data_15073 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR assignments of CO-bound ferrous Corynebacterium diphtheria Heme Oxygenase ; _BMRB_accession_number 15073 _BMRB_flat_file_name bmr15073.str _Entry_type original _Submission_date 2006-12-12 _Accession_date 2006-12-12 _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 Hom Kellie . . 2 Deshmukh Rahul . . 3 Furci Lena M. . 4 Wilks Angela . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 163 "13C chemical shifts" 472 "15N chemical shifts" 163 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-31 update BMRB 'complete entry citation; add related entry' 2007-06-26 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15070 'apo cd-HO-G135A' 15071 'apo Corynebacterium diptheriae heme oxygenase' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR assignments of cd-HO, a 24 kDa heme oxygenase from Corynebacterium diphtheria' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19636825 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hom Kellie . . 2 Deshmukh Rahul . . 3 Furci Lena M. . 4 Wilks Angela . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 1 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 55 _Page_last 56 _Year 2007 _Details . loop_ _Keyword 'Corynebacterium diptheriae' 'heme oxygenase' NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name cdHO _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'heme oxygenase' $heme_oxygenase 'ferrous heme' $HEM stop_ _System_molecular_weight 24138 _System_physical_state native _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details 'heme oxygenase with CO-bound ferrous heme' save_ ######################## # Monomeric polymers # ######################## save_heme_oxygenase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common heme_oxygenase _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 215 _Mol_residue_sequence ; MTTATAGLAVELKQSTAQAH EKAEHSTFMSDLLKGRLGVA EFTRLQEQAWLFYTALEQAV DAVRASGFAESLLDPALNRA EVLARDLDKLNGSSEWRSRI TASPAVIDYVNRLEEIRDNV DGPALVAHHYVRYLGDLSGG QVIARMMQRHYGVDPEALGF YHFEGIAKLKVYKDEYREKL NNLELSDEQREHLLKEATDA FVFNHQVFADLGKGL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 THR 4 ALA 5 THR 6 ALA 7 GLY 8 LEU 9 ALA 10 VAL 11 GLU 12 LEU 13 LYS 14 GLN 15 SER 16 THR 17 ALA 18 GLN 19 ALA 20 HIS 21 GLU 22 LYS 23 ALA 24 GLU 25 HIS 26 SER 27 THR 28 PHE 29 MET 30 SER 31 ASP 32 LEU 33 LEU 34 LYS 35 GLY 36 ARG 37 LEU 38 GLY 39 VAL 40 ALA 41 GLU 42 PHE 43 THR 44 ARG 45 LEU 46 GLN 47 GLU 48 GLN 49 ALA 50 TRP 51 LEU 52 PHE 53 TYR 54 THR 55 ALA 56 LEU 57 GLU 58 GLN 59 ALA 60 VAL 61 ASP 62 ALA 63 VAL 64 ARG 65 ALA 66 SER 67 GLY 68 PHE 69 ALA 70 GLU 71 SER 72 LEU 73 LEU 74 ASP 75 PRO 76 ALA 77 LEU 78 ASN 79 ARG 80 ALA 81 GLU 82 VAL 83 LEU 84 ALA 85 ARG 86 ASP 87 LEU 88 ASP 89 LYS 90 LEU 91 ASN 92 GLY 93 SER 94 SER 95 GLU 96 TRP 97 ARG 98 SER 99 ARG 100 ILE 101 THR 102 ALA 103 SER 104 PRO 105 ALA 106 VAL 107 ILE 108 ASP 109 TYR 110 VAL 111 ASN 112 ARG 113 LEU 114 GLU 115 GLU 116 ILE 117 ARG 118 ASP 119 ASN 120 VAL 121 ASP 122 GLY 123 PRO 124 ALA 125 LEU 126 VAL 127 ALA 128 HIS 129 HIS 130 TYR 131 VAL 132 ARG 133 TYR 134 LEU 135 GLY 136 ASP 137 LEU 138 SER 139 GLY 140 GLY 141 GLN 142 VAL 143 ILE 144 ALA 145 ARG 146 MET 147 MET 148 GLN 149 ARG 150 HIS 151 TYR 152 GLY 153 VAL 154 ASP 155 PRO 156 GLU 157 ALA 158 LEU 159 GLY 160 PHE 161 TYR 162 HIS 163 PHE 164 GLU 165 GLY 166 ILE 167 ALA 168 LYS 169 LEU 170 LYS 171 VAL 172 TYR 173 LYS 174 ASP 175 GLU 176 TYR 177 ARG 178 GLU 179 LYS 180 LEU 181 ASN 182 ASN 183 LEU 184 GLU 185 LEU 186 SER 187 ASP 188 GLU 189 GLN 190 ARG 191 GLU 192 HIS 193 LEU 194 LEU 195 LYS 196 GLU 197 ALA 198 THR 199 ASP 200 ALA 201 PHE 202 VAL 203 PHE 204 ASN 205 HIS 206 GLN 207 VAL 208 PHE 209 ALA 210 ASP 211 LEU 212 GLY 213 LYS 214 GLY 215 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 15070 heme_oxygenase 100.00 215 99.53 99.53 9.57e-154 BMRB 15071 cdHO 100.00 215 100.00 100.00 1.38e-154 PDB 1IW0 "Crystal Structure Of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed With Heme In The Ferric State" 100.00 215 100.00 100.00 1.38e-154 PDB 1IW1 "Crystal Structure Of A Heme Oxygenase (Hmuo) From Corynebacterium Diphtheriae Complexed With Heme In The Ferrous State" 100.00 215 100.00 100.00 1.38e-154 PDB 1V8X "Crystal Structure Of The Dioxygen-Bound Heme Oxygenase From Corynebacterium Diphtheriae" 100.00 215 100.00 100.00 1.38e-154 PDB 1WNV "D136a Mutant Of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)" 