data_5660 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5660 _Entry.Title ; Partial proton resonance assignements for the different conformers of ferricytochrome c produced in 30% acetonitrile and 70% water solution ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2003-01-14 _Entry.Accession_date 2003-01-14 _Entry.Last_release_date 2003-02-25 _Entry.Original_release_date 2003-02-25 _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 Sivashankar Sivakolundu . G. . 5660 2 Patricia Mabrouk . A. . 5660 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 5 5660 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 39 5660 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 . . 2003-02-25 2003-01-14 original author . 5660 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5372 'chemical shifts and coupling constants of reduced cytochrome c.' 5660 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5660 _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 ; Insights into the Alkaline Transformation of Ferricyt c from 1H NMR Study in 30% Acetonitrile-Water ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _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 2291 _Citation.Page_last 2300 _Citation.Year 2001 _Citation.Details ; The V* form described in the citation is a histidine-ligated conformer of ferricyt c and not hydroxide-ligated cyt c. This was proved later and submitted for publication by the same authors in Journal of Inorganic Biochemistry in 2003. ; 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 Sivashankar Sivakolundu . G. . 5660 1 2 Patricia Mabrouk . A. . 5660 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'alkaline transition' 5660 1 'non-aqueous enzymology' 5660 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5660 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Wilson MT, Greenwood C (1996) In: Scott RA, Mauk AG (eds) Cytochrome c: A Multidisciplinary Approach. University Science Books, Sausalito, California p 738. ; _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 5660 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9558351 _Citation.Full_citation ; Pollock WBR, Rosell FI, Twitchett MB, Dumont ME, Mauk AG (1998) Biochemistry 37: 6124-6131. ; _Citation.Title 'Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 37 _Citation.Journal_issue 17 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _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 6124 _Citation.Page_last 6131 _Citation.Year 1998 _Citation.Details ; Saccharomyces cerevisiae iso-1-cytochrome c has been expressed in Escherichia coli by coexpression of the genes encoding the cytochrome (CYC1) and yeast cytochrome c heme lyase (CYC3). Construction of this expression system involved cloning the two genes in parallel into the vector pUC18 to give the plasmid pBPCYC1(wt)/3. Transcription was directed by two promoters, Lac and Trc, that were located upstream from CYC1. Both proteins were expressed in the cytoplasm of E. coli cells harboring the plasmid. Semianaerobic cultures grown in a fermentor produced 15 mg of recombinant iso-1-cytochrome c per liter of culture. Attempts to increase production by addition of IPTG suppressed the number of copies of the CYC1 gene within the population. Wild-type iso-1-cytochrome c expressed with pBPCYC1(wt)/3 in E. coli was compared to the same protein expressed in yeast. At neutral pH, the two proteins exhibit indistinguishable spectroscopic and physical (Tm, Em') characteristics. However, electrospray mass spectrometry revealed that the lysyl residue at position 72 is not trimethylated by E. coli as it is by S. cerevisiae. Interestingly, the pKa of the alkaline transition of the protein expressed in E. coli is approximately 0.6 pKa unit lower than that observed for the cytochrome expressed in yeast (8.5-8.7). 1H NMR spectroscopy of the bacterially expressed cytochrome collected at high pH revealed the presence of a third alkaline conformer that is not observed in the corresponding spectrum of the cytochrome expressed in yeast. These observations suggest that Lys72 can serve as an axial ligand to the heme iron of alkaline iso-1-ferricytochrome c if it is not modified posttranscriptionally to trimethyllysine. ; 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 'W. B.' Pollock W. B. . 5660 3 2 'F. I.' Rosell F. I. . 5660 3 3 'M. B.' Twitchett M. B. . 5660 3 4 'M. E.' Dumont M. E. . 5660 3 5 'A. G.' Mauk A. G. . 5660 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5660 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10880578 _Citation.Full_citation ; Russell BS, Melenkivitz R, Bren KL (2000) Proc. Natl. Acad. Sci. U.S.A. 97: 8312-8317. ; _Citation.Title 'NMR investigation of ferricytochrome c unfolding: detection of an equilibrium unfolding intermediate and residual structure in the denatured state.