data_25286 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for Scapharca dimeric hemoglobin (HbI) in the unliganded state ; _BMRB_accession_number 25286 _BMRB_flat_file_name bmr25286.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" 138 "13C chemical shifts" 383 "15N chemical shifts" 138 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-07-11 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25285 'HbI homodimer (bound to CO)' 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 homodymer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HbI, chain 1' $Scapharca_dimeric_hemoglobin_(HbI) 'HbI, chain 2' $Scapharca_dimeric_hemoglobin_(HbI) Heme $entity_HEM 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 Heme 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 IDQLDNPDDLVCVVEKFAVN 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 ILE 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 4SDH HbI . . . . . 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 $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_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . 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(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _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 1 1 PRO C C 172.469 0.2 . 2 1 1 PRO CA C 62.389 0.2 . 3 1 1 PRO CB C 32.590 0.2 . 4 2 2 SER H H 8.942 0.02 . 5 2 2 SER C C 175.379 0.2 . 6 2 2 SER CA C 57.475 0.2 . 7 2 2 SER CB C 64.949 0.2 . 8 2 2 SER N N 116.893 0.1 . 9 3 3 VAL H H 8.558 0.02 . 10 3 3 VAL C C 177.191 0.2 . 11 3 3 VAL CA C 65.791 0.2 . 12 3 3 VAL CB C 31.036 0.2 . 13 3 3 VAL N N 124.874 0.1 . 14 4 4 TYR H H 7.543 0.02 . 15 4 4 TYR C C 178.148 0.2 . 16 4 4 TYR CA C 62.460 0.2 . 17 4 4 TYR CB C 38.124 0.2 . 18 4 4 TYR N N 119.147 0.1 . 19 5 5 ASP H H 7.725 0.02 . 20 5 5 ASP C C 178.734 0.2 . 21 5 5 ASP CA C 57.263 0.2 . 22 5 5 ASP CB C 39.918 0.2 . 23 5 5 ASP N N 120.953 0.1 . 24 6 6 ALA H H 7.617 0.02 . 25 6 6 ALA C C 181.084 0.2 . 26 6 6 ALA CA C 54.796 0.2 . 27 6 6 ALA CB C 18.169 0.2 . 28 6 6 ALA N N 122.652 0.1 . 29 7 7 ALA H H 8.210 0.02 . 30 7 7 ALA C C 179.309 0.2 . 31 7 7 ALA CA C 54.498 0.2 . 32 7 7 ALA CB C 16.571 0.2 . 33 7 7 ALA N N 123.152 0.1 . 34 8 8 ALA H H 7.677 0.02 . 35 8 8 ALA C C 178.449 0.2 . 36 8 8 ALA CA C 53.706 0.2 . 37 8 8 ALA CB C 17.732 0.2 . 38 8 8 ALA N N 121.476 0.1 . 39 9 9 GLN H H 7.006 0.02 . 40 9 9 GLN C C 176.251 0.2 . 41 9 9 GLN CA C 55.619 0.2 . 42 9 9 GLN CB C 27.935 0.2 . 43 9 9 GLN N N 114.113 0.1 . 44 10 10 LEU H H 7.222 0.02 . 45 10 10 LEU C C 174.579 0.2 . 46 10 10 LEU CA C 53.167 0.2 . 47 10 10 LEU CB C 38.282 0.2 . 48 10 10 LEU N N 120.603 0.1 . 49 11 11 THR H H 6.884 0.02 . 50 11 11 THR C C 174.789 0.2 . 51 11 11 THR CA C 60.860 0.2 . 52 11 11 THR CB C 70.567 0.2 . 53 11 11 THR N N 114.443 0.1 . 