100.00 215 99.53 99.53 1.95e-153 PDB 1WNW "D136n Mutant Of Heme Oxygenase From Corynebacterium Diphtheriae (hmuo)" 100.00 215 99.53 100.00 6.67e-154 PDB 1WNX "D136e Mutant Of Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo)" 100.00 215 99.53 100.00 7.69e-154 PDB 1WZD "Crystal Structure Of An Artificial Metalloprotein: Fe(10-Ch2ch2cooh- Salophen)WILD TYPE HEME OXYGENASE" 100.00 215 100.00 100.00 1.38e-154 PDB 1WZF "Crystal Structure Of An Artificial Metalloprotein: Fe(10-Cooh- Salophen)WILD TYPE HEME OXYGENASE" 100.00 215 100.00 100.00 1.38e-154 PDB 1WZG "Crystal Structure Of An Artificial Metalloprotein: Fe(Salophen)WILD Type Heme Oxygenase" 100.00 215 100.00 100.00 1.38e-154 PDB 2Z68 "Crystal Structure Of An Artificial Metalloprotein: Cr[n- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]WILD Type Heme Oxygen" 100.00 215 100.00 100.00 1.38e-154 PDB 3I8R "Crystal Structure Of The Heme Oxygenase From Corynebacterium Diphtheriae (Hmuo) In Complex With Heme Binding Ditiothreit" 100.00 215 100.00 100.00 1.38e-154 PDB 3MOO "Crystal Structure Of The Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, In Complex With Azide-Bound Verdoheme" 100.00 215 100.00 100.00 1.38e-154 PDB 4GOH "Structure Of The Substrate-free Hmuo, Ho From Corynebacterium Diphtheriae" 100.00 215 100.00 100.00 1.38e-154 PDB 4GPC "Structure Of The Biliverdin-hmuo, Heme Oxygenase From Corynebacterium Diphtheriae" 100.00 215 100.00 100.00 1.38e-154 PDB 4GPF "Structure Of The Fe3+-biliverdin-hmuo, Heme Oxygenase From Corynebacterium Diphtheriae (data Set Iii)" 100.00 215 100.00 100.00 1.38e-154 PDB 4GPH "Structure Of Hmuo, Heme Oxygenase From Corynebacterium Diphtheriae, In Complex With The Putative Reaction Intermediates Between" 100.00 215 100.00 100.00 1.38e-154 DBJ BAA76407 "Heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 100.00 100.00 1.38e-154 EMBL CAE50198 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 97.67 98.60 3.20e-150 EMBL CKH06070 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 100.00 100.00 1.38e-154 GB AAC44832 "HmuO [Corynebacterium diphtheriae]" 100.00 215 100.00 100.00 1.38e-154 GB AEX42338 "heme oxygenase [Corynebacterium diphtheriae 31A]" 100.00 215 98.60 98.60 6.89e-152 GB AEX44660 "heme oxygenase [Corynebacterium diphtheriae 241]" 100.00 215 98.14 99.07 2.53e-151 GB AEX46855 "heme oxygenase [Corynebacterium diphtheriae INCA 402]" 100.00 215 98.60 99.53 9.21e-153 GB AEX67845 "heme oxygenase [Corynebacterium diphtheriae C7 (beta)]" 100.00 215 100.00 100.00 1.38e-154 REF WP_003852259 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 98.14 99.07 3.76e-151 REF WP_010935240 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 97.67 98.60 3.20e-150 REF WP_014302152 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 98.14 99.07 2.53e-151 REF WP_014303664 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 98.60 99.53 9.21e-153 REF WP_014307115 "heme oxygenase [Corynebacterium diphtheriae]" 100.00 215 99.07 99.07 1.34e-152 SP P71119 "RecName: Full=Heme oxygenase" 100.00 215 97.67 98.60 3.20e-150 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEM (PROTOPORPHYRIN IX CONTAINING FE)" _BMRB_code . _PDB_code HEM _Molecular_mass 616.487 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Oct 5 09:46:19 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? NA NA N . 0 . ? NB NB N . 0 . ? NC NC N . 0 . ? ND ND N . 0 . ? FE FE FE . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA HMA H . 0 . ? HMAA HMAA H . 0 . ? HMAB HMAB H . 0 . ? HAA HAA H . 0 . ? HAAA HAAA H . 0 . ? HBA HBA H . 0 . ? HBAA HBAA H . 0 . ? HMB HMB H . 0 . ? HMBA HMBA H . 0 . ? HMBB HMBB H . 0 . ? HAB HAB H . 0 . ? HBB HBB H . 0 . ? HBBA HBBA H . 0 . ? HMC HMC H . 0 . ? HMCA HMCA H . 0 . ? HMCB HMCB H . 0 . ? HAC HAC H . 0 . ? HBC HBC H . 0 . ? HBCA HBCA H . 0 . ? HMD HMD H . 0 . ? HMDA HMDA H . 0 . ? HMDB HMDB H . 0 . ? HAD HAD H . 0 . ? HADA HADA H . 0 . ? HBD HBD H . 