data_5291 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Investigation of Penetratin Peptides. Part 1: The Environment Dependent Conformational Properties of Penetratin and two of its Derivatives ; _BMRB_accession_number 5291 _BMRB_flat_file_name bmr5291.str _Entry_type original _Submission_date 2002-02-15 _Accession_date 2002-02-15 _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 Czajlik Andras . . 2 Mesko Eszter . . 3 Penke Botond . . 4 Perczel Andras . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 109 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-03-29 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5289 'Third helix of Antennapedia homeodomain' 5290 'Double mutant [W6F,W14F]' stop_ _Original_release_date 2002-03-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Investigation of Penetratin Peptides. Part 1: The Environment Dependent Conformational Properties of Penetratin and two of its Derivatives ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21986604 _PubMed_ID 11991205 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Czajlik Andras . . 2 Mesko Eszter . . 3 Penke Botond . . 4 Perczel Andras . . stop_ _Journal_abbreviation 'J. Pept. Sci.' _Journal_volume 8 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 151 _Page_last 171 _Year 2002 _Details . loop_ _Keyword 'helical structure' NMR 'trifluoro-ethanol/water mixtures' stop_ save_ ################################## # Molecular system description # ################################## save_system_penetratin_12 _Saveframe_category molecular_system _Mol_system_name '12 amino acid long derivative of the third helix of Antennapedia homeodomain' _Abbreviation_common 'penetratin 12' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'penetratin 12' $penetratin_12 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Translocation through biological membranes.' ; Transportation of covalently linked oligonucleotides and oligopeptides through biological membranes. ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_penetratin_12 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common '12 amino acid long derivative of the third helix of Antennapedia homeodomain' _Abbreviation_common 'penetratin 12' _Molecular_mass 1716 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 12 _Mol_residue_sequence RQIKIWFRKWKK loop_ _Residue_seq_code _Residue_label 1 ARG 2 GLN 3 ILE 4 LYS 5 ILE 6 TRP 7 PHE 8 ARG 9 LYS 10 TRP 11 LYS 12 LYS stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2005-11-22 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 BMRB 5291 '12 amino acid long derivative of the third helix of Antennapedia homeodomain' 100.00 12 100 100 6.0 PDB 1KZ5 'A Chain A, Solution Structure Of The ThirdHelix Of Antennapedia Homeodomain Derivatives(Rqikiwfrkwkk)' 100.00 12 100 100 6.0 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 $penetratin_12 'fruit fly' 7227 Eukaryota Metazoa Drosophila melanogaster 'Engineered 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 _Details $penetratin_12 'chemical synthesis' . . . . . 'Solid phase peptide synthesis. Boc strategy.' 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 $penetratin_12 1.5 mM . trifluoroethanol 90 % . water 10 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97.2 loop_ _Task 'peak assignment' 'peak picking' 'raw spectral data processing' stop_ _Details 'Accelrys Inc.