data_4960 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Conformation of the Met 61 to His 61 Mutant of Pseudomonas stutzeri substarin ZoBell Ferrocytochrome c-551 ; _BMRB_accession_number 4960 _BMRB_flat_file_name bmr4960.str _Entry_type original _Submission_date 2001-02-21 _Accession_date 2001-02-21 _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 Miller Gregory T. . 2 Hardman John K. . 3 Timkovich Russell . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 419 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-03-09 original author . stop_ _Original_release_date 2001-03-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Conformation of the Met 61 to His 61 Mutant of Pseudomonas stutzeri ZoBell Foerrocytochrome c-551 ; _Citation_status submitted _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miller Gregory T. . 2 Hardman John K. . 3 Timkovich Russell . . stop_ _Journal_abbreviation 'Biophys. J.' _Journal_volume 80 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_M61H _Saveframe_category molecular_system _Mol_system_name 'methionine to histidine mutant of cyt c-551' _Abbreviation_common M61H _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'M61H cyt c-551' $c-551 '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 transport chain' 'bacterial respiration' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_c-551 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome c-551' _Name_variant M61H _Abbreviation_common c-551 _Molecular_mass 9500 _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 82 _Mol_residue_sequence ; QDGEALFKSKPCAACHSVDT KMVGPALKEVAAKNAGVEGA ADTLALHIKNGSQGVWGPIP HPPNPVTEEEAKILAEWVLS LK ; loop_ _Residue_seq_code _Residue_label 1 GLN 2 ASP 3 GLY 4 GLU 5 ALA 6 LEU 7 PHE 8 LYS 9 SER 10 LYS 11 PRO 12 CYS 13 ALA 14 ALA 15 CYS 16 HIS 17 SER 18 VAL 19 ASP 20 THR 21 LYS 22 MET 23 VAL 24 GLY 25 PRO 26 ALA 27 LEU 28 LYS 29 GLU 30 VAL 31 ALA 32 ALA 33 LYS 34 ASN 35 ALA 36 GLY 37 VAL 38 GLU 39 GLY 40 ALA 41 ALA 42 ASP 43 THR 44 LEU 45 ALA 46 LEU 47 HIS 48 ILE 49 LYS 50 ASN 51 GLY 52 SER 53 GLN 54 GLY 55 VAL 56 TRP 57 GLY 58 PRO 59 ILE 60 PRO 61 HIS 62 PRO 63 PRO 64 ASN 65 PRO 66 VAL 67 THR 68 GLU 69 GLU 70 GLU 71 ALA 72 LYS 73 ILE 74 LEU 75 ALA 76 GLU 77 TRP 78 VAL 79 LEU 80 SER 81 LEU 82 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-09-14 