data_5372 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure Of Reduced Horse Heart Cytochrome c in 30% Acetonitrile Solution ; _BMRB_accession_number 5372 _BMRB_flat_file_name bmr5372.str _Entry_type original _Submission_date 2002-05-09 _Accession_date 2002-05-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sivakolundu Sivashankar G. . 2 Mabrouk Patricia A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 589 "coupling constants" 73 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-06-09 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5660 'four conformers of ferricyt c.' stop_ _Original_release_date 2003-06-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure-function Relationship of Reduced Cytochrome c Probed by Complete Solution Structure Determination in 30% Acetonitrile/Water Solution ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22648577 _PubMed_ID 12764601 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sivakolundu Sivashankar G. . 2 Mabrouk Patricia A. . stop_ _Journal_abbreviation 'J. Biol. Inorg. Chem.' _Journal_name_full 'Journal of Biological Inorganic Chemistry' _Journal_volume 8 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 527 _Page_last 539 _Year 2003 _Details . loop_ _Keyword 'cytochrome c' 'organic solvent' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Wand, A. J.; Stefano, D. L. D. Biochemistry 1989, 28, 186-194. ; _Citation_title 'Proton resonance assignments of horse ferrocytochrome c.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 2539854 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wand 'A. J.' J. . 2 'Di Stefano' 'D. L.' L. . 3 Feng 'Y. Q.' Q. . 4 Roder H. . . 5 Englander 'S. W.' W. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 28 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 186 _Page_last 194 _Year 1989 _Details ; Two-dimensional nuclear magnetic resonance (NMR) spectroscopy was used to assign the proton resonances of horse ferrocytochrome c. Assignments were based on the main chain directed (MCD) and sequential assignment procedures. The fundamental units of the MCD approach, the main-chain NH-C alpha H-C beta H J-coupled subspin systems of each amino acid residue (NAB sets), were defined by analysis of direct and relayed coherence transfer spectra. Recognition of main-chain NOE connectivity patterns specified in the MCD algorithm then allowed NAB sets to be aligned in their proper juxtaposition within secondary structural units. The units of secondary structure were placed within the polypeptide sequence of identification of a small number of side-chain J-coupled spin systems, found by direct recognition in 2D spectra of some J-coupled spin systems and by pairwise comparisons of the J-correlated spectra of six homologous cytochromes c having a small number of known amino acid differences. The placement of a given segment in this way defines the amino acid identity of all its NAB sets. This foreknowledge allowed the vast majority of the side-chain resonances to be discerned in J-correlated spectra. Extensive confirmation of the assignments derives internally from multiple main-chain NOE connectivities and their consistency following temperature-induced changes of the chemical shifts of NOE-correlated protons. The observed patterns of main-chain NOEs provide some structural information and suggest small but potentially significant differences between the solution structure observed by NMR and that defined earlier in crystallographic studies at 2.8-A resolution. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Banci, L.; Bertini, I.; Huber, J. G.; Spyroulias, G. A.; Turano, P. J. Biol. Inorg. Chem. 1999, 4, 21-31. ; _Citation_title 'Solution structure of reduced horse heart cytochrome c.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10499099 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci L. . . 2 Bertini I. . . 3 Huber 'J. G.' G. . 4 Spyroulias 'G. A.' A. . 