data_16511 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; A Doppel alpha-helix Peptide Fragment Mimics the Copper(II) Interactions with the whole Protein ; _BMRB_accession_number 16511 _BMRB_flat_file_name bmr16511.str _Entry_type new _Submission_date 2009-09-23 _Accession_date 2009-09-23 _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 Isernia Carla . . 2 'La Mendola' Diego . . 3 Magri' Antonio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 133 "coupling constants" 17 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-08-12 update BMRB 'Complete entry citation' 2010-04-26 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16522 'A Doppel alpha-helix Peptide Fragment' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20411530 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'La Mendola' Diego . . 2 Magri Antonio . . 3 Campagna Tiziana . . 4 Campitiello 'Maria Anna' . . 5 Raiola Luca . . 6 Isernia Carla . . 7 Hansson Orjan . . 8 Bonomo Raffaele P. . 9 Rizzarelli Enrico . . stop_ _Journal_abbreviation Chemistry _Journal_name_full 'Chemistry (Weinheim an der Bergstrasse, Germany)' _Journal_volume 16 _Journal_issue 21 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6212 _Page_last 6223 _Year 2010 _Details . loop_ _Keyword copper peptides doppel prion 'helical structure' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name hDpl(122-139)D124N _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hDpl(122-139)D124N $hDpl(122-139)D124N 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_hDpl(122-139)D124N _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hDpl(122-139)D124N _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 18 _Mol_residue_sequence KPNNKLHQQVLWRLVQEL loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 122 LYS 2 123 PRO 3 124 ASN 4 125 ASN 5 126 LYS 6 127 LEU 7 128 HIS 8 129 GLN 9 130 GLN 10 131 VAL 11 132 LEU 12 133 TRP 13 134 ARG 14 135 LEU 15 136 VAL 16 137 GLN 17 138 GLU 18 139 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $hDpl(122-139)D124N Human 9606 Eukaryota Metazoa Homo sapiens 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 $hDpl(122-139)D124N '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 _Isotopic_labeling $hDpl(122-139)D124N 1.2 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _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 temperature 300 . K pH 5.1 . pH pressure 1 . atm 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 . . . 