data_25285 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for Scapharca dimeric hemoglobin (HbI) bound to CO ; _BMRB_accession_number 25285 _BMRB_flat_file_name bmr25285.str _Entry_type original _Submission_date 2014-10-15 _Accession_date 2014-10-15 _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 Laine Jennifer M. . 2 Massi Francesca . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 141 "13C chemical shifts" 419 "15N chemical shifts" 141 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-07-11 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25286 'HbI homodymer (in the unliganded state)' stop_ _Original_release_date 2014-10-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Insight into the allosteric mechanism of Scapharca dimeric hemoglobin. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25356908 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Laine Jennifer M. . 2 Amat Miguel . . 3 Morgan Brittany R. . 4 Royer William E. Jr 5 Massi Francesca . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 53 _Journal_issue 46 _Journal_ISSN 1520-4995 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7199 _Page_last 7210 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HbI homodimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HbI, chain 1' $Scapharca_dimeric_hemoglobin_(HbI) 'HbI, chain 2' $Scapharca_dimeric_hemoglobin_(HbI) HEM $entity_HEM CO $entity_CMO stop_ _System_molecular_weight 15946.3 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'HbI, chain 1' 1 'HbI, chain 2' 1 HEM 1 CO stop_ loop_ _Biological_function 'Oxygen transport' stop_ _Database_query_date . _Details 'symmetric dimer' save_ ######################## # Monomeric polymers # ######################## save_Scapharca_dimeric_hemoglobin_(HbI) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Scapharca_dimeric_hemoglobin_(HbI) _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'OXYGEN TRANSPORT' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 146 _Mol_residue_sequence ; PSVYDAAAQLTADVKKDLRD SWKVIGSDKKGNGVALMTTL FADNQETIGYFKRLGDVSQG MANDKLRGHSITLMYALQNF LDQLDNPDDLVCVVEKFAVN HITRKISAAEFGKINGPIKK VLASKNFGDKYANAWAKLVA VVQAAL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 PRO 2 2 SER 3 3 VAL 4 4 TYR 5 5 ASP 6 6 ALA 7 7 ALA 8 8 ALA 9 9 GLN 10 10 LEU 11 11 THR 12 12 ALA 13 13 ASP 14 14 VAL 15 15 LYS 16 16 LYS 17 17 ASP 18 18 LEU 19 19 ARG 20 20 ASP 21 21 SER 22 22 TRP 23 23 LYS 24 24 VAL 25 25 ILE 26 26 GLY 27 27 SER 28 28 ASP 29 29 LYS 30 30 LYS 31 31 GLY 32 32 ASN 33 33 GLY 34 34 VAL 35 35 ALA 36 36 LEU 37 37 MET 38 38 THR 39 39 THR 40 40 LEU 41 41 PHE 42 42 ALA 43 43 ASP 44 44 ASN 45 45 GLN 46 46 GLU 47 47 THR 48 48 ILE 49 49 GLY 50 50 TYR 51 51 PHE 52 52 LYS 53 53 ARG 54 54 LEU 55 55 GLY 56 56 ASP 57 57 VAL 58 58 SER 59 59 GLN 60 60 GLY 61 61 MET 62 62 ALA 63 63 ASN 64 64 ASP 65 65 LYS 66 66 LEU 67 67 ARG 68 68 GLY 69 69 HIS 70 70 SER 71 71 ILE 72 72 THR 73 73 LEU 74 74 MET 75 75 TYR 76 76 ALA 77 77 LEU 78 78 GLN 79 79 ASN 80 80 PHE 81 81 LEU 82 82 ASP 83 83 GLN 84 84 LEU 85 85 ASP 86 86 ASN 87 87 PRO 88 88 ASP 89 89 ASP 90 90 LEU 91 91 VAL 92 92 CYS 93 93 VAL 94 94 VAL 95 95 GLU 96 96 LYS 97 97 PHE 98 98 ALA 99 99 VAL 100 100 ASN 101 101 HIS 102 102 ILE 103 103 THR 104 104 ARG 105 105 LYS 106 106 ILE 107 107 SER 108 108 ALA 109 109 ALA 110 110 GLU 111 111 PHE 112 112 GLY 113 113 LYS 114 114 ILE 115 115 ASN 116 116 GLY 117 117 PRO 118 118 ILE 119 119 LYS 120 120 LYS 121 121 VAL 122 122 LEU 123 123 ALA 124 