data_4439 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4439 _Entry.Title ; Hyperfine Cys Proton Signals from Oxidized Human Ferredoxin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1999-10-15 _Entry.Accession_date 1999-10-15 _Entry.Last_release_date 1999-10-15 _Entry.Original_release_date 1999-10-15 _Entry.Origination author _Entry.NMR_STAR_version 3.1.2.6 _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.ORCID _Entry_author.Entry_ID 1 Bin Xia . . . . 4439 2 Daniel Jenk . . . . 4439 3 David LeMaster . M. . . 4439 4 William Westler . M. . . 4439 5 John Markley . L. . . 4439 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4439 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 12 4439 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 . . 2000-01-12 . original BMRB . 4439 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4439 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Electron-Nuclear Interactions in two Prototypical [2Fe-2S] Proteins: Selective (Chiral) Deuteration and Analysis of 1H and 2H NMR Signals from the Alpha and Beta Hydrogens of Cysteinyl Residues that Ligate the Iron in the Active Sites of Human Ferredoxin and Anabaena 7120 Vegetative Ferredoxin ; _Citation.Status 'in press' _Citation.Type journal _Citation.Journal_abbrev 'Arch. Biochem. Biophys.' _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 . 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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Bin Xia . . . . 4439 1 2 Daniel Jenk . . . . 4439 1 3 David LeMaster . M. . . 4439 1 4 William Westler . M. . . 4439 1 5 John Markley . L. . . 4439 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID Adrenodoxin 4439 1 'Anabaena 7120' 4439 1 'Ferredoxin, human' 4439 1 'Ferredoxin, plant-type' 4439 1 'Hyperfine NMR' 4439 1 'Stable Isotope Labeling' 4439 1 'iron-sulfur cluster' 4439 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_HuFd _Assembly.Sf_category assembly _Assembly.Sf_framecode system_HuFd _Assembly.Entry_ID 4439 _Assembly.ID 1 _Assembly.Name 'Human Ferredoxin oxidized' _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 'other bound and free' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details 'Both Fe atoms are Fe(III).' _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4439 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 'Human Ferredoxin' 1 $HuFd . . . native . . . . . 4439 1 2 FES 2 $entity_FES . . . native . . . . . 4439 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 metal-coordination single . 1 . 1 CYS 46 46 SG . 2 . 2 FES 1 1 FE1 . . . . . . . . . . 4439 1 2 metal-coordination single . 1 . 1 CYS 52 52 SG . 2 . 2 FES 1 1 FE1 . . . . . . . . . . 4439 1 3 metal-coordination single . 1 . 1 CYS 55 55 SG . 2 . 2 FES 1 1 FE2 . . . . . . . . . . 4439 1 4 metal-coordination single . 1 . 1 CYS 92 92 SG . 2 . 2 FES 1 1 FE2 . . . . . . . . . . 