data_16330 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C chemical shift assignments for the reduced form of the DsbA oxidoreductase from Staphylococcus aureus ; _BMRB_accession_number 16330 _BMRB_flat_file_name bmr16330.str _Entry_type original _Submission_date 2009-06-03 _Accession_date 2009-06-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Williams Martin L. . 2 Chalmers David K. . 3 Martin Jennifer L. . 4 Scanlon Martin J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 158 "13C chemical shifts" 498 "15N chemical shifts" 158 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-12-16 update author 'update chemical shifts' 2010-05-20 update BMRB 'complete entry citation' 2009-12-11 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16329 'SaDsbA Oxidoreductase, Oxidised Form' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone and side chain 1H, 15N and 13C assignments for the oxidised and reduced forms of the oxidoreductase protein DsbA from Staphylococcus aureus.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19936968 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Williams Martin L. . 2 Chalmers David K. . 3 Martin Jennifer L. . 4 Scanlon Martin J. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 4 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 25 _Page_last 28 _Year 2010 _Details . loop_ _Keyword 'Bacterial oxidoreductase' 'Disulfide formation' DsbA 'Gram positive' 'Staphylococcus aureus' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'DsbA monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DsbA monomer' $SaDsbA_Oxidoreductase stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Catalysis of post-translational disulfide bond formation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SaDsbA_Oxidoreductase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SaDsbA_Oxidoreductase _Molecular_mass 21635 _Mol_thiol_state 'all free' loop_ _Biological_function 'Thiol:disulfide oxidoreductase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 186 _Mol_residue_sequence ; MASATTSSKNGKPLVVVYGD YKCPYCKELDEKVMPKLRKN YIDNHKVEYQFVNLAFLGKD SIVGSRASHAVLMYAPKSFL DFQKQLFAAQQDENKEWLTK ELLDKHIKQLHLDKETENKI IKDYKTKDSKSWKAAEKDKK IAKDNHIKTTPTAFINGEKV EDPYDYESYEKLLKDKIKLE HHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 4 MET 2 5 ALA 3 6 SER 4 7 ALA 5 8 THR 6 9 THR 7 10 SER 8 11 SER 9 12 LYS 10 13 ASN 11 14 GLY 12 15 LYS 13 16 PRO 14 17 LEU 15 18 VAL 16 19 VAL 17 20 VAL 18 21 TYR 19 22 GLY 20 23 ASP 21 24 TYR 22 25 LYS 23 26 CYS 24 27 PRO 25 28 TYR 26 29 CYS 27 30 LYS 28 31 GLU 29 32 LEU 30 33 ASP 31 34 GLU 32 35 LYS 33 36 VAL 34 37 MET 35 38 PRO 36 39 LYS 37 40 LEU 38 41 ARG 39 42 LYS 40 43 ASN 41 44 TYR 42 45 ILE 43 46 ASP 44 47 ASN 45 48 HIS 46 49 LYS 47 50 VAL 48 51 GLU 49 52 TYR 50 53 GLN 51 54 PHE 52 55 VAL 53 56 ASN 54 57 LEU 55 58 ALA 56 59 PHE 57 60 LEU 58 61 GLY 59 62 LYS 60 63 ASP 61 64 SER 62 65 ILE 63 66 VAL 64 67 GLY 65 68 SER 66 69 ARG 67 70 ALA 68 71 SER 69 72 HIS 70 73 ALA 71 74 VAL 72 75 LEU 73 76 MET 74 77 TYR 75 78 ALA 76 79 PRO 77 80 LYS 78 81 SER 79 82 PHE 80 83 LEU 81 84 ASP 82 85 PHE 83 86 GLN 84 87 LYS 85 88 GLN 86 89 LEU 87 90 PHE 88 91 ALA 89 92 ALA 90 93 GLN 91 94 GLN 92 95 ASP 93 96 GLU 94 97 ASN 95 98 LYS 96 99 GLU 97 100 TRP 98 101 LEU 99 102 THR 100 103 LYS 101 104 GLU 102 105 LEU 103 106 LEU 104 107 ASP 105 108 LYS 106 109 HIS 107 110 ILE 108 111 LYS 109 112 GLN 110 113 LEU 111 114 HIS 112 115 LEU 113 116 ASP 114 117 LYS 115 118 GLU 116 119 THR 117 120 GLU 118 121 ASN 119 122 LYS 120 123 ILE 121 124 ILE 122 125 LYS 123 126 ASP 124 127 TYR 125 128 LYS 126 129 THR 127 130 LYS 128 131 ASP 129 132 SER 130 133 LYS 131 134 SER 132 135 TRP 133 136 LYS 134 137 ALA 135 138 ALA 136 139 GLU 137 140 LYS 138 141 ASP 139 142 LYS 140 143 LYS 141 144 ILE 142 145 ALA 143 146 LYS 144 147 ASP 145 148 ASN 146 149 HIS 147 150 ILE 148 151 LYS 149 152 THR 150 153 THR 151 154 PRO 152 155 THR 153 156 ALA 154 157 PHE 155 158 ILE 156 159 ASN 157 160 GLY 158 161 GLU 159 162 LYS 160 163 VAL 161 164 GLU 162 165 ASP 163 166 PRO 164 167 TYR 165 168 ASP 166 169 TYR 167 170 GLU 168 171 SER 169 172 TYR 170 173 GLU 171 174 LYS 172 175 LEU 173 176 LEU 174 177 LYS 175 178 ASP 176 179 LYS 177 180 ILE 178 181 LYS 179 182 LEU 180 183 GLU 181 184 HIS 182 185 HIS 183 186 HIS 184 187 HIS 185 188 HIS 186 189 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-18 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 BMRB 16329 SaDsbA_oxidoreductase 100.00 186 100.00 100.00 