0 . ? HBDA HBDA H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HHA HHA H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? DOUB C1A C2A ? ? SING C1A NA ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING C4A NA ? ? SING CMA HMA ? ? SING CMA HMAA ? ? SING CMA HMAB ? ? SING CAA CBA ? ? SING CAA HAA ? ? SING CAA HAAA ? ? SING CBA CGA ? ? SING CBA HBA ? ? SING CBA HBAA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING C1B C2B ? ? SING C1B NB ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? DOUB C4B NB ? ? SING CMB HMB ? ? SING CMB HMBA ? ? SING CMB HMBB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB ? ? SING CBB HBBA ? ? SING C1C C2C ? ? SING C1C NC ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING C4C NC ? ? SING CMC HMC ? ? SING CMC HMCA ? ? SING CMC HMCB ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC ? ? SING CBC HBCA ? ? SING C1D C2D ? ? DOUB C1D ND ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING C4D ND ? ? SING CMD HMD ? ? SING CMD HMDA ? ? SING CMD HMDB ? ? SING CAD CBD ? ? SING CAD HAD ? ? SING CAD HADA ? ? SING CBD CGD ? ? SING CBD HBD ? ? SING CBD HBDA ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2A H2A ? ? SING O2D H2D ? ? SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $heme_oxygenase 'Corynebacterium diphtheria' 1717 Bacteria . Corynebacterium diphtheriae 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 $heme_oxygenase 'recombinant technology' . Escherichia coli . pET21a 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 $heme_oxygenase . mM 1 2 '[U-13C; U-15N]' $HEM . mM 1 2 'natural abundance' H2O 95 % . . 'natural abundance' D2O 5 % . . [U-2H] 'potassium chloride' 100 mM . . 'natural abundance' 'potassium phosphate' 50 mM . . 'natural abundance' DSS 0.5 mM . . 'natural abundance' CO . mM 1 2 'natural abundance' 'sodium dithionite' . mM 2 5 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.11 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 7 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCA' '3D HNCO' '3D HNCACB' '3D HN(CO)CA' '3D 1H-15N NOESY' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'heme oxygenase' _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 4 4 ALA C C 176.9 0.2 1 2 4 4 ALA CA C 50.13 0.2 1 3 4 4 ALA CB C 16.83 0.2 1 4 5 5 THR H H 8.224 0.02 1 5 5 5 THR C C 173.2 0.2 1 6 5 5 THR CA C 59.20 0.2 1 7 5 5 THR CB C 67.14 0.2 1 8 5 5 THR N N 113.7 0.2 1 9 6 6 ALA H H 8.329 0.02 1 10 6 6 ALA C C 176.5 0.2 1 11 6 6 ALA CA C 49.56 0.2 1 12 6 6 ALA CB C 17.60 0.2 1 13 6 6 ALA N N 126.6 0.2 1 14 7 7 GLY H H 8.414 0.02 1 15 7 7 GLY C C 173.6 0.2 1 16 7 7 GLY CA C 42.30 0.2 1 17 7 7 GLY N N 108.4 0.2 1 18 8 8 LEU H H 8.615 0.02 1 19 8 8 LEU C C 176.8 0.2 1 20 8 8 LEU CA C 55.70 0.2 1 21 8 8 LEU N N 125.0 0.2 1 22 9 9 ALA H H 9.128 0.02 1 23 9 9 ALA C C 179.7 0.2 1 24 9 9 ALA CA C 53.82 0.2 1 25 9 9 ALA CB C 15.79 0.2 1 26 9 9 ALA N N 117.7 0.2 1 27 10 10 VAL H H 7.622 0.02 1 28 10 10 VAL C C 178.9 0.2 1 29 10 10 VAL CA C 62.90 0.2 1 30 10 10 VAL CB C 29.69 0.2 1 31 10 10 VAL N N 119.0 0.2 1 32 11 11 GLU H H 8.204 0.02 1 33 11 11 GLU C C 179.8 0.2 1 34 11 11 GLU CA C 57.24 0.2 1 35 11 11 GLU CB C 27.36 0.2 1 36 11 11 GLU N N 121.7 0.2 1 37 12 12 LEU H H 8.975 0.02 1 38 12 12 LEU C C 177.3 0.2 1 39 12 12 LEU CA C 56.18 0.2 1 40 12 12 LEU CB C 39.39 0.2 1 41 12 12 LEU N N 122.0 0.2 1 42 13 13 LYS H H 7.222 0.02 1 43 13 13 LYS C C 177.9 0.2 1 44 13 13 LYS CA C 57.04 0.2 1 45 13 13 LYS CB C 30.12 0.2 1 46 13 13 LYS N N 121.9 0.2 1 47 14 14 GLN H H 8.561 0.02 1 48 14 14 GLN C C 178.9 0.2 1 49 14 14 GLN CA C 56.16 0.2 1 50 14 14 GLN CB C 26.00 0.2 1 51 14 14 GLN N N 115.9 0.2 1 52 15 15 SER H H 8.681 0.02 1 53 15 15 SER C C 175.1 0.2 1 54 15 15 SER CA C 58.79 0.2 1 55 15 15 SER CB C 60.92 0.2 1 56 15 15 SER N N 114.2 0.2 1 57 16 16 THR H H 7.315 0.02 1 58 16 16 THR C C 173.3 0.2 1 59 16 16 THR CA C 58.62 0.2 1 60 16 16 THR CB C 66.94 0.2 1 61 16 16 THR N N 107.4 0.2 1 62 17 17 ALA H H 6.924 0.02 1 63 17 17 ALA C C 179.6 0.2 1 64 17 17 ALA CA C 53.23 0.2 1 65 17 17 ALA CB C 15.26 0.2 1 66 17 17 ALA N N 126.4 0.2 1 67 18 18 GLN H H 8.300 0.02 1 68 18 18 GLN C C 177.3 0.2 1 69 18 18 GLN CA C 56.22 0.2 1 70 18 18 GLN CB C 25.04 0.2 1 71 18 18 GLN N N 118.0 0.2 1 72 19 19 ALA H H 7.641 0.02 1 73 19 19 ALA C C 179.0 0.2 1 74 19 19 ALA CA C 51.61 0.2 1 75 19 19 ALA CB C 14.50 0.2 1 76 19 19 ALA N N 124.5 0.2 1 77 20 20 HIS H H 7.996 0.02 1 78 20 20 HIS C C 175.2 0.2 1 79 20 20 HIS CA C 58.17 0.2 1 80 20 20 HIS CB C 23.80 0.2 1 81 20 20 HIS N N 121.0 0.2 1 82 21 21 GLU H H 7.209 0.02 1 83 21 21 GLU C C 177.3 0.2 1 84 21 21 GLU CA C 56.67 0.2 1 85 21 21 GLU CB C 26.60 0.2 1 86 21 21 GLU N N 120.4 0.2 1 87 22 22 LYS H H 7.263 0.02 1 88 22 22 LYS C C 177.5 0.2 1 89 22 22 LYS CA C 55.97 0.2 1 90 22 22 LYS CB C 29.50 0.2 1 91 22 22 LYS N N 116.7 0.2 1 92 23 23 ALA H H 7.188 0.02 1 93 23 23 ALA C C 178.2 0.2 1 94 23 23 ALA CA C 52.81 0.2 1 95 23 23 ALA CB C 16.45 0.2 1 96 23 23 ALA N N 121.3 0.2 1 97 