data_15071 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Assignments of the apo Corynebacterium diphtheria Heme Oxygenase ; _BMRB_accession_number 15071 _BMRB_flat_file_name bmr15071.str _Entry_type original _Submission_date 2006-12-07 _Accession_date 2006-12-07 _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 . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 185 "13C chemical shifts" 505 "15N chemical shifts" 180 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' 15073 'complex form, 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 Furci Lena M. . 3 Deshmukh Rahul . . 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 . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name cdHO _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label cdHO $cdHO stop_ _System_molecular_weight 24138 _System_physical_state native _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cdHO _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common cdHO _Molecular_mass 24138 _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 15073 heme_oxygenase 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_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cdHO '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 $cdHO '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 $cdHO . mM 1 2 '[U-13C; U-15N; U-2H]' H2O 95 % . . 'natural abundance' D2O 5 % . . 'natural abundance' DSS 1 mM . . 'natural abundance' 'potassium phosphate' 50 mM . . 'natural abundance' 'potassium chloride' 100 mM . . '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 'chemical shift assignment' 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_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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 7.4 . 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 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCO' '3D HNCA' '3D HN(CO)CA' '3D 1H-15N NOESY' '3D HN(CA)CO' '3D HNCACB' 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 cdHO _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 176.7 0.2 1 2 4 4 ALA CA C 49.32 0.2 1 3 5 5 THR H H 8.220 0.02 1 4 5 5 THR C C 172.9 0.2 1 5 5 5 THR CA C 58.91 0.2 1 6 5 5 THR CB C 67.01 0.2 1 7 5 5 THR N N 113.3 0.2 1 8 6 6 ALA H H 8.321 0.02 1 9 6 6 ALA C C 176.2 0.2 1 10 6 6 ALA CA C 49.44 0.2 1 11 6 6 ALA CB C 17.40 0.2 1 12 6 6 ALA N N 126.0 0.2 1 13 7 7 GLY H H 8.374 0.02 1 14 7 7 GLY C C 173.4 0.2 1 15 7 7 GLY CA C 41.82 0.2 1 16 7 7 GLY N N 107.9 0.2 1 17 8 8 LEU H H 8.606 0.02 1 18 8 8 LEU C C 176.9 0.2 1 19 8 8 LEU CA C 55.15 0.2 1 20 8 8 LEU CB C 38.78 0.2 1 21 8 8 LEU N N 124.3 0.2 1 22 9 9 ALA H H 9.055 0.02 1 23 9 9 ALA C C 179.6 0.2 1 24 9 9 ALA CA C 53.00 0.2 1 25 9 9 ALA CB C 15.39 0.2 1 26 9 9 ALA N N 117.1 0.2 1 27 10 10 VAL H H 7.666 0.02 1 28 10 10 VAL C C 177.1 0.2 1 29 10 10 VAL CA C 62.91 0.2 1 30 10 10 VAL CB C 28.92 0.2 1 31 10 10 VAL N N 119.0 0.2 1 32 11 11 GLU H H 8.094 0.02 1 33 11 11 GLU C C 179.1 0.2 1 34 11 11 GLU CA C 56.82 0.2 1 35 11 11 GLU CB C 26.89 0.2 1 36 11 11 GLU N N 121.5 0.2 1 37 12 12 LEU H H 8.884 0.02 1 38 12 12 LEU C C 178.1 0.2 1 39 12 12 LEU CA C 55.44 0.2 1 40 12 12 LEU CB C 39.16 0.2 1 41 12 12 LEU N N 120.6 0.2 1 42 13 13 LYS H H 7.496 0.02 1 43 13 13 LYS C C 177.7 0.2 1 44 13 13 LYS CA C 56.52 0.2 1 45 13 13 LYS CB C 29.11 0.2 1 46 13 13 LYS N N 121.2 0.2 1 47 14 14 GLN H H 8.168 0.02 1 48 14 14 GLN C C 178.5 0.2 1 49 14 14 GLN CA C 55.64 0.2 1 50 14 14 GLN CB C 25.48 0.2 1 51 14 14 GLN N N 117.2 0.2 1 52 15 15 SER H H 8.507 0.02 1 53 15 15 SER C C 175.4 0.2 1 54 15 15 SER CA C 59.40 0.2 1 55 15 15 SER CB C 60.71 0.2 1 56 15 15 SER N N 115.1 0.2 1 57 16 16 THR H H 7.689 0.02 1 58 