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 7296 H47A_c-551 100.00 82 97.56 97.56 1.82e-48 PDB 1CCH "The Solution Conformation Of Cytochrome C-551 From P.Stutzeri Zobell Determined By Nmr+" 100.00 82 98.78 98.78 1.11e-49 PDB 1FI3 "Solution Structure Of The M61h Mutant Of Pseudomonas Stutzeri Substrain Zobell Ferrocytochrome C-551" 100.00 82 100.00 100.00 8.66e-51 PDB 2I8F "Solution Conformation Of The H47a Mutant Of Pseudomonas Stutzeri Zobell Ferrocytochrome C-551" 100.00 82 97.56 97.56 1.82e-48 EMBL CAA40153 "pseudomonas cytochrome c-551 precursor [Pseudomonas stutzeri]" 100.00 104 98.78 98.78 7.07e-50 GB EHY75989 "cytochrome c-551 [Pseudomonas stutzeri ATCC 14405 = CCUG 16156]" 100.00 104 98.78 98.78 7.07e-50 REF WP_003279940 "cytochrome C biogenesis protein CcsA [Pseudomonas stutzeri]" 100.00 104 98.78 98.78 7.07e-50 SP P00101 "RecName: Full=Cytochrome c-551; AltName: Full=Cytochrome C8; AltName: Full=Cytochrome c551; Flags: Precursor [Pseudomonas stutz" 100.00 104 98.78 98.78 7.07e-50 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 Thu Jun 16 11:03:01 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 _Strain $c-551 'Pseudomonas stutzeri ZoBell' 96564 Bacteria . Pseudomonas stutzeri ZoBell 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 $c-551 'recombinant technology' 'E. coli' Escherichia coli 'DH5 alpha' . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_literature_sample _Saveframe_category sample _Sample_type solution _Details ; Conditions reported here produced the reported chemical shifts. Chemical shift assignment ambiguities were resolved by studying samples at different pH values and temperatures. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $c-551 . mM 4 5 . H2O 90 % . . . D2O 10 % . . . 'sodium borate buffer' . mM . . . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 95 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $literature_sample save_ save_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $literature_sample save_ save_HOHAHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HOHAHA _Sample_label $literature_sample save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HOHAHA _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_literature_sample_conditions _Saveframe_category sample_conditions _Details ; Sample was in 90%H2O/10%D2O in sodium borate buffer at pH 9.2. after deoxygenation by repeated cycles of vacuum and argon flushing, it was reduced by addition of solid sodium dithionite and sealed in a 5 mm NMR tube under an argon atmosphere. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 9.2 0.1 n/a temperature 323 1 K 'ionic strength' 0.15 0.05 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details ; The chemical shift are nominally reported versus TSP. The internal water peak was used to set the reference scale and was assigned a value of 4.484 ppm at 323K. The meso peak at 9.00 ppm is largely temeperature independent. ; 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H 1 'methyl protons' ppm 0.00 internal indirect . internal . 100.0 $entry_citation $entry_citation 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_standard_shift_set _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label NOESY DQF-COSY HOHAHA stop_ loop_ _Sample_label $literature_sample stop_ _Sample_conditions_label $literature_sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'M61H cyt c-551' _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 . 2 ASP HA H 4.65 0.02 1 2 . 2 ASP HB2 H 2.72 0.02 2 3 . 3 GLY HA2 H 3.26 0.02 2 4 . 4 GLU H H 7.18 0.02 1 5 . 4 GLU HA H 2.64 0.02 1 6 . 4 GLU HB2 H 1.78 0.02 2 7 . 4 GLU HG2 H 2.14 0.02 2 8 . 5 ALA H H 7.37 0.02 1 9 . 5 ALA HA H 3.94 0.02 1 10 . 5 ALA HB H 1.40 0.02 1 11 . 6 LEU H H 7.67 0.02 1 12 . 6 LEU HA H 4.06 0.02 1 13 . 6 LEU HB2 H 1.89 0.02 2 14 . 6 LEU HB3 H 1.37 0.02 2 15 . 6 LEU HG H 1.72 0.02 1 16 . 6 LEU HD1 H 0.96 0.02 2 17 . 7 PHE H H 8.20 0.02 1 18 . 7 PHE HA H 4.09 0.02 1 19 . 7 PHE HB2 H 2.76 0.02 2 20 . 7 PHE HB3 H 2.69 0.02 2 21 . 7 PHE HD1 H 6.98 0.02 3 22 . 7 PHE HE1 H 6.65 0.02 3 23 . 7 PHE HZ H 6.57 0.02 1 24 . 8 LYS H H 7.50 0.02 1 25 . 8 LYS HA H 3.88 0.02 1 26 . 8 LYS HB2 H 1.79 0.02 2 27 . 8 LYS HG2 H 1.72 0.02 2 28 . 8 LYS HD2 H 2.08 0.02 2 29 . 8 LYS HE2 H 2.98 0.02 2 30 . 9 SER H H 7.73 0.02 1 31 . 9 SER HA H 4.57 0.02 1 32 . 9 SER HB2 H 4.06 0.02 2 33 . 9 SER HB3 H 3.94 0.02 2 34 . 10 LYS H H 7.48 0.02 1 35 . 10 LYS HA H 5.03 0.02 1 36 . 10 LYS HB2 H 2.71 0.02 2 37 . 10 LYS HB3 H 2.20 0.02 2 38 . 10 LYS HG2 H 1.96 0.02 2 39 . 10 LYS HG3 H 2.13 0.02 2 40 . 10 LYS HD2 H 1.61 0.02 2 41 . 10 LYS HE2 H 2.94 0.02 2 42 . 11 PRO HA H 4.83 0.02 1 43 . 