data_6987 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N, and 13CB Chemical Shift Assignments for Cyanide-Inhibited P. aeruginosa Heme Oxygenase ; _BMRB_accession_number 6987 _BMRB_flat_file_name bmr6987.str _Entry_type original _Submission_date 2006-02-14 _Accession_date 2006-02-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Ferric paramagnetic protein' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rodriguez 'Juan Carlos' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 181 "13C chemical shifts" 521 "15N chemical shifts" 181 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-04-27 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6983 'heme-heme oxygenase-azide complex' stop_ _Original_release_date 2006-04-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone NMR Assignments and H/D Exchange Studies on the Ferric Azide- and Cyanide-Inhibited Forms of Pseudomonas aeruginosa Heme Oxygenase ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16584193 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rodriguez 'Juan Carlos' . . 2 Wilks Angela . . 3 Rivera Mario . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 45 _Journal_issue 14 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4578 _Page_last 4592 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Heme-heme oxygenase-cyanide complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Heme oxygenase polypeptide' $Cyanide-inhibited_heme-heme_oxygenase_complex 'PROTOPORPHYRIN IX CONTAINING FE 1' $HEM azide $CYN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state 'protein-ligand system' _System_paramagnetic yes _System_thiol_state 'not present' loop_ _Biological_function 'Heme metabolism in P. aeruginosa' stop_ _Database_query_date . _Details 'Heme-heme oxygenase-cyanide complex' save_ ######################## # Monomeric polymers # ######################## save_Cyanide-inhibited_heme-heme_oxygenase_complex _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Cyanide-inhibited pa-HO' _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'Heme cleavage' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 198 _Mol_residue_sequence ; MDTLAPESTRQNLRSQRLNL LTNEPHQRLESLVKSKEPFA SRDNFARFVAAQYLFQHDLE PLYRNEALARLFPGLASRAR DDAARADLADLGHPVPEGDQ SVREADLSLAEALGWLFVSE GSKLGAAFLFKKAAALELDE NFGARHLAEPEGGRAQGWKS FVAILDGIELNEEEERLAAK GASDAFNRFGDLLERTFA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 THR 4 LEU 5 ALA 6 PRO 7 GLU 8 SER 9 THR 10 ARG 11 GLN 12 ASN 13 LEU 14 ARG 15 SER 16 GLN 17 ARG 18 LEU 19 ASN 20 LEU 21 LEU 22 THR 23 ASN 24 GLU 25 PRO 26 HIS 27 GLN 28 ARG 29 LEU 30 GLU 31 SER 32 LEU 33 VAL 34 LYS 35 SER 36 LYS 37 GLU 38 PRO 39 PHE 40 ALA 41 SER 42 ARG 43 ASP 44 ASN 45 PHE 46 ALA 47 ARG 48 PHE 49 VAL 50 ALA 51 ALA 52 GLN 53 TYR 54 LEU 55 PHE 56 GLN 57 HIS 58 ASP 59 LEU 60 GLU 61 PRO 62 LEU 63 TYR 64 ARG 65 ASN 66 GLU 67 ALA 68 LEU 69 ALA 70 ARG 71 LEU 72 PHE 73 PRO 74 GLY 75 LEU 76 ALA 77 SER 78 ARG 79 ALA 80 ARG 81 ASP 82 ASP 83 ALA 84 ALA 85 ARG 86 ALA 87 ASP 88 LEU 89 ALA 90 ASP 91 LEU 92 GLY 93 HIS 94 PRO 95 VAL 96 PRO 97 GLU 98 GLY 99 ASP 100 GLN 101 SER 102 VAL 103 ARG 104 GLU 105 ALA 106 ASP 107 LEU 108 SER 109 LEU 110 ALA 111 GLU 112 ALA 113 LEU 114 GLY 115 TRP 116 LEU 117 PHE 118 VAL 119 SER 120 GLU 121 GLY 122 SER 123 LYS 124 LEU 125 GLY 126 ALA 127 ALA 128 PHE 129 LEU 130 PHE 131 LYS 132 LYS 133 ALA 134 ALA 135 ALA 136 LEU 137 GLU 138 LEU 139 ASP 140 GLU 141 ASN 142 PHE 143 GLY 144 ALA 145 ARG 146 HIS 147 LEU 148 ALA 149 GLU 150 PRO 151 GLU 152 GLY 153 GLY 154 ARG 155 ALA 156 GLN 157 GLY 158 TRP 159 LYS 160 SER 161 PHE 162 VAL 163 ALA 164 ILE 165 LEU 166 ASP 167 GLY 168 ILE 169 GLU 170 LEU 171 ASN 172 GLU 173 GLU 174 GLU 175 GLU 176 ARG 177 LEU 178 ALA 179 ALA 180 LYS 181 GLY 182 ALA 183 SER 184 ASP 185 ALA 186 PHE 187 ASN 188 ARG 189 PHE 190 GLY 191 ASP 192 LEU 193 LEU 194 GLU 195 ARG 196 THR 197 PHE 198 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 Sep 28 17:43:14 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_ save_CYN _Saveframe_category ligand _Mol_type non-polymer _Name_common "CYN (CYANIDE ION)" _BMRB_code . _PDB_code CYN _Molecular_mass 26.017 _Mol_charge -1 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Sep 28 17:41:52 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . -1 . ? N N N . 