54 12 12 ALA H H 8.895 0.02 . 55 12 12 ALA C C 180.278 0.2 . 56 12 12 ALA CA C 56.562 0.2 . 57 12 12 ALA CB C 18.408 0.2 . 58 12 12 ALA N N 123.432 0.1 . 59 13 13 ASP H H 8.448 0.02 . 60 13 13 ASP C C 177.053 0.2 . 61 13 13 ASP CA C 57.193 0.2 . 62 13 13 ASP CB C 40.720 0.2 . 63 13 13 ASP N N 117.355 0.1 . 64 14 14 VAL H H 6.888 0.02 . 65 14 14 VAL C C 178.086 0.2 . 66 14 14 VAL CA C 65.771 0.2 . 67 14 14 VAL CB C 32.207 0.2 . 68 14 14 VAL N N 121.878 0.1 . 69 15 15 LYS H H 8.435 0.02 . 70 15 15 LYS C C 177.764 0.2 . 71 15 15 LYS CA C 60.907 0.2 . 72 15 15 LYS CB C 32.418 0.2 . 73 15 15 LYS N N 118.148 0.1 . 74 16 16 LYS H H 7.651 0.02 . 75 16 16 LYS C C 177.706 0.2 . 76 16 16 LYS CA C 59.610 0.2 . 77 16 16 LYS CB C 32.049 0.2 . 78 16 16 LYS N N 120.090 0.1 . 79 17 17 ASP H H 7.714 0.02 . 80 17 17 ASP C C 181.087 0.2 . 81 17 17 ASP CA C 57.865 0.2 . 82 17 17 ASP CB C 39.442 0.2 . 83 17 17 ASP N N 120.823 0.1 . 84 18 18 LEU H H 8.506 0.02 . 85 18 18 LEU C C 177.902 0.2 . 86 18 18 LEU CA C 58.406 0.2 . 87 18 18 LEU CB C 41.818 0.2 . 88 18 18 LEU N N 124.575 0.1 . 89 19 19 ARG H H 8.318 0.02 . 90 19 19 ARG C C 180.086 0.2 . 91 19 19 ARG CA C 61.236 0.2 . 92 19 19 ARG CB C 30.423 0.2 . 93 19 19 ARG N N 119.691 0.1 . 94 20 20 ASP H H 9.464 0.02 . 95 20 20 ASP C C 178.973 0.2 . 96 20 20 ASP CA C 57.707 0.2 . 97 20 20 ASP CB C 40.356 0.2 . 98 20 20 ASP N N 121.450 0.1 . 99 21 21 SER H H 7.756 0.02 . 100 21 21 SER C C 177.710 0.2 . 101 21 21 SER CA C 60.329 0.2 . 102 21 21 SER CB C 62.966 0.2 . 103 21 21 SER N N 112.189 0.1 . 104 22 22 TRP H H 9.193 0.02 . 105 22 22 TRP C C 177.714 0.2 . 106 22 22 TRP CA C 59.719 0.2 . 107 22 22 TRP CB C 30.442 0.2 . 108 22 22 TRP N N 127.828 0.1 . 109 23 23 LYS H H 7.953 0.02 . 110 23 23 LYS C C 177.516 0.2 . 111 23 23 LYS CA C 59.664 0.2 . 112 23 23 LYS CB C 32.518 0.2 . 113 23 23 LYS N N 119.839 0.1 . 114 24 24 VAL H H 6.584 0.02 . 115 24 24 VAL C C 179.545 0.2 . 116 24 24 VAL CA C 64.749 0.2 . 117 24 24 VAL CB C 33.401 0.2 . 118 24 24 VAL N N 114.862 0.1 . 119 25 25 ILE H H 8.477 0.02 . 120 25 25 ILE C C 177.353 0.2 . 121 25 25 ILE CA C 62.625 0.2 . 122 25 25 ILE CB C 37.201 0.2 . 123 25 25 ILE N N 119.596 0.1 . 124 26 26 GLY H H 8.364 0.02 . 125 26 26 GLY C C 173.117 0.2 . 126 26 26 GLY CA C 43.540 0.2 . 127 26 26 GLY N N 108.197 0.1 . 128 27 27 SER H H 6.659 0.02 . 129 27 27 SER C C 173.742 0.2 . 130 27 27 SER CA C 59.523 0.2 . 131 27 27 SER CB C 63.764 0.2 . 132 27 27 SER N N 113.500 0.1 . 133 28 28 ASP H H 6.400 0.02 . 134 28 28 ASP C C 175.422 0.2 . 135 28 28 ASP CA C 52.183 0.2 . 136 28 28 ASP CB C 39.719 0.2 . 137 28 28 ASP N N 120.884 0.1 . 138 29 29 LYS H H 8.746 0.02 . 139 29 29 LYS C C 178.399 0.2 . 140 29 29 LYS CA C 61.322 0.2 . 141 29 29 LYS CB C 32.223 0.2 . 142 29 29 LYS N N 124.559 0.1 . 143 30 30 LYS H H 8.442 0.02 . 