4439 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID HuFd abbreviation 4439 1 'Human Ferredoxin oxidized' system 4439 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HuFd _Entity.Sf_category entity _Entity.Sf_framecode HuFd _Entity.Entry_ID 4439 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Human Ferredoxin' _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 ; SSSEDKITVHFINRDGETLT TKGKVGDSLLDVVVENNLDI DGFGACEGTLACSTCHLIFE DHIYEKLDAITDEENDMLDL AYGLTDRSRLGCQICLTKSM DNMTVRVPETVADARQSIDV GKTS ; _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 124 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'other bound and free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . no BMRB 4073 . 'human ferredoxin' . . . . . 100.00 124 100.00 100.00 1.78e-65 . . . . 4439 1 . no BMRB 4074 . 'human ferredoxin' . . . . . 100.00 124 100.00 100.00 1.78e-65 . . . . 4439 1 . no BMRB 4440 . 'Human Ferredoxin' . . . . . 100.00 124 100.00 100.00 1.78e-65 . . . . 4439 1 . no BMRB 5337 . 'human adrenodoxin' . . . . . 89.52 111 99.10 100.00 1.76e-57 . . . . 4439 1 . no BMRB 6026 . 'Oxidized Human Ferredoxin' . . . . . 100.00 124 100.00 100.00 1.78e-65 . . . . 4439 1 . no GenBank AAA35829 . ferredoxin . . . . . 100.00 184 100.00 100.00 9.33e-67 . . . . 4439 1 . no GenBank AAA35855 . ferredoxin . . . . . 64.52 80 100.00 100.00 7.45e-40 . . . . 4439 1 . no GenBank AAA35856 . ferredoxin . . . . . 64.52 80 100.00 100.00 7.45e-40 . . . . 4439 1 . no GenBank AAA50462 . adrenodoxin . . . . . 100.00 184 100.00 100.00 9.33e-67 . . . . 4439 1 . no GenBank AAA76853 . ferredoxin . . . . . 100.00 184 100.00 100.00 9.33e-67 . . . . 4439 1 . no REF NP_004100 . 'ferredoxin 1 precursor [Homo sapiens]' . . . . . 100.00 184 100.00 100.00 9.33e-67 . . . . 4439 1 . no REF XP_001105034 . 'PREDICTED: similar to Adrenodoxin, mitochondrial precursor (Adrenal ferredoxin) (Ferredoxin-1) (Hepatoredoxin) [Macaca mulatta]' . . . . . 100.00 184 99.19 100.00 2.40e-66 . . . . 4439 1 . no REF XP_508877 . 'PREDICTED: similar to Adrenodoxin, mitochondrial precursor (Adrenal ferredoxin) (Ferredoxin-1) (Hepatoredoxin) [Pan troglodytes]' . . . . . 98.39 253 100.00 100.00 2.28e-66 . . . . 4439 1 . no SWISS-PROT P10109 . 'Adrenodoxin, mitochondrial precursor (Adrenal ferredoxin) (Ferredoxin-1) (Hepatoredoxin)' . . . . . 100.00 184 100.00 100.00 9.33e-67 . . . . 4439 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID HuFd abbreviation 4439 1 'Human Ferredoxin' common 4439 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . SER . 4439 1 2 . SER . 4439 1 3 . SER . 4439 1 4 . GLU . 4439 1 5 . ASP . 4439 1 6 . LYS . 4439 1 7 . ILE . 4439 1 8 . THR . 4439 1 9 . VAL . 4439 1 10 . HIS . 4439 1 11 . PHE . 4439 1 12 . ILE . 4439 1 13 . ASN . 4439 1 14 . ARG . 4439 1 15 . ASP . 4439 1 16 . GLY . 4439 1 17 . GLU . 4439 1 18 . THR . 4439 1 19 . LEU . 4439 1 20 . THR . 4439 1 21 . THR . 4439 1 22 . LYS . 4439 1 23 . GLY . 4439 1 24 . LYS . 4439 1 25 . VAL . 4439 1 26 . GLY . 4439 1 27 . ASP . 4439 1 28 . SER . 4439 1 29 . LEU . 4439 1 30 . LEU . 4439 1 31 . ASP . 4439 1 32 . VAL . 4439 1 33 . VAL . 4439 1 34 . VAL . 4439 1 35 . GLU . 4439 1 36 . ASN . 4439 1 37 . ASN . 4439 1 38 . LEU . 4439 1 39 . ASP . 4439 1 40 . ILE . 4439 1 41 . ASP . 4439 1 42 . GLY . 