data_4744 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical Shift Assignments for fully oxidized cytochrome c7 from Desulfuromonas acetoxidans ; _BMRB_accession_number 4744 _BMRB_flat_file_name bmr4744.str _Entry_type original _Submission_date 2000-05-22 _Accession_date 2000-05-23 _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 Assfalg M. . . 2 Banci L. . . 3 Bertini I. . . 4 Bruschi M. . . 5 Turano P. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 4 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 376 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-07-13 original author . stop_ _Original_release_date 2000-07-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98430963 _PubMed_ID 9760163 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Assfalg M. . . 2 Banci L. . . 3 Bertini I. . . 4 Bruschi M. . . 5 Turano P. . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 256 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 261 _Page_last 270 _Year 1998 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full . _Citation_title '800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9760163 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Assfalg M. . . 2 Banci L. . . 3 Bertini I. . . 4 Bruschi M. . . 5 Turano P. . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full 'European journal of biochemistry / FEBS' _Journal_volume 256 _Journal_issue 2 _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 261 _Page_last 270 _Year 1998 _Details ; The solution structure of Desulfuromonas acetoxidans cytochrome c7 has been refined by using 1H-NMR spectra recorded at 800 MHz and by using pseudocontact shifts in the final energy minimization procedure. The protein, composed of 68 amino acids, contains three paramagnetic heme moieties, each with one unpaired electron. The largely distributed paramagnetism broadens the lines in several protein parts. The structure is now relatively well resolved all over the backbone by the use of 1315 meaningful NOEs and 90 pseudocontact shifts. The statistical analysis of the structure indicates its satisfactory quality. The protein-fold is quite similar to that of the analogous four-heme cytochromes c3 for those parts which can be considered homologous. The solvent accessibility and the electrostatic potential surfaces surrounding the three hemes have been analyzed in terms of their reduction potentials. The resulting magnetic susceptibility anisotropy data obtained from pseudocontact shifts are analyzed in terms of structural data. ; save_ ################################## # Molecular system description # ################################## save_system_cyt_c7 _Saveframe_category molecular_system _Mol_system_name 'cytochrome c7' _Abbreviation_common 'cyt c7, cyt