data_25726 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; cFLIP-derived R4 peptide ; _BMRB_accession_number 25726 _BMRB_flat_file_name bmr25726.str _Entry_type original _Submission_date 2015-07-24 _Accession_date 2015-07-24 _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 Panaitiu Alexandra E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 57 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-11-16 original BMRB . stop_ _Original_release_date 2015-11-16 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Identification and Characterization of the Interaction Site between cFLIPL and Calmodulin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26529318 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gaidos Gabriel . . 2 Panaitiu Alexandra E. . 3 Guo Bingqian . . 4 Pellegrini Maria . . 5 Mierke Dale . . stop_ _Journal_abbreviation 'PLOS ONE' _Journal_volume 10 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e0141692 _Page_last e0141692 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'R4 peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 1561.995 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 12 _Mol_residue_sequence ; VRRFDLLKRILK ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 ARG 3 ARG 4 PHE 5 ASP 6 LEU 7 LEU 8 LYS 9 ARG 10 ILE 11 LEU 12 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 $entity Human 9606 Eukaryota Metazoa Homo sapiens 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 $entity '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 $entity 0.5 mM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' 'calcium chloride' 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _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 'ionic strength' 0.15 . M pH 6.5 . pH pressure 1 . atm temperature 288 . 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 TSP H 1 'methyl protons' ppm 0 internal direct . . . 1 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 NOESY' 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 entity _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 2 2 ARG HA H 4.197 . 1 2 2 2 ARG HB3 H 1.577 . 1 3 2 2 ARG HD3 H 3.018 . 1 4 3 3 ARG H H 8.397 . 1 5 3 3 ARG HA H 4.117 . 1 6 3 3 ARG HB3 H 1.572 . 1 7 3 3 ARG HG3 H 1.441 . 1 8 4 4 PHE H H 8.250 . 1 9 4 4 PHE HA H 4.453 . 1 10 4 4 PHE HB2 H 2.844 . 2 11 4 4 PHE HB3 H 2.985 . 2 12 4 4 PHE HD1 H 7.089 . 1 13 4 4 PHE HE1 H 7.178 . 1 14 4 4 PHE HZ H 7.122 . 1 15 5 5 ASP H H 8.198 . 1 16 5 5 ASP HA H 4.398 . 1 17 5 5 ASP HB3 H 2.497 . 1 18 6 6 LEU H H 7.938 . 1 19 6 6 LEU HA H 4.070 . 1 20 6 6 LEU HB3 H 1.522 . 1 21 6 6 LEU HG H 1.465 . 1 22 6 6 LEU HD1 H 0.716 . 2 23 6 6 LEU HD2 H 0.778 . 2 24 7 7 LEU H H 8.060 . 1 25 7 7 LEU HA H 4.152 . 1 26 7 7 LEU HB3 H 1.488 . 1 27 7 7 LEU HG H 1.430 . 1 28 7 7 LEU HD1 H 0.702 . 2 29 7 7 LEU HD2 H 0.767 . 2 30 8 8 LYS H H 7.905 . 1 31 8 8 LYS HA H 4.125 . 1 32 8 8 LYS HB3 H 1.654 . 1 33 8 8 LYS HG2 H 1.210 . 2 34 8 8 LYS HG3 H 1.279 . 2 35 8 8 LYS HD3 H 1.599 . 1 36 9 9 ARG H H 8.061 . 1 37 9 9 ARG HA H 4.148 . 1 38 9 9 ARG HB3 H 1.653 . 1 39 9 9 ARG HG3 H 1.618 . 1 40 10 10 ILE H H 8.085 . 1 41 10 10 ILE HA H 3.989 . 1 42 10 10 ILE HB H 1.697 . 1 43 10 10 ILE HG12 H 1.338 . 2 44 10 10 ILE HG2 H 1.039 . 1 45 10 10 ILE HD1 H 0.738 . 1 46 10 10 ILE HD1 H 0.702 . 1 47 10 10 ILE HD1 H 0.738 . 1 48 11 11 LEU H H 8.217 . 1 49 11 11 LEU HA H 4.249 . 1 50 11 11 LEU HB3 H 1.469 . 1 51 11 11 LEU HD1 H 0.698 . 2 52 11 11 LEU HD2 H 0.743 . 2 53 12 12 LYS H H 7.728 . 1 54 12 12 LYS HA H 3.981 . 1 55 12 12 LYS HB3 H 1.645 . 1 56 12 12 LYS HG3 H 1.221 . 1 57 12 12 LYS HD3 H 1.554 . 1 stop_ save_