data_4837 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of Methylophilus methylotrophus Cytochrome C'': Insights into the Structural Basis of Heme-ligand Detachment ; _BMRB_accession_number 4837 _BMRB_flat_file_name bmr4837.str _Entry_type original _Submission_date 2000-09-20 _Accession_date 2000-09-20 _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 Brennan L. . . 2 Turner D. L. . 3 Fareleira P. . . 4 Santos H. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 759 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-11 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of Methylophilus methylotrophus Cytochrome C'': Insights into the Structural Basis of Heme-ligand Detachment ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21226872 _PubMed_ID 11327772 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Brennan L. . . 2 Turner D. L. . 3 Fareleira P. . . 4 Santos H. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 308 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 353 _Page_last 365 _Year 2001 _Details . loop_ _Keyword 'Cytochrome C''' Hemeprotein 'NMR structure' 'REDOX-BOHR effect' 'Heme-Ligand detachment' stop_ save_ ################################## # Molecular system description # ################################## save_CYTOCHROME_C _Saveframe_category molecular_system _Mol_system_name 'CYTOCHROME C''' _Abbreviation_common 'CYTOCHROME C''' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CYTOCHROME C''' $cytochrome 'Heme C' $HEC_ox stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cytochrome _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CYTOCHROME C''' _Abbreviation_common 'CYTOCHROME C''' _Molecular_mass 15000 _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; DVTNAEKLVYKYTNIAHSAN PMYEAPSITDGKIFFNRKFK TPSGKEAACASCHTNNPANV GKNIVTGKEIPPLAPRVNTK RFTDIDKVEDEFTKHCNDIL GADCSPSEKANFIAYLLTET KPTK ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 VAL 3 THR 4 ASN 5 ALA 6 GLU 7 LYS 8 LEU 9 VAL 10 TYR 11 LYS 12 TYR 13 THR 14 ASN 15 ILE 16 ALA 17 HIS 18 SER 19 ALA 20 ASN 21 PRO 22 MET 23 TYR 24 GLU 25 ALA 26 PRO 27 SER 28 ILE 29 THR 30 ASP 31 GLY 32 LYS 33 ILE 34 PHE 35 PHE 36 ASN 37 ARG 38 LYS 39 PHE 40 LYS 41 THR 42 PRO 43 SER 44 GLY 45 LYS 46 GLU 47 ALA 48 ALA 49 CYS 50 ALA 51 SER 52 CYS 53 HIS 54 THR 55 ASN 56 ASN 57 PRO 58 ALA 59 ASN 60 VAL 61 GLY 62 LYS 63 ASN 64 ILE 65 VAL 66 THR 67 GLY 68 LYS 69 GLU 70 ILE 71 PRO 72 PRO 73 LEU 74 ALA 75 PRO 76 ARG 77 VAL 78 ASN 79 THR 80 LYS 81 ARG 82 PHE 83 THR 84 ASP 85 ILE 86 ASP 87 LYS 88 VAL 89 GLU 90 ASP 91 GLU 92 PHE 93 THR 94 LYS 95 HIS 96 CYS 97 ASN 98 ASP 99 ILE 100 LEU 101 GLY 102 ALA 103 ASP 104 CYS 105 SER 106 PRO 107 SER 108 GLU 109 LYS 110 ALA 111 ASN 112 PHE 113 ILE 114 ALA 115 TYR 116 LEU 117 LEU 118 THR 119 GLU 120 THR 121 LYS 122 PRO 123 THR 124 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-09 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 1E8E "Solution Structure Of Methylophilus Methylotrophus Cytochrome C''. Insights Into The Structural Basis Of Haem- Ligand Detachmen" 100.00 124 100.00 100.00 1.94e-84 PDB 1GU2 'Crystal Structure Of Oxidized Cytochrome C" From Methylophilus Methylotrophus' 100.00 124 100.00 100.00 1.94e-84 PDB 1OAE 'Crystal Structure Of The Reduced Form Of Cytochrome C" From Methylophilus Methylotrophus' 100.00 124 100.00 100.00 1.94e-84 GB AAB27865 'ferricytochrome c" {N-terminal} [Methylophilus