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 TRIP C N ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _Organism_acronym _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Cyanide-inhibited_heme-heme_oxygenase_complex 'Pseudomonas aeruginosa' 'Pseudomonas aeruginosa' 287 Bacteria Protista Pseudomonas aeruginosa 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 $Cyanide-inhibited_heme-heme_oxygenase_complex 'recombinant technology' 'E. coli' . . . . 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 $Cyanide-inhibited_heme-heme_oxygenase_complex 2.4 mM '[U-13C; U-15N]' Cyanide 24 mM . 'Phosphates buffer' 50 mM . H2O 95 % . D2O 5 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Inova' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_Fast-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_Fast-HSQC _Sample_label $sample_1 save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_(HCA)CO(CA)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name (HCA)CO(CA)NH _Sample_label $sample_1 save_ save_15N-NOESY_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY_HSQC _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 pH temperature 305 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 1H15N_Fast-HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'Heme oxygenase polypeptide' _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 5 5 ALA H H 8.1 0.02 1 2 5 5 ALA N N 125.65 . 1 3 9 9 THR H H 7.87 0.02 1 4 9 9 THR CA C 62.6 0.2 1 5 9 9 THR CB C 69.94 0.2 1 6 9 9 THR N N 120.68 0.2 1 7 10 10 ARG H H 8.13 0.02 1 8 10 10 ARG CA C 57.18 0.2 1 9 10 10 ARG CB C 30.68 0.2 1 10 10 10 ARG N N 122.54 0.2 1 11 11 11 GLN H H 8.34 0.02 1 12 11 11 GLN C C 175.52 0.2 1 13 11 11 GLN CA C 56.13 0.2 1 14 11 11 GLN CB C 29.75 0.2 1 15 11 11 GLN N N 120.75 0.2 1 16 12 12 ASN H H 8.32 0.02 1 17 12 12 ASN C C 174.9 0.2 1 18 12 12 ASN CA C 53.36 0.2 1 19 12 12 ASN CB C 39.01 0.2 1 20 12 12 ASN N N 119.07 0.2 1 21 13 13 LEU H H 7.99 0.02 1 22 13 13 LEU C C 177.53 0.2 1 23 13 13 LEU CA C 54.63 0.2 1 24 13 13 LEU CB C 42.87 0.2 1 25 13 13 LEU N N 121.25 0.2 1 26 14 14 ARG H H 8.82 0.02 1 27 14 14 ARG C C 178.21 0.2 1 28 14 14 ARG CA C 61.3 0.2 1 29 14 14 ARG CB C 28.88 0.2 1 30 14 14 ARG N N 128.09 0.2 1 31 15 15 SER H H 11.52 0.2 1 32 15 15 SER C C 176.97 0.2 1 33 15 15 SER CA C 60.69 0.2 1 34 15 15 SER CB C 61.74 0.2 1 35 15 15 SER N N 117.61 0.2 1 36 16 16 GLN H H 6.7 0.02 1 37 16 16 GLN C C 178.67 0.2 1 38 16 16 GLN CA C 58.6 0.2 1 39 16 16 GLN CB C 28.6 0.2 1 40 16 16 GLN N N 121.85 0.2 1 41 17 17 ARG H H 8.19 0.2 1 42 17 17 ARG C C 179.86 0.2 1 43 17 17 ARG CA C 60.63 0.2 1 44 17 17 ARG CB C 30.44 0.2 1 45 17 17 ARG N N 121.65 0.2 1 46 18 18 LEU H H 8.89 0.02 1 47 18 18 LEU C C 179.73 0.2 1 48 18 18 LEU CA C 58.03 0.2 1 49 18 18 LEU CB C 40.22 0.2 1 50 18 18 LEU N N 118.84 0.2 1 51 19 19 ASN H H 8.02 0.02 1 52 19 19 ASN C C 177.45 0.2 1 53 19 19 ASN CA C 57.43 0.2 1 54 19 19 ASN CB C 39.32 0.2 1 55 19 19 ASN N N 120.71 0.2 1 56 20 20 LEU H H 8.04 0.02 1 57 20 20 LEU C C 180.86 0.2 1 58 20 20 LEU CA C 58.88 0.2 1 59 20 20 LEU CB C 42.26 0.2 1 60 20 20 LEU N N 119.81 0.2 1 61 21 21 LEU H H 8.39 0.02 1 62 21 21 LEU C C 179.08 0.2 1 63 21 21 LEU CA C 58.18 0.2 1 64 21 21 LEU CB C 43.12 0.2 1 65 21 21 LEU N N 119.39 0.2 1 66 22 22 THR H H 8.13 0.02 1 67 22 22 THR C C 175.67 0.2 1 68 22 22 THR CA C 62.88 0.2 1 69 22 22 THR CB C 70.5 0.2 1 70 22 22 THR N N 105.93 0.2 1 71 23 23 ASN H H 8.24 0.02 1 72 23 23 ASN C C 178.31 0.2 1 73 23 23 ASN CA C 59.91 0.2 1 74 23 23 ASN CB C 40.55 0.2 1 75 23 23 ASN N N 124.31 0.2 1 76 24 24 GLU H H 9.83 0.02 1 77 24 24 GLU C C 177.73 0.2 1 78 24 24 GLU N N 120.02 0.2 1 79 25 25 PRO C C 179.8 0.2 1 80 25 25 PRO CA C 67.05 0.2 1 81 25 25 PRO CB C 30.78 0.2 1 82 26 26 HIS H H 10.36 0.02 1 83 26 26 HIS C C 179.49 0.2 1 84 26 26 HIS CA C 82.52 0.2 1 85 26 26 HIS CB C 24.64 0.2 1 86 26 26 HIS N N 120.44 0.2 1 87 27 27 GLN H H 10.63 0.02 1 88 27 27 GLN C C 180.48 0.2 1 89 27 27 GLN CA C 61.35 0.2 1 90 27 27 GLN CB C 29.88 0.2 1 91 27 27 GLN N N 123.13 0.2 1 92 28 28 ARG H H 8.85 0.02 