data_5290 ####################### # 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 5290 _BMRB_flat_file_name bmr5290.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" 143 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' 5291 'penetratin 12' 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 'irregular helix' NMR 'trifluoro-ethanol/water mixtures' stop_ save_ ################################## # Molecular system description # ################################## save_system_penetratin_mutant _Saveframe_category molecular_system _Mol_system_name 'third helix[W6F,W14F] of Antennapedia homeodomain' _Abbreviation_common 'penetratin double mutant[W6F,W14F]' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'third helix[W6F,W14F] of Antennapedia homeodomain' $penetratin_mutant 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_mutant _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'third helix[W6F,W14F] of Antennapedia homeodomain' _Abbreviation_common 'penetratin double mutant[W6F,W14F]' _Molecular_mass 2168 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 16 _Mol_residue_sequence RQIKIFFQNRRMKFKK loop_ _Residue_seq_code _Residue_label 1 ARG 2 GLN 3 ILE 4 LYS 5 ILE 6 PHE 7 PHE 8 GLN 9 ASN 10 ARG 11 ARG 12 MET 13 LYS 14 PHE 15 LYS 16 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 5543 Penetratin_W48F_W56F 100.00 16 100.00 100.00 3.83e+00 PDB 1KZ2 "Solution Structure Of The Third Helix Of Antennapedia Homeodomain Derivative [w6f,W14f]" 100.00 16 100.00 100.00 3.83e+00 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_mutant 'fruit fly' 7227 Eukaryota Metazoa Drosophila melanogaster 'Engineered biopolymer.' 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_mutant '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_mutant 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 'Aromatic amino acids can be only partly assigned.' loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'third helix[W6F,W14F] of Antennapedia homeodomain' _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 4.04 0.01 1 2 . 1 ARG HB2 H 2.16 0.01 2 3 . 1 ARG HB3 H 2.08 0.01 2 4 . 1 ARG HG2 H 1.83 0.01 1 5 . 1 ARG HG3 H 1.83 0.01 1 6 . 1 ARG HD2 H 3.23 0.01 1 7 . 1 ARG HD3 H 3.23 0.01 1 8 . 1 ARG HE H 7.20 0.01 1 9 . 1 ARG HH11 H 6.52 0.01 1 10 . 1 ARG HH12 H 6.52 0.01 1 11 . 1 ARG HH21 H 6.52 0.01 1 12 . 1 ARG HH22 H 6.52 0.01 1 13 . 2 GLN H H 9.08 0.01 1 14 . 2 GLN HA H 4.20 0.01 1 15 . 2 GLN HB2 H 2.19 0.01 2 16 . 2 GLN HB3 H 2.05 0.01 2 17 . 2 GLN HG2 H 2.54 0.01 2 18 . 2 GLN HG3 H 2.44 0.01 2 19 . 2 GLN HE21 H 6.91 0.01 2 20 . 2 GLN HE22 H 6.06 0.01 2 21 . 3 ILE H H 7.40 0.01 1 22 . 3 ILE HA H 4.02 0.01 1 23 . 3 ILE HB H 1.96 0.01 1 24 . 3 ILE HG12 H 1.55 0.01 2 25 . 3 ILE HG13 H 1.24 0.01 2 26 . 3 ILE HG2 H 0.94 0.01 1 27 . 3 ILE HD1 H 0.94 0.01 1 28 . 4 LYS H H 7.58 0.01 1 29 . 4 LYS HA H 4.16 0.01 1 30 . 4 LYS HB2 H 1.93 0.01 1 31 . 4 LYS HB3 H 1.93 0.01 1 32 . 4 LYS HG2 H 1.78 0.01 1 33 . 4 LYS HG3 H 1.78 0.01 1 34 . 4 LYS HD2 H 1.62 0.01 2 35 . 4 LYS HD3 H 1.55 0.01 2 36 . 4 LYS HE2 H 3.04 0.01 1 37 . 4 LYS HE3 H 3.04 0.01 1 38 . 5 ILE H H 7.39 0.01 1 39 . 