methylotrophus, NCIB 10515, Peptide Partial, 61 aa]' 50.00 61 98.39 98.39 1.32e-33 GB AAF13764 "cytochrome c'' [Methylophilus methylotrophus]" 100.00 144 100.00 100.00 9.63e-85 REF WP_018987197 "cytochrome C [Methylophilus methylotrophus]" 100.00 144 100.00 100.00 9.63e-85 SP Q9RQB9 "RecName: Full=Cytochrome c''; Flags: Precursor [Methylophilus methylotrophus]" 100.00 144 100.00 100.00 9.63e-85 stop_ save_ ############# # Ligands # ############# save_HEC_ox _Saveframe_category ligand _Mol_type non-polymer _Name_common 'PROTOPORPHYRIN IX CONTAINING FE' _Abbreviation_common 'heme c' _BMRB_code HEC_ox _PDB_code . _Molecular_mass . _Mol_charge . _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 . ? 3HBB 3HBB 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 . ? 3HBC 3HBC 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 ? ? 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_ _Mol_thiol_state . _Sequence_homology_query_date . save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _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' 'Heme C' 1 HEC_ox CAB 'CYTOCHROME C''' 49 CYS SG single 'metal coordination' 'Heme C' 1 HEC_ox CAC 'CYTOCHROME C''' 52 CYS SG single 'metal coordination' 'Heme C' 1 HEC_ox FE 'CYTOCHROME C''' 95 HIS NE2 single 'metal coordination' 'Heme C' 1 HEC_ox FE 'CYTOCHROME C''' 53 HIS NE2 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cytochrome . 17 Eubacteria . Methylophilus methylotrophus 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 $cytochrome 'purified from the natural source' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cytochrome 3.5 mM . ampicillin 70 uM . kanamicine 50 uM . chloramphenicol 50 uM . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D-1H-NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-1H-NOESY _Sample_label . save_ save_2D-1H-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-1H-TOCSY _Sample_label . save_ save_2D-1H-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-1H-COSY _Sample_label . save_ save_3D-(15N,1H)_TOCSY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-(15N,1H) TOCSY-HSQC' _Sample_label . save_ save_3D-(15N,1H)_NOESY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-(15N,1H) NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-1H-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-1H-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-1H-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-(15N,1H) TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D-(15N,1H) NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.6 0.1 n/a temperature 298 1 K 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 H2O H 1 protons ppm 4.67 internal direct . . . 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _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 . 1 ASP HA H 4.32 . 1 2 . 1 ASP HB2 H 3.14 . 2 3 . 1 ASP HB3 H 2.93 . 2 4 . 2 VAL H H 8.68 . 1 5 . 2 VAL HA H 3.31 . 1 6 . 2 VAL HB H 1.96 . 1 7 . 2 VAL HG1 H 0.77 . 2 8 . 2 VAL HG2 H 0.82 . 2 9 . 3 THR H H 7.78 . 1 10 . 3 THR HA H 3.91 . 1 11 . 3 THR HB H 4.10 . 1 12 . 3 THR HG2 H 1.18 . 1 13 . 4 ASN H H 8.41 . 1 14 . 4 ASN HA H 4.41 . 1 15 . 4 ASN HB2 H 3.09 . 2 16 . 4 ASN HB3 H 2.52 . 2 17 . 4 ASN HD21 H 7.71 . 2 18 . 4 ASN HD22 H 6.93 . 2 19 . 5 ALA H H 7.41 . 1 20 . 5 ALA HA H 3.44 . 1 21 . 5 ALA HB H 0.85 . 1 22 . 6 GLU H H 8.17 . 1 23 . 6 GLU HA H 3.58 . 1 24 . 6 GLU HB2 H 2.04 . 2 25 . 