144 30 30 LYS C C 176.957 0.2 . 145 30 30 LYS CA C 60.157 0.2 . 146 30 30 LYS CB C 32.120 0.2 . 147 30 30 LYS N N 118.267 0.1 . 148 31 31 GLY H H 8.135 0.02 . 149 31 31 GLY C C 177.685 0.2 . 150 31 31 GLY CA C 47.919 0.2 . 151 31 31 GLY N N 106.937 0.1 . 152 32 32 ASN H H 8.202 0.02 . 153 32 32 ASN C C 177.169 0.2 . 154 32 32 ASN CA C 55.790 0.2 . 155 32 32 ASN CB C 37.967 0.2 . 156 32 32 ASN N N 117.226 0.1 . 157 33 33 GLY H H 8.287 0.02 . 158 33 33 GLY C C 175.914 0.2 . 159 33 33 GLY CA C 48.155 0.2 . 160 33 33 GLY N N 111.818 0.1 . 161 34 34 VAL H H 7.905 0.02 . 162 34 34 VAL C C 178.689 0.2 . 163 34 34 VAL CA C 66.448 0.2 . 164 34 34 VAL CB C 31.411 0.2 . 165 34 34 VAL N N 122.358 0.1 . 166 35 35 ALA H H 7.752 0.02 . 167 35 35 ALA C C 180.716 0.2 . 168 35 35 ALA CA C 55.729 0.2 . 169 35 35 ALA CB C 18.362 0.2 . 170 35 35 ALA N N 124.092 0.1 . 171 36 36 LEU H H 8.494 0.02 . 172 36 36 LEU C C 178.740 0.2 . 173 36 36 LEU CA C 59.407 0.2 . 174 36 36 LEU N N 121.847 0.1 . 175 37 37 MET H H 7.693 0.02 . 176 37 37 MET C C 177.160 0.2 . 177 37 37 MET CA C 55.189 0.2 . 178 37 37 MET N N 115.733 0.1 . 179 38 38 THR H H 8.877 0.02 . 180 38 38 THR C C 178.129 0.2 . 181 38 38 THR CA C 65.936 0.2 . 182 38 38 THR CB C 68.727 0.2 . 183 38 38 THR N N 111.459 0.1 . 184 39 39 THR H H 7.938 0.02 . 185 39 39 THR C C 175.242 0.2 . 186 39 39 THR CA C 67.281 0.2 . 187 39 39 THR CB C 68.191 0.2 . 188 39 39 THR N N 120.606 0.1 . 189 40 40 LEU H H 8.190 0.02 . 190 40 40 LEU C C 178.361 0.2 . 191 40 40 LEU CA C 59.834 0.2 . 192 40 40 LEU CB C 33.236 0.2 . 193 40 40 LEU N N 125.087 0.1 . 194 41 41 PHE H H 7.618 0.02 . 195 41 41 PHE C C 177.585 0.2 . 196 41 41 PHE CA C 57.011 0.2 . 197 41 41 PHE CB C 37.404 0.2 . 198 41 41 PHE N N 115.584 0.1 . 199 42 42 ALA H H 7.731 0.02 . 200 42 42 ALA C C 179.902 0.2 . 201 42 42 ALA CA C 54.552 0.2 . 202 42 42 ALA CB C 19.163 0.2 . 203 42 42 ALA N N 120.489 0.1 . 204 43 43 ASP H H 8.248 0.02 . 205 43 43 ASP C C 176.971 0.2 . 206 43 43 ASP CA C 55.731 0.2 . 207 43 43 ASP N N 117.222 0.1 . 208 44 44 ASN H H 8.303 0.02 . 209 44 44 ASN C C 175.396 0.2 . 210 44 44 ASN CA C 52.859 0.2 . 211 44 44 ASN CB C 40.232 0.2 . 212 44 44 ASN N N 121.425 0.1 . 213 45 45 GLN H H 9.215 0.02 . 214 45 45 GLN C C 177.741 0.2 . 215 45 45 GLN CA C 59.568 0.2 . 216 45 45 GLN CB C 28.476 0.2 . 217 45 45 GLN N N 125.403 0.1 . 218 46 46 GLU H H 9.783 0.02 . 219 46 46 GLU C C 178.311 0.2 . 220 46 46 GLU CA C 58.516 0.2 . 221 46 46 GLU CB C 27.008 0.2 . 222 46 46 GLU N N 121.960 0.1 . 223 47 47 THR H H 8.273 0.02 . 224 47 47 THR C C 176.196 0.2 . 225 47 47 THR CA C 64.628 0.2 . 226 47 47 THR CB C 70.484 0.2 . 227 47 47 THR N N 113.413 0.1 . 228 48 48 ILE H H 7.122 0.02 . 229 48 48 ILE C C 178.127 0.2 . 230 48 48 ILE CA C 64.691 0.2 . 231 48 48 ILE CB C 37.792 0.2 . 