data_5597 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bartalesi Ilaria . . 2 Bertini Ivano . . 3 Rosato Antonio . . stop_ _BMRB_accession_number 5597 _BMRB_flat_file_name bmr5597.str _Entry_type new _Submission_date 2002-11-25 _Accession_date 2002-11-25 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 375 '15N chemical shifts' 75 stop_ loop_ _Related_BMRB_accession_number _Relationship 5172 "oxidized cytochrome c553 from Bacillus pasteurii" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Structure and Dynamics of Reduced Bacillus pasteurii Cytochrome c: Oxidation State Dependent Properties and Implications for Electron Transfer Processes ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 22422606 _PubMed_ID 12534286 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bartalesi Ilaria . . 2 Bertini Ivano . . 3 Rosato Antonio . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 3 _Page_first 739 _Page_last 745 _Year 2003 loop_ _Keyword "cytochrome c" "redox" "electron transfer" stop_ save_ ################################## # Molecular system description # ################################## save_system_cytc _Saveframe_category molecular_system _Mol_system_name "cytochrome c" _Abbreviation_common cytc _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "cytochrome C" $cytc "heme cofactor" $HEC stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "not reported" loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1N9C ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_cytc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "cytochrome c" _Name_variant . _Abbreviation_common cytc _Mol_thiol_state "not reported" ############################## # Polymer residue sequence # ############################## _Residue_count 71 _Mol_residue_sequence ; VDAEAVVQQKCISCHGGDLT GASAPAIDKAGANYSEEEIL DIILNGQGGMPGGIAKGAEA EAVAAWLAEKK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 22 VAL 2 23 ASP 3 24 ALA 4 25 GLU 5 26 ALA 6 27 VAL 7 28 VAL 8 29 GLN 9 30 GLN 10 31 LYS 11 32 CYS 12 33 ILE 13 34 SER 14 35 CYS 15 36 HIS 16 37 GLY 17 38 GLY 18 39 ASP 19 40 LEU 20 41 THR 21 42 GLY 22 43 ALA 23 44 SER 24 45 ALA 25 46 PRO 26 47 ALA 27 48 ILE 28 49 ASP 29 50 LYS 30 51 ALA 31 52 GLY 32 53 ALA 33 54 ASN 34 55 TYR 35 56 SER 36 57 GLU 37 58 GLU 38 59 GLU 39 60 ILE 40 61 LEU 41 62 ASP 42 63 ILE 43 64 ILE 44 65 LEU 45 66 ASN 46 67 GLY 47 68 GLN 48 69 GLY 49 70 GLY 50 71 MET 51 72 PRO 52 73 GLY 53 74 GLY 54 75 ILE 55 76 ALA 56 77 LYS 57 78 GLY 58 79 ALA 59 80 GLU 60 81 