data_26886 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments of ferrous THB1 ; _BMRB_accession_number 26886 _BMRB_flat_file_name bmr26886.str _Entry_type original _Submission_date 2016-09-03 _Accession_date 2016-09-03 _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 Lecomte Juliette TJ . 2 Preimesberger Matthew R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 129 "13C chemical shifts" 389 "15N chemical shifts" 129 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-02-07 update BMRB 'update entry citation' 2016-10-04 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 26885 'Ferric THB1' stop_ _Original_release_date 2016-10-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Dynamics of Lysine as a Heme Axial Ligand: NMR Analysis of the Chlamydomonas reinhardtii Hemoglobin THB1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28032976 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Preimesberger Matthew R. . 2 Majumdar Ananya . . 3 Lecomte Juliette TJ . stop_ _Journal_abbreviation Biochemistry _Journal_volume 56 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 551 _Page_last 569 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'ferrous THB1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label polypeptide $THB1 Heme $entity_HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_THB1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common THB1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 135 _Mol_residue_sequence ; AADTAPADSLYSRMGGEAAV EKAVDVFYERIVADPQLAPF FANVDMKKQRRKQVAFMTYV FGGSGAYEGRDLGASHRRLI REQGMNHHHFDLVAAHLDST LQELGVAQELKAEAMAIVAS ARPLIFGTGEAGAAN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 ALA 2 3 ALA 3 4 ASP 4 5 THR 5 6 ALA 6 7 PRO 7 8 ALA 8 9 ASP 9 10 SER 10 11 LEU 11 12 TYR 12 13 SER 13 14 ARG 14 15 MET 15 16 GLY 16 17 GLY 17 18 GLU 18 19 ALA 19 20 ALA 20 21 VAL 21 22 GLU 22 23 LYS 23 24 ALA 24 25 VAL 25 26 ASP 26 27 VAL 27 28 PHE 28 29 TYR 29 30 GLU 30 31 ARG 31 32 ILE 32 33 VAL 33 34 ALA 34 35 ASP 35 36 PRO 36 37 GLN 37 38 LEU 38 39 ALA 39 40 PRO 40 41 PHE 41 42 PHE 42 43 ALA 43 44 ASN 44 45 VAL 45 46 ASP 46 47 MET 47 48 LYS 48 49 LYS 49 50 GLN 50 51 ARG 51 52 ARG 52 53 LYS 53 54 GLN 54 55 VAL 55 56 ALA 56 57 PHE 57 58 MET 58 59 THR 59 60 TYR 60 61 VAL 61 62 PHE 62 63 GLY 63 64 GLY 64 65 SER 65 66 GLY 66 67 ALA 67 68 TYR 68 69 GLU 69 70 GLY 70 71 ARG 71 72 ASP 72 73 LEU 73 74 GLY 74 75 ALA 75 76 SER 76 77 HIS 77 78 ARG 78 79 ARG 79 80 LEU 80 81 ILE 81 82 ARG 82 83 GLU 83 84 GLN 84 85 GLY 85 86 MET 86 87 ASN 87 88 HIS 88 89 HIS 89 90 HIS 90 91 PHE 91 92 ASP 92 93 LEU 93 94 VAL 94 95 ALA 95 96 ALA 96 97 HIS 97 98 LEU 98 99 ASP 99 100 SER 100 101 THR 101 102 LEU 102 103 GLN 103 104 GLU 104 105 LEU 105 106 GLY 106 107 VAL 107 108 ALA 108 109 GLN 109 110 GLU 110 111 LEU 111 112 LYS 112 113 ALA 113 114 GLU 114 115 ALA 115 116 MET 116 117 ALA 117 118 ILE 118 119 VAL 119 120 ALA 120 121 SER 121 122 ALA 122 123 ARG 123 124 PRO 124 125 LEU 125 126 ILE 126 127 PHE 127 128 GLY 128 129 THR 129 130 GLY 130 131 GLU 131 132 ALA 132 133 GLY 133 134 ALA 134 135 ALA 135 136 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UniprotKB A8JAR4 THB1 . . . . . stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type NON-POLYMER _Name_common 'PROTOPORPHYRIN IX CONTAINING FE' _BMRB_code HEM _PDB_code HEM _Molecular_mass 616.487 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . 