data_6634 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments for the K45Q-mutated ferricytochrome c3 from Desulfovibrio vulgaris Hildenborough ; _BMRB_accession_number 6634 _BMRB_flat_file_name bmr6634.str _Entry_type original _Submission_date 2005-05-13 _Accession_date 2005-05-13 _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 Messias Ana C. . 2 Aguiar Antonio P. . 3 Brennan Lorraine . . 4 Salgueiro Carlos A. . 5 Saraiva Ligia M. . 6 Xavier Antonio V. . 7 Turner David L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 5 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 583 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-01-26 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5625 'Wild-type ferricytochrome c3 chemical shift assignments.' stop_ _Original_release_date 2007-01-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structures of tetrahaem ferricytochrome c(3) from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16527248 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Messias Ana C. . 2 Aguiar Antonio P. . 3 Brennan Lorraine . . 4 Salgueiro Carlos A. . 5 Saraiva Ligia M. . 6 Xavier Antonio V. . 7 Turner David L. . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta.' _Journal_volume 1757 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 143 _Page_last 153 _Year 2006 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_1 _Saveframe_category citation _Citation_full ; Ligia M. Saraiva, Carlos A. Salgueiro, Patricia N. da Costa, Ana C. Messias, Jean LeGall, Walter M. A. M. van Dongen and Antonio V. Xavier (1998) Biochemistry, 37, 12160-12165, "Replacement of Lysine 45 by uncharged residues modulates the redox-Bohr effect in tetraheme cytochrome c3 of Desulfovibrio vulgaris (Hildenborough)". ; _Citation_title 'Replacement of lysine 45 by uncharged residues modulates the redox-Bohr effect in tetraheme cytochrome c3 of Desulfovibrio vulgaris (Hildenborough).' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9724528 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saraiva 'L. M.' M. . 2 Salgueiro 'C. A.' A. . 3 'da Costa' 'P. N.' N. . 4 Messias 'A. C.' C. . 5 LeGall J. . . 6 'van Dongen' 'W. M.' M. . 7 Xavier 'A. V.' V. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 37 _Journal_issue 35 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 12160 _Page_last 12165 _Year 1998 _Details ; The structural basis for the pH dependence of the redox potential in the tetrahemic Desulfovibrio vulgaris (Hildenborough) cytochrome c3 was investigated by site-directed mutagenesis of charged residues in the vicinity of heme I. Mutation of lysine 45, located in the neighborhood of the propionates of heme I, by uncharged residues, namely threonine, glutamine and leucine, was performed. The replacement of a conserved charged residue, aspartate 7, present in the N-terminal region and near heme I was also attempted. The analysis of the redox interactions as well as the redox-Bohr behavior of the mutated cytochromes c3 allowed the conclusion that residue 45 has a functional role in the control of the pKa of the propionate groups of heme I and confirms the involvement of this residue in the redox-Bohr effect. ; save_ ################################## # Molecular system description # ################################## save_system_K45Q_cyt_c3 _Saveframe_category molecular_system _Mol_system_name 'K45Q cytochrome c3' _Abbreviation_common 'K45Q cyt c3' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'K45Q cytochrome c3' $cyt_c3 'heme, I' $HEC 'heme, II' $HEC 'heme, III' $HEC 'heme, IV' $HEC 