data_5172 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Chemical Shift Assignments of oxidized cytochrome c553 from B. pasteurii ; _BMRB_accession_number 5172 _BMRB_flat_file_name bmr5172.str _Entry_type original _Submission_date 2001-10-05 _Accession_date 2001-10-05 _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 Banci Lucia . . 2 Bertini Ivano . . 3 Ciurli Stefano . . 4 Dikiy Alexander . . 5 Dittmer Jens . . 6 Rosato Antonio . . 7 Sciara Giuliano . . 8 Thompsett Andrew R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 391 "15N chemical shifts" 73 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-06 original author . stop_ _Original_release_date 2002-05-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Solution Structure, Backbone Mobility, and Homology Modeling of C-Type Cytochromes from Gram-positive Bacteria ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21929523 _PubMed_ID 11933230 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci Lucia . . 2 Bertini Ivano . . 3 Ciurli Stefano . . 4 Dikiy Alexander . . 5 Dittmer Jens . . 6 Rosato Antonio . . 7 Sciara Giuliano . . 8 Thompsett Andrew R. . stop_ _Journal_abbreviation Chembiochem _Journal_volume 3 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 299 _Page_last 310 _Year 2002 _Details . loop_ _Keyword 'Oxidized cytochrome c553 from Bacillus pasteurii' stop_ save_ ################################## # Molecular system description # ################################## save_system_B_pasteurii_cyt_c553 _Saveframe_category molecular_system _Mol_system_name 'Oxidized cytochrome c553 from Bacillus pasteurii' _Abbreviation_common 'B. pasteurii cyt c553' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'B. pasteurii cyt c553' $cyt_c553 Heme $HEM_ox 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_c553 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Bacillus pasteurii cytochrome' _Abbreviation_common 'cyt c553' _Molecular_mass . _Mol_thiol_state 'all other bound' _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 5597 'cytochrome c' 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_ox _Saveframe_category ligand _Mol_type non-polymer _Name_common 'PROTOPORPHYRIN IX CONTAINING FE' _Abbreviation_common heme _BMRB_code HEM_ox _PDB_code HEM _Molecular_mass . _Mol_charge 1- _Mol_paramagnetic yes _Mol_aromatic yes _Details . _Synonym HEME loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 3+ 3+ ? CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? NA 'N A' 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 'N B' 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 'N C' 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 'N D' 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 . ? 