1 93 28 28 ARG C C 179.19 0.2 1 94 28 28 ARG CA C 56.95 0.2 1 95 28 28 ARG CB C 30.51 0.2 1 96 28 28 ARG N N 120.43 0.2 1 97 29 29 LEU H H 8.53 0.02 1 98 29 29 LEU C C 176.97 0.2 1 99 29 29 LEU CA C 55.51 0.2 1 100 29 29 LEU CB C 42.84 0.2 1 101 29 29 LEU N N 122.51 0.2 1 102 30 30 GLU H H 8.47 0.02 1 103 30 30 GLU C C 177.66 0.2 1 104 30 30 GLU CA C 59.01 0.2 1 105 30 30 GLU CB C 27.77 0.2 1 106 30 30 GLU N N 120.05 0.2 1 107 31 31 SER H H 7.15 0.02 1 108 31 31 SER C C 176.37 0.2 1 109 31 31 SER CA C 61.61 0.2 1 110 31 31 SER CB C 62.89 0.2 1 111 31 31 SER N N 112.88 0.2 1 112 32 32 LEU H H 7.44 0.02 1 113 32 32 LEU C C 179.62 0.2 1 114 32 32 LEU CA C 57.67 0.2 1 115 32 32 LEU CB C 41.64 0.2 1 116 32 32 LEU N N 124.55 0.2 1 117 33 33 VAL H H 7.7 0.02 1 118 33 33 VAL C C 177.04 0.2 1 119 33 33 VAL CA C 66.9 0.2 1 120 33 33 VAL CB C 30.22 0.2 1 121 33 33 VAL N N 118.81 0.2 1 122 34 34 LYS H H 7.07 0.02 1 123 34 34 LYS C C 180.31 0.2 1 124 34 34 LYS CA C 60.15 0.2 1 125 34 34 LYS CB C 31.75 0.2 1 126 34 34 LYS N N 116.32 0.2 1 127 35 35 SER H H 7.52 0.02 1 128 35 35 SER C C 174.64 0.2 1 129 35 35 SER CA C 61.22 0.2 1 130 35 35 SER CB C 63.08 0.2 1 131 35 35 SER N N 115.03 0.2 1 132 36 36 LYS H H 6.86 0.02 1 133 36 36 LYS C C 175.11 0.2 1 134 36 36 LYS CA C 54.26 0.2 1 135 36 36 LYS CB C 30.01 0.2 1 136 36 36 LYS N N 119.22 0.2 1 137 37 37 GLU H H 7.31 0.02 1 138 37 37 GLU C C 175.02 0.2 1 139 37 37 GLU N N 110.76 0.2 1 140 38 38 PRO C C 173.54 0.2 1 141 38 38 PRO CA C 65.08 0.2 1 142 38 38 PRO CB C 31.85 0.2 1 143 39 39 PHE H H 7.82 0.02 1 144 39 39 PHE C C 175.88 0.2 1 145 39 39 PHE CA C 57.59 0.2 1 146 39 39 PHE CB C 38.13 0.2 1 147 39 39 PHE N N 108.49 0.2 1 148 40 40 ALA H H 7.7 0.02 1 149 40 40 ALA C C 177.82 0.2 1 150 40 40 ALA CA C 54.7 0.2 1 151 40 40 ALA CB C 19.96 0.2 1 152 40 40 ALA N N 120.66 0.2 1 153 41 41 SER H H 7.42 0.02 1 154 41 41 SER C C 174.29 0.2 1 155 41 41 SER N N 104.67 0.2 1 156 42 42 ARG C C 177.33 0.2 1 157 42 42 ARG CA C 61.42 0.2 1 158 42 42 ARG CB C 30.62 0.2 1 159 43 43 ASP H H 8.18 0.02 1 160 43 43 ASP C C 178.1 0.2 1 161 43 43 ASP CA C 57.82 0.2 1 162 43 43 ASP CB C 41.11 0.2 1 163 43 43 ASP N N 117.96 0.2 1 164 44 44 ASN H H 7.94 0.02 1 165 44 44 ASN C C 177.39 0.2 1 166 44 44 ASN CA C 56.2 0.2 1 167 44 44 ASN CB C 37.24 0.2 1 168 44 44 ASN N N 120.72 0.2 1 169 45 45 PHE H H 8.53 0.02 1 170 45 45 PHE C C 178.42 0.2 1 171 45 45 PHE CA C 63.38 0.2 1 172 45 45 PHE CB C 39.33 0.2 1 173 45 45 PHE N N 123.84 0.2 1 174 46 46 ALA H H 8.82 0.02 1 175 46 46 ALA C C 178.83 0.2 1 176 46 46 ALA CA C 55.54 0.2 1 177 46 46 ALA CB C 17.94 0.2 1 178 46 46 ALA N N 120.68 0.2 1 179 47 47 ARG H H 6.98 0.02 1 180 47 47 ARG C C 178.62 0.2 1 181 47 47 ARG CA C 59.67 0.2 1 182 47 47 ARG CB C 27.73 0.2 1 183 47 47 ARG N N 116.51 0.2 1 184 48 48 PHE H H 7.48 0.02 1 185 48 48 PHE C C 176.66 0.2 1 186 48 48 PHE CA C 60.18 0.2 1 187 48 48 PHE CB C 38.99 0.2 1 188 48 48 PHE N N 123.6 0.2 1 189 49 49 VAL H H 8.81 0.02 1 190 49 49 VAL C C 177.68 0.2 1 191 49 49 VAL CA C 66.86 0.2 1 192 49 49 VAL CB C 30.74 0.2 1 193 49 49 VAL N N 121.14 0.2 1 194 50 50 ALA H H 8.44 0.02 1 195 50 50 ALA C C 178.36 0.2 1 196 50 50 ALA CA C 56.25 0.2 1 197 50 50 ALA CB C 17.37 0.2 1 198 50 50 ALA N N 121.86 0.2 1 199 51 51 ALA H H 7.04 0.02 1 200 51 51 ALA C C 178.35 0.2 1 201 51 51 ALA CA C 55.96 0.2 1 202 51 51 ALA CB C 16.72 0.2 1 203 51 51 ALA N N 121.05 0.2 1 204 52 52 GLN H H 7.82 0.02 1 205 52 52 GLN C C 179.6 0.2 1 206 52 52 GLN CA C 59.97 0.2 1 207 52 52 GLN CB C 29.11 0.2 1 208 52 52 GLN N N 116.45 0.2 1 209 53 53 TYR H H 9.46 0.02 1 210 53 53 TYR C C 176.2 0.2 1 211 53 53 TYR CA C 62.48 0.2 1 212 53 53 TYR CB C 37.96 0.2 1 213 53 53 TYR N N 119.14 0.2 1 214 54 54 LEU H H 8.34 0.02 1 215 54 54 LEU C C 179.03 0.2 1 216 54 54 LEU CA C 58.46 0.2 1 217 54 54 LEU CB C 42.62 0.2 1 218 54 54 LEU N N 120.11 0.2 1 219 55 55 PHE H H 8.51 0.02 1 220 55 55 PHE C C 177.31 0.2 1 221 55 55 PHE CA C 60.74 0.2 1 222 55 55 PHE CB C 40 0.2 1 223 55 55 PHE N N 122.35 0.2 1 224 56 56 GLN H H 8.49 0.02 1 225 56 56 GLN C C 178.93 0.2 1 226 56 56 GLN CA C 58.51 0.2 1 227 56 56 GLN CB C 27.66 0.2 1 228 56 56 GLN N N 115.11 0.2 1 229 57 57 HIS H H 9.09 