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D DQF-COSY' 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 hDpl(122-139)D124N _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 1 122 1 LYS H H 8.14 0.02 1 2 122 1 LYS HA H 4.46 0.02 1 3 122 1 LYS HB2 H 1.70 0.02 1 4 122 1 LYS HB3 H 1.70 0.02 1 5 122 1 LYS HD2 H 1.60 0.02 1 6 122 1 LYS HD3 H 1.60 0.02 1 7 122 1 LYS HE2 H 2.91 0.02 1 8 122 1 LYS HE3 H 2.91 0.02 1 9 122 1 LYS HG2 H 1.37 0.02 1 10 122 1 LYS HG3 H 1.37 0.02 1 11 122 1 LYS HZ H 7.73 0.02 1 12 123 2 PRO HA H 4.30 0.02 1 13 123 2 PRO HB2 H 2.19 0.02 2 14 123 2 PRO HB3 H 1.80 0.02 2 15 123 2 PRO HD2 H 3.75 0.02 2 16 123 2 PRO HD3 H 3.53 0.02 2 17 123 2 PRO HG2 H 1.93 0.02 1 18 123 2 PRO HG3 H 1.93 0.02 1 19 124 3 ASN H H 8.45 0.02 1 20 124 3 ASN HA H 4.58 0.02 1 21 124 3 ASN HB2 H 2.72 0.02 1 22 124 3 ASN HB3 H 2.72 0.02 1 23 124 3 ASN HD21 H 7.52 0.02 2 24 124 3 ASN HD22 H 7.52 0.02 2 25 125 4 ASN H H 8.29 0.02 1 26 125 4 ASN HA H 4.56 0.02 1 27 125 4 ASN HB2 H 2.71 0.02 1 28 125 4 ASN HB3 H 2.71 0.02 1 29 125 4 ASN HD21 H 7.50 0.02 2 30 125 4 ASN HD22 H 7.50 0.02 2 31 126 5 LYS H H 8.16 0.02 1 32 126 5 LYS HA H 4.14 0.02 1 33 126 5 LYS HB2 H 1.68 0.02 1 34 126 5 LYS HB3 H 1.68 0.02 1 35 126 5 LYS HD2 H 1.61 0.02 1 36 126 5 LYS HD3 H 1.61 0.02 1 37 126 5 LYS HE2 H 2.89 0.02 1 38 126 5 LYS HE3 H 2.89 0.02 1 39 126 5 LYS HG2 H 1.31 0.02 1 40 126 5 LYS HG3 H 1.31 0.02 1 41 126 5 LYS HZ H 7.43 0.02 1 42 127 6 LEU H H 7.89 0.02 1 43 127 6 LEU HA H 4.16 0.02 1 44 127 6 LEU HB2 H 1.49 0.02 2 45 127 6 LEU HB3 H 1.37 0.02 1 46 127 6 LEU HD1 H 0.80 0.02 2 47 127 6 LEU HD2 H 0.74 0.02 2 48 127 6 LEU HG H 1.37 0.02 1 49 128 7 HIS H H 8.30 0.02 1 50 128 7 HIS HA H 4.55 0.02 1 51 128 7 HIS HB2 H 3.15 0.02 2 52 128 7 HIS HB3 H 3.06 0.02 2 53 128 7 HIS HD2 H 7.13 0.02 1 54 128 7 HIS HE1 H 8.41 0.02 1 55 129 8 GLN H H 8.21 0.02 1 56 129 8 GLN HA H 4.22 0.02 1 57 129 8 GLN HB2 H 1.96 0.02 2 58 129 8 GLN HB3 H 1.85 0.02 2 59 129 8 GLN HE21 H 7.39 0.02 2 60 129 8 GLN HE22 H 6.76 0.02 2 61 129 8 GLN HG2 H 2.22 0.02 1 62 129 8 GLN HG3 H 2.22 0.02 1 63 130 9 GLN H H 8.36 0.02 1 64 130 9 GLN HA H 4.21 0.02 1 65 130 9 GLN HB2 H 1.93 0.02 2 66 130 9 GLN HB3 H 1.89 0.02 2 67 130 9 GLN HE21 H 7.40 0.02 2 68 130 9 GLN HE22 H 6.76 0.02 2 69 130 9 GLN HG2 H 2.23 0.02 1 70 130 9 GLN HG3 H 2.23 0.02 1 71 131 10 VAL H H 8.09 0.02 1 72 131 10 VAL HA H 3.91 0.02 1 73 131 10 VAL HB H 1.84 0.02 1 74 131 10 VAL HG1 H 0.78 0.02 2 75 131 10 VAL HG2 H 0.67 0.02 2 76 132 11 LEU H H 8.12 0.02 1 77 132 11 LEU HA H 4.19 0.02 1 78 132 11 LEU HB2 H 1.50 0.02 1 79 132 11 LEU HB3 H 1.50 0.02 1 80 132 11 LEU HD1 H 0.78 0.02 1 81 132 11 LEU HD2 H 0.78 0.02 1 82 132 11 LEU HG H 1.50 0.02 1 83 133 12 TRP H