6 GLU HB3 H 2.35 . 2 26 . 6 GLU HG2 H 2.23 . 2 27 . 6 GLU HG3 H 1.80 . 2 28 . 7 LYS H H 7.86 . 1 29 . 7 LYS HA H 3.99 . 1 30 . 7 LYS HB2 H 2.01 . 2 31 . 7 LYS HB3 H 1.81 . 2 32 . 7 LYS HG2 H 1.39 . 2 33 . 7 LYS HG3 H 1.38 . 2 34 . 7 LYS HD2 H 1.68 . 2 35 . 7 LYS HD3 H 1.64 . 2 36 . 7 LYS HE2 H 2.87 . 1 37 . 7 LYS HE3 H 2.87 . 1 38 . 8 LEU H H 7.74 . 1 39 . 8 LEU HA H 3.93 . 1 40 . 8 LEU HB2 H 1.84 . 2 41 . 8 LEU HB3 H 1.36 . 2 42 . 8 LEU HG H 1.65 . 1 43 . 8 LEU HD1 H 0.72 . 1 44 . 8 LEU HD2 H 0.78 . 1 45 . 9 VAL H H 8.01 . 1 46 . 9 VAL HA H 3.35 . 1 47 . 9 VAL HB H 2.11 . 1 48 . 9 VAL HG1 H 0.79 . 1 49 . 9 VAL HG2 H 0.85 . 1 50 . 10 TYR H H 7.85 . 1 51 . 10 TYR HA H 4.20 . 1 52 . 10 TYR HB2 H 3.15 . 2 53 . 10 TYR HB3 H 3.05 . 2 54 . 10 TYR HD1 H 7.11 . 1 55 . 10 TYR HE1 H 6.75 . 3 56 . 10 TYR HE2 H 6.74 . 3 57 . 10 TYR HD2 H 7.11 . 1 58 . 11 LYS H H 8.06 . 1 59 . 11 LYS HA H 3.93 . 1 60 . 11 LYS HB2 H 1.82 . 2 61 . 11 LYS HB3 H 1.62 . 2 62 . 11 LYS HG2 H 0.92 . 2 63 . 11 LYS HG3 H 1.35 . 2 64 . 11 LYS HD2 H 1.44 . 2 65 . 11 LYS HD3 H 1.45 . 2 66 . 11 LYS HE2 H 2.78 . 1 67 . 11 LYS HE3 H 2.78 . 1 68 . 12 TYR H H 8.77 . 1 69 . 12 TYR HA H 4.33 . 1 70 . 12 TYR HB2 H 3.44 . 2 71 . 12 TYR HB3 H 2.59 . 2 72 . 12 TYR HD1 H 6.81 . 1 73 . 12 TYR HE1 H 6.69 . 1 74 . 12 TYR HE2 H 6.69 . 1 75 . 12 TYR HD2 H 6.81 . 1 76 . 13 THR H H 8.51 . 1 77 . 13 THR HA H 3.82 . 1 78 . 13 THR HB H 4.26 . 1 79 . 13 THR HG2 H 1.05 . 1 80 . 13 THR HG1 H 4.63 . 1 81 . 14 ASN H H 7.73 . 1 82 . 14 ASN HA H 4.44 . 1 83 . 14 ASN HB2 H 3.32 . 2 84 . 14 ASN HB3 H 2.78 . 2 85 . 14 ASN HD21 H 7.33 . 2 86 . 14 ASN HD22 H 6.16 . 2 87 . 15 ILE H H 7.94 . 1 88 . 15 ILE HA H 3.75 . 1 89 . 15 ILE HB H 1.83 . 1 90 . 15 ILE HG2 H 0.99 . 1 91 . 15 ILE HG12 H 1.11 . 1 92 . 15 ILE HG13 H 1.11 . 1 93 . 15 ILE HD1 H 0.86 . 1 94 . 16 ALA H H 8.73 . 1 95 . 16 ALA HA H 3.83 . 1 96 . 16 ALA HB H 0.90 . 1 97 . 17 HIS H H 9.10 . 1 98 . 17 HIS HA H 4.90 . 1 99 . 17 HIS HB2 H 3.53 . 1 100 . 17 HIS HB3 H 3.31 . 1 101 . 17 HIS HD2 H 7.34 . 1 102 . 17 HIS HE1 H 8.69 . 1 103 . 18 SER H H 7.81 . 1 104 . 18 SER HA H 4.09 . 1 105 . 18 SER HB2 H 3.96 . 1 106 . 18 SER HB3 H 4.02 . 1 107 . 19 ALA H H 7.13 . 1 108 . 19 ALA HA H 4.33 . 1 109 . 19 ALA HB H 1.42 . 1 110 . 20 ASN H H 7.74 . 1 111 . 20 ASN HA H 4.95 . 1 112 . 20 ASN HB2 H 2.73 . 2 113 . 20 ASN HB3 H 2.98 . 2 114 . 20 ASN HD21 H 7.68 . 2 115 . 20 ASN HD22 H 7.00 . 2 116 . 21 PRO HA H 3.89 . 1 117 . 21 PRO HB2 H 1.87 . 2 118 . 21 PRO HB3 H 2.16 . 2 119 . 21 PRO HG2 H 1.94 . 2 120 . 21 PRO HD2 H 3.82 . 2 121 . 21 PRO HD3 H 3.49 . 2 122 . 22 MET H H 7.41 . 1 123 . 22 MET HA H 4.34 . 1 124 . 22 MET HB2 H 2.52 . 2 125 . 22 MET HB3 H 2.15 . 2 126 . 22 MET HG2 H 2.69 . 2 127 . 22 MET HG3 H 2.03 . 2 128 . 22 MET HE H 2.09 . 1 129 . 23 TYR H H 8.37 . 1 130 . 23 TYR HA H 4.38 . 1 131 . 23 TYR HB2 H 3.23 . 2 132 . 23 TYR HB3 H 2.64 . 2 133 . 23 TYR HD1 H 6.92 . 1 134 . 23 TYR HE1 H 6.56 . 1 135 . 23 TYR HE2 H 6.56 . 1 136 . 23 TYR HD2 H 6.92 . 1 137 . 23 TYR HH H 7.37 . 1 138 . 24 GLU H H 8.56 . 1 139 . 24 GLU HA H 4.31 . 1 140 . 24 GLU HB2 H 1.71 . 1 141 . 24 GLU HB3 H 1.89 . 1 142 . 24 GLU HG2 H 2.05 . 1 143 . 24 GLU HG3 H 2.20 . 1 144 . 25 ALA H H 7.01 . 1 145 . 25 ALA HA H 4.33 . 1 146 . 25 ALA HB H 1.15 . 1 147 . 26 PRO HA H 4.68 . 1 148 . 26 PRO HB2 H 1.97 . 2 149 . 26 PRO HB3 H 1.44 . 2 150 . 26 PRO HG2 H 1.75 . 2 151 . 26 PRO HG3 H 1.27 . 2 152 . 26 PRO HD2 H 3.56 . 