16 16 THR C C 174.2 0.2 1 59 16 16 THR CA C 60.49 0.2 1 60 16 16 THR CB C 66.66 0.2 1 61 16 16 THR N N 110.6 0.2 1 62 17 17 ALA H H 7.476 0.02 1 63 17 17 ALA C C 178.9 0.2 1 64 17 17 ALA CA C 52.72 0.2 1 65 17 17 ALA CB C 15.81 0.2 1 66 17 17 ALA N N 124.7 0.2 1 67 18 18 GLN H H 8.242 0.02 1 68 18 18 GLN C C 176.9 0.2 1 69 18 18 GLN CA C 55.25 0.2 1 70 18 18 GLN CB C 25.28 0.2 1 71 18 18 GLN N N 116.4 0.2 1 72 19 19 ALA H H 7.836 0.02 1 73 19 19 ALA C C 178.0 0.2 1 74 19 19 ALA CA C 51.61 0.2 1 75 19 19 ALA CB C 16.18 0.2 1 76 19 19 ALA N N 122.4 0.2 1 77 20 20 HIS H H 8.170 0.02 1 78 20 20 HIS C C 176.6 0.2 1 79 20 20 HIS CA C 55.78 0.2 1 80 20 20 HIS N N 117.7 0.2 1 81 21 21 GLU H H 7.591 0.02 1 82 21 21 GLU CA C 54.61 0.2 1 83 21 21 GLU CB C 29.86 0.2 1 84 21 21 GLU N N 117.0 0.2 1 85 29 29 MET C C 177.1 0.2 1 86 29 29 MET CA C 52.83 0.2 1 87 30 30 SER H H 8.076 0.02 1 88 30 30 SER C C 175.6 0.2 1 89 30 30 SER CA C 58.43 0.2 1 90 30 30 SER CB C 59.97 0.2 1 91 30 30 SER N N 114.2 0.2 1 92 31 31 ASP H H 8.639 0.02 1 93 31 31 ASP CA C 54.96 0.2 1 94 31 31 ASP CB C 36.63 0.2 1 95 31 31 ASP N N 120.0 0.2 1 96 33 33 LEU H H 7.947 0.02 1 97 33 33 LEU C C 175.9 0.2 1 98 33 33 LEU CA C 54.74 0.2 1 99 33 33 LEU CB C 38.62 0.2 1 100 34 34 LYS H H 7.624 0.02 1 101 34 34 LYS CA C 52.92 0.2 1 102 34 34 LYS CB C 29.91 0.2 1 103 34 34 LYS N N 114.3 0.2 1 104 35 35 GLY H H 7.098 0.02 1 105 35 35 GLY C C 173.7 0.2 1 106 35 35 GLY CA C 42.91 0.2 1 107 35 35 GLY N N 106.3 0.2 1 108 36 36 ARG H H 7.961 0.02 1 109 36 36 ARG CA C 53.47 0.2 1 110 36 36 ARG CB C 28.20 0.2 1 111 36 36 ARG N N 115.8 0.2 1 112 37 37 LEU H H 7.432 0.02 1 113 37 37 LEU C C 172.3 0.2 1 114 37 37 LEU CA C 49.54 0.2 1 115 37 37 LEU CB C 37.36 0.2 1 116 37 37 LEU N N 118.7 0.2 1 117 38 38 GLY H H 6.969 0.02 1 118 38 38 GLY C C 170.8 0.2 1 119 38 38 GLY CA C 41.96 0.2 1 120 38 38 GLY N N 109.2 0.2 1 121 39 39 VAL H H 8.555 0.02 1 122 39 39 VAL C C 177.0 0.2 1 123 39 39 VAL CA C 62.59 0.2 1 124 39 39 VAL CB C 28.93 0.2 1 125 39 39 VAL N N 118.4 0.2 1 126 40 40 ALA H H 9.021 0.02 1 127 40 40 ALA CA C 53.26 0.2 1 128 40 40 ALA CB C 15.38 0.2 1 129 40 40 ALA N N 126.7 0.2 1 130 41 41 GLU H H 8.162 0.02 1 131 41 41 GLU C C 177.1 0.2 1 132 41 41 GLU CA C 58.47 0.2 1 133 42 42 PHE H H 7.547 0.02 1 134 42 42 PHE C C 174.7 0.2 1 135 42 42 PHE CA C 57.77 0.2 1 136 42 42 PHE CB C 25.52 0.2 1 137 42 42 PHE N N 118.1 0.2 1 138 43 43 THR H H 8.554 0.02 1 139 43 43 THR C C 174.1 0.2 1 140 43 43 THR CA C 64.68 0.2 1 141 43 43 THR N N 115.4 0.2 1 142 44 44 ARG H H 7.958 0.02 1 143 44 44 ARG CA C 56.72 0.2 1 144 44 44 ARG CB C 27.64 0.2 1 145 44 44 ARG N N 119.4 0.2 1 146 49 49 ALA C C 177.9 0.2 1 147 49 49 ALA CA C 50.01 0.2 1 148 50 50 TRP H H 8.626 0.02 1 149 50 50 TRP C C 178.0 0.2 1 150 50 50 TRP CA C 60.94 0.2 1 151 50 50 TRP CB C 24.52 0.2 1 152 50 50 TRP N N 121.3 0.2 1 153 51 51 LEU H H 7.479 0.02 1 154 51 51 LEU C C 179.3 0.2 1 155 51 51 LEU CA C 55.38 0.2 1 156 51 51 LEU CB C 38.41 0.2 1 157 51 51 LEU N N 118.9 0.2 1 158 52 52 PHE H H 7.727 0.02 1 159 52 52 PHE C C 176.8 0.2 1 160 52 52 PHE CA C 56.35 0.2 1 161 52 52 PHE CB C 35.77 0.2 1 162 52 52 PHE N N 114.8 0.2 1 163 53 53 TYR H H 9.919 0.02 1 164 53 53 TYR C C 177.7 0.2 1 165 53 53 TYR CA C 61.82 0.2 1 166 53 53 TYR CB C 33.81 0.2 1 167 53 53 TYR N N 124.5 0.2 1 168 54 54 THR H H 7.652 0.02 1 169 54 54 THR C C 175.3 0.2 1 170 54 54 THR CA C 64.81 0.2 1 171 54 54 THR N N 115.7 0.2 1 172 55 55 ALA H H 6.720 0.02 1 173 55 55 ALA C C 178.4 0.2 1 174 55 55 ALA CA C 52.14 0.2 1 175 55 55 ALA CB C 16.90 0.2 1 176 55 55 ALA N N 122.0 0.2 1 177 56 56 LEU H H 8.837 0.02 1 178 56 56 LEU CA C 55.58 0.2 1 179 56 56 LEU CB C 38.95 0.2 