11 PRO HB2 H 2.84 0.02 2 44 . 11 PRO HB3 H 2.71 0.02 2 45 . 11 PRO HG2 H 2.41 0.02 2 46 . 11 PRO HG3 H 2.48 0.02 2 47 . 11 PRO HD2 H 4.07 0.02 2 48 . 11 PRO HD3 H 4.15 0.02 2 49 . 12 CYS H H 8.11 0.02 1 50 . 12 CYS HA H 4.85 0.02 1 51 . 12 CYS HB2 H 2.74 0.02 1 52 . 12 CYS HB3 H 2.32 0.02 1 53 . 13 ALA H H 7.87 0.02 1 54 . 13 ALA HA H 4.11 0.02 1 55 . 13 ALA HB H 1.08 0.02 1 56 . 14 ALA H H 7.89 0.02 1 57 . 14 ALA HA H 4.17 0.02 1 58 . 14 ALA HB H 1.72 0.02 1 59 . 15 CYS H H 6.66 0.02 1 60 . 15 CYS HA H 4.35 0.02 1 61 . 15 CYS HB2 H 1.92 0.02 1 62 . 15 CYS HB3 H 1.05 0.02 1 63 . 16 HIS H H 6.98 0.02 1 64 . 16 HIS HA H 4.04 0.02 1 65 . 16 HIS HB2 H 1.13 0.02 1 66 . 16 HIS HB3 H 1.18 0.02 1 67 . 16 HIS HD1 H 8.51 0.02 1 68 . 16 HIS HD2 H 0.58 0.02 1 69 . 16 HIS HE1 H 0.69 0.02 1 70 . 17 SER H H 8.00 0.02 1 71 . 17 SER HA H 4.46 0.02 1 72 . 17 SER HB2 H 3.74 0.02 2 73 . 17 SER HB3 H 3.68 0.02 2 74 . 18 VAL HA H 3.16 0.02 1 75 . 18 VAL HB H 1.81 0.02 1 76 . 18 VAL HG1 H 0.75 0.02 2 77 . 18 VAL HG2 H 0.70 0.02 2 78 . 19 ASP H H 7.72 0.02 1 79 . 19 ASP HA H 4.48 0.02 1 80 . 19 ASP HB2 H 2.48 0.02 2 81 . 19 ASP HB3 H 2.38 0.02 2 82 . 20 THR H H 7.21 0.02 1 83 . 20 THR HA H 4.40 0.02 1 84 . 20 THR HB H 3.75 0.02 1 85 . 20 THR HG2 H 0.99 0.02 1 86 . 21 LYS HA H 3.58 0.02 1 87 . 21 LYS HB2 H 1.63 0.02 2 88 . 21 LYS HB3 H 1.53 0.02 2 89 . 21 LYS HG2 H 1.13 0.02 2 90 . 21 LYS HD2 H 1.53 0.02 2 91 . 21 LYS HE2 H 2.86 0.02 2 92 . 22 MET H H 7.26 0.02 1 93 . 22 MET HA H 4.35 0.02 1 94 . 22 MET HB2 H 1.34 0.02 2 95 . 22 MET HB3 H 1.64 0.02 2 96 . 22 MET HG2 H 2.00 0.02 2 97 . 23 VAL H H 6.99 0.02 1 98 . 23 VAL HA H 3.95 0.02 1 99 . 23 VAL HB H 1.97 0.02 1 100 . 23 VAL HG1 H 1.19 0.02 2 101 . 23 VAL HG2 H 1.66 0.02 2 102 . 24 GLY H H 6.52 0.02 1 103 . 24 GLY HA2 H 3.84 0.02 1 104 . 24 GLY HA3 H 0.41 0.02 1 105 . 25 PRO HA H 3.57 0.02 1 106 . 25 PRO HB2 H 0.48 0.02 1 107 . 25 PRO HB3 H 0.91 0.02 1 108 . 25 PRO HG2 H -0.01 0.02 1 109 . 25 PRO HG3 H 0.19 0.02 1 110 . 25 PRO HD2 H 2.33 0.02 1 111 . 25 PRO HD3 H 2.94 0.02 1 112 . 26 ALA H H 8.15 0.02 1 113 . 26 ALA HA H 3.81 0.02 1 114 . 26 ALA HB H 0.67 0.02 1 115 . 27 LEU H H 7.89 0.02 1 116 . 27 LEU HA H 3.34 0.02 1 117 . 27 LEU HB2 H 1.04 0.02 2 118 . 27 LEU HB3 H 0.85 0.02 2 119 . 27 LEU HG H 0.54 0.02 1 120 . 27 LEU HD1 H 0.00 0.02 1 121 . 