0.2 1 230 57 57 HIS C C 177.92 0.2 1 231 57 57 HIS CA C 59.56 0.2 1 232 57 57 HIS CB C 28.37 0.2 1 233 57 57 HIS N N 121.85 0.2 1 234 58 58 ASP H H 7.94 0.02 1 235 58 58 ASP C C 175.74 0.2 1 236 58 58 ASP CA C 58.06 0.2 1 237 58 58 ASP CB C 40.69 0.2 1 238 58 58 ASP N N 122.29 0.2 1 239 59 59 LEU H H 6.79 0.02 1 240 59 59 LEU C C 178.02 0.2 1 241 59 59 LEU CA C 54.36 0.2 1 242 59 59 LEU CB C 42.92 0.2 1 243 59 59 LEU N N 113.19 0.2 1 244 60 60 GLU H H 7.5 0.02 1 245 60 60 GLU C C 174.26 0.2 1 246 60 60 GLU N N 124.55 0.2 1 247 61 61 PRO C C 178.57 0.2 1 248 61 61 PRO CA C 65.47 0.2 1 249 61 61 PRO CB C 31.2 0.2 1 250 62 62 LEU H H 7.62 0.02 1 251 62 62 LEU C C 178.17 0.2 1 252 62 62 LEU CA C 57.56 0.2 1 253 62 62 LEU CB C 41.54 0.2 1 254 62 62 LEU N N 116.3 0.2 1 255 63 63 TYR H H 7.78 0.02 1 256 63 63 TYR C C 176.8 0.2 1 257 63 63 TYR CA C 63.16 0.2 1 258 63 63 TYR CB C 39.05 0.2 1 259 63 63 TYR N N 115.1 0.2 1 260 64 64 ARG H H 7.37 0.02 1 261 64 64 ARG C C 175.83 0.2 1 262 64 64 ARG CA C 55.82 0.2 1 263 64 64 ARG CB C 30.09 0.2 1 264 64 64 ARG N N 111.85 0.2 1 265 65 65 ASN H H 7.25 0.02 1 266 65 65 ASN C C 176.3 0.2 1 267 65 65 ASN CA C 55.38 0.2 1 268 65 65 ASN CB C 40.81 0.2 1 269 65 65 ASN N N 122.79 0.2 1 270 66 66 GLU H H 9.11 0.02 1 271 66 66 GLU C C 177.87 0.2 1 272 66 66 GLU CA C 60.28 0.2 1 273 66 66 GLU CB C 30.06 0.2 1 274 66 66 GLU N N 128.34 0.2 1 275 67 67 ALA H H 7.92 0.02 1 276 67 67 ALA C C 181.71 0.2 1 277 67 67 ALA CA C 55.67 0.2 1 278 67 67 ALA CB C 18.15 0.2 1 279 67 67 ALA N N 122.34 0.2 1 280 68 68 LEU H H 8.4 0.02 1 281 68 68 LEU C C 179.15 0.2 1 282 68 68 LEU CA C 58.24 0.2 1 283 68 68 LEU CB C 42.1 0.2 1 284 68 68 LEU N N 119.12 0.2 1 285 69 69 ALA H H 8.38 0.02 1 286 69 69 ALA C C 179.14 0.2 1 287 69 69 ALA CA C 54.66 0.2 1 288 69 69 ALA CB C 18.37 0.2 1 289 69 69 ALA N N 122.28 0.2 1 290 70 70 ARG H H 7.28 0.02 1 291 70 70 ARG C C 177.5 0.2 1 292 70 70 ARG CA C 58.59 0.2 1 293 70 70 ARG CB C 30.6 0.2 1 294 70 70 ARG N N 114.72 0.2 1 295 71 71 LEU H H 7.09 0.02 1 296 71 71 LEU C C 175.3 0.2 1 297 71 71 LEU CA C 56.34 0.2 1 298 71 71 LEU CB C 44.13 0.2 1 299 71 71 LEU N N 118.44 0.2 1 300 72 72 PHE H H 7.97 0.02 1 301 72 72 PHE C C 172.09 0.2 1 302 72 72 PHE N N 115.67 0.2 1 303 73 73 PRO C C 178.23 0.2 1 304 73 73 PRO CA C 58.89 0.2 1 305 73 73 PRO CB C 29.36 0.2 1 306 74 74 GLY H H 8.98 0.02 1 307 74 74 GLY C C 176.42 0.2 1 308 74 74 GLY CA C 46.4 0.2 1 309 74 74 GLY N N 115.79 0.2 1 310 75 75 LEU H H 7.98 0.02 1 311 75 75 LEU C C 178.14 0.2 1 312 75 75 LEU CA C 59.44 0.2 1 313 75 75 LEU CB C 41.88 0.2 1 314 75 75 LEU N N 123.2 0.2 1 315 76 76 ALA H H 8.8 0.02 1 316 76 76 ALA C C 180.67 0.2 1 317 76 76 ALA CA C 56.05 0.2 1 318 76 76 ALA CB C 18.24 0.2 1 319 76 76 ALA N N 117.65 0.2 1 320 77 77 SER H H 7.92 0.02 1 321 77 77 SER C C 175.07 0.2 1 322 77 77 SER CA C 60.38 0.2 1 323 77 77 SER CB C 63.9 0.2 1 324 77 77 SER N N 111.62 0.2 1 325 78 78 ARG H H 8.18 0.02 1 326 78 78 ARG C C 176.39 0.2 1 327 78 78 ARG CA C 57.07 0.2 1 328 78 78 ARG CB C 30.67 0.2 1 329 78 78 ARG N N 119.95 0.2 1 330 79 79 ALA H H 6.79 0.02 1 331 79 79 ALA C C 178.16 0.2 1 332 79 79 ALA CA C 53.44 0.2 1 333 79 79 ALA CB C 20.14 0.2 1 334 79 79 ALA N N 123.05 0.2 1 335 80 80 ARG H H 7.82 0.02 1 336 80 80 ARG C C 175.86 0.2 1 337 80 80 ARG CA C 56.08 0.2 1 338 80 80 ARG CB C 33.01 0.2 1 339 80 80 ARG N N 117.45 0.2 1 340 81 81 ASP H H 8.98 0.02 1 341 81 81 ASP C C 177.12 0.2 1 342 81 81 ASP CA C 58.71 0.2 1 343 81 81 ASP CB C 39.09 0.2 1 344 81 81 ASP N N 120.61 0.2 1 345 82 82 ASP H H 8.3 0.02 1 346 82 82 ASP C C 175.69 0.2 1 347 82 82 ASP CA C 58.04 0.2 1 348 82 82 ASP CB C 40.44 0.2 1 349 82 82 ASP N N 119.81 0.2 1 350 83 83 ALA H H 8.16 0.02 1 351 83 83 ALA C C 178.08 0.2 1 352 83 83 ALA CA C 55.64 0.2 1 353 83 83 ALA CB C 18.22 0.2 1 354 83 83 ALA N N 123.71 0.2 1 355 84 84 ALA H H 8.18 0.02 1 356 84 84 ALA C C 178.46 0.2 1 357 84 84 ALA CA C 55.41 0.2 1 358 84 84 ALA CB C 17.53 0.2 1 359 84 84 ALA N N 117.27 0.2 1 360 85 85 ARG H H 8.43 0.02 1 361 85 85 ARG C C 178.85 0.2 1 362 85 85 ARG CA C 60.48 0.2 1 363 85 85 ARG CB C 30.22 0.2 1 364 85 85 ARG N N 118.27 0.2 1 365 86 86 ALA H H 7.98 0.02 1 366 86 86 ALA C C 