1HMA 1HMA H . 0 . ? 2HMA 2HMA H . 0 . ? 3HMA 3HMA H . 0 . ? 1HAA 1HAA H . 0 . ? 2HAA 2HAA H . 0 . ? 1HBA 1HBA H . 0 . ? 2HBA 2HBA H . 0 . ? H2A H2A H . 0 . ? 1HMB 1HMB H . 0 . ? 2HMB 2HMB H . 0 . ? 3HMB 3HMB H . 0 . ? HAB HAB H . 0 . ? 1HBB 1HBB H . 0 . ? 2HBB 2HBB H . 0 . ? 1HMC 1HMC H . 0 . ? 2HMC 2HMC H . 0 . ? 3HMC 3HMC H . 0 . ? HAC HAC H . 0 . ? 1HBC 1HBC H . 0 . ? 2HBC 2HBC H . 0 . ? 1HMD 1HMD H . 0 . ? 2HMD 2HMD H . 0 . ? 3HMD 3HMD H . 0 . ? 1HAD 1HAD H . 0 . ? 2HAD 2HAD H . 0 . ? 1HBD 1HBD H . 0 . ? 2HBD 2HBD 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 ? ? 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 ? ? DOUB 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 ? ? DOUB 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_ _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_c553 'Bacillus pasteurii' 1474 Prokaryota . 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 $cyt_c553 'recombinant technology' . 'Escherichia coli.' Escherichia coli DH5(.PET20b) 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_c553 . mM 1 1.5 '[U-98% 15N]' 'phosphate buffer' 10 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 loop_ _Task 'data processing' stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Task 'data analysis' assignment stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 400 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_1H-15N_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1D_NOE_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1D NOE' _Sample_label . save_ save_3D_NHHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NHHA' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1D NOE' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NHHA' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details 'The temperature range is 288-298 K.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 n/a temperature 293 0.1 K 'ionic strength' 10 . mM 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 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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 'B. pasteurii cyt c553' _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 VAL HA H 3.71 0.02 1 2 . 