232 48 48 ILE N N 122.268 0.1 . 233 49 49 GLY H H 7.233 0.02 . 234 49 49 GLY C C 175.431 0.2 . 235 49 49 GLY CA C 46.439 0.2 . 236 49 49 GLY N N 105.703 0.1 . 237 50 50 TYR H H 6.379 0.02 . 238 50 50 TYR C C 174.916 0.2 . 239 50 50 TYR CA C 59.238 0.2 . 240 50 50 TYR N N 116.599 0.1 . 241 51 51 PHE H H 6.405 0.02 . 242 51 51 PHE C C 175.259 0.2 . 243 51 51 PHE CA C 56.172 0.2 . 244 51 51 PHE CB C 35.903 0.2 . 245 51 51 PHE N N 115.299 0.1 . 246 52 52 LYS H H 6.277 0.02 . 247 52 52 LYS C C 177.928 0.2 . 248 52 52 LYS CA C 58.918 0.2 . 249 52 52 LYS CB C 31.625 0.2 . 250 52 52 LYS N N 121.361 0.1 . 251 53 53 ARG H H 7.665 0.02 . 252 53 53 ARG C C 176.546 0.2 . 253 53 53 ARG CA C 57.699 0.2 . 254 53 53 ARG CB C 30.942 0.2 . 255 53 53 ARG N N 119.470 0.1 . 256 54 54 LEU H H 6.709 0.02 . 257 54 54 LEU C C 176.200 0.2 . 258 54 54 LEU CA C 54.721 0.2 . 259 54 54 LEU CB C 39.347 0.2 . 260 54 54 LEU N N 110.011 0.1 . 261 55 55 GLY H H 6.818 0.02 . 262 55 55 GLY C C 173.591 0.2 . 263 55 55 GLY CA C 45.272 0.2 . 264 55 55 GLY N N 106.235 0.1 . 265 56 56 ASP H H 8.343 0.02 . 266 56 56 ASP C C 178.323 0.2 . 267 56 56 ASP CA C 53.270 0.2 . 268 56 56 ASP CB C 38.748 0.2 . 269 56 56 ASP N N 121.912 0.1 . 270 57 57 VAL H H 7.445 0.02 . 271 57 57 VAL C C 177.045 0.2 . 272 57 57 VAL CA C 62.988 0.2 . 273 57 57 VAL CB C 30.163 0.2 . 274 57 57 VAL N N 123.181 0.1 . 275 58 58 SER H H 7.964 0.02 . 276 58 58 SER C C 175.292 0.2 . 277 58 58 SER CA C 60.850 0.2 . 278 58 58 SER CB C 62.594 0.2 . 279 58 58 SER N N 120.078 0.1 . 280 59 59 GLN H H 6.721 0.02 . 281 59 59 GLN C C 177.436 0.2 . 282 59 59 GLN CA C 55.816 0.2 . 283 59 59 GLN CB C 29.811 0.2 . 284 59 59 GLN N N 118.684 0.1 . 285 60 60 GLY H H 7.172 0.02 . 286 60 60 GLY C C 173.919 0.2 . 287 60 60 GLY CA C 46.600 0.2 . 288 60 60 GLY N N 106.741 0.1 . 289 61 61 MET H H 8.723 0.02 . 290 61 61 MET C C 174.719 0.2 . 291 61 61 MET CA C 56.726 0.2 . 292 61 61 MET CB C 32.204 0.2 . 293 61 61 MET N N 125.008 0.1 . 294 62 62 ALA H H 7.138 0.02 . 295 62 62 ALA C C 177.093 0.2 . 296 62 62 ALA CA C 52.660 0.2 . 297 62 62 ALA CB C 18.677 0.2 . 298 62 62 ALA N N 116.656 0.1 . 299 63 63 ASN H H 7.531 0.02 . 300 63 63 ASN C C 174.284 0.2 . 301 63 63 ASN CA C 51.909 0.2 . 302 63 63 ASN CB C 38.009 0.2 . 303 63 63 ASN N N 118.224 0.1 . 304 64 64 ASP H H 8.377 0.02 . 305 64 64 ASP C C 177.457 0.2 . 306 64 64 ASP CA C 57.427 0.2 . 307 64 64 ASP CB C 40.800 0.2 . 308 64 64 ASP N N 127.157 0.1 . 309 65 65 LYS H H 7.592 0.02 . 310 65 65 LYS C C 180.457 0.2 . 311 65 65 LYS CA C 58.733 0.2 . 312 65 65 LYS CB C 32.340 0.2 . 313 65 65 LYS N N 119.800 0.1 . 314 66 66 LEU H H 7.572 0.02 . 315 66 66 LEU C C 179.500 0.2 . 316 66 66 LEU CA C 56.905 0.2 . 317 66 66 LEU CB C 40.094 0.2 . 318 66 66 LEU N N 123.654 0.1 . 319 67 67 ARG H H 8.929 0.02 . 