1.09e-131 PDB 3BCI "Crystal Structure Of Staphylococcus Aureus Dsba" 100.00 186 100.00 100.00 1.09e-131 PDB 3BCK "Crystal Structure Of Staphylococcus Aureus Dsba T153v" 100.00 186 99.46 99.46 6.31e-131 PDB 3BD2 "Crystal Structure Of Staphylococcus Aureus Dsba E96q" 100.00 186 99.46 100.00 2.63e-131 DBJ BAB43499 "conserved hypothetical protein [Staphylococcus aureus subsp. aureus N315]" 94.62 199 99.43 100.00 5.74e-123 DBJ BAB58571 "putative protein-disulfide isomerase [Staphylococcus aureus subsp. aureus Mu50]" 94.62 199 99.43 100.00 5.74e-123 DBJ BAB96196 "conserved hypothetical protein [Staphylococcus aureus subsp. aureus MW2]" 94.62 199 99.43 100.00 5.74e-123 DBJ BAF68580 "protein-disulfide isomerase [Staphylococcus aureus subsp. aureus str. Newman]" 94.62 199 100.00 100.00 3.25e-123 DBJ BAF79276 "conserved hypothetical protein [Staphylococcus aureus subsp. aureus Mu3]" 94.62 199 99.43 100.00 5.74e-123 EMBL CAG41479 "putative lipoprotein [Staphylococcus aureus subsp. aureus MRSA252]" 94.62 199 98.86 99.43 2.51e-122 EMBL CAG44113 "putative lipoprotein [Staphylococcus aureus subsp. aureus MSSA476]" 94.62 199 99.43 100.00 5.74e-123 EMBL CAI81978 "probable lipoprotein [Staphylococcus aureus RF122]" 94.62 199 99.43 100.00 5.74e-123 EMBL CAQ50840 "lipoprotein, putative [Staphylococcus aureus subsp. aureus ST398]" 94.62 199 98.30 99.43 2.66e-121 EMBL CBI50404 "putative lipoprotein [Staphylococcus aureus subsp. aureus TW20]" 94.62 199 100.00 100.00 3.25e-123 GB AAG41993 "disulfide bond protein A [Staphylococcus aureus]" 94.62 199 100.00 100.00 3.25e-123 GB AAW37232 "lipoprotein, putative [Staphylococcus aureus subsp. aureus COL]" 94.62 199 100.00 100.00 3.25e-123 GB ABD21498 "putative lipoprotein [Staphylococcus aureus subsp. aureus USA300_FPR3757]" 94.62 199 100.00 100.00 3.25e-123 GB ABD31702 "conserved hypothetical protein [Staphylococcus aureus subsp. aureus NCTC 8325]" 94.62 199 100.00 100.00 3.25e-123 GB ABQ50211 "Protein-disulfide isomerase-like protein [Staphylococcus aureus subsp. aureus JH9]" 94.62 199 99.43 100.00 5.74e-123 REF WP_000162799 "hypothetical protein [Staphylococcus aureus]" 94.62 199 98.86 99.43 3.19e-122 REF WP_000162803 "protein disulfide-isomerase [Staphylococcus aureus]" 94.62 199 98.86 100.00 1.66e-122 REF WP_000162804 "protein disulfide-isomerase [Staphylococcus aureus]" 94.62 199 98.86 99.43 2.51e-122 REF WP_000162805 "protein disulfide-isomerase [Staphylococcus aureus]" 94.62 199 98.86 100.00 3.84e-122 REF WP_000162807 "protein disulfide-isomerase [Staphylococcus aureus]" 94.62 199 98.30 99.43 2.66e-121 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SaDsbA_Oxidoreductase 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $SaDsbA_Oxidoreductase 'recombinant technology' . Escherichia coli BL21 DE3 pET21a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '10mM HEPES, 50mM NaCl, pH 6.8' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SaDsbA_Oxidoreductase 0.24 mM '[U-95% 13C; U-90% 15N]' HEPES 10 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.113 loop_ _Vendor _Address _Electronic_address Goddard 'University of California, San Francisco' . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details Cryoprobe 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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACO' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_C(CO)NH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH-TOCSY' _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' 10 . mM pH 6.8 . pH pressure 1 . atm temperature 318 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HNCACO' '3D HCCH-TOCSY' '3D C(CO)NH-TOCSY' 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 'DsbA monomer' _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 12 9 LYS C C 175.173 0.03 1 2 12 9 LYS CA C 56.368 0.019 1 3 12 9 LYS CB C 33.259 0.037 1 4 13 10 ASN H H 7.965 0.007 1 5 13 10 ASN CA C 54.96 0.068 1 6 13 10 ASN CB C 41.242 0.048 1 7 13 10 ASN N N 125.518 0.023 1 8 14 11 GLY H H 8.16 0.006 1 9 14 11 GLY C C 174.145 0.009 1 10 14 11 GLY CA C 45.447 0.041 1 11 14 11 GLY N N 113.592 0.025 1 12 15 12 LYS H H 8.14 0.008 1 13 15 12 LYS C C 174.149 0 1 14 15 12 LYS CA C 54.599 0 1 15 15 12 LYS CB C 33.08 0 1 16 15 12 LYS N N 121.837 0.059 1 17 16 13 PRO C C 173.62 0.036 1 18 16 13 PRO CA C 63.012 0.062 1 19 16 13 PRO CB C 32.278 0.036 1 20 17 14 LEU H H 8.206 0.01 1 21 17 14 LEU C C 175.816 0.045 1 22 17 14 LEU CA C 53.74 0.015 1 23 17 14 LEU CB C 44.555 0.064 1 