179.98 0.2 1 367 86 86 ALA CA C 55.63 0.2 1 368 86 86 ALA CB C 17.51 0.2 1 369 86 86 ALA N N 123.2 0.2 1 370 87 87 ASP H H 8.38 0.02 1 371 87 87 ASP C C 178.96 0.2 1 372 87 87 ASP CA C 58.8 0.2 1 373 87 87 ASP CB C 41.53 0.2 1 374 87 87 ASP N N 122.22 0.2 1 375 88 88 LEU H H 7.89 0.02 1 376 88 88 LEU C C 178.77 0.2 1 377 88 88 LEU CA C 58.97 0.2 1 378 88 88 LEU CB C 40.59 0.2 1 379 88 88 LEU N N 119.04 0.2 1 380 89 89 ALA H H 7.51 0.02 1 381 89 89 ALA C C 182.37 0.2 1 382 89 89 ALA CA C 55.27 0.2 1 383 89 89 ALA CB C 17.75 0.2 1 384 89 89 ALA N N 120.7 0.2 1 385 90 90 ASP H H 8.28 0.02 1 386 90 90 ASP C C 177.54 0.2 1 387 90 90 ASP CA C 57.73 0.2 1 388 90 90 ASP CB C 40.39 0.2 1 389 90 90 ASP N N 121.49 0.2 1 390 91 91 LEU H H 7.58 0.02 1 391 91 91 LEU C C 176.91 0.2 1 392 91 91 LEU CA C 55.16 0.2 1 393 91 91 LEU CB C 42.7 0.2 1 394 91 91 LEU N N 115.96 0.2 1 395 92 92 GLY H H 8.03 0.02 1 396 92 92 GLY C C 176.12 0.2 1 397 92 92 GLY CA C 46.51 0.2 1 398 92 92 GLY N N 109.24 0.2 1 399 93 93 HIS H H 8.21 0.02 1 400 93 93 HIS C C 174.97 0.2 1 401 93 93 HIS N N 122.81 0.2 1 402 94 94 PRO C C 177 0.2 1 403 94 94 PRO CA C 62.58 0.2 1 404 94 94 PRO CB C 32.98 0.2 1 405 95 95 VAL H H 8.86 0.02 1 406 95 95 VAL C C 178.22 0.2 . 407 95 95 VAL N N 124.06 0.2 1 408 96 96 PRO C C 175.48 0.2 1 409 96 96 PRO CA C 62.49 0.2 1 410 96 96 PRO CB C 32.26 0.2 1 411 97 97 GLU H H 8.43 0.02 1 412 97 97 GLU C C 176.95 0.2 1 413 97 97 GLU CA C 56.9 0.2 1 414 97 97 GLU CB C 30.67 0.2 1 415 97 97 GLU N N 119.88 0.2 1 416 98 98 GLY H H 8.46 0.02 1 417 98 98 GLY C C 173.3 0.2 1 418 98 98 GLY CA C 45 0.2 1 419 98 98 GLY N N 111.11 0.2 1 420 99 99 ASP H H 8.67 0.02 1 421 99 99 ASP C C 177.17 0.2 1 422 99 99 ASP CA C 53.3 0.2 1 423 99 99 ASP CB C 43.45 0.2 1 424 99 99 ASP N N 120 0.2 1 425 100 100 GLN H H 8.75 0.02 1 426 100 100 GLN C C 176.67 0.2 1 427 100 100 GLN CA C 55.41 0.2 1 428 100 100 GLN CB C 28.96 0.2 1 429 100 100 GLN N N 117.79 0.2 1 430 101 101 SER H H 8.82 0.02 1 431 101 101 SER C C 175.38 0.2 1 432 101 101 SER CA C 62.63 0.2 1 433 101 101 SER CB C 63.67 0.2 1 434 101 101 SER N N 117.01 0.2 1 435 102 102 VAL H H 8.31 0.02 1 436 102 102 VAL C C 178.2 0.2 1 437 102 102 VAL CA C 64.52 0.2 1 438 102 102 VAL CB C 32.72 0.2 1 439 102 102 VAL N N 122.82 0.2 1 440 103 103 ARG H H 8.33 0.02 1 441 103 103 ARG C C 178.04 0.2 1 442 103 103 ARG CA C 59.26 0.2 1 443 103 103 ARG CB C 31.53 0.2 1 444 103 103 ARG N N 121.58 0.2 1 445 104 104 GLU H H 7.79 0.02 1 446 104 104 GLU C C 176.03 0.2 1 447 104 104 GLU CA C 55.95 0.2 1 448 104 104 GLU CB C 29.21 0.2 1 449 104 104 GLU N N 114.43 0.2 1 450 105 105 ALA H H 7.2 0.02 1 451 105 105 ALA C C 177.05 0.2 1 452 105 105 ALA CA C 53.19 0.2 1 453 105 105 ALA CB C 18.9 0.2 1 454 105 105 ALA N N 122.88 0.2 1 455 106 106 ASP H H 8.39 0.02 1 456 106 106 ASP C C 175.44 0.2 1 457 106 106 ASP CA C 53.64 0.2 1 458 106 106 ASP CB C 39.89 0.2 1 459 106 106 ASP N N 120.81 0.2 1 460 107 107 LEU H H 7.74 0.02 1 461 107 107 LEU C C 177.73 0.2 1 462 107 107 LEU CA C 55.46 0.2 1 463 107 107 LEU CB C 43.35 0.2 1 464 107 107 LEU N N 121.59 0.2 1 465 108 108 SER H H 8.5 0.02 1 466 108 108 SER C C 174.07 0.2 1 467 108 108 SER CA C 58.62 0.2 1 468 108 108 SER CB C 65.45 0.2 1 469 108 108 SER N N 118.96 0.2 1 470 109 109 LEU H H 8.54 0.02 1 471 109 109 LEU C C 178.3 0.2 1 472 109 109 LEU CA C 59.75 0.2 1 473 109 109 LEU CB C 41.71 0.2 1 474 109 109 LEU N N 123.23 0.2 1 475 110 110 ALA H H 8.3 0.02 1 476 110 110 ALA C C 178.73 0.2 1 477 110 110 ALA CA C 56.08 0.2 1 478 110 110 ALA CB C 20.28 0.2 1 479 110 110 ALA N N 116.92 0.2 1 480 111 111 GLU H H 7.43 0.02 1 481 111 111 GLU C C 179.99 0.2 1 482 111 111 GLU CA C 59.81 0.2 1 483 111 111 GLU CB C 31.53 0.2 1 484 111 111 GLU N N 115.46 0.2 1 485 112 112 ALA H H 8.65 0.02 1 486 112 112 ALA C C 179.44 0.2 1 487 112 112 ALA CA C 55.76 0.2 1 488 112 112 ALA CB C 19.4 0.2 1 489 112 112 ALA N N 120.94 0.2 1 490 113 113 LEU H H 8.11 0.02 1 491 113 113 LEU C C 179.23 0.2 1 492 113 113 LEU CA C 58.66 0.2 1 493 113 113 LEU CB C 41.78 0.2 1 494 113 113 LEU N N 115.75 0.2 1 495 114 114 GLY H H 7.67 0.02 1 496 114 114 GLY C C 175.58 0.2 1 497 114 114 GLY CA C 48.19 0.2 1 498 114 114 GLY N N 104.28 