320 67 67 ARG C C 177.583 0.2 . 321 67 67 ARG CA C 61.456 0.2 . 322 67 67 ARG CB C 30.666 0.2 . 323 67 67 ARG N N 126.688 0.1 . 324 68 68 GLY H H 8.403 0.02 . 325 68 68 GLY C C 177.202 0.2 . 326 68 68 GLY CA C 47.964 0.2 . 327 68 68 GLY N N 106.051 0.1 . 328 69 69 HIS H H 7.779 0.02 . 329 69 69 HIS C C 175.000 0.2 . 330 69 69 HIS CA C 60.773 0.2 . 331 69 69 HIS N N 123.437 0.1 . 332 70 70 SER H H 8.851 0.02 . 333 70 70 SER N N 128.080 0.1 . 334 71 71 ILE H H 8.174 0.02 . 335 71 71 ILE C C 176.098 0.2 . 336 71 71 ILE CA C 54.791 0.2 . 337 71 71 ILE N N 120.097 0.1 . 338 72 72 THR H H 8.083 0.02 . 339 72 72 THR C C 173.446 0.2 . 340 72 72 THR CA C 61.842 0.2 . 341 72 72 THR CB C 70.138 0.2 . 342 72 72 THR N N 116.833 0.1 . 343 73 73 LEU H H 7.887 0.02 . 344 73 73 LEU C C 181.191 0.2 . 345 73 73 LEU CA C 57.938 0.2 . 346 73 73 LEU CB C 33.887 0.2 . 347 73 73 LEU N N 129.671 0.1 . 348 74 74 MET H H 7.334 0.02 . 349 74 74 MET CA C 56.343 0.2 . 350 74 74 MET N N 117.003 0.1 . 351 78 78 GLN H H 7.299 0.02 . 352 78 78 GLN C C 175.031 0.2 . 353 78 78 GLN CA C 58.573 0.2 . 354 78 78 GLN CB C 29.235 0.2 . 355 78 78 GLN N N 116.743 0.1 . 356 79 79 ASN H H 5.843 0.02 . 357 79 79 ASN C C 175.519 0.2 . 358 79 79 ASN CA C 54.941 0.2 . 359 79 79 ASN CB C 36.961 0.2 . 360 79 79 ASN N N 116.376 0.1 . 361 80 80 PHE H H 6.674 0.02 . 362 80 80 PHE C C 177.522 0.2 . 363 80 80 PHE CA C 57.309 0.2 . 364 80 80 PHE CB C 36.822 0.2 . 365 80 80 PHE N N 114.833 0.1 . 366 81 81 ILE H H 7.463 0.02 . 367 81 81 ILE C C 179.143 0.2 . 368 81 81 ILE CA C 61.021 0.2 . 369 81 81 ILE CB C 34.817 0.2 . 370 81 81 ILE N N 116.322 0.1 . 371 82 82 ASP H H 8.117 0.02 . 372 82 82 ASP C C 178.448 0.2 . 373 82 82 ASP CA C 56.484 0.2 . 374 82 82 ASP CB C 39.198 0.2 . 375 82 82 ASP N N 122.103 0.1 . 376 83 83 GLN H H 7.460 0.02 . 377 83 83 GLN C C 176.993 0.2 . 378 83 83 GLN CA C 53.727 0.2 . 379 83 83 GLN CB C 27.168 0.2 . 380 83 83 GLN N N 117.893 0.1 . 381 84 84 LEU H H 6.800 0.02 . 382 84 84 LEU C C 177.162 0.2 . 383 84 84 LEU CA C 58.249 0.2 . 384 84 84 LEU CB C 42.950 0.2 . 385 84 84 LEU N N 115.833 0.1 . 386 85 85 ASP H H 7.930 0.02 . 387 85 85 ASP C C 175.135 0.2 . 388 85 85 ASP CA C 54.912 0.2 . 389 85 85 ASP CB C 41.065 0.2 . 390 85 85 ASP N N 112.918 0.1 . 391 86 86 ASN H H 7.676 0.02 . 392 86 86 ASN C C 171.631 0.2 . 393 86 86 ASN N N 119.042 0.1 . 394 87 87 PRO C C 177.038 0.2 . 395 87 87 PRO CA C 65.518 0.2 . 396 87 87 PRO CB C 31.854 0.2 . 397 88 88 ASP H H 7.821 0.02 . 398 88 88 ASP C C 179.466 0.2 . 399 88 88 ASP CA C 57.319 0.2 . 400 88 88 ASP CB C 40.178 0.2 . 401 88 88 ASP N N 114.975 0.1 . 402 89 89 ASP H H 7.616 0.02 . 403 89 89 ASP C C 177.984 0.2 . 404 89 89 ASP CA C 55.943 0.2 . 405 89 89 ASP CB C 39.455 0.2 . 406 89 89 ASP N N 123.243 0.1 . 407 90 90 LEU H H 8.318 0.02 . 408 90 90 LEU C C 177.697 0.2 . 