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_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $THB1 'green algae' 3055 Eukaryota Viridiplantae Chlamydomonas reinhardtii 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 $THB1 'recombinant technology' . Escherichia coli . pJExpress414 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 $THB1 . mM 1 2 '[U-100% 13C; U-100% 15N]' $entity_HEM . mM 1 2 'natural abundance' 'potassium phosphate' 90 mM . . 'natural abundance' 'sodium dithionite' 5 mM . . 'natural abundance' H2O 5 mM . . 'natural abundance' D2O 5 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . 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 Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.2 . M pH 6.9 . 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 DSS C 13 'methyl protons' ppm 0 internal indirect . . . 0.25144953 water H 1 protons ppm 4.76 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 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_ _Software_label $SPARKY stop_ loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 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 3 2 ALA C C 177.3 0.1 . 2 3 2 ALA CA C 52.5 0.1 . 3 3 2 ALA CB C 19.1 0.1 . 4 4 3 ASP H H 8.44 0.01 . 5 4 3 ASP C C 176.2 0.1 . 6 4 3 ASP CA C 54.4 0.1 . 7 4 3 ASP CB C 41.1 0.1 . 8 4 3 ASP N N 119.5 0.1 . 9 5 4 THR H H 8.12 0.01 . 10 5 4 THR C C 173.8 0.1 . 11 5 4 THR CA C 61.5 0.1 . 12 5 4 THR CB C 69.9 0.1 . 13 5 4 THR N N 114.4 0.1 . 14 6 5 ALA H H 8.27 0.01 . 15 6 5 ALA C C 175.3 0.1 . 16 6 5 ALA CA C 50.6 0.1 . 17 6 5 ALA CB C 18.2 0.1 . 18 6 5 ALA N N 128.0 0.1 . 19 7 6 PRO C C 177.8 0.1 . 20 7 6 PRO CA C 63.0 0.1 . 21 7 6 PRO CB C 32.5 0.1 . 22 8 7 ALA H H 8.78 0.01 . 23 8 7 ALA C C 177.6 0.1 . 24 8 7 ALA CA C 53.5 0.1 . 25 8 7 ALA CB C 18.8 0.1 . 26 8 7 ALA N N 125.6 0.1 . 27 9 8 ASP H H 8.27 0.01 . 28 9 8 ASP C C 176.2 0.1 . 29 9 8 ASP CA C 52.9 0.1 . 30 9 8 ASP CB C 40.0 0.1 . 31 9 8 ASP N N 115.6 0.1 . 32 10 9 SER H H 7.77 0.01 . 33 10 9 SER C C 175.8 0.1 . 34 10 9 SER CA C 58.3 0.1 . 35 10 9 SER CB C 64.2 0.1 . 36 10 9 SER N N 113.8 0.1 . 37 11 10 LEU H H 8.88 0.01 . 38 11 10 LEU C C 177.5 0.1 . 39 11 10 LEU CA C 56.3 0.1 . 40 11 10 LEU CB C 42.9 0.1 . 41 11 10 LEU N N 125.1 0.1 . 42 12 11 TYR H H 7.96 0.01 . 43 12 11 TYR C C 178.2 0.1 . 44 12 11 TYR CA C 60.9 0.1 . 45 12 11 TYR CB C 37.9 0.1 . 46 12 11 TYR N N 117.5 0.1 . 47 13 12 SER H H 8.64 0.01 . 48 13 12 SER C C 178.9 0.1 . 49 13 12 SER CA C 62.1 0.1 . 50 13 12 SER CB C 62.1 0.1 . 51 13 12 SER N N 114.3 0.1 . 52 14 13 ARG H H 8.32 0.01 . 53 14 13 ARG C C 177.8 0.1 . 54 14 13 ARG CA C 59.0 0.1 . 