124 SER 125 125 LYS 126 126 ASN 127 127 PHE 128 128 GLY 129 129 ASP 130 130 LYS 131 131 TYR 132 132 ALA 133 133 ASN 134 134 ALA 135 135 TRP 136 136 ALA 137 137 LYS 138 138 LEU 139 139 VAL 140 140 ALA 141 141 VAL 142 142 VAL 143 143 GLN 144 144 ALA 145 145 ALA 146 146 LEU 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 PDB 3SDH HbI . . . . . stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type "non-polymer (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_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_CMO _Saveframe_category ligand _Mol_type NON-POLYMER _Name_common 'CARBON MONOXIDE' _BMRB_code CMO _PDB_code CMO _Molecular_mass 28.010 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . -1 . ? O O O . 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 TRIP C O ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Scapharca_dimeric_hemoglobin_(HbI) 'ark clam' 6561 Eukaryota Metazoa SCAPHARCA INAEQUIVALVIS 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 _Details $Scapharca_dimeric_hemoglobin_(HbI) 'recombinant technology' . Escherichia coli W3110lacIq-L8 pCS26 'Protein Engineering vol. 8 no.6 pp593-599, 1995' 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 $Scapharca_dimeric_hemoglobin_(HbI) 0.4 mM '[U-13C; U-15N; U-2H]' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _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' 0.15 . M pH 7 . pH pressure ambient . 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 water C 13 protons ppm 4.754 internal indirect . . . 0.25144952 water H 1 protons ppm 4.754 internal direct . . . 1 water N 15 protons ppm 4.754 internal indirect . . . 0.10132905 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N TROSY' '3D HNCO' '3D HNCA' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'HbI, chain 1' _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 2 2 SER C C 175.676 0.2 . 2 2 2 SER CA C 57.174 0.2 . 3 2 2 SER CB C 64.374 0.2 . 4 3 3 VAL H H 8.763 0.02 . 5 3 3 VAL C C 177.222 0.2 . 6 3 3 VAL CA C 65.409 0.2 . 7 3 3 VAL CB C 30.908 0.2 . 8 3 3 VAL N N 124.888 0.1 . 9 4 4 TYR H H 7.512 0.02 . 10 4 4 TYR C C 178.811 0.2 . 11 4 4 TYR CA C 62.219 0.2 . 12 4 4 TYR CB C 37.770 0.2 . 13 4 4 TYR N N 119.296 0.1 . 14 5 5 ASP H H 7.774 0.02 . 15 5 5 ASP C C 178.850 0.2 . 16 5 5 ASP CA C 56.914 0.2 . 17 5 5 ASP CB C 39.759 0.2 . 18 5 5 ASP N N 121.227 0.1 . 19 6 6 ALA H H 7.724 0.02 . 20 6 6 ALA C C 181.399 0.2 . 21 6 6 ALA CA C 54.501 0.2 . 22 6 6 ALA CB C 17.776 0.2 . 23 6 6 ALA N N 122.587 0.1 . 24 7 7 ALA H H 8.375 0.02 . 25 7 7 ALA C C 179.574 0.2 . 26 7 7 ALA CA C 54.322 0.2 . 27 7 7 ALA CB C 16.626 0.2 . 28 7 7 ALA N N 123.147 0.1 . 29 8 8 ALA H H 7.752 0.02 . 30 8 8 ALA C C 178.731 0.2 . 31 8 8 ALA CA C 53.515 0.2 . 32 8 8 ALA CB C 17.264 0.2 . 33 8 8 ALA N N 121.452 0.1 . 34 9 9 GLN H H 7.117 0.02 . 35 9 9 GLN C C 176.447 0.2 . 36 9 9 GLN CA C 55.382 0.2 . 37 9 9 GLN CB C 27.561 0.2 . 38 9 9 GLN N N 114.126 0.1 . 39 10 10 LEU H H 7.348 0.02 . 40 10 10 LEU C C 174.649 0.2 . 41 10 10 LEU CA C 52.872 0.2 . 42 10 10 LEU CB C 37.720 0.2 . 43 10 10 LEU N N 120.680 0.1 . 44 11 11 THR H H 6.934 0.02 . 45 11 11 THR C C 174.896 0.2 . 46 11 11 THR CA C 60.672 0.2 . 47 11 11 THR CB C 69.993 0.2 . 48 11 11 THR N N 114.129 0.1 . 49 12 12 ALA H H 8.923 0.02 . 50 12 12 ALA C C 180.411 0.2 . 51 12 12 ALA CA C 55.915 0.2 . 52 12 12 ALA CB C 18.003 0.2 . 53 12 12 ALA N N 122.674 0.1 . 54 13 13 ASP H H 8.435 0.02 . 55 13 13 ASP C C 177.086 0.2 . 56 13 13 ASP CA C 56.828 0.2 . 