409 90 90 LEU CA C 58.077 0.2 . 410 90 90 LEU CB C 39.671 0.2 . 411 90 90 LEU N N 123.135 0.1 . 412 91 91 VAL H H 8.145 0.02 . 413 91 91 VAL C C 177.646 0.2 . 414 91 91 VAL CA C 67.244 0.2 . 415 91 91 VAL CB C 30.827 0.2 . 416 91 91 VAL N N 117.415 0.1 . 417 92 92 CYS H H 7.022 0.02 . 418 92 92 CYS C C 178.572 0.2 . 419 92 92 CYS CA C 60.892 0.2 . 420 92 92 CYS CB C 25.752 0.2 . 421 92 92 CYS N N 115.466 0.1 . 422 93 93 VAL H H 7.687 0.02 . 423 93 93 VAL C C 178.468 0.2 . 424 93 93 VAL CA C 66.025 0.2 . 425 93 93 VAL N N 121.308 0.1 . 426 94 94 VAL H H 7.993 0.02 . 427 94 94 VAL C C 176.717 0.2 . 428 94 94 VAL CA C 66.440 0.2 . 429 94 94 VAL CB C 29.907 0.2 . 430 94 94 VAL N N 128.026 0.1 . 431 95 95 GLU H H 8.126 0.02 . 432 95 95 GLU C C 178.659 0.2 . 433 95 95 GLU CA C 60.143 0.2 . 434 95 95 GLU CB C 28.558 0.2 . 435 95 95 GLU N N 119.054 0.1 . 436 96 96 LYS H H 6.782 0.02 . 437 96 96 LYS C C 177.072 0.2 . 438 96 96 LYS CA C 58.114 0.2 . 439 96 96 LYS CB C 30.511 0.2 . 440 96 96 LYS N N 120.074 0.1 . 441 97 97 PHE H H 7.215 0.02 . 442 97 97 PHE C C 177.694 0.2 . 443 97 97 PHE CA C 59.417 0.2 . 444 97 97 PHE CB C 37.179 0.2 . 445 97 97 PHE N N 122.347 0.1 . 446 98 98 ALA H H 8.087 0.02 . 447 98 98 ALA C C 176.069 0.2 . 448 98 98 ALA CA C 58.268 0.2 . 449 98 98 ALA CB C 19.382 0.2 . 450 98 98 ALA N N 123.214 0.1 . 451 99 99 VAL H H 7.617 0.02 . 452 99 99 VAL N N 120.035 0.1 . 453 103 103 THR H H 8.175 0.02 . 454 103 103 THR C C 175.254 0.2 . 455 103 103 THR CA C 61.911 0.2 . 456 103 103 THR CB C 70.177 0.2 . 457 103 103 THR N N 113.948 0.1 . 458 104 104 ARG H H 6.388 0.02 . 459 104 104 ARG C C 175.366 0.2 . 460 104 104 ARG CA C 50.837 0.2 . 461 104 104 ARG N N 120.908 0.1 . 462 105 105 LYS H H 7.871 0.02 . 463 105 105 LYS N N 113.221 0.1 . 464 106 106 ILE H H 7.300 0.02 . 465 106 106 ILE C C 174.820 0.2 . 466 106 106 ILE CA C 61.234 0.2 . 467 106 106 ILE N N 119.914 0.1 . 468 107 107 SER H H 8.360 0.02 . 469 107 107 SER C C 174.893 0.2 . 470 107 107 SER CA C 57.361 0.2 . 471 107 107 SER CB C 66.314 0.2 . 472 107 107 SER N N 123.809 0.1 . 473 108 108 ALA H H 9.253 0.02 . 474 108 108 ALA C C 181.198 0.2 . 475 108 108 ALA CA C 56.599 0.2 . 476 108 108 ALA CB C 18.697 0.2 . 477 108 108 ALA N N 123.391 0.1 . 478 109 109 ALA H H 8.631 0.02 . 479 109 109 ALA C C 180.746 0.2 . 480 109 109 ALA CA C 55.297 0.2 . 481 109 109 ALA CB C 18.680 0.2 . 482 109 109 ALA N N 122.302 0.1 . 483 110 110 GLU H H 8.353 0.02 . 484 110 110 GLU C C 175.903 0.2 . 485 110 110 GLU CA C 55.707 0.2 . 486 110 110 GLU N N 122.319 0.1 . 487 111 111 PHE H H 8.080 0.02 . 488 111 111 PHE C C 177.153 0.2 . 489 111 111 PHE CA C 57.069 0.2 . 490 111 111 PHE CB C 33.029 0.2 . 491 111 111 PHE N N 122.847 0.1 . 492 112 112 GLY H H 8.368 0.02 . 493 112 112 GLY C C 174.099 0.2 . 