24 17 14 LEU N N 123.337 0.042 1 25 18 15 VAL H H 9.197 0.009 1 26 18 15 VAL C C 173.697 0.026 1 27 18 15 VAL CA C 61.116 0.047 1 28 18 15 VAL CB C 33.014 0.069 1 29 18 15 VAL N N 129.437 0.018 1 30 19 16 VAL H H 9.152 0.01 1 31 19 16 VAL C C 175.184 0.017 1 32 19 16 VAL CA C 60.077 0.023 1 33 19 16 VAL CB C 34.852 0.04 1 34 19 16 VAL N N 127.218 0.03 1 35 20 17 VAL H H 8.509 0.009 1 36 20 17 VAL C C 173.891 0.005 1 37 20 17 VAL CA C 61.556 0.032 1 38 20 17 VAL CB C 35.245 0.023 1 39 20 17 VAL N N 125.915 0.03 1 40 21 18 TYR H H 9.281 0.009 1 41 21 18 TYR C C 176.215 0.037 1 42 21 18 TYR CA C 56.049 0.052 1 43 21 18 TYR CB C 39.099 0.052 1 44 21 18 TYR N N 125.937 0.032 1 45 22 19 GLY H H 8.392 0.007 1 46 22 19 GLY C C 170.352 0.073 1 47 22 19 GLY CA C 47.598 0.071 1 48 22 19 GLY N N 107.933 0.038 1 49 23 20 ASP H H 7.865 0.015 1 50 23 20 ASP C C 178.073 0.116 1 51 23 20 ASP CA C 55.143 0.071 1 52 23 20 ASP CB C 46.112 0.01 1 53 23 20 ASP N N 119.883 0.073 1 54 24 21 TYR H H 7.877 0.018 1 55 24 21 TYR C C 175.989 0.004 1 56 24 21 TYR CA C 62.128 0.027 1 57 24 21 TYR CB C 37.722 0.063 1 58 24 21 TYR N N 125.361 0.076 1 59 25 22 LYS H H 9.741 0.018 1 60 25 22 LYS C C 176.13 0.061 1 61 25 22 LYS CA C 57.163 0.062 1 62 25 22 LYS CB C 32.157 0.078 1 63 25 22 LYS N N 115.895 0.047 1 64 26 23 CYS H H 7.651 0.007 1 65 26 23 CYS C C 177.014 0 1 66 26 23 CYS CA C 57.586 0 1 67 26 23 CYS CB C 30.696 0 1 68 26 23 CYS N N 122.836 0.04 1 69 27 24 PRO C C 179.488 0 1 70 27 24 PRO CA C 64.394 0.039 1 71 27 24 PRO CB C 32.09 0.028 1 72 28 25 TYR H H 9.242 0.008 1 73 28 25 TYR C C 179.414 0.017 1 74 28 25 TYR CA C 61.198 0.024 1 75 28 25 TYR CB C 37.18 0.041 1 76 28 25 TYR N N 126.948 0.008 1 77 29 26 CYS H H 9.499 0.013 1 78 29 26 CYS C C 176.441 0.049 1 79 29 26 CYS CA C 64.29 0.06 1 80 29 26 CYS CB C 29.193 0.038 1 81 29 26 CYS N N 128.257 0.027 1 82 30 27 LYS H H 7.498 0.007 1 83 30 27 LYS C C 177.129 0.094 1 84 30 27 LYS CA C 59.803 0.044 1 85 30 27 LYS CB C 32.381 0.036 1 86 30 27 LYS N N 121.531 0.013 1 87 31 28 GLU H H 7.228 0.007 1 88 31 28 GLU C C 178.354 0.006 1 89 31 28 GLU CA C 59.655 0.067 1 90 31 28 GLU CB C 29.249 0.034 1 91 31 28 GLU N N 119.257 0.015 1 92 32 29 LEU H H 7.83 0.008 1 93 32 29 LEU C C 179.566 0.015 1 94 32 29 LEU CA C 60.961 0.043 1 95 32 29 LEU CB C 42.834 0.01 1 96 32 29 LEU N N 121.297 0.034 1 97 33 30 ASP H H 8.048 0.008 1 98 33 30 ASP C C 177.938 0.011 1 99 33 30 ASP CA C 59.049 0.109 1 100 33 30 ASP CB C 43.981 0.037 1 101 33 30 ASP N N 122.24 0.028 1 102 34 31 GLU H H 8.134 0.007 1 103 34 31 GLU C C 178.762 0.027 1 104 34 31 GLU CA C 59.131 0.125 1 105 34 31 GLU CB C 30.714 0.043 1 106 34 31 GLU N N 115.623 0.012 1 107 35 32 LYS H H 8.467 0.007 1 108 35 32 LYS C C 178.72 0.077 1 109 35 32 LYS CA C 58.719 0.057 1 110 35 32 LYS CB C 35.07 0.048 1 111 35 32 LYS N N 114.739 0.046 1 112 36 33 VAL H H 8.643 0.007 1 113 36 33 VAL C C 176.462 0.022 1 114 36 33 VAL CA C 64.697 0.029 1 115 36 33 VAL CB C 34.004 0.121 1 116 36 33 VAL N N 118.534 0.028 1 117 37 34 MET H H 7.094 0.006 1 118 37 34 MET C C 174.719 0 1 119 37 34 MET CA C 58.086 0 1 120 37 34 MET CB C 28.458 0 1 121 37 34 MET N N 116.831 0.016 1 122 38 35 PRO C C 180.099 0.041 1 123 38 35 PRO CA C 67.12 0.014 1 124 38 35 PRO CB C 31.148 0.014 1 125 39 36 LYS H H 7.185 0.006 1 126 39 36 LYS C C 178.465 0.058 1 127 39 36 LYS CA C 59.16 0.033 1 128 39 36 LYS CB C 32.584 0.079 1 129 39 36 LYS N N 115.941 0.017 1 130 40 37 LEU H H 8.163 0.006 1 131 40 37 LEU C C 180.461 0.02 1 132 40 37 LEU CA C 58.754 0.022 1 133 40 37 LEU CB C 43.194 0.013 1 134 40 37 LEU N N 121.305 0.034 1 135 41 38 ARG H H 9.506 0.009 1 136 41 38 ARG C C 177.336 0.005 1 137 41 38 ARG CA C 60.539 0.051 1 138 41 38 ARG CB C 30.144 0.054 1 139 41 38 ARG N N 118.882 0.012 1 140 42 39 LYS H H 7.208 0.009 1 141 42 39 LYS C C 177.454 0.09 1 142 42 39 LYS CA C 58.788 0.033 1 143 42 39 LYS CB C 33.056 0.085 1 144 42 39 LYS N N 116.87 0.036 1 145 43 40 ASN H H 7.832 0.008 1 146 43 40 ASN C C 175.949 0.033 1 147 43 40 ASN CA C 55.016 0.044 1 148 43 40 ASN CB C 40.474 0.08 1 149 43 40 ASN N N 111.275 0.028 1 150 44 41 TYR H H 7.891 0.008 1 151 44 41 TYR C C 175.139 0.006 1 152 44 41 TYR CA C 60.82 0.016 1 153 44 41 TYR CB C 41.929 0.092 1 154 44 41 TYR N N 115.297 0.009 1 155 45 42 ILE H H 7.987 0.008 1 156 45 42 ILE C C 179.903 0.012 1 157 45 42 ILE CA C 64.81 0.031 1 158 45 42 ILE CB C 39.767 0.088 1 159 45 42 ILE N N 117.648 0.032 1 160 46 43 ASP H H 9.427 0.008 1 161 46 43 ASP C