55 14 13 ARG CB C 31.3 0.1 . 56 14 13 ARG N N 123.3 0.1 . 57 15 14 MET H H 7.82 0.01 . 58 15 14 MET C C 175.4 0.1 . 59 15 14 MET CA C 55.4 0.1 . 60 15 14 MET CB C 32.9 0.1 . 61 15 14 MET N N 116.4 0.1 . 62 16 15 GLY H H 7.58 0.01 . 63 16 15 GLY C C 174.8 0.1 . 64 16 15 GLY CA C 44.4 0.1 . 65 16 15 GLY N N 103.9 0.1 . 66 17 16 GLY H H 8.39 0.01 . 67 17 16 GLY C C 173.1 0.1 . 68 17 16 GLY CA C 43.5 0.1 . 69 17 16 GLY N N 111.0 0.1 . 70 18 17 GLU H H 8.79 0.01 . 71 18 17 GLU C C 177.5 0.1 . 72 18 17 GLU CA C 60.7 0.1 . 73 18 17 GLU CB C 29.7 0.1 . 74 18 17 GLU N N 120.0 0.1 . 75 19 18 ALA H H 8.43 0.01 . 76 19 18 ALA C C 180.3 0.1 . 77 19 18 ALA CA C 54.9 0.1 . 78 19 18 ALA CB C 17.6 0.1 . 79 19 18 ALA N N 119.3 0.1 . 80 20 19 ALA H H 7.25 0.01 . 81 20 19 ALA C C 180.5 0.1 . 82 20 19 ALA CA C 54.5 0.1 . 83 20 19 ALA CB C 18.2 0.1 . 84 20 19 ALA N N 121.4 0.1 . 85 21 20 VAL H H 7.57 0.01 . 86 21 20 VAL C C 176.7 0.1 . 87 21 20 VAL CA C 66.5 0.1 . 88 21 20 VAL CB C 30.8 0.1 . 89 21 20 VAL N N 119.7 0.1 . 90 22 21 GLU H H 8.44 0.01 . 91 22 21 GLU C C 178.8 0.1 . 92 22 21 GLU CA C 59.9 0.1 . 93 22 21 GLU CB C 29.4 0.1 . 94 22 21 GLU N N 120.3 0.1 . 95 23 22 LYS H H 7.43 0.01 . 96 23 22 LYS C C 177.7 0.1 . 97 23 22 LYS CA C 58.6 0.1 . 98 23 22 LYS CB C 31.7 0.1 . 99 23 22 LYS N N 118.0 0.1 . 100 24 23 ALA H H 7.48 0.01 . 101 24 23 ALA C C 179.0 0.1 . 102 24 23 ALA CA C 55.0 0.1 . 103 24 23 ALA CB C 17.0 0.1 . 104 24 23 ALA N N 120.3 0.1 . 105 25 24 VAL H H 8.18 0.01 . 106 25 24 VAL C C 176.5 0.1 . 107 25 24 VAL CA C 67.0 0.1 . 108 25 24 VAL CB C 31.2 0.1 . 109 25 24 VAL N N 115.9 0.1 . 110 26 25 ASP H H 8.10 0.01 . 111 26 25 ASP C C 178.3 0.1 . 112 26 25 ASP CA C 57.9 0.1 . 113 26 25 ASP CB C 41.1 0.1 . 114 26 25 ASP N N 122.6 0.1 . 115 27 26 VAL H H 7.89 0.01 . 116 27 26 VAL C C 178.4 0.1 . 117 27 26 VAL CA C 66.2 0.1 . 118 27 26 VAL CB C 31.7 0.1 . 119 27 26 VAL N N 119.8 0.1 . 120 28 27 PHE H H 8.08 0.01 . 121 28 27 PHE C C 175.1 0.1 . 122 28 27 PHE CA C 58.8 0.1 . 123 28 27 PHE CB C 38.9 0.1 . 124 28 27 PHE N N 121.4 0.1 . 125 29 28 TYR H H 8.68 0.01 . 126 29 28 TYR C C 175.9 0.1 . 127 29 28 TYR CA C 61.4 0.1 . 128 29 28 TYR CB C 38.6 0.1 . 129 29 28 TYR N N 121.3 0.1 . 130 30 29 GLU H H 7.43 0.01 . 131 30 29 GLU C C 179.0 0.1 . 132 30 29 GLU CA C 58.7 0.1 . 133 30 29 GLU CB C 29.0 0.1 . 134 30 29 GLU N N 114.8 0.1 . 135 31 30 ARG H H 7.21 0.01 . 136 31 30 ARG C C 178.8 0.1 . 137 31 30 ARG CA C 58.7 0.1 . 138 31 30 ARG CB C 30.0 0.1 . 139 31 30 ARG N N 117.1 0.1 . 140 32 31 ILE H H 6.93 0.01 . 141 32 31 ILE C C 176.3 0.1 . 142 32 31 ILE CA C 64.9 0.1 . 143 32 31 ILE CB C 36.5 0.1 . 144 32 31 ILE N N 114.3 0.1 . 145 33 32 VAL H H 6.46 0.01 . 146 33 32 VAL C C 176.4 0.1 . 147 33 32 VAL CA C 63.9 0.1 . 148 33 32 VAL CB C 30.6 0.1 . 149 33 32 VAL N N 112.5 0.1 . 150 34 33 ALA H H 6.57 0.01 . 151 34 33 ALA C C 177.8 0.1 . 152 34 33 ALA CA C 51.4 0.1 . 153 34 33 ALA CB C 19.4 0.1 . 154 34 33 ALA N N 118.0 0.1 . 155 35 34 ASP H H 7.02 0.01 . 156 35 34 ASP C C 175.9 0.1 . 