data_11021 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR STRUCTURE OF THE MUTANT OF CHIGNOLIN, CLN025 ; _BMRB_accession_number 11021 _BMRB_flat_file_name bmr11021.str _Entry_type new _Submission_date 2007-12-12 _Accession_date 2007-12-12 _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 KATO Yusuke . . 2 ISHIMURA Miyuki . . 3 HONDA Shinya . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 52 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-11-25 update BMRB 'complete entry citation' 2008-11-11 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Crystal Structure of a Ten-Amino Acid Protein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18950166 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 HONDA Shinya . . 2 AKIBA Toshihiko . . 3 KATO Yusuke S. . 4 SAWADA Yoshito . . 5 SEKIJIMA Masakazu . . 6 ISHIMURA Miyuki . . 7 OOISHI Ayako . . 8 WATANABE Hideki . . 9 ODAHARA Takayuki . . 10 HARATA Kazuaki . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 130 _Journal_issue 46 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 15327 _Page_last 15331 _Year 2008 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_2 _Saveframe_category citation _Citation_full . _Citation_title '10 residue folded peptide designed by segment statistics' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15296744 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 HONDA Shinya . . 2 YAMASAKI Kazuhiko . . 3 SAWADA Yoshito . . 4 MORII Hisayuki . . stop_ _Journal_abbreviation Structure _Journal_name_full . _Journal_volume 12 _Journal_issue 8 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1507 _Page_last 1518 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CLN025 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CLN025 $CLN025 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_CLN025 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CLN025 _Molecular_mass 1295.344 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 10 _Mol_residue_sequence YYDPETGTWY loop_ _Residue_seq_code _Residue_label 1 TYR 2 TYR 3 ASP 4 PRO 5 GLU 6 THR 7 GLY 8 THR 9 TRP 10 TYR 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 $CLN025 . . . . . . 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 $CLN025 'chemical synthesis' . . . . . 'Designed protein having an artificial sequence' 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 $CLN025 2 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' DSS 0.01 % 'natural abundance' H2O 95 % . D2O 5 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_ProcheckNMR _Saveframe_category software _Name ProcheckNMR _Version . loop_ _Vendor _Address _Electronic_address 'Laskowski and MacArthur' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details 'equipped with a Varian triple resonance probe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_ROESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H ROESY' _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_1H-1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _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 298 . K pH 5.7 . 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 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_ _Experiment_label '2D 1H-1H TOCSY' 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 CLN025 _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 TYR H H 8.555 0.001 1 2 1 1 TYR HA H 4.161 0.004 1 3 1 1 TYR HB2 H 2.685 0.003 2 4 1 1 TYR HB3 H 2.855 0.003 2 5 1 1 TYR HD1 H 6.965 0.004 3 6 1 1 TYR HE1 H 6.785 0.002 3 7 2 2 TYR H H 8.556 0.001 1 8 2 2 TYR HA H 4.511 0.002 1 9 2 2 TYR HB2 H 2.042 0.002 2 10 2 2 TYR HB3 H 2.382 0.003 2 11 2 2 TYR HD1 H 6.457 0.004 3 12 2 2 TYR HE1 H 6.216 0.004 3 13 3 3 ASP H H 8.337 0.000 1 14 3 3 ASP HA H 4.953 0.000 1 15 3 3 ASP HB2 H 2.540 0.006 2 16 3 3 ASP HB3 H 2.970 0.002 2 17 4 4 PRO HA H 4.064 0.005 1 18 4 4 PRO HB2 H 2.385 0.002 2 19 4 4 PRO HD2 H 3.958 0.002 2 20 4 4 PRO HG2 H 2.060 0.006 2 21 5 5 GLU H H 8.140 0.001 1 22 5 5 GLU HA H 4.161 0.003 1 23 5 5 GLU HB2 H 2.145 0.000 2 24 5 5 GLU HB3 H 2.219 0.001 2 25 5 5 GLU HG2 H 2.337 0.003 2 26 6 6 THR H H 7.254 0.003 1 27 6 6 THR HA H 4.348 0.001 1 28 6 6 THR HB H 4.348 0.001 1 29 6 6 THR HG2 H 1.209 0.002 1 30 7 7 GLY H H 8.303 0.001 1 31 7 7 GLY HA2 H 4.019 0.006 2 32 7 7 GLY HA3 H 3.734 0.007 2 33 8 8 THR H H 7.233 0.001 1 34 8 8 THR HA H 4.447 0.000 1 35 8 8 THR HB H 3.907 0.001 1 36 8 8 THR HG2 H 0.986 0.002 1 37 9 9 TRP H H 8.501 0.000 1 38 9 9 TRP HA H 5.022 0.001 1 39 9 9 TRP HB2 H 3.075 0.002 2 40 9 9 TRP HB3 H 3.236 0.005 2 41 9 9 TRP HD1 H 7.265 0.002 1 42 9 9 TRP HE1 H 10.088 0.002 1 43 9 9 TRP HE3 H 7.344 0.003 1 44 9 9 TRP HH2 H 6.838 0.005 1 45 9 9 TRP HZ2 H 7.130 0.008 1 46 9 9 TRP HZ3 H 7.072 0.007 1 47 10 10 TYR H H 8.369 0.001 1 48 10 10 TYR HA H 4.385 0.001 1 49 10 10 TYR HB2 H 2.477 0.003 2 50 10 10 TYR HB3 H 2.917 0.007 2 51 10 10 TYR HD1 H 6.932 0.004 3 52 10 10 TYR HE1 H 6.662 0.002 3 stop_ save_