C 176.346 0.042 1 162 46 43 ASP CA C 57.179 0.016 1 163 46 43 ASP CB C 39.853 0.083 1 164 46 43 ASP N N 122.997 0.021 1 165 47 44 ASN H H 7.653 0.008 1 166 47 44 ASN C C 175.353 0.017 1 167 47 44 ASN CA C 51.781 0.021 1 168 47 44 ASN CB C 36.961 0.085 1 169 47 44 ASN N N 112.758 0.014 1 170 48 45 HIS H H 7.844 0.008 1 171 48 45 HIS C C 174.735 0.094 1 172 48 45 HIS CA C 57.012 0.056 1 173 48 45 HIS CB C 27.215 0.054 1 174 48 45 HIS N N 111.524 0.038 1 175 49 46 LYS H H 8.055 0.008 1 176 49 46 LYS C C 176.814 0.043 1 177 49 46 LYS CA C 58.725 0.016 1 178 49 46 LYS CB C 34.393 0.077 1 179 49 46 LYS N N 116.984 0.04 1 180 50 47 VAL H H 7.644 0.007 1 181 50 47 VAL C C 174.533 0.047 1 182 50 47 VAL CA C 58.057 0.053 1 183 50 47 VAL CB C 35.139 0.058 1 184 50 47 VAL N N 107.475 0.044 1 185 51 48 GLU H H 8.876 0.007 1 186 51 48 GLU C C 173.909 0.032 1 187 51 48 GLU CA C 55.237 0.009 1 188 51 48 GLU CB C 31.935 0.07 1 189 51 48 GLU N N 121.645 0.028 1 190 52 49 TYR H H 8.681 0.008 1 191 52 49 TYR C C 173.91 0.015 1 192 52 49 TYR CA C 55.538 0.039 1 193 52 49 TYR CB C 42.582 0.069 1 194 52 49 TYR N N 125.121 0.024 1 195 53 50 GLN H H 8.754 0.008 1 196 53 50 GLN C C 171.338 0.019 1 197 53 50 GLN CA C 54.196 0.017 1 198 53 50 GLN CB C 32.159 0.051 1 199 53 50 GLN N N 130.294 0.021 1 200 54 51 PHE H H 8.335 0.007 1 201 54 51 PHE C C 175.355 0.031 1 202 54 51 PHE CA C 55.067 0.039 1 203 54 51 PHE CB C 40.893 0.065 1 204 54 51 PHE N N 126.442 0.011 1 205 55 52 VAL H H 8.898 0.006 1 206 55 52 VAL C C 172.81 0.052 1 207 55 52 VAL CA C 61.278 0.005 1 208 55 52 VAL CB C 32.54 0.021 1 209 55 52 VAL N N 132.58 0.015 1 210 56 53 ASN H H 9.074 0.009 1 211 56 53 ASN C C 175.635 0 1 212 56 53 ASN CA C 50.877 0.015 1 213 56 53 ASN CB C 40.003 0.059 1 214 56 53 ASN N N 127.553 0.031 1 215 57 54 LEU H H 8.872 0.008 1 216 57 54 LEU C C 177.152 0.029 1 217 57 54 LEU CA C 59.665 0.021 1 218 57 54 LEU CB C 44.192 0.039 1 219 57 54 LEU N N 127.581 0.036 1 220 58 55 ALA H H 8.952 0.007 1 221 58 55 ALA C C 176.837 0.06 1 222 58 55 ALA CA C 52.663 0.03 1 223 58 55 ALA CB C 17.492 0.099 1 224 58 55 ALA N N 119.042 0.033 1 225 59 56 PHE H H 8.763 0.009 1 226 59 56 PHE C C 176.63 0.066 1 227 59 56 PHE CA C 56.426 0.041 1 228 59 56 PHE CB C 41.224 0.028 1 229 59 56 PHE N N 117.213 0.016 1 230 60 57 LEU H H 7.957 0.01 1 231 60 57 LEU C C 176.119 0.069 1 232 60 57 LEU CA C 55.583 0.04 1 233 60 57 LEU CB C 41.561 0.061 1 234 60 57 LEU N N 126.287 0.053 1 235 61 58 GLY H H 7.489 0.006 1 236 61 58 GLY C C 175.639 0 1 237 61 58 GLY CA C 44.459 0 1 238 61 58 GLY N N 105.607 0.008 1 239 62 59 LYS C C 176.62 0.028 1 240 62 59 LYS CA C 59.18 0.003 1 241 62 59 LYS CB C 32.434 0.078 1 242 63 60 ASP H H 10.174 0.009 1 243 63 60 ASP C C 177.69 0.047 1 244 63 60 ASP CA C 54.241 0.017 1 245 63 60 ASP CB C 38.71 0.043 1 246 63 60 ASP N N 114.572 0.026 1 247 64 61 SER H H 7.387 0.009 1 248 64 61 SER C C 178.37 0.025 1 249 64 61 SER CA C 63.607 0.071 1 250 64 61 SER CB C 62.296 0.093 1 251 64 61 SER N N 117.539 0.017 1 252 65 62 ILE H H 7.869 0.008 1 253 65 62 ILE C C 174.879 0.066 1 254 65 62 ILE CA C 60.966 0.052 1 255 65 62 ILE CB C 38.466 0.094 1 256 65 62 ILE N N 118.706 0.031 1 257 66 63 VAL H H 6.995 0.009 1 258 66 63 VAL C C 178.345 0.009 1 259 66 63 VAL CA C 66.817 0.048 1 260 66 63 VAL CB C 30.898 0.101 1 261 66 63 VAL N N 125.502 0.045 1 262 67 64 GLY H H 7.228 0.007 1 263 67 64 GLY C C 174.412 0.081 1 264 67 64 GLY CA C 47.661 0.05 1 265 67 64 GLY N N 101.49 0.018 1 266 68 65 SER H H 7.864 0.006 1 267 68 65 SER C C 177.796 0.018 1 268 68 65 SER CA C 59.95 0.036 1 269 68 65 SER CB C 64.4 0.005 1 270 68 65 SER N N 113.44 0.014 1 271 69 66 ARG H H 8.534 0.007 1 272 69 66 ARG C C 177.98 0.011 1 273 69 66 ARG CA C 60.44 0.055 1 274 69 66 ARG CB C 31.754 0.044 1 275 69 66 ARG N N 118.834 0.028 1 276 70 67 ALA H H 7.85 0.008 1 277 70 67 ALA C C 177.976 0.023 1 278 70 67 ALA CA C 55.975 0.026 1 279 70 67 ALA CB C 18.305 0.03 1 280 70 67 ALA N N 119.861 0.048 1 281 71 68 SER H H 8.039 0.007 1 282 71 68 SER C C 176.54 0.052 1 283 71 68 SER CA C 61.202 0.012 1 284 71 68 SER CB C 63.7 0.015 1 285 71 68 SER N N 110.161 0.031 1 286 72 69 HIS H H 8.823 0.01 1 287 72 69 HIS C C 177.959 0.013 1 288 72 69 HIS CA C 61.528 0.025 1 289 72 69 HIS CB C 31.438 0.053 1 290 72 69 HIS N N 118.483 0.032 1 291 73 70 ALA H H 8.555 0.007 1 292 73 70 ALA C C 178.869 0.009 1 293 73 70 ALA CA C 55.945 0.036 1 294 73 70 ALA CB C 19.558 0.087 1 295 73 70 ALA N N 124.107 0.017 1 296 74 71 