157 35 34 ASP CA C 52.0 0.1 . 158 35 34 ASP CB C 42.2 0.1 . 159 35 34 ASP N N 123.7 0.1 . 160 36 35 PRO C C 178.9 0.1 . 161 36 35 PRO CA C 65.0 0.1 . 162 36 35 PRO CB C 32.4 0.1 . 163 37 36 GLN H H 9.00 0.01 . 164 37 36 GLN C C 176.4 0.1 . 165 37 36 GLN CA C 58.0 0.1 . 166 37 36 GLN CB C 30.8 0.1 . 167 37 36 GLN N N 113.8 0.1 . 168 38 37 LEU H H 7.85 0.01 . 169 38 37 LEU C C 177.1 0.1 . 170 38 37 LEU CA C 54.4 0.1 . 171 38 37 LEU CB C 44.0 0.1 . 172 38 37 LEU N N 117.2 0.1 . 173 39 38 ALA H H 8.83 0.01 . 174 39 38 ALA C C 177.0 0.1 . 175 39 38 ALA CA C 57.0 0.1 . 176 39 38 ALA CB C 16.9 0.1 . 177 39 38 ALA N N 122.3 0.1 . 178 40 39 PRO C C 179.4 0.1 . 179 40 39 PRO CA C 66.1 0.1 . 180 40 39 PRO CB C 31.3 0.1 . 181 41 40 PHE H H 7.93 0.01 . 182 41 40 PHE C C 176.0 0.1 . 183 41 40 PHE CA C 59.8 0.1 . 184 41 40 PHE CB C 38.4 0.1 . 185 41 40 PHE N N 112.8 0.1 . 186 42 41 PHE H H 7.91 0.01 . 187 42 41 PHE C C 176.6 0.1 . 188 42 41 PHE CA C 59.1 0.1 . 189 42 41 PHE CB C 40.2 0.1 . 190 42 41 PHE N N 114.3 0.1 . 191 43 42 ALA H H 7.31 0.01 . 192 43 42 ALA C C 177.9 0.1 . 193 43 42 ALA CA C 55.2 0.1 . 194 43 42 ALA CB C 19.0 0.1 . 195 43 42 ALA N N 123.0 0.1 . 196 44 43 ASN H H 8.60 0.01 . 197 44 43 ASN C C 174.8 0.1 . 198 44 43 ASN CA C 52.5 0.1 . 199 44 43 ASN CB C 38.9 0.1 . 200 44 43 ASN N N 113.1 0.1 . 201 45 44 VAL H H 7.48 0.01 . 202 45 44 VAL C C 175.5 0.1 . 203 45 44 VAL CA C 63.8 0.1 . 204 45 44 VAL CB C 31.9 0.1 . 205 45 44 VAL N N 122.0 0.1 . 206 46 45 ASP H H 8.33 0.01 . 207 46 45 ASP C C 175.8 0.1 . 208 46 45 ASP CA C 53.3 0.1 . 209 46 45 ASP CB C 41.9 0.1 . 210 46 45 ASP N N 129.2 0.1 . 211 47 46 MET H H 8.58 0.01 . 212 47 46 MET C C 178.7 0.1 . 213 47 46 MET CA C 58.2 0.1 . 214 47 46 MET CB C 31.7 0.1 . 215 47 46 MET N N 118.6 0.1 . 216 48 47 LYS H H 8.13 0.01 . 217 48 47 LYS C C 179.3 0.1 . 218 48 47 LYS CA C 59.6 0.1 . 219 48 47 LYS CB C 31.7 0.1 . 220 48 47 LYS N N 119.6 0.1 . 221 49 48 LYS H H 8.11 0.01 . 222 49 48 LYS C C 177.4 0.1 . 223 49 48 LYS CA C 59.7 0.1 . 224 49 48 LYS CB C 31.9 0.1 . 225 49 48 LYS N N 122.7 0.1 . 226 50 49 GLN H H 8.50 0.01 . 227 50 49 GLN C C 177.3 0.1 . 228 50 49 GLN CA C 59.5 0.1 . 229 50 49 GLN CB C 28.0 0.1 . 230 50 49 GLN N N 119.0 0.1 . 231 51 50 ARG H H 7.53 0.01 . 232 51 50 ARG C C 178.3 0.1 . 233 51 50 ARG CA C 58.0 0.1 . 234 51 50 ARG CB C 28.8 0.1 . 235 51 50 ARG N N 117.1 0.1 . 236 52 51 ARG H H 7.62 0.01 . 237 52 51 ARG C C 180.0 0.1 . 238 52 51 ARG CA C 60.3 0.1 . 239 52 51 ARG CB C 31.1 0.1 . 240 52 51 ARG N N 117.6 0.1 . 241 53 52 LYS H H 8.48 0.01 . 242 53 52 LYS C C 176.9 0.1 . 243 53 52 LYS CA C 59.8 0.1 . 244 53 52 LYS CB C 31.2 0.1 . 245 53 52 LYS N N 122.2 0.1 . 246 54 53 GLN H H 7.83 0.01 . 247 54 53 GLN C C 178.2 0.1 . 248 54 53 GLN CA C 60.5 0.1 . 249 54 53 GLN CB C 27.7 0.1 . 250 54 53 GLN N N 117.6 0.1 . 251 55 54 VAL H H 8.09 0.01 . 252 55 54 VAL C C 179.1 0.1 . 253 55 54 VAL CA C 66.7 0.1 . 254 55 54 VAL CB C 32.1 0.1 . 255 55 54 VAL N N 119.1 0.1 . 256 56 55 ALA H H 8.40 0.01 . 257 56 55 ALA C C 179.4 0.1 . 