4439 1 43 . PHE . 4439 1 44 . GLY . 4439 1 45 . ALA . 4439 1 46 . CYS . 4439 1 47 . GLU . 4439 1 48 . GLY . 4439 1 49 . THR . 4439 1 50 . LEU . 4439 1 51 . ALA . 4439 1 52 . CYS . 4439 1 53 . SER . 4439 1 54 . THR . 4439 1 55 . CYS . 4439 1 56 . HIS . 4439 1 57 . LEU . 4439 1 58 . ILE . 4439 1 59 . PHE . 4439 1 60 . GLU . 4439 1 61 . ASP . 4439 1 62 . HIS . 4439 1 63 . ILE . 4439 1 64 . TYR . 4439 1 65 . GLU . 4439 1 66 . LYS . 4439 1 67 . LEU . 4439 1 68 . ASP . 4439 1 69 . ALA . 4439 1 70 . ILE . 4439 1 71 . THR . 4439 1 72 . ASP . 4439 1 73 . GLU . 4439 1 74 . GLU . 4439 1 75 . ASN . 4439 1 76 . ASP . 4439 1 77 . MET . 4439 1 78 . LEU . 4439 1 79 . ASP . 4439 1 80 . LEU . 4439 1 81 . ALA . 4439 1 82 . TYR . 4439 1 83 . GLY . 4439 1 84 . LEU . 4439 1 85 . THR . 4439 1 86 . ASP . 4439 1 87 . ARG . 4439 1 88 . SER . 4439 1 89 . ARG . 4439 1 90 . LEU . 4439 1 91 . GLY . 4439 1 92 . CYS . 4439 1 93 . GLN . 4439 1 94 . ILE . 4439 1 95 . CYS . 4439 1 96 . LEU . 4439 1 97 . THR . 4439 1 98 . LYS . 4439 1 99 . SER . 4439 1 100 . MET . 4439 1 101 . ASP . 4439 1 102 . ASN . 4439 1 103 . MET . 4439 1 104 . THR . 4439 1 105 . VAL . 4439 1 106 . ARG . 4439 1 107 . VAL . 4439 1 108 . PRO . 4439 1 109 . GLU . 4439 1 110 . THR . 4439 1 111 . VAL . 4439 1 112 . ALA . 4439 1 113 . ASP . 4439 1 114 . ALA . 4439 1 115 . ARG . 4439 1 116 . GLN . 4439 1 117 . SER . 4439 1 118 . ILE . 4439 1 119 . ASP . 4439 1 120 . VAL . 4439 1 121 . GLY . 4439 1 122 . LYS . 4439 1 123 . THR . 4439 1 124 . SER . 4439 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . SER 1 1 4439 1 . SER 2 2 4439 1 . SER 3 3 4439 1 . GLU 4 4 4439 1 . ASP 5 5 4439 1 . LYS 6 6 4439 1 . ILE 7 7 4439 1 . THR 8 8 4439 1 . VAL 9 9 4439 1 . HIS 10 10 4439 1 . PHE 11 11 4439 1 . ILE 12 12 4439 1 . ASN 13 13 4439 1 . ARG 14 14 4439 1 . ASP 15 15 4439 1 . GLY 16 16 4439 1 . GLU 17 17 4439 1 . THR 18 18 4439 1 . LEU 19 19 4439 1 . THR 20 20 4439 1 . THR 21 21 4439 1 . LYS 22 22 4439 1 . GLY 23 23 4439 1 . LYS 24 24 4439 1 . VAL 25 25 4439 1 . GLY 26 26 4439 1 . ASP 27 27 4439 1 . SER 28 28 4439 1 . LEU 29 29 4439 1 . LEU 30 30 4439 1 . ASP 31 31 4439 1 . VAL 32 32 4439 1 . VAL 33 33 4439 1 . VAL 34 34 4439 1 . GLU 35 35 4439 1 . ASN 36 36 4439 1 . ASN 37 37 4439 1 . LEU 38 38 4439 1 . ASP 39 39 4439 1 . ILE 40 40 4439 1 . ASP 41 41 4439 1 . GLY 42 42 4439 1 . PHE 43 43 4439 1 . GLY 44 44 4439 1 . ALA 45 45 4439 1 . CYS 46 46 4439 1 . GLU 47 47 4439 1 . GLY 48 48 4439 1 . THR 49 49 4439 1 . LEU 50 50 4439 1 . ALA 51 51 4439 1 . CYS 52 52 4439 1 . SER 53 53 4439 1 . THR 54 54 4439 1 . CYS 55 55 4439 1 . HIS 56 56 4439 1 . LEU 57 57 4439 1 . ILE 58 58 4439 1 . PHE 59 59 4439 1 . GLU 60 60 4439 1 . ASP 61 61 4439 1 . HIS 62 62 4439 1 . ILE 63 63 4439 1 . TYR 64 64 4439 1 . GLU 65 65 4439 1 . LYS 66 66 4439 1 . LEU 67 67 4439 1 . ASP 68 68 4439 1 . ALA 69 69 4439 1 . ILE 70 70 4439 1 . THR 71 71 4439 1 . ASP 72 72 4439 1 . GLU 73 73 4439 1 . GLU 74 74 4439 1 . ASN 75 75 4439 1 . ASP 76 76 4439 1 . MET 77 77 4439 1 . LEU 78 78 4439 1 . ASP 79 79 4439 1 . LEU 80 80 4439 1 . ALA 81 81 4439 1 . TYR 82 