1 180 56 56 LEU N N 120.6 0.2 1 181 57 57 GLU C C 177.8 0.2 1 182 58 58 GLN H H 7.674 0.02 1 183 58 58 GLN C C 179.2 0.2 1 184 58 58 GLN CA C 56.14 0.2 1 185 58 58 GLN N N 119.5 0.2 1 186 59 59 ALA H H 7.835 0.02 1 187 59 59 ALA C C 177.7 0.2 1 188 59 59 ALA CA C 53.29 0.2 1 189 59 59 ALA CB C 14.82 0.2 1 190 59 59 ALA N N 123.8 0.2 1 191 60 60 VAL H H 9.432 0.02 1 192 60 60 VAL C C 176.7 0.2 1 193 60 60 VAL CA C 63.92 0.2 1 194 60 60 VAL CB C 29.33 0.2 1 195 60 60 VAL N N 119.7 0.2 1 196 61 61 ASP H H 8.274 0.02 1 197 61 61 ASP C C 178.3 0.2 1 198 61 61 ASP CA C 54.52 0.2 1 199 61 61 ASP CB C 37.27 0.2 1 200 61 61 ASP N N 118.6 0.2 1 201 62 62 ALA H H 7.597 0.02 1 202 62 62 ALA C C 179.1 0.2 1 203 62 62 ALA CA C 52.17 0.2 1 204 62 62 ALA CB C 16.39 0.2 1 205 62 62 ALA N N 121.5 0.2 1 206 63 63 VAL H H 8.449 0.02 1 207 63 63 VAL C C 178.9 0.2 1 208 63 63 VAL CA C 63.48 0.2 1 209 63 63 VAL CB C 29.33 0.2 1 210 63 63 VAL N N 119.0 0.2 1 211 64 64 ARG H H 9.867 0.02 1 212 64 64 ARG C C 178.7 0.2 1 213 64 64 ARG CA C 57.53 0.2 1 214 64 64 ARG CB C 27.34 0.2 1 215 64 64 ARG N N 125.0 0.2 1 216 65 65 ALA H H 7.864 0.02 1 217 65 65 ALA C C 177.3 0.2 1 218 65 65 ALA CA C 51.80 0.2 1 219 65 65 ALA CB C 15.33 0.2 1 220 65 65 ALA N N 119.8 0.2 1 221 66 66 SER H H 7.663 0.02 1 222 66 66 SER C C 173.7 0.2 1 223 66 66 SER CA C 56.62 0.2 1 224 66 66 SER CB C 62.51 0.2 1 225 66 66 SER N N 113.1 0.2 1 226 67 67 GLY H H 8.123 0.02 1 227 67 67 GLY C C 172.1 0.2 1 228 67 67 GLY CA C 42.95 0.2 1 229 67 67 GLY N N 110.8 0.2 1 230 68 68 PHE H H 7.146 0.02 1 231 68 68 PHE C C 171.5 0.2 1 232 68 68 PHE CA C 54.88 0.2 1 233 68 68 PHE CB C 38.01 0.2 1 234 68 68 PHE N N 123.1 0.2 1 235 69 69 ALA H H 8.111 0.02 1 236 69 69 ALA C C 176.7 0.2 1 237 69 69 ALA CA C 49.10 0.2 1 238 69 69 ALA CB C 14.44 0.2 1 239 69 69 ALA N N 122.8 0.2 1 240 70 70 GLU H H 7.666 0.02 1 241 70 70 GLU C C 177.4 0.2 1 242 70 70 GLU CA C 58.57 0.2 1 243 70 70 GLU CB C 27.05 0.2 1 244 70 70 GLU N N 115.4 0.2 1 245 71 71 SER H H 8.265 0.02 1 246 71 71 SER C C 175.1 0.2 1 247 71 71 SER CA C 57.00 0.2 1 248 71 71 SER CB C 60.06 0.2 1 249 71 71 SER N N 110.0 0.2 1 250 72 72 LEU H H 7.421 0.02 1 251 72 72 LEU C C 177.6 0.2 1 252 72 72 LEU CA C 53.82 0.2 1 253 72 72 LEU CB C 40.78 0.2 1 254 72 72 LEU N N 122.3 0.2 1 255 73 73 LEU H H 7.190 0.02 1 256 73 73 LEU C C 175.6 0.2 1 257 73 73 LEU CA C 49.72 0.2 1 258 73 73 LEU CB C 34.04 0.2 1 259 73 73 LEU N N 120.1 0.2 1 260 74 74 ASP H H 7.879 0.02 1 261 74 74 ASP CA C 48.94 0.2 1 262 74 74 ASP CB C 39.86 0.2 1 263 74 74 ASP N N 123.6 0.2 1 264 75 75 PRO C C 176.9 0.2 1 265 75 75 PRO CA C 60.93 0.2 1 266 76 76 ALA H H 8.380 0.02 1 267 76 76 ALA C C 177.9 0.2 1 268 76 76 ALA CA C 51.26 0.2 1 269 76 76 ALA CB C 15.40 0.2 1 270 76 76 ALA N N 121.9 0.2 1 271 77 77 LEU H H 7.486 0.02 1 272 77 77 LEU C C 175.7 0.2 1 273 77 77 LEU CA C 52.50 0.2 1 274 77 77 LEU CB C 37.57 0.2 1 275 77 77 LEU N N 114.0 0.2 1 276 78 78 ASN H H 7.284 0.02 1 277 78 78 ASN C C 177.3 0.2 1 278 78 78 ASN CA C 51.74 0.2 1 279 78 78 ASN CB C 35.37 0.2 1 280 78 78 ASN N N 115.5 0.2 1 281 79 79 ARG H H 12.69 0.02 1 282 79 79 ARG C C 177.0 0.2 1 283 79 79 ARG CA C 52.13 0.2 1 284 79 79 ARG N N 127.0 0.2 1 285 80 80 ALA H H 10.24 0.02 1 286 80 80 ALA C C 177.8 0.2 1 287 80 80 ALA CA C 55.69 0.2 1 288 80 80 ALA CB C 15.87 0.2 1 289 80 80 ALA N N 125.1 0.2 1 290 81 81 GLU H H 8.504 0.02 1 291 81 81 GLU C C 178.4 0.2 1 292 81 81 GLU CA C 56.48 0.2 1 293 81 81 GLU CB C 26.11 0.2 1 294 81 81 GLU N N 114.9 0.2 1 295 82 82 VAL H H 7.785 0.02 1 296 82 82 VAL C C 176.5 0.2 1 297 82 82 VAL CA C 62.88 0.2 1 298 82 82 VAL CB C 28.74 0.2 1 299 82 82 VAL N N 120.6 0.2 1 300 83 83 LEU H H 