0.2 1 499 115 115 TRP H H 7.54 0.02 1 500 115 115 TRP C C 178.93 0.2 1 501 115 115 TRP CA C 62.59 0.2 1 502 115 115 TRP CB C 28.39 0.2 1 503 115 115 TRP N N 121.63 0.2 1 504 116 116 LEU H H 8.49 0.02 1 505 116 116 LEU C C 178.25 0.2 1 506 116 116 LEU CA C 58.01 0.2 1 507 116 116 LEU CB C 42.6 0.2 1 508 116 116 LEU N N 117.62 0.2 1 509 117 117 PHE H H 8.53 0.02 1 510 117 117 PHE C C 175.81 0.2 1 511 117 117 PHE CA C 62.77 0.2 1 512 117 117 PHE CB C 39.22 0.2 1 513 117 117 PHE N N 119.54 0.2 1 514 118 118 VAL H H 7.18 0.02 1 515 118 118 VAL C C 177.1 0.2 1 516 118 118 VAL CA C 65.62 0.2 1 517 118 118 VAL CB C 31.1 0.2 1 518 118 118 VAL N N 118.12 0.2 1 519 119 119 SER H H 7.99 0.02 1 520 119 119 SER C C 179.53 0.2 1 521 119 119 SER CA C 61.87 0.2 1 522 119 119 SER CB C 63.87 0.2 1 523 119 119 SER N N 112 0.2 1 524 120 120 GLU H H 9.05 0.02 1 525 120 120 GLU C C 179.42 0.2 1 526 120 120 GLU CA C 58.92 0.2 1 527 120 120 GLU CB C 28.59 0.2 1 528 120 120 GLU N N 117.54 0.2 1 529 121 121 GLY H H 7.75 0.02 1 530 121 121 GLY C C 173.13 0.2 1 531 121 121 GLY CA C 45.39 0.2 1 532 121 121 GLY N N 111.94 0.2 1 533 122 122 SER H H 6.51 0.02 1 534 122 122 SER N N 114.35 0.2 1 535 124 124 LEU H H 8.2 0.02 1 536 124 124 LEU N N 120.1 0.2 1 537 125 125 GLY H H 9.1 0.02 1 538 125 125 GLY N N 123 0.2 1 539 126 126 ALA H H 13.2 0.02 1 540 126 126 ALA CA C 58.53 0.2 1 541 126 126 ALA CB C 21.95 0.2 1 542 126 126 ALA N N 124.1 0.2 1 543 127 127 ALA H H 8.49 0.02 1 544 127 127 ALA C C 180.51 0.2 1 545 127 127 ALA CA C 56.56 0.2 1 546 127 127 ALA CB C 19.28 0.2 1 547 127 127 ALA N N 119.53 0.2 1 548 128 128 PHE H H 8.21 0.02 1 549 128 128 PHE C C 179.28 0.2 1 550 128 128 PHE CA C 60.63 0.2 1 551 128 128 PHE CB C 38.77 0.2 1 552 128 128 PHE N N 117.68 0.2 1 553 129 129 LEU H H 8.6 0.02 1 554 129 129 LEU C C 178.45 0.2 1 555 129 129 LEU CA C 58.87 0.2 1 556 129 129 LEU CB C 44.56 0.2 1 557 129 129 LEU N N 120.45 0.2 1 558 130 130 PHE H H 10.04 0.02 1 559 130 130 PHE C C 177.59 0.2 1 560 130 130 PHE CA C 62.98 0.2 1 561 130 130 PHE CB C 39.77 0.2 1 562 130 130 PHE N N 120.39 0.2 1 563 131 131 LYS H H 7.4 0.02 1 564 131 131 LYS C C 179.98 0.2 1 565 131 131 LYS CA C 59.51 0.2 1 566 131 131 LYS CB C 32.67 0.2 1 567 131 131 LYS N N 117.03 0.2 1 568 132 132 LYS H H 7.41 0.02 1 569 132 132 LYS C C 178.86 0.2 1 570 132 132 LYS CA C 60.06 0.2 1 571 132 132 LYS CB C 30.85 0.2 1 572 132 132 LYS N N 119.57 0.2 1 573 133 133 ALA H H 8.14 0.02 1 574 133 133 ALA C C 178.67 0.2 1 575 133 133 ALA CA C 54.72 0.2 1 576 133 133 ALA CB C 17.26 0.2 1 577 133 133 ALA N N 122.19 0.2 1 578 134 134 ALA H H 7.39 0.02 1 579 134 134 ALA C C 181.46 0.2 1 580 134 134 ALA CA C 55.12 0.2 1 581 134 134 ALA CB C 17.99 0.2 1 582 134 134 ALA N N 120.86 0.2 1 583 135 135 ALA H H 7.44 0.02 1 584 135 135 ALA C C 178.85 0.2 1 585 135 135 ALA CA C 54.73 0.2 1 586 135 135 ALA CB C 18.79 0.2 1 587 135 135 ALA N N 121.03 0.2 1 588 136 136 LEU H H 7.46 0.02 1 589 136 136 LEU C C 175.39 0.2 1 590 136 136 LEU CA C 54.09 0.2 1 591 136 136 LEU CB C 42.53 0.2 1 592 136 136 LEU N N 116.92 0.2 1 593 137 137 GLU H H 8.17 0.02 1 594 137 137 GLU C C 173.8 0.2 1 595 137 137 GLU CA C 57.79 0.2 1 596 137 137 GLU CB C 26.71 0.2 1 597 137 137 GLU N N 115.27 0.2 1 598 138 138 LEU H H 6.83 0.02 1 599 138 138 LEU C C 176.24 0.2 1 600 138 138 LEU CA C 53.31 0.2 1 601 138 138 LEU CB C 42.74 0.2 1 602 138 138 LEU N N 116.44 0.2 1 603 139 139 ASP H H 9.33 0.02 1 604 139 139 ASP C C 175.66 0.2 1 605 139 139 ASP CA C 54.61 0.2 1 606 139 139 ASP CB C 41.19 0.2 1 607 139 139 ASP N N 121.21 0.2 1 608 140 140 GLU H H 10.52 0.02 1 609 140 140 GLU C C 174.8 0.2 1 610 140 140 GLU CA C 59.03 0.2 1 611 140 140 GLU CB C 28.84 0.2 1 612 140 140 GLU N N 116.79 0.2 1 613 141 141 ASN H H 8.86 0.02 1 614 141 141 ASN C C 174.56 0.2 1 615 141 141 ASN CA C 53.34 0.2 1 616 141 141 ASN CB C 41.42 0.2 1 617 141 141 ASN N N 116.63 0.2 1 618 142 142 PHE H H 7.89 0.02 1 619 142 142 PHE C C 175.15 0.2 1 620 142 142 PHE CA C 58.82 0.2 1 621 142 142 PHE CB C 40.64 0.2 1 622 142 142 PHE N N 122.56 0.2 1 623 143 143 GLY H H 9.72 0.02 1 624 143 143 GLY C C 170.94 0.2 1 625 143 143 GLY CA C 47.93 0.2 1 626 143 143 GLY N N 119.12 0.2 1 627 144 144 