data_15282 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H Chemical Shift Assignments for N-Me-Phe5 ; _BMRB_accession_number 15282 _BMRB_flat_file_name bmr15282.str _Entry_type new _Submission_date 2007-06-05 _Accession_date 2007-06-05 _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 Sabo Jennifer K. . 2 Harris Karen S. . 3 Coley Andrew M. . 4 Karas John A. . 5 Casey Joanne L. . 6 Tan 'Yen Yee' . . 7 Norton Raymond S. . 8 Hughes Andrew B. . 9 Scanlon Denis . . 10 Foley Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-04-17 update BMRB 'complete entry citation' 2009-02-06 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15284 N-Me-Leu8 15285 N-Me-Lys11 15287 N-Me-Phe12 15291 N-Me-Gly13 15292 N-Me-Ser14 15293 N-Me-Leu8/N-Me-Ser14 15294 N-Me-Val1/N-Me-Leu8/N-Me-Ser14 stop_ save_ ############################# # Citation for this entry # ############################# save_N-Me-Phe5_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19164290 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Harris Karen S. . 2 Casey Joanne L. . 3 Coley Andrew M. . 4 Karas John A. . 5 Sabo Jennifer K. . 6 Tan 'Yen Yee' . . 7 Dolezal Olan . . 8 Norton Raymond S. . 9 Hughes Andrew B. . 10 Scanlon Denis . . 11 Foley Michael . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 284 _Journal_issue 14 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9361 _Page_last 9371 _Year 2009 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name N-Me-Phe5 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label N-Me-Phe5 $N-Me-Phe5 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Methylation of the backbone amide for Phe5' save_ ######################## # Monomeric polymers # ######################## save_N-Me-Phe5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common N-Me-Phe5 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 20 _Mol_residue_sequence VFAEXLPLFSKFGSRMHILK loop_ _Residue_seq_code _Residue_label 1 VAL 2 PHE 3 ALA 4 GLU 5 MEA 6 LEU 7 PRO 8 LEU 9 PHE 10 SER 11 LYS 12 PHE 13 GLY 14 SER 15 ARG 16 MET 17 HIS 18 ILE 19 LEU 20 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_MEA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common N-METHYLPHENYLALANINE _BMRB_code . _PDB_code MEA _Standard_residue_derivative . _Molecular_mass 179.216 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 21 22:49:45 2007 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C N 0 . ? N N N N 0 . ? C3 C3 C S 0 . ? C C C N 0 . ? O O O N 0 . ? C' C' C N 0 . ? C1' C1' C N 0 . ? C2' C2' C N 0 . ? C3' C3' C N 0 . ? C4' C4' C N 0 . ? C5' C5' C N 0 . ? C6' C6' C N 0 . ? OXT OXT O N 0 . ? H1C1 H1C1 H N 0 . ? H1C2 H1C2 H N 0 . ? H1C3 H1C3 H N 0 . ? H H H N 0 . ? H3 H3 H N 0 . ? H'C1 H'C1 H N 0 . ? H'C2 H'C2 H N 0 . ? H2' H2' H N 0 . ? H3' H3' H N 0 . ? H4' H4' H N 0 . ? H5' H5' H N 0 . ? H6' H6' H N 0 . ? HXT HXT H N 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 N C1 N SING C1 H1C1 C1 H1C1 SING C1 H1C2 C1 H1C2 SING C1 H1C3 C1 H1C3 SING N C3 N C3 SING N H N H SING C3 C C3 C SING C3 C' C3 C' SING C3 H3 C3 H3 DOUB C O C O SING C OXT C OXT SING C' C1' C' C1' SING C' H'C1 C' H'C1 SING C' H'C2 C' H'C2 DOUB C1' C2' C1' C2' SING C1' C6' C1' C6' SING C2' C3' C2' C3' SING C2' H2' C2' H2' DOUB C3' C4' C3' C4' SING C3' H3' C3' H3' SING C4' C5' C4' C5' SING C4' H4' C4' H4' DOUB C5' C6' C5' C6' SING C5' H5' C5' H5' SING C6' H6' C6' H6' SING OXT HXT OXT HXT stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $N-Me-Phe5 . . . . . . 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 _Details $N-Me-Phe5 'chemical synthesis' . . . . . 