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 ; _BMRB_accession_number 5597 _BMRB_flat_file_name bmr5597.str _Entry_type original _Submission_date 2002-11-25 _Accession_date 2002-11-25 _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 Bartalesi Ilaria . . 2 Bertini Ivano . . 3 Rosato Antonio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 375 "13C chemical shifts" 1 "15N chemical shifts" 75 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-07-15 update BMRB 'added time domain data' 2003-02-21 original author 'original release' 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_full . _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 _CAS_abstract_code . _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 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 739 _Page_last 745 _Year 2003 _Details . 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' $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cytc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome c' _Abbreviation_common cytc _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # 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 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 EMBL CAC39450 'cytochrome c553 [Sporosarcina pasteurii]' 100.00 85 98.59 98.59 1.98e-31 SWISS-PROT P82599 'Cytochrome c-553 (Cytochrome c553)' 100.00 92 100.00 100.00 3.31e-32 PDB 1K3H 'Nmr Solution Structure Of Oxidized Cytochrome C-553 From Bacillus Pasteurii' 100.00 71 100.00 100.00 8.94e-32 PDB 1N9C 'Structure And Dynamics Of Reduced Bacillus Pasteurii Cytochrome C: Oxidation State Dependent Properties And Implications For Electron Transfer Processes' 100.00 71 100.00 100.00 8.94e-32 PDB 1C75 '0.97 A "ab Initio" Crystal Structure Of Cytochrome C-553 From Bacillus Pasteurii' 98.59 71 100.00 100.00 3.69e-31 PDB 1K3G 'Nmr Solution Structure Of Oxidized Cytochrome C-553 From Bacillus Pasteurii' 98.59 71 100.00 100.00 3.15e-31 BMRB 5172 'Bacillus pasteurii cytochrome' 100.00 71 100.00 100.00 8.94e-32 PDB 1B7V 'Structure Of The C-553 Cytochrome From Bacillus Pasteurii To 1.7 A Resolution' 100.00 71 100.00 100.00 8.94e-32 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEM (PROTOPORPHYRIN IX CONTAINING FE)" _BMRB_code . _PDB_code HEM _Molecular_mass 616.487 _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 Mon Jul 25 14:22:15 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 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 . ? 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 . ? 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 . ? 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 . ? NA NA N . 0 . ? NB NB N . 0 . ? NC NC N . 0 . ? ND ND N . 0 . ? FE FE FE . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA HMA H . 0 . ? HMAA HMAA H . 0 . ? HMAB HMAB H . 0 . ? HAA HAA H . 0 . ? HAAA HAAA H . 0 . ? HBA HBA H . 0 . ? HBAA HBAA H . 0 . ? HMB HMB H . 0 . ? HMBA HMBA H . 0 . ? HMBB HMBB H . 0 . ? HAB HAB H . 0 . ? HBB HBB H . 0 . ? HBBA HBBA H . 0 . ? HMC HMC H . 0 . ? HMCA HMCA H . 0 . ? HMCB HMCB H . 0 . ? HAC HAC H . 0 . ? HBC HBC H . 0 . ? HBCA HBCA H . 0 . ? HMD HMD H . 0 . ? HMDA HMDA H . 0 . ? HMDB HMDB H . 0 . ? HAD HAD H . 0 . ? HADA HADA H . 0 . ? HBD HBD H . 0 . ? HBDA HBDA H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HHA HHA 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 CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? DOUB C1A C2A ? ? SING C1A NA ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING C4A NA ? ? SING CMA HMA ? ? SING CMA HMAA ? ? SING CMA HMAB ? ? SING CAA CBA ? ? SING CAA HAA ? ? SING CAA HAAA ? ? SING CBA CGA ? ? SING CBA HBA ? ? SING CBA HBAA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING C1B C2B ? ? SING C1B NB ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? DOUB C4B NB ? ? SING CMB HMB ? ? SING CMB HMBA ? ? SING CMB HMBB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB ? ? SING CBB HBBA ? ? SING C1C C2C ? ? SING C1C NC ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING C4C NC ? ? SING CMC HMC ? ? SING CMC HMCA ? ? SING CMC HMCB ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC ? ? SING CBC HBCA ? ? SING C1D C2D ? ? DOUB C1D ND ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING C4D ND ? ? SING CMD HMD ? ? SING CMD HMDA ? ? SING CMD HMDB ? ? SING CAD CBD ? ? SING CAD HAD ? ? SING CAD HADA ? ? SING CBD CGD ? ? SING CBD HBD ? ? SING CBD HBDA ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2A H2A ? ? SING O2D H2D ? ? SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? 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 $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 _Details . 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 _Details . 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 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNHB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_N15_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'N15 HSQC' _Sample_label . save_ save_NMR_spectrometer_expt_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spectrometer_expt_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'N15 HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition1 _Saveframe_category sample_conditions _Details . 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 _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $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_csset1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample2 stop_ _Sample_conditions_label $condition1 _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 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 _Details . loop_ _Sample_label $sample2 stop_ _Sample_conditions_label $condition1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'heme cofactor' _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 HEM QM1 H 3.30 . . 2 . 1 HEM QM8 H 2.94 . . 3 . 1 HEM HDM H 8.99 . . 4 . 1 HEM HT2A H 5.83 . . 5 . 1 HEM QT2 H 1.82 . . 6 . 1 HEM HAM H 9.79 . . 7 . 1 HEM QM3 H 3.77 . . 8 . 1 HEM QT4 H 2.19 . . 9 . 1 HEM HT4A H 6.25 . . 10 . 1 HEM HBM H 9.37 . . 11 . 1 HEM QM5 H 3.30 . . 12 . 1 HEM HGM H 9.58 . . 13 . 1 HEM HAP61 H 4.31 . . 14 . 1 HEM HAP62 H 3.85 . . 15 . 1 HEM HBP63 H 3.07 . . 16 . 1 HEM HBP64 H 2.82 . . 17 . 1 HEM HAP71 H 4.39 . . 18 . 1 HEM HAP72 H 4.49 . . 19 . 1 HEM HBP73 H 3.17 . . 20 . 1 HEM HBP74 H 2.94 . . stop_ save_