data_5479 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structures of phage-display peptides that bind to the malarial surface protein, apical membrane antigen 1, and block erythrocyte invasion ; _BMRB_accession_number 5479 _BMRB_flat_file_name bmr5479.str _Entry_type original _Submission_date 2002-07-24 _Accession_date 2002-07-25 _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 Keizer David W. . 2 Miles Luke A. . 3 Li Felomena . . 4 Nair Margie . . 5 Anders Robin F. . 6 Coley Andrew M. . 7 Foley Michael . . 8 Norton Raymond S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 48 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-08-11 original author 'original release' 2003-12-19 update author 'update of the citation' stop_ loop_ _Related_BMRB_accession_number _Relationship 5476 'F1 peptide' 5477 'tF1 peptide' 5478 'F1tbp peptide' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structures of phage-display peptides that bind to the malarial surface protein, apical membrane antigen 1, and block erythrocyte invasion ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12924940 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Keizer David W. . 2 Miles Luke A. . 3 Li Felomena . . 4 Nair Margie . . 5 Anders Robin F. . 6 Coley Andrew M. . 7 Foley Michael . . 8 Norton Raymond S. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 33 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9915 _Page_last 9923 _Year 2003 _Details ; Biochemistry, ASAP Article 10.1021/bi034376b S0006-2960(03)04376-9 Web Release Date: July 30, 2003 http://pubs.acs.org/cgi-bin/asap.cgi/bichaw/asap/abs/bi034376b.html ; save_ ################################## # Molecular system description # ################################## save_system_sF1 _Saveframe_category molecular_system _Mol_system_name sF1 _Abbreviation_common sF1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'sF1 peptide' $sF1_peptide stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomeric _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_sF1_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common sF1 _Abbreviation_common sF1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 15 _Mol_residue_sequence AMSPWFRSLGFGSLG loop_ _Residue_seq_code _Residue_label 1 ALA 2 MET 3 SER 4 PRO 5 TRP 6 PHE 7 ARG 8 SER 9 LEU 10 GLY 11 PHE 12 GLY 13 SER 14 LEU 15 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2005-12-09 save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $sF1_peptide 'Enterobacteria phage M13' 10870 Viruses . Inovirus 'Enterobacteria phage' M13 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 $sF1_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 $sF1_peptide 1.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_Xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Task 'data collection' processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Task 'Peak assignments' stop_ _Details 'C. Bartels et. al., J. Biomol. NMR 1995, 6, 1-10.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQF-COSY' _Sample_label . save_ save_2D_1H-1H_E.COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H E.COSY' _Sample_label . save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_2D_1H-1H_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQF-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H E.COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 0.1 n/a temperature 278 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 0.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'sF1 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 ALA HA H 4.08 0.02 1 2 . 1 ALA HB H 1.51 0.02 1 3 . 2 MET H H 8.82 0.02 1 4 . 2 MET HA H 4.49 0.02 1 5 . 2 MET HB3 H 2.01 0.02 2 6 . 2 MET HG3 H 2.54 0.02 2 7 . 3 SER H H 8.69 0.02 1 8 . 3 SER HA H 4.66 0.02 1 9 . 3 SER HB2 H 3.67 0.02 2 10 . 3 SER HB3 H 3.76 0.02 2 11 . 4 PRO HA H 4.36 0.02 1 12 . 4 PRO HB2 H 1.63 0.02 2 13 . 4 PRO HB3 H 2.18 0.02 2 14 . 4 PRO HG2 H 1.79 0.02 2 15 . 4 PRO HG3 H 1.93 0.02 2 16 . 4 PRO HD2 H 3.61 0.02 2 17 . 4 PRO HD3 H 3.79 0.02 2 18 . 5 TRP H H 7.95 0.02 1 19 . 5 TRP HA H 4.59 0.02 1 20 . 5 TRP HB3 H 3.19 0.02 2 21 . 5 TRP HD1 H 7.11 0.02 1 22 . 5 TRP HE1 H 10.21 0.02 1 23 . 5 TRP HZ2 H 7.48 0.02 1 24 . 6 PHE H H 7.72 0.02 1 25 . 6 PHE HA H 4.34 0.02 1 26 . 6 PHE HB3 H 2.92 0.02 2 27 . 6 PHE HD1 H 7.15 0.02 3 28 . 6 PHE HE1 H 7.32 0.02 3 29 . 7 ARG H H 8.05 0.02 1 30 . 7 ARG HA H 4.12 0.02 1 31 . 7 ARG HB2 H 1.62 0.02 2 32 . 7 ARG HB3 H 1.72 0.02 2 33 . 7 ARG HG3 H 1.49 0.02 2 34 . 7 ARG HD3 H 3.10 0.02 2 35 . 7 ARG HE H 7.19 0.02 1 36 . 8 SER H H 8.26 0.02 1 37 . 9 LEU H H 8.37 0.02 1 38 . 9 LEU HA H 4.32 0.02 1 39 . 11 PHE H H 8.26 0.02 1 40 . 11 PHE HA H 4.56 0.02 1 41 . 11 PHE HB2 H 3.04 0.02 2 42 . 11 PHE HB3 H 3.15 0.02 2 43 . 11 PHE HD1 H 7.24 0.02 3 44 . 12 GLY H H 8.54 0.02 1 45 . 12 GLY HA2 H 3.82 0.02 2 46 . 12 GLY HA3 H 3.94 0.02 2 47 . 14 LEU H H 8.38 0.02 1 48 . 14 LEU HA H 4.32 0.02 1 stop_ save_