1 VAL HB H 1.64 0.02 1 3 . 1 VAL HG1 H 0.57 0.02 2 4 . 1 VAL HG2 H 0.73 0.02 2 5 . 2 ASP H H 8.43 0.02 1 6 . 2 ASP HA H 4.46 0.02 1 7 . 2 ASP HB2 H 2.37 0.02 1 8 . 2 ASP HB3 H 2.74 0.02 1 9 . 2 ASP N N 126.24 0.05 1 10 . 3 ALA H H 8.19 0.02 1 11 . 3 ALA HA H 3.12 0.02 1 12 . 3 ALA HB H 0.62 0.02 1 13 . 3 ALA N N 126.81 0.05 1 14 . 4 GLU H H 7.57 0.02 1 15 . 4 GLU HA H 2.48 0.02 1 16 . 4 GLU HB2 H 2.01 0.02 2 17 . 4 GLU HB3 H 1.97 0.02 2 18 . 4 GLU HG2 H 1.74 0.02 2 19 . 4 GLU HG3 H 1.55 0.02 2 20 . 4 GLU N N 115.33 0.05 1 21 . 5 ALA H H 7.05 0.02 1 22 . 5 ALA HA H 3.91 0.02 1 23 . 5 ALA HB H 1.25 0.02 1 24 . 5 ALA N N 120.88 0.05 1 25 . 6 VAL H H 7.43 0.02 1 26 . 6 VAL HA H 3.28 0.02 1 27 . 6 VAL HB H 1.49 0.02 1 28 . 6 VAL HG1 H 0.17 0.02 1 29 . 6 VAL HG2 H 0.61 0.02 1 30 . 6 VAL N N 118.54 0.05 1 31 . 7 VAL H H 7.80 0.02 1 32 . 7 VAL HA H 3.11 0.02 1 33 . 7 VAL HB H 1.77 0.02 1 34 . 7 VAL HG1 H 0.78 0.02 1 35 . 7 VAL HG2 H 0.25 0.02 1 36 . 7 VAL N N 120.50 0.05 1 37 . 8 GLN H H 7.91 0.02 1 38 . 8 GLN HA H 4.17 0.02 1 39 . 8 GLN HB2 H 2.16 0.02 1 40 . 8 GLN HB3 H 2.26 0.02 1 41 . 8 GLN HG2 H 2.61 0.02 2 42 . 8 GLN HG3 H 2.54 0.02 2 43 . 8 GLN HE21 H 7.81 0.02 1 44 . 8 GLN HE22 H 7.25 0.02 1 45 . 8 GLN N N 118.26 0.05 1 46 . 8 GLN NE2 N 112.21 0.05 1 47 . 9 GLN H H 7.61 0.02 1 48 . 9 GLN HA H 4.19 0.02 1 49 . 9 GLN HB2 H 2.00 0.02 2 50 . 9 GLN HB3 H 2.27 0.02 2 51 . 9 GLN HG2 H 2.44 0.02 2 52 . 9 GLN HE21 H 7.43 0.02 2 53 . 9 GLN HE22 H 6.77 0.02 2 54 . 9 GLN N N 115.87 0.05 1 55 . 9 GLN NE2 N 111.12 0.05 1 56 . 10 LYS H H 8.34 0.02 1 57 . 10 LYS HA H 4.31 0.02 1 58 . 10 LYS HB2 H 1.07 0.02 2 59 . 10 LYS HB3 H 0.86 0.02 2 60 . 10 LYS HG2 H 1.21 0.02 2 61 . 10 LYS HG3 H 0.97 0.02 2 62 . 10 LYS HD2 H 0.93 0.02 2 63 . 10 LYS HE2 H 2.74 0.02 2 64 . 10 LYS N N 112.80 0.05 1 65 . 11 CYS H H 8.54 0.02 1 66 . 11 CYS HA H 4.63 0.02 1 67 . 11 CYS HB2 H 2.88 0.02 1 68 . 11 CYS HB3 H 2.92 0.02 1 69 . 11 CYS N N 113.82 0.05 1 70 . 12 ILE H H 7.84 0.02 1 71 . 12 ILE HA H 5.86 0.02 1 72 . 12 ILE HB H 2.63 0.02 1 73 . 12 ILE HG12 H 1.94 0.02 2 74 . 12 ILE HG13 H 1.86 0.02 2 75 . 12 ILE HG2 H 1.79 0.02 1 76 . 12 ILE HD1 H 1.37 0.02 1 77 . 12 ILE N N 113.75 0.05 1 78 . 13 SER HA H 4.77 0.02 1 79 . 13 SER HB2 H 4.34 0.02 2 80 . 