data_15162 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Chemical Shift Assignments of Cholera Toxin Enzymatic Domain (1-167) ; _BMRB_accession_number 15162 _BMRB_flat_file_name bmr15162.str _Entry_type original _Submission_date 2007-03-06 _Accession_date 2007-03-06 _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 Ampapathi Ravi S. . 2 Lou 'In Hye' . . 3 Creath Andrea L. . 4 Blanke Steven R. . 5 Legge Glen B. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 131 "13C chemical shifts" 390 "15N chemical shifts" 131 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-02 update BMRB 'complete entry citation' 2007-06-20 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Order-disorder-order transitions mediate the activation of cholera toxin' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18272180 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ampapathi Ravi S. . 2 Creath Andrea L. . 3 Lou Dianne I. . 4 Craft John W. . 5 Blanke Steven R. . 6 Legge Glen B. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 377 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 748 _Page_last 60 _Year 2008 _Details . loop_ _Keyword Activation Cholera Folding NMR 'Retro translocation' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CTA1-T2 _Enzyme_commission_number 2.4.2.36 loop_ _Mol_system_component_name _Mol_label CTA1-T2 $CTA1-T2 stop_ _System_molecular_weight 18891.8 _System_physical_state 'molten globule' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CTA1-T2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CTA1-T2 _Molecular_mass 18891.8 _Mol_thiol_state 'not present' loop_ _Biological_function 'Vibrio Cholerare Primary virulance factor (ADP-ribosyl transferase)' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 167 _Mol_residue_sequence ; NDDKLYRADSRPPDEIKQSG GLMPRGQSDYFDRGTQMNIN LYDHARGTQTGFVRHDDGYV STSISLRSAHLVGQTILSGH STYYIYVIATAPNMFNVNDV LGAYSPHPDEQDVSALGGIP YSQIVGWYRVHFGVLDEQLH RNRGYRDRYYSNLDIAPAAD GYGLAGF ; loop_ _Residue_seq_code _Residue_label 1 ASN 2 ASP 3 ASP 4 LYS 5 LEU 6 TYR 7 ARG 8 ALA 9 ASP 10 SER 11 ARG 12 PRO 13 PRO 14 ASP 15 GLU 16 ILE 17 LYS 18 GLN 19 SER 20 GLY 21 GLY 22 LEU 23 MET 24 PRO 25 ARG 26 GLY 27 GLN 28 SER 29 ASP 30 TYR 31 PHE 32 ASP 33 ARG 34 GLY 35 THR 36 GLN 37 MET 38 ASN 39 ILE 40 ASN 41 LEU 42 TYR 43 ASP 44 HIS 45 ALA 46 ARG 47 GLY 48 THR 49 GLN 50 THR 51 GLY 52 PHE 53 VAL 54 ARG 55 HIS 56 ASP 57 ASP 58 GLY 59 TYR 60 VAL 61 SER 62 THR 63 SER 64 ILE 65 SER 66 LEU 67 ARG 68 SER 69 ALA 70 HIS 71 LEU 72 VAL 73 GLY 74 GLN 75 THR 76 ILE 77 LEU 78 SER 79 GLY 80 HIS 81 SER 82 THR 83 TYR 84 TYR 85 ILE 86 TYR 87 VAL 88 ILE 89 ALA 90 THR 91 ALA 92 PRO 93 ASN 94 MET 95 PHE 96 ASN 97 VAL 98 ASN 99 ASP 100 VAL 101 LEU 102 GLY 103 ALA 104 TYR 105 SER 106 PRO 107 HIS 108 PRO 109 ASP 110 GLU 111 GLN 112 ASP 113 VAL 114 SER 115 ALA 116 LEU 117 GLY 118 GLY 119 ILE 120 PRO 121 TYR 122 SER 123 GLN 124 ILE 125 VAL 126 GLY 127 TRP 128 TYR 129 ARG 130 VAL 131 HIS 132 PHE 133 GLY 134 VAL 135 LEU 136 ASP 137 GLU 138 GLN 139 LEU 140 HIS 141 ARG 142 ASN 143 ARG 144 GLY 145 TYR 146 ARG 147 ASP 148 ARG 149 TYR 150 TYR 151 SER 152 ASN 153 LEU 154 ASP 155 ILE 156 ALA 157 PRO 158 ALA 159 ALA 160 ASP 161 GLY 162 TYR 163 GLY 164 LEU 165 ALA 166 GLY 167 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 1S5B "Cholera Holotoxin With An A-Subunit Y30s Mutation Form 3" 100.00 240 97.60 98.80 8.51e-114 PDB 1S5C "Cholera Holotoxin With An A-Subunit Y30s Mutation, Crystal Form 1" 100.00 240 97.60 98.80 8.51e-114 PDB 1S5D "Cholera Holotoxin With An A-Subunit Y30s Mutation, Crystal Form 2" 100.00 240 97.60 98.80 8.51e-114 PDB 1S5E "Cholera Holotoxin, Crystal Form 1" 100.00 240 98.20 99.40 