data_1139 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Conformational Requirement of Signal Sequences Functioning in Yeast: Circular Dichroism and 1H Nuclear Magnetic Resonance Studies of Synthetic Peptides ; _BMRB_accession_number 1139 _BMRB_flat_file_name bmr1139.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Yamamoto Yoshio . . 2 Ohkubo Tadayasu . . 3 Kohara Atuko . . 4 Tanaka Toshiki . . 5 Tanaka Toshiaki . . 6 Kikuchi Masakazu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 119 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-14 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Yamamoto, Yoshio, Ohkubo, Tadayasu, Kohara, Atuko, Tanaka, Toshiki, Tanaka, Toshiaki, Kikuchi, Masakazu, "Conformational Requirement of Signal Sequences Functioning in Yeast: Circular Dichroism and 1H Nuclear Magnetic Resonance Studies of Synthetic Peptides," Biochemistry 29, 8998-9006 (1990). ; _Citation_title ; Conformational Requirement of Signal Sequences Functioning in Yeast: Circular Dichroism and 1H Nuclear Magnetic Resonance Studies of Synthetic Peptides ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yamamoto Yoshio . . 2 Ohkubo Tadayasu . . 3 Kohara Atuko . . 4 Tanaka Toshiki . . 5 Tanaka Toshiaki . . 6 Kikuchi Masakazu . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8998 _Page_last 9006 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_synthesized_signal_peptide _Saveframe_category molecular_system _Mol_system_name 'synthesized signal peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'synthesized signal peptide' $synthesized_signal_peptide stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_synthesized_signal_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'synthesized signal peptide' _Name_variant L8PL2-M5 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 23 _Mol_residue_sequence ; MRLLLLLLLLPLLLAALGKV FER ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 LEU 4 LEU 5 LEU 6 LEU 7 LEU 8 LEU 9 LEU 10 LEU 11 PRO 12 LEU 13 LEU 14 LEU 15 ALA 16 ALA 17 LEU 18 GLY 19 LYS 20 VAL 21 PHE 22 GLU 23 ARG 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 $synthesized_signal_peptide human 9606 Eukaryota Metazoa Homo sapiens generic 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 $synthesized_signal_peptide 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.1 . na temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label DSS H . . ppm 0 . . . . . $entry_citation $entry_citation 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'synthesized signal 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 MET HA H 4.21 . 1 2 . 1 MET HB2 H 2.23 . 1 3 . 1 MET HB3 H 2.23 . 1 4 . 1 MET HG2 H 2.69 . 2 5 . 1 MET HG3 H 2.62 . 2 6 . 1 MET HE H 2.15 . 1 7 . 2 ARG H H 8.44 . 1 8 . 2 ARG HA H 4.51 . 1 9 . 2 ARG HB2 H 1.95 . 2 10 . 2 ARG HB3 H 1.85 . 2 11 . 