data_25134 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; H, N, Calpha assignments of AMA1-bound R1 peptide at pH 7 and 313k ; _BMRB_accession_number 25134 _BMRB_flat_file_name bmr25134.str _Entry_type original _Submission_date 2014-08-07 _Accession_date 2014-08-07 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone assignment of R1 peptide bound to malarial protein Apical Membrane Antigen 1 (AMA1)' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Geqing . . 2 MacRaild Christopher A. . 3 Mohanty Biswaranjan . . 4 Mobli Mehdi . . 5 Norton Raymond S. . 6 Scanlon Martin J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 12 "13C chemical shifts" 15 "15N chemical shifts" 12 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-07-11 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 19864 'R1 peptide' stop_ _Original_release_date 2014-08-07 save_ ############################# # Citation for this entry # ############################# save_Citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Identification of the Binding Site of Apical Membrane Antigen 1 (AMA1) Inhibitors Using a Paramagnetic Probe ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30653832 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Akter Mansura . . 2 Drinkwater Nyssa . . 3 Devine Shane M. . 4 Drew Simon C. . 5 Krishnarjuna Bankala . . 6 Debono Cael O. . 7 Wang Geqing . . 8 Scanlon Martin J. . 9 Scammells Peter J. . 10 McGowan Sheena . . 11 MacRaild Christopher A. . 12 Norton Raymond S. . stop_ _Journal_abbreviation ChemMedChem _Journal_name_full ChemMedChem _Journal_volume 14 _Journal_issue 5 _Journal_ISSN 1860-7187 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 603 _Page_last 612 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name AMA1-R1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'R1 peptide' $R1_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_R1_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common R1_peptide _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 20 _Mol_residue_sequence ; VFAEFLPLFSKFGSRMHILK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 VAL 2 2 PHE 3 3 ALA 4 4 GLU 5 5 PHE 6 6 LEU 7 7 PRO 8 8 LEU 9 9 PHE 10 10 SER 11 11 LYS 12 12 PHE 13 13 GLY 14 14 SER 15 15 ARG 16 16 MET 17 17 HIS 18 18 ILE 19 19 LEU 20 20 LYS 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 $R1_peptide 'E. coli' 562 Bacteria . Escherichia coli 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 $R1_peptide 'recombinant technology' . Escherichia coli . pET32a 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 $R1_peptide 0.3 mM '[U-95% 13C; U-90% 15N; U-72% 2H]' AMA1 0.32 mM '[U-72% 2H]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium azide' 0.01 '% w/v' 'natural abundance' 'Roche protease inhibitor cocktail' 0.2 '% w/v' 'natural abundance' Arginine 50 mM 'natural abundance' 'Glutamic acid' 50 mM 'natural abundance' D2O 5 '% v/v' 'natural abundance' H2O 90 % '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 processing stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details 'University of Queensland' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'Monash Institute of Pharmaceutical Science' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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' 0.02 . M pH 7.0 . pH pressure 1 . atm temperature 313 . 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 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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-15N HSQC' '3D HNCA' '3D HN(CO)CA' 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 'R1 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 2 2 PHE CA C 56.893 0.000 . 2 3 3 ALA H H 8.266 0.000 . 3 3 3 ALA CA C 51.059 0.000 . 4 3 3 ALA N N 124.491 0.000 . 5 4 4 GLU H H 8.733 0.000 . 6 4 4 GLU CA C 57.708 0.000 . 7 4 4 GLU N N 118.832 0.000 . 8 5 5 PHE CA C 56.492 0.000 . 9 6 6 LEU H H 8.699 0.000 . 10 6 6 LEU CA C 52.794 0.000 . 11 6 6 LEU N N 125.811 0.000 . 12 7 7 PRO CA C 62.009 0.000 . 13 8 8 LEU H H 8.115 0.000 . 14 8 8 LEU CA C 54.096 0.000 . 15 8 8 LEU N N 123.076 0.000 . 16 9 9 PHE H H 7.492 0.000 . 17 9 9 PHE N N 128.328 0.000 . 18 12 12 PHE H H 8.077 0.000 . 19 12 12 PHE CA C 56.605 0.000 . 20 12 12 PHE N N 116.906 0.000 . 21 13 13 GLY H H 8.599 0.000 . 22 13 13 GLY CA C 43.141 0.000 . 23 13 13 GLY N N 107.890 0.000 . 24 15 15 ARG CA C 55.281 0.000 . 25 16 16 MET H H 9.359 0.000 . 26 16 16 MET CA C 58.769 0.000 . 27 16 16 MET N N 127.824 0.000 . 28 17 17 HIS H H 8.757 0.000 . 29 17 17 HIS CA C 55.241 0.000 . 30 17 17 HIS N N 118.400 0.000 . 31 18 18 ILE H H 8.051 0.000 . 32 18 18 ILE CA C 60.652 0.000 . 33 18 18 ILE N N 122.626 0.000 . 34 19 19 LEU H H 8.199 0.000 . 35 19 19 LEU CA C 54.727 0.000 . 36 19 19 LEU N N 126.771 0.000 . 37 20 20 LYS H H 7.791 0.000 . 38 20 20 LYS CA C 57.380 0.000 . 39 20 20 LYS N N 127.634 0.000 . stop_ save_