data_15267 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of the anticoccidial peptide PW2 in DPC micelles ; _BMRB_accession_number 15267 _BMRB_flat_file_name bmr15267.str _Entry_type original _Submission_date 2007-05-28 _Accession_date 2007-05-28 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'PW2 structure in DPC micelles' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Almeida Fabio C.L. . 2 Tinoco Luzineide W. . 3 Gomes-Neto Francisco . . 4 Valente 'Ana Paula' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 78 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-02 update BMRB 'complete entry citation' 2007-10-29 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural biology of membrane-acting peptides: Conformational plasticity of anticoccidial peptide PW2 probed by solution NMR' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17927950 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cruzeiro-Silva C. . . 2 Gomes-Neto Francisco . . 3 Tinoco Luzineide W. . 4 Cilli E. M. . 5 Barros P. V.R. . 6 Lapido-Loureiro P. A. . 7 Bisch P. M. . 8 Almeida Fabio C.L. . 9 Valente 'Ana Paula' C.L. . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta.' _Journal_volume 1768 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3182 _Page_last 3192 _Year 2007 _Details . loop_ _Keyword 'antimicrobial peptide' Eimeria membrane micelles PW2 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_2 _Saveframe_category citation _Citation_full . _Citation_title 'NMR structure of PW2 bound to SDS micelles. A tryptophan-rich anticoccidial peptide selected from phage display libraries.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12130641 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tinoco Luzineide W. . 2 DaSilva Arnaldo . Jr. 3 Leite Adilson . . 4 Valente 'Ana Paula' . . 5 Almeida Fabio C.L. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full . _Journal_volume 277 _Journal_issue 39 _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 36351 _Page_last 36356 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PW2 in DPC micelles' _Enzyme_commission_number na loop_ _Mol_system_component_name _Mol_label PW2 $pw2 stop_ _System_molecular_weight 1601 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'PW2 in DPC micelles' save_ ######################## # Monomeric polymers # ######################## save_pw2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common pw2 _Molecular_mass 1601 _Mol_thiol_state 'not present' loop_ _Biological_function anticoccidial antimicrobial stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 12 _Mol_residue_sequence HPLKQYWWRPSI loop_ _Residue_seq_code _Residue_label 1 HIS 2 PRO 3 LEU 4 LYS 5 GLN 6 TYR 7 TRP 8 TRP 9 ARG 10 PRO 11 SER 12 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 PDB 1MO2 pw2 . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $pw2 . . . . . . 