5 Turano P. . . stop_ _Journal_abbreviation 'J. Biol. Inorg. Chem.' _Journal_name_full 'Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry' _Journal_volume 4 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 21 _Page_last 31 _Year 1999 _Details ; In the frame of a broad study on the structural differences between the two redox forms of cytochromes to be related to the electron transfer process, the NMR solution structure of horse heart cytochrome c in the reduced form has been determined. The structural data obtained in the present work are compared to those already available in the literature on the same protein and the presence of conformational differences is discussed in the light of the experimental method employed for the structure determination. Redox-state dependent changes are analyzed and in particular they are related to the role of propionate-7 of the heme. Also some hydrogen bonds are changed upon reduction of the heme iron. A substantial similarity is observed for the backbone fold, independently of the oxidation state. At variance, some meaningful differences are observed in the orientation of a few side chains. These changes are related to those found in the case of the highly homologous cytochrome c from Saccharomyces cerevisiae. The exchangeability of the NH protons has been investigated and found to be smaller than in the case of the oxidized protein. We think that this is a characteristic of reduced cytochromes and that mobility is a medium for molecular recognition in vivo. ; save_ ################################## # Molecular system description # ################################## save_system_cyt_c _Saveframe_category molecular_system _Mol_system_name 'CYTOCHROME C' _Abbreviation_common 'cyt c' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CYTOCHROME C' $cyt_c 'HEME C' $HEC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'electron transfer' 'cell apoptosis' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cyt_c _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome c' _Abbreviation_common 'cyt c' _Molecular_mass 12384 _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; GDVEKGKKIFVQKCAQCHTV EKGGKHKTGPNLHGLFGRKT GQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKM IFAGIKKKTEREDLIAYLKK ATNE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ASP 3 VAL 4 GLU 5 LYS 6 GLY 7 LYS 8 LYS 9 ILE 10 PHE 11 VAL 12 GLN 13 LYS 14 CYS 15 ALA 16 GLN 17 CYS 18 HIS 19 THR 20 VAL 21 GLU 22 LYS 23 GLY 24 GLY 25 LYS 26 HIS 27 LYS 28 THR 29 GLY 30 PRO 31 ASN 32 LEU 33 HIS 34 GLY 35 LEU 36 PHE 37 GLY 38 ARG 39 LYS 40 THR 41 GLY 42 GLN 43 ALA 44 PRO 45 GLY 46 PHE 47 THR 48 TYR 49 THR 50 ASP 51 ALA 52 ASN 53 LYS 54 ASN 55 LYS 56 GLY 57 ILE 58 THR 59 TRP 60 LYS 61 GLU 62 GLU 63 THR 64 LEU 65 MET 66 GLU 67 TYR 68 LEU 69 GLU 70 ASN 71 PRO 72 LYS 73 LYS 74 TYR 75 ILE 76 PRO 77 GLY 78 THR 79 LYS 80 MET 81 ILE 82 PHE 83 ALA 84 GLY 85 ILE 86 LYS 87 LYS 88 LYS 89 THR 90 GLU 91 ARG 92 GLU 93 ASP 94 LEU 95 ILE 96 ALA 97 TYR 98 LEU 99 LYS 100 LYS 101 ALA 102 THR 103 ASN 104 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value SWISS-PROT P68097 'Cytochrome c' 100.00 105 99.04 100.00 1.64e-53 SWISS-PROT P68096 'Cytochrome c' 100.00 105 99.04 100.00 1.64e-53 SWISS-PROT P00004 'Cytochrome c' 100.00 105 100.00 100.00 9.71e-54 REF XP_001498872 'PREDICTED: similar to Cytochrome c, somatic [Equus caballus]' 100.00 105 99.04 100.00 1.64e-53 PRF 610169A 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 GenBank AAB33495 'apocytochrome c [horses, heart, Peptide, 104 aa]' 100.00 104 98.08 98.08 4.15e-52 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 PDB 2GIW 'Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, 40 Structures' 100.00 104 100.00 100.00 1.19e-53 PDB 2FRC 'Cytochrome C (Reduced) From Equus Caballus, Nmr, Minimized Average Structure' 100.00 104 100.00 100.00 1.19e-53 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 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 PDB 1OCD 'Cytochrome C (Oxidized) From Equus Caballus, Nmr, Minimized Average Structure' 100.00 104 100.00 100.00 1.19e-53 PDB 1M60 'Solution Structure Of Zinc-Substituted Cytochrome C' 100.00 104 100.00 100.00 1.19e-53 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 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 PDB 1I5T 'Solution Structure Of Cyanoferricytochrome C' 100.00 104 100.00 100.00 1.19e-53 PDB 1HRC 'High-Resolution Three-Dimensional Structure Of Horse Heart Cytochrome C' 100.00 104 100.00 100.00 1.19e-53 PDB 1GIW 'Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, Minimized Average Structure' 99.04 104 100.00 100.00 4.08e-53 PDB 1FI9 'Solution Structure Of The Imidazole Complex Of Cytochrome C' 100.00 104 100.00 100.00 1.19e-53 PDB 1FI7 'Solution Structure Of The Imidazole Complex Of Cytochrome C' 100.00 104 100.00 100.00 1.19e-53 PDB 1CRC 'Cytochrome C At Low Ionic Strength' 100.00 104 100.00 100.00 1.19e-53 PDB 1AKK 'Solution Structure Of Oxidized Horse Heart Cytochrome C, Nmr, Minimized Average Structure' 100.00 104 100.00 100.00 