data_6983 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 'Backbone 1H, 13C, 15N, and 13CB Chemical Shift Assignments for Azide-Inhibited P. aeruginosa Heme Oxygenase' ; _BMRB_accession_number 6983 _BMRB_flat_file_name bmr6983.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" 180 "13C chemical shifts" 511 "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 6987 'Heme-heme oxygenase-cyanide 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-azide complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Azide-inhibited heme-heme oxygenase from P. aeruginosa' $Azide-inhibited_heme_oxygenase_polypeptide 'PROTOPORPHYRIN IX CONTAINING FE 1' $HEM azide $AZI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state 'protein-ligand system' _System_paramagnetic yes _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'Azide-inhibited heme-heme oxygenase from P. aeruginosa' stop_ loop_ _Biological_function 'Heme metabolism in P. aeruginosa' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Azide-inhibited_heme_oxygenase_polypeptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Azide-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 Mon Sep 19 15:04:12 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_AZI _Saveframe_category ligand _Mol_type non-polymer _Name_common "AZI (AZIDE ION)" _BMRB_code . _PDB_code AZI _Molecular_mass 42.020 _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 Mon Sep 19 15:05:26 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . -1 . ? N2 N2 N . 1 . ? N3 N3 N . -1 . ? 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 DOUB N1 N2 ? ? DOUB N2 N3 ? ? 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 $Azide-inhibited_heme_oxygenase_polypeptide 'Pseudomonas aeruginosa' 287 Bacteria . 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 $Azide-inhibited_heme_oxygenase_polypeptide '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 $Azide-inhibited_heme_oxygenase_polypeptide 2.4 mM '[U-13C; U-15N]' $AZI 24 mM . 'Phosphate Buffer' 50 mM . H2O 95 % . D2O 5 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Inova' _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_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_HSQC HNCA HN(CO)CA HNCACB CBCA(CO)NH HNCO (HCA)CO(CA)NH 15N-NOESY-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 'Azide-inhibited heme-heme oxygenase from P. aeruginosa' _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 3 3 THR H H 7.8 0.02 1 2 3 3 THR N N 119.17 0.2 1 3 5 5 ALA H H 8.2 0.02 1 4 5 5 ALA N N 126.16 0.2 1 5 8 8 SER H H 8.35 0.02 1 6 8 8 SER N N 117.05 0.2 1 7 10 10 ARG CA C 56.87 0.2 1 8 10 10 ARG CB C 30.39 0.2 1 9 11 11 GLN H H 8.34 0.02 1 10 11 11 GLN CA C 55.81 0.2 1 11 11 11 GLN CB C 29.54 0.2 1 12 11 11 GLN N N 120.95 0.2 1 13 12 12 ASN H H 8.37 0.02 1 14 12 12 ASN C C 174.92 0.2 1 15 12 12 ASN CA C 53.11 0.2 1 16 12 12 ASN CB C 38.73 0.2 1 17 12 12 ASN N N 119.32 0.2 1 18 13 13 LEU H H 7.96 0.02 1 19 13 13 LEU C C 177.52 0.2 1 20 13 13 LEU CA C 54.34 0.2 1 21 13 13 LEU CB C 42.59 0.2 1 22 13 13 LEU N N 121.29 0.2 1 23 14 14 ARG H H 8.83 0.02 1 24 14 14 ARG C C 178.22 0.2 1 25 14 14 ARG CA C 60.97 0.2 1 26 14 14 ARG CB C 28.64 0.2 1 27 14 14 ARG N N 128.01 0.2 1 28 15 15 SER H H 11.55 0.02 1 29 15 15 SER C C 177 0.2 1 30 15 15 SER CA C 60.46 0.2 1 31 15 15 SER CB C 61.49 0.2 1 32 15 15 SER N N 117.66 0.2 1 33 16 16 GLN H H 6.76 0.02 1 34 16 16 GLN C C 178.74 0.2 1 35 16 16 GLN CA C 58.32 0.2 1 36 16 16 GLN CB C 28.36 0.2 1 37 16 16 GLN N N 121.96 0.2 1 38 17 17 ARG H H 8.11 0.02 1 39 17 17 ARG C C 179.92 0.2 1 40 17 17 ARG CA C 60.34 0.2 1 41 17 17 ARG CB C 30.14 0.2 1 42 17 17 ARG N N 121.53 0.2 1 43 18 18 LEU H H 8.88 0.02 1 44 18 18 LEU C C 179.52 0.2 1 45 18 18 LEU CA C 57.88 