24 24 GLU H H 7.676 0.02 1 98 24 24 GLU C C 175.8 0.2 1 99 24 24 GLU CA C 56.69 0.2 1 100 24 24 GLU N N 118.2 0.2 1 101 25 25 HIS H H 7.362 0.02 1 102 25 25 HIS C C 174.3 0.2 1 103 25 25 HIS CA C 52.47 0.2 1 104 25 25 HIS CB C 26.74 0.2 1 105 25 25 HIS N N 111.4 0.2 1 106 26 26 SER H H 7.411 0.02 1 107 26 26 SER CA C 56.30 0.2 1 108 26 26 SER CB C 61.83 0.2 1 109 26 26 SER N N 118.6 0.2 1 110 33 33 LEU C C 175.9 0.2 1 111 34 34 LYS H H 7.523 0.02 1 112 34 34 LYS C C 176.2 0.2 1 113 34 34 LYS CA C 53.33 0.2 1 114 34 34 LYS CB C 30.72 0.2 1 115 34 34 LYS N N 114.7 0.2 1 116 35 35 GLY H H 7.111 0.02 1 117 35 35 GLY C C 174.0 0.2 1 118 35 35 GLY CA C 43.40 0.2 1 119 35 35 GLY N N 106.3 0.2 1 120 36 36 ARG H H 7.960 0.02 1 121 36 36 ARG C C 175.2 0.2 1 122 36 36 ARG CA C 54.11 0.2 1 123 36 36 ARG N N 116.1 0.2 1 124 37 37 LEU H H 7.568 0.02 1 125 37 37 LEU C C 172.6 0.2 1 126 37 37 LEU CA C 49.71 0.2 1 127 37 37 LEU N N 119.5 0.2 1 128 38 38 GLY H H 7.044 0.02 1 129 38 38 GLY C C 170.9 0.2 1 130 38 38 GLY CA C 42.39 0.2 1 131 38 38 GLY N N 110.2 0.2 1 132 39 39 VAL H H 8.465 0.02 1 133 39 39 VAL C C 177.4 0.2 1 134 39 39 VAL CA C 63.04 0.2 1 135 39 39 VAL CB C 29.43 0.2 1 136 39 39 VAL N N 118.4 0.2 1 137 40 40 ALA H H 8.996 0.02 1 138 40 40 ALA C C 178.2 0.2 1 139 40 40 ALA CA C 53.52 0.2 1 140 40 40 ALA CB C 15.18 0.2 1 141 40 40 ALA N N 126.9 0.2 1 142 41 41 GLU H H 8.424 0.02 1 143 41 41 GLU N N 118.4 0.2 1 144 47 47 GLU C C 177.2 0.2 1 145 47 47 GLU CA C 56.60 0.2 1 146 48 48 GLN H H 7.182 0.02 1 147 48 48 GLN C C 177.1 0.2 1 148 48 48 GLN CA C 55.62 0.2 1 149 48 48 GLN CB C 25.19 0.2 1 150 48 48 GLN N N 114.7 0.2 1 151 49 49 ALA H H 8.559 0.02 1 152 49 49 ALA C C 178.0 0.2 1 153 49 49 ALA CA C 50.74 0.2 1 154 49 49 ALA CB C 14.05 0.2 1 155 49 49 ALA N N 120.1 0.2 1 156 50 50 TRP H H 8.499 0.02 1 157 50 50 TRP C C 178.3 0.2 1 158 50 50 TRP CA C 61.22 0.2 1 159 50 50 TRP N N 121.4 0.2 1 160 51 51 LEU H H 7.401 0.02 1 161 51 51 LEU CA C 55.53 0.2 1 162 51 51 LEU N N 119.2 0.2 1 163 52 52 PHE H H 7.689 0.02 1 164 52 52 PHE C C 176.9 0.2 1 165 52 52 PHE CA C 56.93 0.2 1 166 52 52 PHE CB C 35.46 0.2 1 167 52 52 PHE N N 115.9 0.2 1 168 53 53 TYR H H 9.861 0.02 1 169 53 53 TYR C C 178.2 0.2 1 170 53 53 TYR CA C 62.21 0.2 1 171 53 53 TYR CB C 34.19 0.2 1 172 53 53 TYR N N 125.5 0.2 1 173 54 54 THR H H 7.618 0.02 1 174 54 54 THR C C 175.7 0.2 1 175 54 54 THR CA C 65.57 0.2 1 176 54 54 THR N N 115.8 0.2 1 177 55 55 ALA H H 6.609 0.02 1 178 55 55 ALA C C 178.7 0.2 1 179 55 55 ALA CA C 52.25 0.2 1 180 55 55 ALA CB C 17.64 0.2 1 181 55 55 ALA N N 122.6 0.2 1 182 56 56 LEU H H 9.060 0.02 1 183 56 56 LEU C C 177.7 0.2 1 184 56 56 LEU CA C 55.82 0.2 1 185 56 56 LEU N N 122.8 0.2 1 186 57 57 GLU H H 8.716 0.02 1 187 57 57 GLU C C 177.8 0.2 1 188 57 57 GLU CA C 58.12 0.2 1 189 57 57 GLU CB C 24.87 0.2 1 190 57 57 GLU N N 118.3 0.2 1 191 58 58 GLN H H 7.508 0.02 1 192 58 58 GLN C C 179.3 0.2 1 193 58 58 GLN CA C 56.57 0.2 1 194 58 58 GLN CB C 26.21 0.2 1 195 58 58 GLN N N 119.8 0.2 1 196 59 59 ALA H H 7.862 0.02 1 197 59 59 ALA C C 178.0 0.2 1 198 59 59 ALA CA C 53.60 0.2 1 199 59 59 ALA CB C 15.07 0.2 1 200 59 59 ALA N N 124.4 0.2 1 201 60 60 VAL H H 9.465 0.02 1 202 60 60 VAL C C 175.4 0.2 1 203 60 60 VAL CA C 64.43 0.2 1 204 60 60 VAL CB C 29.80 0.2 1 205 60 60 VAL N N 120.0 0.2 1 206 61 61 ASP H H 8.167 0.02 1 207 61 61 ASP C C 178.6 0.2 1 208 61 61 ASP CA C 54.90 0.2 1 209 61 61 ASP CB C 37.59 0.2 1 210 61 61 ASP N N 119.1 0.2 1 211 62 62 ALA H H 7.573 0.02 1 212 62 62 ALA C C 179.4 0.2 1 213 62 62 ALA CA C 52.52 0.2 1 214 62 62 ALA CB C 16.70 0.2 1 215 62 62 ALA N N 121.9 0.2 1 216 63 63 VAL H H 8.416 0.02 1 217 63 63 VAL C C 179.1 0.2 1 218 63 63 VAL CA C 64.10 0.2 1 219 63 63 VAL N N 119.3 0.2 1 220 64 64 ARG H H 9.859 0.02 1 221 64 64 ARG C C 179.1 0.2 1 222 64 64 ARG CA C 58.00 0.2 1 223 64 64 ARG CB C 27.60 0.2 1 224 64 64 ARG N N 125.4 0.2 1 225 65 65 ALA H H 7.848 0.02 1 226 65 65 ALA C C 177.6 0.2 1 227 65 65 ALA CA C 52.17 0.2 1 228 65 65 ALA CB C 15.42 0.2 1 229 65 65 ALA N N 120.2 0.2 1 230 66 66 SER H H 7.671 0.02 1 231 66 66 SER C C 174.0 0.2 1 232 66 66 SER CA C 57.09 0.2 1 233 66 66 SER CB C 62.64 0.2 1 234 66 66 SER N N 113.5 0.2 1 235 67 67 GLY H H 8.123 0.02 1 236 67 67 GLY C C 172.3 0.2 1 237 67 67 GLY CA C 42.92 0.2 1 238 67 67 GLY N N 111.2 0.2 1 239 68 68 PHE H H 7.187 0.02 1 240 68 68 PHE C C 171.9 0.2 1 241 68 68 PHE CA C 55.48 0.2 1 242 68 68 PHE CB C 38.26 0.2 1 243 