data_15169 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Trp-cage: Optimizing the Stability of a Globular Miniprotein ; _BMRB_accession_number 15169 _BMRB_flat_file_name bmr15169.str _Entry_type new _Submission_date 2007-03-09 _Accession_date 2007-03-09 _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 Barua Bipasha . . 2 Andersen Niels H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-02 update BMRB 'complete entry citation' 2008-02-11 original author 'original release' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_Trp-cage_JMB _Saveframe_category citation _Citation_full . _Citation_title 'The Trp-cage: optimizing the stability of a globular miniprotein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18203802 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Barua Bipasha . . 2 Lin Jasper C. . 3 Williams Victoria D. . 4 Kummler Phillip . . 5 Neidigh Jonathan W. . 6 Andersen Niels H. . stop_ _Journal_abbreviation 'Protein Eng. Des. Sel.' _Journal_name_full . _Journal_volume 21 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 171 _Page_last 185 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name monomer _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label trp-cage $TRPCAGE 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_TRPCAGE _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TRPCAGE _Molecular_mass 2092.290 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 20 _Mol_residue_sequence DAYAQWLKDGGPSSGRPPPS loop_ _Residue_seq_code _Residue_label 1 ASP 2 ALA 3 TYR 4 ALA 5 GLN 6 TRP 7 LEU 8 LYS 9 ASP 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 2015-06-23 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 2JOF "The Trp-Cage: Optimizing The Stability Of A Globular Miniprotein" 100.00 20 100.00 100.00 4.08e-04 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TRPCAGE . . . . . . 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 $TRPCAGE 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1.0-2.0 mM TC10b' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TRPCAGE . mM 1.0 2.0 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_AMBER _Saveframe_category software _Name AMBER _Version 6 loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll' . . stop_ loop_ _Task refinement stop_ _Details . save_ 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 'structure solution' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.11 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version 2.3 loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version 2.6 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 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 280 0.1 K pH 7.00 0.05 pH pressure 1 . atm 'ionic strength' 0.020 0.001 M 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 0.000 internal direct . . . 