VAL H H 8.153 0.007 1 297 74 71 VAL C C 177.037 0.027 1 298 74 71 VAL CA C 67.307 0.023 1 299 74 71 VAL CB C 31.484 0.051 1 300 74 71 VAL N N 119.801 0.032 1 301 75 72 LEU H H 8.217 0.006 1 302 75 72 LEU C C 177.661 0.014 1 303 75 72 LEU CA C 58.408 0.022 1 304 75 72 LEU CB C 41.33 0.024 1 305 75 72 LEU N N 118.574 0.034 1 306 76 73 MET H H 7.839 0.007 1 307 76 73 MET C C 178.118 0.032 1 308 76 73 MET CA C 58.452 0.15 1 309 76 73 MET CB C 33.194 0.072 1 310 76 73 MET N N 113.047 0.012 1 311 77 74 TYR H H 7.712 0.008 1 312 77 74 TYR C C 175.501 0.057 1 313 77 74 TYR CA C 58.578 0.029 1 314 77 74 TYR CB C 39.044 0.062 1 315 77 74 TYR N N 114.95 0.01 1 316 78 75 ALA H H 9.18 0.005 1 317 78 75 ALA C C 173.705 0 1 318 78 75 ALA CA C 50.833 0 1 319 78 75 ALA CB C 20.157 0 1 320 78 75 ALA N N 124.657 0.029 1 321 79 76 PRO C C 180.413 0 1 322 79 76 PRO CA C 65.998 0.069 1 323 79 76 PRO CB C 31.089 0.063 1 324 80 77 LYS H H 8.689 0.007 1 325 80 77 LYS C C 178.465 0.091 1 326 80 77 LYS CA C 58.911 0 1 327 80 77 LYS CB C 31.722 0.052 1 328 80 77 LYS N N 117.146 0.025 1 329 81 78 SER H H 8.453 0.009 1 330 81 78 SER C C 174.209 0.022 1 331 81 78 SER CA C 59.876 0.062 1 332 81 78 SER CB C 64.735 0.021 1 333 81 78 SER N N 115.434 0.065 1 334 82 79 PHE H H 7.593 0.006 1 335 82 79 PHE C C 175.9 0.003 1 336 82 79 PHE CA C 62.313 0.019 1 337 82 79 PHE CB C 40.55 0.064 1 338 82 79 PHE N N 121.193 0.018 1 339 83 80 LEU H H 8.588 0.008 1 340 83 80 LEU C C 180.171 0.016 1 341 83 80 LEU CA C 58.473 0.034 1 342 83 80 LEU CB C 40.155 0.077 1 343 83 80 LEU N N 118.636 0.036 1 344 84 81 ASP H H 8.022 0.006 1 345 84 81 ASP C C 177.896 0.044 1 346 84 81 ASP CA C 57.537 0.084 1 347 84 81 ASP CB C 39.991 0.085 1 348 84 81 ASP N N 120.563 0.027 1 349 85 82 PHE H H 8.168 0.006 1 350 85 82 PHE C C 177 0.035 1 351 85 82 PHE CA C 61.527 0.042 1 352 85 82 PHE CB C 39.24 0.064 1 353 85 82 PHE N N 121.582 0.073 1 354 86 83 GLN H H 8.363 0.008 1 355 86 83 GLN C C 176.9 0.02 1 356 86 83 GLN CA C 60.478 0.082 1 357 86 83 GLN CB C 29.87 0.062 1 358 86 83 GLN N N 117.574 0.045 1 359 87 84 LYS H H 7.68 0.005 1 360 87 84 LYS C C 179.964 0.02 1 361 87 84 LYS CA C 58.975 0.014 1 362 87 84 LYS CB C 32.341 0.073 1 363 87 84 LYS N N 117.806 0.021 1 364 88 85 GLN H H 7.735 0.01 1 365 88 85 GLN C C 178.069 0.028 1 366 88 85 GLN CA C 58.106 0.069 1 367 88 85 GLN CB C 28.628 0.053 1 368 88 85 GLN N N 116.79 0.062 1 369 89 86 LEU H H 7.685 0.007 1 370 89 86 LEU C C 179.197 0.035 1 371 89 86 LEU CA C 57.61 0.113 1 372 89 86 LEU CB C 40.739 0.051 1 373 89 86 LEU N N 121.948 0.026 1 374 90 87 PHE H H 8.073 0.006 1 375 90 87 PHE C C 179.144 0.092 1 376 90 87 PHE CA C 63.247 0.011 1 377 90 87 PHE CB C 38.773 0.036 1 378 90 87 PHE N N 115.387 0.031 1 379 91 88 ALA H H 7.725 0.006 1 380 91 88 ALA C C 178.659 0.049 1 381 91 88 ALA CA C 54.365 0.029 1 382 91 88 ALA CB C 18.19 0.04 1 383 91 88 ALA N N 118.278 0.091 1 384 92 89 ALA H H 7.286 0.006 1 385 92 89 ALA C C 175.575 0.056 1 386 92 89 ALA CA C 51.206 0.018 1 387 92 89 ALA CB C 19.728 0.082 1 388 92 89 ALA N N 120.488 0.049 1 389 93 90 GLN H H 6.814 0.007 1 390 93 90 GLN C C 175.744 0 1 391 93 90 GLN CA C 57.8 0.038 1 392 93 90 GLN CB C 31.987 0.075 1 393 93 90 GLN N N 117.975 0.043 1 394 94 91 GLN H H 3.512 0.004 1 395 94 91 GLN C C 173.654 0 1 396 94 91 GLN CA C 53.132 0.021 1 397 94 91 GLN CB C 30.441 0.034 1 398 94 91 GLN N N 123.518 0.015 1 399 95 92 ASP H H 7.736 0.008 1 400 95 92 ASP C C 176.427 0.04 1 401 95 92 ASP CA C 55.695 0.022 1 402 95 92 ASP CB C 42.735 0.02 1 403 95 92 ASP N N 119.944 0.015 1 404 96 93 GLU H H 9.061 0.007 1 405 96 93 GLU C C 176.653 0.075 1 406 96 93 GLU CA C 59.006 0.097 1 407 96 93 GLU CB C 29.803 0.031 1 408 96 93 GLU N N 122.036 0.021 1 409 97 94 ASN H H 8.442 0.008 1 410 97 94 ASN C C 175.484 0.029 1 411 97 94 ASN CA C 53.953 0.071 1 412 97 94 ASN CB C 38.707 0.033 1 413 97 94 ASN N N 115.496 0.043 1 414 98 95 LYS H H 8.215 0.007 1 415 98 95 LYS C C 176.93 0 1 416 98 95 LYS CA C 55.249 0.106 1 417 98 95 LYS CB C 34.461 0.05 1 418 98 95 LYS N N 120.914 0.021 1 419 99 96 GLU H H 8.684 0.002 1 420 99 96 GLU C C 175.655 0 1 421 99 96 GLU CA C 55.474 0.146 1 422 99 96 GLU CB C 27.824 0.029 1 423 99 96 GLU N N 125.265 0.007 1 424 100 97 TRP H H 7.37 0.007 1 425 100 97 TRP C C 176.805 0.013 1 426 100 97 TRP CA C 55.883 0.046 1 427 100 97 TRP CB C 30.048 0.089 1 428 100 97 TRP N N 120.066 0.018 1 429 101 98 LEU H H 8.912 0.005 1 430 101 98 LEU C C 174.802 0 1 431 101 98 LEU CA C 54.244 0.01 