82 4439 1 . GLY 83 83 4439 1 . LEU 84 84 4439 1 . THR 85 85 4439 1 . ASP 86 86 4439 1 . ARG 87 87 4439 1 . SER 88 88 4439 1 . ARG 89 89 4439 1 . LEU 90 90 4439 1 . GLY 91 91 4439 1 . CYS 92 92 4439 1 . GLN 93 93 4439 1 . ILE 94 94 4439 1 . CYS 95 95 4439 1 . LEU 96 96 4439 1 . THR 97 97 4439 1 . LYS 98 98 4439 1 . SER 99 99 4439 1 . MET 100 100 4439 1 . ASP 101 101 4439 1 . ASN 102 102 4439 1 . MET 103 103 4439 1 . THR 104 104 4439 1 . VAL 105 105 4439 1 . ARG 106 106 4439 1 . VAL 107 107 4439 1 . PRO 108 108 4439 1 . GLU 109 109 4439 1 . THR 110 110 4439 1 . VAL 111 111 4439 1 . ALA 112 112 4439 1 . ASP 113 113 4439 1 . ALA 114 114 4439 1 . ARG 115 115 4439 1 . GLN 116 116 4439 1 . SER 117 117 4439 1 . ILE 118 118 4439 1 . ASP 119 119 4439 1 . VAL 120 120 4439 1 . GLY 121 121 4439 1 . LYS 122 122 4439 1 . THR 123 123 4439 1 . SER 124 124 4439 1 stop_ save_ save_entity_FES _Entity.Sf_category entity _Entity.Sf_framecode entity_FES _Entity.Entry_ID 4439 _Entity.ID 2 _Entity.BMRB_code FES _Entity.Name 'FE2/S2 (INORGANIC) CLUSTER' _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _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 FES _Entity.Nonpolymer_comp_label $chem_comp_FES _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components 1 _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 175.820 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'FE2/S2 (INORGANIC) CLUSTER' BMRB 4439 2 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 'FE2/S2 (INORGANIC) CLUSTER' BMRB 4439 2 FES 'Three letter code' 4439 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 FES $chem_comp_FES 4439 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4439 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $HuFd . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . placenta . . . . . . . . . . 4439 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 4439 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $HuFd . 'recombinant technology' . . . . . . . . . . . . . . . . 4439 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_FES _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_FES _Chem_comp.Entry_ID 4439 _Chem_comp.ID FES _Chem_comp.Provenance PDB _Chem_comp.Name 'FE2/S2 (INORGANIC) CLUSTER' _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code FES _Chem_comp.PDB_code FES _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-11-20 _Chem_comp.Modified_date 2012-11-20 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code FES _Chem_comp.Number_atoms_all 4 _Chem_comp.Number_atoms_nh 4 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/2Fe.2S _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'Fe2 S2' _Chem_comp.Formula_weight 175.820 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1CZP _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID InChI=1S/2Fe.2S InChI InChI 1.03 4439 FES NIXDOXVAJZFRNF-UHFFFAOYSA-N InChIKey InChI 1.03 4439 FES S1[Fe]S[Fe]1 SMILES CACTVS 3.341 4439 FES S1[Fe]S[Fe]1 SMILES 'OpenEye OEToolkits' 1.5.0 4439 FES S1[Fe]S[Fe]1 SMILES_CANONICAL CACTVS 3.341 4439 FES S1[Fe]S[Fe]1 SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 4439 FES [Fe]1S[Fe]S1 SMILES ACDLabs 10.04 4439 FES stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID 1,3-dithia-2$l^{2},4$l^{2}-diferracyclobutane 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 4439 FES di-mu-sulfidediiron 'SYSTEMATIC NAME' ACDLabs 10.04 4439 FES stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID FE1 FE1 FE1 FE1 . FE . . N 0 . . . 