data_18519 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Retro Trp-cage peptide ; _BMRB_accession_number 18519 _BMRB_flat_file_name bmr18519.str _Entry_type original _Submission_date 2012-06-13 _Accession_date 2012-06-13 _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 Bathula 'Sreenivas Reddy' . . 2 Sklenar Vladimir . . 3 Zidek Lukas . . 4 Vondrasek Jiri . . 5 Vymetal Jiri . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 124 "13C chemical shifts" 65 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-12-05 update author 'update assignments, etc.' 2012-07-13 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'From a Structure to Disorder. Retro Operation on the Trp-cage Miniprotein Sequence Produces an Unstructured Molecule Capable of Folding Similar to the Original Only upon TFE Addition' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vymetal Jiri . . 2 Bathula 'Sreenivas Reddy' . . 3 Cerny Jiri . . 4 Chaloupkova Radka . . 5 Zidek Lukas . . 6 Sklenar Vladimir . . 7 Vondrasek Jiri . . stop_ _Journal_abbreviation 'Protein Eng. Des. Sel.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Retro Trp-cage peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Retro Trp-cage peptide' $Retro_Trp-cage_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_Retro_Trp-cage_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Retro_Trp-cage_peptide _Molecular_mass 2171.435 _Mol_thiol_state 'not presnet' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 20 _Mol_residue_sequence SPPPRGSSPGGDKLWQIYLN loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 SER 2 2 PRO 3 3 PRO 4 4 PRO 5 5 ARG 6 6 GLY 7 7 SER 8 8 SER 9 9 PRO 10 10 GLY 11 11 GLY 12 12 ASP 13 13 LYS 14 14 LEU 15 15 TRP 16 16 GLN 17 17 ILE 18 18 TYR 19 19 LEU 20 20 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-22 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 2LUF "Retro Trp-cage Peptide" 100.00 20 100.00 100.00 2.22e-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 $Retro_Trp-cage_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 $Retro_Trp-cage_peptide '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 H2O 60 % 'natural abundance' D2O 10 % '[U-100% 2H]' TFE 30 % '[U-99% 2H]' 'sodium azide' 0.03 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 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_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' 'peak picking' stop_ _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version . loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _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 'ionic strength' 0.015 . M pH 7.0 . pH pressure 1 . atm temperature 275 . K 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 C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 water H 1 protons ppm 5.039 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_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-1H TOCSY' '2D 1H-13C HSQC' 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 'Retro Trp-cage 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 1 1 SER HA H 4.109 . 