1 432 101 98 LEU CB C 39.547 0.075 1 433 101 98 LEU N N 129.673 0.023 1 434 102 99 THR H H 7.335 0.007 1 435 102 99 THR C C 175.213 0.009 1 436 102 99 THR CA C 58.836 0.07 1 437 102 99 THR CB C 71.604 0.017 1 438 102 99 THR N N 110.905 0.021 1 439 103 100 LYS H H 8.756 0.007 1 440 103 100 LYS C C 177.695 0.037 1 441 103 100 LYS CA C 58.911 0.141 1 442 103 100 LYS CB C 32.207 0.013 1 443 103 100 LYS N N 119.983 0.036 1 444 104 101 GLU H H 8.196 0.009 1 445 104 101 GLU C C 179.392 0.018 1 446 104 101 GLU CA C 60.288 0.031 1 447 104 101 GLU CB C 29.182 0.039 1 448 104 101 GLU N N 116.642 0.029 1 449 105 102 LEU H H 7.747 0.008 1 450 105 102 LEU C C 179.038 0.042 1 451 105 102 LEU CA C 58.88 0.049 1 452 105 102 LEU CB C 42.351 0.048 1 453 105 102 LEU N N 122.599 0.013 1 454 106 103 LEU H H 8.737 0.007 1 455 106 103 LEU C C 178.907 0.018 1 456 106 103 LEU CA C 58.686 0.041 1 457 106 103 LEU CB C 40.745 0.053 1 458 106 103 LEU N N 121.354 0.047 1 459 107 104 ASP H H 8.972 0.006 1 460 107 104 ASP C C 178.781 0.046 1 461 107 104 ASP CA C 58.038 0.093 1 462 107 104 ASP CB C 39.373 0.064 1 463 107 104 ASP N N 120.013 0.023 1 464 108 105 LYS H H 7.381 0.01 1 465 108 105 LYS C C 179.423 0.008 1 466 108 105 LYS CA C 60.172 0.134 1 467 108 105 LYS CB C 32.069 0.096 1 468 108 105 LYS N N 119.682 0.032 1 469 109 106 HIS H H 8.447 0.006 1 470 109 106 HIS C C 178.687 0.006 1 471 109 106 HIS CA C 61.226 0.028 1 472 109 106 HIS CB C 29.491 0 1 473 109 106 HIS N N 119.825 0.029 1 474 110 107 ILE H H 9.008 0.007 1 475 110 107 ILE C C 179.572 0.014 1 476 110 107 ILE CA C 65.695 0.01 1 477 110 107 ILE CB C 38.365 0.076 1 478 110 107 ILE N N 122.552 0.023 1 479 111 108 LYS H H 8.385 0.007 1 480 111 108 LYS C C 179.382 0.047 1 481 111 108 LYS CA C 59.851 0.013 1 482 111 108 LYS CB C 32.227 0.05 1 483 111 108 LYS N N 121.337 0.031 1 484 112 109 GLN H H 7.74 0.007 1 485 112 109 GLN C C 175.851 0.025 1 486 112 109 GLN CA C 56.986 0.025 1 487 112 109 GLN CB C 28.339 0.021 1 488 112 109 GLN N N 118.053 0.039 1 489 113 110 LEU H H 7.389 0.009 1 490 113 110 LEU C C 176.715 0.015 1 491 113 110 LEU CA C 55.806 0.041 1 492 113 110 LEU CB C 41.787 0.042 1 493 113 110 LEU N N 116.911 0.019 1 494 114 111 HIS H H 7.796 0.006 1 495 114 111 HIS C C 174.63 0.014 1 496 114 111 HIS CA C 56.589 0.027 1 497 114 111 HIS CB C 26.41 0.059 1 498 114 111 HIS N N 113.639 0.036 1 499 115 112 LEU H H 9.24 0.007 1 500 115 112 LEU C C 177.429 0.012 1 501 115 112 LEU CA C 53.803 0.01 1 502 115 112 LEU CB C 43.239 0.037 1 503 115 112 LEU N N 119.62 0.026 1 504 116 113 ASP H H 8.064 0.007 1 505 116 113 ASP C C 176.392 0.024 1 506 116 113 ASP CA C 54.352 0.047 1 507 116 113 ASP CB C 41.539 0.073 1 508 116 113 ASP N N 117.976 0.04 1 509 117 114 LYS H H 8.511 0.007 1 510 117 114 LYS C C 178.36 0.034 1 511 117 114 LYS CA C 59.143 0.039 1 512 117 114 LYS CB C 32.199 0.01 1 513 117 114 LYS N N 122.048 0.047 1 514 118 115 GLU H H 8.345 0.008 1 515 118 115 GLU C C 179.45 0.002 1 516 118 115 GLU CA C 59.738 0.041 1 517 118 115 GLU CB C 29.245 0.032 1 518 118 115 GLU N N 117.855 0.024 1 519 119 116 THR H H 8.019 0.009 1 520 119 116 THR C C 175.572 0.032 1 521 119 116 THR CA C 67.317 0.016 1 522 119 116 THR N N 119.57 0.044 1 523 120 117 GLU H H 8.485 0.008 1 524 120 117 GLU C C 177.156 0.017 1 525 120 117 GLU CA C 60.918 0.023 1 526 120 117 GLU CB C 31.549 0.076 1 527 120 117 GLU N N 121.722 0.019 1 528 121 118 ASN H H 8.208 0.008 1 529 121 118 ASN C C 177.792 0.048 1 530 121 118 ASN CA C 56.049 0.057 1 531 121 118 ASN CB C 38.488 0.067 1 532 121 118 ASN N N 114.379 0.03 1 533 122 119 LYS H H 7.792 0.008 1 534 122 119 LYS C C 178.729 0.016 1 535 122 119 LYS CA C 59.98 0.033 1 536 122 119 LYS CB C 32.241 0.025 1 537 122 119 LYS N N 120.53 0.023 1 538 123 120 ILE H H 7.866 0.009 1 539 123 120 ILE C C 176.831 0.023 1 540 123 120 ILE CA C 66.196 0.052 1 541 123 120 ILE CB C 38.738 0.102 1 542 123 120 ILE N N 119.954 0.113 1 543 124 121 ILE H H 7.836 0.008 1 544 124 121 ILE C C 176.219 0.034 1 545 124 121 ILE CA C 65.587 0.075 1 546 124 121 ILE CB C 38.322 0.034 1 547 124 121 ILE N N 117.773 0.042 1 548 125 122 LYS H H 7.75 0.008 1 549 125 122 LYS C C 180.461 0.005 1 550 125 122 LYS CA C 58.759 0.045 1 551 125 122 LYS CB C 32.737 0.033 1 552 125 122 LYS N N 114.288 0.013 1 553 126 123 ASP H H 8.343 0.006 1 554 126 123 ASP C C 180.613 0.013 1 555 126 123 ASP CA C 59.121 0.022 1 556 126 123 ASP CB C 44.445 0.044 1 557 126 123 ASP N N 121.168 0.025 1 558 127 124 TYR H H 7.956 0.008 