27 LEU HD2 H -.70 0.02 1 122 . 28 LYS H H 8.58 0.02 1 123 . 28 LYS HA H 3.76 0.02 1 124 . 28 LYS HB2 H 1.62 0.02 2 125 . 28 LYS HG2 H 1.25 0.02 2 126 . 28 LYS HD2 H 1.52 0.02 2 127 . 28 LYS HE2 H 2.80 0.02 2 128 . 28 LYS HE3 H 2.74 0.02 2 129 . 29 GLU H H 6.91 0.02 1 130 . 29 GLU HA H 4.19 0.02 1 131 . 29 GLU HB2 H 1.99 0.02 2 132 . 29 GLU HG2 H 2.22 0.02 2 133 . 30 VAL H H 7.08 0.02 1 134 . 30 VAL HA H 3.95 0.02 1 135 . 30 VAL HB H 2.21 0.02 1 136 . 30 VAL HG1 H 1.40 0.02 2 137 . 30 VAL HG2 H 0.60 0.02 2 138 . 31 ALA H H 7.85 0.02 1 139 . 31 ALA HA H 3.83 0.02 1 140 . 31 ALA HB H 1.57 0.02 1 141 . 32 ALA H H 7.68 0.02 1 142 . 32 ALA HA H 4.07 0.02 1 143 . 32 ALA HB H 1.53 0.02 1 144 . 33 LYS H H 7.88 0.02 1 145 . 33 LYS HA H 4.17 0.02 1 146 . 33 LYS HB2 H 2.24 0.02 2 147 . 33 LYS HB3 H 2.06 0.02 2 148 . 33 LYS HG2 H 1.58 0.02 4 149 . 33 LYS HG3 H 1.00 0.02 4 150 . 33 LYS HD2 H 1.40 0.02 4 151 . 33 LYS HD3 H 1.63 0.02 4 152 . 33 LYS HE2 H 2.84 0.02 2 153 . 34 ASN H H 7.30 0.02 1 154 . 34 ASN HA H 4.77 0.02 1 155 . 34 ASN HB2 H 2.79 0.02 2 156 . 34 ASN HB3 H 2.41 0.02 2 157 . 34 ASN HD21 H 8.58 0.02 2 158 . 34 ASN HD22 H 7.68 0.02 2 159 . 35 ALA H H 7.51 0.02 1 160 . 35 ALA HA H 4.23 0.02 1 161 . 35 ALA HB H 1.51 0.02 1 162 . 36 GLY HA2 H 4.00 0.02 2 163 . 36 GLY HA3 H 3.90 0.02 2 164 . 37 VAL H H 7.47 0.02 1 165 . 37 VAL HA H 3.99 0.02 1 166 . 37 VAL HB H 2.19 0.02 1 167 . 37 VAL HG1 H 0.94 0.02 2 168 . 38 GLU HA H 4.16 0.02 1 169 . 38 GLU HB2 H 2.01 0.02 2 170 . 38 GLU HG2 H 2.29 0.02 2 171 . 39 GLY HA2 H 4.02 0.02 2 172 . 39 GLY HA3 H 4.14 0.02 2 173 . 40 ALA H H 7.61 0.02 1 174 . 40 ALA HA H 4.11 0.02 1 175 . 40 ALA HB H 1.57 0.02 1 176 . 41 ALA HA H 3.85 0.02 1 177 . 41 ALA HB H 1.41 0.02 1 178 . 42 ASP H H 7.44 0.02 1 179 . 42 ASP HA H 4.34 0.02 1 180 . 42 ASP HB2 H 2.61 0.02 2 181 . 43 THR H H 7.60 0.02 1 182 . 43 THR HA H 3.62 0.02 1 183 . 43 THR HB H 4.05 0.02 1 184 . 43 THR HG2 H 0.84 0.02 1 185 . 44 LEU H H 8.67 0.02 1 186 . 44 LEU HA H 3.82 0.02 1 187 . 44 LEU HB2 H 2.03 0.02 2 188 . 44 LEU HB3 H 1.40 0.02 2 189 . 44 LEU HG H 2.05 0.02 1 190 . 44 LEU HD1 H 1.15 0.02 2 191 . 44 LEU HD2 H 0.99 0.02 2 192 . 45 ALA H H 8.05 0.02 1 193 . 45 ALA HA H 3.81 0.02 1 194 . 45 ALA HB H 1.39 0.02 1 195 . 46 LEU H H 7.20 0.02 1 196 . 46 LEU HA H 3.85 0.02 1 197 . 46 LEU HB2 H 1.70 0.02 2 198 . 46 LEU HG H 1.64 0.02 4 199 . 