data_5476 ####################### # 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 5476 _BMRB_flat_file_name bmr5476.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" 71 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-08-12 original author 'original release' 2003-12-19 update author 'update of the citation' stop_ loop_ _Related_BMRB_accession_number _Relationship 5477 'tF1 peptide' 5478 'F1tbp peptide' 5479 'sF1 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_F1 _Saveframe_category molecular_system _Mol_system_name F1 _Abbreviation_common F1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'F1 peptide' $F1_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_F1_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common F1 _Abbreviation_common F1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 15 _Mol_residue_sequence GWRLLGFGPASSFSM loop_ _Residue_seq_code _Residue_label 1 GLY 2 TRP 3 ARG 4 LEU 5 LEU 6 GLY 7 PHE 8 GLY 9 PRO 10 ALA 11 SER 12 SER 13 PHE 14 SER 15 MET 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 _Details $F1_peptide 'Enterobacteria phage M13' 10870 Viruses . Inovirus 'Enterobacteria phage' M13 'Sequence inserted into gpIII protein.' 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 $F1_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 $F1_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 'F1 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 GLY HA3 H 3.79 0.02 2 2 . 2 TRP H H 8.61 0.02 1 3 . 2 TRP HA H 4.68 0.02 1 4 . 2 TRP HB3 H 3.24 0.02 2 5 . 2 TRP HD1 H 7.25 0.02 1 6 . 2 TRP HE3 H 7.59 0.02 1 7 . 2 TRP HE1 H 10.20 0.02 1 8 . 2 TRP HZ3 H 7.13 0.02 1 9 . 2 TRP HZ2 H 7.47 0.02 1 10 . 2 TRP HH2 H 7.23 0.02 1 11 . 3 ARG H H 8.13 0.02 1 12 . 3 ARG HA H 4.14 0.02 1 13 . 3 ARG HB2 H 1.52 0.02 2 14 . 3 ARG HB3 H 1.65 0.02 2 15 . 3 ARG HG3 H 1.35 0.02 2 16 . 3 ARG HD3 H 3.04 0.02 2 17 . 3 ARG HE H 7.13 0.02 1 18 . 4 LEU H H 8.23 0.02 1 19 . 4 LEU HA H 4.24 0.02 1 20 . 4 LEU HB3 H 1.58 0.02 2 21 . 4 LEU HG H 1.56 0.02 1 22 . 4 LEU HD1 H 0.94 0.02 2 23 . 4 LEU HD2 H 0.88 0.02 2 24 . 5 LEU H H 8.35 0.02 1 25 . 5 LEU HA H 4.33 0.02 1 26 . 5 LEU HB3 H 1.64 0.02 2 27 . 5 LEU HG H 1.53 0.02 1 28 . 5 LEU HD1 H 0.92 0.02 2 29 . 5 LEU HD2 H 0.85 0.02 2 30 . 6 GLY H H 8.34 0.02 1 31 . 6 GLY HA2 H 3.80 0.02 2 32 . 6 GLY HA3 H 3.86 0.02 2 33 . 7 PHE H H 8.21 0.02 1 34 . 7 PHE HA H 4.70 0.02 1 35 . 7 PHE HB2 H 3.20 0.02 2 36 . 7 PHE HB3 H 2.97 0.02 2 37 . 7 PHE HD1 H 7.24 0.02 3 38 . 7 PHE HE1 H 7.34 0.02 3 39 . 8 GLY H H 8.40 0.02 1 40 . 8 GLY HA2 H 4.02 0.02 2 41 . 8 GLY HA3 H 4.06 0.02 2 42 . 9 PRO HA H 4.42 0.02 1 43 . 9 PRO HG3 H 1.99 0.02 2 44 . 9 PRO HB3 H 2.29 0.02 2 45 . 9 PRO HD2 H 3.56 0.02 2 46 . 9 PRO HD3 H 3.60 0.02 2 47 . 10 ALA H H 8.61 0.02 1 48 . 10 ALA HA H 4.29 0.02 1 49 . 10 ALA HB H 1.41 0.02 1 50 . 11 SER H H 8.35 0.02 1 51 . 11 SER HA H 4.42 0.02 1 52 . 11 SER HB2 H 3.88 0.02 2 53 . 11 SER HB3 H 3.82 0.02 2 54 . 12 SER H H 8.37 0.02 1 55 . 12 SER HA H 4.42 0.02 1 56 . 12 SER HB3 H 3.80 0.02 2 57 . 13 PHE H H 8.29 0.02 1 58 . 13 PHE HA H 4.62 0.02 1 59 . 13 PHE HB2 H 3.02 0.02 2 60 . 13 PHE HB3 H 3.13 0.02 2 61 . 13 PHE HD1 H 7.21 0.02 3 62 . 13 PHE HE1 H 7.32 0.02 3 63 . 14 SER H H 8.25 0.02 1 64 . 14 SER HA H 4.40 0.02 1 65 . 14 SER HB3 H 3.81 0.02 2 66 . 15 MET H H 8.40 0.02 1 67 . 15 MET HA H 4.45 0.02 1 68 . 15 MET HB2 H 1.99 0.02 2 69 . 15 MET HB3 H 2.14 0.02 2 70 . 15 MET HG2 H 2.54 0.02 2 71 . 15 MET HG3 H 2.63 0.02 2 stop_ save_