data_17253 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and backbone 15N chemical shifts of a peptide inhibitor for the Malaria surface protein, Apical Membrane Antigen 1 ; _BMRB_accession_number 17253 _BMRB_flat_file_name bmr17253.str _Entry_type new _Submission_date 2010-10-12 _Accession_date 2010-10-12 _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 Lee Erinna . . 2 Yao Shenggen . . 3 Norton Raymond . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 124 "15N chemical shifts" 18 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-05-19 update BMRB 'update entry citation' 2011-01-12 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Peptide inhibitors of the malaria surface protein, apical membrane antigen 1: Identification of key binding residues.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21213258 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee Erinna F. . 2 Yao Shenggen . . 3 Sabo Jennifer K. . 4 Fairlie 'W. Douglas' . . 5 Stevenson Rachel A. . 6 Harris Karen S. . 7 Anders Robin F. . 8 Foley Michael . . 9 Norton Raymond S. . stop_ _Journal_abbreviation Biopolymers _Journal_name_full Biopolymers _Journal_volume 95 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 354 _Page_last 364 _Year 2011 _Details . loop_ _Keyword 'apical membrane antigen 1' malaria 'Plasmodium falciparum' 'peptide expression' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'AMA1 inhibitor peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'R2 peptide' $R2_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_R2_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common R2_peptide _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 20 _Mol_residue_sequence VFAEFLPLFSKFGSRLHILK loop_ _Residue_seq_code _Residue_label 1 VAL 2 PHE 3 ALA 4 GLU 5 PHE 6 LEU 7 PRO 8 LEU 9 PHE 10 SER 11 LYS 12 PHE 13 GLY 14 SER 15 ARG 16 LEU 17 HIS 18 ILE 19 LEU 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 $R2_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 $R2_peptide 'recombinant technology' . Escherichia coli . 'pET15b (modified)' 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 'sodium acetate' 10 mM 'natural abundance' 'sodium azide' 0.03 % 'natural abundance' $R2_peptide 2 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'sodium acetate' 10 mM 'natural abundance' 'sodium azide' 0.03 % 'natural abundance' $R2_peptide 1 mM [U-15N] H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'data analysis' 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _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_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 278 . K pH 4.1 . pH pressure 1 . atm 'ionic strength' 0.01 . M 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 water H 1 protons ppm 5.002 internal direct . . . 1.0 'ammonium nitrate' N 15 nitrogen ppm 21.0 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '2D DQF-COSY' '2D 1H-15N HSQC' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'R2 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 VAL HA H 3.76 0.02 1 2 1 1 VAL HB H 2.19 0.02 1 3 1 1 VAL HG1 H 0.98 0.02 2 4 1 1 VAL HG2 H 0.98 0.02 2 5 2 2 PHE H H 8.82 0.02 1 6 2 2 PHE HA H 4.66 0.02 1 7 2 2 PHE HB2 H 3.08 0.02 2 8 2 2 PHE HB3 H 3.08 0.02 2 9 2 2 PHE HD1 H 7.28 0.02 3 10 2 2 PHE HD2 H 7.28 0.02 3 11 2 2 PHE N N 125.5 0.2 1 12 3 3 ALA H H 8.40 0.02 1 13 3 3 ALA HA H 4.22 0.02 1 14 3 3 ALA HB H 1.27 0.02 1 15 3 3 ALA N N 127.6 0.2 1 16 4 4 GLU H H 8.24 0.02 1 17 4 4 GLU HA H 4.13 0.02 1 18 4 4 GLU HB2 H 1.87 0.02 2 19 4 4 GLU HB3 H 1.87 0.02 2 20 4 4 GLU HG2 H 2.24 0.02 2 21 4 4 GLU HG3 H 2.16 0.02 2 22 4 4 GLU N N 