0.2 1 46 18 18 LEU CB C 40.36 0.2 1 47 18 18 LEU N N 118.86 0.2 1 48 19 19 ASN H H 8.16 0.02 1 49 19 19 ASN C C 177.54 0.2 1 50 19 19 ASN CA C 57.01 0.2 1 51 19 19 ASN CB C 39.21 0.2 1 52 19 19 ASN N N 120.87 0.2 1 53 20 20 LEU H H 8.1 0.02 1 54 20 20 LEU C C 180.81 0.2 1 55 20 20 LEU CA C 58.61 0.2 1 56 20 20 LEU CB C 41.78 0.2 1 57 20 20 LEU N N 119.82 0.2 1 58 21 21 LEU H H 8.32 0.02 1 59 21 21 LEU C C 179.01 0.2 1 60 21 21 LEU CA C 57.82 0.2 1 61 21 21 LEU CB C 42.82 0.2 1 62 21 21 LEU N N 119.35 0.2 1 63 22 22 THR H H 8.08 0.02 1 64 22 22 THR C C 175.64 0.2 1 65 22 22 THR CA C 62.51 0.2 1 66 22 22 THR CB C 69.97 0.2 1 67 22 22 THR N N 105.93 0.2 1 68 23 23 ASN H H 8.24 0.02 1 69 23 23 ASN C C 178.4 0.2 1 70 23 23 ASN CA C 59.61 0.2 1 71 23 23 ASN CB C 40.26 0.2 1 72 23 23 ASN N N 124.29 0.2 1 73 24 24 GLU H H 9.86 0.02 1 74 24 24 GLU C C 177.43 0.2 1 75 24 24 GLU N N 120 0.2 1 76 25 25 PRO C C 179.93 0.2 1 77 25 25 PRO CA C 66.79 0.2 1 78 25 25 PRO CB C 30.41 0.2 1 79 26 26 HIS H H 10.37 0.02 1 80 26 26 HIS C C 180.65 0.2 1 81 26 26 HIS CA C 76.82 0.2 1 82 26 26 HIS CB C 40.46 0.2 1 83 26 26 HIS N N 121.28 0.2 1 84 27 27 GLN H H 10.88 0.02 1 85 27 27 GLN C C 180.92 0.2 1 86 27 27 GLN CA C 61.28 0.2 1 87 27 27 GLN CB C 29.72 0.2 1 88 27 27 GLN N N 123.45 0.2 1 89 28 28 ARG H H 9.16 0.02 1 90 28 28 ARG C C 179.66 0.2 1 91 28 28 ARG CA C 59.91 0.2 1 92 28 28 ARG CB C 30.37 0.2 1 93 28 28 ARG N N 120.79 0.2 1 94 29 29 LEU H H 9.1 0.02 1 95 29 29 LEU C C 177.87 0.2 1 96 29 29 LEU CA C 56.82 0.2 1 97 29 29 LEU CB C 40.3 0.2 1 98 29 29 LEU N N 123.08 0.2 1 99 30 30 GLU H H 9.74 0.02 1 100 30 30 GLU C C 178.45 0.2 1 101 30 30 GLU CA C 60.04 0.2 1 102 30 30 GLU CB C 28.32 0.2 1 103 30 30 GLU N N 121.21 0.2 1 104 31 31 SER H H 7.67 0.02 1 105 31 31 SER C C 176.65 0.2 1 106 31 31 SER CA C 61.57 0.2 1 107 31 31 SER CB C 62.8 0.2 1 108 31 31 SER N N 113.48 0.2 1 109 32 32 LEU H H 7.93 0.02 1 110 32 32 LEU C C 180.01 0.2 1 111 32 32 LEU CA C 56.36 0.2 1 112 32 32 LEU CB C 42.11 0.2 1 113 32 32 LEU N N 125.08 0.2 1 114 33 33 VAL H H 8.45 0.02 1 115 33 33 VAL C C 177.25 0.2 1 116 33 33 VAL CA C 67.1 0.2 1 117 33 33 VAL CB C 30.63 0.2 1 118 33 33 VAL N N 118.89 0.2 1 119 34 34 LYS H H 7.42 0.02 1 120 34 34 LYS C C 180.52 0.2 1 121 34 34 LYS CA C 59.97 0.2 1 122 34 34 LYS CB C 31.61 0.2 1 123 34 34 LYS N N 116.6 0.2 1 124 35 35 SER H H 7.78 0.02 1 125 35 35 SER C C 174.75 0.2 1 126 35 35 SER CA C 61.06 0.2 1 127 35 35 SER CB C 62.91 0.2 1 128 35 35 SER N N 115.34 0.2 1 129 36 36 LYS H H 7.02 0.02 1 130 36 36 LYS C C 175.12 0.2 1 131 36 36 LYS CA C 54.09 0.2 1 132 36 36 LYS CB C 29.76 0.2 1 133 36 36 LYS N N 119.36 0.2 1 134 37 37 GLU H H 7.45 0.02 1 135 37 37 GLU C C 179.02 0.2 1 136 37 37 GLU N N 110.96 0.2 1 137 38 38 PRO C C 173.57 0.2 1 138 38 38 PRO CA C 64.88 0.2 1 139 38 38 PRO CB C 31.6 0.2 1 140 39 39 PHE H H 7.87 0.02 1 141 39 39 PHE C C 175.84 0.2 1 142 39 39 PHE CA C 57.44 0.2 1 143 39 39 PHE CB C 37.83 0.2 1 144 39 39 PHE N N 108.36 0.2 1 145 40 40 ALA H H 7.76 0.02 1 146 40 40 ALA C C 177.86 0.2 1 147 40 40 ALA CA C 54.44 0.2 1 148 40 40 ALA CB C 19.64 0.2 1 149 40 40 ALA N N 120.81 0.2 1 150 41 41 SER H H 7.44 0.02 1 151 41 41 SER C C 174.32 0.2 1 152 41 41 SER N N 104.51 0.2 1 153 42 42 ARG C C 177.34 0.2 1 154 42 42 ARG CA C 61.11 0.2 1 155 42 42 ARG CB C 30.31 0.2 1 156 43 43 ASP H H 8.19 0.02 1 157 43 43 ASP C C 178.13 0.2 1 158 43 43 ASP CA C 57.59 0.2 1 159 43 43 ASP CB C 40.83 0.2 1 160 43 43 ASP N N 118.06 0.2 1 161 44 44 ASN H H 7.98 0.02 1 162 44 44 ASN C C 177.44 0.2 1 163 44 44 ASN CA C 55.91 0.2 1 164 44 44 ASN CB C 37 0.2 1 165 44 44 ASN N N 120.85 0.2 1 166 45 45 PHE H H 8.57 0.02 1 167 45 45 PHE C C 178.4 0.2 1 168 45 45 PHE CA C 63.27 0.2 1 169 45 45 PHE CB C 