1.19e-53 BMRB 948 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 947 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 946 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 944 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 673 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 672 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 665 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 645 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 630 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 5830 'Horse cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 5829 'Horse cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 5828 'Horse cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 5827 'Horse cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 5660 'oxidized cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 546 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 545 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 544 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 543 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 5026 'cytochrome C' 100.00 104 100.00 100.00 1.19e-53 BMRB 499 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 4810 'ferric cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 4809 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 4808 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 4805 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 439 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 438 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 437 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 436 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 4189 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 336 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 317 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 316 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 286 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 285 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 274 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 244 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 243 'cytochrome c' 100.00 104 100.00 100.00 1.19e-53 BMRB 2368 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 2367 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 2366 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 224 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 220 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 216 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1789 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1787 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1785 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1783 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1736 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1404 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1171 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1170 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1116 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1114 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1113 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1112 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1111 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1110 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1109 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1108 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1107 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 BMRB 1058 'cytochrome c' 99.04 104 98.06 98.06 4.26e-51 stop_ save_ ############# # Ligands # ############# save_HEC _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEC (HEME C)" _BMRB_code . _PDB_code HEC _Molecular_mass 618.503 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 20 14:17:51 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 0 . ? CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? NA NA N . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? NB NB N . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? NC NC N . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? ND ND N . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? HHA HHA H . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA1 HMA1 H . 0 . ? HMA2 HMA2 H . 0 . ? HMA3 HMA3 H . 0 . ? HAA1 HAA1 H . 0 . ? HAA2 HAA2 H . 0 . ? HBA1 HBA1 H . 0 . ? HBA2 HBA2 H . 0 . ? H2A H2A H . 0 . ? HMB1 HMB1 H . 0 . ? HMB2 HMB2 H . 0 . ? HMB3 HMB3 H . 