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Citation.Journal_volume 97 _Citation.Journal_issue 15 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0027-8424 _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 8312 _Citation.Page_last 8317 _Citation.Year 2000 _Citation.Details ; Horse ferricytochrome c (cyt c) undergoes exchange of one of its axial heme ligands (Met-80) for one or more non-native ligands under denaturing conditions. We have used (1)H NMR spectroscopy to detect two conformations of paramagnetic cyt c with non-native heme ligation through a range of urea concentrations. One non-native form is an equilibrium unfolding intermediate observed under partially denaturing conditions and is attributed to replacement of Met-80 with one or more Lys side chains. The second non-native form, in which the native Met ligand is replaced by a His, is observed under strongly denaturing conditions. Thermodynamic analysis of these data indicates a relatively small DeltaG (17 kJ/mol) for the transition from native to the Lys-ligated intermediate and a significantly larger DeltaG (47 kJ/mol) for the transition from native to the His-ligated species. Although CD and fluorescence data indicate that the equilibrium unfolding of cyt c is a two-state process, these NMR results implicate an intermediate with His-Lys ligation. ; 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 'B. S.' Russell B. S. . 5660 4 2 R. Melenkivitz R. . . 5660 4 3 'K. L.' Bren K. L. . 5660 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_cyt_c _Assembly.Sf_category assembly _Assembly.Sf_framecode system_cyt_c _Assembly.Entry_ID 5660 _Assembly.ID 1 _Assembly.Name 'oxidized cytochrome c' _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 'all other bound' _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 5660 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 'cytochrome c' 1 $cyt_c . . . denatured . . . . . 5660 1 2 'HEME C' 2 $HEM . . . denatured . . . . . 5660 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 thioether single . 1 . 1 CYS 14 14 SG . 2 . 2 HEM 1 1 CAB . . . . . . . . . . 5660 1 2 thioether single . 1 . 1 CYS 17 17 SG . 2 . 2 HEM 1 1 CAC . . . . . . . . . . 5660 1 3 'metal coordination' single . 1 . 1 HIS 18 18 NE2 . 2 . 2 HEM 1 1 FE . . . . . . . . . . 5660 1 4 'metal coordination' single . 1 . 1 MET 80 80 SD . 2 . 2 HEM 1 1 FE . . . . . . . . . . 5660 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1AKK . . . . . ; Ferricyt c in our case is dissolved in 30% acetonitrile and 70% water solution whereas in 1AKK it is studied in aqueous solution. ; 5660 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'oxidized cytochrome c' system 5660 1 'cyt c' abbreviation 5660 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'electron transfer' 5660 1 'cell apoptosis' 5660 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_cyt_c _Entity.Sf_category entity _Entity.Sf_framecode cyt_c _Entity.Entry_ID 5660 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'oxidized cytochrome c' _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 ; GDVEKGKKIFVQKCAQCHTV EKGGKHKTGPNLHGLFGRKT GQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKM IFAGIKKKTEREDLIAYLKK ATNE ; _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 104 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all other bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 12384 _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 . . SWISS-PROT P68097 . 'Cytochrome c' . . . . . 100.00 105 99.04 100.00 1.64e-53 . . . . 5660 1 . . SWISS-PROT P68096 . 'Cytochrome c' . . . . . 100.00 105 99.04 100.00 1.64e-53 . . . . 5660 1 . . SWISS-PROT P00004 . 'Cytochrome c' . . . . . 100.00 105 100.00 100.00 9.71e-54 . . . . 5660 1 . . REF XP_001498872 . 'PREDICTED: similar to Cytochrome c, somatic [Equus caballus]' . . . . . 100.00 105 99.04 100.00 1.64e-53 . . . . 5660 1 . . PRF 610169A . 'cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . GenBank AAB33495 . 'apocytochrome c [horses, heart, Peptide, 104 aa]' . . . . . 100.00 104 98.08 98.08 4.15e-52 . . . . 5660 1 . . PDB 2PCB . 'Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 2GIW . 'Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, 40 Structures' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 2FRC . 'Cytochrome C (Reduced) From Equus Caballus, Nmr, Minimized Average Structure' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1WEJ . 'Igg1 Fab Fragment (Of E8 Antibody) Complexed With Horse Cytochrome C At 1.8 A Resolution' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1U75 . 'Electron Transfer Complex Between Horse Heart Cytochrome C And Zinc-Porphyrin Substituted Cytochrome C Peroxidase' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1OCD . 'Cytochrome C (Oxidized) From Equus Caballus, Nmr, Minimized Average Structure' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1M60 . 'Solution Structure Of Zinc-Substituted Cytochrome C' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1LC2 . 'Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr 30 Structures' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1LC1 . 'Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr Minimized Average Structure' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1I5T . 'Solution Structure Of Cyanoferricytochrome C' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1HRC . 'High-Resolution Three-Dimensional Structure Of Horse Heart Cytochrome C' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1GIW . 'Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, Minimized Average Structure' . . . . . 99.04 104 100.00 100.00 4.08e-53 . . . . 5660 1 . . PDB 1FI9 . 'Solution Structure Of The Imidazole Complex Of Cytochrome C' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1FI7 . 'Solution Structure Of The Imidazole Complex Of Cytochrome C' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1CRC . 