data_15291 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H Chemical Shift Assignments for N-Me-Gly13 ; _BMRB_accession_number 15291 _BMRB_flat_file_name bmr15291.str _Entry_type original _Submission_date 2007-06-06 _Accession_date 2007-06-06 _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" 109 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-04-17 update BMRB 'complete entry citation' 2009-02-09 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15282 N-Me-Phe5 15284 N-Me-Leu8 15285 N-Me-Lys11 15287 N-Me-Phe12 15292 N-Me-Ser14 15293 N-Me-Leu8/N-Me-Ser14 15294 N-Me-Val1/N-Me-Leu8/N-Me-Ser14 stop_ _Original_release_date 2007-06-07 save_ ############################# # Citation for this entry # ############################# save_N-Me-Gly13_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-Gly13 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label N-Me-Gly13 $N-Me-Gly13 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 Gly13' save_ ######################## # Monomeric polymers # ######################## save_N-Me-Gly13 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common N-Me-Gly13 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 20 _Mol_residue_sequence ; VFAEFLPLFSKFXSRMHILK ; 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 SAR 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_SAR _Saveframe_category polymer_residue _Mol_type 'PEPTIDE LINKING' _Name_common SARCOSINE _BMRB_code SAR _PDB_code SAR _Standard_residue_derivative . _Molecular_mass 89.093 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? CN CN C . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HA2 HA2 H . 0 . ? HA3 HA3 H . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? HN3 HN3 H . 0 . ? HXT HXT H . 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 N CA ? ? SING N CN ? ? SING N H ? ? SING CA C ? ? SING CA HA2 ? ? SING CA HA3 ? ? DOUB C O ? ? SING C OXT ? ? SING CN HN1 ? ? SING CN HN2 ? ? SING CN HN3 ? ? SING 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-Gly13 . . . . . . 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-Gly13 '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-Gly13 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 pH 4.6 0.2 pH pressure 1 . atm temperature 278 0.1 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 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-Gly13 _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 2.18 0.02 1 3 1 1 VAL HG1 H 1.00 0.02 1 4 2 2 PHE H H 8.82 0.02 1 5 2 2 PHE HA H 4.65 0.02 1 6 2 2 PHE HB3 H 3.07 0.02 1 7 2 2 PHE HD1 H 7.28 0.02 1 8 2 2 PHE HE1 H 7.34 0.02 1 9 3 3 ALA H H 8.40 0.02 1 10 3 3 ALA HA H 4.21 0.02 1 11 3 3 ALA HB H 1.26 0.02 1 12 4 4 GLU H H 8.26 0.02 1 13 4 4 GLU HA H 4.11 0.02 1 14 4 4 GLU HB2 H 1.83 0.02 2 15 4 4 GLU HB3 H 1.88 0.02 2 16 