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_cyt_c3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'K45Q cytochrome c3' _Abbreviation_common 'K45Q cyt c3' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; APKAPADGLKMEATKQPVVF NHSTHKSVKCGDCHHPVNGK EDYRQCGTAGCHDSMDKKDK SAKGYYHVMHDKNTKFKSCV GCHVEVAGADAAKKKDLTGC KKSKCHE ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 PRO 3 LYS 4 ALA 5 PRO 6 ALA 7 ASP 8 GLY 9 LEU 10 LYS 11 MET 12 GLU 13 ALA 14 THR 15 LYS 16 GLN 17 PRO 18 VAL 19 VAL 20 PHE 21 ASN 22 HIS 23 SER 24 THR 25 HIS 26 LYS 27 SER 28 VAL 29 LYS 30 CYS 31 GLY 32 ASP 33 CYS 34 HIS 35 HIS 36 PRO 37 VAL 38 ASN 39 GLY 40 LYS 41 GLU 42 ASP 43 TYR 44 ARG 45 GLN 46 CYS 47 GLY 48 THR 49 ALA 50 GLY 51 CYS 52 HIS 53 ASP 54 SER 55 MET 56 ASP 57 LYS 58 LYS 59 ASP 60 LYS 61 SER 62 ALA 63 LYS 64 GLY 65 TYR 66 TYR 67 HIS 68 VAL 69 MET 70 HIS 71 ASP 72 LYS 73 ASN 74 THR 75 LYS 76 PHE 77 LYS 78 SER 79 CYS 80 VAL 81 GLY 82 CYS 83 HIS 84 VAL 85 GLU 86 VAL 87 ALA 88 GLY 89 ALA 90 ASP 91 ALA 92 ALA 93 LYS 94 LYS 95 LYS 96 ASP 97 LEU 98 THR 99 GLY 100 CYS 101 LYS 102 LYS 103 SER 104 LYS 105 CYS 106 HIS 107 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-21 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4291 cytochrome_c3_peptide 100.00 107 99.07 100.00 8.95e-69 BMRB 5239 c3 100.00 107 99.07 100.00 8.95e-69 BMRB 5625 cyt_c3 100.00 107 99.07 100.00 8.95e-69 PDB 1A2I "Solution Structure Of Desulfovibrio Vulgaris (Hildenborough) Ferrocytochrome C3, Nmr, 20 Structures" 100.00 107 99.07 100.00 8.95e-69 PDB 1GX7 "Best Model Of The Electron Transfer Complex Between Cytochrome C3 And [fe]-Hydrogenase" 100.00 107 99.07 100.00 8.95e-69 PDB 1MDV "Key Role Of Phenylalanine 20 In Cytochrome C3: Structure, Stability And Function Studies" 100.00 107 98.13 99.07 3.42e-68 PDB 2BPN "Solution Structure Of Desulfovibrio Vulgaris (Hildenborough) Ferricytochrome C3, Nmr, 20 Structures" 100.00 107 99.07 100.00 8.95e-69 PDB 2CTH "Cytochrome C3 From Desulfovibrio Vulgaris Hildenborough" 100.00 107 99.07 100.00 8.95e-69 PDB 2CYM "Effects Of Amino Acid Substitution On Three-Dimensional Structure: An X-Ray Analysis Of Cytochrome C3 From Desulfovibrio Vulgar" 100.00 107 99.07 100.00 8.95e-69 EMBL CAA27847 "unnamed protein product [Desulfovibrio vulgaris str. Hildenborough]" 100.00 129 99.07 100.00 4.14e-69 GB AAS97641 "cytochrome c3 [Desulfovibrio vulgaris str. Hildenborough]" 100.00 129 99.07 100.00 4.14e-69 GB ABM27239 "cytochrome c, class III [Desulfovibrio vulgaris DP4]" 100.00 129 99.07 100.00 4.14e-69 GB ADP88070 "Cytochrome c, class III, conserved region [Desulfovibrio vulgaris RCH1]" 100.00 129 99.07 100.00 4.14e-69 REF WP_010940429 "cytochrome C [Desulfovibrio vulgaris]" 100.00 129 99.07 100.00 4.14e-69 REF YP_005703708 "cytochrome c, class III, conserved region [Desulfovibrio vulgaris RCH1]" 100.00 129 99.07 100.00 4.14e-69 REF YP_012381 "cytochrome c3 [Desulfovibrio vulgaris str. Hildenborough]" 100.00 129 99.07 100.00 4.14e-69 REF YP_965666 "cytochrome C class III [Desulfovibrio vulgaris DP4]" 100.00 129 99.07 100.00 4.14e-69 SP P00131 "RecName: Full=Cytochrome c3; Flags: Precursor [Desulfovibrio vulgaris str. Hildenborough]" 100.00 129 99.07 100.00 4.14e-69 stop_ save_ ############# # Ligands # ############# save_HEC _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEC (HEME C)" _BMRB_code . _PDB_code HEC _Molecular_mass 618.503 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Aug 8 12:09:17 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 0 . ? CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? NA NA N . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? NB NB N . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? NC NC N . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? ND ND N . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? HHA HHA H . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA1 HMA1 H . 0 . ? HMA2 HMA2 H . 0 . ? HMA3 HMA3 H . 0 . ? HAA1 HAA1 H . 0 . ? HAA2 HAA2 H . 0 . ? HBA1 HBA1 H . 0 . ? HBA2 HBA2 H . 0 . ? H2A H2A H . 0 . ? HMB1 HMB1 H . 0 . ? HMB2 HMB2 H . 0 . ? HMB3 HMB3 H . 0 . ? HAB HAB H . 0 . ? HBB1 HBB1 H . 0 . ? HBB2 HBB2 H . 0 . ? HBB3 HBB3 H . 0 . ? HMC1 HMC1 H . 0 . ? HMC2 HMC2 H . 0 . ? HMC3 HMC3 H . 0 . ? HAC HAC H . 0 . ? HBC1 HBC1 H . 0 . ? HBC2 HBC2 H . 0 . ? HBC3 HBC3 H . 0 . ? HMD1 HMD1 H . 0 . ? HMD2 HMD2 H . 0 . ? HMD3 HMD3 H . 0 . ? HAD1 HAD1 H . 0 . ? HAD2 HAD2 H . 0 . ? HBD1 HBD1 H . 0 . ? HBD2 HBD2 H . 0 . ? H2D H2D H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? DOUB CHA C1A ? ? SING CHA C4D ? ? SING CHA HHA ? ? DOUB CHB C4A ? ? SING CHB C1B ? ? SING CHB HHB ? ? DOUB CHC C4B ? ? SING CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING C1A C2A ? ? DOUB C2A C3A ? ? SING C2A CAA ? ? SING C3A C4A ? ? SING C3A CMA ? ? SING CMA HMA1 ? ? SING CMA HMA2 ? ? SING CMA HMA3 ? ? SING CAA CBA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CBA CGA ? ? SING CBA HBA1 ? ? SING CBA HBA2 ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? SING NB C1B ? ? SING NB C4B ? ? DOUB C1B C2B ? ? SING C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? DOUB C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? SING CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING CBB HBB3 ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? DOUB C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? SING CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? SING CBC HBC3 ? ? SING ND C1D ? ? SING ND C4D ? ? DOUB C1D C2D ? ? SING C2D C3D ? ? SING C2D CMD ? ? DOUB C3D C4D ? ? SING C3D CAD ? ? SING CMD HMD1 ? ? SING CMD HMD2 ? ? SING CMD HMD3 ? ? SING CAD CBD ? ? SING CAD HAD1 ? ? SING CAD HAD2 ? ? SING CBD CGD ? ? SING CBD HBD1 ? ? SING CBD HBD2 ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Fraction $cyt_c3 'Desulfovibrio vulgaris Hildenborough' 881 Eubacteria . Desulfovibrio vulgaris Hildenborough periplasm stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $cyt_c3 'recombinant technology' 'Desulfovibrio desulfuricans G200' Desulfovibrio desulfuricans G200 plasmid pJRD215 'Please see citation_1.' 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 $cyt_c3 0.85 mM . ampicillin 127 uM . kanamicin 78 uM . chloramphenicol 141 uM . H2O 92 % . D2O 8 % . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D-1H-NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-1H-NOESY _Sample_label $sample_1 save_ save_2D-1H-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-1H-TOCSY _Sample_label $sample_1 save_ save_2D-1H-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-1H-COSY _Sample_label $sample_1 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_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 7.1 0.1 pH temperature 303 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 _Indirect_shift_ratio H2O H 1 protons ppm 4.7 internal secondary . . . 1.0 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_ _Experiment_label 2D-1H-NOESY 2D-1H-TOCSY 2D-1H-COSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'K45Q cytochrome c3' _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 ALA HA H 3.62 0.01 1 2 . 1 ALA HB H 0.72 0.01 1 3 . 2 PRO HA H 3.36 0.01 1 4 . 2 PRO HB2 H -0.31 0.01 2 5 . 