'Cytochrome C At Low Ionic Strength' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . PDB 1AKK . 'Solution Structure Of Oxidized Horse Heart Cytochrome C, Nmr, Minimized Average Structure' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 948 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 947 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 946 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 944 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 673 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 672 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 665 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 645 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 630 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 5830 . 'Horse cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 5829 . 'Horse cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 5828 . 'Horse cytochrome c' . . . . . 100.00 104 98.08 100.00 2.67e-52 . . . . 5660 1 . . BMRB 5827 . 'Horse cytochrome c' . . . . . 100.00 104 98.08 100.00 2.67e-52 . . . . 5660 1 . . BMRB 546 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 545 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 544 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 543 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 5372 . 'cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 5026 . 'cytochrome C' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 499 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 4810 . 'ferric cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 4809 . 'cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 4808 . 'cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 4805 . 'cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 439 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 438 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 437 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 436 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 4189 . 'cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 336 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 317 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 316 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 286 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 285 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 274 . 'cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 244 . 'cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 243 . 'cytochrome c' . . . . . 100.00 104 100.00 100.00 1.19e-53 . . . . 5660 1 . . BMRB 2368 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 2367 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 2366 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 224 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 220 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 216 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1789 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1787 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1785 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1783 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1736 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1404 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1171 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1170 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1116 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1114 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1113 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1112 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1111 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1110 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1109 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1108 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1107 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 . . BMRB 1058 . 'cytochrome c' . . . . . 99.04 104 98.06 98.06 4.26e-51 . . . . 5660 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'oxidized cytochrome c' common 5660 1 'cyt c' abbreviation 5660 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 . GLY . 5660 1 2 . ASP . 5660 1 3 . VAL . 5660 1 4 . GLU . 5660 1 5 . LYS . 5660 1 6 . GLY . 5660 1 7 . LYS . 5660 1 8 . LYS . 5660 1 9 . ILE . 5660 1 10 . PHE . 5660 1 11 . VAL . 5660 1 12 . GLN . 5660 1 13 . LYS . 5660 1 14 . CYS . 5660 1 15 . ALA . 5660 1 16 . GLN . 5660 1 17 . CYS . 5660 1 18 . HIS . 5660 1 19 . THR . 5660 1 20 . VAL . 5660 1 21 . GLU . 5660 1 22 . LYS . 5660 1 23 . GLY . 5660 1 24 . GLY . 5660 1 25 . LYS . 5660 1 26 . HIS . 5660 1 27 . LYS . 5660 1 28 . THR . 5660 1 29 . GLY . 5660 1 30 . PRO . 5660 1 31 . ASN . 5660 1 32 . LEU . 5660 1 33 . HIS . 5660 1 34 . GLY . 5660 1 35 . LEU . 5660 1 36 . PHE . 5660 1 37 . GLY . 5660 1 38 . ARG . 5660 1 39 . LYS . 5660 1 40 . THR . 5660 1 41 . GLY . 5660 1 42 . GLN . 5660 1 43 . ALA . 5660 1 44 . PRO . 5660 1 45 . GLY . 5660 1 46 . PHE . 5660 1 47 . THR . 5660 1 48 . TYR . 5660 1 49 . THR . 5660 1 50 . ASP . 5660 1 51 . ALA . 5660 1 52 . ASN . 5660 1 53 . LYS . 5660 1 54 . ASN . 5660 1 55 . LYS . 5660 1 56 . GLY . 5660 1 57 . ILE . 5660 1 58 . THR . 5660 1 59 . TRP . 5660 1 60 . LYS . 5660 1 61 . GLU . 5660 1 62 . GLU . 5660 1 63 . THR . 5660 1 64 . LEU . 5660 1 65 . MET . 5660 1 66 . GLU . 