4 4 GLU HG2 H 2.12 0.02 2 17 4 4 GLU HG3 H 2.19 0.02 2 18 5 5 PHE H H 8.41 0.02 1 19 5 5 PHE HA H 4.64 0.02 1 20 5 5 PHE HB2 H 3.00 0.02 2 21 5 5 PHE HB3 H 3.09 0.02 2 22 5 5 PHE HD1 H 7.23 0.02 1 23 5 5 PHE HE1 H 7.33 0.02 1 24 6 6 LEU H H 8.20 0.02 1 25 6 6 LEU HA H 4.59 0.02 1 26 6 6 LEU HB3 H 1.55 0.02 1 27 6 6 LEU HD2 H 0.89 0.02 1 28 6 6 LEU HG H 1.49 0.02 1 29 7 7 PRO HA H 4.30 0.02 1 30 7 7 PRO HB2 H 1.75 0.02 2 31 7 7 PRO HB3 H 2.21 0.02 2 32 7 7 PRO HD2 H 3.58 0.02 2 33 7 7 PRO HD3 H 3.69 0.02 2 34 7 7 PRO HG3 H 1.97 0.02 1 35 8 8 LEU H H 8.35 0.02 1 36 8 8 LEU HA H 4.20 0.02 1 37 8 8 LEU HB3 H 1.55 0.02 1 38 8 8 LEU HD1 H 0.83 0.02 1 39 8 8 LEU HD2 H 0.89 0.02 1 40 8 8 LEU HG H 1.40 0.02 1 41 9 9 PHE H H 8.23 0.02 1 42 9 9 PHE HA H 4.62 0.02 1 43 9 9 PHE HB2 H 3.02 0.02 2 44 9 9 PHE HB3 H 3.12 0.02 2 45 9 9 PHE HD1 H 7.22 0.02 1 46 9 9 PHE HE1 H 7.32 0.02 1 47 10 10 SER H H 8.17 0.02 1 48 10 10 SER HA H 4.34 0.02 1 49 10 10 SER HB2 H 3.71 0.02 2 50 10 10 SER HB3 H 3.77 0.02 2 51 11 11 LYS H H 8.34 0.02 1 52 11 11 LYS HA H 4.2 0.02 1 53 11 11 LYS HB2 H 1.59 0.02 2 54 11 11 LYS HB3 H 1.67 0.02 2 55 11 11 LYS HD3 H 1.62 0.02 1 56 11 11 LYS HE3 H 2.94 0.02 1 57 11 11 LYS HG2 H 1.25 0.02 2 58 11 11 LYS HG3 H 1.31 0.02 2 59 11 11 LYS HZ H 7.6 0.02 1 60 12 12 PHE H H 8.29 0.02 1 61 12 12 PHE HA H 5.09 0.02 1 62 12 12 PHE HB2 H 2.92 0.02 2 63 12 12 PHE HB3 H 3.11 0.02 2 64 12 12 PHE HD1 H 7.26 0.02 1 65 12 12 PHE HE1 H 7.35 0.02 1 66 13 13 SAR H H 3.04 0.02 1 67 13 13 SAR HA3 H 4.10 0.02 2 68 14 14 SER H H 8.43 0.02 1 69 14 14 SER HA H 4.42 0.02 1 70 14 14 SER HB2 H 3.85 0.02 2 71 14 14 SER HB3 H 3.90 0.02 2 72 15 15 ARG H H 8.6 0.02 1 73 15 15 ARG HA H 4.35 0.02 1 74 15 15 ARG HB2 H 1.74 0.02 2 75 15 15 ARG HB3 H 1.88 0.02 2 76 15 15 ARG HD3 H 3.17 0.02 1 77 15 15 ARG HE H 7.22 0.02 1 78 15 15 ARG HG3 H 1.62 0.02 1 79 16 16 MET H H 8.37 0.02 1 80 16 16 MET HA H 4.41 0.02 1 81 16 16 MET HB3 H 1.94 0.02 1 82 16 16 MET HG2 H 2.45 0.02 2 83 16 16 MET HG3 H 2.53 0.02 2 84 17 17 HIS H H 8.67 0.02 1 85 17 17 HIS HA H 4.72 0.02 1 86 17 17 HIS HB2 H 3.12 0.02 2 87 17 17 HIS HB3 H 3.22 0.02 2 88 17 17 HIS HD2 H 7.25 0.02 1 89 17 17 HIS HE1 H 8.58 0.02 1 90 18 18 ILE H H 8.36 0.02 1 91 18 18 ILE HA H 4.11 0.02 1 92 18 18 ILE HB H 1.81 0.02 1 93 18 18 ILE HD1 H 0.83 0.02 1 94 18 18 ILE HG12 H 1.16 0.02 1 95 18 18 ILE HG13 H 1.41 0.02 1 96 18 18 ILE HG2 H 0.88 0.02 1 97 19 19 LEU H H 8.54 0.02 1 98 19 19 LEU HA H 4.38 0.02 1 99 19 19 LEU HB3 H 1.62 0.02 1 100 19 19 LEU HD1 H 0.85 0.02 1 101 19 19 LEU HD2 H 0.93 0.02 1 102 20 20 LYS H H 7.99 0.02 1 103 20 20 LYS HA H 4.14 0.02 1 104 20 20 LYS HB2 H 1.71 0.02 2 105 20 20 LYS HB3 H 1.79 0.02 2 106 20 20 LYS HD3 H 1.66 0.02 1 107 20 20 LYS HE3 H 2.98 0.02 1 108 20 20 LYS HG3 H 1.38 0.02 1 109 20 20 LYS HZ H 7.59 0.02 1 stop_ save_