8.50e-115 PDB 1S5F "Cholera Holotoxin, Crystal Form 2" 100.00 240 98.20 99.40 8.50e-115 PDB 1XTC "Cholera Toxin" 100.00 194 97.01 99.40 6.59e-114 PDB 2A5D "Structural Basis For The Activation Of Cholera Toxin By Human Arf6-Gtp" 100.00 193 98.20 99.40 3.45e-114 PDB 2A5F "Cholera Toxin A1 Subunit Bound To Its Substrate, Nad+, And Its Human Protein Activator, Arf6" 100.00 193 98.20 99.40 3.45e-114 PDB 2A5G "Cholera Toxin A1 Subunit Bound To Arf6(Q67l)" 100.00 193 98.20 99.40 3.45e-114 DBJ BAA06288 "cholera toxin [Vibrio cholerae O37]" 100.00 258 97.60 99.40 1.87e-114 DBJ BAA06290 "cholera toxin [Vibrio cholerae O139]" 100.00 258 98.20 99.40 6.77e-115 DBJ BAG06738 "cholera toxin A subunit [Vibrio phage CTX]" 71.26 192 98.32 99.16 2.92e-77 DBJ BAG66065 "cholera toxin A subunit [Vibrio phage CTX]" 62.87 178 98.10 99.05 2.14e-66 DBJ BAI50777 "cholera enterotoxin subunit A, partial [Vibrio cholerae O1]" 71.26 192 98.32 99.16 2.92e-77 EMBL CAA24995 "unnamed protein product [Vibrio cholerae]" 100.00 258 98.20 99.40 7.23e-115 EMBL CAA41590 "cholera toxin A protein (CTA) [Vibrio cholerae]" 100.00 258 98.20 99.40 6.77e-115 EMBL CAA41592 "cholera toxin A protein (CTA) [Vibrio cholerae]" 100.00 258 98.20 99.40 6.77e-115 EMBL CAE11218 "enterotoxin subunit A [Vibrio cholerae]" 100.00 258 97.01 99.40 1.07e-113 EMBL CRZ40571 "cholera enterotoxin%2C A subunit [Vibrio cholerae]" 100.00 258 98.20 99.40 6.77e-115 GB AAA27514 "enterotoxin prepeptide, partial [Vibrio cholerae]" 100.00 212 98.20 99.40 9.60e-115 GB AAD51359 "cholera enterotoxin A-subunit [Vibrio cholerae]" 100.00 258 98.20 99.40 6.77e-115 GB AAF94614 "cholera enterotoxin, A subunit [Vibrio cholerae O1 biovar El Tor str. N16961]" 100.00 258 98.20 99.40 6.77e-115 GB AAL09681 "CtxA [Vibrio phage CTX]" 100.00 258 98.20 99.40 6.77e-115 GB AAL60525 "CtxA [Vibrio cholerae]" 100.00 258 97.60 99.40 1.87e-114 PRF 1001196A toxin,cholera 100.00 382 98.20 99.40 3.19e-115 REF NP_231100 "cholera enterotoxin subunit A [Vibrio cholerae O1 biovar El Tor str. N16961]" 100.00 258 98.20 99.40 6.77e-115 REF WP_001881225 "enterotoxin [Vibrio cholerae]" 100.00 258 98.20 99.40 6.77e-115 REF WP_001888508 "MULTISPECIES: enterotoxin [Vibrio]" 100.00 258 97.60 99.40 1.87e-114 REF WP_001911232 "enterotoxin [Vibrio cholerae]" 100.00 258 97.01 98.80 2.13e-113 REF WP_005514365 "enterotoxin [Vibrio mimicus]" 100.00 258 97.60 99.40 2.18e-114 SP P01555 "RecName: Full=Cholera enterotoxin subunit A; AltName: Full=Cholera enterotoxin, A chain; Contains: RecName: Full=Cholera entero" 100.00 258 98.20 99.40 6.77e-115 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CTA1-T2 'Vibrio comma' 666 Bacteria . Vibrio cholerae 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 $CTA1-T2 'recombinant technology' . Escherichia coli BL21DE3 pET-20(b) ; Recombinant protein was refolded from inclusion bodies. Full length, refolded CTA1 binds its CTA2, ARF6 and NAD+ ligands. HSQC spectra are presented in the published article. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; Sample was stable at higher salts (200mM) and at lower temperatures (288K). Sample required 100% deuteration to acheive concentrationr anges of 0.2 mM required for NMR heteronuclear studies. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CTA1-T2 0.2 mM . TRIS 20 mM '[U-99% 2H]' 'sodium chloride' 200 mM 'natural abundance' D2O 6 '% v/v' '[U-99% 2H]' 'sodium azide' 0.05 '% w/v' 'natural abundance' EDTA 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Vendor _Address _Electronic_address Goddard 'University of California, San Francisco' sparky@cgl.ucsf.edu stop_ loop_ _Task 'data analysis' 'peak picking' stop_ _Details ; Peak picking and analysis software from UCSF. http://www.cgl.ucsf.edu/home/sparky/ ; save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 'Script Version 2002.044.17.08' loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' NIH http://spin.niddk.nih.gov/bax/software stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version 'Script Version 2002.044.17.08' loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' NIH http://spin.niddk.nih.gov/bax/software stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details 'Equipped with a cryogenic z-gradient TXI probe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details TXI-probe save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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 pH 7.2 . pH temperature 288 . 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 TSP C 13 'methyl protons' ppm 0 . indirect . . . 0.101329118 TSP H 1 'methyl protons' ppm 0 internal direct . . . 1.0 TSP N 15 'methyl protons' ppm 0 . indirect . . . 0.251449530 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 '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D CBCA(CO)NH' 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 CTA1-T2 _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 ASP C C 175.65 0.20 1 2 2 2 ASP CA C 53.92 0.20 1 3 2 2 ASP CB C 40.41 0.20 1 4 3 3 ASP H H 8.29 0.02 1 5 3 3 ASP C C 175.70 0.20 1 6 3 3 ASP CA C 54.24 0.20 1 7 3 3 ASP CB C 40.59 0.20 1 8 3 3 ASP N N 121.37 0.20 1 9 4 4 LYS H H 7.91 0.02 1 10 4 4 LYS C C 174.97 0.20 1 11 4 4 LYS CA C 53.99 0.20 1 12 4 4 LYS CB C 33.79 0.20 1 13 4 4 LYS N N 120.28 0.20 1 14 5 5 LEU H H 8.59 0.02 1 15 5 5 LEU C C 175.53 0.20 1 16 5 5 LEU CA C 52.79 0.20 1 17 5 5 LEU CB C 44.63 0.20 1 18 5 5 LEU N N 119.55 0.20 1 19 6 6 TYR H H 8.46 0.02 1 20 6 6 TYR C C 175.81 0.20 1 21 6 6 TYR CA C 56.64 0.20 1 22 6 6 TYR CB C 42.49 0.20 1 23 6 6 TYR N N 116.14 0.20 1 24 7 7 ARG H H 9.32 0.02 1 25 7 7 ARG C C 174.88 0.20 1 26 7 7 ARG CA C 53.90 0.20 1 27 7 7 ARG CB C 33.66 0.20 1 28 7 7 ARG N N 122.72 0.20 1 29 8 8 ALA H H 9.40 0.02 1 30 8 8 ALA C C 176.84 0.20 1 31 8 8 ALA CA C 51.50 0.20 1 32 8 8 ALA CB C 17.76 0.20 1 33 8 8 ALA N N 133.90 0.20 1 34 9 9 ASP H H 10.16 0.02 1 35 9 9 ASP C C 174.34 0.20 1 36 9 9 ASP CA C 54.13 0.20 1 37 9 9 ASP CB C 47.89 0.20 1 38 9 9 ASP N N 122.39 0.20 1 39 10 10 SER H H 8.72 0.02 1 40 10 10 SER C C 174.85 0.20 1 41 10 10 SER CA C 59.59 0.20 1 42 10 10 SER CB C 62.27 0.20 1 43 10 10 SER N N 120.10 0.20 1 44 11 11 ARG H H 9.60 0.02 1 45 11 11 ARG CA C 54.49 0.20 1 46 11 11 ARG CB C 29.51 0.20 1 47 11 11 ARG N N 128.49 0.20 1 48 13 13 PRO C C 178.55 0.20 1 49 13 13 PRO CA C 65.46 0.20 1 50 13 13 PRO CB C 30.69 0.20 1 51 14 14 ASP H H 8.53 0.02 1 52 14 14 ASP C C 178.57 0.20 1 53 14 14 ASP CA C 56.42 0.20 1 54 14 14 ASP CB C 39.19 0.20 1 55 14 14 ASP N N 114.70 0.20 1 56 15 15 GLU H H 7.18 0.02 1 57 15 15 GLU C C 178.80 0.20 1 58 15 15 GLU CA C 58.41 0.20 1 59 15 15 GLU CB C 28.48 0.20 1 60 15 15 GLU N N 122.51 0.20 1 61 16 16 ILE H H 7.40 0.02 1 62 16 16 ILE C C 173.58 0.20 1 63 16 16 ILE CA C 61.63 0.20 1 64 16 16 ILE CB C 34.47 0.20 1 65 16 16 ILE N N 120.50 0.20 1 66 17 17 LYS H H 8.09 0.02 1 67 17 17 LYS C C 179.81 0.20 1 68 17 17 LYS CA C 57.62 0.20 1 69 17 17 LYS CB C 39.06 0.20 1 70 17 17 LYS N N 120.58 0.20 1 71 18 18 GLN H H 7.46 0.02 1 72 18 18 GLN C C 178.01 0.20 1 73 18 18 GLN CA C 58.20 0.20 1 74 18 18 GLN CB C 27.60 0.20 1 75 18 18 GLN N N 118.80 0.20 1 76 19 19 SER H H 7.94 0.02 1 77 19 19 SER C C 173.33 0.20 1 78 19 19 SER CA C 59.80 0.20 1 79 19 19 SER CB C 63.73 0.20 1 80 19 19 SER N N 113.40 0.20 1 81 20 20 GLY H H 7.59 0.02 1 82 20 20 GLY C C 174.71 0.20 1 83 20 20 GLY CA C 44.57 