46 LEU HD1 H 0.81 0.02 2 200 . 47 HIS H H 7.71 0.02 1 201 . 47 HIS HA H 4.00 0.02 1 202 . 47 HIS HB2 H 2.81 0.02 2 203 . 47 HIS HB3 H 2.30 0.02 2 204 . 47 HIS HD2 H 6.71 0.02 1 205 . 47 HIS HE1 H 7.96 0.02 1 206 . 48 ILE H H 8.56 0.02 1 207 . 48 ILE HA H 1.75 0.02 1 208 . 48 ILE HB H 1.67 0.02 1 209 . 48 ILE HG12 H 1.12 0.02 2 210 . 48 ILE HG13 H 1.75 0.02 2 211 . 48 ILE HG2 H 0.81 0.02 1 212 . 48 ILE HD1 H 1.32 0.02 1 213 . 49 LYS H H 7.01 0.02 1 214 . 49 LYS HA H 3.76 0.02 1 215 . 49 LYS HB2 H 1.59 0.02 2 216 . 49 LYS HG2 H 1.27 0.02 2 217 . 49 LYS HD2 H 1.42 0.02 2 218 . 49 LYS HD3 H 1.54 0.02 2 219 . 49 LYS HE2 H 3.05 0.02 2 220 . 49 LYS HE3 H 3.12 0.02 2 221 . 50 ASN H H 7.94 0.02 1 222 . 50 ASN HA H 4.56 0.02 1 223 . 50 ASN HB2 H 2.74 0.02 2 224 . 50 ASN HB3 H 2.62 0.02 2 225 . 51 GLY H H 7.58 0.02 1 226 . 51 GLY HA2 H 2.76 0.02 1 227 . 51 GLY HA3 H 4.03 0.02 . 228 . 52 SER H H 7.24 0.02 1 229 . 52 SER HA H 3.91 0.02 1 230 . 52 SER HB2 H 2.64 0.02 2 231 . 52 SER HB3 H 2.59 0.02 2 232 . 53 GLN H H 7.69 0.02 1 233 . 53 GLN HA H 4.27 0.02 1 234 . 53 GLN HB2 H 1.82 0.02 2 235 . 53 GLN HG2 H 1.40 0.02 4 236 . 54 GLY H H 8.02 0.02 1 237 . 54 GLY HA2 H 4.21 0.02 2 238 . 54 GLY HA3 H 3.83 0.02 2 239 . 55 VAL H H 10.38 0.02 1 240 . 55 VAL HA H 3.70 0.02 1 241 . 55 VAL HB H 2.36 0.02 1 242 . 55 VAL HG1 H 0.90 0.02 2 243 . 55 VAL HG2 H 0.54 0.02 2 244 . 56 TRP H H 10.59 0.02 1 245 . 56 TRP HA H 4.58 0.02 1 246 . 56 TRP HB2 H 3.76 0.02 2 247 . 56 TRP HB3 H 3.65 0.02 2 248 . 56 TRP HD1 H 7.64 0.02 1 249 . 56 TRP HE1 H 12.30 0.02 1 250 . 56 TRP HE3 H 7.89 0.02 1 251 . 56 TRP HZ2 H 7.44 0.02 1 252 . 56 TRP HZ3 H 7.17 0.02 1 253 . 56 TRP HH2 H 6.98 0.02 1 254 . 57 GLY H H 8.08 0.02 1 255 . 57 GLY HA2 H 4.16 0.02 2 256 . 57 GLY HA3 H 4.55 0.02 2 257 . 58 PRO HA H 4.81 0.02 1 258 . 58 PRO HB2 H 2.31 0.02 2 259 . 58 PRO HB3 H 2.20 0.02 2 260 . 58 PRO HG2 H 2.25 0.02 2 261 . 58 PRO HG3 H 1.99 0.02 2 262 . 58 PRO HD2 H 3.61 0.02 2 263 . 58 PRO HD3 H 3.90 0.02 2 264 . 59 ILE H H 7.48 0.02 1 265 . 59 ILE HA H 4.68 0.02 1 266 . 59 ILE HB H 2.28 0.02 1 267 . 59 ILE HG12 H 1.54 0.02 1 268 . 59 ILE HG13 H 1.89 0.02 1 269 . 59 ILE HG2 H 1.20 0.02 1 270 . 59 ILE HD1 H 1.18 0.02 1 271 . 60 PRO HA H 4.77 0.02 1 272 . 60 PRO HB2 H 2.00 0.02 2 273 . 60 PRO HB3 H 2.07 0.02 2 274 . 60 PRO HG2 H 2.30 0.02 2 275 . 