2 153 . 26 PRO HD3 H 3.40 . 2 154 . 27 SER H H 8.15 . 1 155 . 27 SER HA H 3.96 . 1 156 . 27 SER HB2 H 3.64 . 2 157 . 27 SER HB3 H 3.81 . 2 158 . 28 ILE H H 8.69 . 1 159 . 28 ILE HA H 3.75 . 1 160 . 28 ILE HB H 1.89 . 1 161 . 28 ILE HG2 H 1.02 . 1 162 . 28 ILE HG12 H 1.21 . 2 163 . 28 ILE HG13 H 1.49 . 2 164 . 28 ILE HD1 H 0.88 . 1 165 . 29 THR H H 7.94 . 1 166 . 29 THR HA H 3.82 . 1 167 . 29 THR HB H 3.95 . 1 168 . 29 THR HG2 H 1.20 . 1 169 . 30 ASP H H 8.01 . 1 170 . 30 ASP HA H 4.44 . 1 171 . 30 ASP HB2 H 2.53 . 1 172 . 30 ASP HB3 H 2.61 . 1 173 . 31 GLY H H 8.20 . 1 174 . 31 GLY HA2 H 3.70 . 2 175 . 31 GLY HA3 H 3.66 . 2 176 . 32 LYS H H 7.71 . 1 177 . 32 LYS HA H 3.03 . 1 178 . 32 LYS HB2 H 0.97 . 2 179 . 32 LYS HB3 H 0.94 . 2 180 . 32 LYS HG2 H 1.73 . 2 181 . 32 LYS HG3 H 1.66 . 2 182 . 32 LYS HD2 H 1.16 . 1 183 . 32 LYS HD3 H 1.16 . 1 184 . 32 LYS HE2 H 3.14 . 1 185 . 32 LYS HE3 H 3.14 . 1 186 . 33 ILE H H 8.13 . 1 187 . 33 ILE HA H 3.63 . 1 188 . 33 ILE HB H 1.81 . 1 189 . 33 ILE HG2 H 0.83 . 1 190 . 33 ILE HG12 H 1.72 . 2 191 . 33 ILE HG13 H 1.02 . 2 192 . 33 ILE HD1 H 0.81 . 1 193 . 34 PHE H H 8.04 . 1 194 . 34 PHE HA H 3.84 . 1 195 . 34 PHE HB2 H 3.10 . 2 196 . 34 PHE HD1 H 6.65 . 1 197 . 34 PHE HD2 H 6.65 . 1 198 . 34 PHE HE1 H 6.04 . 1 199 . 34 PHE HE2 H 6.04 . 1 200 . 34 PHE HZ H 6.33 . 1 201 . 35 PHE H H 7.57 . 1 202 . 35 PHE HA H 3.30 . 1 203 . 35 PHE HB2 H 3.26 . 2 204 . 35 PHE HB3 H 2.17 . 2 205 . 35 PHE HD1 H 7.18 . 1 206 . 35 PHE HD2 H 7.18 . 1 207 . 35 PHE HE1 H 8.87 . 1 208 . 35 PHE HE2 H 8.87 . 1 209 . 35 PHE HZ H 9.98 . 1 210 . 36 ASN H H 7.17 . 1 211 . 36 ASN HA H 4.34 . 1 212 . 36 ASN HB2 H 2.48 . 1 213 . 36 ASN HB3 H 2.57 . 1 214 . 36 ASN HD21 H 7.53 . 2 215 . 36 ASN HD22 H 8.35 . 2 216 . 37 ARG H H 7.48 . 1 217 . 37 ARG HA H 3.89 . 1 218 . 37 ARG HB2 H 1.61 . 1 219 . 37 ARG HB3 H 1.50 . 1 220 . 37 ARG HG2 H 1.32 . 2 221 . 37 ARG HG3 H 1.15 . 2 222 . 37 ARG HD2 H 2.89 . 2 223 . 37 ARG HD3 H 2.85 . 2 224 . 37 ARG HE H 6.79 . 1 225 . 37 ARG HH21 H 6.67 . 2 226 . 37 ARG HH22 H 6.31 . 2 227 . 38 LYS H H 8.14 . 1 228 . 38 LYS HA H 4.11 . 1 229 . 38 LYS HB2 H 1.31 . 1 230 . 38 LYS HB3 H 1.46 . 1 231 . 38 LYS HG2 H 0.97 . 1 232 . 38 LYS HG3 H 0.97 . 1 233 . 38 LYS HD2 H 1.20 . 2 234 . 38 LYS HD3 H 1.21 . 2 235 . 38 LYS HE2 H 2.70 . 1 236 . 38 LYS HE3 H 2.70 . 1 237 . 39 PHE H H 8.35 . 1 238 . 39 PHE HA H 4.54 . 1 239 . 39 PHE HB2 H 2.38 . 1 240 . 39 PHE HB3 H 2.63 . 1 241 . 39 PHE HD1 H 6.31 . 1 242 . 39 PHE HD2 H 6.31 . 1 243 . 39 PHE HE1 H 6.08 . 1 244 . 39 PHE HE2 H 6.08 . 1 245 . 39 PHE HZ H 4.92 . 1 246 . 40 LYS H H 8.20 . 1 247 . 40 LYS HA H 4.61 . 1 248 . 40 LYS HB2 H 1.57 . 2 249 . 40 LYS HG2 H 1.48 . 2 250 . 40 LYS HD2 H 1.26 . 1 251 . 40 LYS HD3 H 1.26 . 1 252 . 40 LYS HE2 H 2.85 . 1 253 . 40 LYS HE3 H 2.85 . 1 254 . 41 THR H H 8.42 . 1 255 . 41 THR HA H 4.65 . 1 256 . 41 THR HB H 4.53 . 1 257 . 41 THR HG2 H 0.85 . 1 258 . 41 THR HG1 H 4.96 . 1 259 . 42 PRO HA H 4.33 . 1 260 . 42 PRO HB2 H 2.50 . 1 261 . 42 PRO HB3 H 2.24 . 1 262 . 42 PRO HG2 H 1.97 . 1 263 . 42 PRO HG3 H 1.91 . 1 264 . 42 PRO HD2 H 3.80 . 2 265 . 42 PRO HD3 H 3.78 . 2 266 . 43 SER H H 7.60 . 1 267 . 43 SER HA H 4.38 . 1 268 . 43 SER HB2 H 3.92 . 1 269 . 43 SER HB3 H 3.82 . 1 270 . 44 GLY H H 8.29 . 1 271 . 44 GLY HA2 H 3.46 . 2 272 . 44 GLY HA3 H 4.26 . 2 273 . 45 LYS H H 7.06 . 1 274 . 45 LYS HA H 4.22 . 1 275 . 45 LYS HB2 H 1.54 . 1 276 . 45 LYS HB3 H 1.54 . 