data_21086 ####################### # 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, ZE conformation ; _BMRB_accession_number 21086 _BMRB_flat_file_name bmr21086.str _Entry_type new _Submission_date 2019-10-25 _Accession_date 2019-10-25 _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. Peptide bonds connecting monomeric units are in Z and E conformations. Configurations of three beta-proline ring chiral centres of monomeric units are: residue 1 S,S,R; residue 2 R,R,S; 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" 46 "13C chemical shifts" 37 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' 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 C1 C 138.138 0.000 . 2 1 1 UVR C3 C 126.063 0.000 . 3 1 1 UVR C4 C 128.638 0.000 . 4 1 1 UVR C6 C 129.755 0.000 . 5 1 1 UVR CA C 60.930 0.009 . 6 1 1 UVR CB C 46.825 0.000 . 7 1 1 UVR CD C 58.840 0.000 . 8 1 1 UVR CG C 34.396 0.005 . 9 1 1 UVR H3 H 7.844 0.003 . 10 1 1 UVR H4 H 7.517 0.001 . 11 1 1 UVR H5 H 7.801 0.002 . 12 1 1 UVR H6 H 7.693 0.002 . 13 1 1 UVR HN H 3.128 0.003 . 14 1 1 UVR HA H 4.433 0.002 . 15 1 1 UVR HB H 2.632 0.004 . 16 1 1 UVR HD H 3.746 0.003 . 17 1 1 UVR HG1 H 1.919 0.003 . 18 1 1 UVR HG2 H 1.972 0.004 . 19 2 2 UVR C1 C 137.131 0.000 . 20 2 2 UVR C4 C 128.777 0.000 . 21 2 2 UVR C5 C 127.103 0.000 . 22 2 2 UVR C6 C 129.913 0.020 . 23 2 2 UVR CA C 59.072 0.008 . 24 2 2 UVR CB C 47.297 0.000 . 25 2 2 UVR CD C 58.978 0.000 . 26 2 2 UVR CE C 171.809 0.000 . 27 2 2 UVR CG C 32.081 0.000 . 28 2 2 UVR H4 H 7.434 0.002 . 29 2 2 UVR H5 H 7.546 0.005 . 30 2 2 UVR H6 H 8.272 0.003 . 31 2 2 UVR HA H 4.622 0.002 . 32 2 2 UVR HB H 2.471 0.002 . 33 2 2 UVR HD H 3.956 0.003 . 34 2 2 UVR HG1 H 2.166 0.002 . 35 2 2 UVR HG2 H 1.688 0.007 . 36 3 3 UVR C C 171.743 0.025 . 37 3 3 UVR C1 C 137.459 0.067 . 38 3 3 UVR C3 C 125.726 0.000 . 39 3 3 UVR C4 C 127.731 0.000 . 40 3 3 UVR C6 C 127.749 0.009 . 41 3 3 UVR CA C 61.629 0.010 . 42 3 3 UVR CB C 47.164 0.000 . 43 3 3 UVR CD C 60.561 0.023 . 44 3 3 UVR CE C 171.700 0.010 . 45 3 3 UVR CG C 32.323 0.000 . 46 3 3 UVR H3 H 7.499 0.001 . 47 3 3 UVR H4 H 7.274 0.002 . 48 3 3 UVR H5 H 7.389 0.001 . 49 3 3 UVR H6 H 7.539 0.003 . 50 3 3 UVR HA H 5.168 0.004 . 51 3 3 UVR HB H 3.444 0.001 . 52 3 3 UVR HD H 4.284 0.001 . 53 3 3 UVR HG1 H 2.547 0.003 . 54 3 3 UVR HG2 H 2.643 0.003 . 55 3 3 UVR CM1 C 73.804 0.000 . 56 3 3 UVR CM10 C 16.785 0.016 . 57 3 3 UVR CM2 C 46.538 0.000 . 58 3 3 UVR CM3 C 23.323 0.000 . 59 3 3 UVR CM4 C 33.834 0.005 . 60 3 3 UVR CM5 C 30.698 0.000 . 61 3 3 UVR CM6 C 39.185 0.015 . 62 3 3 UVR CM7 C 22.019 0.000 . 63 3 3 UVR CM8 C 26.255 0.000 . 64 3 3 UVR CM9 C 20.874 0.001 . 65 3 3 UVR H1 H 4.067 0.003 . 66 3 3 UVR H101 H 0.592 0.001 1 67 3 3 UVR H102 H 0.592 0.001 1 68 3 3 UVR H103 H 0.592 0.001 1 69 3 3 UVR H2 H 0.937 0.002 . 70 3 3 UVR H31 H 0.818 0.003 . 71 3 3 UVR H32 H 1.450 0.001 . 72 3 3 UVR H41 H 0.554 0.000 . 73 3 3 UVR H42 H 1.443 0.000 . 74 3 3 UVR H61 H -0.250 0.005 . 75 3 3 UVR H62 H 0.377 0.001 . 76 3 3 UVR H71 H 0.605 0.006 1 77 3 3 UVR H72 H 0.605 0.006 1 78 3 3 UVR H73 H 0.605 0.006 1 79 3 3 UVR H8 H 1.598 0.002 . 80 3 3 UVR H91 H 0.757 0.000 1 81 3 3 UVR H92 H 0.757 0.000 1 82 3 3 UVR H93 H 0.757 0.000 1 83 3 3 UVR HM5 H 1.070 0.000 . stop_ save_