2 PRO HB3 H 0.80 0.01 2 6 . 2 PRO HG2 H -0.23 0.01 2 7 . 2 PRO HG3 H 0.54 0.01 2 8 . 2 PRO HD2 H 2.66 0.01 2 9 . 2 PRO HD3 H 1.74 0.01 2 10 . 3 LYS H H 6.69 0.01 1 11 . 3 LYS HA H 2.75 0.01 1 12 . 3 LYS HB2 H 0.76 0.01 2 13 . 3 LYS HG2 H 0.67 0.01 2 14 . 3 LYS HD2 H 1.12 0.01 2 15 . 3 LYS HE2 H 2.61 0.01 2 16 . 4 ALA H H 6.69 0.01 1 17 . 4 ALA HA H -2.07 0.01 1 18 . 4 ALA HB H 0.32 0.01 1 19 . 6 ALA H H 8.64 0.01 1 20 . 6 ALA HA H 4.99 0.01 1 21 . 6 ALA HB H 1.91 0.01 1 22 . 7 ASP H H 9.42 0.01 1 23 . 7 ASP HA H 6.33 0.01 1 24 . 7 ASP HB2 H 3.11 0.01 2 25 . 7 ASP HB3 H 3.41 0.01 2 26 . 8 GLY H H 9.05 0.01 1 27 . 8 GLY HA2 H 3.49 0.01 2 28 . 8 GLY HA3 H 4.22 0.01 2 29 . 9 LEU H H 7.54 0.01 1 30 . 9 LEU HA H 4.35 0.01 1 31 . 9 LEU HB2 H 2.39 0.01 2 32 . 9 LEU HB3 H 2.43 0.01 2 33 . 9 LEU HG H 2.21 0.01 1 34 . 9 LEU HD1 H 1.02 0.01 2 35 . 9 LEU HD2 H 1.66 0.01 2 36 . 10 LYS H H 8.64 0.01 1 37 . 10 LYS HA H 4.05 0.01 1 38 . 10 LYS HB2 H 1.49 0.01 2 39 . 10 LYS HB3 H 1.16 0.01 2 40 . 10 LYS HG2 H 1.04 0.01 2 41 . 10 LYS HD2 H 1.56 0.01 2 42 . 10 LYS HE2 H 2.90 0.01 2 43 . 10 LYS HE3 H 2.84 0.01 2 44 . 11 MET H H 8.50 0.01 1 45 . 11 MET HA H 3.60 0.01 1 46 . 11 MET HB2 H 0.69 0.01 2 47 . 11 MET HB3 H 1.03 0.01 2 48 . 11 MET HG2 H 0.92 0.01 2 49 . 11 MET HE H -0.52 0.01 1 50 . 12 GLU H H 8.17 0.01 1 51 . 12 GLU HA H 4.82 0.01 1 52 . 12 GLU HB2 H 1.53 0.01 2 53 . 12 GLU HG2 H 2.06 0.01 2 54 . 13 ALA H H 9.85 0.01 1 55 . 13 ALA HA H 4.28 0.01 1 56 . 13 ALA HB H 1.14 0.01 1 57 . 14 THR H H 10.15 0.01 1 58 . 14 THR HA H 5.06 0.01 1 59 . 14 THR HB H 4.83 0.01 1 60 . 14 THR HG2 H 1.64 0.01 1 61 . 14 THR HG1 H 7.37 0.01 1 62 . 15 LYS H H 8.42 0.01 1 63 . 15 LYS HA H 4.61 0.01 1 64 . 15 LYS HB2 H 2.08 0.01 2 65 . 15 LYS HG2 H 2.35 0.01 2 66 . 15 LYS HG3 H 1.76 0.01 2 67 . 15 LYS HD2 H 1.85 0.01 2 68 . 16 GLN H H 9.31 0.01 1 69 . 16 GLN HA H 5.91 0.01 1 70 . 16 GLN HB2 H 3.55 0.01 2 71 . 16 GLN HB3 H 3.36 0.01 2 72 . 16 GLN HG2 H 2.66 0.01 2 73 . 17 PRO HA H 4.88 0.01 1 74 . 17 PRO HB2 H 2.23 0.01 2 75 . 17 PRO HB3 H 1.78 0.01 2 76 . 17 PRO HG2 H 2.11 0.01 2 77 . 17 PRO HD2 H 4.15 0.01 2 78 . 17 PRO HD3 H 3.73 0.01 2 79 . 18 VAL H H 7.89 0.01 1 80 . 18 VAL HA H 4.17 0.01 1 81 . 18 VAL HB H -0.82 0.01 1 82 . 18 VAL HG1 H -1.25 0.01 2 83 . 18 VAL HG2 H -2.05 0.01 2 84 . 19 VAL H H 7.61 0.01 1 85 . 19 VAL HA H 3.88 0.01 1 86 . 19 VAL HB H 1.47 0.01 1 87 . 19 VAL HG1 H 0.68 0.01 2 88 . 19 VAL HG2 H 0.43 0.01 2 89 . 20 PHE H H 9.02 0.01 1 90 . 20 PHE HA H 3.52 0.01 1 91 . 20 PHE HB2 H 1.62 0.01 2 92 . 20 PHE HB3 H 0.90 0.01 2 93 . 20 PHE HD1 H 6.04 0.01 3 94 . 21 ASN H H 9.05 0.01 1 95 . 21 ASN HA H 6.16 0.01 1 96 . 21 ASN HB2 H 2.95 0.01 2 97 . 21 ASN HD21 H 8.01 0.01 2 98 . 21 ASN HD22 H 5.96 0.01 2 99 . 22 HIS H H 11.86 0.01 1 100 . 22 HIS HA H 8.85 0.01 1 101 . 22 HIS HB2 H 10.58 0.01 2 102 . 22 HIS HB3 H 9.28 0.01 2 103 . 23 SER H H 12.02 0.01 1 104 . 23 SER HA H 5.54 0.01 1 105 . 23 SER HB2 H 4.98 0.01 2 106 . 23 SER HB3 H 4.55 0.01 2 107 . 24 THR H H 8.11 0.01 1 108 . 24 THR HA H 4.64 0.01 1 109 . 24 THR HB H 2.89 0.01 1 110 . 24 THR HG2 H 0.29 0.01 1 111 . 25 HIS H H 10.40 0.01 1 112 . 25 HIS HA H 7.45 0.01 1 113 . 25 HIS HB2 H 9.66 0.01 2 114 . 25 HIS HB3 H 10.64 0.01 2 115 . 26 LYS H H 8.76 0.01 1 116 . 26 LYS HA H 5.64 0.01 1 117 . 26 LYS HB2 H 2.77 0.01 2 118 . 26 LYS HG2 H 2.38 0.01 2 119 . 26 LYS HD2 H 2.30 0.01 2 120 . 26 LYS HE2 H 3.49 0.01 2 121 . 28 VAL H H 8.71 0.01 1 122 . 28 VAL HA H 4.27 0.01 1 123 . 28 VAL HB H 2.74 0.01 1 124 . 28 VAL HG1 H 0.48 0.01 2 125 . 28 VAL HG2 H 0.66 0.01 2 126 . 29 LYS H H 8.60 0.01 1 127 . 