39.06 0.2 1 170 45 45 PHE N N 123.85 0.2 1 171 46 46 ALA H H 8.86 0.02 1 172 46 46 ALA C C 178.91 0.2 1 173 46 46 ALA CA C 55.34 0.2 1 174 46 46 ALA CB C 17.63 0.2 1 175 46 46 ALA N N 120.7 0.2 1 176 47 47 ARG H H 7.04 0.02 1 177 47 47 ARG C C 178.7 0.2 1 178 47 47 ARG CA C 59.47 0.2 1 179 47 47 ARG CB C 27.5 0.2 1 180 47 47 ARG N N 116.63 0.2 1 181 48 48 PHE H H 7.56 0.02 1 182 48 48 PHE C C 176.67 0.2 1 183 48 48 PHE CA C 59.9 0.2 1 184 48 48 PHE CB C 38.73 0.2 1 185 48 48 PHE N N 123.61 0.2 1 186 49 49 VAL H H 8.87 0.02 1 187 49 49 VAL C C 177.65 0.2 1 188 49 49 VAL CA C 66.59 0.2 1 189 49 49 VAL CB C 30.35 0.2 1 190 49 49 VAL N N 120.94 0.2 1 191 50 50 ALA H H 8.46 0.02 1 192 50 50 ALA C C 178.38 0.2 1 193 50 50 ALA CA C 56.05 0.2 1 194 50 50 ALA CB C 17.1 0.2 1 195 50 50 ALA N N 122.02 0.2 1 196 51 51 ALA H H 7.09 0.02 1 197 51 51 ALA C C 178.35 0.2 1 198 51 51 ALA CA C 55.79 0.2 1 199 51 51 ALA CB C 16.41 0.2 1 200 51 51 ALA N N 121.07 0.2 1 201 52 52 GLN H H 7.9 0.02 1 202 52 52 GLN C C 179.72 0.2 1 203 52 52 GLN CA C 59.51 0.2 1 204 52 52 GLN CB C 28.92 0.2 1 205 52 52 GLN N N 116.34 0.2 1 206 53 53 TYR H H 9.47 0.02 1 207 53 53 TYR C C 176.05 0.2 1 208 53 53 TYR CA C 62.19 0.2 1 209 53 53 TYR CB C 37.65 0.2 1 210 53 53 TYR N N 119.11 0.2 1 211 54 54 LEU H H 8.29 0.02 1 212 54 54 LEU C C 178.87 0.2 1 213 54 54 LEU CA C 58.19 0.2 1 214 54 54 LEU CB C 42.43 0.2 1 215 54 54 LEU N N 120.05 0.2 1 216 55 55 PHE H H 8.44 0.02 1 217 55 55 PHE C C 177.17 0.2 1 218 55 55 PHE CA C 60.23 0.2 1 219 55 55 PHE CB C 39.55 0.2 1 220 55 55 PHE N N 122.02 0.2 1 221 56 56 GLN H H 8.38 0.02 1 222 56 56 GLN C C 178.81 0.2 1 223 56 56 GLN CA C 58.07 0.2 1 224 56 56 GLN CB C 27.2 0.2 1 225 56 56 GLN N N 114.81 0.2 1 226 57 57 HIS H H 9.08 0.02 1 227 57 57 HIS C C 178.01 0.2 1 228 57 57 HIS CA C 59.25 0.2 1 229 57 57 HIS CB C 28.15 0.2 1 230 57 57 HIS N N 121.85 0.2 1 231 58 58 ASP H H 7.86 0.02 1 232 58 58 ASP C C 175.57 0.2 1 233 58 58 ASP CA C 57.73 0.2 1 234 58 58 ASP CB C 40.27 0.2 1 235 58 58 ASP N N 122.28 0.2 1 236 59 59 LEU H H 6.67 0.02 1 237 59 59 LEU C C 177.94 0.2 1 238 59 59 LEU CA C 54.09 0.2 1 239 59 59 LEU CB C 42.62 0.2 1 240 59 59 LEU N N 112.77 0.2 1 241 60 60 GLU H H 7.46 0.02 1 242 60 60 GLU C C 174.09 0.2 1 243 60 60 GLU N N 124.77 0.2 1 244 61 61 PRO C C 178.37 0.2 1 245 61 61 PRO CA C 65.12 0.2 1 246 61 61 PRO CB C 30.86 0.2 1 247 62 62 LEU H H 7.57 0.02 1 248 62 62 LEU C C 178.13 0.2 1 249 62 62 LEU CA C 57.16 0.2 1 250 62 62 LEU CB C 40.75 0.2 1 251 62 62 LEU N N 116.03 0.2 1 252 63 63 TYR H H 7.76 0.02 1 253 63 63 TYR C C 176.8 0.2 1 254 63 63 TYR CA C 62.95 0.2 1 255 63 63 TYR CB C 38.83 0.2 1 256 63 63 TYR N N 115.09 0.2 1 257 64 64 ARG H H 7.32 0.02 1 258 64 64 ARG C C 175.75 0.2 1 259 64 64 ARG CA C 55.54 0.2 1 260 64 64 ARG CB C 29.72 0.2 1 261 64 64 ARG N N 111.62 0.2 1 262 65 65 ASN H H 7.2 0.02 1 263 65 65 ASN C C 176.26 0.2 1 264 65 65 ASN CA C 55.09 0.2 1 265 65 65 ASN CB C 40.51 0.2 1 266 65 65 ASN N N 122.72 0.2 1 267 66 66 GLU H H 9.09 0.02 1 268 66 66 GLU C C 177.83 0.2 1 269 66 66 GLU CA C 59.97 0.2 1 270 66 66 GLU CB C 29.73 0.2 1 271 66 66 GLU N N 128.31 0.2 1 272 67 67 ALA H H 7.89 0.02 1 273 67 67 ALA C C 181.77 0.2 1 274 67 67 ALA CA C 55.42 0.2 1 275 67 67 ALA CB C 17.83 0.2 1 276 67 67 ALA N N 122.4 0.2 1 277 68 68 LEU H H 8.4 0.02 1 278 68 68 LEU C C 179.16 0.2 1 279 68 68 LEU CA C 57.9 0.2 1 280 68 68 LEU CB C 41.67 0.2 1 281 68 68 LEU N N 119.11 0.2 1 282 69 69 ALA H H 8.36 0.02 1 283 69 69 ALA C C 179.12 0.2 1 284 69 69 ALA CA C 54.35 0.2 1 285 69 69 ALA CB C 18.06 0.2 1 286 69 69 ALA N N 122.35 0.2 1 287 70 70 ARG H H 7.25 0.02 1 288 70 70 ARG C C 177.48 0.2 1 289 70 70 ARG CA C 58.29 0.2 1 290 70 70 ARG CB C 30.29 0.2 1 291 70 70 ARG N N 114.68 