0.20 1 84 20 20 GLY N N 107.20 0.20 1 85 21 21 GLY H H 8.08 0.02 1 86 21 21 GLY C C 171.47 0.20 1 87 21 21 GLY CA C 44.04 0.20 1 88 21 21 GLY N N 106.30 0.20 1 89 22 22 LEU H H 8.51 0.02 1 90 22 22 LEU C C 174.94 0.20 1 91 22 22 LEU CA C 53.58 0.20 1 92 22 22 LEU CB C 43.00 0.20 1 93 22 22 LEU N N 121.12 0.20 1 94 23 23 MET H H 8.42 0.02 1 95 23 23 MET CA C 51.62 0.20 1 96 23 23 MET CB C 30.62 0.20 1 97 23 23 MET N N 123.29 0.20 1 98 25 25 ARG C C 179.31 0.20 1 99 25 25 ARG CA C 56.49 0.20 1 100 25 25 ARG CB C 30.56 0.20 1 101 26 26 GLY H H 8.65 0.02 1 102 26 26 GLY C C 175.47 0.20 1 103 26 26 GLY CA C 47.06 0.20 1 104 26 26 GLY N N 109.45 0.20 1 105 27 27 GLN H H 8.53 0.02 1 106 27 27 GLN C C 177.30 0.20 1 107 27 27 GLN CA C 56.90 0.20 1 108 27 27 GLN CB C 29.38 0.20 1 109 27 27 GLN N N 117.55 0.20 1 110 28 28 SER H H 7.68 0.02 1 111 28 28 SER C C 172.47 0.20 1 112 28 28 SER CA C 64.90 0.20 1 113 28 28 SER CB C 68.92 0.20 1 114 28 28 SER N N 113.84 0.20 1 115 29 29 ASP H H 8.01 0.02 1 116 29 29 ASP C C 175.45 0.20 1 117 29 29 ASP CA C 57.45 0.20 1 118 29 29 ASP CB C 40.38 0.20 1 119 29 29 ASP N N 124.35 0.20 1 120 30 30 TYR H H 7.98 0.02 1 121 30 30 TYR C C 175.32 0.20 1 122 30 30 TYR CA C 57.57 0.20 1 123 30 30 TYR CB C 38.56 0.20 1 124 30 30 TYR N N 121.40 0.20 1 125 31 31 PHE H H 7.98 0.02 1 126 31 31 PHE C C 174.86 0.20 1 127 31 31 PHE CA C 57.47 0.20 1 128 31 31 PHE CB C 39.13 0.20 1 129 31 31 PHE N N 121.88 0.20 1 130 32 32 ASP H H 8.28 0.02 1 131 32 32 ASP C C 176.20 0.20 1 132 32 32 ASP CA C 53.87 0.20 1 133 32 32 ASP CB C 40.87 0.20 1 134 32 32 ASP N N 122.86 0.20 1 135 33 33 ARG H H 8.35 0.02 1 136 33 33 ARG C C 177.18 0.20 1 137 33 33 ARG CA C 56.45 0.20 1 138 33 33 ARG CB C 29.50 0.20 1 139 33 33 ARG N N 122.82 0.20 1 140 34 34 GLY H H 8.48 0.02 1 141 34 34 GLY C C 174.76 0.20 1 142 34 34 GLY CA C 45.44 0.20 1 143 34 34 GLY N N 109.14 0.20 1 144 35 35 THR H H 7.98 0.02 1 145 35 35 THR C C 174.84 0.20 1 146 35 35 THR CA C 61.90 0.20 1 147 36 35 THR CB C 69.40 0.20 1 148 35 35 THR N N 113.80 0.20 1 149 36 36 GLN H H 8.37 0.02 1 150 36 36 GLN C C 175.84 0.20 1 151 36 36 GLN CA C 55.90 0.20 1 152 37 36 GLN CB C 28.40 0.20 1 153 36 36 GLN N N 122.30 0.20 1 154 37 37 MET H H 8.27 0.02 1 155 37 37 MET C C 175.87 0.20 1 156 37 37 MET CA C 55.40 0.20 1 157 37 37 MET CB C 32.24 0.20 1 158 37 37 MET N N 120.90 0.20 1 159 38 38 ASN H H 8.42 0.02 1 160 38 38 ASN C C 175.31 0.20 1 161 38 38 ASN CA C 53.30 0.20 1 162 38 38 ASN CB C 38.40 0.20 1 163 38 38 ASN N N 119.90 0.20 1 164 39 39 ILE H H 8.12 0.02 1 165 39 39 ILE C C 177.16 0.20 1 166 39 39 ILE CA C 55.20 0.20 1 167 39 39 ILE CB C 41.34 0.20 1 168 39 39 ILE N N 122.60 0.20 1 169 40 40 ASN H H 8.02 0.02 1 170 40 40 ASN C C 175.61 0.20 1 171 40 40 ASN CA C 57.80 0.20 1 172 40 40 ASN CB C 38.00 0.20 1 173 40 40 ASN N N 119.50 0.20 1 174 41 41 LEU H H 8.08 0.02 1 175 41 41 LEU C C 177.95 0.20 1 176 41 41 LEU CA C 57.60 0.20 1 177 41 41 LEU CB C 40.43 0.20 1 178 41 41 LEU N N 122.00 0.20 1 179 42 42 TYR H H 8.26 0.02 1 180 42 42 TYR C C 174.10 0.20 1 181 42 42 TYR CA C 58.60 0.20 1 182 42 42 TYR CB C 28.82 0.20 1 183 42 42 TYR N N 117.27 0.20 1 184 43 43 ASP H H 8.04 0.02 1 185 43 43 ASP C C 177.30 0.20 1 186 43 43 ASP CA C 54.70 0.20 1 187 43 43 ASP CB C 41.50 0.20 1 188 43 43 ASP N N 123.80 0.20 1 189 44 44 HIS H H 8.31 0.02 1 190 44 44 HIS C C 175.57 0.20 1 191 44 44 HIS CA C 56.70 0.20 1 192 44 44 HIS CB C 29.60 0.20 1 193 44 44 HIS N N 124.70 0.20 1 194 45 45 ALA H H 8.22 0.02 1 195 45 45 ALA C C 178.14 0.20 1 196 45 45 ALA CA C 52.70 0.20 1 197 45 45 ALA CB C 18.30 0.20 1 198 45 45 ALA N N 123.82 0.20 1 199 46 46 ARG H H 8.14 0.02 1 200 46 46 ARG C C 177.10 0.20 1 