0 . ? HAB HAB H . 0 . ? HBB1 HBB1 H . 0 . ? HBB2 HBB2 H . 0 . ? HBB3 HBB3 H . 0 . ? HMC1 HMC1 H . 0 . ? HMC2 HMC2 H . 0 . ? HMC3 HMC3 H . 0 . ? HAC HAC H . 0 . ? HBC1 HBC1 H . 0 . ? HBC2 HBC2 H . 0 . ? HBC3 HBC3 H . 0 . ? HMD1 HMD1 H . 0 . ? HMD2 HMD2 H . 0 . ? HMD3 HMD3 H . 0 . ? HAD1 HAD1 H . 0 . ? HAD2 HAD2 H . 0 . ? HBD1 HBD1 H . 0 . ? HBD2 HBD2 H . 0 . ? H2D H2D H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? DOUB CHA C1A ? ? SING CHA C4D ? ? SING CHA HHA ? ? DOUB CHB C4A ? ? SING CHB C1B ? ? SING CHB HHB ? ? DOUB CHC C4B ? ? SING CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING C1A C2A ? ? DOUB C2A C3A ? ? SING C2A CAA ? ? SING C3A C4A ? ? SING C3A CMA ? ? SING CMA HMA1 ? ? SING CMA HMA2 ? ? SING CMA HMA3 ? ? SING CAA CBA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CBA CGA ? ? SING CBA HBA1 ? ? SING CBA HBA2 ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? SING NB C1B ? ? SING NB C4B ? ? DOUB C1B C2B ? ? SING C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? DOUB C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? SING CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING CBB HBB3 ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? DOUB C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? SING CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? SING CBC HBC3 ? ? SING ND C1D ? ? SING ND C4D ? ? DOUB C1D C2D ? ? SING C2D C3D ? ? SING C2D CMD ? ? DOUB C3D C4D ? ? SING C3D CAD ? ? SING CMD HMD1 ? ? SING CMD HMD2 ? ? SING CMD HMD3 ? ? SING CAD CBD ? ? SING CAD HAD1 ? ? SING CAD HAD2 ? ? SING CBD CGD ? ? SING CBD HBD1 ? ? SING CBD HBD2 ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cyt_c Horse 9796 Eukaryota Metazoa Equus caballus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Vendor_name _Details $cyt_c vendor . . . . . Sigma ; formerly type VI prepared without using TCA ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cyt_c 5 mM . $HEC 5 mM . 'phosphate buffer' 50 mM . acetonitrile 30 '% v/v' . H2O 70 '% v/v' . stop_ save_ ############################ # Computer software used # ############################ save_RNMR _Saveframe_category software _Name RNMR _Version 1.0 loop_ _Task collection stop_ _Details 'David Ruben' save_ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 loop_ _Task processing stop_ _Details MSI save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details ; Guntert, P.; Mumenthaler, C.; Wuthrich, K. J. Mol. Biol. 1997, 273, 283-298. ; save_ save_AMBER _Saveframe_category software _Name AMBER _Version 5.0 loop_ _Task refinement stop_ _Details ; (1) Weiner, S. J.; Kollman, P. A.; Case, D. A.; Singh, U. C.; Ghio, C.; Alagona, G.; Salvatore Profeta, J.; Weiner, P. J. Am. Chem. Soc. 1984, 106, 765-784. (2) Weiner, S. J.; Kollman, P. A.; Nguyen, D. T.; Case, D. A. Journal of Computational Chemistry 1986, 7, 230-252. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer 'home built' _Model 'home built' _Field_strength 591.1 _Details 'Home built by Center for Magnetic Resonance at MIT/Harvard.' save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.1 n/a temperature 298 2 K 'ionic strength' 50 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CYTOCHROME C' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLY H H 8.14 . 1 2 . 1 GLY HA2 H 3.90 . 2 3 . 1 GLY HA3 H 3.80 . 2 4 . 2 ASP H H 9.33 . 1 5 . 2 ASP HA H 4.74 . 1 6 . 2 ASP HB2 H 2.82 . 1 7 . 2 ASP HB3 H 2.47 . 1 8 . 3 VAL H H 8.38 . 1 9 . 3 VAL HA H 3.67 . 1 10 . 3 VAL HB H 2.17 . 1 11 . 4 GLU H H 8.10 . 1 12 . 4 GLU HA H 4.07 . 1 13 . 4 GLU HB2 H 2.12 . 1 14 . 4 GLU HB3 H 2.09 . 1 15 . 4 GLU HG2 H 2.32 . 1 16 . 4 GLU HG3 H 2.25 . 1 17 . 5 LYS H H 8.00 . 1 18 . 5 LYS HA H 3.98 . 1 19 . 5 LYS HB2 H 1.80 . 1 20 . 5 LYS HB3 H 1.80 . 1 21 . 5 LYS HG2 H 1.41 . 1 22 . 5 LYS HG3 H 1.53 . 1 23 . 5 LYS HD2 H 1.68 . 2 24 . 5 LYS HE2 H 3.17 . 2 25 . 5 LYS HZ H 6.30 . 1 26 . 6 GLY H H 8.82 . 1 27 . 6 GLY HA2 H 3.53 . 1 28 . 6 GLY HA3 H 4.18 . 1 29 . 7 LYS H H 8.00 . 1 30 . 7 LYS HA H 2.28 . 1 31 . 7 LYS HB2 H 1.80 . 1 32 . 7 LYS HB3 H 1.80 . 1 33 . 7 LYS HG2 H 1.41 . 2 34 . 7 LYS HG3 H 1.53 . 2 35 . 7 LYS HD2 H 0.96 . 2 36 . 8 LYS H H 7.01 . 1 37 . 8 LYS HA H 3.90 . 1 38 . 8 LYS HB2 H 1.93 . 1 39 . 8 LYS HB3 H 1.93 . 1 40 . 8 LYS HG2 H 1.38 . 2 41 . 8 LYS HD2 H 1.72 . 2 42 . 8 LYS HE2 H 2.83 . 2 43 . 9 ILE H H 7.72 . 1 44 . 9 ILE HA H 3.78 . 1 45 . 9 ILE HB H 2.05 . 1 46 . 9 ILE HG2 H 1.30 . 1 47 . 9 ILE HG12 H 1.09 . 1 48 . 9 ILE HG13 H 1.09 . 1 49 . 10 PHE H H 8.68 . 1 50 . 10 PHE HA H 4.02 . 