120.4 0.2 1 23 5 5 PHE H H 8.40 0.02 1 24 5 5 PHE HA H 4.64 0.02 1 25 5 5 PHE HB2 H 3.10 0.02 2 26 5 5 PHE HB3 H 3.01 0.02 2 27 5 5 PHE HD1 H 7.24 0.02 3 28 5 5 PHE HD2 H 7.24 0.02 3 29 5 5 PHE HE1 H 7.33 0.02 3 30 5 5 PHE HE2 H 7.33 0.02 3 31 5 5 PHE N N 121.7 0.2 1 32 6 6 LEU H H 8.21 0.02 1 33 6 6 LEU HA H 4.61 0.02 1 34 6 6 LEU HB2 H 1.56 0.02 2 35 6 6 LEU HB3 H 1.56 0.02 2 36 6 6 LEU HD1 H 0.89 0.02 2 37 6 6 LEU HD2 H 0.89 0.02 2 38 6 6 LEU N N 126.5 0.2 1 39 7 7 PRO HA H 4.31 0.02 1 40 7 7 PRO HB2 H 2.23 0.02 2 41 7 7 PRO HB3 H 1.77 0.02 2 42 7 7 PRO HD2 H 3.69 0.02 2 43 7 7 PRO HD3 H 3.58 0.02 2 44 7 7 PRO HG2 H 1.99 0.02 2 45 7 7 PRO HG3 H 1.99 0.02 2 46 8 8 LEU H H 8.36 0.02 1 47 8 8 LEU HA H 4.22 0.02 1 48 8 8 LEU HB2 H 1.47 0.02 2 49 8 8 LEU HB3 H 1.57 0.02 2 50 8 8 LEU HD1 H 0.91 0.02 2 51 8 8 LEU HD2 H 0.84 0.02 2 52 8 8 LEU HG H 1.41 0.02 1 53 8 8 LEU N N 121.8 0.2 1 54 9 9 PHE H H 8.26 0.02 1 55 9 9 PHE HA H 4.63 0.02 1 56 9 9 PHE HB2 H 3.11 0.02 2 57 9 9 PHE HB3 H 3.04 0.02 2 58 9 9 PHE HD1 H 7.22 0.02 3 59 9 9 PHE HD2 H 7.22 0.02 3 60 9 9 PHE N N 120.4 0.2 1 61 10 10 SER H H 8.27 0.02 1 62 10 10 SER HA H 4.38 0.02 1 63 10 10 SER HB2 H 3.86 0.02 2 64 10 10 SER HB3 H 3.76 0.02 2 65 10 10 SER N N 117.4 0.2 1 66 11 11 LYS H H 8.45 0.02 1 67 11 11 LYS HA H 4.16 0.02 1 68 11 11 LYS HB2 H 1.62 0.02 2 69 11 11 LYS HB3 H 1.62 0.02 2 70 11 11 LYS HD2 H 1.60 0.02 2 71 11 11 LYS HD3 H 1.60 0.02 2 72 11 11 LYS HE2 H 2.90 0.02 2 73 11 11 LYS HE3 H 2.90 0.02 2 74 11 11 LYS HG2 H 1.19 0.02 2 75 11 11 LYS HG3 H 1.19 0.02 2 76 11 11 LYS N N 123.7 0.2 1 77 12 12 PHE H H 8.27 0.02 1 78 12 12 PHE HA H 4.63 0.02 1 79 12 12 PHE HB2 H 3.23 0.02 2 80 12 12 PHE HB3 H 2.96 0.02 2 81 12 12 PHE HD1 H 7.26 0.02 3 82 12 12 PHE HD2 H 7.26 0.02 3 83 12 12 PHE HE1 H 7.37 0.02 3 84 12 12 PHE HE2 H 7.37 0.02 3 85 12 12 PHE N N 120.1 0.2 1 86 13 13 GLY H H 8.31 0.02 1 87 13 13 GLY HA2 H 3.98 0.02 2 88 13 13 GLY HA3 H 3.85 0.02 2 89 13 13 GLY N N 110.4 0.2 1 90 14 14 SER H H 8.28 0.02 1 91 14 14 SER HA H 4.44 0.02 1 92 14 14 SER HB2 H 3.98 0.02 2 93 14 14 SER HB3 H 3.86 0.02 2 94 14 14 SER N N 115.9 0.2 1 95 15 15 ARG H H 8.54 0.02 1 96 15 15 ARG HA H 4.32 0.02 1 97 15 15 ARG HB2 H 1.86 0.02 2 98 15 15 ARG HB3 H 1.75 0.02 2 99 15 15 ARG HD2 H 3.88 0.02 2 100 15 15 ARG HD3 H 3.16 0.02 2 101 15 15 ARG HG2 H 1.61 0.02 2 102 15 15 ARG HG3 H 1.61 0.02 2 103 15 15 ARG N N 123.2 0.2 1 104 16 16 LEU H H 8.21 0.02 1 105 16 16 LEU HA H 4.26 0.02 1 106 16 16 LEU HB2 H 1.56 0.02 2 107 16 16 LEU HB3 H 1.43 0.02 2 108 16 16 LEU HD1 H 0.85 0.02 2 109 16 16 LEU HD2 H 0.85 0.02 2 110 16 16 LEU N N 122.5 0.2 1 111 17 17 HIS H H 8.63 0.02 1 112 17 17 HIS HA H 4.71 0.02 1 113 17 17 HIS HB2 H 3.22 0.02 2 114 17 17 HIS HB3 H 3.11 0.02 2 115 17 17 HIS HD2 H 7.24 0.02 1 116 17 17 HIS HE1 H 8.57 0.02 1 117 17 17 HIS N N 119.7 0.2 1 118 18 18 ILE H H 8.30 0.02 1 119 18 18 ILE HA H 4.12 0.02 1 120 18 18 ILE HB H 1.82 0.02 1 121 18 18 ILE HG12 H 1.43 0.02 2 122 18 18 ILE HG13 H 1.15 0.02 2 123 18 18 ILE HG2 H 0.88 0.02 1 124 18 18 ILE N N 123.3 0.2 1 125 19 19 LEU H H 8.54 0.02 1 126 19 19 LEU HA H 4.38 0.02 1 127 19 19 LEU HB2 H 1.62 0.02 2 128 19 19 LEU HB3 H 1.62 0.02 2 129 19 19 LEU HD1 H 0.88 0.02 2 130 19 19 LEU HD2 H 0.88 0.02 2 131 19 19 LEU N N 127.9 0.2 1 132 20 20 LYS H H 8.02 0.02 1 133 20 20 LYS HA H 4.15 0.02 1 134 20 20 LYS HB2 H 1.80 0.02 2 135 20 20 LYS HB3 H 1.72 0.02 2 136 20 20 LYS HD2 H 1.62 0.02 2 137 20 20 LYS HD3 H 1.62 0.02 2 138 20 20 LYS HE2 H 2.97 0.02 2 139 20 20 LYS HE3 H 2.97 0.02 2 140 20 20 LYS HG2 H 1.38 0.02 2 141 20 20 LYS HG3 H 1.38 0.02 2 142 20 20 LYS N N 127.4 0.2 1 stop_ save_