29 LYS HA H 4.63 0.01 1 128 . 29 LYS HB2 H 1.96 0.01 2 129 . 29 LYS HB3 H 2.07 0.01 2 130 . 29 LYS HG2 H 1.81 0.01 2 131 . 29 LYS HG3 H 1.76 0.01 2 132 . 30 CYS H H 8.34 0.01 1 133 . 30 CYS HA H 4.82 0.01 1 134 . 30 CYS HB2 H 2.93 0.01 2 135 . 30 CYS HB3 H 2.31 0.01 2 136 . 31 GLY H H 9.17 0.01 1 137 . 31 GLY HA2 H 5.54 0.01 2 138 . 31 GLY HA3 H 4.58 0.01 2 139 . 32 ASP H H 8.15 0.01 1 140 . 32 ASP HA H 5.09 0.01 1 141 . 32 ASP HB2 H 1.94 0.01 2 142 . 32 ASP HB3 H 2.54 0.01 2 143 . 33 CYS H H 7.02 0.01 1 144 . 33 CYS HA H 3.09 0.01 1 145 . 33 CYS HB2 H 0.91 0.01 2 146 . 33 CYS HB3 H -2.81 0.01 2 147 . 34 HIS H H 10.50 0.01 1 148 . 34 HIS HA H 7.05 0.01 1 149 . 34 HIS HB2 H 6.06 0.01 2 150 . 34 HIS HB3 H 13.70 0.01 2 151 . 35 HIS H H 11.59 0.01 1 152 . 35 HIS HA H 9.02 0.01 1 153 . 35 HIS HB2 H 11.23 0.01 2 154 . 35 HIS HB3 H 8.22 0.01 2 155 . 36 PRO HA H 6.45 0.01 1 156 . 36 PRO HB2 H 3.19 0.01 2 157 . 36 PRO HB3 H 3.44 0.01 2 158 . 36 PRO HG2 H 3.43 0.01 2 159 . 36 PRO HG3 H 3.79 0.01 2 160 . 36 PRO HD2 H 6.55 0.01 2 161 . 36 PRO HD3 H 6.27 0.01 2 162 . 37 VAL H H 10.27 0.01 1 163 . 37 VAL HA H 4.71 0.01 1 164 . 37 VAL HB H 2.48 0.01 1 165 . 37 VAL HG1 H 1.51 0.01 2 166 . 37 VAL HG2 H 0.08 0.01 2 167 . 38 ASN H H 9.77 0.01 1 168 . 38 ASN HA H 4.41 0.01 1 169 . 38 ASN HB2 H 2.83 0.01 2 170 . 38 ASN HB3 H 3.08 0.01 2 171 . 38 ASN HD21 H 7.50 0.01 2 172 . 38 ASN HD22 H 6.60 0.01 2 173 . 40 LYS H H 8.11 0.01 1 174 . 40 LYS HA H 5.36 0.01 1 175 . 40 LYS HB2 H 2.27 0.01 2 176 . 40 LYS HB3 H 2.15 0.01 2 177 . 40 LYS HG2 H 1.79 0.01 2 178 . 40 LYS HD2 H 1.96 0.01 2 179 . 40 LYS HE2 H 3.25 0.01 2 180 . 41 GLU H H 9.63 0.01 1 181 . 41 GLU HA H 5.32 0.01 1 182 . 41 GLU HB2 H 2.66 0.01 2 183 . 41 GLU HB3 H 3.08 0.01 2 184 . 41 GLU HG2 H 3.61 0.01 2 185 . 41 GLU HG3 H 3.34 0.01 2 186 . 42 ASP H H 9.19 0.01 1 187 . 42 ASP HA H 5.54 0.01 1 188 . 42 ASP HB2 H 4.33 0.01 2 189 . 42 ASP HB3 H 3.29 0.01 2 190 . 43 TYR H H 9.45 0.01 1 191 . 43 TYR HA H 6.83 0.01 1 192 . 43 TYR HB2 H 2.51 0.01 2 193 . 43 TYR HB3 H 2.96 0.01 2 194 . 43 TYR HD1 H 5.54 0.01 1 195 . 43 TYR HE1 H 5.46 0.01 1 196 . 43 TYR HE2 H 5.46 0.01 1 197 . 43 TYR HD2 H 5.54 0.01 1 198 . 44 ARG H H 8.78 0.01 1 199 . 44 ARG HA H 4.58 0.01 1 200 . 44 ARG HB2 H 2.05 0.01 2 201 . 44 ARG HB3 H 2.06 0.01 2 202 . 44 ARG HG2 H 2.03 0.01 2 203 . 44 ARG HD2 H 3.19 0.01 2 204 . 44 ARG HD3 H 3.47 0.01 2 205 . 44 ARG HE H 8.90 0.01 1 206 . 45 GLN H H 8.41 0.01 1 207 . 45 GLN HA H 4.08 0.01 1 208 . 45 GLN HB2 H 2.73 0.01 2 209 . 45 GLN HB3 H 2.47 0.01 2 210 . 45 GLN HG2 H 2.46 0.01 2 211 . 45 GLN HE21 H 7.52 0.01 2 212 . 45 GLN HE22 H 6.83 0.01 2 213 . 46 CYS H H 7.62 0.01 1 214 . 46 CYS HA H 1.33 0.01 1 215 . 46 CYS HB2 H 0.91 0.01 2 216 . 46 CYS HB3 H 0.00 0.01 2 217 . 47 GLY H H 8.62 0.01 1 218 . 47 GLY HA2 H 5.89 0.01 2 219 . 47 GLY HA3 H 3.90 0.01 2 220 . 48 THR H H 7.40 0.01 1 221 . 48 THR HA H 4.09 0.01 1 222 . 48 THR HB H 4.17 0.01 1 223 . 48 THR HG2 H 1.46 0.01 1 224 . 49 ALA H H 8.55 0.01 1 225 . 49 ALA HA H 4.77 0.01 1 226 . 49 ALA HB H 1.59 0.01 1 227 . 50 GLY H H 9.22 0.01 1 228 . 50 GLY HA2 H 3.81 0.01 2 229 . 50 GLY HA3 H 4.37 0.01 2 230 . 51 CYS H H 9.28 0.01 1 231 . 51 CYS HA H 4.18 0.01 1 232 . 51 CYS HB2 H 4.33 0.01 2 233 . 51 CYS HB3 H 5.17 0.01 2 234 . 52 HIS H H 12.61 0.01 1 235 . 52 HIS HA H 10.81 0.01 1 236 . 52 HIS HB2 H 9.29 0.01 2 237 . 52 HIS HB3 H 16.07 0.01 2 238 . 52 HIS HD1 H 12.86 0.01 1 239 . 53 ASP H H 9.63 0.01 1 240 . 53 ASP HA H 5.77 0.01 1 241 . 53 ASP HB2 H 3.75 0.01 2 242 . 53 ASP HB3 H 3.38 0.01 2 243 . 54 SER H H 9.85 0.01 1 244 . 54 SER HA H 5.57 0.01 1 245 . 