13 SER HB3 H 4.28 0.02 2 81 . 14 CYS H H 8.65 0.02 1 82 . 14 CYS HB2 H 6.94 0.02 1 83 . 14 CYS HB3 H 3.72 0.02 1 84 . 14 CYS N N 117.58 0.05 1 85 . 15 HIS H H 13.01 0.02 1 86 . 15 HIS HA H 10.34 0.02 1 87 . 15 HIS HB2 H 10.16 0.02 1 88 . 15 HIS HB3 H 15.88 0.02 1 89 . 15 HIS HD1 H 15.92 0.02 1 90 . 15 HIS HD2 H 26.69 0.02 1 91 . 15 HIS HE1 H -20.25 0.02 1 92 . 15 HIS N N 116.43 0.05 1 93 . 16 GLY H H 10.34 0.02 1 94 . 16 GLY HA2 H 4.92 0.02 2 95 . 16 GLY HA3 H 5.86 0.02 2 96 . 16 GLY N N 112.73 0.05 1 97 . 17 GLY H H 9.55 0.02 1 98 . 17 GLY HA2 H 4.43 0.02 1 99 . 17 GLY HA3 H 4.50 0.02 1 100 . 17 GLY N N 110.61 0.05 1 101 . 18 ASP H H 8.45 0.02 1 102 . 18 ASP HA H 5.20 0.02 1 103 . 18 ASP HB2 H 3.43 0.02 2 104 . 18 ASP HB3 H 2.97 0.02 2 105 . 18 ASP N N 117.17 0.05 1 106 . 19 LEU H H 8.98 0.02 1 107 . 19 LEU HA H 5.60 0.02 1 108 . 19 LEU HB2 H 2.85 0.02 1 109 . 19 LEU HB3 H 2.47 0.02 1 110 . 19 LEU HG H 2.17 0.02 1 111 . 19 LEU HD1 H 1.16 0.02 2 112 . 19 LEU HD2 H 1.83 0.02 2 113 . 19 LEU N N 110.13 0.05 1 114 . 20 THR H H 8.77 0.02 1 115 . 20 THR HA H 5.08 0.02 1 116 . 20 THR HG2 H 1.52 0.02 1 117 . 20 THR N N 107.75 0.05 1 118 . 21 GLY H H 9.75 0.02 1 119 . 21 GLY HA2 H 5.38 0.02 1 120 . 21 GLY HA3 H 5.59 0.02 1 121 . 21 GLY N N 112.80 0.05 1 122 . 22 ALA H H 9.81 0.02 1 123 . 22 ALA HA H 5.08 0.02 1 124 . 22 ALA HB H 2.38 0.02 1 125 . 22 ALA N N 126.70 0.05 1 126 . 23 SER H H 9.02 0.02 1 127 . 23 SER HA H 4.31 0.02 1 128 . 23 SER HB2 H 4.00 0.02 2 129 . 23 SER HB3 H 3.73 0.02 2 130 . 23 SER HG H 6.10 0.02 1 131 . 23 SER N N 119.70 0.05 1 132 . 24 ALA H H 9.31 0.02 1 133 . 24 ALA HA H 3.65 0.02 1 134 . 24 ALA HB H 0.44 0.02 1 135 . 24 ALA N N 124.62 0.05 1 136 . 25 PRO HA H 4.74 0.02 1 137 . 25 PRO HB2 H 1.10 0.02 1 138 . 25 PRO HB3 H 2.00 0.02 1 139 . 25 PRO HG2 H 0.73 0.02 2 140 . 25 PRO HG3 H -0.25 0.02 2 141 . 25 PRO HD2 H -0.53 0.02 1 142 . 25 PRO HD3 H 1.94 0.02 1 143 . 26 ALA H H 9.19 0.02 1 144 . 26 ALA HA H 5.48 0.02 1 145 . 26 ALA HB H 1.95 0.02 1 146 . 26 ALA N N 123.80 0.05 1 147 . 27 ILE H H 9.91 0.02 1 148 . 27 ILE HA H 4.44 0.02 1 149 . 27 ILE HB H 1.12 0.02 1 150 . 27 ILE HG12 H 3.21 0.02 2 151 . 27 ILE HG13 H 2.05 0.02 2 152 . 27 ILE HG2 H -0.50 0.02 1 153 . 27 ILE HD1 H -1.02 0.02 1 154 . 27 ILE N N 112.38 0.05 1 155 . 28 ASP H H 9.19 0.02 1 156 . 28 ASP HA H 4.01 0.02 1 157 . 28 ASP HB2 H 2.77 0.02 2 158 . 28 ASP HB3 H 2.85 0.02 2 159 . 