68 68 PHE N N 123.7 0.2 1 244 69 69 ALA H H 8.128 0.02 1 245 69 69 ALA C C 177.0 0.2 1 246 69 69 ALA CA C 49.31 0.2 1 247 69 69 ALA CB C 14.97 0.2 1 248 69 69 ALA N N 123.4 0.2 1 249 70 70 GLU H H 7.584 0.02 1 250 70 70 GLU C C 177.8 0.2 1 251 70 70 GLU CA C 59.06 0.2 1 252 70 70 GLU CB C 27.58 0.2 1 253 70 70 GLU N N 115.8 0.2 1 254 71 71 SER H H 8.275 0.02 1 255 71 71 SER C C 175.6 0.2 1 256 71 71 SER CA C 57.33 0.2 1 257 71 71 SER CB C 60.22 0.2 1 258 71 71 SER N N 110.2 0.2 1 259 72 72 LEU H H 7.440 0.02 1 260 72 72 LEU C C 177.9 0.2 1 261 72 72 LEU CA C 54.29 0.2 1 262 72 72 LEU N N 123.5 0.2 1 263 73 73 LEU H H 7.169 0.02 1 264 73 73 LEU C C 175.9 0.2 1 265 73 73 LEU CA C 50.23 0.2 1 266 73 73 LEU N N 120.2 0.2 1 267 74 74 ASP H H 7.953 0.02 1 268 74 74 ASP C C 176.1 0.2 1 269 74 74 ASP CA C 48.93 0.2 1 270 74 74 ASP CB C 40.28 0.2 1 271 74 74 ASP N N 124.2 0.2 1 272 75 75 PRO C C 177.1 0.2 1 273 75 75 PRO CA C 61.78 0.2 1 274 75 75 PRO CB C 29.38 0.2 1 275 76 76 ALA H H 8.324 0.02 1 276 76 76 ALA C C 178.2 0.2 1 277 76 76 ALA CA C 51.53 0.2 1 278 76 76 ALA CB C 15.89 0.2 1 279 76 76 ALA N N 122.1 0.2 1 280 77 77 LEU H H 7.513 0.02 1 281 77 77 LEU C C 175.8 0.2 1 282 77 77 LEU CA C 52.89 0.2 1 283 77 77 LEU N N 114.2 0.2 1 284 78 78 ASN H H 7.224 0.02 1 285 78 78 ASN CA C 51.78 0.2 1 286 78 78 ASN CB C 35.70 0.2 1 287 78 78 ASN N N 116.3 0.2 1 288 79 79 ARG H H 12.73 0.02 1 289 79 79 ARG C C 177.4 0.2 1 290 79 79 ARG CA C 52.80 0.2 1 291 79 79 ARG CB C 35.13 0.2 1 292 79 79 ARG N N 127.6 0.2 1 293 80 80 ALA H H 9.898 0.02 1 294 80 80 ALA C C 178.7 0.2 1 295 80 80 ALA CA C 55.89 0.2 1 296 80 80 ALA CB C 15.90 0.2 1 297 80 80 ALA N N 124.9 0.2 1 298 81 81 GLU H H 8.390 0.02 1 299 81 81 GLU C C 178.6 0.2 1 300 81 81 GLU CA C 56.90 0.2 1 301 81 81 GLU CB C 26.71 0.2 1 302 81 81 GLU N N 115.1 0.2 1 303 82 82 VAL H H 7.713 0.02 1 304 82 82 VAL C C 176.8 0.2 1 305 82 82 VAL CA C 63.20 0.2 1 306 82 82 VAL CB C 29.15 0.2 1 307 82 82 VAL N N 121.0 0.2 1 308 83 83 LEU H H 8.800 0.02 1 309 83 83 LEU C C 176.9 0.2 1 310 83 83 LEU CA C 54.79 0.2 1 311 83 83 LEU N N 122.6 0.2 1 312 84 84 ALA CA C 52.59 0.2 1 313 84 84 ALA CB C 14.91 0.2 1 314 85 85 ARG H H 7.249 0.02 1 315 85 85 ARG C C 179.2 0.2 1 316 85 85 ARG CA C 57.28 0.2 1 317 85 85 ARG CB C 27.75 0.2 1 318 85 85 ARG N N 116.5 0.2 1 319 86 86 ASP H H 8.222 0.02 1 320 86 86 ASP CA C 55.76 0.2 1 321 86 86 ASP CB C 37.72 0.2 1 322 86 86 ASP N N 123.3 0.2 1 323 87 87 LEU C C 179.0 0.2 1 324 87 87 LEU CA C 55.54 0.2 1 325 88 88 ASP H H 8.346 0.02 1 326 88 88 ASP C C 179.0 0.2 1 327 88 88 ASP CA C 54.40 0.2 1 328 88 88 ASP CB C 37.30 0.2 1 329 88 88 ASP N N 122.4 0.2 1 330 89 89 LYS H H 7.475 0.02 1 331 89 89 LYS C C 179.1 0.2 1 332 89 89 LYS CA C 56.09 0.2 1 333 89 89 LYS CB C 29.83 0.2 1 334 89 89 LYS N N 120.5 0.2 1 335 90 90 LEU H H 9.282 0.02 1 336 90 90 LEU C C 178.5 0.2 1 337 90 90 LEU CA C 55.34 0.2 1 338 90 90 LEU N N 122.0 0.2 1 339 91 91 ASN H H 8.546 0.02 1 340 91 91 ASN C C 175.7 0.2 1 341 91 91 ASN CA C 52.34 0.2 1 342 91 91 ASN CB C 37.84 0.2 1 343 91 91 ASN N N 113.6 0.2 1 344 92 92 GLY H H 7.615 0.02 1 345 92 92 GLY C C 171.8 0.2 1 346 92 92 GLY CA C 43.73 0.2 1 347 92 92 GLY N N 110.2 0.2 1 348 93 93 SER H H 7.984 0.02 1 349 93 93 SER C C 171.9 0.2 1 350 93 93 SER CA C 54.70 0.2 1 351 93 93 SER CB C 61.61 0.2 1 352 93 93 SER N N 112.4 0.2 1 353 94 94 SER H H 8.520 0.02 1 354 94 94 SER C C 175.6 0.2 1 355 94 94 SER CA C 56.03 0.2 1 356 94 94 SER N N 113.2 0.2 1 357 95 95 GLU H H 8.297 0.02 1 358 95 95 GLU C C 175.7 0.2 1 359 95 95 GLU CA C 55.99 0.2 1 360 95 95 GLU CB C 26.62 0.2 1 361 95 95 GLU N N 122.3 0.2 1 362 96 96 TRP H H 7.314 0.02 1 363 96 96 TRP C C 176.1 0.2 1 364 96 96 TRP CA C 55.47 0.2 1 365 96 96 TRP CB C 26.02 0.2 1 366 96 96 TRP N N 119.1 0.2 1 367 97 97 ARG H H 5.964 0.02 1 368 97 97 ARG C C 176.8 0.2 1 369 97 97 ARG CA C 56.68 0.2 1 370 97 97 ARG CB C 26.94 0.2 1 371 97 97 ARG N N 120.7 0.2 1 372 98 98 SER H H 7.381 0.02 1 373 98 98 SER C C 173.3 0.2 1 374 98 98 SER CA C 56.16 0.2 1 375 98 98 SER CB C 61.10 0.2 1 376 98 98 SER N N 111.0 0.2 1 377 99 99 ARG H H 7.381 0.02 1 378 99 99 ARG C C 175.8 0.2 1 379 99 99 ARG CA C 53.62 0.2 1 380 99 99 ARG CB C 29.58 0.2 1 381 99 99 ARG N N 119.6 0.2 1 382 100 100 ILE H H 7.622 0.02 1 383 100 100 ILE C C 174.2 0.2 1 384 100 100 ILE CA C 59.65 0.2 1 385 100 100 ILE CB C 37.13 0.2 1 386 100 100 ILE N N 118.0 0.2 1 387 101 101 THR H H 8.443 0.02 1 388 101 101 THR C