c551.1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytochrome c7' $cyt_c7 'heme c, 1' $HEC 'heme c, 2' $HEC 'heme c, 3' $HEC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all other bound' loop_ _Biological_function 'electron transfer' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cyt_c7 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome c7' _Abbreviation_common 'cyt c7' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 68 _Mol_residue_sequence ; ADVVTYENKKGNVTFDHKAH AEKLGCDACHEGTPAKIAID KKSAHKDACKTCHKSNNGPT KCGGCHIK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 VAL 4 VAL 5 THR 6 TYR 7 GLU 8 ASN 9 LYS 10 LYS 11 GLY 12 ASN 13 VAL 14 THR 15 PHE 16 ASP 17 HIS 18 LYS 19 ALA 20 HIS 21 ALA 22 GLU 23 LYS 24 LEU 25 GLY 26 CYS 27 ASP 28 ALA 29 CYS 30 HIS 31 GLU 32 GLY 33 THR 34 PRO 35 ALA 36 LYS 37 ILE 38 ALA 39 ILE 40 ASP 41 LYS 42 LYS 43 SER 44 ALA 45 HIS 46 LYS 47 ASP 48 ALA 49 CYS 50 LYS 51 THR 52 CYS 53 HIS 54 LYS 55 SER 56 ASN 57 ASN 58 GLY 59 PRO 60 THR 61 LYS 62 CYS 63 GLY 64 GLY 65 CYS 66 HIS 67 ILE 68 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 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 BMRB 4743 "CYTOCHROME C7" 100.00 68 100.00 100.00 4.27e-39 PDB 1EHJ "A Proton-Nmr Investigation Of The Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans" 98.53 68 100.00 100.00 1.47e-38 PDB 1F22 "A Proton-Nmr Investigation Of The Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between The Reduced A" 100.00 68 100.00 100.00 4.27e-39 PDB 1HH5 "Cytochrome C7 From Desulfuromonas Acetoxidans" 100.00 68 100.00 100.00 4.27e-39 PDB 1KWJ "Solution Structure Determination Of The Fully Oxidized Double Mutant K9-10a Cytochrome C7 From Desulfuromonas Acetoxidans, Mini" 98.53 68 97.01 97.01 3.23e-37 PDB 1L3O "Solution Structure Determination Of The Fully Oxidized Double Mutant K9-10a Cytochrome C7 From Desulfuromonas Acetoxidans, Ense" 100.00 68 97.06 97.06 8.86e-38 PDB 1LM2 "Nmr Structural Characterization Of The Reduction Of Chromium(Vi) To Chromium(Iii) By Cytochrome C7" 98.53 68 100.00 100.00 1.47e-38 PDB 1NEW "Cytochrome C551.5, Nmr" 98.53 68 100.00 100.00 1.47e-38 GB AAC46253 "cytochrome c7 [Desulfuromonas acetoxidans]" 100.00 68 100.00 100.00 4.27e-39 PRF 711089A "cytochrome c551.5" 100.00 68 100.00 100.00 4.27e-39 SP P00137 "RecName: Full=Cytochrome c3; AltName: Full=Cytochrome c551.5; AltName: Full=Cytochrome c7" 100.00 68 100.00 100.00 4.27e-39 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 Tue Jul 19 11:12:47 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_c7 bacteria 891 Eubacteria . Desulfuromonas acetoxidans 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 $cyt_c7 'purified from the natural source' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $cyt_c7 . mM 2 3 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details '1H NOESY, 1H TOCSY, 1H COSY' save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 n/a temperature 298 1 K pressure 1 . atm 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'cytochrome c7' _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 ALA HA H 5.411 . . 