60 PRO HG3 H 1.41 0.02 2 276 . 60 PRO HD2 H 4.15 0.02 2 277 . 60 PRO HD3 H 3.75 0.02 2 278 . 61 HIS H H 8.00 0.02 1 279 . 61 HIS HA H 2.48 0.02 1 280 . 61 HIS HB2 H 0.45 0.02 1 281 . 61 HIS HB3 H -1.23 0.02 1 282 . 61 HIS HD1 H 9.20 0.02 1 283 . 61 HIS HE1 H 4.16 0.02 1 284 . 62 PRO HB2 H 1.49 0.02 2 285 . 62 PRO HG2 H 1.79 0.02 1 286 . 62 PRO HG3 H 0.88 0.02 1 287 . 62 PRO HD2 H 2.87 0.02 1 288 . 62 PRO HD3 H 0.23 0.02 1 289 . 63 PRO HA H 3.53 0.02 1 290 . 63 PRO HB2 H 1.74 0.02 2 291 . 63 PRO HB3 H 1.95 0.02 2 292 . 63 PRO HG2 H 1.75 0.02 2 293 . 63 PRO HG3 H 1.62 0.02 2 294 . 63 PRO HD2 H 3.20 0.02 2 295 . 63 PRO HD3 H 3.10 0.02 2 296 . 64 ASN H H 7.39 0.02 1 297 . 64 ASN HA H 5.02 0.02 1 298 . 64 ASN HB2 H 2.05 0.02 1 299 . 64 ASN HB3 H 2.47 0.02 1 300 . 64 ASN HD21 H 5.52 0.02 1 301 . 64 ASN HD22 H 3.64 0.02 1 302 . 65 PRO HA H 4.80 0.02 1 303 . 65 PRO HB2 H 1.87 0.02 2 304 . 65 PRO HB3 H 1.83 0.02 2 305 . 65 PRO HG2 H 2.24 0.02 2 306 . 65 PRO HG3 H 2.06 0.02 2 307 . 65 PRO HD2 H 3.70 0.02 2 308 . 65 PRO HD3 H 3.67 0.02 2 309 . 66 VAL H H 8.07 0.02 1 310 . 66 VAL HA H 5.06 0.02 1 311 . 66 VAL HB H 2.45 0.02 1 312 . 66 VAL HG1 H 0.76 0.02 2 313 . 66 VAL HG2 H 0.61 0.02 2 314 . 67 THR H H 8.93 0.02 1 315 . 67 THR HA H 4.42 0.02 1 316 . 67 THR HB H 4.82 0.02 1 317 . 67 THR HG2 H 1.29 0.02 1 318 . 68 GLU HA H 3.89 0.02 1 319 . 68 GLU HB2 H 2.01 0.02 2 320 . 68 GLU HG2 H 2.30 0.02 2 321 . 69 GLU HA H 4.04 0.02 1 322 . 69 GLU HB2 H 2.08 0.02 2 323 . 69 GLU HB3 H 1.96 0.02 2 324 . 70 GLU H H 7.76 0.02 1 325 . 70 GLU HA H 3.81 0.02 1 326 . 70 GLU HB2 H 2.57 0.02 2 327 . 70 GLU HB3 H 2.49 0.02 2 328 . 70 GLU HG2 H 1.75 0.02 2 329 . 71 ALA H H 8.68 0.02 1 330 . 71 ALA HA H 4.00 0.02 1 331 . 71 ALA HB H 1.59 0.02 1 332 . 72 LYS H H 7.67 0.02 1 333 . 72 LYS HA H 4.08 0.02 1 334 . 72 LYS HB2 H 2.05 0.02 2 335 . 72 LYS HB3 H 1.92 0.02 2 336 . 72 LYS HG2 H 1.43 0.02 2 337 . 72 LYS HD2 H 1.67 0.02 2 338 . 72 LYS HE2 H 2.92 0.02 2 339 . 73 ILE H H 7.94 0.02 1 340 . 73 ILE HA H 3.83 0.02 1 341 . 73 ILE HB H 1.92 0.02 1 342 . 73 ILE HG12 H 1.85 0.02 2 343 . 73 ILE HG13 H 1.15 0.02 2 344 . 73 ILE HG2 H 0.85 0.02 1 345 . 73 ILE HD1 H 0.85 0.02 1 346 . 74 LEU H H 8.69 0.02 1 347 . 74 LEU HA H 4.38 0.02 1 348 . 74 LEU HB2 H 2.51 0.02 2 349 . 74 LEU HB3 H 1.79 0.02 2 350 . 74 LEU HG H 2.00 0.02 1 351 . 