1 277 . 45 LYS HG2 H 1.41 . 2 278 . 45 LYS HG3 H 1.37 . 2 279 . 45 LYS HD2 H 1.17 . 2 280 . 45 LYS HD3 H 1.11 . 2 281 . 45 LYS HE2 H 2.78 . 2 282 . 45 LYS HE3 H 2.77 . 2 283 . 46 GLU H H 8.30 . 1 284 . 46 GLU HA H 4.71 . 1 285 . 46 GLU HB2 H 1.52 . 1 286 . 46 GLU HB3 H 1.62 . 1 287 . 46 GLU HG2 H 1.95 . 2 288 . 46 GLU HG3 H 1.72 . 2 289 . 47 ALA H H 8.24 . 1 290 . 47 ALA HA H 3.73 . 1 291 . 47 ALA HB H 0.12 . 1 292 . 48 ALA H H 7.09 . 1 293 . 48 ALA HA H 3.84 . 1 294 . 48 ALA HB H 0.62 . 1 295 . 49 CYS H H 8.96 . 1 296 . 49 CYS HA H 2.17 . 1 297 . 49 CYS HB2 H 0.22 . 2 298 . 49 CYS HB3 H -0.03 . 2 299 . 50 ALA H H 6.65 . 1 300 . 50 ALA HA H 5.27 . 1 301 . 50 ALA HB H 1.29 . 1 302 . 51 SER H H 7.96 . 1 303 . 51 SER HA H 4.40 . 1 304 . 51 SER HB2 H 3.51 . 2 305 . 51 SER HB3 H 3.81 . 2 306 . 52 CYS H H 7.34 . 1 307 . 52 CYS HA H 6.63 . 1 308 . 52 CYS HB2 H 4.47 . 2 309 . 53 HIS H H 12.81 . 1 310 . 53 HIS HA H 11.38 . 1 311 . 53 HIS HB2 H 15.43 . 2 312 . 53 HIS HB3 H 10.83 . 2 313 . 53 HIS HD1 H 20.75 . 1 314 . 54 THR H H 9.77 . 1 315 . 54 THR HA H 5.69 . 1 316 . 54 THR HB H 5.59 . 1 317 . 54 THR HG2 H 2.62 . 1 318 . 54 THR HG1 H 6.87 . 1 319 . 55 ASN H H 8.86 . 1 320 . 55 ASN HA H 5.30 . 1 321 . 55 ASN HB2 H 3.61 . 2 322 . 55 ASN HB3 H 3.25 . 2 323 . 55 ASN HD21 H 7.15 . 2 324 . 55 ASN HD22 H 7.89 . 2 325 . 56 ASN H H 9.87 . 1 326 . 56 ASN HA H 5.89 . 1 327 . 56 ASN HB2 H 3.18 . 1 328 . 56 ASN HB3 H 3.87 . 1 329 . 56 ASN HD21 H 7.77 . 2 330 . 56 ASN HD22 H 7.52 . 2 331 . 57 PRO HA H 6.90 . 1 332 . 57 PRO HB2 H 2.98 . 2 333 . 57 PRO HB3 H 2.54 . 2 334 . 57 PRO HG2 H 1.91 . 2 335 . 57 PRO HG3 H 1.80 . 2 336 . 57 PRO HD2 H 4.43 . 2 337 . 58 ALA H H 9.07 . 1 338 . 58 ALA HA H 4.63 . 1 339 . 58 ALA HB H 1.43 . 1 340 . 59 ASN H H 8.88 . 1 341 . 59 ASN HA H 5.48 . 1 342 . 59 ASN HB2 H 3.70 . 1 343 . 59 ASN HB3 H 4.34 . 1 344 . 59 ASN HD21 H 8.02 . 2 345 . 59 ASN HD22 H 7.54 . 2 346 . 60 VAL H H 8.92 . 1 347 . 60 VAL HA H 4.70 . 1 348 . 60 VAL HB H 2.46 . 1 349 . 60 VAL HG1 H 1.49 . 1 350 . 60 VAL HG2 H 1.43 . 1 351 . 61 GLY H H 10.59 . 1 352 . 61 GLY HA2 H 6.48 . 2 353 . 61 GLY HA3 H 6.10 . 2 354 . 62 LYS H H 9.96 . 1 355 . 62 LYS HA H 4.93 . 1 356 . 62 LYS HB2 H 2.11 . 2 357 . 62 LYS HB3 H 1.98 . 2 358 . 62 LYS HG2 H 1.06 . 1 359 . 62 LYS HG3 H 1.15 . 1 360 . 62 LYS HD2 H 1.74 . 1 361 . 62 LYS HD3 H 1.97 . 1 362 . 62 LYS HE2 H 3.05 . 2 363 . 62 LYS HE3 H 3.04 . 2 364 . 63 ASN H H 8.91 . 1 365 . 63 ASN HA H 3.72 . 1 366 . 63 ASN HB2 H 2.75 . 2 367 . 63 ASN HB3 H 1.38 . 2 368 . 63 ASN HD21 H 6.08 . 2 369 . 63 ASN HD22 H 6.27 . 2 370 . 64 ILE H H 7.18 . 1 371 . 64 ILE HA H 3.87 . 1 372 . 64 ILE HB H 1.82 . 1 373 . 64 ILE HG2 H 0.85 . 1 374 . 64 ILE HG12 H 0.92 . 1 375 . 64 ILE HG13 H 1.09 . 1 376 . 64 ILE HD1 H 0.57 . 1 377 . 65 VAL H H 7.67 . 1 378 . 65 VAL HA H 3.56 . 1 379 . 65 VAL HB H 1.55 . 1 380 . 65 VAL HG1 H 0.60 . 1 381 . 65 VAL HG2 H 0.44 . 1 382 . 66 THR H H 6.21 . 1 383 . 66 THR HA H 4.13 . 1 384 . 66 THR HB H 4.08 . 1 385 . 66 THR HG2 H 0.76 . 1 386 . 66 THR HG1 H 4.99 . 1 387 . 67 GLY H H 8.34 . 1 388 . 67 GLY HA2 H 3.52 . 1 389 . 67 GLY HA3 H 4.10 . 1 390 . 68 LYS H H 7.10 . 1 391 . 68 LYS HA H 4.14 . 1 392 . 68 LYS HB2 H 1.47 . 2 393 . 68 LYS HB3 H 1.38 . 2 394 . 68 LYS HG2 H 1.18 . 2 395 . 68 LYS HG3 H 1.19 . 2 396 . 68 LYS HD2 H 1.27 . 2 397 . 68 LYS HD3 H 1.26 . 2 398 . 68 LYS HE2 H 2.75 . 1 399 . 68 LYS HE3 H 2.75 . 1 400 . 69 GLU H H 8.64 . 