201 46 46 ARG CA C 56.22 0.20 1 202 46 46 ARG CB C 29.85 0.20 1 203 46 46 ARG N N 119.70 0.20 1 204 47 47 GLY H H 8.31 0.02 1 205 47 47 GLY C C 174.50 0.20 1 206 47 47 GLY CA C 45.20 0.20 1 207 47 47 GLY N N 109.65 0.20 1 208 48 48 THR H H 8.06 0.02 1 209 48 48 THR C C 174.80 0.20 1 210 48 48 THR CA C 61.66 0.20 1 211 48 48 THR CB C 69.44 0.20 1 212 48 48 THR N N 113.80 0.20 1 213 49 49 GLN H H 8.50 0.02 1 214 49 49 GLN C C 176.20 0.20 1 215 49 49 GLN CA C 55.70 0.20 1 216 49 49 GLN CB C 28.70 0.20 1 217 49 49 GLN N N 122.90 0.20 1 218 50 50 THR H H 8.22 0.02 1 219 50 50 THR C C 174.50 0.20 1 220 50 50 THR CA C 61.80 0.20 1 221 50 50 THR CB C 69.43 0.20 1 222 50 50 THR N N 115.20 0.20 1 223 51 51 GLY H H 8.37 0.02 1 224 51 51 GLY C C 174.94 0.20 1 225 51 51 GLY CA C 45.03 0.20 1 226 51 51 GLY N N 111.15 0.20 1 227 52 52 PHE H H 8.10 0.02 1 228 52 52 PHE C C 175.18 0.20 1 229 52 52 PHE CA C 57.50 0.20 1 230 52 52 PHE CB C 39.21 0.20 1 231 52 52 PHE N N 120.77 0.20 1 232 53 53 VAL H H 8.03 0.02 1 233 53 53 VAL C C 175.05 0.20 1 234 53 53 VAL CA C 61.39 0.20 1 235 53 53 VAL CB C 32.62 0.20 1 236 53 53 VAL N N 123.20 0.20 1 237 54 54 ARG H H 8.38 0.02 1 238 54 54 ARG C C 176.42 0.20 1 239 54 54 ARG CA C 55.50 0.20 1 240 54 54 ARG CB C 30.42 0.20 1 241 54 54 ARG N N 125.39 0.20 1 242 55 55 HIS H H 8.38 0.02 1 243 55 55 HIS C C 176.50 0.20 1 244 55 55 HIS CA C 55.52 0.20 1 245 55 55 HIS CB C 30.40 0.20 1 246 55 55 HIS N N 125.40 0.20 1 247 56 56 ASP H H 8.48 0.02 1 248 56 56 ASP C C 174.45 0.20 1 249 56 56 ASP CA C 53.33 0.20 1 250 56 56 ASP CB C 38.13 0.20 1 251 56 56 ASP N N 118.20 0.20 1 252 57 57 ASP H H 8.49 0.02 1 253 57 57 ASP C C 176.33 0.20 1 254 57 57 ASP CA C 53.97 0.20 1 255 57 57 ASP CB C 40.60 0.20 1 256 57 57 ASP N N 121.11 0.20 1 257 58 58 GLY H H 8.42 0.02 1 258 58 58 GLY C C 176.40 0.20 1 259 58 58 GLY CA C 45.11 0.20 1 260 58 58 GLY N N 109.15 0.20 1 261 59 59 TYR H H 8.04 0.02 1 262 59 59 TYR C C 178.01 0.20 1 263 59 59 TYR CA C 54.74 0.20 1 264 59 59 TYR CB C 41.50 0.20 1 265 59 59 TYR N N 115.23 0.20 1 266 60 60 VAL H H 8.04 0.02 1 267 60 60 VAL C C 175.50 0.20 1 268 60 60 VAL CA C 57.83 0.20 1 269 60 60 VAL CB C 38.02 0.20 1 270 60 60 VAL N N 119.60 0.20 1 271 61 61 SER H H 8.19 0.02 1 272 61 61 SER CA C 57.86 0.20 1 273 61 61 SER CB C 63.22 0.20 1 274 61 61 SER N N 117.61 0.20 1 275 62 62 THR C C 175.00 0.20 1 276 63 63 SER C C 175.00 0.20 1 277 65 65 SER H H 7.98 0.02 1 278 65 65 SER CA C 55.15 0.20 1 279 65 65 SER CB C 63.22 0.20 1 280 65 65 SER N N 120.82 0.20 1 281 68 68 SER C C 176.74 0.20 1 282 68 68 SER CA C 61.98 0.20 1 283 69 69 ALA H H 8.02 0.02 1 284 69 69 ALA C C 179.50 0.20 1 285 69 69 ALA CA C 54.58 0.20 1 286 69 69 ALA CB C 18.93 0.20 1 287 69 69 ALA N N 125.27 0.20 1 288 70 70 HIS H H 8.59 0.02 1 289 70 70 HIS C C 176.85 0.20 1 290 70 70 HIS CA C 57.60 0.20 1 291 70 70 HIS CB C 31.15 0.20 1 292 70 70 HIS N N 120.14 0.20 1 293 71 71 LEU H H 8.55 0.02 1 294 71 71 LEU C C 175.80 0.20 1 295 71 71 LEU CA C 58.00 0.20 1 296 71 71 LEU CB C 29.70 0.20 1 297 71 71 LEU N N 123.40 0.20 1 298 72 72 VAL H H 8.20 0.02 1 299 72 72 VAL CA C 55.56 0.20 1 300 72 72 VAL CB C 30.54 0.20 1 301 72 72 VAL N N 120.30 0.20 1 302 73 73 GLY H H 8.34 0.02 1 303 73 73 GLY C C 176.60 0.20 1 304 73 73 GLY CA C 46.30 0.20 1 305 73 73 GLY N N 116.20 0.20 1 306 74 74 GLN H H 8.46 0.02 1 307 74 74 GLN C C 179.25 0.20 1 308 74 74 GLN CA C 53.40 0.20 1 309 74 74 GLN N N 117.90 0.20 1 310 75 75 THR H H 7.98 0.02 1 311 75 75 THR C C 176.60 0.20 1 312 75 75 THR CA C 61.86 0.20 1 313 75 75 THR CB C 69.39 0.20 1 314 75 75 THR N N 115.21 0.20 1 315 76 76 ILE H H 8.10 0.02 1 316 76 76 ILE C C 175.80 0.20 1 317 76 76 ILE CA C 