57 13 13 ASP CB C 40.273 0.2 . 58 13 13 ASP N N 117.197 0.1 . 59 14 14 VAL H H 6.910 0.02 . 60 14 14 VAL C C 178.228 0.2 . 61 14 14 VAL CA C 65.458 0.2 . 62 14 14 VAL CB C 31.626 0.2 . 63 14 14 VAL N N 121.739 0.1 . 64 15 15 LYS H H 8.513 0.02 . 65 15 15 LYS C C 177.982 0.2 . 66 15 15 LYS CA C 60.483 0.2 . 67 15 15 LYS CB C 31.714 0.2 . 68 15 15 LYS N N 117.812 0.1 . 69 16 16 LYS H H 7.666 0.02 . 70 16 16 LYS C C 177.854 0.2 . 71 16 16 LYS CA C 59.213 0.2 . 72 16 16 LYS CB C 31.495 0.2 . 73 16 16 LYS N N 119.883 0.1 . 74 17 17 ASP H H 7.699 0.02 . 75 17 17 ASP C C 181.260 0.2 . 76 17 17 ASP CA C 57.783 0.2 . 77 17 17 ASP CB C 39.083 0.2 . 78 17 17 ASP N N 120.960 0.1 . 79 18 18 LEU H H 8.548 0.02 . 80 18 18 LEU C C 178.143 0.2 . 81 18 18 LEU CA C 57.931 0.2 . 82 18 18 LEU CB C 40.858 0.2 . 83 18 18 LEU N N 124.300 0.1 . 84 19 19 ARG H H 8.365 0.02 . 85 19 19 ARG C C 180.246 0.2 . 86 19 19 ARG CA C 60.685 0.2 . 87 19 19 ARG CB C 29.704 0.2 . 88 19 19 ARG N N 119.359 0.1 . 89 20 20 ASP H H 9.492 0.02 . 90 20 20 ASP C C 179.041 0.2 . 91 20 20 ASP CA C 57.362 0.2 . 92 20 20 ASP CB C 39.794 0.2 . 93 20 20 ASP N N 121.395 0.1 . 94 21 21 SER H H 7.751 0.02 . 95 21 21 SER C C 177.782 0.2 . 96 21 21 SER CA C 59.967 0.2 . 97 21 21 SER CB C 62.420 0.2 . 98 21 21 SER N N 112.037 0.1 . 99 22 22 TRP H H 9.174 0.02 . 100 22 22 TRP C C 177.793 0.2 . 101 22 22 TRP CA C 59.266 0.2 . 102 22 22 TRP CB C 30.287 0.2 . 103 22 22 TRP N N 127.628 0.1 . 104 23 23 LYS H H 7.923 0.02 . 105 23 23 LYS C C 177.518 0.2 . 106 23 23 LYS CA C 59.248 0.2 . 107 23 23 LYS CB C 31.827 0.2 . 108 23 23 LYS N N 119.568 0.1 . 109 24 24 VAL H H 6.570 0.02 . 110 24 24 VAL C C 179.468 0.2 . 111 24 24 VAL CA C 64.313 0.2 . 112 24 24 VAL CB C 32.554 0.2 . 113 24 24 VAL N N 114.652 0.1 . 114 25 25 ILE H H 8.292 0.02 . 115 25 25 ILE C C 177.214 0.2 . 116 25 25 ILE CA C 62.360 0.2 . 117 25 25 ILE CB C 36.717 0.2 . 118 25 25 ILE N N 118.691 0.1 . 119 26 26 GLY H H 8.264 0.02 . 120 26 26 GLY C C 173.260 0.2 . 121 26 26 GLY CA C 43.230 0.2 . 122 26 26 GLY N N 108.105 0.1 . 123 27 27 SER H H 6.611 0.02 . 124 27 27 SER C C 173.724 0.2 . 125 27 27 SER CA C 59.248 0.2 . 126 27 27 SER CB C 63.121 0.2 . 127 27 27 SER N N 113.334 0.1 . 128 28 28 ASP H H 6.349 0.02 . 129 28 28 ASP C C 175.408 0.2 . 130 28 28 ASP CA C 51.740 0.2 . 131 28 28 ASP CB C 39.147 0.2 . 132 28 28 ASP N N 120.712 0.1 . 133 29 29 LYS H H 8.674 0.02 . 134 29 29 LYS C C 178.428 0.2 . 135 29 29 LYS CA C 60.684 0.2 . 136 29 29 LYS CB C 31.746 0.2 . 137 29 29 LYS N N 124.213 0.1 . 138 30 30 LYS H H 8.438 0.02 . 139 30 30 LYS C C 176.994 0.2 . 140 30 30 LYS CA C 59.781 0.2 . 141 30 30 LYS CB C 31.417 0.2 . 142 30 30 LYS N N 118.230 0.1 . 143 31 31 GLY H H 8.057 0.02 . 144 31 31 GLY C C 177.524 0.2 . 145 31 31 GLY CA C 47.147 0.2 . 146 31 31 GLY N N 106.908 0.1 . 147 32 32 ASN H H 8.010 0.02 . 148 32 32 ASN C C 176.857 0.2 . 149 32 32 ASN CA C 55.071 0.2 . 150 32 32 ASN CB C 37.062 0.2 . 151 32 32 ASN N N 117.890 0.1 . 152 33 33 GLY H H 7.926 0.02 . 153 33 33 GLY C C 175.312 0.2 . 154 33 33 GLY CA C 46.981 0.2 . 155 33 33 GLY N N 111.052 0.1 . 156 34 34 VAL H H 7.637 0.02 . 157 34 34 VAL C C 178.500 0.2 . 158 34 34 VAL CA C 65.884 0.2 . 159 34 34 VAL CB C 30.540 0.2 . 160 34 34 VAL N N 121.788 0.1 . 161 35 35 ALA H H 7.469 0.02 . 162 35 35 ALA C C 180.349 0.2 . 163 35 35 ALA CA C 54.872 0.2 . 164 35 35 ALA CB C 17.562 0.2 . 165 35 35 ALA N N 123.308 0.1 . 166 36 36 LEU H H 7.866 0.02 . 167 36 36 LEU C C 177.766 0.2 . 