1 401 . 69 GLU HA H 4.64 . 1 402 . 69 GLU HB2 H 1.98 . 2 403 . 69 GLU HB3 H 1.97 . 2 404 . 69 GLU HG2 H 2.43 . 1 405 . 69 GLU HG3 H 2.33 . 1 406 . 70 ILE H H 7.98 . 1 407 . 70 ILE HA H 4.14 . 1 408 . 70 ILE HB H 2.93 . 1 409 . 70 ILE HG2 H 0.71 . 1 410 . 70 ILE HG12 H 1.55 . 2 411 . 70 ILE HG13 H 1.56 . 2 412 . 70 ILE HD1 H -0.22 . 1 413 . 71 PRO HA H 4.98 . 1 414 . 71 PRO HB2 H 2.37 . 2 415 . 71 PRO HB3 H 1.73 . 2 416 . 71 PRO HG2 H 1.15 . 2 417 . 71 PRO HG3 H 1.61 . 2 418 . 71 PRO HD2 H 3.38 . 2 419 . 71 PRO HD3 H 2.89 . 2 420 . 72 PRO HA H 5.63 . 1 421 . 72 PRO HB2 H 3.06 . 2 422 . 72 PRO HB3 H 1.90 . 2 423 . 72 PRO HG2 H 2.32 . 2 424 . 72 PRO HG3 H 2.22 . 2 425 . 72 PRO HD2 H 3.65 . 1 426 . 72 PRO HD3 H 4.36 . 1 427 . 73 LEU H H 9.12 . 1 428 . 73 LEU HA H 4.06 . 1 429 . 73 LEU HB2 H 5.90 . 2 430 . 73 LEU HB3 H 2.94 . 2 431 . 73 LEU HG H 1.45 . 1 432 . 73 LEU HD1 H -0.45 . 1 433 . 73 LEU HD2 H 3.41 . 1 434 . 74 ALA H H 7.76 . 1 435 . 74 ALA HA H 4.12 . 1 436 . 74 ALA HB H 1.48 . 1 437 . 75 PRO HA H 3.32 . 1 438 . 75 PRO HB2 H 1.52 . 2 439 . 75 PRO HB3 H 0.09 . 2 440 . 75 PRO HG2 H 0.24 . 2 441 . 75 PRO HG3 H 0.55 . 2 442 . 75 PRO HD2 H 4.02 . 1 443 . 75 PRO HD3 H 4.02 . 1 444 . 76 ARG H H 8.38 . 1 445 . 76 ARG HA H 4.51 . 1 446 . 76 ARG HB3 H 1.90 . 2 447 . 76 ARG HG2 H 1.55 . 2 448 . 76 ARG HG3 H 0.73 . 2 449 . 76 ARG HD2 H 3.14 . 2 450 . 76 ARG HD3 H 2.92 . 2 451 . 76 ARG HE H 7.46 . 1 452 . 77 VAL H H 7.10 . 1 453 . 77 VAL HA H 4.13 . 1 454 . 77 VAL HB H 2.09 . 1 455 . 77 VAL HG1 H 1.21 . 1 456 . 77 VAL HG2 H 1.01 . 1 457 . 78 ASN H H 7.98 . 1 458 . 78 ASN HA H 4.95 . 1 459 . 78 ASN HB2 H 2.58 . 2 460 . 78 ASN HB3 H 2.46 . 2 461 . 78 ASN HD21 H 7.04 . 2 462 . 78 ASN HD22 H 7.26 . 2 463 . 79 THR H H 8.24 . 1 464 . 79 THR HA H 4.28 . 1 465 . 79 THR HB H 4.38 . 1 466 . 79 THR HG2 H 1.24 . 1 467 . 80 LYS H H 7.18 . 1 468 . 80 LYS HA H 3.94 . 1 469 . 80 LYS HB2 H 1.60 . 1 470 . 80 LYS HB3 H 1.54 . 1 471 . 80 LYS HG2 H 1.34 . 2 472 . 80 LYS HG3 H 1.24 . 2 473 . 80 LYS HD2 H 1.50 . 2 474 . 80 LYS HD3 H 1.47 . 2 475 . 80 LYS HE2 H 2.82 . 2 476 . 80 LYS HE3 H 2.83 . 2 477 . 81 ARG H H 7.11 . 1 478 . 81 ARG HA H 3.45 . 1 479 . 81 ARG HB2 H 1.34 . 2 480 . 81 ARG HB3 H 0.80 . 2 481 . 81 ARG HG2 H 1.09 . 1 482 . 81 ARG HG3 H 1.17 . 1 483 . 81 ARG HD2 H 2.13 . 2 484 . 81 ARG HD3 H 1.57 . 2 485 . 81 ARG HE H 6.28 . 1 486 . 82 PHE H H 8.71 . 1 487 . 82 PHE HB2 H 2.77 . 2 488 . 82 PHE HB3 H 3.38 . 2 489 . 82 PHE HD1 H 6.67 . 1 490 . 82 PHE HD2 H 6.67 . 1 491 . 82 PHE HE1 H 6.54 . 1 492 . 82 PHE HE2 H 6.54 . 1 493 . 82 PHE HZ H 6.02 . 1 494 . 83 THR H H 7.67 . 1 495 . 83 THR HA H 3.92 . 1 496 . 83 THR HB H 3.98 . 1 497 . 83 THR HG2 H 1.07 . 1 498 . 84 ASP H H 8.14 . 1 499 . 84 ASP HA H 4.77 . 1 500 . 84 ASP HB2 H 2.67 . 2 501 . 84 ASP HB3 H 2.38 . 2 502 . 85 ILE H H 8.27 . 1 503 . 85 ILE HA H 3.67 . 1 504 . 85 ILE HB H 1.81 . 1 505 . 85 ILE HG2 H 0.90 . 1 506 . 85 ILE HG12 H 1.46 . 1 507 . 85 ILE HG13 H 1.16 . 1 508 . 85 ILE HD1 H 0.82 . 1 509 . 86 ASP H H 8.22 . 1 510 . 86 ASP HA H 4.47 . 1 511 . 86 ASP HB2 H 2.72 . 2 512 . 86 ASP HB3 H 2.69 . 2 513 . 87 LYS H H 7.71 . 1 514 . 87 LYS HA H 4.39 . 1 515 . 87 LYS HB2 H 1.89 . 2 516 . 87 LYS HB3 H 1.78 . 2 517 . 87 LYS HG2 H 1.50 . 2 518 . 87 LYS HG3 H 1.40 . 2 519 . 87 LYS HD2 H 1.66 . 2 520 . 88 VAL H H 7.98 . 1 521 . 88 VAL HA H 3.71 . 1 522 . 88 VAL HB H 2.01 . 1 523 . 88 VAL HG1 H 0.77 . 1 524 . 88 VAL HG2 H 0.71 . 