61.31 0.20 1 318 76 76 ILE CB C 38.06 0.20 1 319 76 76 ILE N N 124.92 0.20 1 320 77 77 LEU H H 8.48 0.02 1 321 77 77 LEU C C 177.28 0.20 1 322 77 77 LEU CA C 53.25 0.20 1 323 77 77 LEU CB C 38.37 0.20 1 324 77 77 LEU N N 121.81 0.20 1 325 78 78 SER H H 7.26 0.02 1 326 78 78 SER C C 175.71 0.20 1 327 78 78 SER CA C 60.50 0.20 1 328 78 78 SER CB C 62.56 0.20 1 329 78 78 SER N N 114.06 0.20 1 330 79 79 GLY H H 8.83 0.02 1 331 79 79 GLY C C 174.12 0.20 1 332 79 79 GLY CA C 44.75 0.20 1 333 79 79 GLY N N 110.64 0.20 1 334 80 80 HIS H H 8.40 0.02 1 335 80 80 HIS C C 176.26 0.20 1 336 80 80 HIS CA C 55.91 0.20 1 337 80 80 HIS CB C 28.92 0.20 1 338 80 80 HIS N N 120.40 0.20 1 339 81 81 SER H H 8.49 0.02 1 340 81 81 SER C C 174.60 0.20 1 341 81 81 SER CA C 58.61 0.20 1 342 81 81 SER CB C 63.20 0.20 1 343 81 81 SER N N 116.90 0.20 1 344 82 82 THR H H 7.98 0.02 1 345 82 82 THR C C 173.77 0.20 1 346 82 82 THR CA C 61.60 0.20 1 347 82 82 THR CB C 71.30 0.20 1 348 82 82 THR N N 117.00 0.20 1 349 83 83 TYR H H 8.64 0.02 1 350 83 83 TYR C C 169.71 0.20 1 351 83 83 TYR CA C 56.70 0.20 1 352 83 83 TYR CB C 38.40 0.20 1 353 83 83 TYR N N 122.50 0.20 1 354 84 84 TYR H H 8.58 0.02 1 355 84 84 TYR C C 174.73 0.20 1 356 84 84 TYR CA C 56.60 0.20 1 357 84 84 TYR CB C 42.40 0.20 1 358 84 84 TYR N N 117.30 0.20 1 359 85 85 ILE H H 9.29 0.02 1 360 85 85 ILE C C 175.85 0.20 1 361 85 85 ILE CA C 60.20 0.20 1 362 85 85 ILE CB C 39.30 0.20 1 363 85 85 ILE N N 119.80 0.20 1 364 86 86 TYR H H 9.34 0.02 1 365 86 86 TYR C C 174.62 0.20 1 366 86 86 TYR CA C 60.00 0.20 1 367 86 86 TYR CB C 39.90 0.20 1 368 86 86 TYR N N 127.00 0.20 1 369 87 87 VAL H H 9.18 0.02 1 370 87 87 VAL C C 175.10 0.20 1 371 87 87 VAL CA C 61.40 0.20 1 372 87 87 VAL CB C 31.50 0.20 1 373 87 87 VAL N N 123.90 0.20 1 374 88 88 ILE H H 9.43 0.02 1 375 88 88 ILE C C 174.73 0.20 1 376 88 88 ILE CA C 60.10 0.20 1 377 88 88 ILE CB C 40.73 0.20 1 378 88 88 ILE N N 130.00 0.20 1 379 89 89 ALA H H 8.59 0.02 1 380 89 89 ALA C C 176.98 0.20 1 381 89 89 ALA CA C 51.80 0.20 1 382 89 89 ALA CB C 20.54 0.20 1 383 89 89 ALA N N 128.60 0.20 1 384 90 90 THR H H 8.15 0.02 1 385 90 90 THR C C 173.95 0.20 1 386 90 90 THR CA C 61.15 0.20 1 387 90 90 THR CB C 69.69 0.20 1 388 90 90 THR N N 113.20 0.20 1 389 91 91 ALA H H 8.17 0.02 1 390 91 91 ALA CA C 50.29 0.20 1 391 91 91 ALA CB C 18.10 0.20 1 392 91 91 ALA N N 126.00 0.20 1 393 92 92 PRO C C 174.20 0.20 1 394 92 92 PRO CA C 60.35 0.20 1 395 92 92 PRO CB C 38.17 0.20 1 396 93 93 ASN H H 8.15 0.02 1 397 93 93 ASN C C 174.88 0.20 1 398 93 93 ASN CA C 54.94 0.20 1 399 93 93 ASN CB C 38.40 0.20 1 400 93 93 ASN N N 128.11 0.20 1 401 94 94 MET H H 7.70 0.02 1 402 94 94 MET C C 174.75 0.20 1 403 94 94 MET CA C 61.09 0.20 1 404 94 94 MET CB C 36.66 0.20 1 405 94 94 MET N N 120.64 0.20 1 406 95 95 PHE H H 9.20 0.02 1 407 95 95 PHE C C 175.84 0.20 1 408 95 95 PHE CA C 59.59 0.20 1 409 95 95 PHE CB C 39.44 0.20 1 410 95 95 PHE N N 131.85 0.20 1 411 96 96 ASN H H 8.28 0.02 1 412 96 96 ASN C C 176.20 0.20 1 413 96 96 ASN CA C 53.90 0.20 1 414 96 96 ASN CB C 40.78 0.20 1 415 96 96 ASN N N 122.86 0.20 1 416 97 97 VAL H H 8.35 0.02 1 417 97 97 VAL C C 174.52 0.20 1 418 97 97 VAL CA C 58.96 0.20 1 419 97 97 VAL CB C 29.63 0.20 1 420 97 97 VAL N N 122.80 0.20 1 421 98 98 ASN H H 8.42 0.02 1 422 98 98 ASN C C 175.64 0.20 1 423 98 98 ASN CA C 54.16 0.20 1 424 98 98 ASN CB C 40.55 0.20 1 425 98 98 ASN N N 122.48 0.20 1 426 99 99 ASP H H 8.30 0.02 1 427 99 99 ASP C C 176.35 0.20 1 428 99 99 ASP CA C 54.24 0.20 1 429 99 99 ASP CB C 40.59 0.20 1 430 99 99 ASP N N 121.30 0.20 1 431 100 100 VAL H H 8.02 0.02 1 432 100 100 VAL C C 176.62 0.20 1 433 100 100 VAL CA C 62.53 0.20 1 