1 51 . 10 PHE HB2 H 2.97 . 1 52 . 10 PHE HB3 H 3.10 . 1 53 . 10 PHE HD1 H 7.02 . 1 54 . 10 PHE HE1 H 6.56 . 1 55 . 10 PHE HZ H 6.66 . 1 56 . 10 PHE HE2 H 6.25 . 1 57 . 10 PHE HD2 H 7.09 . 1 58 . 11 VAL H H 8.73 . 1 59 . 11 VAL HA H 3.54 . 1 60 . 11 VAL HB H 2.17 . 1 61 . 11 VAL HG1 H 0.95 . 1 62 . 11 VAL HG2 H 1.12 . 1 63 . 12 GLN H H 7.93 . 1 64 . 12 GLN HA H 4.19 . 1 65 . 12 GLN HB2 H 2.25 . 1 66 . 12 GLN HB3 H 2.30 . 1 67 . 12 GLN HG2 H 2.65 . 2 68 . 12 GLN HG3 H 2.41 . 2 69 . 13 LYS H H 8.92 . 1 70 . 13 LYS HA H 5.00 . 1 71 . 13 LYS HB2 H 2.47 . 1 72 . 13 LYS HB3 H 2.47 . 1 73 . 13 LYS HG2 H 1.76 . 2 74 . 13 LYS HD2 H 2.25 . 2 75 . 13 LYS HD3 H 2.30 . 2 76 . 13 LYS HE2 H 3.15 . 2 77 . 14 CYS H H 8.27 . 1 78 . 14 CYS HA H 5.34 . 1 79 . 14 CYS HB2 H 1.84 . 1 80 . 14 CYS HB3 H 1.09 . 1 81 . 15 ALA H H 7.40 . 1 82 . 15 ALA HA H 3.92 . 1 83 . 15 ALA HB H 1.38 . 1 84 . 16 GLN H H 8.86 . 1 85 . 16 GLN HA H 3.96 . 1 86 . 16 GLN HB2 H 2.26 . 1 87 . 16 GLN HB3 H 2.03 . 1 88 . 16 GLN HG2 H 2.50 . 1 89 . 16 GLN HG3 H 2.73 . 1 90 . 16 GLN HE21 H 7.15 . 2 91 . 16 GLN HE22 H 7.70 . 2 92 . 17 CYS H H 7.00 . 1 93 . 17 CYS HA H 4.18 . 1 94 . 17 CYS HB2 H 0.59 . 1 95 . 17 CYS HB3 H 1.51 . 1 96 . 18 HIS H H 6.37 . 1 97 . 18 HIS HA H 3.63 . 1 98 . 18 HIS HB2 H 0.74 . 1 99 . 18 HIS HB3 H 1.04 . 1 100 . 18 HIS HD1 H 9.55 . 1 101 . 18 HIS HD2 H 0.08 . 1 102 . 18 HIS HE1 H 0.45 . 1 103 . 19 THR H H 7.82 . 1 104 . 19 THR HA H 4.51 . 1 105 . 19 THR HB H 4.42 . 1 106 . 19 THR HG2 H 1.07 . 1 107 . 20 VAL H H 7.70 . 1 108 . 20 VAL HA H 3.91 . 1 109 . 20 VAL HB H 1.53 . 1 110 . 20 VAL HG1 H 0.40 . 2 111 . 20 VAL HG2 H 0.00 . 2 112 . 21 GLU H H 8.91 . 1 113 . 21 GLU HA H 4.20 . 1 114 . 21 GLU HB2 H 2.27 . 1 115 . 21 GLU HB3 H 2.27 . 1 116 . 22 LYS H H 8.76 . 1 117 . 22 LYS HA H 3.11 . 1 118 . 22 LYS HB2 H 1.29 . 1 119 . 22 LYS HB3 H 1.29 . 1 120 . 22 LYS HG2 H 0.52 . 2 121 . 23 GLY H H 9.02 . 1 122 . 23 GLY HA2 H 3.49 . 2 123 . 23 GLY HA3 H 3.82 . 2 124 . 24 GLY H H 7.73 . 1 125 . 24 GLY HA2 H 3.09 . 2 126 . 24 GLY HA3 H 3.77 . 2 127 . 25 LYS H H 8.10 . 1 128 . 25 LYS HA H 3.87 . 1 129 . 25 LYS HB2 H 1.51 . 2 130 . 25 LYS HB3 H 1.70 . 2 131 . 25 LYS HG2 H 1.31 . 2 132 . 25 LYS HD2 H 1.21 . 2 133 . 25 LYS HE2 H 2.86 . 2 134 . 26 HIS H H 8.26 . 1 135 . 26 HIS HA H 4.45 . 1 136 . 26 HIS HB2 H 2.86 . 1 137 . 26 HIS HB3 H 3.07 . 1 138 . 26 HIS HD1 H 6.97 . 1 139 . 26 HIS HD2 H 7.41 . 1 140 . 27 LYS H H 7.69 . 1 141 . 27 LYS HA H 4.46 . 1 142 . 27 LYS HB2 H 1.08 . 1 143 . 27 LYS HB3 H 1.08 . 1 144 . 27 LYS HG2 H 1.31 . 2 145 . 28 THR H H 7.76 . 1 146 . 28 THR HA H 4.09 . 1 147 . 28 THR HB H 4.20 . 1 148 . 28 THR HG2 H 2.06 . 1 149 . 29 GLY H H 7.40 . 1 150 . 29 GLY HA2 H 3.67 . 2 151 . 29 GLY HA3 H -0.25 . 2 152 . 30 PRO HA H 3.59 . 1 153 . 30 PRO HB2 H 1.22 . 1 154 . 30 PRO HB3 H 0.35 . 1 155 . 30 PRO HG2 H 0.53 . 2 156 . 30 PRO HG3 H 1.35 . 2 157 . 30 PRO HD2 H 1.33 . 2 158 . 30 PRO HD3 H 0.90 . 2 159 . 31 ASN H H 10.48 . 1 160 . 31 ASN HA H 4.06 . 1 161 . 31 ASN HB2 H 1.95 . 2 162 . 31 ASN HB3 H 2.09 . 2 163 . 31 ASN HD21 H 8.05 . 2 164 . 31 ASN HD22 H 7.29 . 2 165 . 32 LEU H H 7.85 . 1 166 . 32 LEU HA H 4.00 . 1 167 . 32 LEU HB2 H 1.08 . 1 168 . 32 LEU HB3 H 1.42 . 1 169 . 32 LEU HG H 0.49 . 1 170 . 32 LEU HD1 H -0.65 . 2 171 . 32 LEU HD2 H -0.81 . 2 172 . 33 HIS H H 7.50 . 1 173 . 33 HIS HA H 3.76 . 1 174 . 33 HIS HB2 H 2.95 . 1 175 . 33 HIS HB3 H 2.95 . 1 176 . 33 HIS HD1 H 6.93 . 1 177 . 33 HIS HD2 H 6.84 . 1 178 . 33 HIS HE1 H 7.60 . 1 179 . 34 GLY H H 8.85 . 1 180 . 34 GLY HA2 H 3.90 . 2 181 . 34 GLY HA3 H 3.70 . 2 182 . 35 LEU H H 7.00 . 1 183 . 35 LEU HA H 3.58 . 1 184 . 35 LEU HB2 H 2.11 . 1 185 . 35 LEU HB3 H 1.51 . 1 186 . 35 LEU HG H 1.25 . 1 187 . 35 LEU HD1 H 0.59 . 2 188 . 36 PHE H H 8.63 . 1 189 . 36 PHE HA H 3.96 . 1 190 . 36 PHE HB2 H 2.82 . 1 191 . 36 PHE HB3 H 3.23 . 1 192 . 36 PHE HD1 H 7.34 . 1 193 . 36 PHE HD2 H 7.34 . 1 194 . 36 PHE HE1 H 6.84 . 1 195 . 36 PHE HE2 H 6.84 . 1 196 . 36 PHE HZ H 7.08 . 1 197 . 37 GLY H H 9.42 . 1 198 . 37 GLY HA2 H 3.48 . 1 199 . 37 GLY HA3 H 4.45 . 1 200 . 38 ARG H H 8.33 . 1 201 . 38 ARG HA H 4.70 . 1 202 . 38 ARG HB2 H 2.07 . 2 203 . 38 ARG HB3 H 2.16 . 2 204 . 38 ARG HG2 H 2.30 . 2 205 . 38 ARG HG3 H 1.89 . 2 206 . 38 ARG HD2 H 3.15 . 2 207 . 38 ARG HE H 7.20 . 1 208 . 38 ARG HH11 H 7.71 . 1 209 . 38 ARG HH12 H 7.71 . 1 210 . 39 LYS H H 7.97 . 1 211 . 39 LYS HA H 4.96 . 1 212 . 39 LYS HB2 H 1.61 . 2 213 . 39 LYS HB3 H 1.75 . 2 214 . 39 LYS HG2 H 1.57 . 2 215 . 39 LYS HG3 H 1.52 . 2 216 . 