168 36 36 LEU CA C 58.100 0.2 . 169 36 36 LEU CB C 41.359 0.2 . 170 36 36 LEU N N 121.369 0.1 . 171 37 37 MET H H 6.836 0.02 . 172 37 37 MET C C 176.424 0.2 . 173 37 37 MET CA C 54.567 0.2 . 174 37 37 MET CB C 30.134 0.2 . 175 37 37 MET N N 114.482 0.1 . 176 38 38 THR H H 8.496 0.02 . 177 38 38 THR C C 177.784 0.2 . 178 38 38 THR CA C 65.399 0.2 . 179 38 38 THR CB C 68.053 0.2 . 180 38 38 THR N N 110.138 0.1 . 181 39 39 THR H H 7.593 0.02 . 182 39 39 THR C C 174.800 0.2 . 183 39 39 THR CA C 66.695 0.2 . 184 39 39 THR CB C 67.526 0.2 . 185 39 39 THR N N 120.361 0.1 . 186 40 40 LEU H H 7.349 0.02 . 187 40 40 LEU C C 177.986 0.2 . 188 40 40 LEU CA C 58.678 0.2 . 189 40 40 LEU CB C 39.548 0.2 . 190 40 40 LEU N N 124.696 0.1 . 191 41 41 PHE H H 7.355 0.02 . 192 41 41 PHE C C 177.411 0.2 . 193 41 41 PHE CA C 56.539 0.2 . 194 41 41 PHE CB C 36.804 0.2 . 195 41 41 PHE N N 115.207 0.1 . 196 42 42 ALA H H 7.618 0.02 . 197 42 42 ALA C C 179.821 0.2 . 198 42 42 ALA CA C 54.075 0.2 . 199 42 42 ALA CB C 18.303 0.2 . 200 42 42 ALA N N 120.002 0.1 . 201 43 43 ASP H H 8.081 0.02 . 202 43 43 ASP C C 176.871 0.2 . 203 43 43 ASP CA C 55.301 0.2 . 204 43 43 ASP CB C 40.127 0.2 . 205 43 43 ASP N N 117.373 0.1 . 206 44 44 ASN H H 8.155 0.02 . 207 44 44 ASN C C 175.705 0.2 . 208 44 44 ASN CA C 52.706 0.2 . 209 44 44 ASN CB C 39.149 0.2 . 210 44 44 ASN N N 121.716 0.1 . 211 45 45 GLN H H 9.086 0.02 . 212 45 45 GLN C C 177.976 0.2 . 213 45 45 GLN CA C 59.041 0.2 . 214 45 45 GLN CB C 27.919 0.2 . 215 45 45 GLN N N 124.746 0.1 . 216 46 46 GLU H H 10.263 0.02 . 217 46 46 GLU C C 177.744 0.2 . 218 46 46 GLU CA C 58.385 0.2 . 219 46 46 GLU CB C 26.549 0.2 . 220 46 46 GLU N N 122.321 0.1 . 221 47 47 THR H H 8.411 0.02 . 222 47 47 THR C C 176.802 0.2 . 223 47 47 THR CA C 63.626 0.2 . 224 47 47 THR CB C 70.634 0.2 . 225 47 47 THR N N 113.276 0.1 . 226 48 48 ILE H H 7.440 0.02 . 227 48 48 ILE C C 179.567 0.2 . 228 48 48 ILE CA C 65.767 0.2 . 229 48 48 ILE CB C 37.588 0.2 . 230 48 48 ILE N N 122.680 0.1 . 231 49 49 GLY H H 8.020 0.02 . 232 49 49 GLY C C 176.403 0.2 . 233 49 49 GLY CA C 46.483 0.2 . 234 49 49 GLY N N 106.506 0.1 . 235 50 50 TYR H H 7.609 0.02 . 236 50 50 TYR C C 177.954 0.2 . 237 50 50 TYR CA C 58.254 0.2 . 238 50 50 TYR CB C 37.939 0.2 . 239 50 50 TYR N N 118.527 0.1 . 240 51 51 PHE H H 8.150 0.02 . 241 51 51 PHE C C 176.100 0.2 . 242 51 51 PHE CA C 58.145 0.2 . 243 51 51 PHE CB C 37.407 0.2 . 244 51 51 PHE N N 117.625 0.1 . 245 52 52 LYS H H 7.128 0.02 . 246 52 52 LYS C C 178.417 0.2 . 247 52 52 LYS CA C 59.113 0.2 . 248 52 52 LYS CB C 31.792 0.2 . 249 52 52 LYS N N 120.951 0.1 . 250 53 53 ARG H H 8.800 0.02 . 251 53 53 ARG C C 177.518 0.2 . 252 53 53 ARG CA C 58.405 0.2 . 253 53 53 ARG CB C 30.707 0.2 . 254 53 53 ARG N N 121.055 0.1 . 255 54 54 LEU H H 7.768 0.02 . 256 54 54 LEU C C 176.341 0.2 . 257 54 54 LEU CA C 54.172 0.2 . 258 54 54 LEU CB C 39.584 0.2 . 259 54 54 LEU N N 110.358 0.1 . 260 55 55 GLY H H 7.295 0.02 . 261 55 55 GLY C C 173.780 0.2 . 262 55 55 GLY CA C 45.119 0.2 . 263 55 55 GLY N N 106.486 0.1 . 264 56 56 ASP H H 7.770 0.02 . 265 56 56 ASP C C 178.681 0.2 . 266 56 56 ASP CA C 52.970 0.2 . 267 56 56 ASP CB C 39.022 0.2 . 268 56 56 ASP N N 123.424 0.1 . 269 57 57 VAL H H 7.767 0.02 . 270 57 57 VAL C C 177.328 0.2 . 271 57 57 VAL CA C 63.164 0.2 . 272 57 57 VAL CB C 29.828 0.2 . 273 57 57 VAL N N 123.422 0.1 . 274 58 58 SER H H 8.107 0.02 . 275 58 58 SER C C 175.446 0.2 . 276 58 58 SER CA C 60.677 0.2 . 277 58 58 SER CB C 62.232 0.2 . 