434 100 100 VAL CB C 31.74 0.20 1 435 100 100 VAL N N 120.35 0.20 1 436 101 101 LEU H H 8.27 0.02 1 437 101 101 LEU C C 178.10 0.20 1 438 101 101 LEU CA C 55.29 0.20 1 439 101 101 LEU CB C 41.10 0.20 1 440 101 101 LEU N N 124.26 0.20 1 441 102 102 GLY H H 8.25 0.02 1 442 102 102 GLY C C 175.54 0.20 1 443 102 102 GLY CA C 45.12 0.20 1 444 102 102 GLY N N 110.02 0.20 1 445 103 103 ALA H H 8.12 0.02 1 446 103 103 ALA C C 177.65 0.20 1 447 103 103 ALA CA C 52.22 0.20 1 448 103 103 ALA CB C 18.70 0.20 1 449 103 103 ALA N N 123.90 0.20 1 450 104 104 TYR H H 8.26 0.02 1 451 104 104 TYR C C 174.68 0.20 1 452 104 104 TYR CA C 54.20 0.20 1 453 104 104 TYR CB C 40.70 0.20 1 454 104 104 TYR N N 119.50 0.20 1 455 105 105 SER H H 7.87 0.02 1 456 105 105 SER CA C 60.40 0.20 1 457 105 105 SER CB C 63.90 0.20 1 458 105 105 SER N N 116.60 0.20 1 459 120 120 PRO C C 176.60 0.20 1 460 120 120 PRO CA C 62.50 0.20 1 461 120 120 PRO CB C 32.20 0.20 1 462 121 121 TYR H H 8.11 0.02 1 463 121 121 TYR C C 176.20 0.20 1 464 121 121 TYR CA C 61.30 0.20 1 465 121 121 TYR CB C 38.10 0.20 1 466 121 121 TYR N N 124.90 0.20 1 467 122 122 SER H H 8.58 0.02 1 468 122 122 SER C C 174.80 0.20 1 469 122 122 SER CA C 59.50 0.20 1 470 122 122 SER CB C 62.25 0.20 1 471 122 122 SER N N 110.30 0.20 1 472 123 123 GLN H H 9.60 0.02 1 473 123 123 GLN C C 174.90 0.20 1 474 123 123 GLN CA C 54.50 0.20 1 475 123 123 GLN CB C 29.50 0.20 1 476 123 123 GLN N N 128.40 0.20 1 477 124 124 ILE H H 7.70 0.02 1 478 124 124 ILE C C 175.00 0.20 1 479 124 124 ILE CA C 61.10 0.20 1 480 124 124 ILE CB C 36.70 0.20 1 481 124 124 ILE N N 120.70 0.20 1 482 125 125 VAL H H 8.47 0.02 1 483 125 125 VAL C C 177.26 0.20 1 484 125 125 VAL CA C 59.62 0.20 1 485 125 125 VAL CB C 39.34 0.20 1 486 125 125 VAL N N 115.00 0.20 1 487 126 126 GLY H H 7.93 0.02 1 488 126 126 GLY C C 169.93 0.20 1 489 126 126 GLY CA C 45.62 0.20 1 490 126 126 GLY N N 104.47 0.20 1 491 127 127 TRP H H 8.30 0.02 1 492 127 127 TRP C C 173.70 0.20 1 493 127 127 TRP CA C 55.34 0.20 1 494 127 127 TRP CB C 30.31 0.20 1 495 127 127 TRP N N 117.68 0.20 1 496 128 128 TYR H H 9.07 0.02 1 497 128 128 TYR C C 175.57 0.20 1 498 128 128 TYR CA C 55.73 0.20 1 499 128 128 TYR CB C 40.96 0.20 1 500 128 128 TYR N N 117.42 0.20 1 501 129 129 ARG H H 8.26 0.02 1 502 129 129 ARG C C 173.79 0.20 1 503 129 129 ARG CA C 55.44 0.20 1 504 129 129 ARG CB C 32.24 0.20 1 505 129 129 ARG N N 124.95 0.20 1 506 130 130 VAL H H 8.26 0.02 1 507 130 130 VAL C C 174.69 0.20 1 508 130 130 VAL CA C 60.60 0.20 1 509 130 130 VAL CB C 30.38 0.20 1 510 130 130 VAL N N 124.95 0.20 1 511 131 131 HIS H H 8.14 0.02 1 512 131 131 HIS C C 175.34 0.20 1 513 131 131 HIS CA C 53.76 0.20 1 514 131 131 HIS CB C 31.79 0.20 1 515 131 131 HIS N N 126.21 0.20 1 516 132 132 PHE H H 9.64 0.02 1 517 132 132 PHE C C 176.40 0.20 1 518 132 132 PHE CA C 58.68 0.20 1 519 132 132 PHE CB C 35.78 0.20 1 520 132 132 PHE N N 130.19 0.20 1 521 133 133 GLY H H 8.53 0.02 1 522 133 133 GLY C C 174.50 0.20 1 523 133 133 GLY CA C 44.98 0.20 1 524 133 133 GLY N N 110.70 0.20 1 525 134 134 VAL H H 7.87 0.02 1 526 134 134 VAL C C 175.90 0.20 1 527 134 134 VAL CA C 61.84 0.20 1 528 134 134 VAL CB C 31.46 0.20 1 529 134 134 VAL N N 124.60 0.20 1 530 135 135 LEU H H 8.71 0.02 1 531 135 135 LEU C C 175.20 0.20 1 532 135 135 LEU CA C 55.20 0.20 1 533 135 135 LEU CB C 41.20 0.20 1 534 135 135 LEU N N 133.70 0.20 1 535 136 136 ASP H H 8.50 0.02 1 536 136 136 ASP C C 176.90 0.20 1 537 136 136 ASP CA C 53.40 0.20 1 538 136 136 ASP CB C 40.74 0.20 1 539 136 136 ASP N N 130.10 0.20 1 540 137 137 GLU H H 8.54 0.02 1 541 137 137 GLU C C 173.71 0.20 1 542 137 137 GLU CA C 57.60 0.20 1 543 137 137 GLU CB C 