2 ARG HG2 H 1.73 . 1 12 . 2 ARG HG3 H 1.73 . 1 13 . 2 ARG HD2 H 3.25 . 1 14 . 2 ARG HD3 H 3.25 . 1 15 . 2 ARG HE H 7.18 . 1 16 . 3 LEU H H 8.09 . 1 17 . 3 LEU HA H 4.26 . 1 18 . 3 LEU HB2 H 1.68 . 1 19 . 3 LEU HB3 H 1.68 . 1 20 . 4 LEU H H 7.61 . 1 21 . 4 LEU HA H 4.17 . 1 22 . 4 LEU HB2 H 1.95 . 2 23 . 4 LEU HB3 H 1.65 . 2 24 . 5 LEU H H 7.19 . 1 25 . 5 LEU HA H 4.14 . 1 26 . 5 LEU HB2 H 1.71 . 1 27 . 5 LEU HB3 H 1.71 . 1 28 . 6 LEU H H 7.36 . 1 29 . 6 LEU HA H 4.09 . 1 30 . 6 LEU HB2 H 1.77 . 1 31 . 6 LEU HB3 H 1.77 . 1 32 . 7 LEU H H 7.71 . 1 33 . 7 LEU HA H 4.13 . 1 34 . 7 LEU HB2 H 1.95 . 2 35 . 7 LEU HB3 H 1.86 . 2 36 . 8 LEU H H 7.74 . 1 37 . 8 LEU HA H 4.28 . 1 38 . 8 LEU HB2 H 1.95 . 2 39 . 8 LEU HB3 H 1.62 . 2 40 . 9 LEU H H 7.85 . 1 41 . 9 LEU HA H 4.44 . 1 42 . 9 LEU HB2 H 1.87 . 2 43 . 9 LEU HB3 H 1.67 . 2 44 . 10 LEU H H 8.07 . 1 45 . 10 LEU HA H 4.28 . 1 46 . 10 LEU HB2 H 1.95 . 2 47 . 10 LEU HB3 H 1.79 . 2 48 . 11 PRO HA H 4.25 . 1 49 . 11 PRO HB2 H 2.37 . 2 50 . 11 PRO HB3 H 1.81 . 2 51 . 11 PRO HG2 H 2.21 . 2 52 . 11 PRO HG3 H 1.96 . 2 53 . 11 PRO HD2 H 3.76 . 2 54 . 11 PRO HD3 H 3.64 . 2 55 . 12 LEU H H 7.3 . 1 56 . 12 LEU HA H 4.22 . 1 57 . 12 LEU HB2 H 1.99 . 2 58 . 12 LEU HB3 H 1.75 . 2 59 . 13 LEU H H 8.11 . 1 60 . 13 LEU HA H 4.14 . 1 61 . 13 LEU HB2 H 1.86 . 2 62 . 13 LEU HB3 H 1.75 . 2 63 . 14 LEU H H 8.63 . 1 64 . 14 LEU HA H 4.1 . 1 65 . 14 LEU HB2 H 1.88 . 2 66 . 14 LEU HB3 H 1.46 . 2 67 . 15 ALA H H 7.83 . 1 68 . 15 ALA HA H 4.18 . 1 69 . 15 ALA HB H 1.6 . 1 70 . 16 ALA H H 8.16 . 1 71 . 16 ALA HA H 4.16 . 1 72 . 16 ALA HB H 1.59 . 1 73 . 17 LEU H H 8.5 . 1 74 . 17 LEU HA H 4.18 . 1 75 . 17 LEU HB2 H 1.92 . 2 76 . 17 LEU HB3 H 1.6 . 2 77 . 18 GLY H H 8.14 . 1 78 . 18 GLY HA2 H 3.94 . 1 79 . 18 GLY HA3 H 3.94 . 1 80 . 19 LYS H H 7.7 . 1 81 . 19 LYS HA H 4.26 . 1 82 . 19 LYS HB2 H 2.01 . 2 83 . 19 LYS HB3 H 1.98 . 2 84 . 19 LYS HG2 H 1.58 . 1 85 . 19 LYS HG3 H 1.58 . 1 86 . 19 LYS HD2 H 1.75 . 1 87 . 19 LYS HD3 H 1.75 . 1 88 . 19 LYS HE2 H 3.04 . 1 89 . 19 LYS HE3 H 3.04 . 1 90 . 19 LYS HZ H 7.58 . 1 91 . 20 VAL H H 7.76 . 1 92 . 20 VAL HA H 3.82 . 1 93 . 20 VAL HB H 2.04 . 1 94 . 20 VAL HG1 H .94 . 2 95 . 20 VAL HG2 H .65 . 2 96 . 21 PHE H H 7.85 . 1 97 . 21 PHE HA H 4.66 . 1 98 . 21 PHE HB2 H 3.34 . 2 99 . 21 PHE HB3 H 3.01 . 2 100 . 21 PHE HD1 H 7.32 . 1 101 . 21 PHE HD2 H 7.32 . 1 102 . 21 PHE HE1 H 7.32 . 1 103 . 21 PHE HE2 H 7.32 . 1 104 . 21 PHE HZ H 7.32 . 1 105 . 22 GLU H H 7.8 . 1 106 . 22 GLU HA H 4.4 . 1 107 . 22 GLU HB2 H 2.23 . 2 108 . 22 GLU HB3 H 2.17 . 2 109 . 22 GLU HG2 H 2.56 . 1 110 . 22 GLU HG3 H 2.56 . 1 111 . 23 ARG H H 7.99 . 1 112 . 23 ARG HA H 4.44 . 1 113 . 23 ARG HB2 H 2.01 . 2 114 . 23 ARG HB3 H 1.87 . 2 115 . 23 ARG HG2 H 1.73 . 1 116 . 23 ARG HG3 H 1.73 . 1 117 . 23 ARG HD2 H 3.26 . 1 118 . 23 ARG HD3 H 3.26 . 1 119 . 23 ARG HE H 7.16 . 1 stop_ save_