39 LYS HD2 H 1.43 . 2 217 . 39 LYS HD3 H 1.47 . 2 218 . 39 LYS HE2 H 2.88 . 2 219 . 40 THR H H 7.41 . 1 220 . 40 THR HA H 4.52 . 1 221 . 40 THR HB H 4.47 . 1 222 . 40 THR HG2 H 0.85 . 1 223 . 41 GLY H H 8.41 . 1 224 . 41 GLY HA2 H 3.25 . 2 225 . 41 GLY HA3 H 1.51 . 2 226 . 42 GLN H H 8.50 . 1 227 . 42 GLN HA H 4.49 . 1 228 . 42 GLN HB2 H 1.86 . 1 229 . 42 GLN HB3 H 1.86 . 1 230 . 42 GLN HG2 H 2.29 . 2 231 . 42 GLN HG3 H 2.45 . 2 232 . 43 ALA H H 8.51 . 1 233 . 43 ALA HA H 4.65 . 1 234 . 43 ALA HB H 1.53 . 1 235 . 44 PRO HA H 4.06 . 1 236 . 44 PRO HB2 H 2.04 . 1 237 . 44 PRO HB3 H 2.04 . 1 238 . 44 PRO HG2 H 2.10 . 2 239 . 44 PRO HD2 H 3.81 . 2 240 . 44 PRO HD3 H 4.15 . 2 241 . 45 GLY H H 9.03 . 1 242 . 45 GLY HA2 H 4.30 . 2 243 . 45 GLY HA3 H 3.82 . 2 244 . 46 PHE H H 7.15 . 1 245 . 46 PHE HA H 4.18 . 1 246 . 46 PHE HB2 H 1.06 . 1 247 . 46 PHE HB3 H 2.34 . 1 248 . 46 PHE HD1 H 6.34 . 1 249 . 46 PHE HE1 H 6.88 . 1 250 . 46 PHE HZ H 7.71 . 1 251 . 46 PHE HE2 H 7.41 . 1 252 . 46 PHE HD2 H 4.97 . 1 253 . 47 THR H H 6.96 . 1 254 . 47 THR HA H 4.21 . 1 255 . 47 THR HB H 3.74 . 1 256 . 47 THR HG2 H 1.09 . 1 257 . 48 TYR H H 8.27 . 1 258 . 48 TYR HA H 5.21 . 1 259 . 48 TYR HB2 H 2.79 . 2 260 . 48 TYR HB3 H 3.68 . 2 261 . 48 TYR HD1 H 7.99 . 1 262 . 48 TYR HE1 H 7.09 . 1 263 . 48 TYR HE2 H 7.32 . 1 264 . 48 TYR HD2 H 7.48 . 1 265 . 48 TYR HH H 8.70 . 1 266 . 49 THR H H 10.22 . 1 267 . 49 THR HA H 4.44 . 1 268 . 49 THR HB H 4.71 . 1 269 . 49 THR HG2 H 1.77 . 1 270 . 49 THR HG1 H 8.32 . 1 271 . 50 ASP H H 8.68 . 1 272 . 50 ASP HA H 4.35 . 1 273 . 50 ASP HB2 H 2.57 . 1 274 . 50 ASP HB3 H 2.57 . 1 275 . 51 ALA H H 7.85 . 1 276 . 51 ALA HA H 4.01 . 1 277 . 51 ALA HB H 1.25 . 1 278 . 52 ASN H H 8.35 . 1 279 . 52 ASN HA H 4.22 . 1 280 . 52 ASN HB2 H 3.08 . 1 281 . 52 ASN HB3 H 3.08 . 1 282 . 53 LYS H H 8.00 . 1 283 . 53 LYS HA H 3.54 . 1 284 . 53 LYS HB2 H 1.86 . 1 285 . 53 LYS HB3 H 1.86 . 1 286 . 53 LYS HG2 H 1.40 . 2 287 . 53 LYS HE2 H 3.16 . 2 288 . 54 ASN H H 8.57 . 1 289 . 54 ASN HA H 4.50 . 1 290 . 54 ASN HB2 H 2.75 . 2 291 . 54 ASN HB3 H 2.73 . 2 292 . 55 LYS H H 7.44 . 1 293 . 55 LYS HA H 4.02 . 1 294 . 55 LYS HB2 H 2.08 . 1 295 . 55 LYS HB3 H 1.91 . 1 296 . 55 LYS HG2 H 1.53 . 2 297 . 55 LYS HD2 H 2.30 . 2 298 . 55 LYS HE2 H 3.46 . 2 299 . 56 GLY H H 7.07 . 1 300 . 56 GLY HA2 H 3.80 . 1 301 . 56 GLY HA3 H 3.70 . 1 302 . 57 ILE H H 6.36 . 1 303 . 57 ILE HA H 4.37 . 1 304 . 57 ILE HB H 1.81 . 1 305 . 57 ILE HG2 H 0.73 . 1 306 . 57 ILE HG12 H 0.47 . 2 307 . 57 ILE HG13 H 0.86 . 2 308 . 57 ILE HD1 H -0.62 . 1 309 . 58 THR H H 8.00 . 1 310 . 58 THR HA H 4.18 . 1 311 . 58 THR HB H 3.76 . 1 312 . 58 THR HG2 H 0.96 . 1 313 . 59 TRP H H 8.99 . 1 314 . 59 TRP HA H 4.85 . 1 315 . 59 TRP HB2 H 3.82 . 2 316 . 59 TRP HB3 H 2.48 . 2 317 . 59 TRP HD1 H 6.95 . 1 318 . 59 TRP HE3 H 7.56 . 1 319 . 59 TRP HE1 H 9.98 . 1 320 . 59 TRP HZ3 H 6.65 . 1 321 . 59 TRP HZ2 H 7.01 . 1 322 . 59 TRP HH2 H 5.69 . 1 323 . 60 LYS H H 8.14 . 1 324 . 60 LYS HA H 4.39 . 1 325 . 60 LYS HB2 H 2.42 . 1 326 . 60 LYS HB3 H 2.04 . 1 327 . 60 LYS HG2 H 1.50 . 2 328 . 60 LYS HD2 H 1.68 . 2 329 . 60 LYS HD3 H 1.75 . 2 330 . 60 LYS HE2 H 2.97 . 2 331 . 60 LYS HE3 H 3.09 . 2 332 . 61 GLU H H 10.83 . 1 333 . 61 GLU HA H 3.91 . 1 334 . 61 GLU HB2 H 2.65 . 1 335 . 61 GLU HB3 H 2.65 . 1 336 . 61 GLU HG2 H 2.25 . 2 337 . 62 GLU H H 9.70 . 1 338 . 62 GLU HA H 4.06 . 1 339 . 62 GLU HB2 H 2.12 . 1 340 . 62 GLU HB3 H 2.12 . 1 341 . 62 GLU HG2 H 2.40 . 2 342 . 63 THR H H 7.15 . 1 343 . 63 THR HA H 4.31 . 1 344 . 63 THR HB H 4.48 . 1 345 . 63 THR HG2 H 1.37 . 1 346 . 63 THR HG1 H 5.17 . 1 347 . 64 LEU H H 8.84 . 1 348 . 64 LEU HA H 4.31 . 1 349 . 64 LEU HB2 H 2.04 . 1 350 . 64 LEU HB3 H 2.04 . 1 351 . 64 LEU HG H 1.89 . 1 352 . 64 LEU HD1 H 0.71 . 2 353 . 64 LEU HD2 H 0.45 . 2 354 . 65 MET H H 8.44 . 1 355 . 65 MET HA H 3.95 . 1 356 . 65 MET HB2 H 2.29 . 1 357 . 65 MET HB3 H 2.29 . 1 358 . 65 MET HG2 H 2.74 . 2 359 . 65 MET HG3 H 2.60 . 2 360 . 65 MET HE H 2.07 . 1 361 . 66 GLU H H 6.71 . 1 362 . 66 GLU HA H 4.01 . 1 363 . 66 GLU HB2 H 1.53 . 1 364 . 66 GLU HB3 H 1.72 . 1 365 . 66 GLU HG2 H 1.94 . 2 366 . 66 GLU HG3 H 2.24 . 2 367 . 67 TYR H H 8.17 . 1 368 . 67 TYR HA H 3.59 . 1 369 . 67 TYR HB2 H 3.32 . 1 370 . 67 TYR HB3 H 2.68 . 1 371 . 67 TYR HD1 H 0.73 . 1 372 . 67 TYR HE1 H 0.08 . 1 373 . 67 TYR HE2 H 0.44 . 1 374 . 67 TYR HD2 H 0.92 . 1 375 . 67 TYR HH H 3.07 . 1 376 . 68 LEU H H 8.26 . 1 377 . 68 LEU HA H 3.07 . 1 378 . 68 LEU HB2 H 1.70 . 1 379 . 68 LEU HB3 H 1.70 . 1 380 . 68 LEU HG H 1.86 . 