28.74 0.20 1 544 137 137 GLU N N 123.82 0.20 1 545 138 138 GLN H H 8.20 0.02 1 546 138 138 GLN C C 175.40 0.20 1 547 138 138 GLN CA C 55.13 0.20 1 548 138 138 GLN CB C 28.42 0.20 1 549 138 138 GLN N N 120.50 0.20 1 550 139 139 LEU H H 8.30 0.02 1 551 139 139 LEU C C 176.19 0.20 1 552 139 139 LEU CA C 54.90 0.20 1 553 139 139 LEU CB C 40.40 0.20 1 554 139 139 LEU N N 130.23 0.20 1 555 140 140 HIS H H 8.36 0.02 1 556 140 140 HIS C C 174.10 0.20 1 557 140 140 HIS CA C 54.59 0.20 1 558 140 140 HIS CB C 28.65 0.20 1 559 140 140 HIS N N 128.84 0.20 1 560 141 141 ARG H H 8.30 0.02 1 561 141 141 ARG C C 175.46 0.20 1 562 141 141 ARG CA C 55.35 0.20 1 563 141 141 ARG CB C 28.99 0.20 1 564 141 141 ARG N N 123.42 0.20 1 565 142 142 ASN H H 7.59 0.02 1 566 142 142 ASN CA C 51.37 0.20 1 567 142 142 ASN CB C 38.15 0.20 1 568 142 142 ASN N N 120.50 0.20 1 569 149 149 TYR C C 174.20 0.20 1 570 150 150 TYR H H 8.40 0.02 1 571 150 150 TYR C C 175.50 0.20 1 572 150 150 TYR CA C 53.30 0.20 1 573 150 150 TYR CB C 38.20 0.20 1 574 150 150 TYR N N 121.30 0.20 1 575 151 151 SER H H 8.19 0.02 1 576 151 151 SER C C 174.00 0.20 1 577 151 151 SER CA C 57.90 0.20 1 578 151 151 SER CB C 63.60 0.20 1 579 151 151 SER N N 117.60 0.20 1 580 152 152 ASN H H 8.40 0.02 1 581 152 152 ASN C C 175.10 0.20 1 582 152 152 ASN CA C 53.20 0.20 1 583 152 152 ASN CB C 38.20 0.20 1 584 152 152 ASN N N 121.10 0.20 1 585 153 153 LEU H H 8.13 0.02 1 586 153 153 LEU C C 177.10 0.20 1 587 153 153 LEU CA C 55.05 0.20 1 588 153 153 LEU CB C 41.43 0.20 1 589 153 153 LEU N N 122.12 0.20 1 590 154 154 ASP H H 8.24 0.02 1 591 154 154 ASP C C 175.90 0.20 1 592 154 154 ASP CA C 54.30 0.20 1 593 154 154 ASP CB C 40.60 0.20 1 594 154 154 ASP N N 121.20 0.20 1 595 155 155 ILE H H 7.87 0.02 1 596 155 155 ILE C C 175.60 0.20 1 597 155 155 ILE CA C 60.30 0.20 1 598 155 155 ILE CB C 38.12 0.20 1 599 155 155 ILE N N 120.60 0.20 1 600 156 156 ALA H H 8.35 0.02 1 601 156 156 ALA CA C 50.30 0.20 1 602 156 156 ALA CB C 17.52 0.20 1 603 156 156 ALA N N 129.90 0.20 1 604 157 157 PRO C C 175.91 0.20 1 605 157 157 PRO CA C 62.31 0.20 1 606 157 157 PRO CB C 33.60 0.20 1 607 158 158 ALA H H 8.53 0.02 1 608 158 158 ALA C C 177.75 0.20 1 609 158 158 ALA CA C 52.45 0.20 1 610 158 158 ALA CB C 18.62 0.20 1 611 158 158 ALA N N 125.61 0.20 1 612 159 159 ALA H H 8.38 0.02 1 613 159 159 ALA C C 177.60 0.20 1 614 159 159 ALA CA C 52.22 0.20 1 615 159 159 ALA CB C 18.20 0.20 1 616 159 159 ALA N N 124.10 0.20 1 617 160 160 ASP H H 8.26 0.02 1 618 160 160 ASP C C 176.75 0.20 1 619 160 160 ASP CA C 54.20 0.20 1 620 160 160 ASP CB C 40.67 0.20 1 621 160 160 ASP N N 119.48 0.20 1 622 161 161 GLY H H 8.24 0.02 1 623 161 161 GLY C C 174.20 0.20 1 624 161 161 GLY CA C 44.98 0.20 1 625 161 161 GLY N N 109.30 0.20 1 626 162 162 TYR H H 8.14 0.02 1 627 162 162 TYR C C 176.61 0.20 1 628 162 162 TYR CA C 58.24 0.20 1 629 162 162 TYR CB C 38.04 0.20 1 630 162 162 TYR N N 120.65 0.20 1 631 163 163 GLY H H 8.37 0.02 1 632 163 163 GLY C C 174.20 0.20 1 633 163 163 GLY CA C 45.13 0.20 1 634 163 163 GLY N N 111.15 0.20 1 635 164 164 LEU H H 8.04 0.02 1 636 164 164 LEU C C 177.32 0.20 1 637 164 164 LEU CA C 54.82 0.20 1 638 164 164 LEU CB C 41.53 0.20 1 639 164 164 LEU N N 121.98 0.20 1 640 165 165 ALA H H 8.32 0.02 1 641 165 165 ALA C C 177.94 0.20 1 642 165 165 ALA CA C 52.42 0.20 1 643 165 165 ALA CB C 18.59 0.20 1 644 165 165 ALA N N 124.70 0.20 1 645 166 166 GLY H H 8.22 0.02 1 646 166 166 GLY C C 172.87 0.20 1 647 166 166 GLY CA C 44.80 0.20 1 648 166 166 GLY N N 108.37 0.20 1 649 167 167 PHE H H 7.62 0.02 1 650 167 167 PHE CA C 58.78 0.20 1 651 167 167 PHE CB C 39.61 0.20 1 652 167 167 PHE N N 124.99 0.20 1 stop_ save_