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 $pw2 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '2 mM PW2 in 300 mM DPC pH 5.5' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $pw2 2 mM 'natural abundance' 'phosphate buffer' 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_CNSSOLVE _Saveframe_category software _Name CNSSOLVE _Version 1.1 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 400 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _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 'ionic strength' 0.1 . M pH 5.0 . pH pressure 1 . atm 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 DSS H 1 'methyl protons' ppm 0.00 internal direct cylindrical 'separate tube (no insert) similar to the experimental sample tube' . 1.000000000 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_assignments_pw2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CNSSOLVE stop_ loop_ _Experiment_label '2D 1H-1H NOESY' 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 PW2 _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 HIS H H 7.991 0.02 1 2 1 1 HIS HA H 4.440 0.02 1 3 1 1 HIS HB2 H 3.090 0.02 1 4 1 1 HIS HB3 H 3.224 0.02 1 5 1 1 HIS HD2 H 7.246 0.02 1 6 1 1 HIS HE1 H 7.449 0.02 1 7 2 2 PRO HA H 4.617 0.02 1 8 2 2 PRO HB2 H 1.979 0.02 1 9 2 2 PRO HB3 H 2.432 0.02 1 10 2 2 PRO HD2 H 3.823 0.02 2 11 2 2 PRO HD3 H 3.396 0.02 2 12 2 2 PRO HG2 H 2.046 0.02 2 13 2 2 PRO HG3 H 1.928 0.02 2 14 3 3 LEU H H 9.090 0.02 1 15 3 3 LEU HA H 4.395 0.02 1 16 3 3 LEU HB2 H 1.799 0.02 1 17 3 3 LEU HB3 H 1.676 0.02 1 18 3 3 LEU HD1 H 0.952 0.02 2 19 3 3 LEU HD2 H 0.931 0.02 2 20 3 3 LEU HG H 1.752 0.02 1 21 4 4 LYS H H 8.247 0.02 1 22 4 4 LYS HA H 4.071 0.02 1 23 4 4 LYS HB2 H 1.657 0.02 1 24 4 4 LYS HB3 H 1.756 0.02 1 25 4 4 LYS HE2 H 2.881 0.02 2 26 4 4 LYS HG2 H 1.345 0.02 2 27 5 5 GLN H H 8.114 0.02 1 28 5 5 GLN HA H 4.175 0.02 1 29 5 5 GLN HB2 H 1.813 0.02 2 30 5 5 GLN HE21 H 7.423 0.02 2 31 5 5 GLN HE22 H 6.828 0.02 2 32 5 5 GLN HG2 H 2.092 0.02 2 33 6 6 TYR H H 7.950 0.02 1 34 6 6 TYR HA H 4.322 0.02 1 35 6 6 TYR HB2 H 2.731 0.02 2 36 6 6 TYR HB3 H 2.710 0.02 2 37 6 6 TYR HD1 H 7.026 0.02 3 38 6 6 TYR HE2 H 6.774 0.02 3 39 7 7 TRP H H 7.705 0.02 1 40 7 7 TRP HA H 4.457 0.02 1 41 7 7 TRP HB2 H 3.183 0.02 2 42 7 7 TRP HB3 H 3.183 0.02 2 43 7 7 TRP HD1 H 7.071 0.02 1 44 7 7 TRP HE1 H 10.561 0.02 1 45 7 7 TRP HE3 H 7.501 0.02 1 46 7 7 TRP HH2 H 7.077 0.02 1 47 7 7 TRP HZ2 H 7.453 0.02 1 48 7 7 TRP HZ3 H 6.995 0.02 1 49 8 8 TRP H H 7.074 0.02 1 50 8 8 TRP HA H 4.482 0.02 1 51 8 8 TRP HB2 H 3.085 0.02 1 52 8 8 TRP HB3 H 2.828 0.02 1 53 8 8 TRP HD1 H 6.969 0.02 1 54 8 8 TRP HE1 H 10.561 0.02 1 55 8 8 TRP HE3 H 7.239 0.02 1 56 8 8 TRP HH2 H 7.026 0.02 1 57 8 8 TRP HZ2 H 7.347 0.02 1 58 8 8 TRP HZ3 H 6.903 0.02 1 59 9 9 ARG H H 7.443 0.02 1 60 9 9 ARG HA H 4.432 0.02 1 61 9 9 ARG HB2 H 1.683 0.02 2 62 9 9 ARG HD2 H 3.061 0.02 2 63 9 9 ARG HD3 H 3.066 0.02 2 64 9 9 ARG HE H 7.314 0.02 1 65 9 9 ARG HG2 H 1.361 0.02 2 66 9 9 ARG HG3 H 1.440 0.02 2 67 9 9 ARG HH21 H 6.804 0.02 1 68 10 10 PRO HA H 4.350 0.02 1 69 10 10 PRO HB2 H 2.260 0.02 2 70 10 10 PRO HD2 H 3.547 0.02 2 71 10 10 PRO HD3 H 3.575 0.02 2 72 10 10 PRO HG2 H 1.965 0.02 2 73 10 10 PRO HG3 H 1.899 0.02 2 74 11 11 SER H H 8.467 0.02 1 75 11 11 SER HA H 4.358 0.02 1 76 11 11 SER HB2 H 3.820 0.02 2 77 11 11 SER HB3 H 3.830 0.02 2 78 12 12 ILE H H 7.994 0.02 1 stop_ save_