258 56 55 ALA CA C 55.8 0.1 . 259 56 55 ALA CB C 20.8 0.1 . 260 56 55 ALA N N 125.7 0.1 . 261 57 56 PHE H H 8.80 0.01 . 262 57 56 PHE C C 177.7 0.1 . 263 57 56 PHE CA C 62.0 0.1 . 264 57 56 PHE CB C 39.6 0.1 . 265 57 56 PHE N N 117.9 0.1 . 266 58 57 MET H H 8.65 0.01 . 267 58 57 MET C C 177.9 0.1 . 268 58 57 MET CA C 60.2 0.1 . 269 58 57 MET CB C 34.1 0.1 . 270 58 57 MET N N 116.4 0.1 . 271 59 58 THR H H 8.76 0.01 . 272 59 58 THR C C 177.5 0.1 . 273 59 58 THR CA C 65.6 0.1 . 274 59 58 THR CB C 69.8 0.1 . 275 59 58 THR N N 110.1 0.1 . 276 60 59 TYR H H 9.46 0.01 . 277 60 59 TYR C C 176.2 0.1 . 278 60 59 TYR CA C 63.1 0.1 . 279 60 59 TYR CB C 39.3 0.1 . 280 60 59 TYR N N 124.0 0.1 . 281 61 60 VAL H H 8.07 0.01 . 282 61 60 VAL C C 176.0 0.1 . 283 61 60 VAL CA C 65.4 0.1 . 284 61 60 VAL CB C 31.8 0.1 . 285 61 60 VAL N N 113.2 0.1 . 286 62 61 PHE H H 7.63 0.01 . 287 62 61 PHE C C 176.6 0.1 . 288 62 61 PHE CA C 57.9 0.1 . 289 62 61 PHE CB C 39.9 0.1 . 290 62 61 PHE N N 109.8 0.1 . 291 63 62 GLY H H 7.61 0.01 . 292 63 62 GLY C C 174.4 0.1 . 293 63 62 GLY CA C 46.6 0.1 . 294 63 62 GLY N N 106.1 0.1 . 295 64 63 GLY H H 8.36 0.01 . 296 64 63 GLY C C 174.2 0.1 . 297 64 63 GLY CA C 43.4 0.1 . 298 64 63 GLY N N 107.6 0.1 . 299 65 64 SER H H 9.32 0.01 . 300 65 64 SER C C 176.0 0.1 . 301 65 64 SER CA C 60.3 0.1 . 302 65 64 SER CB C 62.9 0.1 . 303 65 64 SER N N 117.5 0.1 . 304 66 65 GLY H H 8.77 0.01 . 305 66 65 GLY C C 174.6 0.1 . 306 66 65 GLY CA C 45.6 0.1 . 307 66 65 GLY N N 113.5 0.1 . 308 67 66 ALA H H 7.59 0.01 . 309 67 66 ALA C C 177.5 0.1 . 310 67 66 ALA CA C 52.6 0.1 . 311 67 66 ALA CB C 19.9 0.1 . 312 67 66 ALA N N 121.6 0.1 . 313 68 67 TYR H H 8.11 0.01 . 314 68 67 TYR C C 175.4 0.1 . 315 68 67 TYR CA C 59.6 0.1 . 316 68 67 TYR CB C 38.7 0.1 . 317 68 67 TYR N N 118.4 0.1 . 318 69 68 GLU H H 8.53 0.01 . 319 69 68 GLU C C 174.9 0.1 . 320 69 68 GLU CA C 54.8 0.1 . 321 69 68 GLU CB C 30.8 0.1 . 322 69 68 GLU N N 129.9 0.1 . 323 70 69 GLY H H 6.30 0.01 . 324 70 69 GLY C C 172.4 0.1 . 325 70 69 GLY CA C 45.0 0.1 . 326 70 69 GLY N N 107.8 0.1 . 327 71 70 ARG H H 8.30 0.01 . 328 71 70 ARG C C 176.2 0.1 . 329 71 70 ARG CA C 56.5 0.1 . 330 71 70 ARG CB C 31.6 0.1 . 331 71 70 ARG N N 119.1 0.1 . 332 72 71 ASP H H 8.46 0.01 . 333 72 71 ASP C C 178.2 0.1 . 334 72 71 ASP CA C 55.1 0.1 . 335 72 71 ASP CB C 43.1 0.1 . 336 72 71 ASP N N 121.8 0.1 . 337 73 72 LEU H H 9.21 0.01 . 338 73 72 LEU C C 178.8 0.1 . 339 73 72 LEU CA C 57.9 0.1 . 340 73 72 LEU CB C 41.0 0.1 . 341 73 72 LEU N N 128.5 0.1 . 342 74 73 GLY H H 7.97 0.01 . 343 74 73 GLY C C 176.7 0.1 . 344 74 73 GLY CA C 46.8 0.1 . 345 74 73 GLY N N 111.3 0.1 . 346 75 74 ALA H H 8.49 0.01 . 347 75 74 ALA C C 180.3 0.1 . 348 75 74 ALA CA C 54.6 0.1 . 349 75 74 ALA CB C 18.1 0.1 . 350 75 74 ALA N N 126.1 0.1 . 351 76 75 SER H H 7.39 0.01 . 352 76 75 SER C C 172.9 0.1 . 353 76 75 SER CA C 61.4 0.1 . 354 76 75 SER CB C 62.6 0.1 . 355 76 75 SER N N 110.1 0.1 . 356 77 76 HIS H H 5.44 0.01 . 357 77 76 HIS C C 173.1 0.1 . 