28 ASP N N 120.73 0.05 1 160 . 29 LYS H H 8.10 0.02 1 161 . 29 LYS HA H 4.26 0.02 1 162 . 29 LYS HB2 H 1.27 0.02 2 163 . 29 LYS HB3 H 1.75 0.02 2 164 . 29 LYS HG2 H 1.19 0.02 2 165 . 29 LYS HG3 H 1.04 0.02 2 166 . 29 LYS HD2 H 1.41 0.02 2 167 . 29 LYS HD3 H 1.58 0.02 2 168 . 29 LYS HE2 H 2.91 0.02 2 169 . 29 LYS N N 117.92 0.05 1 170 . 30 ALA H H 6.87 0.02 1 171 . 30 ALA HA H 3.84 0.02 1 172 . 30 ALA HB H 0.62 0.02 1 173 . 30 ALA N N 120.66 0.05 1 174 . 31 GLY H H 8.05 0.02 1 175 . 31 GLY HA2 H 4.13 0.02 1 176 . 31 GLY HA3 H 3.49 0.02 1 177 . 31 GLY N N 104.18 0.05 1 178 . 32 ALA H H 7.87 0.02 1 179 . 32 ALA HA H 4.14 0.02 1 180 . 32 ALA HB H 1.50 0.02 1 181 . 32 ALA N N 120.59 0.05 1 182 . 33 ASN H H 7.30 0.02 1 183 . 33 ASN HA H 4.52 0.02 1 184 . 33 ASN HB2 H 2.09 0.02 2 185 . 33 ASN HB3 H 2.05 0.02 2 186 . 33 ASN HD21 H 6.69 0.02 2 187 . 33 ASN HD22 H 7.02 0.02 2 188 . 33 ASN N N 113.41 0.05 1 189 . 33 ASN ND2 N 113.24 0.05 1 190 . 34 TYR H H 7.85 0.02 1 191 . 34 TYR HA H 4.93 0.02 1 192 . 34 TYR HB2 H 2.19 0.02 2 193 . 34 TYR HB3 H 3.12 0.02 2 194 . 34 TYR HD1 H 6.98 0.02 3 195 . 34 TYR HE1 H 6.59 0.02 3 196 . 34 TYR N N 118.50 0.05 1 197 . 35 SER H H 9.16 0.02 1 198 . 35 SER HA H 4.49 0.02 1 199 . 35 SER HB2 H 4.38 0.02 2 200 . 35 SER HB3 H 3.99 0.02 2 201 . 35 SER N N 115.12 0.05 1 202 . 36 GLU H H 9.01 0.02 1 203 . 36 GLU HA H 3.45 0.02 1 204 . 36 GLU HB2 H 1.89 0.02 2 205 . 36 GLU HB3 H 1.93 0.02 2 206 . 36 GLU HG2 H 1.81 0.02 2 207 . 36 GLU HG3 H 1.71 0.02 2 208 . 36 GLU N N 121.82 0.05 1 209 . 37 GLU H H 8.75 0.02 1 210 . 37 GLU HA H 3.93 0.02 1 211 . 37 GLU HB2 H 1.98 0.02 2 212 . 37 GLU HB3 H 2.06 0.02 2 213 . 37 GLU HG2 H 2.40 0.02 2 214 . 37 GLU HG3 H 2.34 0.02 2 215 . 37 GLU N N 116.56 0.05 1 216 . 38 GLU H H 7.87 0.02 1 217 . 38 GLU HA H 4.29 0.02 1 218 . 38 GLU HB2 H 2.69 0.02 1 219 . 38 GLU HB3 H 2.23 0.02 1 220 . 38 GLU HG2 H 2.55 0.02 2 221 . 38 GLU HG3 H 2.52 0.02 2 222 . 38 GLU N N 120.38 0.05 1 223 . 39 ILE H H 8.37 0.02 1 224 . 39 ILE HA H 3.09 0.02 1 225 . 39 ILE HB H 1.49 0.02 1 226 . 39 ILE HG12 H 1.00 0.02 2 227 . 39 ILE HG13 H 0.35 0.02 2 228 . 39 ILE HG2 H 0.21 0.02 1 229 . 39 ILE HD1 H 0.10 0.02 1 230 . 39 ILE N N 119.77 0.05 1 231 . 40 LEU H H 8.47 0.02 1 232 . 40 LEU HA H 3.72 0.02 1 233 . 40 LEU HB2 H 1.16 0.02 1 234 . 40 LEU HB3 H 2.05 0.02 1 235 . 40 LEU HG H 1.69 0.02 1 236 . 40 LEU HD1 H 0.70 0.02 1 237 . 