8.703 0.02 1 301 83 83 LEU C C 176.6 0.2 1 302 83 83 LEU CA C 54.74 0.2 1 303 83 83 LEU CB C 39.83 0.2 1 304 83 83 LEU N N 121.7 0.2 1 305 84 84 ALA H H 7.918 0.02 1 306 84 84 ALA C C 177.7 0.2 1 307 84 84 ALA CA C 52.08 0.2 1 308 84 84 ALA N N 119.5 0.2 1 309 85 85 ARG H H 7.350 0.02 1 310 85 85 ARG C C 178.9 0.2 1 311 85 85 ARG CA C 56.88 0.2 1 312 85 85 ARG CB C 27.25 0.2 1 313 85 85 ARG N N 116.5 0.2 1 314 86 86 ASP H H 8.410 0.02 1 315 86 86 ASP C C 178.1 0.2 1 316 86 86 ASP CA C 55.47 0.2 1 317 86 86 ASP CB C 37.16 0.2 1 318 86 86 ASP N N 122.9 0.2 1 319 87 87 LEU H H 8.395 0.02 1 320 87 87 LEU C C 178.7 0.2 1 321 87 87 LEU CA C 55.28 0.2 1 322 87 87 LEU CB C 38.67 0.2 1 323 87 87 LEU N N 120.4 0.2 1 324 88 88 ASP H H 8.475 0.02 1 325 88 88 ASP C C 178.8 0.2 1 326 88 88 ASP CA C 54.59 0.2 1 327 88 88 ASP CB C 36.95 0.2 1 328 88 88 ASP N N 122.1 0.2 1 329 89 89 LYS H H 7.545 0.02 1 330 89 89 LYS C C 178.7 0.2 1 331 89 89 LYS CA C 55.45 0.2 1 332 89 89 LYS N N 120.1 0.2 1 333 90 90 LEU H H 9.192 0.02 1 334 90 90 LEU C C 178.0 0.2 1 335 90 90 LEU CA C 54.90 0.2 1 336 90 90 LEU CB C 39.76 0.2 1 337 90 90 LEU N N 121.5 0.2 1 338 91 91 ASN H H 8.535 0.02 1 339 91 91 ASN C C 175.4 0.2 1 340 91 91 ASN CA C 52.12 0.2 1 341 91 91 ASN CB C 37.69 0.2 1 342 91 91 ASN N N 112.8 0.2 1 343 92 92 GLY H H 7.707 0.02 1 344 92 92 GLY C C 171.7 0.2 1 345 92 92 GLY CA C 43.35 0.2 1 346 92 92 GLY N N 109.9 0.2 1 347 93 93 SER H H 8.002 0.02 1 348 93 93 SER CA C 54.76 0.2 1 349 93 93 SER CB C 61.51 0.2 1 350 93 93 SER N N 112.1 0.2 1 351 94 94 SER H H 8.511 0.02 1 352 94 94 SER C C 175.3 0.2 1 353 94 94 SER CA C 55.38 0.2 1 354 94 94 SER CB C 61.22 0.2 1 355 94 94 SER N N 112.9 0.2 1 356 95 95 GLU H H 8.311 0.02 1 357 95 95 GLU C C 175.3 0.2 1 358 95 95 GLU CA C 55.29 0.2 1 359 95 95 GLU CB C 26.14 0.2 1 360 95 95 GLU N N 121.6 0.2 1 361 96 96 TRP H H 7.266 0.02 1 362 96 96 TRP C C 175.9 0.2 1 363 96 96 TRP CA C 54.89 0.2 1 364 96 96 TRP CB C 25.97 0.2 1 365 96 96 TRP N N 118.9 0.2 1 366 97 97 ARG H H 5.988 0.02 1 367 97 97 ARG C C 176.5 0.2 1 368 97 97 ARG CA C 56.28 0.2 1 369 97 97 ARG CB C 26.62 0.2 1 370 97 97 ARG N N 120.3 0.2 1 371 98 98 SER H H 7.422 0.02 1 372 98 98 SER C C 173.2 0.2 1 373 98 98 SER CA C 56.00 0.2 1 374 98 98 SER CB C 61.07 0.2 1 375 98 98 SER N N 110.5 0.2 1 376 99 99 ARG H H 7.388 0.02 1 377 99 99 ARG C C 175.2 0.2 1 378 99 99 ARG CA C 53.02 0.2 1 379 99 99 ARG N N 118.9 0.2 1 380 100 100 ILE H H 7.560 0.02 1 381 100 100 ILE C C 174.2 0.2 1 382 100 100 ILE CA C 59.42 0.2 1 383 100 100 ILE CB C 36.69 0.2 1 384 100 100 ILE N N 119.0 0.2 1 385 101 101 THR H H 8.532 0.02 1 386 101 101 THR C C 172.4 0.2 1 387 101 101 THR CA C 57.61 0.2 1 388 101 101 THR CB C 68.44 0.2 1 389 101 101 THR N N 119.2 0.2 1 390 102 102 ALA H H 8.745 0.02 1 391 102 102 ALA C C 176.5 0.2 1 392 102 102 ALA CA C 49.08 0.2 1 393 102 102 ALA CB C 17.47 0.2 1 394 102 102 ALA N N 129.4 0.2 1 395 103 103 SER H H 8.871 0.02 1 396 103 103 SER CA C 55.26 0.2 1 397 103 103 SER CB C 59.23 0.2 1 398 103 103 SER N N 122.5 0.2 1 399 104 104 PRO C C 178.0 0.2 1 400 104 104 PRO CA C 63.36 0.2 1 401 105 105 ALA H H 9.553 0.02 1 402 105 105 ALA C C 179.8 0.2 1 403 105 105 ALA CA C 51.88 0.2 1 404 105 105 ALA N N 118.9 0.2 1 405 106 106 VAL H H 7.566 0.02 1 406 106 106 VAL C C 176.2 0.2 1 407 106 106 VAL CA C 63.95 0.2 1 408 106 106 VAL CB C 29.08 0.2 1 409 106 106 VAL N N 120.2 0.2 1 410 107 107 ILE H H 8.426 0.02 1 411 107 107 ILE C C 177.4 0.2 1 412 107 107 ILE CA C 62.42 0.2 1 413 107 107 ILE CB C 34.79 0.2 1 414 107 107 ILE N N 121.7 0.2 1 415 108 108 ASP H H 7.244 0.02 1 416 108 108 ASP C C 176.8 0.2 1 417 108 108 ASP CA C 54.64 0.2 1 418 108 108 ASP CB C 