data_6088 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; E6-bind Trp-cage (E6apn1) ; _BMRB_accession_number 6088 _BMRB_flat_file_name bmr6088.str _Entry_type original _Submission_date 2004-01-29 _Accession_date 2004-01-29 _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 Liu Y. . . 2 Liu Z. . . 3 Androphy E. . . 4 Chen J. . . 5 Baleja J. D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 133 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'Updating non-standard residue' stop_ loop_ _Related_BMRB_accession_number _Relationship 6063 'E6apc2 peptide' 6064 'E6apc1 peptide' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; DESIGN AND CHARACTERIZATION OF HELICAL PEPTIDES THAT BIND THE E6 PROTEIN OF PAPILLOMAVIRUS ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15182185 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Y. . . 2 Liu Z. . . 3 Androphy E. . . 4 Chen J. . . 5 Baleja J. D. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 43 _Journal_issue 23 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7421 _Page_last 7431 _Year 2004 _Details . loop_ _Keyword 'E6-binding domain' 'HPV E6 protein' 'human papillomavirus' Trp-cage stop_ save_ ################################## # Molecular system description # ################################## save_system_E6apn1 _Saveframe_category molecular_system _Mol_system_name 'E6apn1 peptide' _Abbreviation_common E6apn1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'E6apn1 peptide' $E6apn1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_E6apn1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common E6apn1 _Abbreviation_common E6apn1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 25 _Mol_residue_sequence ; XALQELLGQWLKDGGPSSGR PPPSX ; loop_ _Residue_seq_code _Residue_label 1 ACE 2 ALA 3 LEU 4 GLN 5 GLU 6 LEU 7 LEU 8 GLY 9 GLN 10 TRP 11 LEU 12 LYS 13 ASP 14 GLY 15 GLY 16 PRO 17 SER 18 SER 19 GLY 20 ARG 21 PRO 22 PRO 23 PRO 24 SER 25 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-09 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 1RIJ "E6-Bind Trp-Cage (E6apn1)" 91.30 23 100.00 100.00 1.72e-04 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'ACETYL GROUP' _BMRB_code . _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Aug 30 14:27:57 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? O O O . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 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 DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Aug 29 14:48:08 2011 ; 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 $E6apn1 Papillomavirus 10558 Viruses . Papillomavirus . 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 $E6apn1 '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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $E6apn1 . mM 5.0 6.0 . imidazole 10 mM . . [U-2H] ZnSO4 4 mM . . . DTT 1 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $E6apn1 . mM 5.0 6.0 . imidazole 10 mM . . [U-2H] ZnSO4 4 mM . . . DTT 1 mM . . . H2O 90 % . . . D2O 99.96 % . . . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Task collection processing stop_ _Details 'Bruker BioSpin GmbH' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Task refinement 'structure solution' stop_ _Details 'Brunger, et al.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a pressure 1 . atm temperature 278 . 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 . H 1 . ppm . . . . . . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'E6apn1 peptide' _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 ALA HA H 4.268 . . 2 . 2 ALA HB H 1.429 . . 