data_21085 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Beta-proline heterochiral trimer made of 5-(2-(trifluoromethyl)phenyl)pyrrolidine-2,4-dicarboxylate monomeric units, ZZ conformation ; _BMRB_accession_number 21085 _BMRB_flat_file_name bmr21085.str _Entry_type new _Submission_date 2019-10-25 _Accession_date 2019-12-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Beta-proline heterochiral trimer made of 5-(2-(trifluoromethyl)phenyl)pyrrolidine-2,4-dicarboxylate monomeric units. Both peptide bonds connecting monomeric units are in Z conformation. Configurations of three beta-proline ring chiral centres of monomeric units are: residue 1 S,S,R; residue 2 S,S,R; residue 3 R,R,S. The (+)-menthyl capping group is at the C-terminal end. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mantsyzov Alexey B. . 2 Kudryavtsev Konstantin V. . 3 Polshakov Vladimir I. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 53 "13C chemical shifts" 41 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-06-18 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 21064 'Beta-Pro EZZ' 21065 'Beta-Pro ZZZ' 21066 'Beta-Pro ZEZ' 21067 'Beta-Pro ZZE' 21068 'Beta-Pro ZZEZ' 21069 'Beta-Pro ZEZZ' 21070 'Beta-Pro homodimer' 21071 'Beta-Pro homodimer, Z conformation' 21072 'Beta-Pro heterodimer, E conformation' 21073 'Beta-Pro heterodimer, Z conformation' 21084 'Beta-Pro alternating trimer, ZZ confirmation' 21085 'Beta-Pro heterochiral trimer, ZZ conformation' 21086 'Beta-Pro heterochiral trimer, ZE conformation' stop_ _Original_release_date 2019-12-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Interplay of Pyrrolidine Units with Homo/Hetero Chirality and CF3-Aryl Substituents on Secondary Structures of beta-Proline Tripeptides in Solution ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32526142 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mantsyzov Alexey B. . 2 Sokolov Mikhail N. . 3 Ivantcova Polina M. . 4 Brase Stefan S. . 5 Polshakov Vladimir I. . 6 Kudryavtsev Konstantin V. . stop_ _Journal_abbreviation 'J. Org. Chem.' _Journal_name_full 'The Journal of organic chemistry' _Journal_volume . _Journal_issue . _Journal_ISSN 1520-6904 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name beta-peptide _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label beta-peptide $beta-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_beta-peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common beta-peptide _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 3 _Mol_residue_sequence ; XXX ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 UVR 2 2 UVR 3 3 UVR 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 $beta-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 $beta-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 $beta-peptide 8 mM 'natural abundance' DMSO-d6 100 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ 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 'chemical shift assignment' 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 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _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_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HMBC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMBC' _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 pressure 1 . atm temperature 298 . 