37.74 0.2 1 419 108 108 ASP N N 117.9 0.2 1 420 109 109 TYR H H 7.896 0.02 1 421 109 109 TYR CA C 54.06 0.2 1 422 109 109 TYR N N 132.4 0.2 1 423 109 109 TYR CB C 35.75 0.2 1 424 110 110 VAL H H 9.174 0.02 1 425 110 110 VAL C C 176.6 0.2 1 426 110 110 VAL CA C 64.05 0.2 1 427 110 110 VAL CB C 27.81 0.2 1 428 110 110 VAL N N 118.5 0.2 1 429 111 111 ASN H H 8.406 0.02 1 430 111 111 ASN CA C 53.67 0.2 1 431 111 111 ASN CB C 34.94 0.2 1 432 111 111 ASN N N 117.0 0.2 1 433 112 112 ARG H H 7.570 0.02 1 434 113 113 LEU C C 178.1 0.2 1 435 113 113 LEU CA C 54.68 0.2 1 436 114 114 GLU H H 8.804 0.02 1 437 114 114 GLU C C 177.0 0.2 1 438 114 114 GLU CA C 56.78 0.2 1 439 114 114 GLU N N 119.7 0.2 1 440 115 115 GLU H H 7.760 0.02 1 441 115 115 GLU C C 178.2 0.2 1 442 115 115 GLU CA C 56.77 0.2 1 443 115 115 GLU CB C 27.15 0.2 1 444 115 115 GLU N N 121.2 0.2 1 445 116 116 ILE H H 8.225 0.02 1 446 116 116 ILE C C 176.9 0.2 1 447 116 116 ILE CA C 62.80 0.2 1 448 116 116 ILE N N 120.8 0.2 1 449 117 117 ARG H H 8.144 0.02 1 450 117 117 ARG C C 177.3 0.2 1 451 117 117 ARG CA C 56.77 0.2 1 452 117 117 ARG CB C 27.26 0.2 1 453 117 117 ARG N N 119.6 0.2 1 454 118 118 ASP H H 8.683 0.02 1 455 118 118 ASP C C 176.6 0.2 1 456 118 118 ASP CA C 54.38 0.2 1 457 118 118 ASP CB C 36.79 0.2 1 458 118 118 ASP N N 119.8 0.2 1 459 119 119 ASN H H 8.397 0.02 1 460 119 119 ASN C C 172.8 0.2 1 461 119 119 ASN CA C 50.22 0.2 1 462 119 119 ASN CB C 35.89 0.2 1 463 119 119 ASN N N 115.8 0.2 1 464 120 120 VAL H H 7.908 0.02 1 465 120 120 VAL C C 173.2 0.2 1 466 120 120 VAL CA C 60.21 0.2 1 467 120 120 VAL CB C 26.29 0.2 1 468 120 120 VAL N N 123.4 0.2 1 469 121 121 ASP H H 7.670 0.02 1 470 121 121 ASP C C 174.2 0.2 1 471 121 121 ASP CA C 49.51 0.2 1 472 121 121 ASP CB C 37.69 0.2 1 473 121 121 ASP N N 118.4 0.2 1 474 122 122 GLY H H 7.959 0.02 1 475 122 122 GLY CA C 46.67 0.2 1 476 122 122 GLY N N 111.3 0.2 1 477 123 123 PRO C C 176.2 0.2 1 478 123 123 PRO CA C 63.26 0.2 1 479 123 123 PRO CB C 29.64 0.2 1 480 124 124 ALA H H 7.196 0.02 1 481 124 124 ALA C C 178.1 0.2 1 482 124 124 ALA CA C 51.97 0.2 1 483 124 124 ALA CB C 16.35 0.2 1 484 124 124 ALA N N 114.6 0.2 1 485 125 125 LEU H H 8.480 0.02 1 486 125 125 LEU C C 178.8 0.2 1 487 125 125 LEU CA C 54.08 0.2 1 488 125 125 LEU N N 118.8 0.2 1 489 126 126 VAL H H 8.585 0.02 1 490 126 126 VAL C C 175.4 0.2 1 491 126 126 VAL CA C 64.57 0.2 1 492 126 126 VAL N N 119.5 0.2 1 493 127 127 ALA H H 7.384 0.02 1 494 127 127 ALA C C 177.5 0.2 1 495 127 127 ALA CA C 52.98 0.2 1 496 127 127 ALA CB C 16.35 0.2 1 497 127 127 ALA N N 119.6 0.2 1 498 128 128 HIS H H 7.552 0.02 1 499 128 128 HIS C C 176.6 0.2 1 500 128 128 HIS CA C 58.49 0.2 1 501 128 128 HIS CB C 29.39 0.2 1 502 128 128 HIS N N 114.6 0.2 1 503 129 129 HIS H H 9.152 0.02 1 504 129 129 HIS C C 174.9 0.2 1 505 129 129 HIS CA C 59.03 0.2 1 506 129 129 HIS CB C 30.37 0.2 1 507 129 129 HIS N N 123.3 0.2 1 508 130 130 TYR H H 8.769 0.02 1 509 130 130 TYR C C 176.9 0.2 1 510 130 130 TYR CA C 58.64 0.2 1 511 130 130 TYR CB C 35.66 0.2 1 512 130 130 TYR N N 119.2 0.2 1 513 131 131 VAL H H 7.835 0.02 1 514 131 131 VAL C C 177.1 0.2 1 515 131 131 VAL CA C 63.75 0.2 1 516 131 131 VAL CB C 28.80 0.2 1 517 131 131 VAL N N 117.8 0.2 1 518 132 132 ARG H H 7.581 0.02 1 519 132 132 ARG C C 175.9 0.2 1 520 132 132 ARG CA C 55.60 0.2 1 521 132 132 ARG CB C 27.83 0.2 1 522 132 132 ARG N N 114.4 0.2 1 523 133 133 TYR H H 8.464 0.02 1 524 133 133 TYR CA C 59.16 0.2 1 525 133 133 TYR CB C 34.67 0.2 1 526 133 133 TYR N N 124.3 0.2 1 527 134 134 LEU H H 7.490 0.02 1 528 134 134 LEU C C 179.5 0.2 1 529 134 134 LEU CA C 55.17 0.2 1 530 134 134 LEU CB C 36.39 0.2 1 531 134 134 LEU N N 117.3 