54 SER HB2 H 4.56 0.01 2 246 . 54 SER HB3 H 5.12 0.01 2 247 . 55 MET H H 9.73 0.01 1 248 . 55 MET HA H 5.70 0.01 1 249 . 55 MET HB2 H 2.44 0.01 2 250 . 55 MET HB3 H 2.86 0.01 2 251 . 55 MET HG2 H 3.39 0.01 2 252 . 55 MET HG3 H 2.91 0.01 2 253 . 55 MET HE H 2.19 0.01 1 254 . 56 ASP H H 7.73 0.01 1 255 . 56 ASP HA H 5.11 0.01 1 256 . 56 ASP HB2 H 3.09 0.01 2 257 . 56 ASP HB3 H 3.27 0.01 2 258 . 57 LYS H H 9.17 0.01 1 259 . 57 LYS HA H 4.89 0.01 1 260 . 57 LYS HB2 H 1.74 0.01 2 261 . 57 LYS HB3 H 1.86 0.01 2 262 . 57 LYS HG2 H 1.33 0.01 2 263 . 57 LYS HD2 H 1.08 0.01 2 264 . 57 LYS HE2 H 2.58 0.01 2 265 . 58 LYS H H 8.72 0.01 1 266 . 58 LYS HA H 4.47 0.01 1 267 . 58 LYS HB2 H 2.06 0.01 2 268 . 58 LYS HG2 H 1.52 0.01 2 269 . 58 LYS HD2 H 1.76 0.01 2 270 . 58 LYS HE2 H 3.07 0.01 2 271 . 59 ASP H H 8.29 0.01 1 272 . 59 ASP HA H 4.77 0.01 1 273 . 59 ASP HB2 H 3.17 0.01 2 274 . 59 ASP HB3 H 3.99 0.01 2 275 . 60 LYS H H 9.10 0.01 1 276 . 60 LYS HA H 4.60 0.01 1 277 . 60 LYS HB2 H 1.83 0.01 2 278 . 60 LYS HB3 H 2.15 0.01 2 279 . 60 LYS HG2 H 1.81 0.01 2 280 . 60 LYS HD2 H 2.04 0.01 2 281 . 60 LYS HE2 H 3.40 0.01 2 282 . 61 SER H H 9.08 0.01 1 283 . 61 SER HA H 4.48 0.01 1 284 . 61 SER HB2 H 4.28 0.01 2 285 . 62 ALA H H 8.45 0.01 1 286 . 62 ALA HA H 4.20 0.01 1 287 . 62 ALA HB H -0.44 0.01 1 288 . 63 LYS H H 8.31 0.01 1 289 . 63 LYS HA H 6.94 0.01 1 290 . 63 LYS HB2 H 2.74 0.01 2 291 . 63 LYS HB3 H 3.09 0.01 2 292 . 63 LYS HG2 H 2.12 0.01 2 293 . 63 LYS HG3 H 2.02 0.01 2 294 . 63 LYS HD2 H 3.23 0.01 2 295 . 63 LYS HD3 H 3.35 0.01 2 296 . 64 GLY H H 9.72 0.01 1 297 . 64 GLY HA2 H 5.70 0.01 2 298 . 64 GLY HA3 H 5.31 0.01 2 299 . 65 TYR H H 10.30 0.01 1 300 . 65 TYR HA H 6.61 0.01 1 301 . 65 TYR HB2 H 4.95 0.01 2 302 . 65 TYR HB3 H 4.17 0.01 2 303 . 65 TYR HD1 H 8.28 0.01 1 304 . 65 TYR HE1 H 6.37 0.01 1 305 . 65 TYR HE2 H 6.37 0.01 1 306 . 65 TYR HD2 H 8.28 0.01 1 307 . 66 TYR H H 11.25 0.01 1 308 . 66 TYR HA H 6.44 0.01 1 309 . 66 TYR HB2 H 4.73 0.01 2 310 . 66 TYR HB3 H 4.93 0.01 2 311 . 66 TYR HD1 H 8.92 0.01 1 312 . 66 TYR HE1 H 6.02 0.01 1 313 . 66 TYR HE2 H 6.02 0.01 1 314 . 66 TYR HD2 H 8.92 0.01 1 315 . 67 HIS H H 10.68 0.01 1 316 . 67 HIS HA H 6.02 0.01 1 317 . 67 HIS HB2 H 4.77 0.01 2 318 . 67 HIS HB3 H 5.14 0.01 2 319 . 67 HIS HD2 H 8.21 0.01 1 320 . 67 HIS HE1 H 8.80 0.01 1 321 . 68 VAL H H 9.60 0.01 1 322 . 68 VAL HA H 3.90 0.01 1 323 . 68 VAL HB H 0.99 0.01 1 324 . 68 VAL HG1 H 4.20 0.01 2 325 . 68 VAL HG2 H 2.69 0.01 2 326 . 69 MET H H 8.04 0.01 1 327 . 69 MET HA H 3.20 0.01 1 328 . 69 MET HB2 H 0.20 0.01 2 329 . 69 MET HB3 H -1.54 0.01 2 330 . 69 MET HG2 H 2.30 0.01 2 331 . 69 MET HG3 H 2.85 0.01 2 332 . 69 MET HE H -0.40 0.01 1 333 . 70 HIS H H 9.68 0.01 1 334 . 70 HIS HA H 6.90 0.01 1 335 . 70 HIS HB2 H 8.71 0.01 2 336 . 70 HIS HB3 H 8.85 0.01 2 337 . 71 ASP H H 9.24 0.01 1 338 . 71 ASP HA H 5.72 0.01 1 339 . 71 ASP HB2 H 3.34 0.01 2 340 . 72 LYS H H 8.88 0.01 1 341 . 73 ASN HA H 4.54 0.01 1 342 . 73 ASN HB2 H 2.92 0.01 2 343 . 73 ASN HD21 H 7.63 0.01 2 344 . 73 ASN HD22 H 6.87 0.01 2 345 . 74 THR H H 7.06 0.01 1 346 . 74 THR HA H 4.09 0.01 1 347 . 74 THR HB H 3.98 0.01 1 348 . 74 THR HG2 H 0.69 0.01 1 349 . 74 THR HG1 H 5.15 0.01 1 350 . 75 LYS H H 8.87 0.01 1 351 . 75 LYS HA H 3.57 0.01 1 352 . 75 LYS HB2 H 1.26 0.01 2 353 . 75 LYS HB3 H 0.83 0.01 2 354 . 75 LYS HG2 H 0.47 0.01 2 355 . 75 LYS HD2 H 0.95 0.01 2 356 . 75 LYS HE2 H 2.75 0.01 2 357 . 76 PHE H H 6.18 0.01 1 358 . 76 PHE HA H 4.92 0.01 1 359 . 76 PHE HB2 H 2.22 0.01 2 360 . 76 PHE HB3 H 3.72 0.01 2 361 . 76 PHE HD1 H 8.43 0.01 1 362 . 76 PHE HE1 H 8.80 0.01 1 363 . 