358 77 76 HIS CA C 56.2 0.1 . 359 77 76 HIS CB C 27.8 0.1 . 360 77 76 HIS N N 111.9 0.1 . 361 78 77 ARG H H 6.42 0.01 . 362 78 77 ARG C C 177.4 0.1 . 363 78 77 ARG CA C 59.9 0.1 . 364 78 77 ARG CB C 29.7 0.1 . 365 78 77 ARG N N 121.0 0.1 . 366 79 78 ARG H H 8.21 0.01 . 367 79 78 ARG C C 178.2 0.1 . 368 79 78 ARG CA C 59.7 0.1 . 369 79 78 ARG CB C 29.4 0.1 . 370 79 78 ARG N N 118.3 0.1 . 371 80 79 LEU H H 7.08 0.01 . 372 80 79 LEU C C 179.8 0.1 . 373 80 79 LEU CA C 57.4 0.1 . 374 80 79 LEU CB C 42.1 0.1 . 375 80 79 LEU N N 118.7 0.1 . 376 81 80 ILE H H 7.23 0.01 . 377 81 80 ILE C C 178.3 0.1 . 378 81 80 ILE CA C 64.3 0.1 . 379 81 80 ILE CB C 39.6 0.1 . 380 81 80 ILE N N 119.2 0.1 . 381 82 81 ARG H H 8.24 0.01 . 382 82 81 ARG C C 178.3 0.1 . 383 82 81 ARG CA C 58.9 0.1 . 384 82 81 ARG CB C 31.1 0.1 . 385 82 81 ARG N N 117.7 0.1 . 386 83 82 GLU H H 8.73 0.01 . 387 83 82 GLU C C 178.0 0.1 . 388 83 82 GLU CA C 56.9 0.1 . 389 83 82 GLU CB C 31.2 0.1 . 390 83 82 GLU N N 113.4 0.1 . 391 84 83 GLN H H 7.11 0.01 . 392 84 83 GLN C C 176.2 0.1 . 393 84 83 GLN CA C 55.2 0.1 . 394 84 83 GLN CB C 31.3 0.1 . 395 84 83 GLN N N 114.5 0.1 . 396 85 84 GLY H H 7.58 0.01 . 397 85 84 GLY C C 174.7 0.1 . 398 85 84 GLY CA C 46.7 0.1 . 399 85 84 GLY N N 107.3 0.1 . 400 86 85 MET H H 7.62 0.01 . 401 86 85 MET C C 176.0 0.1 . 402 86 85 MET CA C 57.3 0.1 . 403 86 85 MET CB C 32.4 0.1 . 404 86 85 MET N N 121.9 0.1 . 405 87 86 ASN H H 11.79 0.01 . 406 87 86 ASN C C 176.0 0.1 . 407 87 86 ASN CA C 52.2 0.1 . 408 87 86 ASN CB C 41.3 0.1 . 409 87 86 ASN N N 130.4 0.1 . 410 88 87 HIS H H 7.79 0.01 . 411 88 87 HIS C C 177.5 0.1 . 412 88 87 HIS CA C 60.0 0.1 . 413 88 87 HIS CB C 30.9 0.1 . 414 88 87 HIS N N 116.0 0.1 . 415 89 88 HIS H H 8.49 0.01 . 416 89 88 HIS C C 177.5 0.1 . 417 89 88 HIS CA C 58.7 0.1 . 418 89 88 HIS CB C 28.1 0.1 . 419 89 88 HIS N N 118.6 0.1 . 420 90 89 HIS H H 7.70 0.01 . 421 90 89 HIS C C 178.2 0.1 . 422 90 89 HIS CA C 62.0 0.1 . 423 90 89 HIS CB C 31.3 0.1 . 424 90 89 HIS N N 118.9 0.1 . 425 91 90 PHE H H 7.82 0.01 . 426 91 90 PHE C C 176.5 0.1 . 427 91 90 PHE CA C 62.3 0.1 . 428 91 90 PHE CB C 39.8 0.1 . 429 91 90 PHE N N 118.8 0.1 . 430 92 91 ASP H H 8.69 0.01 . 431 92 91 ASP C C 180.0 0.1 . 432 92 91 ASP CA C 57.8 0.1 . 433 92 91 ASP CB C 39.6 0.1 . 434 92 91 ASP N N 120.5 0.1 . 435 93 92 LEU H H 8.18 0.01 . 436 93 92 LEU C C 179.2 0.1 . 437 93 92 LEU CA C 57.9 0.1 . 438 93 92 LEU CB C 42.7 0.1 . 439 93 92 LEU N N 120.7 0.1 . 440 94 93 VAL H H 8.12 0.01 . 441 94 93 VAL C C 177.6 0.1 . 442 94 93 VAL CA C 68.3 0.1 . 443 94 93 VAL CB C 31.9 0.1 . 444 94 93 VAL N N 121.4 0.1 . 445 95 94 ALA H H 8.75 0.01 . 446 95 94 ALA C C 179.1 0.1 . 447 95 94 ALA CA C 56.0 0.1 . 448 95 94 ALA CB C 17.4 0.1 . 449 95 94 ALA N N 121.7 0.1 . 450 96 95 ALA H H 8.10 0.01 . 451 96 95 ALA C C 181.2 0.1 . 452 96 95 ALA CA C 54.9 0.1 . 453 96 95 ALA CB C 17.9 0.1 . 454 96 95 ALA N N 119.6 0.1 . 455 97 96 HIS H H 8.28 0.01 . 456 97 96 HIS C C 180.0 0.1 . 457 97 96 HIS CA C 60.0 0.1 . 458 97 96 HIS CB C 31.4 0.1 . 