0.2 1 292 71 71 LEU H H 7.07 0.02 1 293 71 71 LEU C C 175.25 0.2 1 294 71 71 LEU CA C 56.05 0.2 1 295 71 71 LEU CB C 43.79 0.2 1 296 71 71 LEU N N 118.37 0.2 1 297 72 72 PHE H H 7.95 0.02 1 298 72 72 PHE C C 171.93 0.2 1 299 72 72 PHE N N 115.72 0.2 1 300 73 73 PRO C C 178.31 0.2 1 301 73 73 PRO CA C 58.64 0.2 1 302 73 73 PRO CB C 29.01 0.2 1 303 74 74 GLY H H 9.01 0.02 1 304 74 74 GLY C C 176.42 0.2 1 305 74 74 GLY CA C 46.13 0.2 1 306 74 74 GLY N N 115.93 0.2 1 307 75 75 LEU H H 8 0.02 1 308 75 75 LEU C C 178.13 0.2 1 309 75 75 LEU CA C 59.21 0.2 1 310 75 75 LEU CB C 41.56 0.2 1 311 75 75 LEU N N 123.21 0.2 1 312 76 76 ALA H H 8.82 0.02 1 313 76 76 ALA C C 180.78 0.2 1 314 76 76 ALA CA C 55.81 0.2 1 315 76 76 ALA CB C 17.88 0.2 1 316 76 76 ALA N N 117.6 0.2 1 317 77 77 SER H H 7.92 0.02 1 318 77 77 SER C C 175.02 0.2 1 319 77 77 SER CA C 60.11 0.2 1 320 77 77 SER CB C 63.61 0.2 1 321 77 77 SER N N 111.65 0.2 1 322 78 78 ARG H H 8.18 0.02 1 323 78 78 ARG C C 176.41 0.2 1 324 78 78 ARG CA C 56.8 0.2 1 325 78 78 ARG CB C 30.27 0.2 1 326 78 78 ARG N N 120.02 0.2 1 327 79 79 ALA H H 6.73 0.02 1 328 79 79 ALA C C 178.13 0.2 1 329 79 79 ALA CA C 56.48 0.2 1 330 79 79 ALA CB C 19.19 0.2 1 331 79 79 ALA N N 123.01 0.2 1 332 80 80 ARG H H 7.69 0.02 1 333 80 80 ARG C C 175.76 0.2 1 334 80 80 ARG CA C 55.73 0.2 1 335 80 80 ARG CB C 32.82 0.2 1 336 80 80 ARG N N 117.17 0.2 1 337 81 81 ASP H H 8.96 0.02 1 338 81 81 ASP C C 177.05 0.2 1 339 81 81 ASP CA C 58.49 0.2 1 340 81 81 ASP CB C 38.62 0.2 1 341 81 81 ASP N N 120.72 0.2 1 342 82 82 ASP H H 8.29 0.02 1 343 82 82 ASP C C 179.16 0.2 1 344 82 82 ASP CA C 57.76 0.2 1 345 82 82 ASP CB C 40.09 0.2 1 346 82 82 ASP N N 120.05 0.2 1 347 83 83 ALA H H 8.21 0.02 1 348 83 83 ALA C C 178.05 0.2 1 349 83 83 ALA CA C 55.33 0.2 1 350 83 83 ALA CB C 17.84 0.2 1 351 83 83 ALA N N 123.9 0.2 1 352 84 84 ALA H H 8.19 0.02 1 353 84 84 ALA C C 178.44 0.2 1 354 84 84 ALA CA C 55.24 0.2 1 355 84 84 ALA CB C 17.23 0.2 1 356 84 84 ALA N N 117.3 0.2 1 357 85 85 ARG H H 8.42 0.02 1 358 85 85 ARG C C 178.86 0.2 1 359 85 85 ARG CA C 60.21 0.2 1 360 85 85 ARG CB C 29.63 0.2 1 361 85 85 ARG N N 118.36 0.2 1 362 86 86 ALA H H 8 0.02 1 363 86 86 ALA C C 179.98 0.2 1 364 86 86 ALA CA C 55.43 0.2 1 365 86 86 ALA CB C 17.21 0.2 1 366 86 86 ALA N N 123.21 0.2 1 367 87 87 ASP H H 8.43 0.02 1 368 87 87 ASP C C 178.95 0.2 1 369 87 87 ASP CA C 58.54 0.2 1 370 87 87 ASP CB C 41.25 0.2 1 371 87 87 ASP N N 122.25 0.2 1 372 88 88 LEU H H 7.91 0.02 1 373 88 88 LEU C C 178.77 0.2 1 374 88 88 LEU CA C 58.7 0.2 1 375 88 88 LEU CB C 40.38 0.2 1 376 88 88 LEU N N 119.11 0.2 1 377 89 89 ALA H H 7.52 0.02 1 378 89 89 ALA C C 182.38 0.2 1 379 89 89 ALA CA C 55.06 0.2 1 380 89 89 ALA CB C 17.45 0.2 1 381 89 89 ALA N N 120.75 0.2 1 382 90 90 ASP H H 8.29 0.02 1 383 90 90 ASP C C 177.52 0.2 1 384 90 90 ASP CA C 57.52 0.2 1 385 90 90 ASP CB C 40.09 0.2 1 386 90 90 ASP N N 121.49 0.2 1 387 91 91 LEU H H 7.57 0.02 1 388 91 91 LEU C C 176.88 0.2 1 389 91 91 LEU CA C 54.93 0.2 1 390 91 91 LEU CB C 42.45 0.2 1 391 91 91 LEU N N 116.03 0.2 1 392 92 92 GLY H H 8.05 0.02 1 393 92 92 GLY C C 174.05 0.2 1 394 92 92 GLY CA C 46.21 0.2 1 395 92 92 GLY N N 109.25 0.2 1 396 93 93 HIS H H 8.2 0.02 1 397 93 93 HIS N N 122.71 0.2 1 398 94 94 PRO C C 177.01 0.2 1 399 94 94 PRO CA C 62.35 0.2 1 400 94 94 PRO CB C 32.78 0.2 1 401 95 95 VAL H H 8.89 0.02 1 402 95 95 VAL C C 178.22 0.2 1 403 95 95 VAL N N 124.25 0.2 1 404 96 96 PRO C C 175.43 0.2 1 405 96 96 PRO CA C 62.2 0.2 1 406 96 96 PRO CB C 31.99 0.2 1 407 97 97 GLU H H 8.42 0.02 1 408 97 97 GLU C C 176.94 0.2 1 409 97 97 GLU CA C 56.56 0.2 1 410 97 97 GLU CB C 30.38 0.2 1 411 97 97 GLU N N 119.82 0.2 1 412 98 98 GLY H H 8.45 0.02 1 413 98 98 GLY C C 173.29 0.2 