data_30453 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Trp-cage tr16b R16Nva : Elimination of pH Dependent Interactions ; _BMRB_accession_number 30453 _BMRB_flat_file_name bmr30453.str _Entry_type original _Submission_date 2018-04-14 _Accession_date 2018-04-14 _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 Byrne A. . . 2 Andersen N. H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-03-07 original BMRB . stop_ _Original_release_date 2018-04-26 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Reversing the typical pH stability profile of the Trp-cage ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30779444 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Graham K. A. . 2 Byrne A. . . 3 Son R. . . 4 Andersen N. H. . stop_ _Journal_abbreviation Biopolymers _Journal_name_full Biopolymers _Journal_volume . _Journal_issue . _Journal_ISSN 1097-0282 _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e23260 _Page_last e23260 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ALA-TYR-ALA-GLN-TRP-LEU-ALA-ASP-DAL-GLY-PRO-ALA-SER-DAL-NVA-PRO-PRO-PRO-SER _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 1893.083 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 21 _Mol_residue_sequence ; XAYAQWLADXGPASXXPPPS X ; loop_ _Residue_seq_code _Residue_label 1 ACE 2 ALA 3 TYR 4 ALA 5 GLN 6 TRP 7 LEU 8 ALA 9 ASP 10 DAL 11 GLY 12 PRO 13 ALA 14 SER 15 DAL 16 NVA 17 PRO 18 PRO 19 PRO 20 SER 21 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'ACETYL GROUP' _BMRB_code ACE _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _Mol_paramagnetic . _Details . 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_DAL _Saveframe_category polymer_residue _Mol_type 'D-PEPTIDE LINKING' _Name_common D-ALANINE _BMRB_code DAL _PDB_code DAL _Standard_residue_derivative . _Molecular_mass 89.093 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HXT HXT 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 CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB HB1 ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ save_chem_comp_NVA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common NORVALINE _BMRB_code NVA _PDB_code NVA _Standard_residue_derivative . _Molecular_mass 117.146 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HD1 HD1 H . 0 . ? HD2 HD2 H . 0 . ? HD3 HD3 H . 0 . ? HXT HXT 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 CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? SING CD HD1 ? ? SING CD HD2 ? ? SING CD HD3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'AMINO GROUP' _BMRB_code NH2 _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details . 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 $entity_1 . 32630 . . . . 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 $entity_1 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM peptide, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CNS _Version 1.2 loop_ _Vendor _Address _Electronic_address 'Brunger A. T. et.al.' . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address 'Goddard & Kneller' . . stop_ loop_ _Task 'chemical shift calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.019 0.001 M pH 2.5 .05 pH pressure 1 0.1 atm temperature 280 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 . . . 