1 2 1 1 SER HB2 H 3.806 . 2 3 1 1 SER HB3 H 3.894 . 2 4 1 1 SER CA C 56.679 . 1 5 1 1 SER CB C 62.688 . 1 6 2 2 PRO HA H 4.582 . 1 7 2 2 PRO HB2 H 1.723 . 1 8 2 2 PRO HB3 H 2.194 . 1 9 2 2 PRO HG2 H 1.783 . 1 10 2 2 PRO HG3 H 1.783 . 1 11 2 2 PRO HD2 H 3.343 . 2 12 2 2 PRO HD3 H 3.495 . 2 13 2 2 PRO CA C 61.587 . 1 14 2 2 PRO CB C 30.152 . 1 15 2 2 PRO CG C 27.121 . 1 16 2 2 PRO CD C 50.157 . 1 17 3 3 PRO HA H 4.627 . 1 18 3 3 PRO HB2 H 1.873 . 1 19 3 3 PRO HB3 H 2.277 . 1 20 3 3 PRO HG2 H 1.990 . 1 21 3 3 PRO HG3 H 1.990 . 1 22 3 3 PRO HD2 H 3.454 . 2 23 3 3 PRO HD3 H 3.692 . 2 24 3 3 PRO CA C 61.315 . 1 25 3 3 PRO CB C 30.450 . 1 26 3 3 PRO CG C 27.128 . 1 27 3 3 PRO CD C 49.965 . 1 28 4 4 PRO HA H 4.407 . 1 29 4 4 PRO HB2 H 1.858 . 1 30 4 4 PRO HB3 H 2.281 . 1 31 4 4 PRO HG2 H 1.999 . 1 32 4 4 PRO HG3 H 1.999 . 1 33 4 4 PRO HD2 H 3.527 . 2 34 4 4 PRO HD3 H 3.742 . 2 35 4 4 PRO CA C 62.871 . 1 36 4 4 PRO CB C 31.820 . 1 37 4 4 PRO CG C 27.350 . 1 38 4 4 PRO CD C 50.173 . 1 39 5 5 ARG H H 8.457 . 1 40 5 5 ARG HA H 4.174 . 1 41 5 5 ARG HB2 H 1.575 . 2 42 5 5 ARG HB3 H 1.721 . 2 43 5 5 ARG HG2 H 1.473 . 1 44 5 5 ARG HG3 H 1.473 . 1 45 5 5 ARG HD2 H 2.974 . 1 46 5 5 ARG HD3 H 2.974 . 1 47 5 5 ARG HE H 7.139 . 1 48 5 5 ARG CA C 56.864 . 1 49 5 5 ARG CB C 30.458 . 1 50 5 5 ARG CG C 26.816 . 1 51 5 5 ARG CD C 43.052 . 1 52 6 6 GLY H H 9.032 . 1 53 6 6 GLY HA2 H 3.942 . 2 54 6 6 GLY HA3 H 4.034 . 2 55 6 6 GLY CA C 44.996 . 1 56 7 7 SER H H 8.204 . 1 57 7 7 SER HA H 4.471 . 1 58 7 7 SER HB2 H 3.844 . 2 59 7 7 SER HB3 H 3.923 . 2 60 7 7 SER CA C 58.842 . 1 61 7 7 SER CB C 63.992 . 1 62 8 8 SER H H 8.242 . 1 63 8 8 SER HA H 4.832 . 1 64 8 8 SER HB2 H 3.916 . 1 65 8 8 SER HB3 H 3.916 . 1 66 8 8 SER CA C 56.407 . 1 67 8 8 SER CB C 63.516 . 1 68 9 9 PRO HA H 4.395 . 1 69 9 9 PRO HB2 H 1.954 . 1 70 9 9 PRO HB3 H 2.320 . 1 71 9 9 PRO HG2 H 2.093 . 1 72 9 9 PRO HG3 H 2.093 . 1 73 9 9 PRO HD2 H 3.750 . 2 74 9 9 PRO HD3 H 3.819 . 2 75 9 9 PRO CA C 64.399 . 1 76 9 9 PRO CB C 31.672 . 1 77 9 9 PRO CG C 27.376 . 1 78 9 9 PRO CD C 50.567 . 1 79 10 10 GLY H H 8.506 . 1 80 10 10 GLY HA2 H 3.928 . 1 81 10 10 GLY HA3 H 3.928 . 1 82 10 10 GLY CA C 45.650 . 1 83 11 11 GLY H H 8.245 . 1 84 11 11 GLY HA2 H 3.906 . 2 85 11 11 GLY HA3 H 4.008 . 2 86 11 11 GLY CA C 46.326 . 1 87 12 12 ASP H H 8.433 . 1 88 12 12 ASP HA H 4.647 . 1 89 12 12 ASP HB2 H 2.772 . 1 90 12 12 ASP HB3 H 2.772 . 1 91 12 12 ASP CA C 55.952 . 1 92 12 12 ASP CB C 40.341 . 1 93 13 13 LYS H H 8.078 . 1 94 13 13 LYS HA H 4.179 . 1 95 13 13 LYS HB2 H 1.889 . 