'solid-phase peptide synthesis' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '95 % H2O / 5 % 2H2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $N-Me-Phe5 1.7 mM 'natural abundance' H2O 95 % . D2O 5 % . stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _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_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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 278 0.1 K pH 4.6 0.2 pH pressure 1 . atm 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 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $TOPSPIN stop_ loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '2D DQF-COSY' 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 N-Me-Phe5 _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 3.75 0.02 1 2 1 1 VAL HB H 2.17 0.02 1 3 1 1 VAL HG1 H 0.98 0.02 1 4 2 2 PHE H H 8.81 0.02 1 5 2 2 PHE HA H 4.65 0.02 1 6 2 2 PHE HB3 H 3.05 0.02 1 7 2 2 PHE HD1 H 7.28 0.02 1 8 2 2 PHE HE1 H 7.36 0.02 1 9 3 3 ALA H H 8.33 0.02 1 10 3 3 ALA HA H 4.18 0.02 1 11 3 3 ALA HB H 1.20 0.02 1 12 4 4 GLU H H 8.09 0.02 1 13 4 4 GLU HA H 4.63 0.02 1 14 4 4 GLU HB2 H 1.72 0.02 2 15 4 4 GLU HB3 H 1.86 0.02 2 16 4 4 GLU HG2 H 2.10 0.02 2 17 4 4 GLU HG3 H 2.27 0.02 2 18 5 5 MEA H H 3.08 0.02 1 19 5 5 MEA HA H 5.22 0.02 1 20 5 5 MEA HB2 H 3.04 0.02 2 21 5 5 MEA HB3 H 3.22 0.02 2 22 5 5 MEA HD1 H 7.22 0.02 1 23 5 5 MEA HE1 H 7.31 0.02 1 24 6 6 LEU H H 8.23 0.02 1 25 6 6 LEU HA H 4.59 0.02 1 26 6 6 LEU HB3 H 1.57 0.02 1 27 6 6 LEU HD2 H 0.90 0.02 1 28 6 6 LEU HG H 1.52 0.02 1 29 7 7 PRO HA H 4.34 0.02 1 30 7 7 PRO HB2 H 1.76 0.02 2 31 7 7 PRO HB3 H 2.22 0.02 2 32 7 7 PRO HD2 H 3.56 0.02 2 33 7 7 PRO HD3 H 3.75 0.02 2 34 7 7 PRO HG3 H 1.99 0.02 1 35 8 8 LEU H H 8.36 0.02 1 36 8 8 LEU HA H 4.21 0.02 1 37 8 8 LEU HB3 H 1.56 0.02 1 38 8 8 LEU HD1 H 0.83 0.02 1 39 8 8 LEU HD2 H 0.90 0.02 1 40 8 8 LEU HG H 1.41 0.02 1 41 9 9 PHE H H 8.26 0.02 1 42 9 9 PHE HA H 4.63 0.02 1 43 9 9 PHE HB2 H 3.03 0.02 2 44 9 9 PHE HB3 H 3.12 0.02 2 45 9 9 PHE HD1 H 7.21 0.02 1 46 9 9 PHE HE1 H 7.33 0.02 1 47 10 10 SER H H 8.23 0.02 1 48 10 10 SER HA H 4.38 0.02 1 49 10 10 SER HB2 H 3.75 0.02 2 50 10 10 SER HB3 H 3.85 0.02 2 51 11 11 LYS H H 8.43 0.02 1 52 11 11 LYS HA H 4.16 0.02 1 53 11 11 LYS HB3 H 1.62 0.02 1 54 11 11 LYS HD3 H 1.59 0.02 1 55 11 11 LYS HE3 H 2.90 0.02 1 56 11 11 LYS HG3 H 1.18 0.02 1 57 11 11 LYS HZ H 7.6 0.02 1 58 12 12 PHE H H 8.29 0.02 1 59 12 12 PHE HA H 4.63 0.02 1 60 12 12 PHE HB2 H 2.96 0.02 2 61 12 12 PHE HB3 H 3.21 0.02 2 62 12 12 PHE HD1 H 7.25 0.02 1 63 12 12 PHE HE1 H 7.36 0.02 1 64 13 13 GLY H H 8.30 0.02 1 65 13 13 GLY HA2 H 3.86 0.02 2 66 13 13 GLY HA3 H 3.97 0.02 2 67 14 14 SER H H 8.31 0.02 1 68 14 14 SER HA H 4.42 0.02 1 69 14 14 SER HB2 H 3.86 0.02 2 70 14 14 SER HB3 H 3.90 0.02 2 71 15 15 ARG H H 8.53 0.02 1 72 15 15 ARG HA H 4.32 0.02 1 73 15 15 ARG HB2 H 1.74 0.02 2 74 15 15 ARG HB3 H 1.87 0.02 2 75 15 15 ARG HD3 H 3.15 0.02 1 76 15 15 ARG HE H 7.22 0.02 1 77 15 15 ARG HG3 H 1.61 0.02 1 78 16 16 MET H H 8.32 0.02 1 79 16 16 MET HA H 4.38 0.02 1 80 16 16 MET HB3 H 1.94 0.02 1 81 16 16 MET HG2 H 2.44 0.02 2 82 16 16 MET HG3 H 2.52 0.02 2 83 17 17 HIS H H 8.63 0.02 1 84 17 17 HIS HA H 4.70 0.02 1 85 17 17 HIS HB2 H 3.11 0.02 2 86 17 17 HIS HB3 H 3.21 0.02 2 87 17 17 HIS HD2 H 7.24 0.02 1 88 17 17 HIS HE1 H 8.57 0.02 1 89 18 18 ILE H H 8.34 0.02 1 90 18 18 ILE HA H 4.11 0.02 1 91 18 18 ILE HB H 1.81 0.02 1 92 18 18 ILE HD1 H 0.84 0.02 1 93 18 18 ILE HG12 H 1.15 0.02 1 94 18 18 ILE HG13 H 1.44 0.02 1 95 18 18 ILE HG2 H 0.88 0.02 1 96 19 19 LEU H H 8.54 0.02 1 97 19 19 LEU HA H 4.38 0.02 1 98 19 19 LEU HB3 H 1.61 0.02 1 99 19 19 LEU HD1 H 0.87 0.02 1 100 19 19 LEU HD2 H 0.93 0.02 1 101 20 20 LYS H H 7.99 0.02 1 102 20 20 LYS HA H 4.14 0.02 1 103 20 20 LYS HB2 H 1.71 0.02 2 104 20 20 LYS HB3 H 1.79 0.02 2 105 20 20 LYS HD3 H 1.66 0.02 1 106 20 20 LYS HE3 H 2.97 0.02 1 107 20 20 LYS HG3 H 1.38 0.02 1 108 20 20 LYS HZ H 7.59 0.02 1 stop_ save_