40 LEU HD2 H 0.95 0.02 1 238 . 40 LEU N N 120.18 0.05 1 239 . 41 ASP H H 8.01 0.02 1 240 . 41 ASP HA H 4.86 0.02 1 241 . 41 ASP HB2 H 3.36 0.02 2 242 . 41 ASP HB3 H 3.11 0.02 2 243 . 41 ASP N N 118.06 0.05 1 244 . 42 ILE H H 8.50 0.02 1 245 . 42 ILE HA H 5.85 0.02 1 246 . 42 ILE HB H 2.99 0.02 1 247 . 42 ILE HG12 H 2.65 0.02 2 248 . 42 ILE HG2 H 6.23 0.02 1 249 . 42 ILE HD1 H 0.89 0.02 1 250 . 42 ILE N N 121.14 0.05 1 251 . 43 ILE H H 8.81 0.02 1 252 . 43 ILE HA H 5.05 0.02 1 253 . 43 ILE HB H 1.82 0.02 1 254 . 43 ILE HG12 H -1.67 0.02 1 255 . 43 ILE HG13 H 1.11 0.02 1 256 . 43 ILE HG2 H -0.29 0.02 1 257 . 43 ILE HD1 H -0.41 0.02 1 258 . 43 ILE N N 118.20 0.05 1 259 . 44 LEU H H 9.89 0.02 1 260 . 44 LEU HA H 4.63 0.02 1 261 . 44 LEU HB2 H 1.78 0.02 2 262 . 44 LEU HB3 H 2.37 0.02 2 263 . 44 LEU HG H 1.08 0.02 1 264 . 44 LEU HD1 H 2.07 0.02 1 265 . 44 LEU N N 118.06 0.05 1 266 . 45 ASN H H 10.16 0.02 1 267 . 45 ASN HA H 5.86 0.02 1 268 . 45 ASN HB2 H 3.89 0.02 1 269 . 45 ASN HB3 H 3.64 0.02 1 270 . 45 ASN HD21 H 8.62 0.02 2 271 . 45 ASN HD22 H 7.48 0.02 2 272 . 45 ASN N N 114.37 0.05 1 273 . 45 ASN ND2 N 116.83 0.05 1 274 . 46 GLY H H 10.52 0.02 1 275 . 46 GLY HA2 H 8.64 0.02 1 276 . 46 GLY HA3 H 6.88 0.02 1 277 . 46 GLY N N 114.09 0.05 1 278 . 47 GLN H H 11.57 0.02 1 279 . 47 GLN HA H 5.78 0.02 1 280 . 47 GLN HB2 H 4.80 0.02 2 281 . 47 GLN HB3 H 4.73 0.02 2 282 . 47 GLN HG2 H 2.95 0.02 1 283 . 47 GLN HG3 H 3.03 0.02 1 284 . 47 GLN HE21 H 8.55 0.02 1 285 . 47 GLN HE22 H 6.86 0.02 1 286 . 47 GLN N N 118.05 0.05 1 287 . 47 GLN NE2 N 111.42 0.05 1 288 . 48 GLY H H 9.88 0.02 1 289 . 48 GLY HA2 H 3.79 0.02 1 290 . 48 GLY HA3 H 3.86 0.02 1 291 . 48 GLY N N 117.50 0.05 1 292 . 49 GLY H H 9.03 0.02 1 293 . 49 GLY HA2 H 3.68 0.02 2 294 . 49 GLY HA3 H 2.69 0.02 2 295 . 49 GLY N N 114.16 0.05 1 296 . 50 MET H H 9.22 0.02 1 297 . 50 MET HA H 1.80 0.02 1 298 . 50 MET HB2 H -0.30 0.02 2 299 . 50 MET HB3 H 12.39 0.02 2 300 . 50 MET HG2 H -1.10 0.02 2 301 . 50 MET HG3 H -24.70 0.02 2 302 . 50 MET HE H -12.23 0.02 1 303 . 50 MET N N 122.98 0.05 1 304 . 51 PRO HA H 5.62 0.02 1 305 . 51 PRO HB2 H 2.35 0.02 1 306 . 51 PRO HB3 H 2.70 0.02 1 307 . 51 PRO HG2 H 1.82 0.02 1 308 . 51 PRO HD2 H 3.11 0.02 2 309 . 51 PRO HD3 H 2.69 0.02 2 310 . 52 GLY H H 9.76 0.02 1 311 . 52 GLY HA2 H 6.00 0.02 2 312 . 52 GLY HA3 H 4.56 0.02 2 313 . 52 GLY N N 107.12 0.05 1 314 . 