0.2 1 532 135 135 GLY H H 6.992 0.02 1 533 135 135 GLY C C 175.9 0.2 1 534 135 135 GLY CA C 44.47 0.2 1 535 135 135 GLY N N 106.6 0.2 1 536 136 136 ASP H H 8.242 0.02 1 537 136 136 ASP C C 178.0 0.2 1 538 136 136 ASP CA C 54.87 0.2 1 539 136 136 ASP CB C 37.81 0.2 1 540 136 136 ASP N N 125.6 0.2 1 541 137 137 LEU H H 8.391 0.02 1 542 137 137 LEU C C 177.1 0.2 1 543 137 137 LEU CA C 54.29 0.2 1 544 137 137 LEU CB C 40.06 0.2 1 545 137 137 LEU N N 119.0 0.2 1 546 138 138 SER H H 7.915 0.02 1 547 138 138 SER CA C 57.46 0.2 1 548 138 138 SER CB C 60.81 0.2 1 549 138 138 SER N N 112.7 0.2 1 550 139 139 GLY C C 175.2 0.2 1 551 139 139 GLY CA C 43.16 0.2 1 552 140 140 GLY H H 8.588 0.02 1 553 140 140 GLY C C 173.9 0.2 1 554 140 140 GLY CA C 45.90 0.2 1 555 140 140 GLY N N 109.9 0.2 1 556 141 141 GLN H H 8.341 0.02 1 557 141 141 GLN C C 177.7 0.2 1 558 141 141 GLN CA C 55.89 0.2 1 559 141 141 GLN CB C 25.68 0.2 1 560 141 141 GLN N N 117.6 0.2 1 561 142 142 VAL H H 7.547 0.02 1 562 142 142 VAL C C 176.4 0.2 1 563 142 142 VAL CA C 62.88 0.2 1 564 142 142 VAL CB C 29.14 0.2 1 565 142 142 VAL N N 118.6 0.2 1 566 143 143 ILE H H 7.362 0.02 1 567 143 143 ILE C C 177.0 0.2 1 568 143 143 ILE CA C 62.95 0.2 1 569 143 143 ILE CB C 35.49 0.2 1 570 143 143 ILE N N 119.8 0.2 1 571 144 144 ALA H H 7.671 0.02 1 572 144 144 ALA C C 178.8 0.2 1 573 144 144 ALA CA C 52.81 0.2 1 574 144 144 ALA CB C 15.38 0.2 1 575 144 144 ALA N N 119.4 0.2 1 576 145 145 ARG H H 7.626 0.02 1 577 145 145 ARG CA C 56.75 0.2 1 578 145 145 ARG CB C 27.31 0.2 1 579 145 145 ARG N N 116.0 0.2 1 580 147 147 MET H H 8.584 0.02 1 581 147 147 MET C C 179.1 0.2 1 582 147 147 MET CA C 53.62 0.2 1 583 148 148 GLN H H 7.490 0.02 1 584 148 148 GLN C C 176.8 0.2 1 585 148 148 GLN CA C 56.56 0.2 1 586 148 148 GLN CB C 26.96 0.2 1 587 148 148 GLN N N 118.2 0.2 1 588 149 149 ARG H H 8.024 0.02 1 589 149 149 ARG CA C 56.19 0.2 1 590 149 149 ARG CB C 27.85 0.2 1 591 149 149 ARG N N 118.5 0.2 1 592 150 150 HIS H H 8.363 0.02 1 593 150 150 HIS CA C 55.33 0.2 1 594 150 150 HIS CB C 27.32 0.2 1 595 150 150 HIS N N 113.0 0.2 1 596 151 151 TYR H H 6.700 0.02 1 597 151 151 TYR C C 175.3 0.2 1 598 151 151 TYR CA C 52.44 0.2 1 599 151 151 TYR CB C 36.86 0.2 1 600 151 151 TYR N N 112.1 0.2 1 601 152 152 GLY H H 7.585 0.02 1 602 152 152 GLY C C 173.2 0.2 1 603 152 152 GLY CA C 44.06 0.2 1 604 152 152 GLY N N 108.7 0.2 1 605 153 153 VAL H H 6.994 0.02 1 606 153 153 VAL C C 173.6 0.2 1 607 153 153 VAL CA C 60.64 0.2 1 608 153 153 VAL CB C 29.25 0.2 1 609 153 153 VAL N N 119.2 0.2 1 610 154 154 ASP H H 8.485 0.02 1 611 154 154 ASP CA C 49.89 0.2 1 612 154 154 ASP CB C 39.89 0.2 1 613 154 154 ASP N N 128.3 0.2 1 614 155 155 PRO C C 178.0 0.2 1 615 155 155 PRO CA C 62.13 0.2 1 616 155 155 PRO CB C 28.89 0.2 1 617 156 156 GLU H H 9.148 0.02 1 618 156 156 GLU C C 174.7 0.2 1 619 156 156 GLU CA C 55.22 0.2 1 620 156 156 GLU CB C 26.27 0.2 1 621 156 156 GLU N N 117.4 0.2 1 622 157 157 ALA H H 8.260 0.02 1 623 157 157 ALA C C 173.2 0.2 1 624 157 157 ALA CA C 48.44 0.2 1 625 157 157 ALA CB C 16.42 0.2 1 626 157 157 ALA N N 121.6 0.2 1 627 158 158 LEU H H 6.939 0.02 1 628 158 158 LEU C C 178.0 0.2 1 629 158 158 LEU CA C 50.60 0.2 1 630 158 158 LEU CB C 39.50 0.2 1 631 158 158 LEU N N 117.0 0.2 1 632 159 159 GLY H H 10.15 0.02 1 633 159 159 GLY C C 176.1 0.2 1 634 159 159 GLY CA C 44.88 0.2 1 635 159 159 GLY N N 118.6 0.2 1 636 160 160 PHE H H 11.22 0.02 1 637 160 160 PHE C C 174.0 0.2 1 638 160 160 PHE CA C 58.12 0.2 1 639 160 160 PHE CB C 37.57 0.2 1 640 160 160 PHE N N 124.6 0.2 1 641 161 161 TYR H H 7.226 0.02 1 642 161 161 TYR C C 172.8 0.2 1 643 161 161 TYR CA C 56.01 0.2 1 644 161 161 TYR CB C 36.24 