494 112 112 GLY CA C 45.428 0.2 . 495 112 112 GLY N N 110.953 0.1 . 496 113 113 LYS H H 8.022 0.02 . 497 113 113 LYS C C 176.042 0.2 . 498 113 113 LYS CA C 60.156 0.2 . 499 113 113 LYS N N 121.077 0.1 . 500 114 114 ILE H H 8.070 0.02 . 501 114 114 ILE C C 176.543 0.2 . 502 114 114 ILE CA C 61.081 0.2 . 503 114 114 ILE N N 116.351 0.1 . 504 115 115 ASN H H 8.806 0.02 . 505 115 115 ASN C C 178.366 0.2 . 506 115 115 ASN CA C 57.785 0.2 . 507 115 115 ASN CB C 38.851 0.2 . 508 115 115 ASN N N 123.389 0.1 . 509 116 116 GLY H H 8.549 0.02 . 510 116 116 GLY C C 176.066 0.2 . 511 116 116 GLY CA C 49.210 0.2 . 512 116 116 GLY N N 108.572 0.1 . 513 117 117 PRO C C 178.142 0.2 . 514 117 117 PRO CA C 66.534 0.2 . 515 118 118 ILE H H 8.754 0.02 . 516 118 118 ILE C C 177.206 0.2 . 517 118 118 ILE CA C 67.263 0.2 . 518 118 118 ILE CB C 38.207 0.2 . 519 118 118 ILE N N 118.265 0.1 . 520 119 119 LYS H H 8.717 0.02 . 521 119 119 LYS C C 179.719 0.2 . 522 119 119 LYS CA C 61.081 0.2 . 523 119 119 LYS CB C 32.264 0.2 . 524 119 119 LYS N N 122.152 0.1 . 525 120 120 LYS H H 8.466 0.02 . 526 120 120 LYS C C 180.230 0.2 . 527 120 120 LYS CA C 60.722 0.2 . 528 120 120 LYS CB C 33.472 0.2 . 529 120 120 LYS N N 120.314 0.1 . 530 121 121 VAL H H 9.042 0.02 . 531 121 121 VAL C C 180.355 0.2 . 532 121 121 VAL CA C 66.817 0.2 . 533 121 121 VAL CB C 31.807 0.2 . 534 121 121 VAL N N 124.415 0.1 . 535 122 122 LEU H H 9.107 0.02 . 536 122 122 LEU C C 179.839 0.2 . 537 122 122 LEU CA C 59.149 0.2 . 538 122 122 LEU CB C 41.151 0.2 . 539 122 122 LEU N N 122.665 0.1 . 540 123 123 ALA H H 8.470 0.02 . 541 123 123 ALA C C 182.279 0.2 . 542 123 123 ALA CA C 55.558 0.2 . 543 123 123 ALA CB C 17.887 0.2 . 544 123 123 ALA N N 123.232 0.1 . 545 124 124 SER H H 8.116 0.02 . 546 124 124 SER C C 174.676 0.2 . 547 124 124 SER CA C 61.383 0.2 . 548 124 124 SER CB C 63.145 0.2 . 549 124 124 SER N N 117.710 0.1 . 550 125 125 LYS H H 7.460 0.02 . 551 125 125 LYS C C 174.479 0.2 . 552 125 125 LYS CA C 53.378 0.2 . 553 125 125 LYS CB C 31.166 0.2 . 554 125 125 LYS N N 121.516 0.1 . 555 126 126 ASN H H 7.804 0.02 . 556 126 126 ASN C C 173.644 0.2 . 557 126 126 ASN CA C 54.895 0.2 . 558 126 126 ASN CB C 36.663 0.2 . 559 126 126 ASN N N 114.207 0.1 . 560 127 127 PHE H H 8.099 0.02 . 561 127 127 PHE C C 175.632 0.2 . 562 127 127 PHE CA C 58.125 0.2 . 563 127 127 PHE CB C 40.097 0.2 . 564 127 127 PHE N N 118.365 0.1 . 565 128 128 GLY H H 8.775 0.02 . 566 128 128 GLY C C 175.539 0.2 . 567 128 128 GLY CA C 44.745 0.2 . 568 128 128 GLY N N 111.838 0.1 . 569 129 129 ASP H H 8.695 0.02 . 570 129 129 ASP C C 177.711 0.2 . 571 129 129 ASP CA C 58.454 0.2 . 572 129 129 ASP CB C 40.790 0.2 . 573 129 129 ASP N N 122.290 0.1 . 574 130 130 LYS H H 8.989 0.02 . 575 130 130 LYS C C 179.439 0.2 . 576 130 130 LYS CA C 60.013 0.2 . 