1 96 13 13 LYS HB3 H 1.889 . 1 97 13 13 LYS HG2 H 1.488 . 2 98 13 13 LYS HG3 H 1.550 . 2 99 13 13 LYS HD2 H 1.712 . 1 100 13 13 LYS HD3 H 1.712 . 1 101 13 13 LYS HE2 H 2.973 . 1 102 13 13 LYS HE3 H 2.973 . 1 103 13 13 LYS CA C 58.463 . 1 104 13 13 LYS CB C 32.032 . 1 105 13 13 LYS CG C 24.791 . 1 106 13 13 LYS CD C 28.771 . 1 107 13 13 LYS CE C 42.006 . 1 108 14 14 LEU H H 7.933 . 1 109 14 14 LEU HA H 4.119 . 1 110 14 14 LEU HB2 H 1.580 . 2 111 14 14 LEU HB3 H 1.780 . 2 112 14 14 LEU HG H 1.663 . 1 113 14 14 LEU HD1 H 0.833 . 2 114 14 14 LEU HD2 H 0.900 . 2 115 14 14 LEU CA C 57.696 . 1 116 14 14 LEU CB C 41.266 . 1 117 14 14 LEU CG C 26.867 . 1 118 14 14 LEU CD1 C 23.031 . 2 119 14 14 LEU CD2 C 24.046 . 2 120 15 15 TRP H H 7.965 . 1 121 15 15 TRP HA H 4.422 . 1 122 15 15 TRP HB2 H 3.384 . 1 123 15 15 TRP HB3 H 3.384 . 1 124 15 15 TRP HD1 H 7.316 . 1 125 15 15 TRP HE1 H 10.065 . 1 126 15 15 TRP HE3 H 7.561 . 1 127 15 15 TRP HZ2 H 7.424 . 1 128 15 15 TRP HZ3 H 7.013 . 1 129 15 15 TRP HH2 H 7.184 . 1 130 15 15 TRP CA C 60.242 . 1 131 15 15 TRP CB C 28.996 . 1 132 15 15 TRP CE3 C 120.370 . 1 133 15 15 TRP CZ2 C 114.554 . 1 134 15 15 TRP CH2 C 124.289 . 1 135 16 16 GLN H H 7.860 . 1 136 16 16 GLN HA H 3.867 . 1 137 16 16 GLN HB2 H 2.133 . 1 138 16 16 GLN HB3 H 2.133 . 1 139 16 16 GLN HG2 H 2.259 . 1 140 16 16 GLN HG3 H 2.259 . 1 141 16 16 GLN HE21 H 6.783 . 1 142 16 16 GLN HE22 H 7.278 . 1 143 16 16 GLN CA C 59.067 . 1 144 16 16 GLN CB C 28.243 . 1 145 16 16 GLN CG C 33.732 . 1 146 17 17 ILE H H 7.930 . 1 147 17 17 ILE HA H 3.701 . 1 148 17 17 ILE HB H 1.973 . 1 149 17 17 ILE HG12 H 1.087 . 2 150 17 17 ILE HG13 H 1.712 . 2 151 17 17 ILE HG2 H 0.828 . 1 152 17 17 ILE HD1 H 0.834 . 1 153 17 17 ILE CA C 64.758 . 1 154 17 17 ILE CB C 38.089 . 1 155 17 17 ILE CG1 C 28.557 . 1 156 17 17 ILE CG2 C 16.512 . 1 157 17 17 ILE CD1 C 12.807 . 1 158 18 18 TYR H H 8.277 . 1 159 18 18 TYR HA H 4.191 . 1 160 18 18 TYR HB2 H 3.054 . 1 161 18 18 TYR HB3 H 3.054 . 1 162 18 18 TYR HD1 H 6.925 . 1 163 18 18 TYR HD2 H 6.925 . 1 164 18 18 TYR HE1 H 6.736 . 1 165 18 18 TYR HE2 H 6.736 . 1 166 18 18 TYR CA C 60.650 . 1 167 18 18 TYR CB C 38.257 . 1 168 18 18 TYR CE1 C 117.873 . 1 169 18 18 TYR CE2 C 117.873 . 1 170 19 19 LEU H H 8.339 . 1 171 19 19 LEU HA H 3.956 . 1 172 19 19 LEU HB2 H 1.438 . 2 173 19 19 LEU HB3 H 1.725 . 2 174 19 19 LEU HG H 1.438 . 1 175 19 19 LEU HD1 H 0.844 . 2 176 19 19 LEU HD2 H 0.845 . 2 177 19 19 LEU CA C 56.525 . 1 178 19 19 LEU CB C 42.055 . 1 179 19 19 LEU CG C 26.820 . 1 180 19 19 LEU CD1 C 22.312 . 2 181 19 19 LEU CD2 C 24.842 . 1 182 20 20 ASN H H 7.732 . 1 183 20 20 ASN HA H 4.556 . 1 184 20 20 ASN HB2 H 2.753 . 2 185 20 20 ASN HB3 H 2.791 . 2 186 20 20 ASN HD21 H 7.731 . 1 187 20 20 ASN HD22 H 6.816 . 1 188 20 20 ASN CA C 53.963 . 1 189 20 20 ASN CB C 39.489 . 1 stop_ save_