C 172.7 0.2 1 389 101 101 THR CA C 57.81 0.2 1 390 101 101 THR CB C 68.96 0.2 1 391 101 101 THR N N 118.5 0.2 1 392 102 102 ALA H H 8.775 0.02 1 393 102 102 ALA C C 176.8 0.2 1 394 102 102 ALA CA C 49.79 0.2 1 395 102 102 ALA CB C 17.50 0.2 1 396 102 102 ALA N N 130.0 0.2 1 397 103 103 SER H H 8.989 0.02 1 398 103 103 SER C C 171.2 0.2 1 399 103 103 SER CA C 55.60 0.2 1 400 103 103 SER CB C 59.38 0.2 1 401 103 103 SER N N 123.4 0.2 1 402 104 104 PRO C C 178.3 0.2 1 403 104 104 PRO CA C 64.50 0.2 1 404 105 105 ALA H H 9.551 0.02 1 405 105 105 ALA C C 179.8 0.2 1 406 105 105 ALA CA C 52.28 0.2 1 407 105 105 ALA CB C 18.07 0.2 1 408 105 105 ALA N N 119.4 0.2 1 409 106 106 VAL H H 7.619 0.02 1 410 106 106 VAL CA C 64.62 0.2 1 411 106 106 VAL CB C 29.33 0.2 1 412 106 106 VAL N N 120.5 0.2 1 413 107 107 ILE C C 177.8 0.2 1 414 107 107 ILE CA C 62.78 0.2 1 415 108 108 ASP H H 7.293 0.02 1 416 108 108 ASP C C 177.0 0.2 1 417 108 108 ASP CA C 55.17 0.2 1 418 108 108 ASP CB C 37.95 0.2 1 419 108 108 ASP N N 118.9 0.2 1 420 109 109 TYR H H 7.998 0.02 1 421 109 109 TYR C C 176.9 0.2 1 422 109 109 TYR CA C 54.37 0.2 1 423 109 109 TYR CB C 36.70 0.2 1 424 109 109 TYR N N 125.2 0.2 1 425 110 110 VAL H H 9.246 0.02 1 426 110 110 VAL C C 176.7 0.2 1 427 110 110 VAL CA C 64.69 0.2 1 428 110 110 VAL N N 118.9 0.2 1 429 111 111 ASN H H 8.491 0.02 1 430 111 111 ASN CA C 53.73 0.2 1 431 111 111 ASN CB C 35.25 0.2 1 432 111 111 ASN N N 118.0 0.2 1 433 113 113 LEU C C 178.3 0.2 1 434 114 114 GLU H H 8.910 0.02 1 435 114 114 GLU C C 177.3 0.2 1 436 114 114 GLU CA C 57.46 0.2 1 437 114 114 GLU CB C 26.78 0.2 1 438 114 114 GLU N N 120.6 0.2 1 439 115 115 GLU H H 7.794 0.02 1 440 115 115 GLU CA C 57.26 0.2 1 441 115 115 GLU CB C 27.92 0.2 1 442 115 115 GLU N N 121.8 0.2 1 443 116 116 ILE C C 177.2 0.2 1 444 116 116 ILE CA C 63.50 0.2 1 445 117 117 ARG H H 8.227 0.02 1 446 117 117 ARG C C 177.4 0.2 1 447 117 117 ARG CA C 57.11 0.2 1 448 117 117 ARG N N 120.0 0.2 1 449 118 118 ASP H H 8.718 0.02 1 450 118 118 ASP C C 177.0 0.2 1 451 118 118 ASP CA C 54.66 0.2 1 452 118 118 ASP CB C 37.33 0.2 1 453 118 118 ASP N N 120.0 0.2 1 454 119 119 ASN H H 8.411 0.02 1 455 119 119 ASN C C 173.2 0.2 1 456 119 119 ASN CA C 50.49 0.2 1 457 119 119 ASN CB C 36.28 0.2 1 458 119 119 ASN N N 116.2 0.2 1 459 120 120 VAL H H 7.895 0.02 1 460 120 120 VAL C C 173.4 0.2 1 461 120 120 VAL CA C 60.50 0.2 1 462 120 120 VAL CB C 27.03 0.2 1 463 120 120 VAL N N 123.1 0.2 1 464 121 121 ASP H H 7.670 0.02 1 465 121 121 ASP C C 174.5 0.2 1 466 121 121 ASP CA C 49.75 0.2 1 467 121 121 ASP CB C 38.11 0.2 1 468 121 121 ASP N N 118.9 0.2 1 469 122 122 GLY H H 7.954 0.02 1 470 122 122 GLY CA C 46.71 0.2 1 471 122 122 GLY N N 111.9 0.2 1 472 123 123 PRO C C 176.4 0.2 1 473 123 123 PRO CA C 63.70 0.2 1 474 124 124 ALA H H 7.265 0.02 1 475 124 124 ALA C C 178.4 0.2 1 476 124 124 ALA CA C 52.46 0.2 1 477 124 124 ALA CB C 16.68 0.2 1 478 124 124 ALA N N 115.3 0.2 1 479 125 125 LEU H H 8.514 0.02 1 480 125 125 LEU C C 178.8 0.2 1 481 125 125 LEU CA C 53.78 0.2 1 482 125 125 LEU N N 119.3 0.2 1 483 126 126 VAL H H 8.680 0.02 1 484 126 126 VAL C C 175.8 0.2 1 485 126 126 VAL CA C 65.21 0.2 1 486 126 126 VAL CB C 28.53 0.2 1 487 126 126 VAL N N 120.1 0.2 1 488 127 127 ALA H H 7.522 0.02 1 489 127 127 ALA C C 178.0 0.2 1 490 127 127 ALA CA C 53.85 0.2 1 491 127 127 ALA CB C 17.30 0.2 1 492 127 127 ALA N N 120.2 0.2 1 493 128 128 HIS H H 7.685 0.02 1 494 128 128 HIS C C 176.4 0.2 1 495 128 128 HIS CA C 59.33 0.2 1 496 128 128 HIS CB C 29.78 0.2 1 497 128 128 HIS N N 115.1 0.2 1 498 129 129 HIS H H 9.120 0.02 1 499 129 129 HIS C C 175.3 0.2 1 500 129 129 HIS CA C 58.85 0.2 1 501 129 129 HIS CB C 31.06 0.2 1 502 129 129 HIS N N 123.0 0.2 1 503 130 130 TYR H H 8.860 0.02 1 504 130 130 TYR C C 175.6 0.2 1 505 130 130 TYR CA C 59.01 0.2 1 506 130 130 TYR CB C 35.74 0.2 1 507 130 130 TYR N N 120.4 0.2 1 508 131 131 VAL H H 8.065 0.02 1 509 131 131 VAL CA C 64.92 0.2 1 510 131 131 VAL N N 115.8 0.2 1 511 134 134 LEU C C 179.2 0.2 1 512 135 135 GLY H H 6.393 0.02 1 513 135 135 GLY C C 172.9 0.2 1 514 135 135 GLY CA C 42.38 0.2 1 515 135 135 GLY N N 106.2 0.2 1 516 136 136 ASP H H 7.676 0.02 1 517 136 136 ASP CA C 55.00 0.2 1 518 136 136 ASP CB C 37.82 0.2 1 519 136 136 ASP N N 126.3 0.2 1 520 137 137 LEU C C 174.9 0.2 1 521 138 138 SER H H 7.071 0.02 1 522 138 138 SER C C 173.9 0.2 1 523 138 138 SER CA C 54.31 0.2 1 524 138 138 SER CB C 61.57 0.2 1 525 138 138 SER