2 . 1 ALA HB H 2.678 . . 3 . 2 ASP H H 10.382 . . 4 . 2 ASP HA H 7.844 . . 5 . 2 ASP HB2 H 4.537 . . 6 . 2 ASP HB3 H 4.086 . . 7 . 3 VAL H H 9.34 . . 8 . 3 VAL HA H 6.548 . . 9 . 3 VAL HB H 2.852 . . 10 . 3 VAL HG2 H 1.941 . . 11 . 3 VAL HG1 H 1.587 . . 12 . 4 VAL H H 10.333 . . 13 . 4 VAL HA H 4.824 . . 14 . 4 VAL HB H 2.643 . . 15 . 4 VAL HG2 H 2.039 . . 16 . 4 VAL HG1 H 0.519 . . 17 . 5 THR H H 8.964 . . 18 . 5 THR HA H 5.389 . . 19 . 5 THR HB H 4.299 . . 20 . 5 THR HG2 H 1.59 . . 21 . 6 TYR HD1 H 5.741 . . 22 . 6 TYR HE1 H 6.545 . . 23 . 6 TYR H H 9.977 . . 24 . 6 TYR HA H 4.732 . . 25 . 6 TYR HB3 H 3.22 . . 26 . 6 TYR HB2 H 3.245 . . 27 . 7 GLU H H 9.156 . . 28 . 7 GLU HA H 5.19 . . 29 . 7 GLU HB2 H 2.228 . . 30 . 7 GLU HB3 H 2.285 . . 31 . 7 GLU HG2 H 2.621 . . 32 . 7 GLU HG3 H 2.46 . . 33 . 8 ASN HD22 H 11.432 . . 34 . 8 ASN HD21 H 8.491 . . 35 . 8 ASN H H 9.103 . . 36 . 8 ASN HA H 5.026 . . 37 . 8 ASN HB2 H 3.098 . . 38 . 8 ASN HB3 H 2.384 . . 39 . 9 LYS H H 9.211 . . 40 . 9 LYS HA H 4.327 . . 41 . 9 LYS HB2 H 1.19 . . 42 . 9 LYS HB3 H 1.283 . . 43 . 9 LYS HG3 H 2.633 . . 44 . 9 LYS HD2 H 1.579 . . 45 . 9 LYS HD3 H 1.579 . . 46 . 10 LYS H H 8.595 . . 47 . 10 LYS HG2 H 0.11 . . 48 . 10 LYS HE2 H 4.402 . . 49 . 10 LYS HA H 4.761 . . 50 . 10 LYS HB2 H 1.013 . . 51 . 10 LYS HD2 H 3.364 . . 52 . 11 GLY H H 9.765 . . 53 . 11 GLY HA2 H 5.696 . . 54 . 11 GLY HA3 H 7.31 . . 55 . 12 ASN HD22 H 7.709 . . 56 . 12 ASN HD21 H 8.319 . . 57 . 12 ASN H H 10.891 . . 58 . 12 ASN HA H 6.871 . . 59 . 12 ASN HB3 H 3.477 . . 60 . 12 ASN HB2 H 4.208 . . 61 . 13 VAL H H 9.866 . . 62 . 13 VAL HA H 6.679 . . 63 . 13 VAL HG1 H 3.434 . . 64 . 13 VAL HB H 6.035 . . 65 . 13 VAL HG2 H 1.003 . . 66 . 14 THR H H 10.363 . . 67 . 14 THR HA H 5.117 . . 68 . 14 THR HB H 4.215 . . 69 . 14 THR HG2 H 1.485 . . 70 . 15 PHE H H 10.229 . . 71 . 15 PHE HA H 5.376 . . 72 . 15 PHE HB3 H 3.052 . . 73 . 15 PHE HB2 H 3.83 . . 74 . 15 PHE HD1 H 5.732 . . 75 . 15 PHE HE1 H 6.545 . . 76 . 15 PHE HZ H 6.569 . . 77 . 16 ASP H H 11.594 . . 78 . 16 ASP HA H 6.799 . . 79 . 16 ASP HB2 H 5.068 . . 80 . 16 ASP HB3 H 3.305 . . 81 . 17 HIS H H 11.517 . . 82 . 17 HIS HA H 8.56 . . 83 . 17 HIS HB2 H 12.443 . . 84 . 17 HIS HB3 H 12.762 . . 85 . 18 LYS H H 12.464 . . 86 . 18 LYS HA H 6.534 . . 87 . 18 LYS HB2 H 4.054 . . 88 . 18 LYS HB3 H 3.934 . . 89 . 18 LYS HE2 H 3.583 . . 90 . 18 LYS HE3 H 3.583 . . 91 . 18 LYS HD2 H 2.604 . . 92 . 18 LYS HD3 H 2.604 . . 93 . 18 LYS HG3 H 2.484 . . 94 . 