ALA 61 82 GLU 62 83 ALA 63 84 VAL 64 85 ALA 65 86 ALA 66 87 TRP 67 88 LEU 68 89 ALA 69 90 GLU 70 91 LYS 71 92 LYS stop_ _Sequence_homology_query_date 2003-02-23 _Sequence_homology_query_revised_last_date 2003-02-23 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 PDB 1B7V "A Chain A, Structure Of The C-553 Cytochrome From Bacillus Pasteurii To 1.7 A Resolution" 100.00% 71 100% 100% 3e-34 PDB 1C75 'A Chain A, 0.97 A "ab Initio" Crystal Structure Of Cytochrome C-553 From Bacillus Pasteurii' 100.00% 71 100% 100% 3e-34 PDB 1K3G "A Chain A, Nmr Solution Structure Of Oxidized Cytochrome C-553 From Bacillus Pasteurii" 100.00% 71 100% 100% 8e-34 PDB 1K3H "A Chain A, Nmr Solution Structure Of Oxidized Cytochrome C-553 From Bacillus Pasteurii" 100.00% 71 100% 100% 3e-34 EMBL CAC39450.1 "cytochrome c553 [Sporosarcina pasteurii]" 83.53% 85 98% 98% 1e-33 SWISS-PROT P82599 "C553_BACPA Cytochrome c-553 (C553)" 77.17% 92 100% 100% 3e-34 stop_ save_ ############# # Ligands # ############# save_HEC _Saveframe_category ligand _Mol_type non-polymer _Name_common 'PROTOPORPHYRIN IX CONTAINING FE' _Abbreviation_common 'heme c' _Name_IUPAC . _PDB_code HEC _Mol_empirical_formula 'C34 H32 N4 O4 FE1' _Mol_charge ? _Mol_paramagnetic no _Mol_aromatic yes _Details . loop_ _Synonym HEME stop_ loop_ _Atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE ? 2+ 2+ 0 CHA C ? 0 ? ? CHB C ? 0 ? ? CHC C ? 0 ? ? CHD C ? 0 ? ? NA N ? 0 ? ? C1A C ? 0 ? ? C2A C ? 0 ? ? C3A C ? 0 ? ? C4A C ? 0 ? ? CMA C ? 0 ? ? CAA C ? 0 ? ? CBA C ? 0 ? ? CGA C ? 0 ? ? O1A O ? 0 ? ? O2A O ? 0 ? ? NB N ? 0 ? ? C1B C ? 0 ? ? C2B C ? 0 ? ? C3B C ? 0 ? ? C4B C ? 0 ? ? CMB C ? 0 ? ? CAB C ? 0 ? ? CBB C ? 0 ? ? NC N ? 0 ? ? C1C C ? 0 ? ? C2C C ? 0 ? ? C3C C ? 0 ? ? C4C C ? 0 ? ? CMC C ? 0 ? ? CAC C ? 0 ? ? CBC C ? 0 ? ? ND N ? 0 ? ? C1D C ? 0 ? ? C2D C ? 0 ? ? C3D C ? 0 ? ? C4D C ? 0 ? ? CMD C ? 0 ? ? CAD C ? 0 ? ? CBD C ? 0 ? ? CGD C ? 0 ? ? O1D O ? 0 ? ? O2D O ? 0 ? ? HHA H ? 0 ? ? HHB H ? 0 ? ? HHC H ? 0 ? ? HHD H ? 0 ? ? 1HMA H ? 0 ? ? 2HMA H ? 0 ? ? 3HMA H ? 0 ? ? 1HAA H ? 0 ? ? 2HAA H ? 0 ? ? 1HBA H ? 0 ? ? 2HBA H ? 0 ? ? H2A H ? 0 ? ? 1HMB H ? 0 ? ? 2HMB H ? 0 ? ? 3HMB H ? 0 ? ? HAB H ? 0 ? ? 1HBB H ? 0 ? ? 2HBB H ? 0 ? ? 3HBB H ? 0 ? ? 1HMC H ? 0 ? ? 2HMC H ? 0 ? ? 3HMC H ? 0 ? ? HAC H ? 0 ? ? 1HBC H ? 0 ? ? 2HBC H ? 0 ? ? 3HBC H ? 0 ? ? 1HMD H ? 0 ? ? 2HMD H ? 0 ? ? 3HMD H ? 0 ? ? 1HAD H ? 0 ? ? 2HAD H ? 0 ? ? 1HBD H ? 0 ? ? 2HBD H ? 0 ? ? H2D H ? 0 ? ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _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 SING CHD C4C DOUB 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 1HMA SING CMA 2HMA SING CMA 3HMA SING CAA CBA SING CAA 1HAA SING CAA 2HAA SING CBA CGA SING CBA 1HBA SING CBA 2HBA DOUB CGA O1A SING CGA O2A SING O2A H2A DOUB NB C1B SING NB C4B SING C1B C2B DOUB C2B C3B SING C2B CMB SING C3B C4B SING C3B CAB SING CMB 1HMB SING CMB 2HMB SING CMB 3HMB SING CAB CBB SING CAB HAB SING CBB 1HBB SING CBB 2HBB SING NC C1C SING NC C4C DOUB C1C C2C SING C2C C3C SING C2C CMC DOUB C3C C4C SING C3C CAC SING CMC 1HMC SING CMC 2HMC SING CMC 3HMC SING CAC CBC SING CAC HAC SING CBC 1HBC SING CBC 2HBC SING ND C1D DOUB ND C4D SING C1D C2D DOUB C2D C3D SING C2D CMD SING C3D C4D SING C3D CAD SING CMD 1HMD SING CMD 2HMD SING CMD 3HMD SING CAD CBD SING CAD 1HAD SING CAD 2HAD SING CBD CGD SING CBD 1HBD SING CBD 2HBD DOUB CGD O1D SING CGD O2D SING O2D H2D stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single "metal coordination" "cytochrome C" 36 GLU OE2 "heme cofactor" . . FE++ stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cytc "B. pasteurii" 1474 Eubacteria . Bacillus pasteurii 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 _Details $cytc 'recombinant technology' "E. coli" Escherichia coli C41(DE3) . ; the protein has been co-expressed with the ccm genes, in order to obtain insertion of the heme cofactor ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cytc 1 mM . "phosphate buffer" 100 mM . stop_ save_ save_sample2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cytc 1 mM "[U-90% 15N]" "phosphate buffer" 100 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N NOESY 1H-15N TOCSY 1H-1H NOESY 1H-1H TOCSY HNHA HNHB ; save_ ####################### # Sample conditions # ####################### save_condition1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 n/a temperature 296 1 K "ionic strength" 100 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_csset1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample2 stop_ _Sample_conditions_label $condition1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "cytochrome C" 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 22 1 VAL HA H 3.87 . 1 2 22 1 VAL HB H 1.74 . 1 3 22 1 VAL HG1 H 0.71 . 1 4 22 1 VAL HG2 H 0.79 . 1 5 23 2 ASP H H 8.49 . 1 6 23 2 ASP N N 126.55 . 1 7 23 2 ASP HA H 4.48 . 1 8 23 2 ASP HB2 H 2.38 . 1 9 23 2 ASP HB3 H 2.77 . 1 10 24 3 ALA H H 8.28 . 1 11 24 3 ALA N N 126.91 . 1 12 24 3 ALA HA H 3.42 . 1 13 24 3 ALA HB H 0.89 . 1 14 25 4 GLU H H 7.59 . 