5660 1 67 . TYR . 5660 1 68 . LEU . 5660 1 69 . GLU . 5660 1 70 . ASN . 5660 1 71 . PRO . 5660 1 72 . LYS . 5660 1 73 . LYS . 5660 1 74 . TYR . 5660 1 75 . ILE . 5660 1 76 . PRO . 5660 1 77 . GLY . 5660 1 78 . THR . 5660 1 79 . LYS . 5660 1 80 . MET . 5660 1 81 . ILE . 5660 1 82 . PHE . 5660 1 83 . ALA . 5660 1 84 . GLY . 5660 1 85 . ILE . 5660 1 86 . LYS . 5660 1 87 . LYS . 5660 1 88 . LYS . 5660 1 89 . THR . 5660 1 90 . GLU . 5660 1 91 . ARG . 5660 1 92 . GLU . 5660 1 93 . ASP . 5660 1 94 . LEU . 5660 1 95 . ILE . 5660 1 96 . ALA . 5660 1 97 . TYR . 5660 1 98 . LEU . 5660 1 99 . LYS . 5660 1 100 . LYS . 5660 1 101 . ALA . 5660 1 102 . THR . 5660 1 103 . ASN . 5660 1 104 . GLU . 5660 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 . GLY 1 1 5660 1 . ASP 2 2 5660 1 . VAL 3 3 5660 1 . GLU 4 4 5660 1 . LYS 5 5 5660 1 . GLY 6 6 5660 1 . LYS 7 7 5660 1 . LYS 8 8 5660 1 . ILE 9 9 5660 1 . PHE 10 10 5660 1 . VAL 11 11 5660 1 . GLN 12 12 5660 1 . LYS 13 13 5660 1 . CYS 14 14 5660 1 . ALA 15 15 5660 1 . GLN 16 16 5660 1 . CYS 17 17 5660 1 . HIS 18 18 5660 1 . THR 19 19 5660 1 . VAL 20 20 5660 1 . GLU 21 21 5660 1 . LYS 22 22 5660 1 . GLY 23 23 5660 1 . GLY 24 24 5660 1 . LYS 25 25 5660 1 . HIS 26 26 5660 1 . LYS 27 27 5660 1 . THR 28 28 5660 1 . GLY 29 29 5660 1 . PRO 30 30 5660 1 . ASN 31 31 5660 1 . LEU 32 32 5660 1 . HIS 33 33 5660 1 . GLY 34 34 5660 1 . LEU 35 35 5660 1 . PHE 36 36 5660 1 . GLY 37 37 5660 1 . ARG 38 38 5660 1 . LYS 39 39 5660 1 . THR 40 40 5660 1 . GLY 41 41 5660 1 . GLN 42 42 5660 1 . ALA 43 43 5660 1 . PRO 44 44 5660 1 . GLY 45 45 5660 1 . PHE 46 46 5660 1 . THR 47 47 5660 1 . TYR 48 48 5660 1 . THR 49 49 5660 1 . ASP 50 50 5660 1 . ALA 51 51 5660 1 . ASN 52 52 5660 1 . LYS 53 53 5660 1 . ASN 54 54 5660 1 . LYS 55 55 5660 1 . GLY 56 56 5660 1 . ILE 57 57 5660 1 . THR 58 58 5660 1 . TRP 59 59 5660 1 . LYS 60 60 5660 1 . GLU 61 61 5660 1 . GLU 62 62 5660 1 . THR 63 63 5660 1 . LEU 64 64 5660 1 . MET 65 65 5660 1 . GLU 66 66 5660 1 . TYR 67 67 5660 1 . LEU 68 68 5660 1 . GLU 69 69 5660 1 . ASN 70 70 5660 1 . PRO 71 71 5660 1 . LYS 72 72 5660 1 . LYS 73 73 5660 1 . TYR 74 74 5660 1 . ILE 75 75 5660 1 . PRO 76 76 5660 1 . GLY 77 77 5660 1 . THR 78 78 5660 1 . LYS 79 79 5660 1 . MET 80 80 5660 1 . ILE 81 81 5660 1 . PHE 82 82 5660 1 . ALA 83 83 5660 1 . GLY 84 84 5660 1 . ILE 85 85 5660 1 . LYS 86 86 5660 1 . LYS 87 87 5660 1 . LYS 88 88 5660 1 . THR 89 89 5660 1 . GLU 90 90 5660 1 . ARG 91 91 5660 1 . GLU 92 92 5660 1 . ASP 93 93 5660 1 . LEU 94 94 5660 1 . ILE 95 95 5660 1 . ALA 96 96 5660 1 . TYR 97 97 5660 1 . LEU 98 98 5660 1 . LYS 99 99 5660 1 . LYS 100 100 5660 1 . ALA 101 101 5660 1 . THR 102 102 5660 1 . ASN 103 103 5660 1 . GLU 104 104 5660 1 stop_ save_ save_HEM _Entity.Sf_category entity _Entity.Sf_framecode HEM _Entity.Entry_ID 5660 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name HEM _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 no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID HEM _Entity.Nonpolymer_comp_label $chem_comp_HEM _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _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 . _Entity.DB_query_revised_last_date . 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 . HEM . 5660 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 5660 _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.Subvariant _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.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $cyt_c . 9796 organism . 'Equus caballus' Horse . . Eukaryota Metazoa Equus caballus . . . heart muscle . . . . . . . mitochrondrion . . . . . . . . 5660 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 5660 _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_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _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.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $cyt_c . vendor . . . . . . . . . . . . . . . . . . . . . . . . Sigma . . . . 5660 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_HEM _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_HEM _Chem_comp.Entry_ID 5660 _Chem_comp.ID HEM _Chem_comp.Provenance . _Chem_comp.Name 'PROTOPORPHYRIN IX CONTAINING FE' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code HEM _Chem_comp.Ambiguous_flag yes _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2009-08-11 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces MHM _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code HEM _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _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 HEME _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic yes _Chem_comp.Formula 'C34 H32 Fe N4 O4' _Chem_comp.Formula_weight 616.487 _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 . _Chem_comp.Model_coordinates_db_code 3IA3 _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jul 26 11:01:26 2011 ; _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 O=C(O)CCc5c(c2nc5cc1nc(C(=C1CCC(=O)O)C)cc4c(c(c(cc3nc(c2)C(=C3\C=C)C)n4)C)\C=C)C SMILES ACDLabs 11.02 5660 HEM InChI=1S/C34H34N4O4/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25/h7-8,13-16,36-37H,1-2,9-12H2,3-6H3,(H,39,40)(H,41,42)/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16- InChI InChI 1.02 5660 HEM FEDYMSUPMFCVOD-UJJXFSCMSA-N InChIKey InChI 1.02 5660 HEM