5 ILE HA H 3.83 0.01 1 40 . 5 ILE HB H 1.96 0.01 1 41 . 5 ILE HG12 H 1.60 0.01 2 42 . 5 ILE HG13 H 1.23 0.01 2 43 . 5 ILE HG2 H 0.91 0.01 1 44 . 5 ILE HD1 H 0.94 0.01 1 45 . 6 PHE H H 7.77 0.01 1 46 . 6 PHE HA H 4.33 0.01 1 47 . 6 PHE HB2 H 3.21 0.01 1 48 . 6 PHE HB3 H 3.21 0.01 1 49 . 6 PHE HD1 H 7.04 0.01 1 50 . 6 PHE HD2 H 7.04 0.01 1 51 . 6 PHE HE1 H 7.22 0.01 1 52 . 6 PHE HE2 H 7.22 0.01 1 53 . 7 PHE H H 8.33 0.01 1 54 . 7 PHE HA H 4.28 0.01 1 55 . 7 PHE HB2 H 3.25 0.01 1 56 . 7 PHE HB3 H 3.25 0.01 1 57 . 7 PHE HD1 H 7.30 0.01 1 58 . 7 PHE HD2 H 7.30 0.01 1 59 . 8 GLN H H 8.59 0.01 1 60 . 8 GLN HA H 4.14 0.01 1 61 . 8 GLN HB2 H 2.34 0.01 2 62 . 8 GLN HB3 H 2.20 0.01 2 63 . 8 GLN HG2 H 2.52 0.01 1 64 . 8 GLN HG3 H 2.52 0.01 1 65 . 8 GLN HE21 H 6.79 0.01 2 66 . 8 GLN HE22 H 6.04 0.01 2 67 . 9 ASN H H 8.33 0.01 1 68 . 9 ASN HA H 4.42 0.01 1 69 . 9 ASN HB2 H 2.97 0.01 2 70 . 9 ASN HB3 H 2.71 0.01 2 71 . 9 ASN HD21 H 7.21 0.01 2 72 . 9 ASN HD22 H 6.14 0.01 2 73 . 10 ARG H H 8.02 0.01 1 74 . 10 ARG HA H 3.96 0.01 1 75 . 10 ARG HB2 H 1.86 0.01 1 76 . 10 ARG HB3 H 1.86 0.01 1 77 . 10 ARG HG2 H 1.65 0.01 2 78 . 10 ARG HG3 H 1.57 0.01 2 79 . 10 ARG HD2 H 2.98 0.01 1 80 . 10 ARG HD3 H 2.98 0.01 1 81 . 10 ARG HE H 6.78 0.01 1 82 . 10 ARG HH11 H 6.24 0.01 1 83 . 10 ARG HH12 H 6.24 0.01 1 84 . 10 ARG HH21 H 6.24 0.01 1 85 . 10 ARG HH22 H 6.24 0.01 1 86 . 11 ARG H H 8.19 0.01 1 87 . 11 ARG HA H 4.03 0.01 1 88 . 11 ARG HB2 H 1.90 0.01 2 89 . 11 ARG HB3 H 1.78 0.01 2 90 . 11 ARG HG2 H 1.62 0.01 1 91 . 11 ARG HG3 H 1.62 0.01 1 92 . 11 ARG HD2 H 3.15 0.01 2 93 . 11 ARG HD3 H 3.09 0.01 2 94 . 11 ARG HE H 6.86 0.01 1 95 . 11 ARG HH11 H 6.41 0.01 1 96 . 11 ARG HH12 H 6.41 0.01 1 97 . 11 ARG HH21 H 6.41 0.01 1 98 . 11 ARG HH22 H 6.41 0.01 1 99 . 12 MET H H 8.10 0.01 1 100 . 12 MET HA H 4.25 0.01 1 101 . 12 MET HB2 H 2.22 0.01 2 102 . 12 MET HB3 H 2.17 0.01 2 103 . 12 MET HG2 H 2.77 0.01 2 104 . 12 MET HG3 H 2.59 0.01 2 105 . 12 MET HE H 2.08 0.01 1 106 . 13 LYS H H 7.92 0.01 1 107 . 13 LYS HA H 4.02 0.01 1 108 . 13 LYS HB2 H 1.81 0.01 2 109 . 13 LYS HB3 H 1.76 0.01 2 110 . 13 LYS HG2 H 1.44 0.01 2 111 . 13 LYS HG3 H 1.25 0.01 2 112 . 13 LYS HD2 H 1.60 0.01 1 113 . 13 LYS HD3 H 1.60 0.01 1 114 . 13 LYS HE2 H 2.94 0.01 1 115 . 13 LYS HE3 H 2.94 0.01 1 116 . 13 LYS HZ H 7.29 0.01 1 117 . 14 PHE H H 7.94 0.01 1 118 . 14 PHE HA H 4.48 0.01 1 119 . 14 PHE HB2 H 3.24 0.01 2 120 . 14 PHE HB3 H 3.10 0.01 2 121 . 14 PHE HD1 H 7.27 0.01 1 122 . 14 PHE HD2 H 7.27 0.01 1 123 . 15 LYS H H 7.85 0.01 1 124 . 15 LYS HA H 4.12 0.01 1 125 . 15 LYS HB2 H 1.95 0.01 1 126 . 15 LYS HB3 H 1.95 0.01 1 127 . 15 LYS HG2 H 1.48 0.01 1 128 . 15 LYS HG3 H 1.48 0.01 1 129 . 15 LYS HD2 H 1.73 0.01 1 130 . 15 LYS HD3 H 1.73 0.01 1 131 . 15 LYS HE2 H 3.06 0.01 1 132 . 15 LYS HE3 H 3.06 0.01 1 133 . 15 LYS HZ H 7.26 0.01 1 134 . 16 LYS H H 7.72 0.01 1 135 . 16 LYS HA H 4.35 0.01 1 136 . 16 LYS HB2 H 1.93 0.01 2 137 . 16 LYS HB3 H 1.82 0.01 2 138 . 16 LYS HG2 H 1.49 0.01 1 139 . 16 LYS HG3 H 1.49 0.01 1 140 . 16 LYS HD2 H 1.72 0.01 1 141 . 16 LYS HD3 H 1.72 0.01 1 142 . 16 LYS HE2 H 3.04 0.01 1 143 . 16 LYS HE3 H 3.04 0.01 1 stop_ save_