1 15 25 4 GLU N N 115.03 . 1 16 25 4 GLU HA H 2.60 . 1 17 25 4 GLU HB2 H 1.55 . 1 18 25 4 GLU HB3 H 1.71 . 1 19 25 4 GLU HG2 H 1.89 . 1 20 25 4 GLU HG3 H 1.96 . 1 21 26 5 ALA H H 7.06 . 1 22 26 5 ALA N N 120.43 . 1 23 26 5 ALA HA H 3.91 . 1 24 26 5 ALA HB H 1.28 . 1 25 27 6 VAL H H 7.55 . 1 26 27 6 VAL N N 118.87 . 1 27 27 6 VAL HA H 3.57 . 1 28 27 6 VAL HB H 1.96 . 1 29 27 6 VAL HG1 H 0.79 . 1 30 27 6 VAL HG2 H 0.86 . 1 31 28 7 VAL H H 8.09 . 1 32 28 7 VAL N N 120.55 . 1 33 28 7 VAL HA H 4.01 . 1 34 28 7 VAL HB H 1.88 . 1 35 28 7 VAL HG1 H 0.76 . 1 36 28 7 VAL HG2 H 1.02 . 1 37 29 8 GLN H H 7.83 . 1 38 29 8 GLN N N 117.07 . 1 39 29 8 GLN HA H 3.86 . 1 40 29 8 GLN HB2 H 2.02 . 1 41 29 8 GLN HB3 H 2.07 . 1 42 29 8 GLN HG2 H 2.34 . 1 43 29 8 GLN HG3 H 2.38 . 1 44 29 8 GLN NE2 N 111.91 . 1 45 29 8 GLN HE21 H 6.83 . 1 46 29 8 GLN HE22 H 7.42 . 1 47 30 9 GLN H H 7.64 . 1 48 30 9 GLN N N 115.63 . 1 49 30 9 GLN HA H 4.21 . 1 50 30 9 GLN HB2 H 2.16 . 1 51 30 9 GLN HB3 H 2.18 . 1 52 30 9 GLN HG2 H 2.33 . 1 53 30 9 GLN HG3 H 2.49 . 1 54 30 9 GLN NE2 N 110.95 . 1 55 30 9 GLN HE21 H 6.77 . 1 56 30 9 GLN HE22 H 7.40 . 1 57 31 10 LYS H H 8.76 . 1 58 31 10 LYS N N 113.83 . 1 59 31 10 LYS HA H 4.86 . 1 60 31 10 LYS HB2 H 2.17 . 1 61 31 10 LYS HB3 H 2.26 . 1 62 31 10 LYS HG2 H 1.51 . 1 63 31 10 LYS HG3 H 1.55 . 1 64 31 10 LYS HD2 H 1.64 . 1 65 31 10 LYS HD3 H 1.80 . 1 66 31 10 LYS HE2 H 3.06 . 1 67 32 11 CYS H H 8.77 . 1 68 32 11 CYS N N 114.98 . 1 69 32 11 CYS HA H 6.04 . 1 70 32 11 CYS HB2 H 2.45 . 1 71 32 11 CYS HB3 H 2.58 . 1 72 33 12 ILE H H 6.96 . 1 73 33 12 ILE N N 110.47 . 1 74 33 12 ILE HA H 3.20 . 1 75 33 12 ILE HB H 1.29 . 1 76 33 12 ILE CG2 C 0.79 . 1 77 33 12 ILE HG12 H 1.04 . 1 78 33 12 ILE HD1 H 0.15 . 1 79 34 13 SER H H 8.52 . 1 80 34 13 SER N N 119.35 . 1 81 34 13 SER HA H 3.87 . 1 82 34 13 SER HB2 H 3.83 . 1 83 34 13 SER HB3 H 3.90 . 1 84 35 14 CYS H H 6.10 . 1 85 35 14 CYS N N 114.67 . 1 86 35 14 CYS HA H 4.37 . 1 87 35 14 CYS HB2 H 2.06 . 1 88 35 14 CYS HB3 H 0.74 . 1 89 36 15 HIS H H 6.12 . 1 90 36 15 HIS N N 112.87 . 1 91 36 15 HIS HA H 2.58 . 1 92 36 15 HIS HB2 H 1.30 . 1 93 36 15 HIS HB3 H 0.87 . 1 94 36 15 HIS ND1 N 164.58 . 1 95 36 15 HIS HD1 H 9.56 . 1 96 36 15 HIS HD2 H 0.47 . 1 97 36 15 HIS HE1 H 0.50 . 1 98 37 16 GLY H H 7.08 . 1 99 37 16 GLY N N 106.75 . 1 100 37 16 GLY HA2 H 3.20 . 1 101 37 16 GLY HA3 H 3.92 . 1 102 38 17 GLY H H 8.31 . 1 103 38 17 GLY N N 108.07 . 1 104 38 17 GLY HA2 H 3.44 . 1 105 38 17 GLY HA3 H 3.67 . 1 106 39 18 ASP H H 7.42 . 