ALA H H 7.51 0.02 1 628 144 144 ALA C C 179.08 0.2 1 629 144 144 ALA CA C 51.35 0.2 1 630 144 144 ALA CB C 18.91 0.2 1 631 144 144 ALA N N 118.82 0.2 1 632 145 145 ARG H H 11.16 0.02 1 633 145 145 ARG C C 183.75 0.2 1 634 145 145 ARG CA C 60.63 0.2 1 635 145 145 ARG CB C 31.66 0.2 1 636 145 145 ARG N N 125.29 0.2 1 637 146 146 HIS H H 11.25 0.2 1 638 146 146 HIS C C 174.95 0.2 1 639 146 146 HIS CA C 59.88 0.2 1 640 146 146 HIS CB C 27.71 0.2 1 641 146 146 HIS N N 116.25 0.2 1 642 147 147 LEU H H 7.65 0.02 1 643 147 147 LEU C C 175.81 0.2 1 644 147 147 LEU CA C 54.62 0.2 1 645 147 147 LEU CB C 44.91 0.2 1 646 147 147 LEU N N 120.44 0.2 1 647 148 148 ALA H H 7.57 0.02 1 648 148 148 ALA C C 176.91 0.2 1 649 148 148 ALA CA C 52.48 0.2 1 650 148 148 ALA CB C 20.76 0.2 1 651 148 148 ALA N N 123.08 0.2 1 652 149 149 GLU H H 8.39 0.02 1 653 149 149 GLU C C 174.68 0.2 1 654 149 149 GLU N N 122.54 0.2 1 655 151 151 GLU C C 179.46 0.2 1 656 151 151 GLU CA C 64.19 0.2 1 657 151 151 GLU CB C 31.7 0.2 1 658 152 152 GLY H H 9.13 0.02 1 659 152 152 GLY C C 174.84 0.2 1 660 152 152 GLY CA C 45.77 0.2 1 661 152 152 GLY N N 113.78 0.2 1 662 153 153 GLY H H 8.16 0.02 1 663 153 153 GLY C C 175.71 0.2 1 664 153 153 GLY CA C 44.56 0.2 1 665 153 153 GLY N N 107.98 0.2 1 666 154 154 ARG H H 9.47 0.02 1 667 154 154 ARG C C 178.17 0.2 1 668 154 154 ARG CA C 59.86 0.2 1 669 154 154 ARG CB C 31.46 0.2 1 670 154 154 ARG N N 125.28 0.2 1 671 155 155 ALA H H 8.67 0.02 1 672 155 155 ALA C C 180.4 0.2 1 673 155 155 ALA CA C 55.86 0.2 1 674 155 155 ALA CB C 17.9 0.2 1 675 155 155 ALA N N 122.5 0.2 1 676 156 156 GLN H H 8.99 0.02 1 677 156 156 GLN C C 179.1 0.2 1 678 156 156 GLN CA C 59.43 0.2 1 679 156 156 GLN CB C 27.8 0.2 1 680 156 156 GLN N N 118.95 0.2 1 681 157 157 GLY H H 7.76 0.02 1 682 157 157 GLY C C 176.95 0.2 1 683 157 157 GLY CA C 47.48 0.2 1 684 157 157 GLY N N 107.15 0.2 1 685 158 158 TRP H H 7.63 0.02 1 686 158 158 TRP C C 176.72 0.2 1 687 158 158 TRP CA C 58.95 0.2 1 688 158 158 TRP CB C 30.73 0.2 1 689 158 158 TRP N N 125.08 0.2 1 690 159 159 LYS H H 8.31 0.02 1 691 159 159 LYS C C 179.53 0.2 1 692 159 159 LYS CA C 60.04 0.2 1 693 159 159 LYS CB C 32.48 0.2 1 694 159 159 LYS N N 118.19 0.2 1 695 160 160 SER H H 8.13 0.02 1 696 160 160 SER C C 176.34 0.2 1 697 160 160 SER CA C 61.24 0.2 1 698 160 160 SER CB C 63.03 0.2 1 699 160 160 SER N N 112.59 0.2 1 700 161 161 PHE H H 7.22 0.02 1 701 161 161 PHE C C 176.58 0.2 1 702 161 161 PHE CA C 61.99 0.2 1 703 161 161 PHE CB C 39.61 0.2 1 704 161 161 PHE N N 123.85 0.2 1 705 162 162 VAL H H 8.34 0.02 1 706 162 162 VAL C C 176.44 0.2 1 707 162 162 VAL CA C 66 0.2 1 708 162 162 VAL CB C 30.88 0.2 1 709 162 162 VAL N N 117.3 0.2 1 710 163 163 ALA H H 7.56 0.02 1 711 163 163 ALA C C 181.06 0.2 1 712 163 163 ALA CA C 55.16 0.2 1 713 163 163 ALA CB C 18.17 0.2 1 714 163 163 ALA N N 119.86 0.2 1 715 164 164 ILE H H 6.77 0.02 1 716 164 164 ILE C C 178.85 0.2 1 717 164 164 ILE CA C 63.99 0.2 1 718 164 164 ILE CB C 37.52 0.2 1 719 164 164 ILE N N 116.89 0.2 1 720 165 165 LEU H H 7.94 0.02 1 721 165 165 LEU C C 178.27 0.2 1 722 165 165 LEU CA C 58.76 0.2 1 723 165 165 LEU CB C 42.52 0.2 1 724 165 165 LEU N N 121.24 0.2 1 725 166 166 ASP H H 8.67 0.02 1 726 166 166 ASP C C 178.23 0.2 1 727 166 166 ASP CA C 57.09 0.2 1 728 166 166 ASP CB C 40.27 0.2 1 729 166 166 ASP N N 116.45 0.2 1 730 167 167 GLY H H 7.48 0.02 1 731 167 167 GLY C C 174.5 0.2 1 732 167 167 GLY CA C 45.35 0.2 1 733 167 167 GLY N N 106.51 0.2 1 734 168 168 ILE H H 6.83 0.02 1 735 168 168 ILE C C 176.06 0.2 1 736 168 168 ILE CA C 62.79 0.2 1 737 168 168 ILE CB C 39.38 0.2 1 738 168 168 ILE N N 121.08 0.2 1 739 169 169 GLU H H 8.71 0.02 1 740 169 169 GLU C C 174.58 0.2 1 741 169 169 GLU CA C 56.21 0.2 1 742 169 169 GLU CB C 29.93 0.2 1 743 169 169 GLU N N 129.48 0.2 1 744 170 170 LEU H H 7.9 0.02 1 745 170 170 LEU C C 177.16 0.2 1 746 170 170 LEU CA C 53.42 0.2 1 747 170 170 LEU CB C 44.45 0.2 1 748 170 170 LEU N N 124.81 0.2 1 749 171 171 ASN H H 9.51 0.02 1 750 171 171 ASN C C 175.4 0.2 1 751 171 171 ASN CA C 51.79 0.2 1 752 171 171 ASN CB C 38.44 0.2 1 753 171 171 ASN N N 121.37 0.2 1 754 172 172 GLU H H 8.47 0.02 1 755 172 172 GLU C C 179.13 