76 PHE HZ H 9.26 0.01 1 364 . 76 PHE HE2 H 8.80 0.01 1 365 . 76 PHE HD2 H 8.43 0.01 1 366 . 77 LYS H H 8.26 0.01 1 367 . 77 LYS HA H 3.24 0.01 1 368 . 77 LYS HB2 H 0.24 0.01 2 369 . 77 LYS HB3 H -0.01 0.01 2 370 . 77 LYS HG2 H 0.82 0.01 2 371 . 77 LYS HD2 H 0.65 0.01 2 372 . 77 LYS HD3 H 0.85 0.01 2 373 . 77 LYS HE2 H 2.59 0.01 2 374 . 78 SER H H 7.36 0.01 1 375 . 78 SER HA H 2.34 0.01 1 376 . 78 SER HB2 H 5.05 0.01 2 377 . 78 SER HB3 H 2.96 0.01 2 378 . 79 CYS HA H -2.67 0.01 1 379 . 79 CYS HB2 H 0.55 0.01 2 380 . 80 VAL H H 6.50 0.01 1 381 . 80 VAL HA H 4.46 0.01 1 382 . 80 VAL HB H 2.99 0.01 1 383 . 80 VAL HG1 H 1.73 0.01 2 384 . 80 VAL HG2 H 2.18 0.01 2 385 . 81 GLY H H 7.87 0.01 1 386 . 81 GLY HA2 H 3.45 0.01 2 387 . 81 GLY HA3 H 3.97 0.01 2 388 . 82 CYS H H 7.32 0.01 1 389 . 82 CYS HA H 3.56 0.01 1 390 . 82 CYS HB2 H 0.19 0.01 2 391 . 82 CYS HB3 H -1.52 0.01 2 392 . 83 HIS H H 8.55 0.01 1 393 . 83 HIS HA H 6.70 0.01 1 394 . 83 HIS HB2 H 19.73 0.01 2 395 . 83 HIS HB3 H 14.42 0.01 2 396 . 84 VAL H H 9.51 0.01 1 397 . 84 VAL HA H 4.22 0.01 1 398 . 84 VAL HB H 2.51 0.01 1 399 . 84 VAL HG1 H 1.24 0.01 2 400 . 84 VAL HG2 H 1.60 0.01 2 401 . 85 GLU H H 7.33 0.01 1 402 . 85 GLU HA H 4.24 0.01 1 403 . 85 GLU HB2 H 2.24 0.01 2 404 . 85 GLU HB3 H 2.12 0.01 2 405 . 85 GLU HG2 H 2.41 0.01 2 406 . 86 VAL H H 8.35 0.01 1 407 . 86 VAL HA H 3.85 0.01 1 408 . 86 VAL HB H 2.80 0.01 1 409 . 86 VAL HG1 H 1.14 0.01 2 410 . 86 VAL HG2 H 1.44 0.01 2 411 . 87 ALA H H 9.04 0.01 1 412 . 87 ALA HA H 4.08 0.01 1 413 . 87 ALA HB H 1.71 0.01 1 414 . 88 GLY H H 7.48 0.01 1 415 . 88 GLY HA2 H 3.92 0.01 2 416 . 89 ALA H H 8.73 0.01 1 417 . 89 ALA HA H 4.47 0.01 1 418 . 89 ALA HB H 1.51 0.01 1 419 . 90 ASP H H 7.76 0.01 1 420 . 90 ASP HA H 4.58 0.01 1 421 . 90 ASP HB2 H 2.65 0.01 2 422 . 90 ASP HB3 H 3.19 0.01 2 423 . 91 ALA H H 8.87 0.01 1 424 . 91 ALA HA H 3.99 0.01 1 425 . 91 ALA HB H 1.53 0.01 1 426 . 92 ALA H H 8.20 0.01 1 427 . 92 ALA HA H 4.16 0.01 1 428 . 92 ALA HB H 1.46 0.01 1 429 . 93 LYS H H 8.14 0.01 1 430 . 93 LYS HA H 4.03 0.01 1 431 . 93 LYS HB2 H 2.02 0.01 2 432 . 93 LYS HB3 H 1.69 0.01 2 433 . 93 LYS HG2 H 1.30 0.01 2 434 . 93 LYS HD2 H 1.52 0.01 2 435 . 93 LYS HE2 H 2.75 0.01 2 436 . 94 LYS H H 8.92 0.01 1 437 . 94 LYS HA H 4.06 0.01 1 438 . 94 LYS HB2 H 2.00 0.01 2 439 . 94 LYS HG2 H 1.54 0.01 2 440 . 94 LYS HD2 H 1.78 0.01 2 441 . 94 LYS HE2 H 3.11 0.01 2 442 . 95 LYS H H 7.94 0.01 1 443 . 95 LYS HA H 4.21 0.01 1 444 . 95 LYS HB2 H 2.11 0.01 2 445 . 95 LYS HB3 H 2.04 0.01 2 446 . 95 LYS HG2 H 1.71 0.01 2 447 . 95 LYS HG3 H 1.58 0.01 2 448 . 96 ASP H H 7.98 0.01 1 449 . 96 ASP HA H 4.51 0.01 1 450 . 96 ASP HB2 H 2.49 0.01 2 451 . 96 ASP HB3 H 1.84 0.01 2 452 . 97 LEU H H 8.95 0.01 1 453 . 97 LEU HA H 5.16 0.01 1 454 . 97 LEU HB2 H 2.93 0.01 2 455 . 97 LEU HB3 H 3.52 0.01 2 456 . 97 LEU HG H 1.40 0.01 1 457 . 97 LEU HD1 H 0.49 0.01 2 458 . 97 LEU HD2 H -2.24 0.01 2 459 . 98 THR H H 8.97 0.01 1 460 . 98 THR HA H 6.28 0.01 1 461 . 98 THR HB H 5.18 0.01 1 462 . 98 THR HG2 H 2.23 0.01 1 463 . 99 GLY H H 8.01 0.01 1 464 . 99 GLY HA2 H 4.51 0.01 2 465 . 99 GLY HA3 H 4.71 0.01 2 466 . 100 CYS H H 8.65 0.01 1 467 . 100 CYS HA H 3.11 0.01 1 468 . 100 CYS HB2 H 1.57 0.01 2 469 . 100 CYS HB3 H -0.12 0.01 2 470 . 101 LYS H H 7.51 0.01 1 471 . 101 LYS HA H 5.28 0.01 1 472 . 101 LYS HB2 H 1.89 0.01 2 473 . 101 LYS HB3 H 1.58 0.01 2 474 . 101 LYS HG2 H 1.15 0.01 2 475 . 101 LYS HD2 H 1.70 0.01 2 476 . 101 LYS HE2 H 2.85 0.01 2 477 . 101 LYS HE3 H 2.73 0.01 2 478 . 102 LYS H H 9.51 0.01 1 479 . 102 LYS HA H 4.54 0.01 1 480 . 102 LYS HB2 H 2.18 0.01 2 481 . 