Cc1c2[nH]c(cc3nc(cc4[nH]c(cc5nc(c2)c(C)c5C=C)c(C)c4C=C)c(C)c3CCC(O)=O)c1CCC(O)=O SMILES_CANONICAL CACTVS 3.352 5660 HEM Cc1c2[nH]c(cc3nc(cc4[nH]c(cc5nc(c2)c(C)c5C=C)c(C)c4C=C)c(C)c3CCC(O)=O)c1CCC(O)=O SMILES CACTVS 3.352 5660 HEM Cc1c2/cc/3\nc(/cc\4/c(c(/c(/[nH]4)c/c5n/c(c\c(c1CCC(=O)O)[nH]2)/C(=C5C)CCC(=O)O)C=C)C)C(=C3C)C=C SMILES_CANONICAL 'OpenEye OEToolkits' 1.7.0 5660 HEM Cc1c2cc3nc(cc4c(c(c([nH]4)cc5nc(cc(c1CCC(=O)O)[nH]2)C(=C5C)CCC(=O)O)C=C)C)C(=C3C)C=C SMILES 'OpenEye OEToolkits' 1.7.0 5660 HEM 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 '3,3'-(7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-diyl)dipropanoic acid' 'SYSTEMATIC NAME' ACDLabs 11.02 5660 HEM '3-[(5Z,10Z,14Z,19Z)-18-(2-carboxyethyl)-8,13-bis(ethenyl)-3,7,12,17-tetramethyl-21,23-dihydroporphyrin-2-yl]propanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.6.1 5660 HEM 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 CHA . CHA . . C . . N 0 . . . . yes no . . . . 2.748 . -19.531 . 39.896 . -2.161 -0.125 0.490 1 . 5660 HEM CHB . CHB . . C . . N 0 . . . . yes no . . . . 3.258 . -17.744 . 35.477 . 1.458 -3.419 0.306 2 . 5660 HEM CHC . CHC . . C . . N 0 . . . . yes no . . . . 1.703 . -21.900 . 33.637 . 4.701 0.169 -0.069 3 . 5660 HEM CHD . CHD . . C . . N 0 . . . . yes no . . . . 1.149 . -23.677 . 38.059 . 1.075 3.460 0.018 4 . 5660 HEM C1A . C1A . . C . . N 0 . . . . yes no . . . . 3.031 . -18.673 . 38.872 . -1.436 -1.305 0.380 5 . 5660 HEM C2A . C2A . . C . . N 0 . . . . yes no . . . . 3.578 . -17.325 . 39.013 . -2.015 -2.587 0.320 6 . 5660 HEM C3A . C3A . . C . . N 0 . . . . yes no . . . . 3.705 . -16.820 . 37.785 . -1.009 -3.500 0.270 7 . 5660 HEM C4A . C4A . . C . . N 0 . . . . yes no . . . . 3.256 . -17.863 . 36.862 . 0.216 -2.803 0.298 8 . 5660 HEM CMA . CMA . . C . . N 0 . . . . no no . . . . 4.227 . -15.469 . 37.393 . -1.175 -4.996 0.197 9 . 5660 HEM CAA . CAA . . C . . N 0 . . . . no no . . . . 3.945 . -16.670 . 40.296 . -3.490 -2.893 0.314 10 . 5660 HEM CBA . CBA . . C . . N 0 . . . . no no . . . . 5.391 . -17.138 . 40.581 . -3.998 -2.926 -1.129 11 . 5660 HEM CGA . CGA . . C . . N 0 . . . . no no . . . . 6.095 . -16.663 . 41.825 . -5.473 -3.232 -1.136 12 . 5660 HEM O1A . O1A . . O . . N 0 . . . . no no . . . . 7.098 . -15.928 . 41.683 . -6.059 -3.405 -0.094 13 . 5660 HEM O2A . O2A . . O . . N 0 . . . . no no . . . . 5.657 . -17.040 . 42.940 . -6.137 -3.311 -2.300 14 . 5660 HEM C1B . C1B . . C . . N 0 . . . . yes no . . . . 2.888 . -18.698 . 34.579 . 2.664 -2.707 0.308 15 . 5660 HEM C2B . C2B . . C . . N 0 . . . . yes no . . . . 2.933 . -18.535 . 33.146 . 3.937 -3.328 0.418 16 . 5660 HEM C3B . C3B . . C . . N 0 . . . . yes no . . . . 2.499 . -19.716 . 32.632 . 4.874 -2.341 0.314 17 . 5660 HEM C4B . C4B . . C . . N 0 . . . . yes no . . . . 2.187 . -20.580 . 33.743 . 4.117 -1.079 0.139 18 . 5660 HEM CMB . CMB . . C . . N 0 . . . . no no . . . . 3.391 . -17.290 . 32.422 . 4.203 -4.798 0.613 19 . 5660 HEM CAB . CAB . . C . . N 0 . . . . no no . . . . 2.345 . -20.140 . 31.217 . 6.339 -2.497 0.365 20 . 5660 HEM CBB . CBB . . C . . N 0 . . . . no no . . . . 1.755 . -19.492 . 30.233 . 6.935 -3.419 -0.385 21 . 5660 HEM C1C . C1C . . C . . N 0 . . . . yes no . . . . 1.395 . -22.786 . 34.659 . 3.964 1.345 -0.174 22 . 5660 HEM C2C . C2C . . C . . N 0 . . . . yes no . . . . 0.854 . -24.130 . 34.500 . 4.531 2.601 -0.445 23 . 5660 HEM C3C . C3C . . C . . N 0 . . . . yes no . . . . 0.689 . -24.626 . 35.757 . 3.510 3.536 -0.437 24 . 5660 HEM C4C . C4C . . C . . N 0 . . . . yes no . . . . 1.139 . -23.583 . 36.674 . 2.304 2.846 -0.139 25 . 5660 HEM CMC . CMC . . C . . N 0 . . . . no no . . . . 0.550 . -24.782 . 33.175 . 5.991 2.880 -0.697 26 . 5660 HEM CAC . CAC . . C . . N 0 . . . . no no . . . . 0.164 . -25.943 . 36.196 . 3.649 4.981 -0.692 27 . 5660 HEM CBC . CBC . . C . . N 0 . . . . no no . . . . 0.498 . -27.158 . 35.750 . 4.201 5.407 -1.823 28 . 5660 HEM C1D . C1D . . C . . N 0 . . . . yes no . . . . 1.550 . -22.718 . 38.980 . -0.102 2.753 0.298 29 . 5660 HEM C2D . C2D . . C . . N 0 . . . . yes no . . . . 1.513 . -22.879 . 40.415 . -1.382 3.388 0.641 30 . 5660 HEM C3D . C3D . . C . . N 0 . . . . yes no . . . . 1.951 . -21.691 . 40.929 . -2.283 2.389 0.774 31 . 5660 HEM C4D . C4D . . C . . N 0 . . . . yes no . . . . 2.277 . -20.826 . 39.811 . -1.561 1.137 0.511 32 . 5660 HEM CMD . CMD . . C . . N 0 . . . . no no . . . . 1.055 . -24.094 . 41.156 . -1.639 4.863 0.811 33 . 5660 HEM CAD . CAD . . C . . N 0 . . . . no no . . . . 2.048 . -21.326 . 42.352 . -3.741 2.532 1.123 34 . 5660 HEM CBD . CBD . . C . . N 0 . . . . no no . . . . 0.741 . -20.498 . 42.530 . -4.573 2.563 -0.160 35 . 5660 HEM CGD . CGD . . C . . N 0 . . . . no no . . . . 0.578 . -19.987 . 43.892 . -6.032 2.706 0.189 36 . 5660 HEM O1D . O1D . . O . . N 0 . . . . no no . . . . 1.387 . -19.103 . 44.303 . -6.372 2.776 1.347 37 . 5660 HEM O2D . O2D . . O . . N 0 . . . . no no . . . . -0.401 . -20.468 . 44.537 . -6.954 2.755 -0.785 38 . 5660 HEM NA . NA . . N . . N 0 . . . . yes no . . . . 2.863 . -18.969 . 37.554 . -0.068 -1.456 0.321 39 . 5660 HEM NB . NB . . N . . N 0 . . . . yes no . . . . 2.439 . -19.944 . 34.911 . 2.820 -1.386 0.207 40 . 5660 HEM NC . NC . . N . . N 0 . . . . yes no . . . . 1.537 . -22.509 . 35.976 . 2.604 1.506 -0.033 41 . 5660 HEM ND . ND . . N . . N 0 . . . . yes no . . . . 2.008 . -21.465 . 38.663 . -0.276 1.431 0.298 42 . 