1 381 . 68 LEU HD1 H 0.32 . 2 382 . 68 LEU HD2 H 1.06 . 2 383 . 69 GLU H H 6.84 . 1 384 . 69 GLU HA H 3.93 . 1 385 . 69 GLU HB2 H 1.72 . 2 386 . 69 GLU HB3 H 2.01 . 2 387 . 69 GLU HG2 H 2.07 . 2 388 . 69 GLU HG3 H 2.19 . 2 389 . 70 ASN H H 6.17 . 1 390 . 70 ASN HA H 4.22 . 1 391 . 70 ASN HB2 H 2.80 . 2 392 . 70 ASN HB3 H 2.78 . 2 393 . 71 PRO HA H 3.94 . 1 394 . 71 PRO HB2 H 1.40 . 1 395 . 71 PRO HB3 H 0.93 . 1 396 . 71 PRO HG2 H -0.01 . 2 397 . 71 PRO HG3 H 0.41 . 2 398 . 71 PRO HD2 H 3.01 . 2 399 . 71 PRO HD3 H 2.68 . 2 400 . 72 LYS H H 7.61 . 1 401 . 72 LYS HA H 3.76 . 1 402 . 72 LYS HB2 H 1.51 . 1 403 . 72 LYS HB3 H 1.66 . 1 404 . 72 LYS HG2 H 1.24 . 2 405 . 72 LYS HD2 H 1.12 . 2 406 . 72 LYS HE2 H 2.79 . 2 407 . 73 LYS H H 6.93 . 1 408 . 73 LYS HA H 3.93 . 1 409 . 73 LYS HB2 H 1.62 . 1 410 . 73 LYS HB3 H 1.53 . 1 411 . 73 LYS HG2 H 1.35 . 2 412 . 73 LYS HE2 H 2.87 . 2 413 . 74 TYR H H 7.30 . 1 414 . 74 TYR HA H 4.36 . 1 415 . 74 TYR HB2 H 3.08 . 2 416 . 74 TYR HB3 H 3.21 . 2 417 . 74 TYR HD1 H 7.19 . 1 418 . 74 TYR HE1 H 6.59 . 1 419 . 75 ILE H H 8.26 . 1 420 . 75 ILE HA H 4.07 . 1 421 . 75 ILE HB H 1.89 . 1 422 . 75 ILE HG2 H 0.61 . 1 423 . 75 ILE HG12 H 1.50 . 2 424 . 75 ILE HG13 H 1.80 . 2 425 . 75 ILE HD1 H 1.03 . 1 426 . 76 PRO HA H 4.52 . 1 427 . 76 PRO HB2 H 2.19 . 2 428 . 76 PRO HB3 H 1.74 . 2 429 . 76 PRO HG2 H 1.92 . 2 430 . 76 PRO HD2 H 3.35 . 1 431 . 76 PRO HD3 H 3.16 . 1 432 . 77 GLY H H 8.52 . 1 433 . 77 GLY HA2 H 4.17 . 2 434 . 77 GLY HA3 H 3.57 . 2 435 . 78 THR H H 8.08 . 1 436 . 78 THR HA H 4.48 . 1 437 . 78 THR HB H 4.24 . 1 438 . 78 THR HG2 H 0.77 . 1 439 . 78 THR HG1 H 8.38 . 1 440 . 79 LYS H H 7.87 . 1 441 . 79 LYS HA H 4.62 . 1 442 . 79 LYS HB2 H 1.96 . 1 443 . 79 LYS HB3 H 2.27 . 1 444 . 79 LYS HG2 H 1.77 . 2 445 . 79 LYS HG3 H 2.10 . 2 446 . 79 LYS HD2 H 1.90 . 2 447 . 79 LYS HD3 H 1.70 . 2 448 . 79 LYS HE2 H 3.55 . 2 449 . 80 MET H H 6.99 . 1 450 . 80 MET HA H 3.07 . 1 451 . 80 MET HB2 H -2.61 . 1 452 . 80 MET HB3 H -0.27 . 1 453 . 80 MET HG2 H -1.92 . 1 454 . 80 MET HG3 H -3.80 . 1 455 . 80 MET HE H -3.33 . 1 456 . 81 ILE H H 7.61 . 1 457 . 81 ILE HA H 3.55 . 1 458 . 81 ILE HB H 2.05 . 1 459 . 81 ILE HG2 H 1.11 . 1 460 . 82 PHE H H 6.40 . 1 461 . 82 PHE HA H 4.25 . 1 462 . 82 PHE HB2 H 0.54 . 1 463 . 82 PHE HB3 H 2.06 . 1 464 . 82 PHE HD1 H 6.66 . 1 465 . 82 PHE HE1 H 7.36 . 1 466 . 82 PHE HZ H 7.19 . 1 467 . 83 ALA H H 8.14 . 1 468 . 83 ALA HA H 3.58 . 1 469 . 83 ALA HB H 1.07 . 1 470 . 84 GLY H H 8.75 . 1 471 . 84 GLY HA2 H 4.22 . 2 472 . 84 GLY HA3 H 2.94 . 2 473 . 85 ILE H H 8.42 . 1 474 . 85 ILE HA H 4.23 . 1 475 . 85 ILE HB H 1.47 . 1 476 . 85 ILE HG2 H 1.05 . 1 477 . 85 ILE HG12 H 1.28 . 2 478 . 85 ILE HG13 H 1.70 . 2 479 . 85 ILE HD1 H 1.01 . 1 480 . 86 LYS H H 8.49 . 1 481 . 86 LYS HA H 4.06 . 1 482 . 86 LYS HB2 H 1.88 . 1 483 . 86 LYS HB3 H 1.88 . 1 484 . 86 LYS HG2 H 1.52 . 2 485 . 86 LYS HD2 H 1.31 . 2 486 . 87 LYS H H 8.26 . 1 487 . 87 LYS HA H 4.32 . 1 488 . 87 LYS HB2 H 1.61 . 2 489 . 87 LYS HB3 H 1.72 . 2 490 . 87 LYS HG2 H 1.86 . 2 491 . 87 LYS HE2 H 3.07 . 2 492 . 88 LYS H H 9.03 . 1 493 . 88 LYS HA H 3.69 . 1 494 . 88 LYS HB2 H 1.88 . 1 495 . 88 LYS HB3 H 1.88 . 1 496 . 88 LYS HG2 H 1.63 . 2 497 . 88 LYS HG3 H 1.31 . 2 498 . 89 THR H H 8.28 . 1 499 . 89 THR HA H 4.06 . 1 500 . 89 THR HB H 4.23 . 1 501 . 89 THR HG2 H 1.33 . 1 502 . 90 GLU H H 6.33 . 1 503 . 90 GLU HA H 4.25 . 1 504 . 90 GLU HB2 H 2.01 . 1 505 . 90 GLU HB3 H 2.05 . 1 506 . 90 GLU HG2 H 2.34 . 2 507 . 91 ARG H H 7.44 . 1 508 . 91 ARG HA H 3.86 . 1 509 . 91 ARG HB2 H 2.16 . 1 510 . 91 ARG HB3 H 2.16 . 1 511 . 91 ARG HD2 H 3.26 . 2 512 . 91 ARG HD3 H 3.31 . 2 513 . 91 ARG HE H 6.23 . 1 514 . 91 ARG HH11 H 6.82 . 1 515 . 91 ARG HH12 H 6.82 . 1 516 . 92 GLU H H 8.49 . 1 517 . 92 GLU HA H 3.87 . 1 518 . 92 GLU HB2 H 2.45 . 1 519 . 92 GLU HB3 H 2.45 . 1 520 . 92 GLU HG2 H 2.29 . 2 521 . 92 GLU HG3 H 2.17 . 2 522 . 93 ASP H H 8.47 . 1 523 . 93 ASP HA H 4.24 . 1 524 . 93 ASP HB2 H 2.74 . 2 525 . 93 ASP HB3 H 2.66 . 2 526 . 94 LEU H H 8.31 . 1 527 . 94 LEU HA H 4.28 . 1 528 . 94 LEU HB2 H 2.28 . 1 529 . 94 LEU HB3 H 2.28 . 1 530 . 94 LEU HG H 1.86 . 1 531 . 94 LEU HD1 H 1.52 . 1 532 . 94 LEU HD2 H 1.45 . 1 533 . 95 ILE H H 8.97 . 1 534 . 95 ILE HA H 3.69 . 1 535 . 95 ILE HB H 2.09 . 1 536 . 95 ILE HG2 H 1.17 . 1 537 . 95 ILE HG12 H 2.00 . 2 538 . 95 ILE HD1 H 0.94 . 1 539 . 96 ALA H H 8.20 . 1 540 . 96 ALA HA H 4.07 . 1 541 . 96 ALA HB H 1.42 . 1 542 . 97 TYR H H 8.13 . 1 543 . 97 TYR HA H 4.23 . 1 544 . 97 TYR HB2 H 3.10 . 