18 LYS HG2 H 2.347 . . 95 . 19 ALA H H 10.866 . . 96 . 19 ALA HA H 5.375 . . 97 . 19 ALA HB H 2.732 . . 98 . 20 HIS H H 12.046 . . 99 . 20 HIS HA H 7.842 . . 100 . 20 HIS HB3 H 7.113 . . 101 . 20 HIS HB2 H 11.418 . . 102 . 21 ALA H H 10.619 . . 103 . 21 ALA HA H 2.753 . . 104 . 21 ALA HB H 0.145 . . 105 . 22 GLU H H 9.087 . . 106 . 22 GLU HA H 3.941 . . 107 . 22 GLU HB2 H 2.658 . . 108 . 22 GLU HG3 H 2.497 . . 109 . 22 GLU HG2 H 2.876 . . 110 . 22 GLU HB3 H 2.364 . . 111 . 23 LYS H H 8.118 . . 112 . 23 LYS HA H 4.441 . . 113 . 23 LYS HD2 H 3.101 . . 114 . 23 LYS HB2 H 2.667 . . 115 . 23 LYS HB3 H 2.515 . . 116 . 23 LYS HG2 H 1.84 . . 117 . 23 LYS HD3 H 2.156 . . 118 . 23 LYS HG3 H 2.086 . . 119 . 24 LEU H H 8.286 . . 120 . 24 LEU HA H 4.325 . . 121 . 24 LEU HB2 H 1.391 . . 122 . 24 LEU HB3 H 0.897 . . 123 . 24 LEU HG H 2.168 . . 124 . 24 LEU HD1 H 0.71 . . 125 . 24 LEU HD2 H 0.362 . . 126 . 25 GLY H H 7.553 . . 127 . 25 GLY HA2 H 3.283 . . 128 . 25 GLY HA3 H 3.949 . . 129 . 26 CYS H H 7.332 . . 130 . 26 CYS HA H 1.835 . . 131 . 26 CYS HB2 H 2.43 . . 132 . 26 CYS HB3 H 1.808 . . 133 . 27 ASP H H 8.438 . . 134 . 27 ASP HA H 5.826 . . 135 . 27 ASP HB2 H 3.009 . . 136 . 27 ASP HB3 H 3.009 . . 137 . 28 ALA H H 7.269 . . 138 . 28 ALA HA H 3.843 . . 139 . 28 ALA HB H 0.687 . . 140 . 29 CYS H H 7.424 . . 141 . 29 CYS HA H 4.586 . . 142 . 29 CYS HB2 H 3.219 . . 143 . 29 CYS HB3 H 1.061 . . 144 . 30 HIS H H 11.649 . . 145 . 30 HIS HA H 9.636 . . 146 . 30 HIS HB3 H 14.117 . . 147 . 30 HIS HB2 H 9.807 . . 148 . 31 GLU H H 10.865 . . 149 . 31 GLU HA H 5.548 . . 150 . 31 GLU HB2 H 2.891 . . 151 . 31 GLU HB3 H 2.827 . . 152 . 32 GLY H H 9.677 . . 153 . 32 GLY HA2 H 4.443 . . 154 . 32 GLY HA3 H 4.776 . . 155 . 33 THR H H 9.148 . . 156 . 33 THR HB H 4.403 . . 157 . 33 THR HG2 H 1.342 . . 158 . 33 THR HA H 4.772 . . 159 . 34 PRO HD3 H 0.852 . . 160 . 34 PRO HA H 8.365 . . 161 . 34 PRO HB2 H 4.837 . . 162 . 34 PRO HB3 H 4.775 . . 163 . 34 PRO HG2 H 3.441 . . 164 . 34 PRO HG3 H 3.39 . . 165 . 34 PRO HD2 H 0.171 . . 166 . 35 ALA H H 11.433 . . 167 . 35 ALA HA H 4.17 . . 168 . 35 ALA HB H 1.796 . . 169 . 36 LYS H H 7.513 . . 170 . 36 LYS HA H 0.265 . . 171 . 36 LYS HB3 H 0.63 . . 172 . 36 LYS HG2 H 0.735 . . 173 . 36 LYS HG3 H 0.819 . . 174 . 36 LYS HE2 H 2.306 . . 175 . 36 LYS HE3 H 2.253 . . 176 . 36 LYS HD2 H 0.862 . . 177 . 36 LYS HD3 H 0.567 . . 178 . 37 ILE H H 1.917 . . 179 . 37 ILE HA H 3.099 . . 180 . 37 ILE HG12 H 0.95 . . 181 . 37 ILE HG13 H 0.867 . . 182 . 38 ALA H H 7.663 . . 183 . 38 ALA HA H 3.068 . . 184 . 38 ALA HB H 0.669 . . 185 . 39 ILE H H 6.978 . . 186 . 39 ILE HA H 2.764 . . 187 . 39 ILE HB H 0.426 . . 188 . 40 ASP H H 6.663 . . 189 . 40 ASP HA H 3.376 . . 190 . 40 ASP HB2 H 2.289 . . 191 . 40 ASP HB3 H 2.094 . . 192 . 41 LYS H H 7.359 . . 