53 GLY H H 8.98 0.02 1 315 . 53 GLY HA2 H 4.00 0.02 1 316 . 53 GLY HA3 H 4.22 0.02 1 317 . 53 GLY N N 106.92 0.05 1 318 . 54 ILE H H 10.00 0.02 1 319 . 54 ILE HA H 3.17 0.02 1 320 . 54 ILE HB H 0.76 0.02 1 321 . 54 ILE HG12 H 0.43 0.02 2 322 . 54 ILE HG13 H 1.17 0.02 2 323 . 54 ILE HG2 H -0.41 0.02 1 324 . 54 ILE HD1 H -0.86 0.02 1 325 . 54 ILE N N 123.39 0.05 1 326 . 55 ALA H H 6.57 0.02 1 327 . 55 ALA HA H 4.13 0.02 1 328 . 55 ALA HB H 0.24 0.02 1 329 . 55 ALA N N 113.48 0.05 1 330 . 56 LYS H H 8.40 0.02 1 331 . 56 LYS HA H 4.48 0.02 1 332 . 56 LYS HB2 H 1.52 0.02 2 333 . 56 LYS HB3 H 1.83 0.02 2 334 . 56 LYS HG2 H 1.36 0.02 2 335 . 56 LYS HG3 H 1.20 0.02 2 336 . 56 LYS HD2 H 1.60 0.02 2 337 . 56 LYS HD3 H 1.69 0.02 2 338 . 56 LYS HE2 H 3.04 0.02 2 339 . 56 LYS N N 115.05 0.05 1 340 . 57 GLY H H 8.61 0.02 1 341 . 57 GLY HA2 H 3.75 0.02 2 342 . 57 GLY HA3 H 3.79 0.02 2 343 . 57 GLY N N 108.07 0.05 1 344 . 58 ALA H H 8.72 0.02 1 345 . 58 ALA HA H 4.05 0.02 1 346 . 58 ALA HB H 1.35 0.02 1 347 . 58 ALA N N 126.75 0.05 1 348 . 59 GLU H H 8.14 0.02 1 349 . 59 GLU HA H 3.71 0.02 1 350 . 59 GLU HB2 H 2.29 0.02 1 351 . 59 GLU HB3 H 2.12 0.02 1 352 . 59 GLU HG2 H 1.00 0.02 2 353 . 59 GLU HG3 H 1.80 0.02 2 354 . 59 GLU N N 117.51 0.05 1 355 . 60 ALA H H 6.66 0.02 1 356 . 60 ALA HA H 3.02 0.02 1 357 . 60 ALA HB H 0.90 0.02 1 358 . 60 ALA N N 119.97 0.05 1 359 . 61 GLU H H 7.91 0.02 1 360 . 61 GLU HA H 3.61 0.02 1 361 . 61 GLU HB2 H 1.86 0.02 2 362 . 61 GLU HB3 H 1.90 0.02 2 363 . 61 GLU HG2 H 2.15 0.02 1 364 . 61 GLU HG3 H 2.29 0.02 1 365 . 61 GLU N N 115.26 0.05 1 366 . 62 ALA H H 7.73 0.02 1 367 . 62 ALA HA H 4.03 0.02 1 368 . 62 ALA HB H 1.25 0.02 1 369 . 62 ALA N N 120.50 0.05 1 370 . 63 VAL H H 7.66 0.02 1 371 . 63 VAL HA H 2.98 0.02 1 372 . 63 VAL HB H 1.16 0.02 1 373 . 63 VAL HG1 H -0.49 0.02 1 374 . 63 VAL HG2 H 0.32 0.02 1 375 . 63 VAL N N 118.40 0.05 1 376 . 64 ALA H H 8.04 0.02 1 377 . 64 ALA HA H 3.24 0.02 1 378 . 64 ALA HB H 1.14 0.02 1 379 . 64 ALA N N 121.34 0.05 1 380 . 65 ALA H H 7.39 0.02 1 381 . 65 ALA HA H 3.65 0.02 1 382 . 65 ALA HB H 1.30 0.02 1 383 . 65 ALA N N 117.38 0.05 1 384 . 66 TRP H H 7.48 0.02 1 385 . 66 TRP HA H 3.99 0.02 1 386 . 66 TRP HB2 H 2.93 0.02 2 387 . 66 TRP HB3 H 2.90 0.02 2 388 . 66 TRP HD1 H 7.22 0.02 1 389 . 66 TRP HE1 H 10.23 0.02 1 390 . 66 TRP HE3 H 6.79 0.02 1 391 . 66 TRP HZ2 H 7.37 0.02 1 392 . 66 TRP HZ3 H 6.44 0.02 1 393 . 