1 559 127 124 TYR C C 175.314 0 1 560 127 124 TYR CA C 59.778 0 1 561 127 124 TYR CB C 36.966 0 1 562 127 124 TYR N N 115.235 0.017 1 563 128 125 LYS C C 176.847 0 1 564 128 125 LYS CA C 56.647 0.037 1 565 128 125 LYS CB C 34.474 0.06 1 566 129 126 THR H H 7.487 0.009 1 567 129 126 THR C C 171.428 0 1 568 129 126 THR CA C 63.127 0 1 569 129 126 THR CB C 70.039 0 1 570 129 126 THR N N 118.942 0.017 1 571 132 129 SER C C 174.575 0.074 1 572 132 129 SER CA C 57.556 0.019 1 573 132 129 SER CB C 65.118 0.042 1 574 133 130 LYS H H 9.529 0.009 1 575 133 130 LYS C C 180.633 0.055 1 576 133 130 LYS CA C 60.856 0.053 1 577 133 130 LYS CB C 32.638 0.014 1 578 133 130 LYS N N 119.238 0.031 1 579 134 131 SER H H 8.797 0.008 1 580 134 131 SER C C 176.56 0.045 1 581 134 131 SER CA C 63.23 0 1 582 134 131 SER N N 116.935 0.024 1 583 135 132 TRP H H 8.208 0.009 1 584 135 132 TRP C C 180.446 0 1 585 135 132 TRP CA C 61.744 0 1 586 135 132 TRP CB C 28.222 0 1 587 135 132 TRP N N 126.96 0.012 1 588 136 133 LYS C C 179.687 0 1 589 136 133 LYS CA C 59.492 0.005 1 590 136 133 LYS CB C 32.437 0.019 1 591 137 134 ALA H H 8.179 0.008 1 592 137 134 ALA C C 179.435 0.035 1 593 137 134 ALA CA C 55.134 0.031 1 594 137 134 ALA CB C 17.62 0.061 1 595 137 134 ALA N N 124.222 0.017 1 596 138 135 ALA H H 7.7 0.008 1 597 138 135 ALA C C 181.058 0.021 1 598 138 135 ALA CA C 54.942 0.112 1 599 138 135 ALA CB C 18.944 0.068 1 600 138 135 ALA N N 119.965 0.015 1 601 139 136 GLU H H 7.469 0.01 1 602 139 136 GLU C C 179.387 0.024 1 603 139 136 GLU CA C 59.116 0.026 1 604 139 136 GLU CB C 29.58 0.062 1 605 139 136 GLU N N 117.543 0.026 1 606 140 137 LYS H H 8.152 0.008 1 607 140 137 LYS C C 178.315 0 1 608 140 137 LYS CA C 59.381 0.05 1 609 140 137 LYS CB C 31.651 0.047 1 610 140 137 LYS N N 123.106 0.022 1 611 141 138 ASP H H 7.567 0.007 1 612 141 138 ASP C C 177.938 0.022 1 613 141 138 ASP CA C 57.308 0.009 1 614 141 138 ASP CB C 41.974 0.064 1 615 141 138 ASP N N 120.572 0.014 1 616 142 139 LYS H H 6.775 0.007 1 617 142 139 LYS C C 179.543 0.007 1 618 142 139 LYS CA C 60.315 0.093 1 619 142 139 LYS CB C 32.028 0.088 1 620 142 139 LYS N N 114.71 0.015 1 621 143 140 LYS H H 7.383 0.008 1 622 143 140 LYS C C 177.598 0.038 1 623 143 140 LYS CA C 59.257 0.021 1 624 143 140 LYS CB C 32.492 0.043 1 625 143 140 LYS N N 121.381 0.028 1 626 144 141 ILE H H 8.522 0.008 1 627 144 141 ILE C C 179.363 0.019 1 628 144 141 ILE CA C 65.199 0.011 1 629 144 141 ILE CB C 37.886 0.091 1 630 144 141 ILE N N 120.663 0.022 1 631 145 142 ALA H H 7.963 0.006 1 632 145 142 ALA C C 178.673 0.016 1 633 145 142 ALA CA C 55.678 0.007 1 634 145 142 ALA CB C 18.68 0.054 1 635 145 142 ALA N N 120.19 0.036 1 636 146 143 LYS H H 7.614 0.007 1 637 146 143 LYS C C 180.979 0.011 1 638 146 143 LYS CA C 59.429 0.046 1 639 146 143 LYS CB C 32.324 0.027 1 640 146 143 LYS N N 118.82 0.009 1 641 147 144 ASP H H 8.951 0.006 1 642 147 144 ASP C C 177.11 0.005 1 643 147 144 ASP CA C 56.855 0.028 1 644 147 144 ASP CB C 39.861 0.074 1 645 147 144 ASP N N 122.11 0.038 1 646 148 145 ASN H H 7.358 0.006 1 647 148 145 ASN C C 173.001 0.061 1 648 148 145 ASN CA C 53.173 0.016 1 649 148 145 ASN CB C 39.153 0.065 1 650 148 145 ASN N N 114.564 0.028 1 651 149 146 HIS H H 7.662 0.008 1 652 149 146 HIS C C 174.041 0.045 1 653 149 146 HIS CA C 56.623 0.015 1 654 149 146 HIS CB C 26.847 0.076 1 655 149 146 HIS N N 114.801 0.04 1 656 150 147 ILE H H 7.912 0.006 1 657 150 147 ILE C C 175.721 0.009 1 658 150 147 ILE CA C 59.211 0.112 1 659 150 147 ILE CB C 35.203 0 1 660 150 147 ILE N N 119.059 0.022 1 661 151 148 LYS H H 8.403 0.007 1 662 151 148 LYS CA C 55.806 0.029 1 663 151 148 LYS CB C 34.98 0.088 1 664 151 148 LYS N N 124.799 0.052 1 665 152 149 THR H H 7.336 0.007 1 666 152 149 THR C C 172.439 0.021 1 667 152 149 THR CA C 60.509 0.033 1 668 152 149 THR CB C 71.16 0.023 1 669 152 149 THR N N 111.901 0.011 1 670 153 150 THR H H 8.168 0.007 1 671 153 150 THR C C 172.04 0 1 672 153 150 THR CA C 57.354 0 1 673 153 150 THR CB C 70.559 0 1 674 153 150 THR N N 111.942 0.024 1 675 154 151 PRO C C 177.602 0 1 676 154 151 PRO CA C 62.605 0.005 1 677 154 151 PRO CB C 35.236 0.021 1 678 155 152 THR H H 8.175 0.006 1 679 155 152 THR C C 171.619 0 1 680 155 152 THR CA C 63.375 0.095 1 681 155 152 THR CB C 71.737 0.061 1 682 155 152 THR N N 114.555 0.025 1 683 156 153 ALA H H 9.233 0.005 1 684 156 153 ALA C C 174.863 0.03 1 685 156 153 ALA CA C 50.379 0.002 1 686 156 153 ALA CB C 23.107 0.08 1 687 156 153 ALA N N 131.118 