data_20076 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure of a TC5b_D9E miniprotein ; _BMRB_accession_number 20076 _BMRB_flat_file_name bmr20076.str _Entry_type new _Submission_date 2009-02-13 _Accession_date 2009-02-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'TC5b variant' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hudaky Peter . . 2 Straner Pal . . 3 Rovo Petra . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-03-12 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Cooperation between a Salt Bridge and the Hydrophobic Core Triggers Fold Stabilization in a Trp-Cage Miniprotein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18161949 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hudaky Peter . . 2 Straner Pal . . 3 Farkas Viktor . . 4 Varadi Gyorgyi . . 5 Toth Gabor . . 6 Perczel Andras . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 47 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1007 _Page_last 1016 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name TC6b _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TC6b $TC6b 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_TC6b _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TC6b _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 20 _Mol_residue_sequence NLYIQWLKEGGPSSGRPPPS loop_ _Residue_seq_code _Residue_label 1 ASN 2 LEU 3 TYR 4 ILE 5 GLN 6 TRP 7 LEU 8 LYS 9 GLU 10 GLY 11 GLY 12 PRO 13 SER 14 SER 15 GLY 16 ARG 17 PRO 18 PRO 19 PRO 20 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 1L2Y TC5b . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TC6b . . . . . . 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 $TC6b 'recombinant technology' . . . . . 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 $TC6b 2 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'geometry optimization' 'structure solution' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 282 . K pH 6.61 . pH 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 0.0 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' 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 TC6b _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 ASN HA H 3.815 . 1 2 1 1 ASN HB2 H 2.723 . . 3 1 1 ASN HB3 H 2.723 . . 4 1 1 ASN HD21 H 7.013 . 2 5 1 1 ASN HD22 H 7.706 . 2 6 2 2 LEU HA H 4.048 . 1 7 2 2 LEU HB2 H 1.652 . . 8 2 2 LEU HB3 H 1.652 . . 9 2 2 LEU HD1 H 0.824 . . 10 2 2 LEU HD2 H 0.779 . . 11 2 2 LEU HG H 1.313 . 1 12 3 3 TYR H H 8.457 . 1 13 3 3 TYR HA H 4.035 . 1 14 3 3 TYR HB2 H 2.991 . . 15 3 3 TYR HB3 H 2.991 . . 16 3 3 TYR HD1 H 6.896 . . 17 3 3 TYR HD2 H 6.896 . . 18 3 3 TYR HE1 H 6.685 . . 19 3 3 TYR HE2 H 6.685 . . 20 4 4 ILE H H 7.960 . 1 21 4 4 ILE HA H 3.637 . 1 22 4 4 ILE HB H 1.805 . 1 23 4 4 ILE HD1 H 0.690 . 