0.2 1 645 161 161 TYR N N 113.0 0.2 1 646 162 162 HIS H H 7.936 0.02 1 647 162 162 HIS C C 172.2 0.2 1 648 162 162 HIS CA C 51.95 0.2 1 649 162 162 HIS CB C 29.65 0.2 1 650 162 162 HIS N N 120.7 0.2 1 651 163 163 PHE H H 8.775 0.02 1 652 163 163 PHE C C 174.3 0.2 1 653 163 163 PHE CA C 53.51 0.2 1 654 163 163 PHE CB C 36.21 0.2 1 655 163 163 PHE N N 126.5 0.2 1 656 164 164 GLU C C 176.6 0.2 1 657 164 164 GLU H H 8.840 0.02 1 658 164 164 GLU CA C 55.75 0.2 1 659 164 164 GLU CB C 26.76 0.2 1 660 164 164 GLU N N 125.4 0.2 1 661 165 165 GLY H H 8.847 0.02 1 662 165 165 GLY C C 172.5 0.2 1 663 165 165 GLY CA C 42.09 0.2 1 664 165 165 GLY N N 107.1 0.2 1 665 166 166 ILE H H 7.178 0.02 1 666 166 166 ILE C C 173.3 0.2 1 667 166 166 ILE CA C 57.58 0.2 1 668 166 166 ILE CB C 35.57 0.2 1 669 166 166 ILE N N 120.0 0.2 1 670 167 167 ALA H H 8.456 0.02 1 671 167 167 ALA C C 177.4 0.2 1 672 167 167 ALA CA C 50.99 0.2 1 673 167 167 ALA CB C 16.29 0.2 1 674 167 167 ALA N N 128.6 0.2 1 675 168 168 LYS H H 8.078 0.02 1 676 168 168 LYS CA C 51.94 0.2 1 677 168 168 LYS CB C 30.39 0.2 1 678 168 168 LYS N N 116.8 0.2 1 679 169 169 LEU C C 177.3 0.2 1 680 169 169 LEU CA C 54.87 0.2 1 681 170 170 LYS H H 8.658 0.02 1 682 170 170 LYS C C 177.6 0.2 1 683 170 170 LYS CA C 57.48 0.2 1 684 170 170 LYS N N 117.7 0.2 1 685 171 171 VAL H H 6.755 0.02 1 686 171 171 VAL C C 176.5 0.2 1 687 171 171 VAL CA C 62.06 0.2 1 688 171 171 VAL CB C 29.25 0.2 1 689 171 171 VAL N N 117.2 0.2 1 690 172 172 TYR H H 8.140 0.02 1 691 172 172 TYR C C 177.2 0.2 1 692 172 172 TYR CA C 59.34 0.2 1 693 172 172 TYR CB C 36.52 0.2 1 694 172 172 TYR N N 121.0 0.2 1 695 173 173 LYS H H 7.831 0.02 1 696 173 173 LYS N N 120.2 0.2 1 697 174 174 ASP H H 7.846 0.02 1 698 174 174 ASP C C 178.2 0.2 1 699 175 175 GLU H H 8.487 0.02 1 700 175 175 GLU C C 177.6 0.2 1 701 175 175 GLU CA C 56.54 0.2 1 702 175 175 GLU CB C 26.38 0.2 1 703 175 175 GLU N N 121.8 0.2 1 704 176 176 TYR H H 8.762 0.02 1 705 176 176 TYR C C 176.4 0.2 1 706 176 176 TYR CA C 59.07 0.2 1 707 176 176 TYR CB C 36.18 0.2 1 708 176 176 TYR N N 123.7 0.2 1 709 177 177 ARG H H 7.993 0.02 1 710 177 177 ARG C C 176.6 0.2 1 711 177 177 ARG CA C 57.67 0.2 1 712 177 177 ARG CB C 27.19 0.2 1 713 177 177 ARG N N 116.9 0.2 1 714 178 178 GLU H H 7.743 0.02 1 715 178 178 GLU C C 177.8 0.2 1 716 178 178 GLU CA C 56.39 0.2 1 717 178 178 GLU CB C 26.22 0.2 1 718 178 178 GLU N N 118.1 0.2 1 719 179 179 LYS H H 7.962 0.02 1 720 179 179 LYS C C 179.8 0.2 1 721 179 179 LYS CA C 56.62 0.2 1 722 179 179 LYS N N 119.0 0.2 1 723 180 180 LEU H H 8.091 0.02 1 724 180 180 LEU C C 177.4 0.2 1 725 180 180 LEU CA C 54.75 0.2 1 726 180 180 LEU CB C 39.09 0.2 1 727 180 180 LEU N N 119.9 0.2 1 728 181 181 ASN H H 7.951 0.02 1 729 181 181 ASN N N 116.2 0.2 1 730 181 181 ASN C C 175.4 0.2 1 731 181 181 ASN CA C 51.89 0.2 1 732 181 181 ASN CB C 35.15 0.2 1 733 182 182 ASN H H 7.621 0.02 1 734 182 182 ASN C C 173.9 0.2 1 735 182 182 ASN CA C 50.26 0.2 1 736 182 182 ASN CB C 37.23 0.2 1 737 182 182 ASN N N 115.9 0.2 1 738 183 183 LEU H H 7.194 0.02 1 739 183 183 LEU C C 175.3 0.2 1 740 183 183 LEU CA C 52.87 0.2 1 741 183 183 LEU CB C 39.15 0.2 1 742 183 183 LEU N N 122.4 0.2 1 743 184 184 GLU H H 8.748 0.02 1 744 184 184 GLU C C 173.9 0.2 1 745 184 184 GLU CA C 53.82 0.2 1 746 184 184 GLU CB C 26.34 0.2 1 747 184 184 GLU N N 127.5 0.2 1 748 185 185 LEU H H 8.181 0.02 1 749 185 185 LEU C C 176.3 0.2 1 750 185 185 LEU CA C 49.71 0.2 1 751 185 185 LEU CB C 42.86 0.2 1 752 185 185 LEU N N 125.3 0.2 1 753 186 186 SER H H 9.332 0.02 1 754 186 186 SER C C 173.7 0.2 1 755 186 186 SER CA C 54.26 0.2 1 756 186 186 SER CB C 62.49 0.2 1 757 186 186 SER N N 119.7 0.2 1 758 