193 . 41 LYS HA H 0.905 . . 194 . 41 LYS HB2 H 1.225 . . 195 . 41 LYS HB3 H 1.225 . . 196 . 42 LYS HD3 H 2.475 . . 197 . 42 LYS HE2 H 3.698 . . 198 . 42 LYS H H 7.933 . . 199 . 42 LYS HA H 6.235 . . 200 . 42 LYS HD2 H 3.375 . . 201 . 42 LYS HB2 H 2.449 . . 202 . 42 LYS HB3 H 2.449 . . 203 . 42 LYS HG2 H 2.211 . . 204 . 42 LYS HG3 H 2.211 . . 205 . 43 SER H H 8.629 . . 206 . 43 SER HA H 4.602 . . 207 . 43 SER HB2 H 3.658 . . 208 . 43 SER HB3 H 3.334 . . 209 . 44 ALA H H 8.758 . . 210 . 44 ALA HA H 2.308 . . 211 . 45 HIS H H 11.412 . . 212 . 45 HIS HA H 8.317 . . 213 . 45 HIS HB2 H 16.304 . . 214 . 45 HIS HB3 H 19.776 . . 215 . 46 LYS H H 8.833 . . 216 . 46 LYS HG2 H 2.473 . . 217 . 46 LYS HG3 H 2.314 . . 218 . 46 LYS HA H 5.215 . . 219 . 46 LYS HD2 H 3.723 . . 220 . 46 LYS HB2 H 2.892 . . 221 . 46 LYS HB3 H 2.68 . . 222 . 47 ASP H H 8.339 . . 223 . 47 ASP HA H 3.816 . . 224 . 47 ASP HB2 H 2.357 . . 225 . 47 ASP HB3 H 2.294 . . 226 . 48 ALA H H 7.706 . . 227 . 48 ALA HA H 2.251 . . 228 . 49 CYS H H 7.707 . . 229 . 49 CYS HA H 4.928 . . 230 . 49 CYS HB2 H 3.053 . . 231 . 49 CYS HB3 H 3.821 . . 232 . 50 LYS H H 7.042 . . 233 . 50 LYS HA H 4.977 . . 234 . 50 LYS HB2 H 1.91 . . 235 . 50 LYS HB3 H 2.597 . . 236 . 50 LYS HG3 H 1.463 . . 237 . 50 LYS HD2 H 1.797 . . 238 . 50 LYS HG2 H 2.304 . . 239 . 50 LYS HD3 H 1.718 . . 240 . 51 THR H H 8.663 . . 241 . 51 THR HA H 3.957 . . 242 . 51 THR HB H 3.732 . . 243 . 51 THR HG2 H 1.104 . . 244 . 52 CYS H H 7.219 . . 245 . 52 CYS HA H 3.743 . . 246 . 52 CYS HB2 H 1.144 . . 247 . 53 HIS H H 8.768 . . 248 . 53 HIS HB3 H 15.395 . . 249 . 53 HIS HB2 H 45.897 . . 250 . 54 LYS H H 8.702 . . 251 . 54 LYS HA H 4.624 . . 252 . 54 LYS HB2 H 2.357 . . 253 . 54 LYS HB3 H 2.296 . . 254 . 54 LYS HG2 H 2.106 . . 255 . 54 LYS HG3 H 1.974 . . 256 . 54 LYS HD2 H 2.191 . . 257 . 54 LYS HD3 H 2.006 . . 258 . 55 SER H H 8.016 . . 259 . 55 SER HA H 4.793 . . 260 . 55 SER HB3 H 3.998 . . 261 . 55 SER HB2 H 3.745 . . 262 . 56 ASN HD22 H 6.089 . . 263 . 56 ASN HD21 H 7.425 . . 264 . 56 ASN H H 7.967 . . 265 . 56 ASN HA H 4.942 . . 266 . 56 ASN HB2 H 2.864 . . 267 . 56 ASN HB3 H 2.843 . . 268 . 57 ASN H H 8.474 . . 269 . 57 ASN HA H 4.649 . . 270 . 57 ASN HB3 H 2.24 . . 271 . 57 ASN HB2 H 2.427 . . 272 . 57 ASN HD22 H 6.581 . . 273 . 57 ASN HD21 H 7.155 . . 274 . 58 GLY H H 9.25 . . 275 . 58 GLY HA2 H 5.031 . . 276 . 59 PRO HA H 4.559 . . 277 . 59 PRO HB3 H 1.307 . . 278 . 59 PRO HB2 H 1.221 . . 279 . 59 PRO HG2 H 0.125 . . 280 . 59 PRO HG3 H 0.125 . . 281 . 60 THR H H 9.037 . . 282 . 60 THR HA H 4.49 . . 283 . 60 THR HB H 1.978 . . 284 . 61 LYS H H 7.64 . . 285 . 61 LYS HA H 3.862 . . 286 . 61 LYS HB2 H 1.48 . . 287 . 61 LYS HB3 H 1.42 . . 288 . 61 LYS HG2 H 1.27 . . 289 . 61 LYS HG3 H 1.18 . . 290 . 61 LYS HD2 H 2.791 . . 291 . 