5660 HEM FE . FE . . FE . . S 0 . . . . no no . . . . 2.196 . -20.749 . 36.814 . 1.010 0.157 -0.060 43 . 5660 HEM HHB . HHB . . H . . N 0 . . . . no no . . . . 3.587 . -16.798 . 35.072 . 1.498 -4.508 0.309 44 . 5660 HEM HHC . HHC . . H . . N 0 . . . . no no . . . . 1.553 . -22.268 . 32.633 . 5.786 0.229 -0.153 45 . 5660 HEM HHD . HHD . . H . . N 0 . . . . no no . . . . 0.802 . -24.613 . 38.472 . 1.018 4.543 -0.083 46 . 5660 HEM HMA . HMA . . H . . N 0 . . . . no no . . . . 5.316 . -15.524 . 37.249 . -1.220 -5.306 -0.847 47 . 5660 HEM HMAA . HMAA . . H . . N 0 . . . . no no . . . . 3.749 . -15.149 . 36.455 . -0.328 -5.480 0.683 48 . 5660 HEM HMAB . HMAB . . H . . N 0 . . . . no no . . . . 3.998 . -14.743 . 38.187 . -2.097 -5.285 0.702 49 . 5660 HEM HAA . HAA . . H . . N 0 . . . . no no . . . . 3.894 . -15.575 . 40.209 . -3.662 -3.862 0.782 50 . 5660 HEM HAAA . HAAA . . H . . N 0 . . . . no no . . . . 3.264 . -16.976 . 41.104 . -4.024 -2.121 0.869 51 . 5660 HEM HBA . HBA . . H . . N 0 . . . . no no . . . . 5.351 . -18.235 . 40.650 . -3.825 -1.956 -1.597 52 . 5660 HEM HBAA . HBAA . . H . . N 0 . . . . no no . . . . 5.999 . -16.792 . 39.732 . -3.464 -3.697 -1.684 53 . 5660 HEM HMB . HMB . . H . . N 0 . . . . no no . . . . 3.319 . -17.449 . 31.336 . 3.256 -5.336 0.660 54 . 5660 HEM HMBA . HMBA . . H . . N 0 . . . . no no . . . . 2.753 . -16.442 . 32.711 . 4.794 -5.175 -0.222 55 . 5660 HEM HMBB . HMBB . . H . . N 0 . . . . no no . . . . 4.435 . -17.072 . 32.692 . 4.752 -4.948 1.543 56 . 5660 HEM HAB . HAB . . H . . N 0 . . . . no no . . . . 2.770 . -21.100 . 30.963 . 6.927 -1.863 1.011 57 . 5660 HEM HBB . HBB . . H . . N 0 . . . . no no . . . . 1.719 . -19.927 . 29.245 . 7.994 -3.600 -0.277 58 . 5660 HEM HBBA . HBBA . . H . . N 0 . . . . no no . . . . 1.308 . -18.526 . 30.414 . 6.360 -3.987 -1.102 59 . 5660 HEM HMC . HMC . . H . . N 0 . . . . no no . . . . 1.438 . -25.328 . 32.822 . 6.554 1.949 -0.639 60 . 5660 HEM HMCA . HMCA . . H . . N 0 . . . . no no . . . . -0.288 . -25.484 . 33.296 . 6.110 3.316 -1.689 61 . 5660 HEM HMCB . HMCB . . H . . N 0 . . . . no no . . . . 0.278 . -24.010 . 32.440 . 6.362 3.578 0.053 62 . 5660 HEM HAC . HAC . . H . . N 0 . . . . no no . . . . -0.583 . -25.916 . 36.975 . 3.303 5.694 0.042 63 . 5660 HEM HBC . HBC . . H . . N 0 . . . . no no . . . . 0.027 . -28.035 . 36.169 . 4.614 4.696 -2.523 64 . 5660 HEM HBCA . HBCA . . H . . N 0 . . . . no no . . . . 1.239 . -27.263 . 34.971 . 4.235 6.464 -2.043 65 . 5660 HEM HMD . HMD . . H . . N 0 . . . . no no . . . . 1.142 . -23.919 . 42.238 . -0.715 5.415 0.639 66 . 5660 HEM HMDA . HMDA . . H . . N 0 . . . . no no . . . . 0.006 . -24.304 . 40.902 . -2.394 5.185 0.094 67 . 5660 HEM HMDB . HMDB . . H . . N 0 . . . . no no . . . . 1.680 . -24.954 . 40.872 . -1.994 5.055 1.824 68 . 5660 HEM HAD . HAD . . H . . N 0 . . . . no no . . . . 2.081 . -22.206 . 43.011 . -4.052 1.687 1.738 69 . 5660 HEM HADA . HADA . . H . . N 0 . . . . no no . . . . 2.951 . -20.739 . 42.575 . -3.893 3.459 1.677 70 . 5660 HEM HBD . HBD . . H . . N 0 . . . . no no . . . . 0.775 . -19.642 . 41.839 . -4.262 3.408 -0.775 71 . 5660 HEM HBDA . HBDA . . H . . N 0 . . . . no no . . . . -0.116 . -21.147 . 42.297 . -4.421 1.636 -0.714 72 . 5660 HEM H2A . H2A . . H . . N 0 . . . . no no . . . . 6.201 . -16.682 . 43.632 . -7.082 -3.510 -2.254 73 . 5660 HEM H2D . H2D . . H . . N 0 . . . . no no . . . . -0.445 . -20.063 . 45.395 . -7.877 2.847 -0.512 74 . 5660 HEM HHA . HHA . . H . . N 0 . . . . no no . . . . 2.913 . -19.150 . 40.893 . -3.246 -0.188 0.567 75 . 5660 HEM 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 CHA C1A yes N 1 . 5660 HEM 2 . DOUB CHA C4D yes N 2 . 5660 HEM 3 . SING CHA HHA no N 3 . 5660 HEM 4 . SING CHB C4A yes N 4 . 5660 HEM 5 . DOUB CHB C1B yes N 5 . 5660 HEM 6 . SING CHB HHB no N 6 . 5660 HEM 7 . SING CHC C4B yes N 7 . 5660 HEM 8 . DOUB CHC C1C yes N 8 . 5660 HEM 9 . SING CHC HHC no N 9 . 5660 HEM 10 . DOUB CHD C4C yes N 10 . 5660 HEM 11 . SING CHD C1D yes N 11 . 5660 HEM 12 . SING CHD HHD no N 12 . 5660 HEM 13 . DOUB C1A C2A yes N 13 . 5660 HEM 14 . SING C1A NA yes N 14 . 5660 HEM 15 . SING C2A C3A yes N 15 . 5660 HEM 16 . SING C2A CAA no N 16 . 5660 HEM 17 . DOUB C3A C4A yes N 17 . 5660 HEM 18 . SING C3A CMA no N 18 . 5660 HEM 19 . SING C4A NA yes N 19 . 5660 HEM 20 . SING CMA HMA no N 20 . 5660 HEM 21 . SING CMA HMAA no N 21 . 5660 HEM 22 . SING CMA HMAB no N 22 . 5660 HEM 23 . SING CAA CBA no N 23 . 5660 HEM 24 . SING CAA HAA no N 24 . 5660 HEM 25 . SING CAA HAAA no N 25 . 5660 HEM 26 . SING CBA CGA no N 26 . 5660 HEM 27 . SING CBA HBA no N 27 . 5660 HEM 28 . SING CBA HBAA no N 28 . 5660 HEM 29 . DOUB CGA O1A no N 29 . 5660 HEM 30 . SING CGA O2A no N 30 . 5660 HEM 31 . SING C1B C2B no N 31 . 5660 HEM 32 . SING C1B NB yes N 32 . 5660 HEM 33 . DOUB C2B C3B yes N 33 . 5660 HEM 34 . SING C2B CMB yes N 34 . 5660 HEM 35 . SING C3B C4B no N 35 . 5660 HEM 36 . SING C3B CAB yes N 36 . 5660 HEM 37 . DOUB C4B NB no N 37 . 5660 HEM 38 . SING CMB HMB yes N 38 . 5660 HEM 39 . SING CMB HMBA no N 39 . 5660 HEM 40 . SING CMB HMBB no N 40 . 5660 HEM 41 . DOUB CAB CBB no N 41 . 5660 HEM 42 . SING CAB HAB no N 42 . 5660 HEM 43 . SING CBB HBB no N 43 . 5660 HEM 44 . SING CBB HBBA no N 44 . 5660 HEM 45 . SING C1C C2C no N 45 . 5660 HEM 46 . SING C1C NC yes N 46 . 5660 HEM 47 . DOUB C2C C3C yes N 47 . 5660 HEM 48 . SING C2C CMC yes N 48 . 5660 HEM 49 . SING C3C C4C no N 49 . 