102 LYS HG2 H 1.61 0.01 2 482 . 102 LYS HD2 H 1.91 0.01 2 483 . 103 SER H H 9.59 0.01 1 484 . 103 SER HA H 5.53 0.01 1 485 . 103 SER HB2 H 4.39 0.01 2 486 . 103 SER HB3 H 5.01 0.01 2 487 . 103 SER HG H 6.18 0.01 1 488 . 104 LYS H H 9.59 0.01 1 489 . 104 LYS HA H 4.02 0.01 1 490 . 104 LYS HB2 H 0.41 0.01 2 491 . 104 LYS HG2 H 0.65 0.01 2 492 . 104 LYS HD2 H 0.79 0.01 2 493 . 104 LYS HD3 H 0.46 0.01 2 494 . 104 LYS HE2 H 2.15 0.01 2 495 . 105 CYS H H 7.77 0.01 1 496 . 105 CYS HA H 4.98 0.01 1 497 . 105 CYS HB2 H 4.36 0.01 2 498 . 106 HIS H H 9.50 0.01 1 499 . 106 HIS HA H 8.65 0.01 1 500 . 106 HIS HB2 H 7.56 0.01 2 501 . 106 HIS HB3 H 18.47 0.01 2 502 . 107 GLU H H 9.97 0.01 1 503 . 107 GLU HA H 4.84 0.01 1 504 . 107 GLU HB2 H 2.58 0.01 2 505 . 107 GLU HG2 H 2.76 0.01 2 stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'heme, I' _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 HAC H -3.16 0.01 1 2 . 1 HEC HBC H -2.36 0.01 1 3 . 1 HEC HMC H 9.66 0.01 1 4 . 1 HEC HHD H -6.20 0.01 1 5 . 1 HEC HMD H 18.14 0.01 1 6 . 1 HEC HAD1 H -0.05 0.01 2 7 . 1 HEC HAD2 H -3.39 0.01 2 8 . 1 HEC HBD1 H 1.40 0.01 2 9 . 1 HEC HBD2 H 0.47 0.01 2 10 . 1 HEC HHA H 11.74 0.01 1 11 . 1 HEC HAA1 H 5.46 0.01 2 12 . 1 HEC HBA1 H 2.74 0.01 2 13 . 1 HEC HBA2 H 2.45 0.01 2 14 . 1 HEC HMA H 29.28 0.01 1 15 . 1 HEC HHB H -3.42 0.01 1 16 . 1 HEC HMB H 18.47 0.01 1 17 . 1 HEC HAB H 2.93 0.01 1 18 . 1 HEC HBB H 0.71 0.01 1 19 . 1 HEC HHC H 12.52 0.01 1 stop_ save_ save_shift_set_3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'heme, II' _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 HAC H 2.13 0.01 1 2 . 1 HEC HBC H 2.27 0.01 1 3 . 1 HEC HMC H 22.08 0.01 1 4 . 1 HEC HHD H 1.07 0.01 1 5 . 1 HEC HMD H 5.16 0.01 1 6 . 1 HEC HAD1 H 1.45 0.01 2 7 . 1 HEC HAD2 H -1.14 0.01 2 8 . 1 HEC HBD1 H -0.90 0.01 2 9 . 1 HEC HBD2 H -0.94 0.01 2 10 . 1 HEC HHA H 2.18 0.01 1 11 . 1 HEC HAA1 H 12.58 0.01 2 12 . 1 HEC HAA2 H 6.32 0.01 2 13 . 1 HEC HBA1 H -0.40 0.01 2 14 . 1 HEC HBA2 H 1.03 0.01 2 15 . 1 HEC HMA H 22.12 0.01 1 16 . 1 HEC HHB H 0.97 0.01 1 17 . 1 HEC HMB H 4.20 0.01 1 18 . 1 HEC HAB H -1.55 0.01 1 19 . 1 HEC HBB H -3.20 0.01 1 20 . 1 HEC HHC H 3.46 0.01 1 stop_ save_ save_shift_set_4 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'heme, III' _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 HAC H -0.69 0.01 1 2 . 1 HEC HBC H -0.75 0.01 1 3 . 1 HEC HMC H 9.93 0.01 1 4 . 1 HEC HHD H 10.30 0.01 1 5 . 1 HEC HMD H 20.37 0.01 1 6 . 1 HEC HAD1 H 17.04 0.01 2 7 . 1 HEC HAD2 H 16.87 0.01 2 8 . 1 HEC HBD1 H 0.06 0.01 2 9 . 1 HEC HBD2 H -1.18 0.01 2 10 . 1 HEC HHA H -0.54 0.01 1 11 . 1 HEC HAA1 H -2.53 0.01 2 12 . 1 HEC HAA2 H 6.61 0.01 2 13 . 1 HEC HBA1 H 0.66 0.01 2 14 . 1 HEC HBA2 H -3.69 0.01 2 15 . 1 HEC HMA H -3.80 0.01 1 16 . 1 HEC HHB H 8.90 0.01 1 17 . 1 HEC HMB H 13.55 0.01 1 18 . 1 HEC HAB H -0.78 0.01 1 19 . 1 HEC HBB H -2.20 0.01 1 20 . 1 HEC HHC H -2.35 0.01 1 stop_ save_ save_shift_set_5 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'heme, IV' _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 HAC H 1.64 0.01 1 2 . 1 HEC HBC H -0.55 0.01 1 3 . 1 HEC HMC H 9.93 0.01 1 4 . 1 HEC HHD H -3.66 0.01 1 5 . 1 HEC HMD H 17.02 0.01 1 6 . 1 HEC HAD1 H -3.45 0.01 2 7 . 1 HEC HAD2 H -0.16 0.01 2 8 . 1 HEC HBD1 H 1.37 0.01 2 9 . 1 HEC HBD2 H 0.51 0.01 2 10 . 1 HEC HHA H 11.89 0.01 1 11 . 1 HEC HAA1 H 9.17 0.01 2 12 . 1 HEC HAA2 H 5.60 0.01 2 13 . 1 HEC HBA1 H 3.26 0.01 2 14 . 1 HEC HMA H 29.51 0.01 1 15 . 1 HEC HHB H -0.27 0.01 1 16 . 1 HEC HMB H 17.95 0.01 1 17 . 1 HEC HAB H 1.54 0.01 1 18 . 1 HEC HBB H 0.94 0.01 1 19 . 1 HEC HHC H 12.50 0.01 1 stop_ save_