577 130 130 LYS CB C 32.488 0.2 . 578 130 130 LYS N N 120.387 0.1 . 579 131 131 TYR H H 7.733 0.02 . 580 131 131 TYR C C 177.747 0.2 . 581 131 131 TYR CA C 62.240 0.2 . 582 131 131 TYR CB C 39.036 0.2 . 583 131 131 TYR N N 118.618 0.1 . 584 132 132 ALA H H 8.020 0.02 . 585 132 132 ALA C C 180.101 0.2 . 586 132 132 ALA CA C 56.306 0.2 . 587 132 132 ALA CB C 17.120 0.2 . 588 132 132 ALA N N 125.394 0.1 . 589 133 133 ASN H H 8.770 0.02 . 590 133 133 ASN C C 177.611 0.2 . 591 133 133 ASN CA C 56.135 0.2 . 592 133 133 ASN CB C 38.255 0.2 . 593 133 133 ASN N N 117.892 0.1 . 594 134 134 ALA H H 7.550 0.02 . 595 134 134 ALA C C 179.331 0.2 . 596 134 134 ALA CA C 55.999 0.2 . 597 134 134 ALA CB C 18.217 0.2 . 598 134 134 ALA N N 124.609 0.1 . 599 135 135 TRP H H 8.368 0.02 . 600 135 135 TRP HE1 H 9.794 0.02 . 601 135 135 TRP C C 178.941 0.2 . 602 135 135 TRP CA C 61.918 0.2 . 603 135 135 TRP CB C 29.021 0.2 . 604 135 135 TRP N N 118.626 0.1 . 605 135 135 TRP NE1 N 128.526 0.1 . 606 136 136 ALA H H 8.611 0.02 . 607 136 136 ALA C C 181.870 0.2 . 608 136 136 ALA CA C 55.241 0.2 . 609 136 136 ALA CB C 17.726 0.2 . 610 136 136 ALA N N 123.880 0.1 . 611 137 137 LYS H H 7.694 0.02 . 612 137 137 LYS C C 179.025 0.2 . 613 137 137 LYS CA C 59.280 0.2 . 614 137 137 LYS CB C 31.785 0.2 . 615 137 137 LYS N N 120.446 0.1 . 616 138 138 LEU H H 7.300 0.02 . 617 138 138 LEU C C 178.673 0.2 . 618 138 138 LEU CA C 58.011 0.2 . 619 138 138 LEU CB C 40.813 0.2 . 620 138 138 LEU N N 122.566 0.1 . 621 139 139 VAL H H 8.790 0.02 . 622 139 139 VAL C C 177.648 0.2 . 623 139 139 VAL CA C 67.458 0.2 . 624 139 139 VAL N N 121.533 0.1 . 625 140 140 ALA H H 7.958 0.02 . 626 140 140 ALA C C 180.249 0.2 . 627 140 140 ALA CA C 54.287 0.2 . 628 140 140 ALA CB C 17.954 0.2 . 629 140 140 ALA N N 121.695 0.1 . 630 141 141 VAL H H 7.231 0.02 . 631 141 141 VAL C C 175.664 0.2 . 632 141 141 VAL CA C 65.739 0.2 . 633 141 141 VAL CB C 30.496 0.2 . 634 141 141 VAL N N 120.952 0.1 . 635 142 142 VAL H H 5.914 0.02 . 636 142 142 VAL C C 178.523 0.2 . 637 142 142 VAL CA C 64.334 0.2 . 638 142 142 VAL CB C 29.314 0.2 . 639 142 142 VAL N N 115.643 0.1 . 640 143 143 GLN H H 8.271 0.02 . 641 143 143 GLN C C 177.346 0.2 . 642 143 143 GLN CA C 60.068 0.2 . 643 143 143 GLN CB C 30.132 0.2 . 644 143 143 GLN N N 115.858 0.1 . 645 144 144 ALA H H 6.959 0.02 . 646 144 144 ALA C C 176.591 0.2 . 647 144 144 ALA CA C 53.823 0.2 . 648 144 144 ALA CB C 17.553 0.2 . 649 144 144 ALA N N 119.209 0.1 . 650 145 145 ALA H H 7.101 0.02 . 651 145 145 ALA C C 175.756 0.2 . 652 145 145 ALA CA C 51.267 0.2 . 653 145 145 ALA CB C 19.763 0.2 . 654 145 145 ALA N N 120.394 0.1 . 655 146 146 LEU H H 6.531 0.02 . 656 146 146 LEU C C 181.640 0.2 . 657 146 146 LEU CA C 55.605 0.2 . 658 146 146 LEU CB C 42.984 0.2 . 659 146 146 LEU N N 124.321 0.1 . stop_ save_