278 58 58 SER N N 119.805 0.1 . 279 59 59 GLN H H 6.924 0.02 . 280 59 59 GLN C C 177.629 0.2 . 281 59 59 GLN CA C 55.524 0.2 . 282 59 59 GLN CB C 29.354 0.2 . 283 59 59 GLN N N 118.725 0.1 . 284 60 60 GLY H H 7.247 0.02 . 285 60 60 GLY C C 173.996 0.2 . 286 60 60 GLY CA C 46.149 0.2 . 287 60 60 GLY N N 106.393 0.1 . 288 61 61 MET H H 8.727 0.02 . 289 61 61 MET C C 174.971 0.2 . 290 61 61 MET CA C 56.279 0.2 . 291 61 61 MET CB C 31.444 0.2 . 292 61 61 MET N N 124.808 0.1 . 293 62 62 ALA H H 7.218 0.02 . 294 62 62 ALA C C 177.154 0.2 . 295 62 62 ALA CA C 52.338 0.2 . 296 62 62 ALA CB C 18.351 0.2 . 297 62 62 ALA N N 116.648 0.1 . 298 63 63 ASN H H 7.642 0.02 . 299 63 63 ASN C C 174.524 0.2 . 300 63 63 ASN CA C 51.644 0.2 . 301 63 63 ASN CB C 37.905 0.2 . 302 63 63 ASN N N 118.088 0.1 . 303 64 64 ASP H H 8.483 0.02 . 304 64 64 ASP C C 177.794 0.2 . 305 64 64 ASP CA C 57.341 0.2 . 306 64 64 ASP CB C 40.331 0.2 . 307 64 64 ASP N N 127.002 0.1 . 308 65 65 LYS H H 7.828 0.02 . 309 65 65 LYS C C 181.124 0.2 . 310 65 65 LYS CA C 58.794 0.2 . 311 65 65 LYS CB C 31.897 0.2 . 312 65 65 LYS N N 119.643 0.1 . 313 66 66 LEU H H 7.907 0.02 . 314 66 66 LEU C C 179.639 0.2 . 315 66 66 LEU CA C 56.928 0.2 . 316 66 66 LEU CB C 39.640 0.2 . 317 66 66 LEU N N 123.660 0.1 . 318 67 67 ARG H H 9.145 0.02 . 319 67 67 ARG C C 177.654 0.2 . 320 67 67 ARG CA C 61.261 0.2 . 321 67 67 ARG CB C 30.805 0.2 . 322 67 67 ARG N N 126.861 0.1 . 323 68 68 GLY H H 8.624 0.02 . 324 68 68 GLY C C 176.693 0.2 . 325 68 68 GLY CA C 47.731 0.2 . 326 68 68 GLY N N 106.966 0.1 . 327 69 69 HIS H H 7.898 0.02 . 328 69 69 HIS C C 176.209 0.2 . 329 69 69 HIS CA C 59.890 0.2 . 330 69 69 HIS CB C 31.063 0.2 . 331 69 69 HIS N N 123.184 0.1 . 332 70 70 SER H H 8.069 0.02 . 333 70 70 SER C C 175.085 0.2 . 334 70 70 SER CA C 62.825 0.2 . 335 70 70 SER CB C 69.517 0.2 . 336 70 70 SER N N 117.184 0.1 . 337 71 71 ILE H H 8.073 0.02 . 338 71 71 ILE C C 177.984 0.2 . 339 71 71 ILE CA C 66.069 0.2 . 340 71 71 ILE CB C 38.641 0.2 . 341 71 71 ILE N N 120.476 0.1 . 342 72 72 THR H H 7.034 0.02 . 343 72 72 THR C C 177.406 0.2 . 344 72 72 THR CA C 68.345 0.2 . 345 72 72 THR N N 115.516 0.1 . 346 73 73 LEU H H 8.059 0.02 . 347 73 73 LEU C C 178.917 0.2 . 348 73 73 LEU CA C 59.649 0.2 . 349 73 73 LEU CB C 40.475 0.2 . 350 73 73 LEU N N 126.838 0.1 . 351 74 74 MET H H 7.225 0.02 . 352 74 74 MET C C 179.760 0.2 . 353 74 74 MET CA C 56.473 0.2 . 354 74 74 MET CB C 29.853 0.2 . 355 74 74 MET N N 117.366 0.1 . 356 75 75 TYR H H 8.022 0.02 . 357 75 75 TYR C C 179.250 0.2 . 358 75 75 TYR CA C 63.097 0.2 . 359 75 75 TYR CB C 39.668 0.2 . 360 75 75 TYR N N 119.089 0.1 . 361 76 76 ALA H H 7.970 0.02 . 362 76 76 ALA C C 177.854 0.2 . 363 76 76 ALA CA C 55.070 0.2 . 364 76 76 ALA CB C 17.697 0.2 . 365 76 76 ALA N N 128.752 0.1 . 366 77 77 LEU H H 7.157 0.02 . 367 77 77 LEU C C 177.580 0.2 . 368 77 77 LEU CA C 57.522 0.2 . 369 77 77 LEU CB C 40.379 0.2 . 370 77 77 LEU N N 114.724 0.1 . 371 78 78 GLN H H 7.892 0.02 . 372 78 78 GLN C C 175.585 0.2 . 373 78 78 GLN CA C 58.350 0.2 . 374 78 78 GLN CB C 29.056 0.2 . 375 78 78 GLN N N 117.989 0.1 . 376 79 79 ASN H H 6.815 0.02 . 377 79 79 ASN C C 176.358 0.2 . 378 79 79 ASN CA C 55.054 0.2 . 379 79 79 ASN CB C 37.432 0.2 . 380 79 79 ASN N N 117.243 0.1 . 381 80 80 PHE H H 7.565 0.02 . 382 80 80 PHE CA C 57.838 0.2 . 383 80 80 PHE N N 115.295 0.1 . 384 81 81 LEU C C 179.564 0.2 . 385 81 81 LEU CA C 60.919 0.2 . 386 81 81 LEU CB C 42.077 0.2 . 