1 414 98 98 GLY CA C 44.69 0.2 1 415 98 98 GLY N N 111.12 0.2 1 416 99 99 ASP H H 8.66 0.02 1 417 99 99 ASP C C 177.15 0.2 1 418 99 99 ASP CA C 52.97 0.2 1 419 99 99 ASP CB C 43.15 0.2 1 420 99 99 ASP N N 119.95 0.2 1 421 100 100 GLN H H 8.74 0.02 1 422 100 100 GLN C C 176.63 0.2 1 423 100 100 GLN CA C 55.09 0.2 1 424 100 100 GLN CB C 28.62 0.2 1 425 100 100 GLN N N 117.86 0.2 1 426 101 101 SER H H 8.8 0.02 1 427 101 101 SER C C 175.32 0.2 1 428 101 101 SER CA C 62.21 0.2 1 429 101 101 SER CB C 63.33 0.2 1 430 101 101 SER N N 116.99 0.2 1 431 102 102 VAL H H 8.26 0.02 1 432 102 102 VAL C C 178.23 0.2 1 433 102 102 VAL CA C 64.23 0.2 1 434 102 102 VAL CB C 32.14 0.2 1 435 102 102 VAL N N 122.86 0.2 1 436 103 103 ARG H H 8.27 0.02 1 437 103 103 ARG C C 177.99 0.2 1 438 103 103 ARG CA C 58.98 0.2 1 439 103 103 ARG CB C 31.12 0.2 1 440 103 103 ARG N N 121.45 0.2 1 441 104 104 GLU H H 7.75 0.02 1 442 104 104 GLU C C 176.03 0.2 1 443 104 104 GLU CA C 55.5 0.2 1 444 104 104 GLU CB C 28.89 0.2 1 445 104 104 GLU N N 114.31 0.2 1 446 105 105 ALA H H 7.15 0.02 1 447 105 105 ALA C C 177.01 0.2 1 448 105 105 ALA CA C 52.88 0.2 1 449 105 105 ALA CB C 18.54 0.2 1 450 105 105 ALA N N 122.78 0.2 1 451 106 106 ASP H H 8.35 0.02 1 452 106 106 ASP C C 175.39 0.2 1 453 106 106 ASP CA C 53.33 0.2 1 454 106 106 ASP CB C 39.51 0.2 1 455 106 106 ASP N N 120.71 0.2 1 456 107 107 LEU H H 7.69 0.02 1 457 107 107 LEU C C 177.69 0.2 1 458 107 107 LEU CA C 55.11 0.2 1 459 107 107 LEU CB C 43.05 0.2 1 460 107 107 LEU N N 121.45 0.2 1 461 108 108 SER H H 8.46 0.02 1 462 108 108 SER C C 173.98 0.2 1 463 108 108 SER CA C 58.3 0.2 1 464 108 108 SER CB C 65.14 0.2 1 465 108 108 SER N N 118.91 0.2 1 466 109 109 LEU H H 8.51 0.02 1 467 109 109 LEU C C 178.3 0.2 1 468 109 109 LEU CA C 59.46 0.2 1 469 109 109 LEU CB C 41.41 0.2 1 470 109 109 LEU N N 123.13 0.2 1 471 110 110 ALA H H 8.26 0.02 1 472 110 110 ALA C C 178.61 0.2 1 473 110 110 ALA CA C 55.74 0.2 1 474 110 110 ALA CB C 19.95 0.2 1 475 110 110 ALA N N 116.93 0.2 1 476 111 111 GLU H H 7.37 0.02 1 477 111 111 GLU C C 179.88 0.2 1 478 111 111 GLU CA C 59.43 0.2 1 479 111 111 GLU CB C 31.14 0.2 1 480 111 111 GLU N N 115.51 0.2 1 481 112 112 ALA H H 8.58 0.02 1 482 112 112 ALA C C 179.32 0.2 1 483 112 112 ALA CA C 55.38 0.2 1 484 112 112 ALA CB C 19.13 0.2 1 485 112 112 ALA N N 120.83 0.2 1 486 113 113 LEU H H 8.04 0.02 1 487 113 113 LEU C C 179.08 0.2 1 488 113 113 LEU CA C 58.31 0.2 1 489 113 113 LEU CB C 41.47 0.2 1 490 113 113 LEU N N 115.68 0.2 1 491 114 114 GLY H H 7.55 0.02 1 492 114 114 GLY C C 175.33 0.2 1 493 114 114 GLY CA C 47.85 0.2 1 494 114 114 GLY N N 104.14 0.2 1 495 115 115 TRP H H 7.38 0.02 1 496 115 115 TRP C C 178.6 0.2 1 497 115 115 TRP CA C 62.03 0.2 1 498 115 115 TRP CB C 27.94 0.2 1 499 115 115 TRP N N 121.4 0.2 1 500 116 116 LEU H H 8.29 0.02 1 501 116 116 LEU C C 177.99 0.2 1 502 116 116 LEU CA C 57.67 0.2 1 503 116 116 LEU CB C 42.02 0.2 1 504 116 116 LEU N N 117.2 0.2 1 505 117 117 PHE H H 8.37 0.02 1 506 117 117 PHE C C 175.3 0.2 1 507 117 117 PHE CA C 62.21 0.2 1 508 117 117 PHE CB C 38.71 0.2 1 509 117 117 PHE N N 119.39 0.2 1 510 118 118 VAL H H 6.76 0.02 1 511 118 118 VAL C C 176.04 0.2 1 512 118 118 VAL CA C 64.4 0.2 1 513 118 118 VAL CB C 29.76 0.2 1 514 118 118 VAL N N 117.66 0.2 1 515 119 119 SER H H 7.39 0.02 1 516 119 119 SER C C 179.1 0.2 1 517 119 119 SER CA C 61.12 0.2 1 518 119 119 SER CB C 63.36 0.2 1 519 119 119 SER N N 111.17 0.2 1 520 120 120 GLU H H 8.71 0.02 1 521 120 120 GLU C C 179.34 0.2 1 522 120 120 GLU CA C 58.6 0.2 1 523 120 120 GLU CB C 28.03 0.2 1 524 120 120 GLU N N 116.94 0.2 1 525 121 121 GLY H H 7.35 0.02 1 526 121 121 GLY N N 111.69 0.2 1 527 123 123 LYS H H 10.18 0.02 1 528 123 123 LYS N N 130.05 0.2 1 