1 107 39 18 ASP N N 115.87 . 1 108 39 18 ASP HA H 4.46 . 1 109 39 18 ASP HB2 H 2.36 . 1 110 39 18 ASP HB3 H 2.78 . 1 111 40 19 LEU H H 7.46 . 1 112 40 19 LEU N N 109.03 . 1 113 40 19 LEU HA H 3.15 . 1 114 40 19 LEU HB2 H 1.01 . 1 115 40 19 LEU HB3 H 1.07 . 1 116 40 19 LEU HD1 H 0.15 . 1 117 40 19 LEU HD2 H 0.62 . 1 118 40 19 LEU HG H 1.79 . 1 119 41 20 THR H H 7.39 . 1 120 41 20 THR N N 105.67 . 1 121 41 20 THR HA H 3.95 . 1 122 41 20 THR HB H 4.25 . 1 123 41 20 THR HG2 H 0.81 . 1 124 42 21 GLY H H 7.61 . 1 125 42 21 GLY N N 111.31 . 1 126 42 21 GLY HA2 H 2.60 . 1 127 42 21 GLY HA3 H 3.98 . 1 128 43 22 ALA H H 7.48 . 1 129 43 22 ALA N N 125.59 . 1 130 43 22 ALA HA H 3.98 . 1 131 43 22 ALA HB H 0.82 . 1 132 44 23 SER H H 7.76 . 1 133 44 23 SER N N 118.63 . 1 134 44 23 SER HA H 4.08 . 1 135 44 23 SER HB2 H 3.78 . 1 136 44 23 SER HB3 H 3.91 . 1 137 45 24 ALA H H 7.30 . 1 138 45 24 ALA N N 125.11 . 1 139 45 24 ALA HA H 4.17 . 1 140 45 24 ALA HB H -1.64 . 1 141 46 25 PRO HA H 3.91 . 1 142 46 25 PRO HB2 H 2.12 . 1 143 46 25 PRO HB3 H 2.17 . 1 144 46 25 PRO HG2 H 1.48 . 1 145 46 25 PRO HG3 H 1.786 . 1 146 46 25 PRO HD2 H 2.41 . 1 147 46 25 PRO HD3 H 3.49 . 1 148 47 26 ALA H H 7.92 . 1 149 47 26 ALA N N 120.31 . 1 150 47 26 ALA HA H 3.37 . 1 151 47 26 ALA HB H 1.10 . 1 152 48 27 ILE H H 7.77 . 1 153 48 27 ILE N N 112.15 . 1 154 48 27 ILE HA H 4.17 . 1 155 48 27 ILE HB H 1.82 . 1 156 48 27 ILE HG2 H -0.84 . 1 157 48 27 ILE HG12 H -0.95 . 1 158 48 27 ILE HG13 H -1.37 . 1 159 48 27 ILE HD1 H 0.41 . 1 160 49 28 ASP H H 8.25 . 1 161 49 28 ASP N N 119.98 . 1 162 49 28 ASP HA H 3.60 . 1 163 49 28 ASP HB2 H 2.13 . 1 164 49 28 ASP HB3 H 2.31 . 1 165 50 29 LYS H H 7.72 . 1 166 50 29 LYS N N 117.43 . 1 167 50 29 LYS HA H 4.22 . 1 168 50 29 LYS HB2 H 1.17 . 1 169 50 29 LYS HB3 H 1.69 . 1 170 50 29 LYS HG2 H 0.86 . 1 171 50 29 LYS HG3 H 0.98 . 1 172 50 29 LYS HD2 H 1.26 . 1 173 50 29 LYS HD3 H 1.42 . 1 174 50 29 LYS HE2 H 2.72 . 1 175 51 30 ALA H H 7.13 . 1 176 51 30 ALA N N 121.03 . 1 177 51 30 ALA HA H 4.24 . 1 178 51 30 ALA HB H 1.55 . 1 179 52 31 GLY H H 8.29 . 1 180 52 31 GLY N N 103.99 . 1 181 52 31 GLY HA2 H 3.67 . 1 182 52 31 GLY HA3 H 4.37 . 1 183 53 32 ALA H H 7.97 . 1 184 53 32 ALA N N 120.67 . 1 185 53 32 ALA HA H 4.16 . 1 186 53 32 ALA HB H 1.40 . 1 187 54 33 ASN H H 7.49 . 1 188 54 33 ASN N N 113.35 . 1 189 54 33 ASN HA H 4.59 . 1 190 54 33 ASN HB2 H 2.21 . 1 191 54 33 ASN HB3 H 2.34 . 1 192 54 33 ASN ND2 N 113.59 . 1 193 54 33 ASN HD21 H 6.74 . 1 194 54 33 ASN HD22 H 7.25 . 