data_6723 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 6723 _Entry.Title ; NMR structure of the heme chaperone CcmE reveals a novel functional motif ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2005-07-01 _Entry.Accession_date 2005-07-01 _Entry.Last_release_date 2005-10-14 _Entry.Original_release_date 2005-10-14 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Elisabeth Enggist . . . 6723 2 Linda Thony-Meyer . . . 6723 3 Peter Guntert . . . 6723 4 Konstantin Pervushin . . . 6723 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 6723 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 877 6723 '13C chemical shifts' 369 6723 '15N chemical shifts' 126 6723 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2005-10-14 2005-07-01 original author . 6723 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 6723 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12429096 _Citation.Full_citation . _Citation.Title 'NMR structure of the heme chaperone CcmE reveals a novel functional motif' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Structure (Cambridge, MA, U. S.)' _Citation.Journal_name_full . _Citation.Journal_volume 10 _Citation.Journal_issue 11 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1551 _Citation.Page_last 1557 _Citation.Year 2002 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Elisabeth Enggist . . . 6723 1 2 Linda Thony-Meyer . . . 6723 1 3 Peter Guntert . . . 6723 1 4 Konstantin Pervushin . . . 6723 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID CcmE 6723 1 'heme chaperone' 6723 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 6723 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; THE PROGRAM XEASY FOR COMPUTER-SUPPORTED NMR SPECTRAL-ANALYSIS OF BIOLOGICAL MACROMOLECULES BARTELS C, XIA TH, BILLETER M, GUNTERT P, WUTHRICH K JOURNAL OF BIOMOLECULAR NMR, 6 (1): 1-10 JUL 1995. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 6723 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; PROCESSING OF MULTIDIMENSIONAL NMR DATA WITH THE NEW SOFTWARE PROSA GUNTERT P, DOTSCH V, WIDER G, WUTHRICH K JOURNAL OF BIOMOLECULAR NMR, 2 (6): 619-629 NOV 1992. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 6723 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9367762 _Citation.Full_citation ; Torsion angle dynamics for NMR structure calculation with the new program DYANA Guntert P, Mumenthaler C, Wuthrich K JOURNAL OF MOLECULAR BIOLOGY, 273 (1): 283-298 OCT 17 1997. ; _Citation.Title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 273 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 283 _Citation.Page_last 298 _Citation.Year 1997 _Citation.Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 P Guntert P. . . 6723 4 2 C Mumenthaler C. . . 6723 4 3 K Wuthrich K. . . 6723 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_apo-CcmE _Assembly.Sf_category assembly _Assembly.Sf_framecode system_apo-CcmE _Assembly.Entry_ID 6723 _Assembly.ID 1 _Assembly.Name 'soluble apo-CcmE' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic yes _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 6723 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 apo-CcmE 1 $apo-CcmE . . . native . . . . . 6723 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'soluble apo-CcmE' system 6723 1 apo-CcmE abbreviation 6723 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'heme chaperone' 6723 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_apo-CcmE _Entity.Sf_category entity _Entity.Sf_framecode apo-CcmE _Entity.Entry_ID 6723 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Escherichia coli apo-CcmE' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; LRSNIDLFYTPGEILYGKRE TQQMPEVGQRLRVGGMVMPG SVQRDPNSLKVTFTIYDAEG SVDVSYEGILPDLFREGQGV VVQGELEKGNHILAKEVLAK HDENYTPPEVEKAMEANHRR PASVYKDPASHHHHHH ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 136 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 15325 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details 'H130 is binding heme covalently.' _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1SR3 . "Solution Structure Of The Heme Chaperone Ccme Of Escherichia Coli" . . . . . 100.00 136 100.00 100.00 3.58e-94 . . . . 6723 1 2 no DBJ BAB36509 . "cytochrome-c biosynthesis heme-carrier protein ccmE [Escherichia coli O157:H7 str. Sakai]" . . . . . 95.59 159 100.00 100.00 2.33e-89 . . . . 6723 1 3 no DBJ BAE76660 . "periplasmic heme chaperone [Escherichia coli str. K-12 substr. W3110]" . . . . . 95.59 159 100.00 100.00 2.33e-89 . . . . 6723 1 4 no DBJ BAG77989 . "cytochrome c-type biogenesis protein [Escherichia coli SE11]" . . . . . 95.59 159 100.00 100.00 2.33e-89 . . . . 6723 1 5 no DBJ BAI26335 . "periplasmic heme chaperone CcmE [Escherichia coli O26:H11 str. 11368]" . . . . . 95.59 159 100.00 100.00 2.33e-89 . . . . 6723 1 6 no DBJ BAI31443 . "periplasmic heme chaperone CcmE [Escherichia coli O103:H2 str. 12009]" . . . . . 95.59 159 100.00 100.00 2.33e-89 . . . . 6723 1 7 no EMBL CAP76699 . "Cytochrome c-type biogenesis protein ccmE [Escherichia coli LF82]" . . . . . 95.59 159 100.00 100.00 2.33e-89 . . . . 6723 1 8 no EMBL CAQ32600 . "ccmE, subunit of CcmCDE protoheme IX reservoir complex, CcmABCDE protoheme IX ABC transporter and CcmEFGH holocytochrome c