data_7367 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of a Beta-Hairpin Peptidomimetic Inhibitor of the BIV Tat-Tar Interaction ; _BMRB_accession_number 7367 _BMRB_flat_file_name bmr7367.str _Entry_type original _Submission_date 2007-01-19 _Accession_date 2007-01-23 _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 Moehle K. . . 2 Patora K. . . 3 Robinson J. A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 91 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-10-31 update BMRB 'redo the release procedure' 2008-07-02 update BMRB 'complete entry citation' 2007-09-26 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure-guided peptidomimetic design leads to nanomolar beta-hairpin inhibitors of the Tat-TAR interaction of bovine immunodeficiency virus' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17223695 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Athanassiou Z. . . 2 Patora K. . . 3 Dias R. L.A. . 4 Moehle K. . . 5 Robinson J. A. . 6 Varani G. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 46 _Journal_issue 3 _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 741 _Page_last 751 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name L-22 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label L-22 $L-22_CYCLIC_PEPTIDE 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_L-22_CYCLIC_PEPTIDE _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common L-22_CYCLIC_PEPTIDE _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 14 _Mol_residue_sequence RVRTRKGRRIRIPP loop_ _Residue_seq_code _Residue_label 1 ARG 2 VAL 3 ARG 4 THR 5 ARG 6 LYS 7 GLY 8 ARG 9 ARG 10 ILE 11 ARG 12 ILE 13 PRO 14 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name 1 covalent L-22 1 ARG N L-22 14 PRO C stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $L-22_CYCLIC_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 $L-22_CYCLIC_PEPTIDE 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details 'unlabeled 5mM L-22 cyclic peptide; 90% H2O, 10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L-22_CYCLIC_PEPTIDE 5 mM unlabeled D2O 10 % . H2O 90 % . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Vendor _Address _Electronic_address 'P.GUNTERT ET AL.' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.53 loop_ _Task 'data analysis' stop_ _Details . save_ save_DYANA2 _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Guntert, P., Mumenthaler, C., Wuthrich, K.' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.3 . 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 . 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 NOESY' '2D TOCSY' DQF-COSY stop_ loop_ _Sample_label $sample stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name L-22 _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 H H 7.751 0.000 . 2 1 1 ARG HA H 4.604 0.003 . 3 1 1 ARG HB2 H 1.809 0.003 . 4 1 1 ARG HB3 H 1.809 0.003 . 5 1 1 ARG HD2 H 3.204 0.000 . 6 1 1 ARG HD3 H 3.204 0.000 . 7 1 1 ARG HE H 7.272 0.000 . 8 1 1 ARG HG2 H 1.603 0.008 . 9 1 1 ARG HG3 H 1.603 0.008 . 10 2 2 VAL H H 8.461 0.000 . 11 2 2 VAL HA H 4.733 0.006 . 12 2 2 VAL HB H 1.867 0.004 . 13 2 2 VAL HG1 H 0.784 0.002 . 14 2 2 VAL HG2 H 0.844 0.004 . 15 3 3 ARG H H 8.971 0.000 . 16 3 3 ARG HA H 4.737 0.000 . 17 3 3 ARG HB2 H 1.624 0.000 . 18 3 3 ARG HB3 H 1.846 0.000 . 19 3 3 ARG HG2 H 1.524 0.000 . 20 3 3 ARG HG3 H 1.555 0.001 . 21 4 4 THR H H 8.585 0.000 . 22 4 4 THR HA H 5.092 0.001 . 23 4 4 THR HB H 3.928 0.004 . 24 4 4 THR HG2 H 1.002 0.002 . 25 5 5 ARG H H 8.976 0.002 . 26 5 5 ARG HA H 4.549 0.000 . 27 5 5 ARG HB2 H 1.623 0.002 . 28 5 5 ARG HB3 H 1.733 0.006 . 29 5 5 ARG HG2 H 1.439 0.002 . 30 5 5 ARG HG3 H 1.622 0.000 . 31 6 6 LYS H H 9.590 0.004 . 32 6 6 LYS HA H 3.900 0.003 . 33 6 6 LYS HB2 H 1.804 0.001 . 34 6 6 LYS HB3 H 2.012 0.001 . 35 6 6 LYS HD2 H 1.691 0.000 . 36 6 6 LYS HD3 H 1.691 0.000 . 37 6 6 LYS HE2 H 2.993 0.000 . 38 6 6 LYS HE3 H 2.993 0.000 . 39 6 6 LYS HG2 H 1.412 0.006 . 40 6 6 LYS HG3 H 1.412 0.006 . 41 7 7 GLY H H 8.477 0.003 . 42 7 7 GLY HA2 H 3.564 0.001 . 43 7 7 GLY HA3 H 4.125 0.000 . 44 8 8 ARG H H 7.840 0.000 . 45 8 8 ARG HA H 4.617 0.000 . 46 8 8 ARG HB2 H 1.785 0.004 . 47 8 8 ARG HB3 H 1.845 0.005 . 48 8 8 ARG HG2 H 1.588 0.000 . 49 8 8 ARG HG3 H 1.639 0.000 . 50 9 9 ARG H H 8.630 0.005 . 51 9 9 ARG HA H 4.690 0.002 . 52 9 9 ARG HB2 H 1.582 0.002 . 53 9 9 ARG HB3 H 1.706 0.005 . 54 9 9 ARG HD2 H 3.110 0.002 . 55 9 9 ARG HD3 H 3.110 0.002 . 56 9 9 ARG HE H 7.166 0.000 . 57 9 9 ARG HG2 H 1.456 0.005 . 58 9 9 ARG HG3 H 1.581 0.004 . 59 10 10 ILE H H 9.072 0.002 . 60 10 10 ILE HA H 4.444 0.001 . 61 10 10 ILE HB H 1.788 0.002 . 62 10 10 ILE HD1 H 0.782 0.002 . 63 10 10 ILE HG12 H 1.061 0.005 . 64 10 10 ILE HG13 H 1.356 0.001 . 65 10 10 ILE HG2 H 0.841 0.003 . 66 11 11 ARG H H 8.582 0.002 . 67 11 11 ARG HA H 4.831 0.000 . 68 11 11 ARG HB2 H 1.669 0.000 . 69 11 11 ARG HB3 H 1.828 0.005 . 70 11 11 ARG HG2 H 1.484 0.005 . 71 11 11 ARG HG3 H 1.568 0.002 . 72 12 12 ILE H H 8.750 0.003 . 73 12 12 ILE HA H 4.552 0.004 . 74 12 12 ILE HB H 1.774 0.002 . 75 12 12 ILE HG12 H 1.060 0.000 . 76 12 12 ILE HG13 H 1.387 0.003 . 77 12 12 ILE HG2 H 0.854 0.005 . 78 13 13 PRO HA H 4.733 0.000 . 79 13 13 PRO HB2 H 1.909 0.000 . 80 13 13 PRO HB3 H 2.287 0.002 . 81 13 13 PRO HD2 H 3.521 0.003 . 82 13 13 PRO HD3 H 3.860 0.002 . 83 13 13 PRO HG2 H 2.006 0.000 . 84 13 13 PRO HG3 H 2.121 0.000 . 85 14 14 PRO HA H 4.547 0.002 . 86 14 14 PRO HB2 H 2.119 0.006 . 87 14 14 PRO HB3 H 2.233 0.003 . 88 14 14 PRO HD2 H 3.738 0.002 . 89 14 14 PRO HD3 H 3.970 0.002 . 90 14 14 PRO HG2 H 1.880 0.007 . 91 14 14 PRO HG3 H 2.104 0.000 . stop_ save_