1 195 55 34 TYR H H 8.07 . 1 196 55 34 TYR N N 118.27 . 1 197 55 34 TYR HA H 5.02 . 1 198 55 34 TYR HB2 H 2.58 . 1 199 55 34 TYR HB3 H 3.32 . 1 200 55 34 TYR HD1 H 7.29 . 1 201 55 34 TYR HE2 H 6.97 . 1 202 56 35 SER H H 9.11 . 1 203 56 35 SER N N 114.91 . 1 204 56 35 SER HA H 4.56 . 1 205 56 35 SER HB2 H 3.96 . 1 206 56 35 SER HB3 H 4.35 . 1 207 57 36 GLU H H 9.02 . 1 208 57 36 GLU N N 121.63 . 1 209 57 36 GLU HA H 3.67 . 1 210 57 36 GLU HB2 H 1.85 . 1 211 57 36 GLU HB3 H 1.99 . 1 212 57 36 GLU HG2 H 1.89 . 1 213 58 37 GLU H H 8.68 . 1 214 58 37 GLU N N 116.23 . 1 215 58 37 GLU HA H 3.81 . 1 216 58 37 GLU HB2 H 1.83 . 1 217 58 37 GLU HB3 H 1.91 . 1 218 58 37 GLU HG2 H 2.19 . 1 219 58 37 GLU HG3 H 2.25 . 1 220 59 38 GLU H H 7.71 . 1 221 59 38 GLU N N 120.07 . 1 222 59 38 GLU HA H 3.94 . 1 223 59 38 GLU HB2 H 2.04 . 1 224 59 38 GLU HB3 H 2.62 . 1 225 59 38 GLU HG2 H 2.30 . 1 226 59 38 GLU HG3 H 2.35 . 1 227 60 39 ILE H H 8.37 . 1 228 60 39 ILE N N 119.71 . 1 229 60 39 ILE HA H 3.36 . 1 230 60 39 ILE HB H 1.91 . 1 231 60 39 ILE HG2 H 0.76 . 1 232 60 39 ILE HG12 H 1.18 . 1 233 60 39 ILE HD1 H 0.68 . 1 234 61 40 LEU H H 8.38 . 1 235 61 40 LEU N N 119.71 . 1 236 61 40 LEU HA H 3.69 . 1 237 61 40 LEU HB2 H 1.19 . 1 238 61 40 LEU HB3 H 1.84 . 1 239 61 40 LEU HD1 H 0.64 . 1 240 61 40 LEU HD2 H 0.80 . 1 241 61 40 LEU HG H 1.40 . 1 242 62 41 ASP H H 7.41 . 1 243 62 41 ASP N N 116.59 . 1 244 62 41 ASP HA H 4.01 . 1 245 62 41 ASP HB2 H 2.50 . 1 246 62 41 ASP HB3 H 2.54 . 1 247 63 42 ILE H H 7.24 . 1 248 63 42 ILE N N 120.43 . 1 249 63 42 ILE HA H 2.54 . 1 250 63 42 ILE HB H 1.26 . 1 251 63 42 ILE HG2 H -1.22 . 1 252 63 42 ILE HG12 H 0.25 . 1 253 63 42 ILE HG13 H 1.31 . 1 254 63 42 ILE HD1 H 0.15 . 1 255 64 43 ILE H H 7.55 . 1 256 64 43 ILE N N 116.23 . 1 257 64 43 ILE HA H 2.25 . 1 258 64 43 ILE HB H 1.47 . 1 259 64 43 ILE HG2 H 0.48 . 1 260 64 43 ILE HG12 H 0.38 . 1 261 64 43 ILE HG13 H 1.74 . 1 262 64 43 ILE HD1 H 0.93 . 1 263 65 44 LEU H H 8.56 . 1 264 65 44 LEU N N 115.63 . 1 265 65 44 LEU HA H 3.70 . 1 266 65 44 LEU HB2 H 1.02 . 1 267 65 44 LEU HB3 H 1.49 . 1 268 65 44 LEU HD1 H 0.49 . 1 269 65 44 LEU HD2 H 1.58 . 1 270 65 44 LEU HG H 0.65 . 1 271 66 45 ASN H H 8.20 . 1 272 66 45 ASN N N 112.51 . 1 273 66 45 ASN HA H 4.46 . 1 274 66 45 ASN HB2 H 2.39 . 1 275 66 45 ASN HB3 H 2.46 . 1 276 66 45 ASN ND2 N 115.99 . 1 277 66 45 ASN HD21 H 6.76 . 1 278 66 45 ASN HD22 H 7.50 . 1 279 67 46 GLY H H 7.48 . 1 280 67 46 GLY N N 111.91 . 1 281 67 46 GLY HA2 H 2.06 . 1 282 67 46 GLY HA3 H 3.21 . 