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQF-COSY' _Sample_label . save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label . save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQF-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3 0.2 n/a temperature 300 1 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 . . . 1.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'penetratin 12' _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 4.03 0.01 1 2 . 1 ARG HB2 H 2.11 0.01 2 3 . 1 ARG HB3 H 2.03 0.01 2 4 . 1 ARG HG2 H 1.78 0.01 1 5 . 1 ARG HG3 H 1.78 0.01 1 6 . 1 ARG HD2 H 3.14 0.01 1 7 . 1 ARG HD3 H 3.14 0.01 1 8 . 1 ARG HE H 7.09 0.01 1 9 . 2 GLN H H 8.88 0.01 1 10 . 2 GLN HA H 4.28 0.01 1 11 . 2 GLN HB2 H 2.19 0.01 2 12 . 2 GLN HB3 H 2.06 0.01 2 13 . 2 GLN HG2 H 2.52 0.01 2 14 . 2 GLN HG3 H 2.44 0.01 2 15 . 2 GLN HE21 H 6.84 0.01 2 16 . 2 GLN HE22 H 6.02 0.01 2 17 . 3 ILE H H 7.43 0.01 1 18 . 3 ILE HA H 4.06 0.01 1 19 . 3 ILE HB H 1.93 0.01 1 20 . 3 ILE HG12 H 1.58 0.01 2 21 . 3 ILE HG13 H 1.27 0.01 2 22 . 3 ILE HG2 H 0.91 0.01 1 23 . 3 ILE HD1 H 0.91 0.01 1 24 . 4 LYS H H 7.60 0.01 1 25 . 4 LYS HA H 4.16 0.01 1 26 . 4 LYS HB2 H 1.87 0.01 1 27 . 4 LYS HB3 H 1.87 0.01 1 28 . 4 LYS HG2 H 1.61 0.01 2 29 . 4 LYS HG3 H 1.49 0.01 2 30 . 4 LYS HD2 H 1.77 0.01 1 31 . 4 LYS HD3 H 1.77 0.01 1 32 . 4 LYS HE2 H 3.04 0.01 1 33 . 4 LYS HE3 H 3.04 0.01 1 34 . 5 ILE H H 7.37 0.01 1 35 . 5 ILE HA H 3.86 0.01 1 36 . 5 ILE HB H 2.00 0.01 1 37 . 5 ILE HG12 H 1.62 0.01 2 38 . 5 ILE HG13 H 1.24 0.01 2 39 . 5 ILE HG2 H 0.92 0.01 1 40 . 5 ILE HD1 H 0.94 0.01 1 41 . 6 TRP H H 7.81 0.01 1 42 . 6 TRP HA H 4.34 0.01 1 43 . 6 TRP HB2 H 3.39 0.01 2 44 . 6 TRP HB3 H 3.31 0.01 2 45 . 6 TRP HD1 H 6.94 0.01 1 46 . 6 TRP HE1 H 9.04 0.01 1 47 . 6 TRP HE3 H 7.50 0.01 1 48 . 6 TRP HZ2 H 7.08 0.01 1 49 . 6 TRP HZ3 H 7.08 0.01 1 50 . 6 TRP HH2 H 7.13 0.01 1 51 . 7 PHE H H 8.29 0.01 1 52 . 7 PHE HA H 4.23 0.01 1 53 . 7 PHE HB2 H 3.25 0.01 2 54 . 7 PHE HB3 H 3.19 0.01 2 55 . 7 PHE HD1 H 7.29 0.01 1 56 . 7 PHE HD2 H 7.29 0.01 1 57 . 7 PHE HE1 H 7.38 0.01 1 58 . 7 PHE HE2 H 7.38 0.01 1 59 . 7 PHE HZ H 7.34 0.01 1 60 . 8 ARG H H 7.86 0.01 1 61 . 8 ARG HA H 4.04 0.01 1 62 . 8 ARG HB2 H 1.98 0.01 2 63 . 8 ARG HB3 H 1.88 0.01 2 64 . 8 ARG HG2 H 1.74 0.01 1 65 . 8 ARG HG3 H 1.74 0.01 1 66 . 8 ARG HD2 H 3.25 0.01 2 67 . 8 ARG HD3 H 3.19 0.01 2 68 . 8 ARG HE H 6.97 0.01 1 69 . 9 LYS H H 7.94 0.01 1 70 . 9 LYS HA H 4.00 0.01 1 71 . 9 LYS HB2 H 1.78 0.01 2 72 . 9 LYS HB3 H 1.70 0.01 2 73 . 9 LYS HG2 H 1.26 0.01 2 74 . 9 LYS HG3 H 1.17 0.01 2 75 . 9 LYS HD2 H 1.49 0.01 1 76 . 9 LYS HD3 H 1.49 0.01 1 77 . 9 LYS HE2 H 2.79 0.01 1 78 . 9 LYS HE3 H 2.79 0.01 1 79 . 10 TRP H H 7.89 0.01 1 80 . 10 TRP HA H 4.48 0.01 1 81 . 10 TRP HB2 H 3.14 0.01 2 82 . 10 TRP HB3 H 2.89 0.01 2 83 . 10 TRP HD1 H 6.82 0.01 1 84 . 10 TRP HE1 H 8.60 0.01 1 85 . 10 TRP HE3 H 7.50 0.01 1 86 . 10 TRP HZ2 H 7.37 0.01 1 87 . 10 TRP HZ3 H 7.10 0.01 1 88 . 10 TRP HH2 H 7.21 0.01 1 89 . 11 LYS H H 7.79 0.01 1 90 . 11 LYS HA H 4.02 0.01 1 91 . 11 LYS HB2 H 1.75 0.01 1 92 . 11 LYS HB3 H 1.75 0.01 1 93 . 11 LYS HG2 H 1.65 0.01 1 94 . 11 LYS HG3 H 1.65 0.01 1 95 . 11 LYS HD2 H 1.31 0.01 1 96 . 11 LYS HD3 H 1.31 0.01 1 97 . 11 LYS HE2 H 2.93 0.01 1 98 . 11 LYS HE3 H 2.93 0.01 1 99 . 11 LYS HZ H 7.12 0.01 1 100 . 12 LYS H H 7.43 0.01 1 101 . 12 LYS HA H 4.06 0.01 1 102 . 12 LYS HB2 H 1.84 0.01 1 103 . 12 LYS HB3 H 1.84 0.01 1 104 . 12 LYS HG2 H 1.42 0.01 2 105 . 12 LYS HG3 H 1.38 0.01 2 106 . 12 LYS HD2 H 1.65 0.01 1 107 . 12 LYS HD3 H 1.65 0.01 1 108 . 12 LYS HE2 H 2.95 0.01 1 109 . 12 LYS HE3 H 2.95 0.01 1 stop_ save_