5660 HEM 50 . SING C3C CAC yes N 50 . 5660 HEM 51 . SING C4C NC no N 51 . 5660 HEM 52 . SING CMC HMC yes N 52 . 5660 HEM 53 . SING CMC HMCA no N 53 . 5660 HEM 54 . SING CMC HMCB no N 54 . 5660 HEM 55 . DOUB CAC CBC no N 55 . 5660 HEM 56 . SING CAC HAC no N 56 . 5660 HEM 57 . SING CBC HBC no N 57 . 5660 HEM 58 . SING CBC HBCA no N 58 . 5660 HEM 59 . SING C1D C2D no N 59 . 5660 HEM 60 . DOUB C1D ND yes N 60 . 5660 HEM 61 . DOUB C2D C3D yes N 61 . 5660 HEM 62 . SING C2D CMD yes N 62 . 5660 HEM 63 . SING C3D C4D no N 63 . 5660 HEM 64 . SING C3D CAD yes N 64 . 5660 HEM 65 . SING C4D ND no N 65 . 5660 HEM 66 . SING CMD HMD yes N 66 . 5660 HEM 67 . SING CMD HMDA no N 67 . 5660 HEM 68 . SING CMD HMDB no N 68 . 5660 HEM 69 . SING CAD CBD no N 69 . 5660 HEM 70 . SING CAD HAD no N 70 . 5660 HEM 71 . SING CAD HADA no N 71 . 5660 HEM 72 . SING CBD CGD no N 72 . 5660 HEM 73 . SING CBD HBD no N 73 . 5660 HEM 74 . SING CBD HBDA no N 74 . 5660 HEM 75 . DOUB CGD O1D no N 75 . 5660 HEM 76 . SING CGD O2D no N 76 . 5660 HEM 77 . SING O2A H2A no N 77 . 5660 HEM 78 . SING O2D H2D no N 78 . 5660 HEM 79 . SING FE NA no N 79 . 5660 HEM 80 . SING FE NB no N 80 . 5660 HEM 81 . SING FE NC no N 81 . 5660 HEM 82 . SING FE ND no N 82 . 5660 HEM stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5660 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; Oxidized cytochrome c dissolved in 30% acetonitrile-70% aqueous solution resulted in formation of four NMR observable cyt c forms distingushed by the identity of the sixth axial ligand of the heme iron. One met80-ligated cyt c designated as III* form, two lysine-ligated cyt c designated as IVa* and IVb* forms, and one histidine ligated cyt c designated as V* form are produced. ; _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 'oxidized cytochrome c' . . . 1 $cyt_c . . 2 . . mM . . . . 5660 1 2 'PROTOPORPHYRIN IX CONTAINING FE' . . . 2 $HEM . . 2 . . mM . . . . 5660 1 3 acetonitrile . . . . . . . 30 . . % . . . . 5660 1 4 H2O . . . . . . . 70 . . % . . . . 5660 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 5660 _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 0.2 n/a 5660 1 temperature 293 1 K 5660 1 stop_ save_ save_Ex-cond_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_2 _Sample_condition_list.Entry_ID 5660 _Sample_condition_list.ID 2 _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 0.2 n/a 5660 2 temperature 313 1 K 5660 2 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 5660 _Software.ID 1 _Software.Name FELIX _Software.Version 2000 _Software.Details http://www.accelyrs.com loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectral processing' 5660 1 'spectral analysis' 5660 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5660 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Mercury _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 300 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5660 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details 'Home made, Center for Magnetic Resonance at MIT/Harvard.' _NMR_spectrometer.Manufacturer 'home made' _NMR_spectrometer.Model . _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_3 _NMR_spectrometer.Entry_ID 5660 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details 'Home made, Center for Magnetic Resonance at MIT/Harvard.' _NMR_spectrometer.Manufacturer 'home made' _NMR_spectrometer.Model . _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5660 _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_1 Varian Mercury . 300 . . . 5660 1 2 NMR_spectrometer_2 'home made' . . 500 'Home made, Center for Magnetic Resonance at MIT/Harvard.' . . 5660 1 3 NMR_spectrometer_3 'home made' . . 600 'Home made, Center for Magnetic Resonance at MIT/Harvard.' . . 5660 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 5660 _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 '1H NOESY' . 1 $NMR_applied_experiment . . . . . . . . 1 $sample_1 . . . . . . . . . . . . . . . . . . . . . . . . . . 5660 1 stop_ save_ save_NMR_applied_experiment _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_applied_experiment _NMR_spec_expt.Entry_ID 5660 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $FELIX _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . 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 5660 _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.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5660 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_shift_set_protein _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_protein _Assigned_chem_shift_list.Entry_ID 5660 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _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 ; Ferricytochrome c in 30% acetonitrile and 70% water solution exists as mixture of atleast four NMR-observable conformers. For this deposition we described each conformer as a component for a single sample (i.e., sample 1). So there are four components representing four conformers of ferricyt c. Proton chemical shifts of component 1 of sample 1. M80-ligated ferricytochrome c (III*-form). ; _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 $sample_1 . 5660 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 18 18 HIS HB2 H 1 9.00 0.02 . 2 . . . . . . . . 5660 1 2 . 1 1 18 18 HIS HB3 H 1 14.60 0.02 . 2 . . . . . . . . 5660 1 3 . 