387 82 82 ASP H H 8.585 0.02 . 388 82 82 ASP C C 178.678 0.2 . 389 82 82 ASP CA C 56.280 0.2 . 390 82 82 ASP CB C 38.943 0.2 . 391 82 82 ASP N N 121.998 0.1 . 392 83 83 GLN H H 7.879 0.02 . 393 83 83 GLN C C 177.411 0.2 . 394 83 83 GLN CA C 53.735 0.2 . 395 83 83 GLN CB C 27.328 0.2 . 396 83 83 GLN N N 118.584 0.1 . 397 84 84 LEU H H 7.057 0.02 . 398 84 84 LEU C C 177.389 0.2 . 399 84 84 LEU CA C 58.144 0.2 . 400 84 84 LEU CB C 42.674 0.2 . 401 84 84 LEU N N 116.331 0.1 . 402 85 85 ASP H H 8.122 0.02 . 403 85 85 ASP C C 175.221 0.2 . 404 85 85 ASP CA C 54.491 0.2 . 405 85 85 ASP CB C 40.591 0.2 . 406 85 85 ASP N N 113.013 0.1 . 407 86 86 ASN H H 7.906 0.02 . 408 86 86 ASN CA C 50.528 0.2 . 409 86 86 ASN CB C 39.793 0.2 . 410 86 86 ASN N N 119.541 0.1 . 411 87 87 PRO C C 177.243 0.2 . 412 87 87 PRO CA C 65.425 0.2 . 413 87 87 PRO CB C 31.279 0.2 . 414 88 88 ASP H H 8.025 0.02 . 415 88 88 ASP C C 179.664 0.2 . 416 88 88 ASP CA C 57.213 0.2 . 417 88 88 ASP CB C 39.547 0.2 . 418 88 88 ASP N N 114.661 0.1 . 419 89 89 ASP H H 7.779 0.02 . 420 89 89 ASP C C 178.042 0.2 . 421 89 89 ASP CA C 55.030 0.2 . 422 89 89 ASP CB C 39.139 0.2 . 423 89 89 ASP N N 123.487 0.1 . 424 90 90 LEU H H 8.559 0.02 . 425 90 90 LEU C C 178.283 0.2 . 426 90 90 LEU CA C 58.096 0.2 . 427 90 90 LEU CB C 39.525 0.2 . 428 90 90 LEU N N 122.801 0.1 . 429 91 91 VAL H H 8.375 0.02 . 430 91 91 VAL C C 177.582 0.2 . 431 91 91 VAL CA C 67.203 0.2 . 432 91 91 VAL CB C 30.645 0.2 . 433 91 91 VAL N N 116.297 0.1 . 434 92 92 CYS H H 7.125 0.02 . 435 92 92 CYS C C 177.925 0.2 . 436 92 92 CYS CA C 60.525 0.2 . 437 92 92 CYS CB C 25.960 0.2 . 438 92 92 CYS N N 115.185 0.1 . 439 93 93 VAL H H 7.794 0.02 . 440 93 93 VAL C C 178.018 0.2 . 441 93 93 VAL CA C 66.099 0.2 . 442 93 93 VAL CB C 30.972 0.2 . 443 93 93 VAL N N 123.475 0.1 . 444 94 94 VAL H H 8.641 0.02 . 445 94 94 VAL C C 178.236 0.2 . 446 94 94 VAL CA C 67.209 0.2 . 447 94 94 VAL CB C 30.561 0.2 . 448 94 94 VAL N N 124.771 0.1 . 449 95 95 GLU H H 8.651 0.02 . 450 95 95 GLU C C 178.581 0.2 . 451 95 95 GLU CA C 59.968 0.2 . 452 95 95 GLU CB C 28.783 0.2 . 453 95 95 GLU N N 117.681 0.1 . 454 96 96 LYS H H 7.018 0.02 . 455 96 96 LYS C C 178.945 0.2 . 456 96 96 LYS CA C 59.797 0.2 . 457 96 96 LYS CB C 30.233 0.2 . 458 96 96 LYS N N 121.668 0.1 . 459 97 97 PHE H H 7.783 0.02 . 460 97 97 PHE C C 179.351 0.2 . 461 97 97 PHE CA C 60.798 0.2 . 462 97 97 PHE CB C 38.448 0.2 . 463 97 97 PHE N N 118.763 0.1 . 464 98 98 ALA H H 9.128 0.02 . 465 98 98 ALA C C 179.597 0.2 . 466 98 98 ALA CA C 55.059 0.2 . 467 98 98 ALA CB C 17.640 0.2 . 468 98 98 ALA N N 126.356 0.1 . 469 99 99 VAL H H 7.509 0.02 . 470 99 99 VAL C C 177.674 0.2 . 471 99 99 VAL CA C 66.790 0.2 . 472 99 99 VAL CB C 31.008 0.2 . 473 99 99 VAL N N 120.409 0.1 . 474 100 100 ASN H H 6.828 0.02 . 475 100 100 ASN C C 174.714 0.2 . 476 100 100 ASN CA C 55.706 0.2 . 477 100 100 ASN CB C 38.474 0.2 . 478 100 100 ASN N N 114.456 0.1 . 479 101 101 HIS H H 6.495 0.02 . 480 101 101 HIS C C 175.957 0.2 . 481 101 101 HIS CA C 60.388 0.2 . 482 101 101 HIS CB C 26.925 0.2 . 483 101 101 HIS N N 114.982 0.1 . 484 102 102 ILE H H 8.729 0.02 . 485 102 102 ILE C C 181.509 0.2 . 486 102 102 ILE CA C 64.933 0.2 . 487 102 102 ILE CB C 38.351 0.2 . 488 102 102 ILE N N 126.548 0.1 . 489 103 103 THR H H 7.756 0.02 . 490 103 103 THR C C 175.022 0.2 . 491 103 103 THR CA C 64.578 0.2 . 492 103 103 THR CB C 68.747 0.2 . 493 103 103 THR N N 112.973 0.1 . 494 104 104 ARG H H 6.377 0.02 . 495 104 104 ARG C C 173.779 0.2 . 