1 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 trp-cage _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 ASP HA H 4.245 0.005 1 2 1 1 ASP HB2 H 2.981 0.005 1 3 1 1 ASP HB3 H 2.981 0.005 1 4 2 2 ALA HA H 4.272 0.005 1 5 2 2 ALA HB H 1.518 0.005 1 6 3 3 TYR H H 8.899 0.005 1 7 3 3 TYR HA H 4.030 0.005 1 8 3 3 TYR HB2 H 3.135 0.005 1 9 3 3 TYR HB3 H 3.135 0.005 1 10 3 3 TYR HD1 H 7.097 0.005 3 11 3 3 TYR HD2 H 7.097 0.005 3 12 3 3 TYR HE1 H 6.830 0.005 3 13 3 3 TYR HE2 H 6.830 0.005 3 14 4 4 ALA H H 8.345 0.005 1 15 4 4 ALA HA H 4.114 0.005 1 16 4 4 ALA HB H 1.581 0.005 1 17 5 5 GLN H H 8.123 0.005 1 18 5 5 GLN HA H 3.899 0.005 1 19 5 5 GLN HB2 H 2.152 0.005 2 20 5 5 GLN HB3 H 2.240 0.005 2 21 6 6 TRP H H 8.147 0.005 1 22 6 6 TRP HA H 4.233 0.005 1 23 6 6 TRP HB2 H 3.143 0.005 1 24 6 6 TRP HB3 H 3.556 0.005 1 25 6 6 TRP HD1 H 6.981 0.005 1 26 6 6 TRP HE1 H 9.712 0.005 1 27 6 6 TRP HE3 H 6.974 0.005 1 28 6 6 TRP HH2 H 7.217 0.005 1 29 6 6 TRP HZ2 H 7.184 0.005 1 30 6 6 TRP HZ3 H 7.130 0.005 1 31 7 7 LEU H H 8.366 0.005 1 32 7 7 LEU HA H 3.389 0.005 1 33 7 7 LEU HB2 H 1.897 0.005 1 34 7 7 LEU HB3 H 1.353 0.005 1 35 7 7 LEU HD1 H 0.995 0.005 1 36 7 7 LEU HD2 H 0.865 0.005 1 37 7 7 LEU HG H 1.628 0.005 1 38 8 8 LYS H H 8.114 0.005 1 39 8 8 LYS HA H 3.926 0.005 1 40 8 8 LYS HB2 H 1.975 0.005 2 41 8 8 LYS HB3 H 1.897 0.005 2 42 9 9 ASP H H 8.001 0.005 1 43 9 9 ASP HA H 4.511 0.005 1 44 9 9 ASP HB2 H 2.716 0.005 1 45 9 9 ASP HB3 H 2.932 0.005 1 46 10 10 GLY H H 7.513 0.005 1 47 10 10 GLY HA2 H 4.170 0.005 2 48 10 10 GLY HA3 H 3.447 0.005 2 49 11 11 GLY H H 8.502 0.005 1 50 12 12 PRO HA H 4.645 0.005 1 51 12 12 PRO HB2 H 2.070 0.005 1 52 12 12 PRO HB3 H 2.539 0.005 1 53 12 12 PRO HD2 H 3.835 0.005 1 54 12 12 PRO HD3 H 3.487 0.005 1 55 12 12 PRO HG2 H 2.175 0.005 1 56 12 12 PRO HG3 H 2.175 0.005 1 57 13 13 SER H H 7.724 0.005 1 58 13 13 SER HA H 4.487 0.005 1 59 13 13 SER HB2 H 3.932 0.005 1 60 13 13 SER HB3 H 3.932 0.005 1 61 14 14 SER H H 8.252 0.005 1 62 14 14 SER HA H 4.128 0.005 1 63 14 14 SER HB2 H 3.464 0.005 1 64 14 14 SER HB3 H 3.841 0.005 1 65 15 15 GLY H H 7.981 0.005 1 66 15 15 GLY HA2 H 3.796 0.005 1 67 15 15 GLY HA3 H 4.293 0.005 1 68 16 16 ARG H H 8.164 0.005 1 69 16 16 ARG HA H 5.084 0.005 1 70 16 16 ARG HB2 H 1.812 0.005 2 71 16 16 ARG HB3 H 1.912 0.005 2 72 16 16 ARG HD2 H 3.217 0.005 2 73 16 16 ARG HD3 H 3.296 0.005 2 74 16 16 ARG HE H 7.748 0.005 1 75 16 16 ARG HG2 H 1.654 0.005 2 76 16 16 ARG HG3 H 1.806 0.005 2 77 17 17 PRO HA H 4.769 0.005 1 78 17 17 PRO HB2 H 1.802 0.005 1 79 17 17 PRO HB3 H 2.349 0.005 1 80 17 17 PRO HD2 H 3.680 0.005 1 81 17 17 PRO HD3 H 3.864 0.005 1 82 17 17 PRO HG2 H 1.988 0.005 2 83 17 17 PRO HG3 H 1.995 0.005 2 84 18 18 PRO HA H 2.401 0.005 1 85 18 18 PRO HB2 H 1.305 0.005 1 86 18 18 PRO HB3 H 0.208 0.005 1 87 18 18 PRO HD2 H 3.513 0.005 1 88 18 18 PRO HD3 H 3.513 0.005 1 89 18 18 PRO HG2 H 1.733 0.005 2 90 18 18 PRO HG3 H 1.657 0.005 2 91 19 19 PRO HA H 4.340 0.005 1 92 19 19 PRO HB2 H 1.996 0.005 1 93 19 19 PRO HB3 H 2.209 0.005 1 94 19 19 PRO HD2 H 2.933 0.005 1 95 19 19 PRO HD3 H 3.143 0.005 1 96 19 19 PRO HG2 H 1.793 0.005 1 97 19 19 PRO HG3 H 1.846 0.005 1 98 20 20 SER H H 7.968 0.005 1 99 20 20 SER HA H 4.158 0.005 1 100 20 20 SER HB2 H 3.772 0.005 1 101 20 20 SER HB3 H 3.772 0.005 1 stop_ save_