61 LYS HD3 H 2.791 . . 292 . 62 CYS H H 7.086 . . 293 . 62 CYS HA H 1.829 . . 294 . 62 CYS HB2 H 0.204 . . 295 . 63 GLY H H 8.621 . . 296 . 63 GLY HA3 H 3.916 . . 297 . 63 GLY HA2 H 5.458 . . 298 . 64 GLY H H 7.308 . . 299 . 64 GLY HA3 H 2.968 . . 300 . 64 GLY HA2 H 3.698 . . 301 . 65 CYS H H 6.299 . . 302 . 65 CYS HA H 4.972 . . 303 . 65 CYS HB2 H 0.757 . . 304 . 65 CYS HB3 H 2.452 . . 305 . 67 ILE H H 10.596 . . 306 . 67 ILE HA H 5.477 . . 307 . 67 ILE HB H 3.054 . . 308 . 67 ILE HG2 H 1.544 . . 309 . 67 ILE HG13 H 2.29 . . 310 . 67 ILE HG12 H 2.213 . . 311 . 67 ILE HD1 H 1.173 . . 312 . 68 LYS H H 9.089 . . 313 . 68 LYS HA H 5.093 . . 314 . 68 LYS HG2 H 3.459 . . 315 . 68 LYS HB2 H 2.496 . . 316 . 68 LYS HB3 H 2.196 . . 317 . 68 LYS HG3 H 2.253 . . stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'heme c, 1' _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 HEC 1HAA H 12.378 . . 2 . 1 HEC 2HAA H 6.802 . . 3 . 1 HEC 1HBA H 1.022 . . 4 . 1 HEC 2HBA H 0.266 . . 5 . 1 HEC HMA H 24.528 . . 6 . 1 HEC HHD H 4.703 . . 7 . 1 HEC HMB H 8.64 . . 8 . 1 HEC HHA H 1.144 . . 9 . 1 HEC HAB H -1.755 . . 10 . 1 HEC HBB H -0.711 . . 11 . 1 HEC HHB H 0.072 . . 12 . 1 HEC HBC H -1.805 . . 13 . 1 HEC HAC H -2.315 . . 14 . 1 HEC HHC H -1.804 . . 15 . 1 HEC HMD H 9.227 . . 16 . 1 HEC 2HAD H 1.765 . . 17 . 1 HEC 1HAD H 1.442 . . 18 . 1 HEC 1HBD H 0.062 . . 19 . 1 HEC 2HBD H 0.108 . . stop_ save_ save_shift_set_3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'heme c, 2' _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 HEC 1HAA H 4.561 . . 2 . 1 HEC 2HAA H 3.119 . . 3 . 1 HEC 1HBA H -1.215 . . 4 . 1 HEC 2HBA H -1.383 . . 5 . 1 HEC HMA H -0.814 . . 6 . 1 HEC HMB H 14.633 . . 7 . 1 HEC HMC H 14.289 . . 8 . 1 HEC HBB H -1.382 . . 9 . 1 HEC HAB H -1.721 . . 10 . 1 HEC HHA H 8.822 . . 11 . 1 HEC HHB H -1.453 . . 12 . 1 HEC HBC H -0.83 . . 13 . 1 HEC HAC H -0.54 . . 14 . 1 HEC HMD H 18.037 . . 15 . 1 HEC 1HAD H 17.92 . . 16 . 1 HEC 2HAD H 17.683 . . 17 . 1 HEC 1HBD H -1.446 . . 18 . 1 HEC 2HBD H -1.095 . . 19 . 1 HEC HHC H 10.26 . . stop_ save_ save_shift_set_4 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'heme c, 3' _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 HEC HMA H 11.76 . . 2 . 1 HEC HMB H 17.031 . . 3 . 1 HEC HMC H 8.843 . . 4 . 1 HEC HHA H -0.676 . . 5 . 1 HEC HBB H 2.212 . . 6 . 1 HEC HAB H 0.596 . . 7 . 1 HEC HHB H 1.793 . . 8 . 1 HEC HAC H -0.555 . . 9 . 1 HEC 1HAA H 0.823 . . 10 . 1 HEC 2HAA H 3.188 . . 11 . 1 HEC 1HBA H -0.863 . . 12 . 1 HEC 2HBA H -1.125 . . 13 . 1 HEC HHD H 1.868 . . 14 . 1 HEC HA H 10.298 . . 15 . 1 HEC HB2 H 9.61 . . 16 . 1 HEC HB3 H 11.494 . . 17 . 1 HEC 1HAD H 7.178 . . 18 . 1 HEC 2HAD H 6.417 . . 19 . 1 HEC 1HBD H -0.447 . . 20 . 1 HEC 2HBD H -1.147 . . 21 . 1 HEC HMD H 20.169 . . stop_ save_