0 no no . . . . 16.237 . 5.409 . 27.398 . 0.000 -0.213 -1.531 1 . 4439 FES FE2 FE2 FE2 FE2 . FE . . N 0 . . . 0 no no . . . . 16.361 . 2.666 . 27.488 . 0.000 -0.213 1.531 2 . 4439 FES S1 S1 S1 S1 . S . . N 0 . . . 1 no no . . . . 17.422 . 4.079 . 28.829 . 1.461 0.372 0.000 3 . 4439 FES S2 S2 S2 S2 . S . . N 0 . . . 1 no no . . . . 15.380 . 3.919 . 25.972 . -1.461 0.372 0.000 4 . 4439 FES stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING FE1 S1 no N 1 . 4439 FES 2 . SING FE1 S2 no N 2 . 4439 FES 3 . SING FE2 S1 no N 3 . 4439 FES 4 . SING FE2 S2 no N 4 . 4439 FES stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_HuFd_oxidized _Sample.Sf_category sample _Sample.Sf_framecode HuFd_oxidized _Sample.Entry_ID 4439 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Human Ferredoxin' . . . 1 $HuFd . . . 2 3 mM . . . . 4439 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions _Sample_condition_list.Entry_ID 4439 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH* 7.2 0.5 na 4439 1 temperature 293 1 K 4439 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 4439 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 400 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4439 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Bruker DMX . 400 . . . 4439 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 4439 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $HuFd_oxidized . . . 1 $sample_conditions . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4439 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4439 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . 4439 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_chemical_shifts_HuFd_oxidized _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shifts_HuFd_oxidized _Assigned_chem_shift_list.Entry_ID 4439 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $HuFd_oxidized . 4439 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 46 46 CYS HA H 1 10 3 . 1 . . . . . . . . 4439 1 2 . 1 1 46 46 CYS HB2 H 1 30 10 . 1 . . . . . . . . 4439 1 3 . 1 1 46 46 CYS HB3 H 1 30 10 . 1 . . . . . . . . 4439 1 4 . 1 1 52 52 CYS HA H 1 10 3 . 1 . . . . . . . . 4439 1 5 . 1 1 52 52 CYS HB2 H 1 30 10 . 1 . . . . . . . . 4439 1 6 . 1 1 52 52 CYS HB3 H 1 30 10 . 1 . . . . . . . . 4439 1 7 . 1 1 55 55 CYS HA H 1 10 3 . 1 . . . . . . . . 4439 1 8 . 1 1 55 55 CYS HB2 H 1 30 10 . 1 . . . . . . . . 4439 1 9 . 1 1 55 55 CYS HB3 H 1 30 10 . 1 . . . . . . . . 4439 1 10 . 1 1 92 92 CYS HA H 1 10 3 . 1 . . . . . . . . 4439 1 11 . 1 1 92 92 CYS HB2 H 1 30 10 . 1 . . . . . . . . 4439 1 12 . 1 1 92 92 CYS HB3 H 1 30 10 . 1 . . . . . . . . 4439 1 stop_ save_