496 104 104 ARG CA C 55.383 0.2 . 497 104 104 ARG CB C 29.291 0.2 . 498 104 104 ARG N N 120.882 0.1 . 499 105 105 LYS H H 7.754 0.02 . 500 105 105 LYS C C 175.258 0.2 . 501 105 105 LYS CA C 56.379 0.2 . 502 105 105 LYS CB C 27.699 0.2 . 503 105 105 LYS N N 113.713 0.1 . 504 106 106 ILE H H 7.175 0.02 . 505 106 106 ILE C C 174.456 0.2 . 506 106 106 ILE CA C 57.861 0.2 . 507 106 106 ILE CB C 34.390 0.2 . 508 106 106 ILE N N 120.369 0.1 . 509 107 107 SER H H 7.759 0.02 . 510 107 107 SER C C 174.567 0.2 . 511 107 107 SER CA C 56.705 0.2 . 512 107 107 SER CB C 65.733 0.2 . 513 107 107 SER N N 122.552 0.1 . 514 108 108 ALA H H 8.928 0.02 . 515 108 108 ALA C C 180.593 0.2 . 516 108 108 ALA CA C 55.983 0.2 . 517 108 108 ALA CB C 17.839 0.2 . 518 108 108 ALA N N 122.702 0.1 . 519 109 109 ALA H H 8.290 0.02 . 520 109 109 ALA C C 180.853 0.2 . 521 109 109 ALA CA C 54.563 0.2 . 522 109 109 ALA CB C 18.037 0.2 . 523 109 109 ALA N N 121.325 0.1 . 524 110 110 GLU H H 7.734 0.02 . 525 110 110 GLU C C 179.029 0.2 . 526 110 110 GLU CA C 59.030 0.2 . 527 110 110 GLU CB C 29.579 0.2 . 528 110 110 GLU N N 120.667 0.1 . 529 111 111 PHE H H 8.686 0.02 . 530 111 111 PHE C C 177.339 0.2 . 531 111 111 PHE CA C 61.059 0.2 . 532 111 111 PHE CB C 40.551 0.2 . 533 111 111 PHE N N 121.185 0.1 . 534 112 112 GLY H H 7.753 0.02 . 535 112 112 GLY C C 175.953 0.2 . 536 112 112 GLY CA C 46.111 0.2 . 537 112 112 GLY N N 99.564 0.1 . 538 113 113 LYS H H 8.167 0.02 . 539 113 113 LYS C C 178.115 0.2 . 540 113 113 LYS CA C 59.181 0.2 . 541 113 113 LYS CB C 32.138 0.2 . 542 113 113 LYS N N 122.915 0.1 . 543 114 114 ILE H H 7.964 0.02 . 544 114 114 ILE C C 175.426 0.2 . 545 114 114 ILE CA C 58.792 0.2 . 546 114 114 ILE CB C 39.887 0.2 . 547 114 114 ILE N N 116.672 0.1 . 548 115 115 ASN H H 7.870 0.02 . 549 115 115 ASN C C 177.814 0.2 . 550 115 115 ASN CA C 56.820 0.2 . 551 115 115 ASN CB C 37.829 0.2 . 552 115 115 ASN N N 122.211 0.1 . 553 116 116 GLY H H 7.911 0.02 . 554 116 116 GLY C C 175.548 0.2 . 555 116 116 GLY CA C 48.053 0.2 . 556 116 116 GLY N N 107.900 0.1 . 557 117 117 PRO C C 177.577 0.2 . 558 117 117 PRO CA C 65.489 0.2 . 559 117 117 PRO CB C 26.135 0.2 . 560 118 118 ILE H H 8.083 0.02 . 561 118 118 ILE C C 176.878 0.2 . 562 118 118 ILE CA C 66.174 0.2 . 563 118 118 ILE CB C 36.946 0.2 . 564 118 118 ILE N N 117.298 0.1 . 565 119 119 LYS H H 8.191 0.02 . 566 119 119 LYS C C 179.595 0.2 . 567 119 119 LYS CA C 60.335 0.2 . 568 119 119 LYS CB C 31.311 0.2 . 569 119 119 LYS N N 121.529 0.1 . 570 120 120 LYS H H 8.062 0.02 . 571 120 120 LYS C C 179.994 0.2 . 572 120 120 LYS CA C 60.145 0.2 . 573 120 120 LYS CB C 32.436 0.2 . 574 120 120 LYS N N 119.739 0.1 . 575 121 121 VAL H H 8.619 0.02 . 576 121 121 VAL C C 180.192 0.2 . 577 121 121 VAL CA C 66.163 0.2 . 578 121 121 VAL CB C 30.894 0.2 . 579 121 121 VAL N N 123.963 0.1 . 580 122 122 LEU H H 8.806 0.02 . 581 122 122 LEU C C 179.771 0.2 . 582 122 122 LEU CA C 58.530 0.2 . 583 122 122 LEU CB C 40.223 0.2 . 584 122 122 LEU N N 122.026 0.1 . 585 123 123 ALA H H 8.280 0.02 . 586 123 123 ALA C C 182.226 0.2 . 587 123 123 ALA CA C 54.990 0.2 . 588 123 123 ALA CB C 17.159 0.2 . 589 123 123 ALA N N 122.915 0.1 . 590 124 124 SER H H 7.918 0.02 . 591 124 124 SER C C 174.602 0.2 . 592 124 124 SER CA C 60.907 0.2 . 593 124 124 SER CB C 62.405 0.2 . 594 124 124 SER N N 117.216 0.1 . 595 125 125 LYS H H 7.307 0.02 . 596 125 125 LYS C C 174.489 0.2 . 597 125 125 LYS CA C 53.001 0.2 . 598 125 125 LYS CB C 30.465 0.2 . 