529 124 124 LEU H H 9.5 0.02 1 530 124 124 LEU N N 120.6 0.2 1 531 125 125 GLY N N 132.7 0.2 1 532 126 126 ALA H H 14.8 0.02 1 533 126 126 ALA CA C 59.15 0.2 1 534 126 126 ALA CB C 22.01 0.2 1 535 126 126 ALA N N 126.9 0.2 1 536 127 127 ALA H H 8.61 0.02 1 537 127 127 ALA CA C 55.32 0.2 1 538 127 127 ALA CB C 17.89 0.2 1 539 127 127 ALA N N 119.82 0.2 1 540 128 128 PHE H H 8.2 0.02 1 541 128 128 PHE N N 117.29 0.2 1 542 129 129 LEU H H 8.14 0.02 1 543 129 129 LEU C C 178.29 0.2 1 544 129 129 LEU CA C 58.25 0.2 1 545 129 129 LEU CB C 44.31 0.2 1 546 129 129 LEU N N 119.98 0.2 1 547 130 130 PHE H H 9.86 0.02 1 548 130 130 PHE C C 177.54 0.2 1 549 130 130 PHE CA C 62.7 0.2 1 550 130 130 PHE CB C 39.3 0.2 1 551 130 130 PHE N N 119.76 0.2 1 552 131 131 LYS H H 7.12 0.02 1 553 131 131 LYS C C 179.99 0.2 1 554 131 131 LYS CA C 59.08 0.2 1 555 131 131 LYS CB C 32.32 0.2 1 556 131 131 LYS N N 116.78 0.2 1 557 132 132 LYS H H 7.33 0.02 1 558 132 132 LYS C C 178.77 0.2 1 559 132 132 LYS CA C 59.83 0.2 1 560 132 132 LYS CB C 30.59 0.2 1 561 132 132 LYS N N 119.69 0.2 1 562 133 133 ALA H H 8.06 0.02 1 563 133 133 ALA C C 178.51 0.2 1 564 133 133 ALA CA C 54.38 0.2 1 565 133 133 ALA CB C 16.84 0.2 1 566 133 133 ALA N N 122.09 0.2 1 567 134 134 ALA H H 7.23 0.02 1 568 134 134 ALA C C 181.4 0.2 1 569 134 134 ALA CA C 54.84 0.2 1 570 134 134 ALA CB C 17.71 0.2 1 571 134 134 ALA N N 120.71 0.2 1 572 135 135 ALA H H 7.46 0.02 1 573 135 135 ALA C C 178.86 0.2 1 574 135 135 ALA CA C 54.44 0.2 1 575 135 135 ALA CB C 18.52 0.2 1 576 135 135 ALA N N 121.1 0.2 1 577 136 136 LEU H H 7.43 0.02 1 578 136 136 LEU C C 175.31 0.2 1 579 136 136 LEU CA C 53.7 0.2 1 580 136 136 LEU CB C 42.29 0.2 1 581 136 136 LEU N N 116.77 0.2 1 582 137 137 GLU H H 8.15 0.02 1 583 137 137 GLU C C 173.69 0.2 1 584 137 137 GLU CA C 57.49 0.2 1 585 137 137 GLU CB C 26.43 0.2 1 586 137 137 GLU N N 115.25 0.2 1 587 138 138 LEU H H 6.85 0.02 1 588 138 138 LEU C C 176.28 0.2 1 589 138 138 LEU CA C 53 0.2 1 590 138 138 LEU CB C 42.45 0.2 1 591 138 138 LEU N N 116.37 0.2 1 592 139 139 ASP H H 9.34 0.02 1 593 139 139 ASP C C 175.67 0.2 1 594 139 139 ASP CA C 54.32 0.2 1 595 139 139 ASP CB C 40.82 0.2 1 596 139 139 ASP N N 121.54 0.2 1 597 140 140 GLU H H 10.58 0.02 1 598 140 140 GLU C C 174.76 0.2 1 599 140 140 GLU CA C 58.73 0.2 1 600 140 140 GLU CB C 28.51 0.2 1 601 140 140 GLU N N 116.82 0.2 1 602 141 141 ASN H H 8.86 0.02 1 603 141 141 ASN C C 174.56 0.2 1 604 141 141 ASN CA C 53.06 0.2 1 605 141 141 ASN CB C 41.13 0.2 1 606 141 141 ASN N N 116.76 0.2 1 607 142 142 PHE H H 7.89 0.02 1 608 142 142 PHE C C 175.17 0.2 1 609 142 142 PHE CA C 58.52 0.2 1 610 142 142 PHE CB C 40.42 0.2 1 611 142 142 PHE N N 122.4 0.2 1 612 143 143 GLY H H 9.72 0.02 1 613 143 143 GLY C C 170.91 0.2 1 614 143 143 GLY CA C 47.67 0.2 1 615 143 143 GLY N N 119.09 0.2 1 616 144 144 ALA H H 7.53 0.02 1 617 144 144 ALA C C 179.12 0.2 1 618 144 144 ALA CA C 51.02 0.2 1 619 144 144 ALA CB C 18.62 0.2 1 620 144 144 ALA N N 118.84 0.2 1 621 145 145 ARG H H 11.14 0.02 1 622 145 145 ARG C C 183.78 0.2 1 623 145 145 ARG CA C 60.38 0.2 1 624 145 145 ARG CB C 31.48 0.2 1 625 145 145 ARG N N 125.24 0.2 1 626 146 146 HIS H H 11.22 0.02 1 627 146 146 HIS C C 174.75 0.2 1 628 146 146 HIS CA C 59.54 0.2 1 629 146 146 HIS CB C 27.47 0.2 1 630 146 146 HIS N N 116.09 0.2 1 631 147 147 LEU H H 7.7 0.02 1 632 147 147 LEU C C 175.87 0.2 1 633 147 147 LEU CA C 54.35 0.2 1 634 147 147 LEU CB C 44.61 0.2 1 635 147 147 LEU N N 120.35 0.2 1 636 148 148 ALA H H 7.59 0.02 1 637 148 148 ALA C C 176.88 0.2 1 638 148 148 ALA CA C 52.17 0.2 1 639 148 148 ALA CB C 20.56 0.2 1 640 148 148 ALA N N 123.05 0.2 1 641 149 149 GLU H H 8.39 0.02 1 642 149 149 GLU N N 122.34 0.2 1 643 151 151 GLU C C 179.47 