0.01 1 688 157 154 PHE H H 9.436 0.007 1 689 157 154 PHE C C 175.416 0.024 1 690 157 154 PHE CA C 56.246 0.023 1 691 157 154 PHE CB C 45.232 0.026 1 692 157 154 PHE N N 118.423 0.011 1 693 158 155 ILE H H 9.037 0.009 1 694 158 155 ILE C C 176.289 0.042 1 695 158 155 ILE CA C 60.525 0.053 1 696 158 155 ILE CB C 39.213 0.034 1 697 158 155 ILE N N 118.518 0.028 1 698 159 156 ASN H H 9.473 0.007 1 699 159 156 ASN C C 175.462 0.031 1 700 159 156 ASN CA C 54.228 0.03 1 701 159 156 ASN CB C 37.134 0.038 1 702 159 156 ASN N N 128.652 0.033 1 703 160 157 GLY H H 8.794 0.008 1 704 160 157 GLY C C 173.374 0 1 705 160 157 GLY CA C 45.749 0.056 1 706 160 157 GLY N N 103.626 0.019 1 707 161 158 GLU H H 8.228 0.008 1 708 161 158 GLU C C 175.028 0.02 1 709 161 158 GLU CA C 55.133 0.017 1 710 161 158 GLU CB C 31.095 0.071 1 711 161 158 GLU N N 122.902 0.041 1 712 162 159 LYS H H 8.535 0.008 1 713 162 159 LYS C C 176.123 0.008 1 714 162 159 LYS CA C 57.05 0.034 1 715 162 159 LYS CB C 32.98 0.083 1 716 162 159 LYS N N 127.013 0.005 1 717 163 160 VAL H H 8.212 0.006 1 718 163 160 VAL C C 176.412 0.034 1 719 163 160 VAL CA C 62.347 0.021 1 720 163 160 VAL CB C 31.155 0.045 1 721 163 160 VAL N N 128.579 0.016 1 722 164 161 GLU H H 8.432 0.006 1 723 164 161 GLU C C 176.449 0.056 1 724 164 161 GLU CA C 59.705 0.015 1 725 164 161 GLU CB C 29.885 0.071 1 726 164 161 GLU N N 128.37 0.004 1 727 165 162 ASP H H 7.259 0.009 1 728 165 162 ASP C C 174.531 0 1 729 165 162 ASP CA C 49.975 0 1 730 165 162 ASP CB C 41.459 0 1 731 165 162 ASP N N 115.07 0.024 1 732 166 163 PRO C C 175.846 0.023 1 733 166 163 PRO CA C 63.177 0.026 1 734 166 163 PRO CB C 31.575 0.061 1 735 167 164 TYR H H 7.597 0.009 1 736 167 164 TYR C C 173.988 0.013 1 737 167 164 TYR CA C 57.204 0.027 1 738 167 164 TYR CB C 38.004 0.064 1 739 167 164 TYR N N 116.702 0.02 1 740 168 165 ASP H H 7.437 0.009 1 741 168 165 ASP C C 176.7 0.02 1 742 168 165 ASP CA C 51.867 0.016 1 743 168 165 ASP CB C 43.086 0.037 1 744 168 165 ASP N N 119.75 0.025 1 745 169 166 TYR H H 9.264 0.007 1 746 169 166 TYR C C 177.007 0.063 1 747 169 166 TYR CA C 62.473 0.038 1 748 169 166 TYR CB C 39.226 0.069 1 749 169 166 TYR N N 127.782 0.03 1 750 170 167 GLU H H 8.568 0.008 1 751 170 167 GLU C C 178.573 0.06 1 752 170 167 GLU CA C 59.67 0.017 1 753 170 167 GLU CB C 29.031 0.074 1 754 170 167 GLU N N 117.246 0.022 1 755 171 168 SER H H 7.85 0.008 1 756 171 168 SER C C 176.338 0.011 1 757 171 168 SER CA C 62.123 0.052 1 758 171 168 SER CB C 63.977 0.051 1 759 171 168 SER N N 115.496 0.052 1 760 172 169 TYR H H 7.512 0.007 1 761 172 169 TYR C C 177.712 0.019 1 762 172 169 TYR CA C 60.448 0.043 1 763 172 169 TYR CB C 37.045 0.087 1 764 172 169 TYR N N 118.769 0.04 1 765 173 170 GLU H H 7.564 0.007 1 766 173 170 GLU C C 177.989 0.027 1 767 173 170 GLU CA C 60.043 0.099 1 768 173 170 GLU CB C 29.969 0.06 1 769 173 170 GLU N N 118.71 0.047 1 770 174 171 LYS H H 7.98 0.007 1 771 174 171 LYS C C 178.245 0.006 1 772 174 171 LYS CA C 59.741 0.027 1 773 174 171 LYS CB C 32.517 0.056 1 774 174 171 LYS N N 116.333 0.012 1 775 175 172 LEU H H 6.766 0.008 1 776 175 172 LEU C C 178.168 0.005 1 777 175 172 LEU CA C 56.275 0.011 1 778 175 172 LEU CB C 43.399 0.073 1 779 175 172 LEU N N 116.812 0.022 1 780 176 173 LEU H H 7.773 0.005 1 781 176 173 LEU C C 178.693 0.037 1 782 176 173 LEU CA C 56.874 0.063 1 783 176 173 LEU CB C 42.766 0.052 1 784 176 173 LEU N N 118.595 0.013 1 785 177 174 LYS H H 8.075 0.008 1 786 177 174 LYS C C 177.417 0.027 1 787 177 174 LYS CA C 59.605 0.037 1 788 177 174 LYS CB C 32.468 0.068 1 789 177 174 LYS N N 118.442 0.03 1 790 178 175 ASP H H 7.945 0.008 1 791 178 175 ASP C C 176.742 0.011 1 792 178 175 ASP CA C 55.254 0.003 1 793 178 175 ASP CB C 41.159 0.041 1 794 178 175 ASP N N 116.157 0.039 1 795 179 176 LYS H H 7.795 0.008 1 796 179 176 LYS C C 176.584 0.031 1 797 179 176 LYS CA C 56.569 0.054 1 798 179 176 LYS CB C 34.184 0.043 1 799 179 176 LYS N N 117.179 0.016 1 800 180 177 ILE H H 7.518 0.006 1 801 180 177 ILE C C 175.159 0.034 1 802 180 177 ILE CA C 60.694 0.012 1 803 180 177 ILE CB C 39.001 0.078 1 804 180 177 ILE N N 117.685 0.008 1 805 181 178 LYS H H 8.204 0.007 1 806 181 178 LYS C C 175.292 0.01 1 807 181 178 LYS CA C 56.012 0.042 1 808 181 178 LYS CB C 32.84 0.078 1 809 181 178 LYS N N 125.061 0.018 1 810 182 179 LEU H H 7.862 0.006 1 811 182 179 LEU C C 182.266 0 1 812 182 179 LEU CA C 56.812 0 1 813 182 179 LEU CB C 43.692 0 1 814 182 179 LEU N N 129.827 0.036 1 stop_ save_