74 LEU HD1 H 1.38 0.02 2 352 . 74 LEU HD2 H 1.26 0.02 2 353 . 75 ALA H H 8.71 0.02 1 354 . 75 ALA HA H 3.99 0.02 1 355 . 75 ALA HB H 1.68 0.02 1 356 . 76 GLU H H 8.36 0.02 1 357 . 76 GLU HA H 3.96 0.02 1 358 . 76 GLU HB2 H 2.19 0.02 2 359 . 76 GLU HB3 H 2.13 0.02 2 360 . 76 GLU HG2 H 2.55 0.02 2 361 . 77 TRP H H 8.42 0.02 1 362 . 77 TRP HA H 4.36 0.02 1 363 . 77 TRP HB2 H 3.75 0.02 2 364 . 77 TRP HB3 H 3.38 0.02 2 365 . 77 TRP HD1 H 7.24 0.02 1 366 . 77 TRP HE1 H 10.12 0.02 1 367 . 77 TRP HE3 H 7.57 0.02 1 368 . 77 TRP HZ2 H 6.96 0.02 1 369 . 77 TRP HZ3 H 6.16 0.02 1 370 . 77 TRP HH2 H 5.62 0.02 1 371 . 78 VAL H H 9.06 0.02 1 372 . 78 VAL HA H 2.71 0.02 1 373 . 78 VAL HB H 2.42 0.02 1 374 . 78 VAL HG1 H 1.39 0.02 2 375 . 78 VAL HG2 H 0.84 0.02 2 376 . 79 LEU H H 7.66 0.02 1 377 . 79 LEU HA H 3.80 0.02 1 378 . 79 LEU HB2 H 1.56 0.02 2 379 . 79 LEU HB3 H 1.89 0.02 2 380 . 79 LEU HG H 1.92 0.02 1 381 . 79 LEU HD1 H 0.88 0.02 2 382 . 80 SER H H 7.61 0.02 1 383 . 80 SER HA H 4.31 0.02 1 384 . 80 SER HB2 H 4.04 0.02 2 385 . 80 SER HB3 H 3.95 0.02 2 386 . 81 LEU H H 7.13 0.02 1 387 . 81 LEU HA H 3.91 0.02 1 388 . 81 LEU HB2 H 1.45 0.02 2 389 . 81 LEU HB3 H 0.84 0.02 2 390 . 81 LEU HG H 1.25 0.02 1 391 . 81 LEU HD1 H 0.14 0.02 2 392 . 81 LEU HD2 H -0.17 0.02 2 393 . 82 LYS H H 7.20 0.02 1 394 . 82 LYS HA H 3.97 0.02 1 395 . 82 LYS HB2 H 1.68 0.02 2 396 . 82 LYS HB3 H 1.60 0.02 2 397 . 82 LYS HG2 H 1.63 0.02 4 398 . 82 LYS HD2 H 1.32 0.02 2 399 . 82 LYS HE2 H 2.97 0.02 2 stop_ save_ save_standard_shift_set_heme _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $literature_sample stop_ _Sample_conditions_label $literature_sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'heme 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 HEC HHB H 9.20 0.01 1 2 . 1 HEC HHC H 9.20 0.01 1 3 . 1 HEC HHD H 9.00 0.01 1 4 . 1 HEC HMA1 H 3.76 0.02 1 5 . 1 HEC HAA1 H 4.60 0.02 1 6 . 1 HEC HAA2 H 4.23 0.02 1 7 . 1 HEC HBA1 H 2.85 0.02 1 8 . 1 HEC HBA2 H 3.54 0.02 1 9 . 1 HEC HBB1 H 1.84 0.02 1 10 . 1 HEC HMB1 H 3.62 0.02 1 11 . 1 HEC HAB H 5.88 0.02 1 12 . 1 HEC HMC1 H 3.27 0.02 1 13 . 1 HEC HAC H 6.13 0.02 1 14 . 1 HEC HMD1 H 3.22 0.02 1 15 . 1 HEC HAD1 H 4.35 0.02 1 16 . 1 HEC HAD2 H 3.84 0.02 1 17 . 1 HEC HBD1 H 3.32 0.02 1 18 . 1 HEC HBD2 H 2.60 0.02 1 19 . 1 HEC HBC1 H 2.47 0.02 1 20 . 1 HEC HHA H 9.55 0.01 1 stop_ save_