N N 113.4 0.2 1 526 139 139 GLY H H 6.094 0.02 1 527 139 139 GLY C C 173.0 0.2 1 528 139 139 GLY CA C 42.26 0.2 1 529 139 139 GLY N N 115.4 0.2 1 530 140 140 GLY H H 7.232 0.02 1 531 140 140 GLY C C 172.9 0.2 1 532 140 140 GLY CA C 43.87 0.2 1 533 140 140 GLY N N 108.6 0.2 1 534 141 141 GLN H H 7.001 0.02 1 535 141 141 GLN C C 178.1 0.2 1 536 141 141 GLN CA C 54.41 0.2 1 537 141 141 GLN CB C 25.46 0.2 1 538 141 141 GLN N N 113.7 0.2 1 539 142 142 VAL H H 6.962 0.02 1 540 142 142 VAL CA C 63.06 0.2 1 541 142 142 VAL N N 119.9 0.2 1 542 144 144 ALA C C 178.9 0.2 1 543 144 144 ALA CA C 52.73 0.2 1 544 144 144 ALA CB C 15.37 0.2 1 545 145 145 ARG H H 7.053 0.02 1 546 145 145 ARG CA C 56.70 0.2 1 547 145 145 ARG N N 116.5 0.2 1 548 149 149 ARG C C 177.4 0.2 1 549 149 149 ARG CA C 56.56 0.2 1 550 149 149 ARG CB C 28.09 0.2 1 551 150 150 HIS H H 8.225 0.02 1 552 150 150 HIS C C 176.7 0.2 1 553 150 150 HIS CA C 55.59 0.2 1 554 150 150 HIS CB C 28.09 0.2 1 555 150 150 HIS N N 113.2 0.2 1 556 151 151 TYR H H 6.906 0.02 1 557 151 151 TYR C C 175.6 0.2 1 558 151 151 TYR CA C 52.80 0.2 1 559 151 151 TYR N N 112.5 0.2 1 560 152 152 GLY H H 7.720 0.02 1 561 152 152 GLY C C 173.6 0.2 1 562 152 152 GLY CA C 44.22 0.2 1 563 152 152 GLY N N 109.3 0.2 1 564 153 153 VAL H H 6.676 0.02 1 565 153 153 VAL C C 173.6 0.2 1 566 153 153 VAL CA C 60.90 0.2 1 567 153 153 VAL CB C 29.95 0.2 1 568 153 153 VAL N N 118.2 0.2 1 569 154 154 ASP H H 8.468 0.02 1 570 154 154 ASP C C 174.6 0.2 1 571 154 154 ASP CA C 49.86 0.2 1 572 154 154 ASP CB C 40.08 0.2 1 573 154 154 ASP N N 129.1 0.2 1 574 155 155 PRO C C 178.2 0.2 1 575 155 155 PRO CA C 62.65 0.2 1 576 155 155 PRO CB C 29.25 0.2 1 577 156 156 GLU H H 9.035 0.02 1 578 156 156 GLU C C 175.0 0.2 1 579 156 156 GLU CA C 55.65 0.2 1 580 156 156 GLU CB C 26.62 0.2 1 581 156 156 GLU N N 117.7 0.2 1 582 157 157 ALA H H 8.159 0.02 1 583 157 157 ALA C C 172.9 0.2 1 584 157 157 ALA CA C 48.77 0.2 1 585 157 157 ALA CB C 16.36 0.2 1 586 157 157 ALA N N 122.0 0.2 1 587 158 158 LEU H H 6.909 0.02 1 588 158 158 LEU C C 178.2 0.2 1 589 158 158 LEU CA C 50.54 0.2 1 590 158 158 LEU N N 117.3 0.2 1 591 159 159 GLY H H 10.00 0.02 1 592 159 159 GLY C C 179.5 0.2 1 593 159 159 GLY CA C 45.37 0.2 1 594 159 159 GLY N N 119.2 0.2 1 595 160 160 PHE H H 8.842 0.02 1 596 160 160 PHE C C 176.9 0.2 1 597 160 160 PHE CA C 58.62 0.2 1 598 160 160 PHE N N 124.7 0.2 1 599 163 163 PHE C C 174.5 0.2 1 600 163 163 PHE CA C 53.96 0.2 1 601 163 163 PHE CB C 36.24 0.2 1 602 164 164 GLU H H 8.569 0.02 1 603 164 164 GLU C C 176.7 0.2 1 604 164 164 GLU CA C 55.74 0.2 1 605 164 164 GLU CB C 27.16 0.2 1 606 164 164 GLU N N 125.0 0.2 1 607 165 165 GLY H H 8.769 0.02 1 608 165 165 GLY C C 172.8 0.2 1 609 165 165 GLY CA C 42.49 0.2 1 610 165 165 GLY N N 108.1 0.2 1 611 166 166 ILE H H 7.233 0.02 1 612 166 166 ILE C C 177.3 0.2 1 613 166 166 ILE N N 120.5 0.2 1 614 167 167 ALA C C 177.6 0.2 1 615 167 167 ALA CA C 52.00 0.2 1 616 167 167 ALA CB C 16.74 0.2 1 617 168 168 LYS H H 8.033 0.02 1 618 168 168 LYS CA C 52.00 0.2 1 619 168 168 LYS CB C 31.06 0.2 1 620 168 168 LYS N N 116.9 0.2 1 621 170 170 LYS C C 177.7 0.2 1 622 170 170 LYS CA C 58.06 0.2 1 623 170 170 LYS CB C 30.13 0.2 1 624 171 171 VAL H H 6.669 0.02 1 625 171 171 VAL C C 176.8 0.2 1 626 171 171 VAL CA C 62.38 0.2 1 627 171 171 VAL CB C 29.70 0.2 1 628 171 171 VAL N N 117.4 0.2 1 629 172 172 TYR H H 8.105 0.02 1 630 172 172 TYR CA C 59.51 0.2 1 631 172 172 TYR CB C 37.15 0.2 1 632 172 172 TYR N N 121.5 0.2 1 633 173 173 LYS C C 177.1 0.2 1 634 173 173 LYS CA C 58.18 0.2 1 635 173 173 LYS CB C 29.78 0.2 1 636 174 174 ASP H H 7.722 0.02 1 637 174 174 ASP C C 178.9 0.2 1 638 174 174 ASP CA C 55.16 0.2 1 639 174 174 ASP CB C 37.31 0.2 1 640 174 174 ASP N N 119.6 0.2 1 641 175 175 GLU H H 8.493 0.02 1 642 175 175 GLU C C 177.7 0.2 1 643 175 175 GLU CA C 56.88 0.2 1 644 175 175 GLU CB C 26.89 0.2 1 645 175 175 GLU N N 122.1 0.2 1 646 176 176 TYR H H 8.872 0.02 1 647 176 176 TYR C C 177.0 0.2 1 648 176 176 TYR CA C 59.65 0.2 1 649 176 176 TYR CB C 36.27 0.2 1 650 176 176 TYR N N 124.7 0.2 1 651 177 177 ARG H H 8.210 0.02 1 652 177 177 ARG C C 177.0 0.2 1 653 177 177 ARG CA C 58.44 0.2 1 654 177 177 ARG CB C 27.71 0.2 1 655 177 177 ARG N N 116.8 0.2 1 656 178 178 GLU H H 7.847 0.02 1 657 178 178 GLU CA C 56.82 0.2 1 658 178 178 GLU CB C 26.84 0.2 1 659 178 178 GLU N N 118.6 0.2 1 660 180 180 LEU C C 177.8 0.2 1 661 180 180 LEU CA C 55.51 0.2 1 662 181 181 