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 TMS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 TMS 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' '2D 1H-1H NOESY' '2D 1H-13C HSQC' '2D 1H-13C HMBC' 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 beta-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 UVR C C 174.198 0.019 . 2 1 1 UVR C5 C 127.354 0.000 . 3 1 1 UVR C6 C 129.605 0.000 . 4 1 1 UVR CA C 62.079 0.012 . 5 1 1 UVR CB C 45.474 0.000 . 6 1 1 UVR CD C 58.958 0.000 . 7 1 1 UVR CG C 35.361 0.008 . 8 1 1 UVR CZ C 52.397 0.000 . 9 1 1 UVR H5 H 7.288 0.003 . 10 1 1 UVR H6 H 7.456 0.003 . 11 1 1 UVR HA H 3.949 0.005 . 12 1 1 UVR HB H 2.850 0.001 . 13 1 1 UVR HD H 3.941 0.006 . 14 1 1 UVR HG1 H 2.486 0.003 . 15 1 1 UVR HG2 H 1.957 0.003 . 16 1 1 UVR HZ1 H 3.694 0.000 1 17 1 1 UVR HZ2 H 3.694 0.000 1 18 1 1 UVR HZ3 H 3.694 0.000 1 19 2 2 UVR C C 167.662 0.022 . 20 2 2 UVR C1 C 137.069 0.012 . 21 2 2 UVR C3 C 125.895 0.000 . 22 2 2 UVR C4 C 128.119 0.000 . 23 2 2 UVR C5 C 132.455 0.000 . 24 2 2 UVR C6 C 130.212 0.000 . 25 2 2 UVR CA C 58.477 0.000 . 26 2 2 UVR CB C 46.470 0.000 . 27 2 2 UVR CD C 58.925 0.000 . 28 2 2 UVR CE C 170.806 0.034 . 29 2 2 UVR CG C 31.034 0.000 . 30 2 2 UVR H3 H 7.595 0.002 . 31 2 2 UVR H4 H 7.343 0.002 . 32 2 2 UVR H5 H 7.030 0.002 . 33 2 2 UVR H6 H 7.322 0.002 . 34 2 2 UVR HA H 5.281 0.003 . 35 2 2 UVR HB H 2.852 0.003 . 36 2 2 UVR HD H 3.529 0.004 . 37 2 2 UVR HG1 H 1.304 0.004 . 38 2 2 UVR HG2 H 1.785 0.008 . 39 2 2 UVR HZ1 H 3.579 0.000 1 40 2 2 UVR HZ2 H 3.579 0.000 1 41 2 2 UVR HZ3 H 3.579 0.000 1 42 3 3 UVR C C 169.504 0.020 . 43 3 3 UVR C1 C 138.203 0.004 . 44 3 3 UVR C3 C 126.891 0.000 . 45 3 3 UVR C4 C 129.589 0.000 . 46 3 3 UVR C5 C 133.623 0.000 . 47 3 3 UVR C6 C 130.068 0.000 . 48 3 3 UVR CA C 59.432 0.005 . 49 3 3 UVR CB C 48.971 0.000 . 50 3 3 UVR CD C 59.373 0.000 . 51 3 3 UVR CE C 171.544 0.018 . 52 3 3 UVR CG C 31.093 0.010 . 53 3 3 UVR CZ C 52.555 0.000 . 54 3 3 UVR H3 H 7.814 0.004 . 55 3 3 UVR H4 H 7.605 0.006 . 56 3 3 UVR H5 H 7.748 0.005 . 57 3 3 UVR H6 H 8.144 0.002 . 58 3 3 UVR HA H 5.527 0.003 . 59 3 3 UVR HB H 3.642 0.003 . 60 3 3 UVR HD H 4.109 0.003 . 61 3 3 UVR HG1 H 2.460 0.007 . 62 3 3 UVR HG2 H 2.288 0.002 . 63 3 3 UVR HZ1 H 3.583 0.002 1 64 3 3 UVR HZ2 H 3.583 0.002 1 65 3 3 UVR HZ3 H 3.583 0.002 1 66 3 3 UVR CM1 C 74.519 0.000 . 67 3 3 UVR CM10 C 16.477 0.019 . 68 3 3 UVR CM2 C 46.525 0.000 . 69 3 3 UVR CM3 C 23.173 0.000 . 70 3 3 UVR CM4 C 33.951 0.016 . 71 3 3 UVR CM5 C 30.866 0.022 . 72 3 3 UVR CM6 C 39.900 0.005 . 73 3 3 UVR CM7 C 22.213 0.000 . 74 3 3 UVR CM8 C 25.880 0.000 . 75 3 3 UVR CM9 C 20.993 0.008 . 76 3 3 UVR H1 H 4.238 0.004 . 77 3 3 UVR H101 H 0.532 0.005 1 78 3 3 UVR H102 H 0.532 0.005 1 79 3 3 UVR H103 H 0.532 0.005 1 80 3 3 UVR H2 H 1.093 0.011 . 81 3 3 UVR H31 H 0.871 0.003 . 82 3 3 UVR H32 H 1.508 0.005 . 83 3 3 UVR H41 H 0.697 0.006 . 84 3 3 UVR H42 H 1.533 0.003 . 85 3 3 UVR H61 H 0.383 0.007 . 86 3 3 UVR H62 H 1.067 0.004 . 87 3 3 UVR H71 H 0.748 0.003 1 88 3 3 UVR H72 H 0.748 0.003 1 89 3 3 UVR H73 H 0.748 0.003 1 90 3 3 UVR H8 H 1.494 0.007 . 91 3 3 UVR H91 H 0.757 0.006 1 92 3 3 UVR H92 H 0.757 0.006 1 93 3 3 UVR H93 H 0.757 0.006 1 94 3 3 UVR HM5 H 1.223 0.004 . stop_ save_