1 525 . 89 GLU H H 8.43 . 1 526 . 89 GLU HA H 4.38 . 1 527 . 89 GLU HB2 H 2.33 . 1 528 . 89 GLU HB3 H 2.33 . 1 529 . 89 GLU HG2 H 2.62 . 2 530 . 89 GLU HG3 H 2.61 . 2 531 . 90 ASP H H 7.95 . 1 532 . 90 ASP HA H 4.93 . 1 533 . 90 ASP HB2 H 3.10 . 2 534 . 90 ASP HB3 H 3.09 . 2 535 . 91 GLU H H 8.99 . 1 536 . 91 GLU HA H 5.09 . 1 537 . 91 GLU HB2 H 2.60 . 2 538 . 91 GLU HB3 H 2.47 . 2 539 . 91 GLU HG2 H 2.89 . 2 540 . 91 GLU HG3 H 2.79 . 2 541 . 92 PHE H H 10.15 . 1 542 . 92 PHE HA H 6.58 . 1 543 . 92 PHE HB2 H 3.76 . 2 544 . 92 PHE HB3 H 3.90 . 2 545 . 92 PHE HD1 H 8.12 . 1 546 . 92 PHE HD2 H 8.12 . 1 547 . 92 PHE HE1 H 6.40 . 1 548 . 92 PHE HE2 H 6.40 . 1 549 . 92 PHE HZ H 6.07 . 1 550 . 93 THR H H 8.57 . 1 551 . 93 THR HA H 5.24 . 1 552 . 93 THR HB H 4.98 . 1 553 . 93 THR HG2 H 1.71 . 1 554 . 94 LYS H H 9.30 . 1 555 . 94 LYS HA H 5.37 . 1 556 . 94 LYS HB2 H 3.58 . 1 557 . 94 LYS HB3 H 3.27 . 1 558 . 94 LYS HG2 H 3.26 . 2 559 . 94 LYS HG3 H 2.68 . 2 560 . 94 LYS HD2 H 2.57 . 2 561 . 94 LYS HE2 H 3.71 . 1 562 . 94 LYS HE3 H 3.71 . 1 563 . 95 HIS H H 12.26 . 1 564 . 95 HIS HA H 11.24 . 1 565 . 95 HIS HB2 H 20.64 . 1 566 . 95 HIS HB3 H 11.89 . 1 567 . 96 CYS H H 11.72 . 1 568 . 96 CYS HA H 5.61 . 1 569 . 96 CYS HB2 H 5.19 . 1 570 . 96 CYS HB3 H 4.31 . 1 571 . 97 ASN H H 9.43 . 1 572 . 97 ASN HA H 4.55 . 1 573 . 97 ASN HB2 H 3.86 . 2 574 . 97 ASN HB3 H 3.35 . 2 575 . 97 ASN HD21 H 7.91 . 2 576 . 97 ASN HD22 H 7.41 . 2 577 . 98 ASP H H 10.59 . 1 578 . 98 ASP HA H 5.29 . 1 579 . 98 ASP HB2 H 5.56 . 1 580 . 98 ASP HB3 H 4.92 . 1 581 . 99 ILE H H 10.16 . 1 582 . 99 ILE HA H 4.00 . 1 583 . 99 ILE HB H 2.33 . 1 584 . 99 ILE HG2 H -1.49 . 1 585 . 99 ILE HG12 H 5.56 . 2 586 . 99 ILE HG13 H 0.96 . 2 587 . 99 ILE HD1 H -0.09 . 1 588 . 100 LEU H H 8.99 . 1 589 . 100 LEU HA H 4.04 . 1 590 . 100 LEU HB2 H 2.22 . 2 591 . 100 LEU HB3 H 1.15 . 2 592 . 100 LEU HG H 0.69 . 1 593 . 100 LEU HD1 H 0.34 . 2 594 . 100 LEU HD2 H -0.70 . 2 595 . 101 GLY H H 8.09 . 1 596 . 101 GLY HA2 H 4.16 . 1 597 . 101 GLY HA3 H 4.37 . 1 598 . 102 ALA H H 7.79 . 1 599 . 102 ALA HA H 4.69 . 1 600 . 102 ALA HB H 1.42 . 1 601 . 103 ASP H H 8.46 . 1 602 . 103 ASP HA H 5.09 . 1 603 . 103 ASP HB2 H 3.00 . 1 604 . 103 ASP HB3 H 2.65 . 1 605 . 104 CYS H H 8.81 . 1 606 . 104 CYS HA H 4.48 . 1 607 . 104 CYS HB2 H 2.99 . 2 608 . 104 CYS HB3 H 2.32 . 2 609 . 105 SER H H 9.17 . 1 610 . 105 SER HA H 4.49 . 1 611 . 105 SER HB2 H 4.13 . 2 612 . 105 SER HB3 H 3.69 . 2 613 . 106 PRO HA H 3.83 . 1 614 . 106 PRO HB2 H 2.30 . 1 615 . 106 PRO HB3 H 1.83 . 1 616 . 106 PRO HG2 H 2.08 . 2 617 . 106 PRO HG3 H 2.03 . 2 618 . 106 PRO HD2 H 3.70 . 2 619 . 107 SER H H 7.54 . 1 620 . 107 SER HA H 3.35 . 1 621 . 107 SER HB2 H 3.24 . 2 622 . 107 SER HB3 H 2.82 . 2 623 . 108 GLU H H 7.07 . 1 624 . 108 GLU HA H 3.37 . 1 625 . 108 GLU HB2 H 1.82 . 2 626 . 108 GLU HB3 H 1.70 . 2 627 . 108 GLU HG2 H 1.48 . 2 628 . 108 GLU HG3 H 0.07 . 2 629 . 109 LYS H H 7.68 . 1 630 . 109 LYS HA H 3.14 . 1 631 . 109 LYS HB2 H 0.70 . 2 632 . 109 LYS HB3 H 0.78 . 2 633 . 109 LYS HG2 H 0.48 . 1 634 . 109 LYS HG3 H 0.48 . 1 635 . 109 LYS HD2 H -0.30 . 1 636 . 109 LYS HD3 H -0.30 . 1 637 . 109 LYS HE2 H 2.21 . 2 638 . 109 LYS HE3 H 2.59 . 2 639 . 110 ALA H H 7.95 . 1 640 . 110 ALA HA H 3.74 . 1 641 . 110 ALA HB H 1.44 . 1 642 . 111 ASN H H 8.42 . 1 643 . 111 ASN HA H 3.95 . 1 644 . 111 ASN HB2 H 2.69 . 2 645 . 111 ASN HB3 H 2.61 . 2 646 . 