ASN H H 8.194 0.02 1 663 181 181 ASN C C 175.7 0.2 1 664 181 181 ASN CA C 52.30 0.2 1 665 181 181 ASN CB C 35.19 0.2 1 666 181 181 ASN N N 117.3 0.2 1 667 182 182 ASN H H 7.725 0.02 1 668 182 182 ASN C C 174.3 0.2 1 669 182 182 ASN CA C 50.52 0.2 1 670 182 182 ASN CB C 37.31 0.2 1 671 182 182 ASN N N 116.2 0.2 1 672 183 183 LEU H H 7.224 0.02 1 673 183 183 LEU C C 175.7 0.2 1 674 183 183 LEU CA C 53.22 0.2 1 675 183 183 LEU CB C 39.73 0.2 1 676 183 183 LEU N N 122.8 0.2 1 677 184 184 GLU H H 8.795 0.02 1 678 184 184 GLU C C 174.2 0.2 1 679 184 184 GLU CA C 53.97 0.2 1 680 184 184 GLU CB C 26.76 0.2 1 681 184 184 GLU N N 128.1 0.2 1 682 185 185 LEU H H 8.164 0.02 1 683 185 185 LEU C C 176.7 0.2 1 684 185 185 LEU CA C 50.46 0.2 1 685 185 185 LEU N N 125.9 0.2 1 686 186 186 SER H H 9.346 0.02 1 687 186 186 SER C C 174.0 0.2 1 688 186 186 SER CA C 54.54 0.2 1 689 186 186 SER CB C 62.54 0.2 1 690 186 186 SER N N 120.2 0.2 1 691 187 187 ASP H H 9.147 0.02 1 692 187 187 ASP C C 178.0 0.2 1 693 187 187 ASP CA C 55.80 0.2 1 694 187 187 ASP CB C 45.74 0.2 1 695 187 187 ASP N N 122.4 0.2 1 696 188 188 GLU H H 8.783 0.02 1 697 188 188 GLU C C 178.8 0.2 1 698 188 188 GLU CA C 57.32 0.2 1 699 188 188 GLU CB C 27.12 0.2 1 700 188 188 GLU N N 119.7 0.2 1 701 189 189 GLN H H 7.908 0.02 1 702 189 189 GLN C C 177.4 0.2 1 703 189 189 GLN CA C 56.51 0.2 1 704 189 189 GLN CB C 28.31 0.2 1 705 189 189 GLN N N 120.0 0.2 1 706 190 190 ARG H H 8.824 0.02 1 707 190 190 ARG C C 176.6 0.2 1 708 190 190 ARG CA C 57.71 0.2 1 709 190 190 ARG CB C 28.12 0.2 1 710 190 190 ARG N N 120.8 0.2 1 711 191 191 GLU H H 8.115 0.02 1 712 191 191 GLU C C 178.2 0.2 1 713 191 191 GLU CA C 57.10 0.2 1 714 191 191 GLU CB C 27.16 0.2 1 715 191 191 GLU N N 118.1 0.2 1 716 192 192 HIS H H 7.999 0.02 1 717 192 192 HIS C C 175.6 0.2 1 718 192 192 HIS CA C 56.32 0.2 1 719 192 192 HIS N N 120.0 0.2 1 720 193 193 LEU H H 7.657 0.02 1 721 193 193 LEU C C 174.6 0.2 1 722 193 193 LEU N N 118.6 0.2 1 723 196 196 GLU C C 177.0 0.2 1 724 196 196 GLU CA C 55.98 0.2 1 725 197 197 ALA H H 8.334 0.02 1 726 197 197 ALA C C 178.7 0.2 1 727 197 197 ALA CA C 52.94 0.2 1 728 197 197 ALA CB C 15.38 0.2 1 729 197 197 ALA N N 120.6 0.2 1 730 198 198 THR H H 7.293 0.02 1 731 198 198 THR C C 175.5 0.2 1 732 198 198 THR CA C 65.66 0.2 1 733 198 198 THR N N 114.2 0.2 1 734 199 199 ASP H H 7.951 0.02 1 735 199 199 ASP C C 177.1 0.2 1 736 199 199 ASP CA C 55.01 0.2 1 737 199 199 ASP CB C 36.75 0.2 1 738 199 199 ASP N N 123.8 0.2 1 739 200 200 ALA H H 9.170 0.02 1 740 200 200 ALA CA C 52.96 0.2 1 741 200 200 ALA CB C 15.49 0.2 1 742 200 200 ALA N N 122.3 0.2 1 743 203 203 PHE C C 177.9 0.2 1 744 203 203 PHE CA C 58.54 0.2 1 745 204 204 ASN H H 7.228 0.02 1 746 204 204 ASN C C 177.2 0.2 1 747 204 204 ASN CA C 55.69 0.2 1 748 204 204 ASN CB C 38.07 0.2 1 749 204 204 ASN N N 116.0 0.2 1 750 205 205 HIS H H 8.956 0.02 1 751 205 205 HIS C C 178.0 0.2 1 752 205 205 HIS CA C 56.34 0.2 1 753 205 205 HIS CB C 29.31 0.2 1 754 205 205 HIS N N 120.1 0.2 1 755 206 206 GLN H H 8.555 0.02 1 756 206 206 GLN C C 177.2 0.2 1 757 206 206 GLN CA C 55.90 0.2 1 758 206 206 GLN CB C 25.63 0.2 1 759 206 206 GLN N N 119.6 0.2 1 760 207 207 VAL H H 8.017 0.02 1 761 207 207 VAL C C 178.0 0.2 1 762 207 207 VAL CA C 65.17 0.2 1 763 207 207 VAL N N 122.5 0.2 1 764 208 208 PHE H H 7.451 0.02 1 765 208 208 PHE C C 178.4 0.2 1 766 208 208 PHE CA C 55.08 0.2 1 767 208 208 PHE N N 116.9 0.2 1 768 209 209 ALA H H 8.453 0.02 1 769 209 209 ALA C C 179.7 0.2 1 770 209 209 ALA CA C 52.98 0.2 1 771 209 209 ALA CB C 15.56 0.2 1 772 209 209 ALA N N 125.2 0.2 1 773 210 210 ASP H H 8.575 0.02 1 774 210 210 ASP C C 179.3 0.2 1 775 210 210 ASP CA C 55.21 0.2 1 776 210 210 ASP CB C 38.09 0.2 1 777 210 210 ASP N N 121.0 0.2 1 778 211 211 LEU H H 8.045 0.02 1 779 211 211 LEU C C 178.6 0.2 1 780 211 211 LEU CA C 55.65 0.2 1 781 211 211 LEU N N 121.8 0.2 1 782 212 212 GLY H H 8.283 0.02 1 783 212 212 GLY C C 174.8 0.2 1 784 212 212 GLY CA C 43.95 0.2 1 785 212 212 GLY N N 105.7 0.2 1 786 213 213 LYS H H 7.813 0.02 1 787 213 213 LYS C C 177.4 0.2 1 788 213 213 LYS CA C 56.09 0.2 1 789 213 213 LYS CB C 30.10 0.2 1 790 213 213 LYS N N 121.8 0.2 1 791 214 214 GLY H H 8.179 0.02 1 792 214 214 GLY C C 174.0 0.2 1 793 214 214 GLY CA C 43.30 0.2 1 794 214 214 GLY N N 107.3 0.2 1 795 215 215 LEU H H 7.768 0.02 1 796 215 215 LEU C C 179.1 0.2 1 797 215 215 LEU CA C 53.03 0.2 1 798 215 215 LEU N N 120.0 0.2 1 stop_ save_