459 97 96 HIS N N 118.6 0.1 . 460 98 97 LEU H H 8.26 0.01 . 461 98 97 LEU C C 177.3 0.1 . 462 98 97 LEU CA C 58.3 0.1 . 463 98 97 LEU CB C 39.2 0.1 . 464 98 97 LEU N N 125.2 0.1 . 465 99 98 ASP H H 8.29 0.01 . 466 99 98 ASP C C 178.2 0.1 . 467 99 98 ASP CA C 58.6 0.1 . 468 99 98 ASP CB C 42.0 0.1 . 469 99 98 ASP N N 121.8 0.1 . 470 100 99 SER H H 8.50 0.01 . 471 100 99 SER C C 176.9 0.1 . 472 100 99 SER CA C 61.7 0.1 . 473 100 99 SER CB C 63.1 0.1 . 474 100 99 SER N N 111.8 0.1 . 475 101 100 THR H H 7.97 0.01 . 476 101 100 THR C C 175.7 0.1 . 477 101 100 THR CA C 68.5 0.1 . 478 101 100 THR N N 119.9 0.1 . 479 102 101 LEU H H 8.44 0.01 . 480 102 101 LEU C C 178.6 0.1 . 481 102 101 LEU CA C 58.0 0.1 . 482 102 101 LEU CB C 40.2 0.1 . 483 102 101 LEU N N 119.1 0.1 . 484 103 102 GLN H H 8.47 0.01 . 485 103 102 GLN C C 180.2 0.1 . 486 103 102 GLN CA C 59.0 0.1 . 487 103 102 GLN CB C 28.6 0.1 . 488 103 102 GLN N N 118.8 0.1 . 489 104 103 GLU H H 8.39 0.01 . 490 104 103 GLU C C 178.5 0.1 . 491 104 103 GLU CA C 59.2 0.1 . 492 104 103 GLU CB C 29.2 0.1 . 493 104 103 GLU N N 121.9 0.1 . 494 105 104 LEU H H 7.77 0.01 . 495 105 104 LEU C C 177.6 0.1 . 496 105 104 LEU CA C 55.3 0.1 . 497 105 104 LEU CB C 42.1 0.1 . 498 105 104 LEU N N 117.7 0.1 . 499 106 105 GLY H H 7.80 0.01 . 500 106 105 GLY C C 174.8 0.1 . 501 106 105 GLY CA C 46.0 0.1 . 502 106 105 GLY N N 107.8 0.1 . 503 107 106 VAL H H 7.41 0.01 . 504 107 106 VAL C C 175.3 0.1 . 505 107 106 VAL CA C 62.5 0.1 . 506 107 106 VAL CB C 31.9 0.1 . 507 107 106 VAL N N 118.7 0.1 . 508 108 107 ALA H H 8.62 0.01 . 509 108 107 ALA C C 178.7 0.1 . 510 108 107 ALA CA C 52.6 0.1 . 511 108 107 ALA CB C 19.1 0.1 . 512 108 107 ALA N N 128.6 0.1 . 513 109 108 GLN H H 8.88 0.01 . 514 109 108 GLN C C 178.2 0.1 . 515 109 108 GLN CA C 59.7 0.1 . 516 109 108 GLN CB C 28.2 0.1 . 517 109 108 GLN N N 122.3 0.1 . 518 110 109 GLU H H 9.60 0.01 . 519 110 109 GLU C C 178.6 0.1 . 520 110 109 GLU CA C 59.8 0.1 . 521 110 109 GLU CB C 28.2 0.1 . 522 110 109 GLU N N 118.0 0.1 . 523 111 110 LEU H H 6.91 0.01 . 524 111 110 LEU C C 177.9 0.1 . 525 111 110 LEU CA C 57.1 0.1 . 526 111 110 LEU CB C 41.5 0.1 . 527 111 110 LEU N N 121.4 0.1 . 528 112 111 LYS H H 8.28 0.01 . 529 112 111 LYS C C 177.7 0.1 . 530 112 111 LYS CA C 60.2 0.1 . 531 112 111 LYS CB C 31.7 0.1 . 532 112 111 LYS N N 120.3 0.1 . 533 113 112 ALA H H 8.29 0.01 . 534 113 112 ALA C C 180.9 0.1 . 535 113 112 ALA CA C 55.0 0.1 . 536 113 112 ALA CB C 17.8 0.1 . 537 113 112 ALA N N 118.9 0.1 . 538 114 113 GLU H H 7.52 0.01 . 539 114 113 GLU C C 179.0 0.1 . 540 114 113 GLU CA C 59.8 0.1 . 541 114 113 GLU CB C 29.9 0.1 . 542 114 113 GLU N N 120.1 0.1 . 543 115 114 ALA H H 8.05 0.01 . 544 115 114 ALA C C 179.4 0.1 . 545 115 114 ALA CA C 55.1 0.1 . 546 115 114 ALA CB C 17.5 0.1 . 547 115 114 ALA N N 121.2 0.1 . 548 116 115 MET H H 8.55 0.01 . 549 116 115 MET C C 180.4 0.1 . 550 116 115 MET CA C 55.4 0.1 . 551 116 115 MET CB C 28.5 0.1 . 552 116 115 MET N N 113.9 0.1 . 553 117 116 ALA H H 8.08 0.01 . 