0.2 1 644 151 151 GLU CA C 63.86 0.2 1 645 151 151 GLU CB C 31.39 0.2 1 646 152 152 GLY H H 9.14 0.02 1 647 152 152 GLY C C 174.78 0.2 1 648 152 152 GLY CA C 45.51 0.2 1 649 152 152 GLY N N 113.91 0.2 1 650 153 153 GLY H H 8.2 0.02 1 651 153 153 GLY C C 175.88 0.2 1 652 153 153 GLY CA C 44.29 0.2 1 653 153 153 GLY N N 108.08 0.2 1 654 154 154 ARG H H 9.61 0.02 1 655 154 154 ARG C C 178.25 0.2 1 656 154 154 ARG CA C 59.79 0.2 1 657 154 154 ARG CB C 31.59 0.2 1 658 154 154 ARG N N 126.36 0.2 1 659 155 155 ALA H H 8.82 0.02 1 660 155 155 ALA C C 180.67 0.2 1 661 155 155 ALA CA C 55.7 0.2 1 662 155 155 ALA CB C 17.67 0.2 1 663 155 155 ALA N N 122.7 0.2 1 664 156 156 GLN H H 9.14 0.02 1 665 156 156 GLN C C 179.19 0.2 1 666 156 156 GLN CA C 59.32 0.2 1 667 156 156 GLN CB C 27.51 0.2 1 668 156 156 GLN N N 119.1 0.2 1 669 157 157 GLY H H 7.88 0.02 1 670 157 157 GLY C C 177.11 0.2 1 671 157 157 GLY CA C 47.27 0.2 1 672 157 157 GLY N N 107.35 0.2 1 673 158 158 TRP H H 7.76 0.02 1 674 158 158 TRP C C 176.77 0.2 1 675 158 158 TRP CA C 58.63 0.2 1 676 158 158 TRP CB C 30.68 0.2 1 677 158 158 TRP N N 125.41 0.2 1 678 159 159 LYS H H 8.44 0.02 1 679 159 159 LYS C C 179.63 0.2 1 680 159 159 LYS CA C 59.8 0.2 1 681 159 159 LYS CB C 32.28 0.2 1 682 159 159 LYS N N 118.37 0.2 1 683 160 160 SER H H 8.26 0.02 1 684 160 160 SER C C 176.46 0.2 1 685 160 160 SER CA C 61.02 0.2 1 686 160 160 SER CB C 62.77 0.2 1 687 160 160 SER N N 112.72 0.2 1 688 161 161 PHE H H 7.28 0.02 1 689 161 161 PHE C C 176.57 0.2 1 690 161 161 PHE CA C 61.99 0.2 1 691 161 161 PHE CB C 39.33 0.2 1 692 161 161 PHE N N 124.06 0.2 1 693 162 162 VAL H H 8.36 0.02 1 694 162 162 VAL C C 176.44 0.2 1 695 162 162 VAL CA C 65.9 0.2 1 696 162 162 VAL CB C 30.72 0.2 1 697 162 162 VAL N N 117.45 0.2 1 698 163 163 ALA H H 7.64 0.02 1 699 163 163 ALA C C 181.09 0.2 1 700 163 163 ALA CA C 54.94 0.2 1 701 163 163 ALA CB C 17.89 0.2 1 702 163 163 ALA N N 119.74 0.2 1 703 164 164 ILE H H 6.8 0.02 1 704 164 164 ILE C C 178.87 0.2 1 705 164 164 ILE CA C 63.9 0.2 1 706 164 164 ILE CB C 37.21 0.2 1 707 164 164 ILE N N 116.98 0.2 1 708 165 165 LEU H H 7.96 0.02 1 709 165 165 LEU C C 178.31 0.2 1 710 165 165 LEU CA C 58.45 0.2 1 711 165 165 LEU CB C 42.2 0.2 1 712 165 165 LEU N N 121.29 0.2 1 713 166 166 ASP H H 8.68 0.02 1 714 166 166 ASP C C 178.24 0.2 1 715 166 166 ASP CA C 56.88 0.2 1 716 166 166 ASP CB C 40.06 0.2 1 717 166 166 ASP N N 116.61 0.2 1 718 167 167 GLY H H 7.5 0.02 1 719 167 167 GLY C C 174.46 0.2 1 720 167 167 GLY CA C 45.07 0.2 1 721 167 167 GLY N N 106.45 0.2 1 722 168 168 ILE H H 6.83 0.02 1 723 168 168 ILE C C 176.04 0.2 1 724 168 168 ILE CA C 62.49 0.2 1 725 168 168 ILE CB C 39.04 0.2 1 726 168 168 ILE N N 121.07 0.2 1 727 169 169 GLU H H 8.71 0.02 1 728 169 169 GLU C C 174.53 0.2 1 729 169 169 GLU CA C 55.92 0.2 1 730 169 169 GLU CB C 29.62 0.2 1 731 169 169 GLU N N 129.5 0.2 1 732 170 170 LEU H H 7.89 0.02 1 733 170 170 LEU C C 177.11 0.2 1 734 170 170 LEU CA C 53.1 0.2 1 735 170 170 LEU CB C 44.14 0.2 1 736 170 170 LEU N N 124.8 0.2 1 737 171 171 ASN H H 9.49 0.02 1 738 171 171 ASN C C 175.33 0.2 1 739 171 171 ASN CA C 51.49 0.2 1 740 171 171 ASN CB C 38.14 0.2 1 741 171 171 ASN N N 121.35 0.2 1 742 172 172 GLU H H 8.46 0.02 1 743 172 172 GLU C C 179.1 0.2 1 744 172 172 GLU CA C 60.76 0.2 1 745 172 172 GLU CB C 29.55 0.2 1 746 172 172 GLU N N 116.91 0.2 1 747 173 173 GLU H H 8.09 0.02 1 748 173 173 GLU C C 179.23 0.2 1 749 173 173 GLU CA C 59.31 0.2 1 750 173 173 GLU CB C 29 0.2 1 751 173 173 GLU N N 121 0.2 1 752 174 174 GLU H H 8.58 0.02 1 753 174 174 GLU C C 178.69 0.2 1 754 174 174 GLU CA C 59.01 0.2 1 755 174 174 GLU CB C 31.18 0.2 1 756 174 174 GLU N N 120.42 0.2 1 757 175 175 GLU H H 8.65 0.02 1 758 175 175 GLU C C 180.59 