W in DPC micelle' save_ ######################## # Monomeric polymers # ######################## save_anoplin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common anoplin _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'antimicrobial peptide' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 11 _Mol_residue_sequence GLLKFIKWLLX loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 LEU 3 3 LEU 4 4 LYS 5 5 PHE 6 6 ILE 7 7 LYS 8 8 TRP 9 9 LEU 10 10 LEU 11 11 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'AMINO GROUP' _BMRB_code NH2 _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details . 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 _Details $anoplin 'Anoplius samariensis' 200614 Eukaryota Metazoa Anoplius samariensis 'double point mutation of naturally occurring peptide' 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 $anoplin '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 $anoplin 3 mM 'natural abundance' DPC 150 mM '[U-98% 2H]' 'potassium phosphate' 10 mM 'natural abundance' 'sodium azide' 2 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % '[U-99% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version 1.5.5 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ save_YASARA _Saveframe_category software _Name YASARA _Version 12.1.19 loop_ _Vendor _Address _Electronic_address 'Yasara Biosciences, Elmar Krieger' . www.yasara.org 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 600 _Details 'RT-TXI 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_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aromatic_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _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 6.5 . pH pressure 1 . atm temperature 310.1 . 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 C 13 protons ppm 4.63 internal indirect . . . 0.25144954 water H 1 protons ppm 4.63 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 1H-13C HSQC aliphatic' '2D 1H-13C HSQC aromatic' 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 anoplin _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 2 2 LEU HA H 4.108 0.01 . 2 2 2 LEU HB2 H 1.709 0.01 . 3 2 2 LEU HD1 H 0.991 0.01 . 4 2 2 LEU HD2 H 0.91 0.01 . 5 3 3 LEU H H 8.935 0.01 . 6 3 3 LEU HA H 4.014 0.01 . 7 3 3 LEU HB2 H 1.732 0.01 . 8 3 3 LEU HB3 H 1.63 0.01 . 9 3 3 LEU HD1 H 0.936 0.01 . 10 3 3 LEU HD2 H 0.881 0.01 . 11 4 4 LYS H H 7.984 0.01 . 12 4 4 LYS HA H 3.897 0.01 . 13 4 4 LYS HB2 H 1.825 0.01 . 14 4 4 LYS HB3 H 1.778 0.01 . 15 4 4 LYS HG2 H 1.409 0.01 . 16 4 4 LYS HG3 H 1.306 0.01 . 17 4 4 LYS HD2 H 1.621 0.01 . 18 4 4 LYS HD3 H 1.621 0.01 . 19 4 4 LYS HE2 H 2.878 0.01 . 20 4 4 LYS HE3 H 2.878 0.01 . 21 5 5 PHE H H 7.876 0.01 . 22 5 5 PHE HA H 4.405 0.01 . 23 5 5 PHE HB2 H 3.312 0.01 . 24 5 5 PHE HB3 H 3.248 0.01 . 25 5 5 PHE HD1 H 7.163 0.01 . 26 5 5 PHE HD2 H 7.163 0.01 . 27 5 5 PHE HE1 H 7.213 0.01 . 28 5 5 PHE HE2 H 7.213 0.01 . 29 5 5 PHE HZ H 7.213 0.01 . 30 6 6 ILE H H 8.357 0.01 . 31 6 6 ILE HA H 3.577 0.01 . 32 6 6 ILE HB H 2.04 0.01 . 33 6 6 ILE HG12 H 1.819 0.01 . 34 6 6 ILE HG13 H 1.313 0.01 . 35 6 6 ILE HG2 H 0.882 0.01 . 36 6 6 ILE HD1 H 0.833 0.01 . 37 7 7 LYS H H 8.284 0.01 . 38 7 7 LYS HA H 3.795 0.01 . 39 7 7 LYS HB2 H 1.893 0.01 . 40 7 7 LYS HB3 H 1.843 0.01 . 41 7 7 LYS HG2 H 1.351 0.01 . 42 7 7 LYS HG3 H 1.583 0.01 . 43 7 7 LYS HD2 H 1.632 0.01 . 44 7 7 LYS HD3 H 1.632 0.01 . 45 7 7 LYS HE2 H 2.86 0.01 . 46 7 7 LYS HE3 H 2.86 0.01 . 47 8 8 TRP H H 7.782 0.01 . 48 8 8 TRP HA H 4.155 0.01 . 49 8 8 TRP HB2 H 3.265 0.01 . 50 8 8 TRP HB3 H 3.536 0.01 . 51 8 8 TRP HD1 H 7.266 0.01 . 52 8 8 TRP HE3 H 7.247 0.01 . 53 8 8 TRP HZ2 H 7.479 0.01 . 54 8 8 TRP HZ3 H 6.837 0.01 . 55 8 8 TRP HH2 H 7.069 0.01 . 56 9 9 LEU H H 8.05 0.01 . 57 9 9 LEU HA H 3.148 0.01 . 58 9 9 LEU HB2 H 1.538 0.01 . 59 9 9 LEU HB3 H 1.428 0.01 . 60 9 9 LEU HD1 H 0.717 0.01 . 61 9 9 LEU HD2 H 0.717 0.01 . 62 10 10 LEU H H 7.559 0.01 . 63 10 10 LEU HA H 3.961 0.01 . 64 10 10 LEU HB2 H 1.652 0.01 . 65 10 10 LEU HB3 H 1.493 0.01 . 66 10 10 LEU HG H 1.761 0.01 . 67 10 10 LEU HD1 H 0.78 0.01 . 68 10 10 LEU HD2 H 0.748 0.01 . stop_ save_