1 283 68 47 GLN H H 6.47 . 1 284 68 47 GLN N N 114.55 . 1 285 68 47 GLN HA H 3.73 . 1 286 68 47 GLN HB2 H 0.88 . 1 287 68 47 GLN HB3 H 1.61 . 1 288 68 47 GLN HG2 H 1.82 . 1 289 68 47 GLN HG3 H 1.90 . 1 290 68 47 GLN NE2 N 110.80 . 1 291 68 47 GLN HE21 H 6.88 . 1 292 68 47 GLN HE22 H 8.55 . 1 293 69 48 GLY H H 8.68 . 1 294 69 48 GLY N N 115.15 . 1 295 69 48 GLY HA2 H 3.44 . 1 296 69 48 GLY HA3 H 3.74 . 1 297 70 49 GLY H H 9.62 . 1 298 70 49 GLY N N 114.79 . 1 299 70 49 GLY HA2 H 3.85 . 1 300 70 49 GLY HA3 H 3.98 . 1 301 71 50 MET H H 8.10 . 1 302 71 50 MET N N 125.23 . 1 303 71 50 MET HA H 3.06 . 1 304 71 50 MET HB2 H -0.59 . 1 305 71 50 MET HB3 H -2.70 . 1 306 71 50 MET HG2 H -1.77 . 1 307 71 50 MET HG3 H 3.55 . 1 308 71 50 MET HE H -3.18 . 1 309 72 51 PRO HA H 3.74 . 1 310 72 51 PRO HB2 H 1.85 . 1 311 72 51 PRO HG2 H 1.26 . 1 312 72 51 PRO HD2 H 7.67 . 1 313 73 52 GLY H H 7.67 . 1 314 73 52 GLY N N 103.40 . 1 315 73 52 GLY HA2 H 2.66 . 1 316 73 52 GLY HA3 H 3.06 . 1 317 74 53 GLY H H 7.53 . 1 318 74 53 GLY N N 106.03 . 1 319 74 53 GLY HA2 H 3.37 . 1 320 74 53 GLY HA3 H 3.56 . 1 321 75 54 ILE H H 9.50 . 1 322 75 54 ILE N N 124.15 . 1 323 75 54 ILE HA H 3.37 . 1 324 75 54 ILE HB H 1.63 . 1 325 75 54 ILE HG2 H 1.30 . 1 326 75 54 ILE HG12 H 0.79 . 1 327 75 54 ILE HG13 H 0.88 . 1 328 75 54 ILE HD1 H 0.40 . 1 329 76 55 ALA H H 6.62 . 1 330 76 55 ALA N N 113.95 . 1 331 76 55 ALA HA H 4.42 . 1 332 76 55 ALA HB H 0.89 . 1 333 77 56 LYS H H 8.42 . 1 334 77 56 LYS N N 114.79 . 1 335 77 56 LYS HA H 4.32 . 1 336 77 56 LYS HB2 H 1.43 . 1 337 77 56 LYS HB3 H 1.65 . 1 338 77 56 LYS HG2 H 1.40 . 1 339 77 56 LYS HD2 H 1.13 . 1 340 77 56 LYS HE2 H 2.81 . 1 341 78 57 GLY H H 8.42 . 1 342 78 57 GLY N N 107.59 . 1 343 78 57 GLY HA2 H 3.64 . 1 344 78 57 GLY HA3 H 3.74 . 1 345 79 58 ALA H H 8.69 . 1 346 79 58 ALA N N 127.15 . 1 347 79 58 ALA HA H 4.04 . 1 348 79 58 ALA HB H 1.35 . 1 349 80 59 GLU H H 8.20 . 1 350 80 59 GLU N N 117.91 . 1 351 80 59 GLU HA H 3.89 . 1 352 80 59 GLU HB2 H 2.04 . 1 353 80 59 GLU HB3 H 2.28 . 1 354 80 59 GLU HG2 H 2.40 . 1 355 80 59 GLU HG3 H 2.46 . 1 356 81 60 ALA H H 6.82 . 1 357 81 60 ALA N N 120.19 . 1 358 81 60 ALA HA H 3.52 . 1 359 81 60 ALA HB H 0.95 . 1 360 82 61 GLU H H 7.94 . 1 361 82 61 GLU N N 114.91 . 1 362 82 61 GLU HA H 3.73 . 1 363 82 61 GLU HB2 H 1.91 . 1 364 82 61 GLU HB3 H 1.95 . 1 365 82 61 GLU HG2 H 2.11 . 1 366 82 61 GLU HG3 H 2.28 . 1 367 83 62 ALA H H 7.91 . 1 368 83 62 ALA N N 120.67 . 1 369 83 62 ALA HA H 4.19 . 1 370 83 62 ALA HB H 1.44 . 