111 ASN HD21 H 8.10 . 2 647 . 111 ASN HD22 H 7.84 . 2 648 . 112 PHE H H 8.38 . 1 649 . 112 PHE HA H 4.06 . 1 650 . 112 PHE HB2 H 3.00 . 2 651 . 112 PHE HB3 H 2.64 . 2 652 . 112 PHE HD1 H 6.71 . 1 653 . 112 PHE HD2 H 6.71 . 1 654 . 112 PHE HE1 H 5.94 . 1 655 . 112 PHE HE2 H 5.94 . 1 656 . 112 PHE HZ H 5.85 . 1 657 . 113 ILE H H 8.24 . 1 658 . 113 ILE HA H 2.72 . 1 659 . 113 ILE HB H 1.78 . 1 660 . 113 ILE HG2 H 0.28 . 1 661 . 113 ILE HG12 H 1.45 . 2 662 . 113 ILE HG13 H 0.56 . 2 663 . 113 ILE HD1 H 0.43 . 1 664 . 114 ALA H H 8.07 . 1 665 . 114 ALA HA H 3.77 . 1 666 . 114 ALA HB H 1.27 . 1 667 . 115 TYR H H 7.97 . 1 668 . 115 TYR HA H 4.31 . 1 669 . 115 TYR HB2 H 3.65 . 1 670 . 115 TYR HB3 H 3.03 . 1 671 . 115 TYR HD1 H 6.76 . 1 672 . 115 TYR HE1 H 6.56 . 1 673 . 115 TYR HD2 H 6.76 . 1 674 . 115 TYR HE2 H 6.56 . 1 675 . 116 LEU H H 8.38 . 1 676 . 116 LEU HA H 2.95 . 1 677 . 116 LEU HB2 H 1.70 . 2 678 . 116 LEU HB3 H 0.76 . 2 679 . 116 LEU HG H 0.54 . 1 680 . 116 LEU HD1 H 0.24 . 2 681 . 116 LEU HD2 H 0.09 . 2 682 . 117 LEU H H 7.33 . 1 683 . 117 LEU HA H 3.75 . 1 684 . 117 LEU HB2 H 1.34 . 2 685 . 117 LEU HB3 H 1.53 . 2 686 . 117 LEU HG H 1.89 . 1 687 . 117 LEU HD1 H 0.64 . 2 688 . 117 LEU HD2 H 0.73 . 2 689 . 118 THR H H 7.85 . 1 690 . 118 THR HA H 4.38 . 1 691 . 118 THR HB H 4.38 . 1 692 . 118 THR HG2 H 1.41 . 1 693 . 118 THR HG1 H 5.61 . 1 694 . 119 GLU H H 6.67 . 1 695 . 119 GLU HA H 5.09 . 1 696 . 119 GLU HB2 H 1.57 . 2 697 . 119 GLU HB3 H 1.83 . 2 698 . 119 GLU HG2 H 2.11 . 2 699 . 119 GLU HG3 H 2.03 . 2 700 . 120 THR H H 8.46 . 1 701 . 120 THR HA H 4.34 . 1 702 . 120 THR HB H 4.34 . 1 703 . 120 THR HG2 H 1.03 . 1 704 . 121 LYS H H 8.55 . 1 705 . 121 LYS HA H 5.04 . 1 706 . 121 LYS HB2 H 1.95 . 1 707 . 121 LYS HB3 H 1.95 . 1 708 . 121 LYS HG2 H 1.53 . 2 709 . 121 LYS HG3 H 1.43 . 2 710 . 121 LYS HD2 H 1.82 . 2 711 . 121 LYS HD3 H 1.80 . 2 712 . 121 LYS HE2 H 3.09 . 2 713 . 121 LYS HE3 H 3.08 . 2 714 . 122 PRO HA H 4.69 . 1 715 . 122 PRO HB2 H 2.75 . 2 716 . 122 PRO HB3 H 2.26 . 2 717 . 122 PRO HG2 H 2.26 . 2 718 . 122 PRO HG3 H 1.43 . 2 719 . 122 PRO HD2 H 3.85 . 2 720 . 122 PRO HD3 H 3.94 . 2 721 . 123 THR H H 9.70 . 1 722 . 123 THR HA H 4.61 . 1 723 . 123 THR HG2 H 1.45 . 1 724 . 124 LYS H H 8.16 . 1 725 . 124 LYS HA H 4.40 . 1 726 . 124 LYS HB2 H 2.02 . 1 727 . 124 LYS HB3 H 2.02 . 1 728 . 124 LYS HG2 H 1.92 . 2 729 . 124 LYS HD2 H 1.61 . 2 730 . 124 LYS HE2 H 3.19 . 2 731 . 124 LYS HE3 H 3.18 . 2 stop_ save_ save_chem_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _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_ox HAC H -0.42 . 1 2 . 1 HEC_ox 1HBC H 0.21 . 1 3 . 1 HEC_ox 2HBC H 0.21 . 1 4 . 1 HEC_ox 3HBC H 0.21 . 1 5 . 1 HEC_ox 1HMC H 17.57 . 1 6 . 1 HEC_ox 2HMC H 17.57 . 1 7 . 1 HEC_ox 3HMC H 17.57 . 1 8 . 1 HEC_ox HHC H 2.43 . 1 9 . 1 HEC_ox 1HMD H 12.80 . 1 10 . 1 HEC_ox 2HMD H 12.80 . 1 11 . 1 HEC_ox 3HMD H 12.80 . 1 12 . 1 HEC_ox 1HAD H 9.61 . 1 13 . 1 HEC_ox 2HAD H 3.83 . 1 14 . 1 HEC_ox 1HBD H -2.16 . 2 15 . 1 HEC_ox 2HBD H 0.62 . 2 16 . 1 HEC_ox 1HAA H 8.11 . 2 17 . 1 HEC_ox 2HAA H 4.63 . 2 18 . 1 HEC_ox 1HBA H -0.09 . 2 19 . 1 HEC_ox 2HBA H -0.40 . 2 20 . 1 HEC_ox 1HMA H 14.56 . 1 21 . 1 HEC_ox 2HMA H 14.56 . 1 22 . 1 HEC_ox 3HMA H 14.56 . 1 23 . 1 HEC_ox HHA H 1.57 . 1 24 . 1 HEC_ox 1HMB H 8.62 . 1 25 . 1 HEC_ox 2HMB H 8.62 . 1 26 . 1 HEC_ox 3HMB H 8.62 . 1 27 . 1 HEC_ox HAB H -2.27 . 1 28 . 1 HEC_ox HHB H -2.38 . 1 stop_ save_