1 1 18 18 HIS HD2 H 1 24.50 0.02 . 2 . . . . . . . . 5660 1 4 . 1 1 30 30 PRO HG2 H 1 -0.90 0.02 . 2 . . . . . . . . 5660 1 5 . 1 1 30 30 PRO HD2 H 1 -4.43 0.02 . 2 . . . . . . . . 5660 1 6 . 1 1 30 30 PRO HD3 H 1 -2.32 0.02 . 2 . . . . . . . . 5660 1 7 . 1 1 59 59 TRP HH2 H 1 7.51 0.02 . 2 . . . . . . . . 5660 1 stop_ save_ save_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5660 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _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 ; Ferricytochrome c in 30% acetonitrile and 70% water solution exists as mixture of atleast four NMR-observable conformers. For this deposition we described each conformer as a component for a single sample (i.e., sample 1). So there are four components representing four conformers of ferricyt c. Proton chemical shifts of component 1 of sample 1. M80-ligated ferricytochrome c (III*-form). ; _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 $sample_1 . 5660 2 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 . 2 2 1 1 HEM HBA1 H 1 1.51 0.02 . 1 . . . . . . . . 5660 2 2 . 2 2 1 1 HEM HBA2 H 1 -0.59 0.02 . 1 . . . . . . . . 5660 2 3 . 2 2 1 1 HEM HAA1 H 1 11.61 0.02 . 1 . . . . . . . . 5660 2 4 . 2 2 1 1 HEM HAA2 H 1 19.14 0.02 . 1 . . . . . . . . 5660 2 5 . 2 2 1 1 HEM HMB1 H 1 7.20 0.02 . 2 . . . . . . . . 5660 2 6 . 2 2 1 1 HEM HBB1 H 1 -2.63 0.02 . 2 . . . . . . . . 5660 2 7 . 2 2 1 1 HEM HBC1 H 1 3.10 0.02 . 2 . . . . . . . . 5660 2 8 . 2 2 1 1 HEM HAC H 1 2.17 0.02 . 1 . . . . . . . . 5660 2 9 . 2 2 1 1 HEM HMC1 H 1 32.44 0.02 . 2 . . . . . . . . 5660 2 10 . 2 2 1 1 HEM HMD1 H 1 9.77 0.02 . 2 . . . . . . . . 5660 2 11 . 2 2 1 1 HEM HAD1 H 1 -1.33 0.02 . 1 . . . . . . . . 5660 2 12 . 2 2 1 1 HEM HAD2 H 1 1.95 0.02 . 1 . . . . . . . . 5660 2 13 . 2 2 1 1 HEM HMA1 H 1 35.74 0.02 . 2 . . . . . . . . 5660 2 14 . 2 2 1 1 HEM HHB H 1 -2.75 0.02 . 1 . . . . . . . . 5660 2 stop_ save_ save_shift_set_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_2 _Assigned_chem_shift_list.Entry_ID 5660 _Assigned_chem_shift_list.ID 3 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _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 ; Ferricytochrome c in 30% acetonitrile and 70% water solution exists as mixture of atleast four NMR-observable conformers. For this deposition we described each conformer as a component for a single sample (i.e., sample 1). So there are four components representing four conformers of ferricyt c. Proton chemical shifts of component 1 of sample 1. Lysine-ligated ferricytochrome c (IVa* form). ; _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 $sample_1 . 5660 3 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 . 2 2 1 1 HEM HBA1 H 1 2.00 0.02 . 1 . . . . . . . . 5660 3 2 . 2 2 1 1 HEM HBA2 H 1 0.98 0.02 . 1 . . . . . . . . 5660 3 3 . 2 2 1 1 HEM HAA1 H 1 0.00 0.02 . 1 . . . . . . . . 5660 3 4 . 2 2 1 1 HEM HAA2 H 1 -1.02 0.02 . 1 . . . . . . . . 5660 3 5 . 2 2 1 1 HEM HMB1 H 1 12.93 0.02 . 2 . . . . . . . . 5660 3 6 . 2 2 1 1 HEM HMC1 H 1 11.45 0.02 . 2 . . . . . . . . 5660 3 7 . 2 2 1 1 HEM HMD1 H 1 21.11 0.02 . 2 . . . . . . . . 5660 3 8 . 2 2 1 1 HEM HMA1 H 1 22.87 0.02 . 2 . . . . . . . . 5660 3 9 . 2 2 1 1 HEM HHB H 1 -6.06 0.02 . 1 . . . . . . . . 5660 3 stop_ save_ save_shift_set_3 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_3 _Assigned_chem_shift_list.Entry_ID 5660 _Assigned_chem_shift_list.ID 4 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _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 ; Ferricytochrome c in 30% acetonitrile and 70% water solution exists as mixture of at least four NMR-observable conformers. For this deposition we described each conformer as a component for a single sample (i.e., sample 1). So there are four components representing four conformers of ferricyt c. Proton chemical shifts of component 1 of sample 1. Lysine-ligated ferricytochrome c (IVb* form). ; _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 $sample_1 . 5660 4 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 . 2 2 1 1 HEM HAA2 H 1 -0.81 0.02 . 1 . . . . . . . . 5660 4 2 . 2 2 1 1 HEM HMB1 H 1 13.64 0.02 . 2 . . . . . . . . 5660 4 3 . 2 2 1 1 HEM HMC1 H 1 11.81 0.02 . 2 . . . . . . . . 5660 4 4 . 2 2 1 1 HEM HMD1 H 1 21.11 0.02 . 2 . . . . . . . . 5660 4 5 . 2 2 1 1 HEM HMA1 H 1 21.56 0.02 . 2 . . . . . . . . 5660 4 6 . 2 2 1 1 HEM HHB H 1 -5.68 0.02 . 1 . . . . . . . . 5660 4 stop_ save_ save_shift_set_4 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_4 _Assigned_chem_shift_list.Entry_ID 5660 _Assigned_chem_shift_list.ID 5 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _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 ; Ferricytochrome c in 30% acetonitrile and 70% water solution exists as mixture of atleast four NMR-observable conformers. For this deposition we described each conformer as a component for a single sample (i.e., sample 1). So there are four components representing four conformers of ferricyt c. Proton chemical shifts of component 1 of sample 1. Histidine -ligated ferricytochrome c (V* form). ; _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 $sample_1 . 5660 5 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 . 2 2 1 1 HEM HMC1 H 1 12.10 0.02 . 2 . . . . . . . . 5660 5 2 . 2 2 1 1 HEM HMD1 H 1 19.34 0.02 . 2 . . . . . . . . 5660 5 3 . 2 2 1 1 HEM HMA1 H 1 24.50 0.02 . 2 . . . . . . . . 5660 5 stop_ save_