1 371 84 63 VAL H H 8.13 . 1 372 84 63 VAL N N 119.23 . 1 373 84 63 VAL HA H 3.61 . 1 374 84 63 VAL HB H 2.13 . 1 375 84 63 VAL HG1 H 1.10 . 1 376 84 63 VAL HG2 H 1.21 . 1 377 85 64 ALA H H 8.60 . 1 378 85 64 ALA N N 121.75 . 1 379 85 64 ALA HA H 4.08 . 1 380 85 64 ALA HB H 1.49 . 1 381 86 65 ALA H H 7.69 . 1 382 86 65 ALA N N 117.31 . 1 383 86 65 ALA HA H 3.86 . 1 384 86 65 ALA HB H 1.44 . 1 385 87 66 TRP H H 7.81 . 1 386 87 66 TRP N N 119.23 . 1 387 87 66 TRP HA H 4.18 . 1 388 87 66 TRP HB2 H 3.15 . 1 389 87 66 TRP HB3 H 3.38 . 1 390 87 66 TRP HD1 H 7.33 . 1 391 87 66 TRP NE1 N 130.14 . 1 392 87 66 TRP HE1 H 10.21 . 1 393 87 66 TRP HZ2 H 6.73 . 1 394 87 66 TRP HZ3 H 7.33 . 1 395 87 66 TRP HH2 H 7.02 . 1 396 88 67 LEU H H 9.07 . 1 397 88 67 LEU N N 118.63 . 1 398 88 67 LEU HA H 3.76 . 1 399 88 67 LEU HB2 H 1.70 . 1 400 88 67 LEU HB3 H 2.01 . 1 401 88 67 LEU HD1 H 1.10 . 1 402 88 67 LEU HD2 H 1.22 . 1 403 88 67 LEU HG H 2.13 . 1 404 89 68 ALA H H 8.10 . 1 405 89 68 ALA N N 118.03 . 1 406 89 68 ALA HA H 3.78 . 1 407 89 68 ALA HB H 1.49 . 1 408 90 69 GLU H H 6.71 . 1 409 90 69 GLU N N 111.67 . 1 410 90 69 GLU HA H 4.09 . 1 411 90 69 GLU HB2 H 1.74 . 1 412 90 69 GLU HB3 H 2.09 . 1 413 90 69 GLU HG2 H 2.16 . 1 414 90 69 GLU HG3 H 2.37 . 1 415 91 70 LYS H H 7.46 . 1 416 91 70 LYS N N 122.83 . 1 417 91 70 LYS HA H 3.98 . 1 418 91 70 LYS HB2 H 1.70 . 1 419 91 70 LYS HB3 H 1.89 . 1 420 91 70 LYS HG2 H 0.83 . 1 421 91 70 LYS HG3 H 1.40 . 1 422 91 70 LYS HD2 H 1.58 . 1 423 91 70 LYS HE2 H 2.12 . 1 424 92 71 LYS H H 7.19 . 1 425 92 71 LYS N N 126.19 . 1 426 92 71 LYS HA H 3.98 . 1 427 92 71 LYS HB2 H 1.39 . 1 428 92 71 LYS HB3 H 1.59 . 1 429 92 71 LYS HG2 H 0.97 . 1 430 92 71 LYS HD2 H 0.90 . 1 431 92 71 LYS HE2 H 2.82 . 1 stop_ save_ save_csheme _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample2 stop_ _Sample_conditions_label $condition1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "heme cofactor" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . HEME QM1 H 3.30 . . 2 . HEME QM8 H 2.94 . . 3 . HEME HDM H 8.99 . . 4 . HEME HT2A H 5.83 . . 5 . HEME QT2 H 1.82 . . 6 . HEME HAM H 9.79 . . 7 . HEME QM3 H 3.77 . . 8 . HEME QT4 H 2.19 . . 9 . HEME HT4A H 6.25 . . 10 . HEME HBM H 9.37 . . 11 . HEME QM5 H 3.30 . . 12 . HEME HGM H 9.58 . . 13 . HEME HAP61 H 4.31 . . 14 . HEME HAP62 H 3.85 . . 15 . HEME HBP63 H 3.07 . . 16 . HEME HBP64 H 2.82 . . 17 . HEME HAP71 H 4.39 . . 18 . HEME HAP72 H 4.49 . . 19 . HEME HBP73 H 3.17 . . 20 . HEME HBP74 H 2.94 . . stop_ save_