1 545 . 97 TYR HB3 H 3.65 . 1 546 . 97 TYR HD1 H 6.55 . 1 547 . 97 TYR HE1 H 5.50 . 1 548 . 97 TYR HE2 H 6.68 . 1 549 . 97 TYR HD2 H 7.09 . 1 550 . 98 LEU H H 9.11 . 1 551 . 98 LEU HA H 3.42 . 1 552 . 98 LEU HB2 H 2.30 . 1 553 . 98 LEU HB3 H 2.30 . 1 554 . 98 LEU HG H 2.19 . 1 555 . 98 LEU HD1 H 1.07 . 1 556 . 98 LEU HD2 H 0.66 . 1 557 . 99 LYS H H 8.94 . 1 558 . 99 LYS HA H 2.64 . 1 559 . 99 LYS HB2 H 1.29 . 1 560 . 99 LYS HB3 H 1.55 . 1 561 . 99 LYS HG2 H 0.73 . 2 562 . 99 LYS HG3 H 0.34 . 2 563 . 99 LYS HE2 H 2.45 . 2 564 . 100 LYS H H 6.84 . 1 565 . 100 LYS HA H 4.05 . 1 566 . 100 LYS HB2 H 1.73 . 1 567 . 100 LYS HB3 H 1.73 . 1 568 . 100 LYS HG2 H 1.20 . 2 569 . 100 LYS HG3 H 1.65 . 2 570 . 100 LYS HD2 H 1.33 . 2 571 . 100 LYS HE2 H 2.84 . 2 572 . 101 ALA H H 8.60 . 1 573 . 101 ALA HA H 3.84 . 1 574 . 101 ALA HB H 0.54 . 1 575 . 102 THR H H 7.89 . 1 576 . 102 THR HA H 4.08 . 1 577 . 102 THR HB H 4.49 . 1 578 . 102 THR HG2 H 0.98 . 1 579 . 103 ASN H H 7.02 . 1 580 . 103 ASN HA H 4.83 . 1 581 . 103 ASN HB2 H 2.50 . 2 582 . 103 ASN HB3 H 2.81 . 2 583 . 103 ASN HD21 H 7.92 . 2 584 . 103 ASN HD22 H 6.57 . 2 585 . 104 GLU H H 7.22 . 1 586 . 104 GLU HA H 4.21 . 1 587 . 104 GLU HB2 H 1.92 . 2 588 . 104 GLU HB3 H 1.97 . 2 589 . 104 GLU HG2 H 2.27 . 2 stop_ save_ ######################## # Coupling constants # ######################## save_J-values_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 591.1 _Mol_system_component_name 'CYTOCHROME C' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 2 ASP HA 2 ASP H 5.0 . . 1.5 2 3JHNHA 3 VAL HA 3 VAL H 4.0 . . 1.5 3 3JHNHA 4 GLU HA 4 GLU H 4.0 . . 1.5 4 3JHNHA 5 LYS HA 5 LYS H 4.0 . . 1.5 5 3JHNHA 7 LYS HA 7 LYS H 4.0 . . 1.5 6 3JHNHA 8 LYS HA 8 LYS H 4.0 . . 1.5 7 3JHNHA 10 PHE HA 10 PHE H 4.4 . . 1.5 8 3JHNHA 11 VAL HA 11 VAL H 4.0 . . 1.5 9 3JHNHA 15 ALA HA 15 ALA H 4.5 . . 1.5 10 3JHNHA 17 CYS HA 17 CYS H 6.5 . . 1.5 11 3JHNHA 18 HIS HA 18 HIS H 6.9 . . 1.5 12 3JHNHA 20 VAL HA 20 VAL H 7.1 . . 1.5 13 3JHNHA 22 LYS HA 22 LYS H 5.5 . . 1.5 14 3JHNHA 25 LYS HA 25 LYS H 4.5 . . 1.5 15 3JHNHA 26 HIS HA 26 HIS H 6.0 . . 1.5 16 3JHNHA 27 LYS HA 27 LYS H 7.0 . . 1.5 17 3JHNHA 28 THR HA 28 THR H 5.5 . . 1.5 18 3JHNHA 31 ASN HA 31 ASN H 7.0 . . 1.5 19 3JHNHA 32 LEU HA 32 LEU H 6.5 . . 1.5 20 3JHNHA 33 HIS HA 33 HIS H 5.0 . . 1.5 21 3JHNHA 36 PHE HA 36 PHE H 6.0 . . 1.5 22 3JHNHA 38 ARG HA 38 ARG H 6.0 . . 1.5 23 3JHNHA 39 LYS HA 39 LYS H 6.0 . . 1.5 24 3JHNHA 42 GLN HA 42 GLN H 7.0 . . 1.5 25 3JHNHA 43 ALA HA 43 ALA H 4.0 . . 1.5 26 3JHNHA 46 PHE HA 46 PHE H 7.0 . . 1.5 27 3JHNHA 47 THR HA 47 THR H 6.0 . . 1.5 28 3JHNHA 48 TYR HA 48 TYR H 9.0 . . 1.5 29 3JHNHA 49 THR HA 49 THR H 6.5 . . 1.5 30 3JHNHA 50 ASP HA 50 ASP H 5.0 . . 1.5 31 3JHNHA 52 ASN HA 52 ASN H 4.0 . . 1.5 32 3JHNHA 53 LYS HA 53 LYS H 4.0 . . 1.5 33 3JHNHA 54 ASN HA 54 ASN H 4.0 . . 1.5 34 3JHNHA 55 LYS HA 55 LYS H 5.0 . . 1.5 35 3JHNHA 57 ILE HA 57 ILE H 3.5 . . 1.5 36 3JHNHA 58 THR HA 58 THR H 5.5 . . 1.5 37 3JHNHA 59 TRP HA 59 TRP H 5.0 . . 1.5 38 3JHNHA 60 LYS HA 60 LYS H 5.0 . . 1.5 39 3JHNHA 61 GLU HA 61 GLU H 4.5 . . 1.5 40 3JHNHA 62 GLU HA 62 GLU H 4.0 . . 1.5 41 3JHNHA 63 THR HA 63 THR H 5.0 . . 1.5 42 3JHNHA 64 LEU HA 64 LEU H 4.0 . . 1.5 43 3JHNHA 65 MET HA 65 MET H 4.0 . . 1.5 44 3JHNHA 66 GLU HA 66 GLU H 4.0 . . 1.5 45 3JHNHA 67 TYR HA 67 TYR H 4.0 . . 1.5 46 3JHNHA 68 LEU HA 68 LEU H 4.0 . . 1.5 47 3JHNHA 69 GLU HA 69 GLU H 5.5 . . 1.5 48 3JHNHA 70 ASN HA 70 ASN H 4.0 . . 1.5 49 3JHNHA 72 LYS HA 72 LYS H 4.0 . . 1.5 50 3JHNHA 73 LYS HA 73 LYS H 5.0 . . 1.5 51 3JHNHA 74 TYR HA 74 TYR H 4.0 . . 1.5 52 3JHNHA 79 LYS HA 79 LYS H 6.5 . . 1.5 53 3JHNHA 80 MET HA 80 MET H 6.0 . . 1.5 54 3JHAHB 80 MET HA 80 MET HB2 8.2 . . 2.0 55 3JHAHB 80 MET HA 80 MET HB3 12.9 . . 2.0 56 3JHNHA 81 ILE HA 81 ILE H 6.0 . . 1.5 57 3JHNHA 82 PHE HA 82 PHE H 4.9 . . 1.5 58 3JHNHA 83 ALA HA 83 ALA H 5.0 . . 1.5 59 3JHNHA 85 ILE HA 85 ILE H 7.0 . . 1.5 60 3JHNHA 87 LYS HA 87 LYS H 5.0 . . 1.5 61 3JHNHA 88 LYS HA 88 LYS H 5.0 . . 1.5 62 3JHNHA 90 GLU HA 90 GLU H 4.0 . . 1.5 63 3JHNHA 91 ARG HA 91 ARG H 4.0 . . 1.5 64 3JHNHA 92 GLU HA 92 GLU H 4.5 . . 1.5 65 3JHNHA 93 ASP HA 93 ASP H 4.0 . . 1.5 66 3JHNHA 94 LEU HA 94 LEU H 4.0 . . 1.5 67 3JHNHA 95 ILE HA 95 ILE H 4.0 . . 1.5 68 3JHNHA 97 TYR HA 97 TYR H 4.0 . . 1.5 69 3JHNHA 98 LEU HA 98 LEU H 4.0 . . 1.5 70 3JHNHA 99 LYS HA 99 LYS H 5.0 . . 1.5 71 3JHNHA 102 THR HA 102 THR H 4.0 . . 1.5 72 3JHNHA 103 ASN HA 103 ASN H 5.9 . . 1.5 73 3JHNHA 104 GLU HA 104 GLU H 4.9 . . 1.5 stop_ save_