66 TRP HH2 H 7.12 0.02 1 394 . 66 TRP N N 118.88 0.05 1 395 . 66 TRP NE1 N 130.09 0.05 1 396 . 67 LEU H H 8.42 0.02 1 397 . 67 LEU HA H 3.33 0.02 1 398 . 67 LEU HB2 H 0.97 0.02 1 399 . 67 LEU HB3 H 0.69 0.02 1 400 . 67 LEU HG H 1.16 0.02 1 401 . 67 LEU HD1 H -0.58 0.02 2 402 . 67 LEU HD2 H -0.28 0.02 2 403 . 67 LEU N N 117.06 0.05 1 404 . 68 ALA H H 7.70 0.02 1 405 . 68 ALA HA H 3.47 0.02 1 406 . 68 ALA HB H 1.29 0.02 1 407 . 68 ALA N N 118.27 0.05 1 408 . 69 GLU H H 6.48 0.02 1 409 . 69 GLU HA H 4.00 0.02 1 410 . 69 GLU HB2 H 1.68 0.02 2 411 . 69 GLU HB3 H 2.03 0.02 2 412 . 69 GLU HG2 H 2.10 0.02 2 413 . 69 GLU HG3 H 2.30 0.02 2 414 . 69 GLU N N 111.77 0.05 1 415 . 70 LYS H H 7.28 0.02 1 416 . 70 LYS HA H 3.99 0.02 1 417 . 70 LYS HB2 H 1.75 0.02 2 418 . 70 LYS HB3 H 1.72 0.02 2 419 . 70 LYS HG2 H 0.74 0.02 2 420 . 70 LYS HG3 H 0.83 0.02 2 421 . 70 LYS HD2 H 1.33 0.02 2 422 . 70 LYS HD3 H 0.99 0.02 2 423 . 70 LYS HE2 H 2.14 0.02 2 424 . 70 LYS N N 121.50 0.05 1 425 . 71 LYS H H 7.24 0.02 1 426 . 71 LYS HA H 3.99 0.02 1 427 . 71 LYS HB2 H 1.63 0.02 2 428 . 71 LYS HB3 H 1.42 0.02 2 429 . 71 LYS HG2 H 0.88 0.02 2 430 . 71 LYS HG3 H 0.98 0.02 2 431 . 71 LYS HE2 H 2.81 0.02 2 432 . 71 LYS N N 126.19 0.05 1 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 _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_ox 1HMB H 14.25 0.02 1 2 . 1 HEM_ox 2HMB H 14.25 0.02 1 3 . 1 HEM_ox 3HMB H 14.25 0.02 1 4 . 1 HEM_ox 1HMC H 29.18 0.02 1 5 . 1 HEM_ox 2HMC H 29.18 0.02 1 6 . 1 HEM_ox 3HMC H 29.18 0.02 1 7 . 1 HEM_ox 1HMD H 20.11 0.02 1 8 . 1 HEM_ox 2HMD H 20.11 0.02 1 9 . 1 HEM_ox 3HMD H 20.11 0.02 1 10 . 1 HEM_ox 1HMA H 29.75 0.02 1 11 . 1 HEM_ox 2HMA H 29.75 0.02 1 12 . 1 HEM_ox 3HMA H 29.75 0.02 1 13 . 1 HEM_ox HHA H 4.62 0.02 1 14 . 1 HEM_ox HHB H 1.46 0.02 1 15 . 1 HEM_ox HHC H 7.28 0.02 1 16 . 1 HEM_ox HHD H -0.31 0.02 1 17 . 1 HEM_ox HAB H -0.21 0.02 1 18 . 1 HEM_ox 1HBB H -0.71 0.02 1 19 . 1 HEM_ox 2HBB H -0.71 0.02 1 20 . 1 HEM_ox 3HBB H -0.71 0.02 1 21 . 1 HEM_ox HAC H 0.83 0.02 1 22 . 1 HEM_ox 1HBC H 1.78 0.02 1 23 . 1 HEM_ox 2HBC H 1.78 0.02 1 24 . 1 HEM_ox 3HBC H 1.78 0.02 1 25 . 1 HEM_ox 1HAD H 5.00 0.02 1 26 . 1 HEM_ox 2HAD H 4.32 0.02 1 27 . 1 HEM_ox 1HBD H 0.76 0.02 1 28 . 1 HEM_ox 2HBD H 0.27 0.02 1 29 . 1 HEM_ox 1HAA H 15.72 0.02 1 30 . 1 HEM_ox 2HAA H 4.45 0.02 1 31 . 1 HEM_ox 1HBA H -1.72 0.02 2 32 . 1 HEM_ox 2HBA H -0116 0.02 2 stop_ save_