554 117 116 ALA C C 180.8 0.1 . 555 117 116 ALA CA C 54.9 0.1 . 556 117 116 ALA CB C 17.6 0.1 . 557 117 116 ALA N N 125.4 0.1 . 558 118 117 ILE H H 7.79 0.01 . 559 118 117 ILE C C 181.3 0.1 . 560 118 117 ILE CA C 64.9 0.1 . 561 118 117 ILE CB C 37.3 0.1 . 562 118 117 ILE N N 121.5 0.1 . 563 119 118 VAL H H 8.66 0.01 . 564 119 118 VAL C C 177.8 0.1 . 565 119 118 VAL CA C 68.0 0.1 . 566 119 118 VAL CB C 31.6 0.1 . 567 119 118 VAL N N 123.7 0.1 . 568 120 119 ALA H H 8.10 0.01 . 569 120 119 ALA C C 181.4 0.1 . 570 120 119 ALA CA C 55.7 0.1 . 571 120 119 ALA CB C 18.1 0.1 . 572 120 119 ALA N N 120.0 0.1 . 573 121 120 SER H H 7.89 0.01 . 574 121 120 SER C C 174.3 0.1 . 575 121 120 SER CA C 61.1 0.1 . 576 121 120 SER CB C 63.9 0.1 . 577 121 120 SER N N 114.1 0.1 . 578 122 121 ALA H H 8.25 0.01 . 579 122 121 ALA C C 178.7 0.1 . 580 122 121 ALA CA C 53.5 0.1 . 581 122 121 ALA CB C 19.7 0.1 . 582 122 121 ALA N N 122.9 0.1 . 583 123 122 ARG H H 7.35 0.01 . 584 123 122 ARG C C 174.2 0.1 . 585 123 122 ARG CA C 62.2 0.1 . 586 123 122 ARG CB C 28.3 0.1 . 587 123 122 ARG N N 119.2 0.1 . 588 124 123 PRO C C 178.8 0.1 . 589 124 123 PRO CA C 64.8 0.1 . 590 124 123 PRO CB C 30.7 0.1 . 591 125 124 LEU H H 6.54 0.01 . 592 125 124 LEU C C 178.1 0.1 . 593 125 124 LEU CA C 56.3 0.1 . 594 125 124 LEU CB C 41.3 0.1 . 595 125 124 LEU N N 117.1 0.1 . 596 126 125 ILE H H 7.26 0.01 . 597 126 125 ILE C C 175.2 0.1 . 598 126 125 ILE CA C 64.0 0.1 . 599 126 125 ILE CB C 37.9 0.1 . 600 126 125 ILE N N 117.8 0.1 . 601 127 126 PHE H H 7.34 0.01 . 602 127 126 PHE C C 176.9 0.1 . 603 127 126 PHE CA C 59.1 0.1 . 604 127 126 PHE CB C 39.6 0.1 . 605 127 126 PHE N N 110.9 0.1 . 606 128 127 GLY H H 7.27 0.01 . 607 128 127 GLY C C 174.0 0.1 . 608 128 127 GLY CA C 45.4 0.1 . 609 128 127 GLY N N 108.8 0.1 . 610 129 128 THR H H 8.07 0.01 . 611 129 128 THR C C 175.3 0.1 . 612 129 128 THR CA C 61.6 0.1 . 613 129 128 THR CB C 69.6 0.1 . 614 129 128 THR N N 110.9 0.1 . 615 130 129 GLY H H 8.35 0.01 . 616 130 129 GLY C C 174.1 0.1 . 617 130 129 GLY CA C 45.2 0.1 . 618 130 129 GLY N N 110.7 0.1 . 619 131 130 GLU H H 8.25 0.01 . 620 131 130 GLU C C 176.4 0.1 . 621 131 130 GLU CA C 56.3 0.1 . 622 131 130 GLU CB C 30.2 0.1 . 623 131 130 GLU N N 120.8 0.1 . 624 132 131 ALA H H 8.37 0.01 . 625 132 131 ALA C C 178.2 0.1 . 626 132 131 ALA CA C 52.7 0.1 . 627 132 131 ALA CB C 18.9 0.1 . 628 132 131 ALA N N 125.1 0.1 . 629 133 132 GLY H H 8.26 0.01 . 630 133 132 GLY C C 173.7 0.1 . 631 133 132 GLY CA C 45.1 0.1 . 632 133 132 GLY N N 108.1 0.1 . 633 134 133 ALA H H 7.96 0.01 . 634 134 133 ALA C C 177.2 0.1 . 635 134 133 ALA CA C 52.2 0.1 . 636 134 133 ALA CB C 19.4 0.1 . 637 134 133 ALA N N 123.5 0.1 . 638 135 134 ALA H H 8.24 0.01 . 639 135 134 ALA C C 176.5 0.1 . 640 135 134 ALA CA C 52.3 0.1 . 641 135 134 ALA CB C 19.2 0.1 . 642 135 134 ALA N N 123.7 0.1 . 643 136 135 ASN H H 7.87 0.01 . 644 136 135 ASN C C 179.4 0.1 . 645 136 135 ASN CA C 54.6 0.1 . 646 136 135 ASN CB C 40.4 0.1 . 647 136 135 ASN N N 123.2 0.1 . stop_ save_