187 187 ASP H H 9.124 0.02 1 759 187 187 ASP C C 177.6 0.2 1 760 187 187 ASP CA C 55.53 0.2 1 761 187 187 ASP CB C 37.04 0.2 1 762 187 187 ASP N N 121.8 0.2 1 763 188 188 GLU H H 8.770 0.02 1 764 188 188 GLU CA C 56.88 0.2 1 765 188 188 GLU CB C 26.67 0.2 1 766 188 188 GLU N N 119.3 0.2 1 767 189 189 GLN H H 7.881 0.02 1 768 189 189 GLN C C 177.2 0.2 1 769 189 189 GLN CA C 55.75 0.2 1 770 189 189 GLN CB C 27.65 0.2 1 771 189 189 GLN N N 119.5 0.2 1 772 190 190 ARG H H 8.807 0.02 1 773 190 190 ARG C C 176.3 0.2 1 774 190 190 ARG CA C 57.15 0.2 1 775 190 190 ARG CB C 27.45 0.2 1 776 190 190 ARG N N 120.3 0.2 1 777 191 191 GLU H H 8.119 0.02 1 778 191 191 GLU CA C 56.96 0.2 1 779 191 191 GLU CB C 26.48 0.2 1 780 191 191 GLU N N 117.6 0.2 1 781 193 193 LEU C C 177.6 0.2 1 782 193 193 LEU CA C 54.16 0.2 1 783 194 194 LEU H H 8.563 0.02 1 784 194 194 LEU C C 179.1 0.2 1 785 194 194 LEU CA C 55.52 0.2 1 786 194 194 LEU CB C 38.86 0.2 1 787 194 194 LEU N N 121.3 0.2 1 788 195 195 LYS H H 8.120 0.02 1 789 195 195 LYS C C 177.8 0.2 1 790 195 195 LYS CB C 29.27 0.2 1 791 195 195 LYS N N 121.1 0.2 1 792 196 196 GLU H H 8.305 0.02 1 793 196 196 GLU C C 176.8 0.2 1 794 196 196 GLU CB C 24.79 0.2 1 795 196 196 GLU N N 120.7 0.2 1 796 197 197 ALA H H 8.404 0.02 1 797 197 197 ALA C C 177.7 0.2 1 798 197 197 ALA CA C 52.55 0.2 1 799 197 197 ALA CB C 15.20 0.2 1 800 197 197 ALA N N 120.0 0.2 1 801 198 198 THR H H 7.336 0.02 1 802 198 198 THR C C 174.6 0.2 1 803 198 198 THR CA C 64.83 0.2 1 804 198 198 THR N N 114.2 0.2 1 805 199 199 ASP H H 7.632 0.02 1 806 199 199 ASP C C 177.1 0.2 1 807 199 199 ASP CA C 54.90 0.2 1 808 199 199 ASP N N 121.7 0.2 1 809 200 200 ALA H H 9.094 0.02 1 810 200 200 ALA C C 178.5 0.2 1 811 200 200 ALA CA C 52.75 0.2 1 812 200 200 ALA CB C 14.92 0.2 1 813 200 200 ALA N N 122.6 0.2 1 814 201 201 PHE H H 8.105 0.02 1 815 201 201 PHE C C 177.8 0.2 1 816 201 201 PHE CA C 60.09 0.2 1 817 201 201 PHE CB C 36.79 0.2 1 818 201 201 PHE N N 118.8 0.2 1 819 202 202 VAL H H 8.220 0.02 1 820 202 202 VAL C C 177.5 0.2 1 821 202 202 VAL CA C 64.41 0.2 1 822 202 202 VAL N N 122.1 0.2 1 823 203 203 PHE H H 8.522 0.02 1 824 203 203 PHE CA C 57.50 0.2 1 825 203 203 PHE N N 118.8 0.2 1 826 204 204 ASN H H 7.494 0.02 1 827 204 204 ASN C C 174.7 0.2 1 828 204 204 ASN CA C 54.66 0.2 1 829 204 204 ASN CB C 36.83 0.2 1 830 204 204 ASN N N 115.1 0.2 1 831 205 205 HIS H H 8.095 0.02 1 832 205 205 HIS N N 117.1 0.2 1 833 206 206 GLN C C 176.6 0.2 1 834 207 207 VAL H H 7.952 0.02 1 835 207 207 VAL C C 177.3 0.2 1 836 207 207 VAL CA C 64.22 0.2 1 837 207 207 VAL N N 120.5 0.2 1 838 208 208 PHE H H 7.240 0.02 1 839 208 208 PHE C C 177.4 0.2 1 840 208 208 PHE CA C 56.45 0.2 1 841 208 208 PHE N N 116.6 0.2 1 842 209 209 ALA H H 8.256 0.02 1 843 209 209 ALA C C 179.5 0.2 1 844 209 209 ALA CA C 51.97 0.2 1 845 209 209 ALA N N 123.6 0.2 1 846 210 210 ASP H H 8.208 0.02 1 847 210 210 ASP C C 178.6 0.2 1 848 210 210 ASP CA C 54.63 0.2 1 849 210 210 ASP CB C 37.73 0.2 1 850 210 210 ASP N N 120.1 0.2 1 851 211 211 LEU H H 7.882 0.02 1 852 211 211 LEU C C 178.9 0.2 1 853 211 211 LEU CA C 55.05 0.2 1 854 211 211 LEU N N 120.8 0.2 1 855 212 212 GLY H H 8.180 0.02 1 856 212 212 GLY C C 173.7 0.2 1 857 212 212 GLY CA C 43.37 0.2 1 858 212 212 GLY N N 105.2 0.2 1 859 213 213 LYS H H 7.580 0.02 1 860 213 213 LYS C C 176.0 0.2 1 861 213 213 LYS CA C 54.63 0.2 1 862 213 213 LYS N N 119.9 0.2 1 863 214 214 GLY H H 8.063 0.02 1 864 214 214 GLY C C 172.6 0.2 1 865 214 214 GLY CA C 42.88 0.2 1 866 214 214 GLY N N 108.4 0.2 1 867 215 215 LEU H H 7.712 0.02 1 868 215 215 LEU CA C 53.72 0.2 1 869 215 215 LEU CB C 39.88 0.2 1 870 215 215 LEU N N 126.3 0.2 1 stop_ save_