1.0 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-1H TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name entity_1 _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 2 ALA H H 8.683 0.02 1 2 2 2 ALA HA H 4.194 0.01 1 3 2 2 ALA HB H 1.480 0.01 1 4 3 3 TYR H H 9.111 0.02 1 5 3 3 TYR HA H 4.062 0.01 1 6 3 3 TYR HB2 H 3.096 0.01 . 7 3 3 TYR HB3 H 3.096 0.01 . 8 3 3 TYR HD1 H 7.086 0.01 . 9 3 3 TYR HD2 H 7.086 0.01 . 10 3 3 TYR HE1 H 6.817 0.01 . 11 3 3 TYR HE2 H 6.817 0.01 . 12 4 4 ALA H H 8.546 0.02 1 13 4 4 ALA HA H 4.124 0.01 1 14 4 4 ALA HB H 1.539 0.01 1 15 5 5 GLN H H 8.101 0.02 1 16 5 5 GLN HA H 4.090 0.01 1 17 5 5 GLN HB2 H 2.167 0.01 . 18 5 5 GLN HB3 H 2.167 0.01 . 19 5 5 GLN HG2 H 2.389 0.01 . 20 5 5 GLN HG3 H 2.389 0.01 . 21 5 5 GLN HE21 H 7.112 0.01 . 22 5 5 GLN HE22 H 7.455 0.01 . 23 6 6 TRP H H 8.126 0.02 1 24 6 6 TRP HA H 4.228 0.01 1 25 6 6 TRP HB2 H 3.163 0.01 . 26 6 6 TRP HB3 H 3.544 0.01 . 27 6 6 TRP HD1 H 7.096 0.01 1 28 6 6 TRP HE1 H 9.593 0.01 1 29 6 6 TRP HE3 H 6.952 0.01 1 30 6 6 TRP HZ2 H 7.197 0.01 1 31 6 6 TRP HZ3 H 7.095 0.01 1 32 6 6 TRP HH2 H 7.217 0.01 1 33 7 7 LEU H H 8.582 0.02 1 34 7 7 LEU HA H 3.315 0.01 1 35 7 7 LEU HB2 H 1.814 0.01 . 36 7 7 LEU HB3 H 1.438 0.01 . 37 7 7 LEU HG H 1.603 0.01 1 38 7 7 LEU HD1 H 0.980 0.01 . 39 7 7 LEU HD2 H 0.901 0.01 . 40 8 8 ALA H H 8.189 0.02 1 41 8 8 ALA HA H 4.070 0.01 1 42 8 8 ALA HB H 1.482 0.01 1 43 9 9 ASP H H 7.791 0.02 1 44 9 9 ASP HA H 4.629 0.01 1 45 9 9 ASP HB2 H 2.986 0.01 . 46 9 9 ASP HB3 H 3.081 0.01 . 47 10 10 DAL H H 7.413 0.02 1 48 10 10 DAL HA H 4.374 0.01 1 49 10 10 DAL HB1 H 1.268 0.01 1 50 10 10 DAL HB2 H 1.268 0.01 1 51 10 10 DAL HB3 H 1.268 0.01 1 52 11 11 GLY H H 8.311 0.02 1 53 11 11 GLY HA2 H 0.752 0.01 . 54 11 11 GLY HA3 H 3.070 0.01 . 55 12 12 PRO HA H 4.617 0.01 1 56 12 12 PRO HB2 H 2.040 0.01 . 57 12 12 PRO HB3 H 2.541 0.01 . 58 12 12 PRO HG2 H 2.196 0.01 . 59 12 12 PRO HG3 H 2.189 0.01 . 60 12 12 PRO HD2 H 3.748 0.01 . 61 12 12 PRO HD3 H 3.452 0.01 . 62 13 13 ALA H H 7.350 0.02 1 63 13 13 ALA HA H 4.228 0.01 1 64 13 13 ALA HB H 1.415 0.01 1 65 14 14 SER H H 8.092 0.02 1 66 14 14 SER HA H 4.165 0.01 1 67 14 14 SER HB2 H 3.907 0.01 . 68 14 14 SER HB3 H 3.569 0.01 . 69 15 15 DAL H H 7.334 0.01 1 70 15 15 DAL HA H 4.428 0.01 1 71 15 15 DAL HB1 H 1.502 0.01 1 72 15 15 DAL HB2 H 1.502 0.01 1 73 15 15 DAL HB3 H 1.502 0.01 1 74 17 17 PRO HA H 4.587 0.01 1 75 17 17 PRO HB2 H 1.748 0.01 . 76 17 17 PRO HB3 H 2.131 0.01 . 77 17 17 PRO HG2 H 1.992 0.01 . 78 17 17 PRO HG3 H 1.992 0.01 . 79 17 17 PRO HD2 H 3.692 0.01 . 80 17 17 PRO HD3 H 3.846 0.01 . 81 18 18 PRO HA H 2.559 0.01 1 82 18 18 PRO HB2 H 1.316 0.01 . 83 18 18 PRO HB3 H 0.444 0.01 . 84 18 18 PRO HG2 H 1.683 0.01 . 85 18 18 PRO HG3 H 1.733 0.01 . 86 18 18 PRO HD2 H 3.479 0.01 . 87 18 18 PRO HD3 H 3.479 0.01 . 88 19 19 PRO HA H 4.352 0.01 1 89 19 19 PRO HB2 H 2.249 0.01 . 90 19 19 PRO HB3 H 2.249 0.01 . 91 19 19 PRO HG2 H 1.839 0.01 . 92 19 19 PRO HG3 H 1.839 0.01 . 93 19 19 PRO HD2 H 2.915 0.01 . 94 19 19 PRO HD3 H 3.171 0.01 . 95 20 20 SER HA H 4.287 0.01 1 96 20 20 SER HB2 H 3.820 0.01 . 97 20 20 SER HB3 H 3.820 0.01 . 98 21 21 NH2 HN1 H 8.381 0.02 1 stop_ save_