3 . 3 LEU H H 8.603 . . 4 . 3 LEU HA H 4.157 . . 5 . 3 LEU HB2 H 1.653 . . 6 . 3 LEU HD1 H 0.854 . . 7 . 3 LEU HD2 H 0.854 . . 8 . 4 GLN H H 8.567 . . 9 . 4 GLN HE21 H 7.734 . . 10 . 4 GLN HE22 H 7.008 . . 11 . 4 GLN HA H 4.077 . . 12 . 4 GLN HB2 H 2.016 . . 13 . 4 GLN HB3 H 2.016 . . 14 . 4 GLN HG2 H 2.427 . . 15 . 4 GLN HG3 H 2.427 . . 16 . 5 GLU H H 8.091 . . 17 . 5 GLU HA H 4.236 . . 18 . 5 GLU HB2 H 2.144 . . 19 . 5 GLU HB3 H 2.144 . . 20 . 5 GLU HG2 H 2.311 . . 21 . 5 GLU HG3 H 2.311 . . 22 . 6 LEU H H 8.269 . . 23 . 6 LEU HA H 4.233 . . 24 . 6 LEU HB2 H 1.894 . . 25 . 6 LEU HB3 H 1.469 . . 26 . 6 LEU HG H 1.762 . . 27 . 6 LEU HD1 H 0.912 . . 28 . 6 LEU HD2 H 0.912 . . 29 . 7 LEU H H 8.915 . . 30 . 7 LEU HA H 4.189 . . 31 . 7 LEU HB2 H 1.871 . . 32 . 7 LEU HB3 H 1.699 . . 33 . 7 LEU HD1 H 0.985 . . 34 . 7 LEU HD2 H 0.887 . . 35 . 8 GLY H H 8.566 . . 36 . 8 GLY HA2 H 4.050 . . 37 . 8 GLY HA3 H 3.884 . . 38 . 9 GLN H H 8.068 . . 39 . 9 GLN HE21 H 7.922 . . 40 . 9 GLN HE22 H 7.043 . . 41 . 9 GLN HA H 4.035 . . 42 . 9 GLN HB2 H 2.146 . . 43 . 9 GLN HB3 H 2.249 . . 44 . 9 GLN HG2 H 2.422 . . 45 . 9 GLN HG3 H 2.422 . . 46 . 10 TRP H H 8.171 . . 47 . 10 TRP HA H 4.371 . . 48 . 10 TRP HB2 H 3.306 . . 49 . 10 TRP HB3 H 3.654 . . 50 . 10 TRP HD1 H 7.105 . . 51 . 10 TRP HE1 H 9.897 . . 52 . 10 TRP HE3 H 7.613 . . 53 . 10 TRP HH2 H 7.170 . . 54 . 10 TRP HZ2 H 7.283 . . 55 . 10 TRP HZ3 H 7.137 . . 56 . 11 LEU H H 8.599 . . 57 . 11 LEU HA H 3.704 . . 58 . 11 LEU HB2 H 1.989 . . 59 . 11 LEU HB3 H 1.989 . . 60 . 11 LEU HG H 1.518 . . 61 . 11 LEU HD1 H 0.991 . . 62 . 11 LEU HD2 H 0.957 . . 63 . 12 LYS H H 8.143 . . 64 . 12 LYS HA H 4.027 . . 65 . 12 LYS HB2 H 1.939 . . 66 . 12 LYS HB3 H 1.939 . . 67 . 12 LYS HG2 H 1.529 . . 68 . 12 LYS HG3 H 1.529 . . 69 . 12 LYS HD2 H 1.673 . . 70 . 12 LYS HD3 H 1.673 . . 71 . 12 LYS HE2 H 2.970 . . 72 . 12 LYS HE3 H 2.970 . . 73 . 13 ASP H H 8.058 . . 74 . 13 ASP HA H 4.571 . . 75 . 13 ASP HB3 H 2.924 . . 76 . 13 ASP HB2 H 2.765 . . 77 . 14 GLY H H 7.687 . . 78 . 14 GLY HA2 H 3.581 . . 79 . 14 GLY HA3 H 4.168 . . 80 . 15 GLY H H 8.495 . . 81 . 15 GLY HA2 H 3.300 . . 82 . 15 GLY HA3 H 1.274 . . 83 . 16 PRO HA H 4.594 . . 84 . 16 PRO HB2 H 2.062 . . 85 . 16 PRO HB3 H 2.481 . . 86 . 16 PRO HG2 H 2.118 . . 87 . 16 PRO HG3 H 2.118 . . 88 . 16 PRO HD2 H 3.809 . . 89 . 16 PRO HD3 H 3.451 . . 90 . 17 SER H H 7.871 . . 91 . 17 SER HA H 4.483 . . 92 . 17 SER HB2 H 3.942 . . 93 . 17 SER HB3 H 3.942 . . 94 . 18 SER H H 8.273 . . 95 . 18 SER HA H 4.187 . . 96 . 18 SER HB2 H 3.571 . . 97 . 18 SER HB3 H 3.891 . . 98 . 19 GLY H H 8.063 . . 99 . 19 GLY HA2 H 3.841 . . 100 . 19 GLY HA3 H 4.253 . . 101 . 20 ARG H H 8.187 . . 102 . 20 ARG HA H 5.032 . . 103 . 20 ARG HB2 H 1.888 . . 104 . 20 ARG HG2 H 1.806 . . 105 . 20 ARG HG3 H 1.678 . . 106 . 20 ARG HD2 H 3.222 . . 107 . 20 ARG HD3 H 3.302 . . 108 . 20 ARG HE H 7.737 . . 109 . 21 PRO HA H 4.761 . . 110 . 21 PRO HB2 H 1.804 . . 111 . 21 PRO HB3 H 2.355 . . 112 . 21 PRO HG2 H 2.018 . . 113 . 21 PRO HG3 H 2.018 . . 114 . 21 PRO HD2 H 3.670 . . 115 . 21 PRO HD3 H 3.871 . . 116 . 22 PRO HA H 2.825 . . 117 . 22 PRO HB2 H 1.240 . . 118 . 22 PRO HB3 H 0.507 . . 119 . 22 PRO HG2 H 1.697 . . 120 . 22 PRO HG3 H 1.646 . . 121 . 22 PRO HD2 H 3.511 . . 122 . 22 PRO HD3 H 3.570 . . 123 . 23 PRO HA H 3.299 . . 124 . 23 PRO HB2 H 1.801 . . 125 . 23 PRO HB3 H 2.242 . . 126 . 23 PRO HG2 H 1.801 . . 127 . 23 PRO HG3 H 1.801 . . 128 . 23 PRO HD2 H 2.988 . . 129 . 23 PRO HD3 H 3.220 . . 130 . 24 SER H H 8.220 . . 131 . 24 SER HA H 4.335 . . 132 . 24 SER HB2 H 3.741 . . 133 . 24 SER HB3 H 3.340 . . stop_ save_