0.2 1 759 175 175 GLU CA C 59.16 0.2 1 760 175 175 GLU CB C 29.05 0.2 1 761 175 175 GLU N N 119.49 0.2 1 762 176 176 ARG H H 7.45 0.02 1 763 176 176 ARG C C 179.77 0.2 1 764 176 176 ARG CA C 59.83 0.2 1 765 176 176 ARG CB C 29.85 0.2 1 766 176 176 ARG N N 118.98 0.2 1 767 177 177 LEU H H 8.03 0.02 1 768 177 177 LEU C C 178.5 0.2 1 769 177 177 LEU CA C 57.84 0.2 1 770 177 177 LEU CB C 40.13 0.2 1 771 177 177 LEU N N 122.52 0.2 1 772 178 178 ALA H H 8.19 0.02 1 773 178 178 ALA C C 179.32 0.2 1 774 178 178 ALA CA C 55.66 0.2 1 775 178 178 ALA CB C 16.37 0.2 1 776 178 178 ALA N N 123.62 0.2 1 777 179 179 ALA H H 7.21 0.02 1 778 179 179 ALA C C 179.66 0.2 1 779 179 179 ALA CA C 54.81 0.2 1 780 179 179 ALA CB C 18.06 0.2 1 781 179 179 ALA N N 118.39 0.2 1 782 180 180 LYS H H 8.11 0.02 1 783 180 180 LYS C C 178.07 0.2 1 784 180 180 LYS CA C 59.61 0.2 1 785 180 180 LYS CB C 32.95 0.2 1 786 180 180 LYS N N 121.53 0.2 1 787 181 181 GLY H H 8.77 0.02 1 788 181 181 GLY C C 173.64 0.2 1 789 181 181 GLY CA C 47.22 0.2 1 790 181 181 GLY N N 106.57 0.2 1 791 182 182 ALA H H 7.49 0.02 1 792 182 182 ALA C C 178.95 0.2 1 793 182 182 ALA CA C 54.2 0.2 1 794 182 182 ALA CB C 17.51 0.2 1 795 182 182 ALA N N 121.05 0.2 1 796 183 183 SER H H 7.76 0.02 1 797 183 183 SER C C 177.46 0.2 1 798 183 183 SER CA C 52.87 0.2 1 799 183 183 SER CB C 62.92 0.2 1 800 183 183 SER N N 112.49 0.2 1 801 184 184 ASP H H 9.15 0.02 1 802 184 184 ASP C C 178.46 0.2 1 803 184 184 ASP CA C 56.99 0.2 1 804 184 184 ASP CB C 39.25 0.2 1 805 184 184 ASP N N 122.41 0.2 1 806 185 185 ALA H H 7.55 0.02 1 807 185 185 ALA C C 179.12 0.2 1 808 185 185 ALA CA C 54.5 0.2 1 809 185 185 ALA CB C 17.83 0.2 1 810 185 185 ALA N N 125.46 0.2 1 811 186 186 PHE H H 7.09 0.02 1 812 186 186 PHE C C 178.8 0.2 1 813 186 186 PHE CA C 63.89 0.2 1 814 186 186 PHE CB C 39.38 0.2 1 815 186 186 PHE N N 114.95 0.2 1 816 187 187 ASN H H 7.55 0.02 1 817 187 187 ASN C C 177.46 0.2 1 818 187 187 ASN CA C 55.88 0.2 1 819 187 187 ASN CB C 37.62 0.2 1 820 187 187 ASN N N 117.29 0.2 1 821 188 188 ARG H H 8.45 0.02 1 822 188 188 ARG C C 177.26 0.2 1 823 188 188 ARG CA C 57.62 0.2 1 824 188 188 ARG CB C 30.67 0.2 1 825 188 188 ARG N N 121.4 0.2 1 826 189 189 PHE H H 7.91 0.02 1 827 189 189 PHE C C 177.26 0.2 1 828 189 189 PHE CA C 62.64 0.2 1 829 189 189 PHE CB C 38.03 0.2 1 830 189 189 PHE N N 119.11 0.2 1 831 190 190 GLY H H 7.55 0.02 1 832 190 190 GLY C C 175.13 0.2 1 833 190 190 GLY CA C 47.72 0.2 1 834 190 190 GLY N N 102.64 0.2 1 835 191 191 ASP H H 7.63 0.02 1 836 191 191 ASP C C 179.72 0.2 1 837 191 191 ASP CA C 57.44 0.2 1 838 191 191 ASP CB C 40.48 0.2 1 839 191 191 ASP N N 121.63 0.2 1 840 192 192 LEU H H 8.16 0.02 1 841 192 192 LEU C C 178.07 0.2 1 842 192 192 LEU CA C 57.9 0.2 1 843 192 192 LEU CB C 41.75 0.2 1 844 192 192 LEU N N 120.87 0.2 1 845 193 193 LEU H H 8.13 0.02 1 846 193 193 LEU C C 178.56 0.2 1 847 193 193 LEU CA C 57.13 0.2 1 848 193 193 LEU CB C 42.43 0.2 1 849 193 193 LEU N N 119.22 0.2 1 850 194 194 GLU H H 7.64 0.02 1 851 194 194 GLU C C 179.69 0.2 1 852 194 194 GLU CA C 58.56 0.2 1 853 194 194 GLU CB C 28.84 0.2 1 854 194 194 GLU N N 115.14 0.2 1 855 195 195 ARG H H 7.69 0.02 1 856 195 195 ARG C C 179.88 0.2 1 857 195 195 ARG CA C 59.33 0.2 1 858 195 195 ARG CB C 30.25 0.2 1 859 195 195 ARG N N 118.1 0.2 1 860 196 196 THR H H 8.73 0.02 1 861 196 196 THR C C 177.42 0.2 1 862 196 196 THR CA C 65.1 0.2 1 863 196 196 THR CB C 67.97 0.2 1 864 196 196 THR N N 110.79 0.2 1 865 197 197 PHE H H 7.71 0.02 1 866 197 197 PHE C C 174.16 0.2 1 867 197 197 PHE CA C 60.33 0.2 1 868 197 197 PHE CB C 38.42 0.2 1 869 197 197 PHE N N 119.96 0.2 1 870 198 198 ALA H H 7.05 0.02 1 871 198 198 ALA C C 182.82 0.2 1 872 198 198 ALA N N 129.37 0.2 1 stop_ save_