1 24 4 4 ILE HG12 H 1.539 . . 25 4 4 ILE HG13 H 1.233 . 2 26 4 4 ILE HG2 H 0.787 . 1 27 5 5 GLN H H 7.787 . 1 28 5 5 GLN HA H 3.891 . 1 29 5 5 GLN HB2 H 2.022 . . 30 5 5 GLN HB3 H 1.947 . 2 31 5 5 GLN HE21 H 6.792 . 2 32 5 5 GLN HE22 H 7.869 . 2 33 5 5 GLN HG2 H 2.259 . . 34 5 5 GLN HG3 H 2.259 . . 35 6 6 TRP H H 7.890 . 1 36 6 6 TRP HA H 4.107 . 1 37 6 6 TRP HB2 H 3.393 . . 38 6 6 TRP HB3 H 3.018 . 2 39 6 6 TRP HD1 H 6.896 . 1 40 6 6 TRP HE1 H 9.569 . 1 41 6 6 TRP HE3 H 7.002 . 1 42 6 6 TRP HH2 H 6.976 . 1 43 6 6 TRP HZ2 H 7.106 . 1 44 6 6 TRP HZ3 H 7.087 . 1 45 7 7 LEU H H 8.239 . 1 46 7 7 LEU HA H 3.362 . 1 47 7 7 LEU HB2 H 1.721 . . 48 7 7 LEU HB3 H 1.436 . 2 49 7 7 LEU HD1 H 0.786 . . 50 7 7 LEU HD2 H 0.686 . . 51 7 7 LEU HG H 1.252 . 1 52 8 8 LYS H H 8.142 . 1 53 8 8 LYS HA H 3.853 . 1 54 8 8 LYS HB2 H 1.803 . . 55 8 8 LYS HB3 H 1.513 . 2 56 8 8 LYS HE2 H 2.800 . . 57 8 8 LYS HE3 H 2.800 . . 58 8 8 LYS HG2 H 1.412 . . 59 8 8 LYS HG3 H 1.261 . 2 60 9 9 GLU H H 7.604 . 1 61 9 9 GLU HA H 4.035 . 1 62 9 9 GLU HB2 H 2.078 . . 63 9 9 GLU HB3 H 1.813 . 2 64 9 9 GLU HG2 H 2.348 . . 65 9 9 GLU HG3 H 2.348 . . 66 10 10 GLY H H 7.507 . 1 67 10 10 GLY HA2 H 4.019 . . 68 10 10 GLY HA3 H 3.380 . 2 69 11 11 GLY H H 8.110 . 1 70 11 11 GLY HA2 H 3.023 . . 71 11 11 GLY HA3 H 1.154 . 2 72 12 12 PRO HA H 4.439 . 1 73 12 12 PRO HB2 H 2.333 . . 74 12 12 PRO HB3 H 1.976 . 2 75 12 12 PRO HD2 H 3.624 . . 76 12 12 PRO HD3 H 3.237 . 2 77 12 12 PRO HG2 H 1.889 . . 78 12 12 PRO HG3 H 1.889 . . 79 13 13 SER H H 7.744 . 1 80 13 13 SER HA H 4.307 . 1 81 13 13 SER HB2 H 3.782 . . 82 13 13 SER HB3 H 3.782 . . 83 14 14 SER H H 8.068 . 1 84 14 14 SER HA H 4.100 . 1 85 14 14 SER HB2 H 3.720 . . 86 14 14 SER HB3 H 3.463 . 2 87 15 15 GLY H H 7.893 . 1 88 15 15 GLY HA2 H 4.100 . . 89 15 15 GLY HA3 H 3.705 . 2 90 16 16 ARG H H 7.955 . 1 91 16 16 ARG HA H 4.771 . 1 92 16 16 ARG HB2 H 1.708 . . 93 16 16 ARG HB3 H 1.708 . . 94 16 16 ARG HD2 H 3.116 . . 95 16 16 ARG HD3 H 3.116 . . 96 16 16 ARG HG2 H 1.599 . . 97 16 16 ARG HG3 H 1.513 . 2 98 17 17 PRO HA H 4.582 . 1 99 17 17 PRO HB2 H 2.163 . . 100 17 17 PRO HB3 H 1.842 . 2 101 17 17 PRO HD2 H 3.715 . . 102 17 17 PRO HD3 H 3.510 . 2 103 17 17 PRO HG2 H 1.639 . . 104 17 17 PRO HG3 H 1.639 . . 105 18 18 PRO HA H 4.302 . 1 106 18 18 PRO HB2 H 2.116 . . 107 18 18 PRO HB3 H 1.832 . 2 108 18 18 PRO HD2 H 4.040 . . 109 18 18 PRO HD3 H 3.387 . 2 110 18 18 PRO HG2 H 1.638 . . 111 18 18 PRO HG3 H 1.568 . 2 112 19 19 PRO HA H 4.201 . 1 113 19 19 PRO HB2 H 2.078 . . 114 19 19 PRO HB3 H 1.809 . 2 115 19 19 PRO HD2 H 3.026 . . 116 19 19 PRO HD3 H 2.884 . 2 117 19 19 PRO HG2 H 1.686 . . 118 19 19 PRO HG3 H 1.686 . . 119 20 20 SER H H 7.801 . 1 120 20 20 SER HA H 4.032 . 1 121 20 20 SER HB2 H 3.638 . . 122 20 20 SER HB3 H 3.638 . . stop_ save_