599 125 125 LYS N N 121.189 0.1 . 600 126 126 ASN H H 7.696 0.02 . 601 126 126 ASN C C 173.609 0.2 . 602 126 126 ASN CA C 54.404 0.2 . 603 126 126 ASN CB C 36.122 0.2 . 604 126 126 ASN N N 111.731 0.1 . 605 127 127 PHE H H 7.985 0.02 . 606 127 127 PHE C C 175.621 0.2 . 607 127 127 PHE CA C 57.745 0.2 . 608 127 127 PHE CB C 39.614 0.2 . 609 127 127 PHE N N 118.100 0.1 . 610 128 128 GLY H H 8.666 0.02 . 611 128 128 GLY C C 175.453 0.2 . 612 128 128 GLY CA C 44.286 0.2 . 613 128 128 GLY N N 111.298 0.1 . 614 129 129 ASP H H 8.566 0.02 . 615 129 129 ASP C C 175.452 0.2 . 616 129 129 ASP CA C 57.682 0.2 . 617 129 129 ASP CB C 39.562 0.2 . 618 129 129 ASP N N 121.845 0.1 . 619 130 130 LYS C C 179.418 0.2 . 620 130 130 LYS CA C 59.570 0.2 . 621 131 131 TYR H H 7.631 0.02 . 622 131 131 TYR C C 177.686 0.2 . 623 131 131 TYR CA C 61.819 0.2 . 624 131 131 TYR CB C 38.459 0.2 . 625 131 131 TYR N N 118.265 0.1 . 626 132 132 ALA H H 7.843 0.02 . 627 132 132 ALA C C 179.938 0.2 . 628 132 132 ALA CA C 55.754 0.2 . 629 132 132 ALA CB C 16.425 0.2 . 630 132 132 ALA N N 125.100 0.1 . 631 133 133 ASN H H 8.620 0.02 . 632 133 133 ASN C C 177.556 0.2 . 633 133 133 ASN CA C 55.699 0.2 . 634 133 133 ASN CB C 37.773 0.2 . 635 133 133 ASN N N 117.475 0.1 . 636 134 134 ALA H H 7.463 0.02 . 637 134 134 ALA C C 179.293 0.2 . 638 134 134 ALA CA C 55.547 0.2 . 639 134 134 ALA CB C 17.588 0.2 . 640 134 134 ALA N N 124.311 0.1 . 641 135 135 TRP H H 8.203 0.02 . 642 135 135 TRP HE1 H 9.945 0.02 . 643 135 135 TRP C C 178.873 0.2 . 644 135 135 TRP CA C 61.527 0.2 . 645 135 135 TRP CB C 28.619 0.2 . 646 135 135 TRP N N 118.184 0.1 . 647 135 135 TRP NE1 N 128.449 0.1 . 648 136 136 ALA H H 8.423 0.02 . 649 136 136 ALA C C 181.885 0.2 . 650 136 136 ALA CA C 54.659 0.2 . 651 136 136 ALA CB C 17.028 0.2 . 652 136 136 ALA N N 123.306 0.1 . 653 137 137 LYS H H 7.626 0.02 . 654 137 137 LYS C C 178.983 0.2 . 655 137 137 LYS CA C 58.796 0.2 . 656 137 137 LYS CB C 31.205 0.2 . 657 137 137 LYS N N 119.926 0.1 . 658 138 138 LEU H H 7.310 0.02 . 659 138 138 LEU C C 178.911 0.2 . 660 138 138 LEU CA C 57.936 0.2 . 661 138 138 LEU CB C 40.320 0.2 . 662 138 138 LEU N N 120.482 0.1 . 663 139 139 VAL H H 8.758 0.02 . 664 139 139 VAL C C 178.081 0.2 . 665 139 139 VAL CA C 67.314 0.2 . 666 139 139 VAL CB C 31.323 0.2 . 667 139 139 VAL N N 121.482 0.1 . 668 140 140 ALA H H 7.961 0.02 . 669 140 140 ALA C C 180.233 0.2 . 670 140 140 ALA CA C 53.807 0.2 . 671 140 140 ALA CB C 17.367 0.2 . 672 140 140 ALA N N 120.961 0.1 . 673 141 141 VAL H H 7.553 0.02 . 674 141 141 VAL C C 176.154 0.2 . 675 141 141 VAL CA C 65.721 0.2 . 676 141 141 VAL CB C 30.198 0.2 . 677 141 141 VAL N N 121.029 0.1 . 678 142 142 VAL H H 6.507 0.02 . 679 142 142 VAL C C 179.297 0.2 . 680 142 142 VAL CA C 63.989 0.2 . 681 142 142 VAL CB C 29.895 0.2 . 682 142 142 VAL N N 115.266 0.1 . 683 143 143 GLN H H 7.284 0.02 . 684 143 143 GLN C C 177.512 0.2 . 685 143 143 GLN CA C 51.033 0.2 . 686 143 143 GLN CB C 29.749 0.2 . 687 143 143 GLN N N 120.472 0.1 . 688 144 144 ALA H H 7.152 0.02 . 689 144 144 ALA C C 176.790 0.2 . 690 144 144 ALA CA C 53.537 0.2 . 691 144 144 ALA CB C 17.281 0.2 . 692 144 144 ALA N N 119.376 0.1 . 693 145 145 ALA H H 7.289 0.02 . 694 145 145 ALA C C 175.624 0.2 . 695 145 145 ALA CA C 50.940 0.2 . 696 145 145 ALA CB C 19.601 0.2 . 697 145 145 ALA N N 120.464 0.1 . 698 146 146 LEU H H 6.644 0.02 . 699 146 146 LEU CA C 55.248 0.2 . 700 146 146 LEU CB C 42.381 0.2 . 701 146 146 LEU N N 125.001 0.1 . stop_ save_