0.2 1 756 172 172 GLU CA C 61.07 0.2 1 757 172 172 GLU CB C 29.86 0.2 1 758 172 172 GLU N N 116.91 0.2 1 759 173 173 GLU H H 8.1 0.02 1 760 173 173 GLU C C 179.3 0.2 1 761 173 173 GLU CA C 59.55 0.2 1 762 173 173 GLU CB C 29.3 0.2 1 763 173 173 GLU N N 121.03 0.2 1 764 174 174 GLU H H 8.6 0.02 1 765 174 174 GLU C C 178.73 0.2 1 766 174 174 GLU CA C 59.34 0.2 1 767 174 174 GLU CB C 31.52 0.2 1 768 174 174 GLU N N 120.45 0.2 1 769 175 175 GLU H H 8.68 0.02 1 770 175 175 GLU C C 180.63 0.2 1 771 175 175 GLU CA C 59.49 0.2 1 772 175 175 GLU CB C 29.4 0.2 1 773 175 175 GLU N N 119.61 0.2 1 774 176 176 ARG H H 7.48 0.02 1 775 176 176 ARG C C 179.81 0.2 1 776 176 176 ARG CA C 59.88 0.2 1 777 176 176 ARG CB C 30.11 0.2 1 778 176 176 ARG N N 119.04 0.2 1 779 177 177 LEU H H 8.07 0.02 1 780 177 177 LEU C C 178.59 0.2 1 781 177 177 LEU CA C 57.98 0.2 1 782 177 177 LEU CB C 42.52 0.2 1 783 177 177 LEU N N 122.57 0.2 1 784 178 178 ALA H H 8.26 0.02 1 785 178 178 ALA C C 179.44 0.2 1 786 178 178 ALA CA C 55.99 0.2 1 787 178 178 ALA CB C 16.73 0.2 1 788 178 178 ALA N N 124 0.2 1 789 179 179 ALA H H 7.28 0.02 1 790 179 179 ALA C C 179.81 0.2 1 791 179 179 ALA CA C 55.33 0.2 1 792 179 179 ALA CB C 18.48 0.2 1 793 179 179 ALA N N 118.49 0.2 1 794 180 180 LYS H H 8.19 0.02 1 795 180 180 LYS C C 178.21 0.2 1 796 180 180 LYS CA C 59.99 0.2 1 797 180 180 LYS CB C 33.32 0.2 1 798 180 180 LYS N N 121.65 0.2 1 799 181 181 GLY H H 8.87 0.02 1 800 181 181 GLY C C 173.85 0.2 1 801 181 181 GLY CA C 47.68 0.2 1 802 181 181 GLY N N 106.71 0.2 1 803 182 182 ALA H H 7.64 0.02 1 804 182 182 ALA C C 179.25 0.2 1 805 182 182 ALA CA C 54.73 0.2 1 806 182 182 ALA CB C 18.05 0.2 1 807 182 182 ALA N N 121.23 0.2 1 808 183 183 SER H H 7.92 0.02 1 809 183 183 SER C C 177.59 0.2 1 810 183 183 SER CA C 53.23 0.2 1 811 183 183 SER CB C 63.28 0.2 1 812 183 183 SER N N 112.69 0.2 1 813 184 184 ASP H H 9.33 0.02 1 814 184 184 ASP C C 178.66 0.2 1 815 184 184 ASP CA C 57.38 0.2 1 816 184 184 ASP CB C 39.58 0.2 1 817 184 184 ASP N N 122.72 0.2 1 818 185 185 ALA H H 7.77 0.02 1 819 185 185 ALA C C 179.46 0.2 1 820 185 185 ALA CA C 55.08 0.2 1 821 185 185 ALA CB C 18.43 0.2 1 822 185 185 ALA N N 125.66 0.2 1 823 186 186 PHE H H 7.43 0.02 1 824 186 186 PHE C C 178.94 0.2 1 825 186 186 PHE CA C 64.29 0.2 1 826 186 186 PHE CB C 39.96 0.2 1 827 186 186 PHE N N 115.46 0.2 1 828 187 187 ASN H H 7.74 0.02 1 829 187 187 ASN C C 177.57 0.2 1 830 187 187 ASN CA C 56.25 0.2 1 831 187 187 ASN CB C 37.98 0.2 1 832 187 187 ASN N N 117.56 0.2 1 833 188 188 ARG H H 8.59 0.2 1 834 188 188 ARG C C 177.42 0.2 1 835 188 188 ARG CA C 63.88 0.2 1 836 188 188 ARG CB C 30.99 0.2 1 837 188 188 ARG N N 121.49 0.2 1 838 189 189 PHE H H 8.08 0.02 1 839 189 189 PHE C C 177.34 0.2 1 840 189 189 PHE CA C 62.9 0.2 1 841 189 189 PHE CB C 38.27 0.2 1 842 189 189 PHE N N 119.28 0.2 1 843 190 190 GLY H H 7.56 0.02 1 844 190 190 GLY C C 175.11 0.2 1 845 190 190 GLY CA C 47.87 0.2 1 846 190 190 GLY N N 102.75 0.2 1 847 191 191 ASP H H 7.62 0.02 1 848 191 191 ASP C C 179.53 0.2 1 849 191 191 ASP CA C 57.66 0.2 1 850 191 191 ASP CB C 40.87 0.2 1 851 191 191 ASP N N 121.67 0.2 1 852 192 192 LEU H H 8.18 0.02 1 853 192 192 LEU C C 178.06 0.2 1 854 192 192 LEU CA C 58.06 0.2 1 855 192 192 LEU CB C 41.99 0.2 1 856 192 192 LEU N N 120.81 0.2 1 857 193 193 LEU H H 8.06 0.02 1 858 193 193 LEU C C 178.5 0.2 1 859 193 193 LEU CA C 57.37 0.2 1 860 193 193 LEU CB C 42.56 0.2 1 861 193 193 LEU N N 119.18 0.2 1 862 194 194 GLU H H 7.56 0.02 1 863 194 194 GLU C C 179.57 0.2 1 864 194 194 GLU CA C 58.82 0.2 1 865 194 194 GLU CB C 29.08 0.2 1 866 194 194 GLU N N 115.21 0.2 1 867 195 195 ARG H H 7.62 0.02 1 868 195 195 ARG C C 179.81 0.2 1 869 195 195 ARG CA C 59.49 0.2 1 870 195 195 ARG CB C 30.49 0.2 1 871 195 195 ARG N N 117.95 0.2 1 872 196 196 THR H H 8.71 0.02 1 873 196 196 THR C C 177.4 0.2 1 874 196 196 THR CA C 65.27 0.2 1 875 196 196 THR CB C 68.21 0.2 1 876 196 196 THR N N 110.87 0.2 1 877 197 197 PHE H H 7.67 0.02 1 878 197 197 PHE C C 174.12 0.2 1 879 197 197 PHE CA C 60.5 0.2 1 880 197 197 PHE CB C 38.6 0.2 1 881 197 197 PHE N N 119.92 0.2 1 882 198 198 ALA H H 7 0.02 1 883 198 198 ALA N N 129.32 0.2 1 stop_ save_