H 7.90 0.02 1 84 133 12 TRP HA H 4.50 0.02 1 85 133 12 TRP HB2 H 3.16 0.02 1 86 133 12 TRP HB3 H 3.16 0.02 1 87 133 12 TRP HD1 H 7.15 0.02 1 88 133 12 TRP HE1 H 10.02 0.02 1 89 133 12 TRP HE3 H 7.47 0.02 1 90 133 12 TRP HH2 H 7.13 0.02 1 91 133 12 TRP HZ2 H 7.40 0.02 1 92 133 12 TRP HZ3 H 7.04 0.02 1 93 134 13 ARG H H 7.76 0.02 1 94 134 13 ARG HA H 4.01 0.02 1 95 134 13 ARG HB2 H 1.60 0.02 2 96 134 13 ARG HB3 H 1.48 0.02 2 97 134 13 ARG HD2 H 3.00 0.02 1 98 134 13 ARG HD3 H 3.00 0.02 1 99 134 13 ARG HE H 7.04 0.02 1 100 134 13 ARG HG2 H 1.28 0.02 1 101 134 13 ARG HG3 H 1.28 0.02 1 102 135 14 LEU H H 7.86 0.02 1 103 135 14 LEU HA H 4.14 0.02 1 104 135 14 LEU HB2 H 1.57 0.02 1 105 135 14 LEU HB3 H 1.57 0.02 1 106 135 14 LEU HD1 H 0.79 0.02 1 107 135 14 LEU HD2 H 0.79 0.02 1 108 135 14 LEU HG H 1.57 0.02 1 109 136 15 VAL H H 7.89 0.02 1 110 136 15 VAL HA H 3.98 0.02 1 111 136 15 VAL HB H 1.96 0.02 1 112 136 15 VAL HG2 H 0.82 0.02 1 113 137 16 GLN H H 8.19 0.02 1 114 137 16 GLN HA H 4.22 0.02 1 115 137 16 GLN HB2 H 1.96 0.02 2 116 137 16 GLN HB3 H 1.85 0.02 2 117 137 16 GLN HE21 H 7.35 0.02 2 118 137 16 GLN HE22 H 6.73 0.02 2 119 137 16 GLN HG2 H 2.22 0.02 1 120 137 16 GLN HG3 H 2.22 0.02 1 121 138 17 GLU H H 8.43 0.02 1 122 138 17 GLU HA H 4.27 0.02 1 123 138 17 GLU HB2 H 2.12 0.02 2 124 138 17 GLU HB3 H 1.92 0.02 2 125 138 17 GLU HG2 H 2.33 0.02 1 126 138 17 GLU HG3 H 2.33 0.02 1 127 139 18 LEU H H 8.08 0.02 1 128 139 18 LEU HA H 4.22 0.02 1 129 139 18 LEU HB2 H 1.47 0.02 2 130 139 18 LEU HB3 H 1.39 0.02 1 131 139 18 LEU HD1 H 0.78 0.02 2 132 139 18 LEU HD2 H 0.72 0.02 2 133 139 18 LEU HG H 1.39 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constant_list_1 _Saveframe_category coupling_constants _Details . loop_ _Experiment_label '2D DQF-COSY' stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name hDpl(122-139)D124N _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 1 LYS H 1 LYS HA 6.7 . . 0.35 2 3JHNHA 3 ASN H 3 ASN HA 6.6 . . 0.35 3 3JHNHA 4 ASN H 4 ASN HA 7.2 . . 0.35 4 3JHNHA 5 LYS H 5 LYS HA 6.9 . . 0.35 5 3JHNHA 6 LEU H 6 LEU HA 7.6 . . 0.35 6 3JHNHA 7 HIS H 7 HIS HA 6.0 . . 0.35 7 3JHNHA 8 GLN H 8 GLN HA 6.9 . . 0.35 8 3JHNHA 9 GLN H 9 GLN HA 6.8 . . 0.35 9 3JHNHA 10 VAL H 10 VAL HA 7.3 . . 0.35 10 3JHNHA 11 LEU H 11 LEU HA 7.5 . . 0.35 11 3JHNHA 12 TRP H 12 TRP HA 6.4 . . 0.35 12 3JHNHA 13 ARG H 13 ARG HA 7.1 . . 0.35 13 3JHNHA 14 LEU H 14 LEU HA 6.1 . . 0.35 14 3JHNHA 15 VAL H 15 VAL HA 7.9 . . 0.35 15 3JHNHA 16 GLN H 16 GLN HA 7.2 . . 0.35 16 3JHNHA 17 GLU H 17 GLU HA 6.7 . . 0.35 17 3JHNHA 18 LEU H 18 LEU HA 6.2 . . 0.35 stop_ save_