data_17503 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Staphylococcus aureus FusB ; _BMRB_accession_number 17503 _BMRB_flat_file_name bmr17503.str _Entry_type original _Submission_date 2011-03-03 _Accession_date 2011-03-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone assignment of Staphylococcus aureus FusB, a protein that confers resistance to fusidic acid.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cox Georgina . . 2 O'Neill Alex J. . 3 Thompson Gary S. . 4 Kalverda Arnout P. . 5 Homans Steve W. . 6 Tomlinson Jennifer H. . 7 Edwards Thomas A. . 8 Jenkins Huw . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 168 "13C chemical shifts" 501 "15N chemical shifts" 169 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-02-17 original author . stop_ _Original_release_date 2012-02-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22308410 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cox Georgina . . 2 Thompson Gary S. . 3 Jenkins Huw T. . 4 Peske Frank . . 5 Savelsbergh Andreas . . 6 Rodnina Marina V. . 7 Wintermeyer Wolfgang . . 8 Homans Steve W. . 9 Edwards Thomas A. . 10 O'Neill Alexander J. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_volume 109 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2102 _Page_last 2107 _Year 2102 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name fusb _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label fusb $fusb stop_ _System_molecular_weight 27325.3922 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_fusb _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common fusb _Molecular_mass 27325.3922 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 233 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPNGSH MKTMIYPHQYNYIRSVILRL KNVYKTVNDKETVKVIQSET YNDINEIFGHIDDDIEESLK VLMNIRLSNKEIEAILNKFL EYVVPFELPSPQKLQKVFKK VKKIKIPQFEEYDLKVSSFV GWNELASNRKYIIYYDEKKQ LKGLYGEISNQVVKGFCTIC NKESNVSLFMKKSKTNSDGQ YVKKGDYICRDSIHCNKQLT DINQFYNFIDKLD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -19 MET 2 -18 GLY 3 -17 SER 4 -16 SER 5 -15 HIS 6 -14 HIS 7 -13 HIS 8 -12 HIS 9 -11 HIS 10 -10 HIS 11 -9 SER 12 -8 SER 13 -7 GLY 14 -6 LEU 15 -5 VAL 16 -4 PRO 17 -3 ASN 18 -2 GLY 19 -1 SER 20 0 HIS 21 1 MET 22 2 LYS 23 3 THR 24 4 MET 25 5 ILE 26 6 TYR 27 7 PRO 28 8 HIS 29 9 GLN 30 10 TYR 31 11 ASN 32 12 TYR 33 13 ILE 34 14 ARG 35 15 SER 36 16 VAL 37 17 ILE 38 18 LEU 39 19 ARG 40 20 LEU 41 21 LYS 42 22 ASN 43 23 VAL 44 24 TYR 45 25 LYS 46 26 THR 47 27 VAL 48 28 ASN 49 29 ASP 50 30 LYS 51 31 GLU 52 32 THR 53 33 VAL 54 34 LYS 55 35 VAL 56 36 ILE 57 37 GLN 58 38 SER 59 39 GLU 60 40 THR 61 41 TYR 62 42 ASN 63 43 ASP 64 44 ILE 65 45 ASN 66 46 GLU 67 47 ILE 68 48 PHE 69 49 GLY 70 50 HIS 71 51 ILE 72 52 ASP 73 53 ASP 74 54 ASP 75 55 ILE 76 56 GLU 77 57 GLU 78 58 SER 79 59 LEU 80 60 LYS 81 61 VAL 82 62 LEU 83 63 MET 84 64 ASN 85 65 ILE 86 66 ARG 87 67 LEU 88 68 SER 89 69 ASN 90 70 LYS 91 71 GLU 92 72 ILE 93 73 GLU 94 74 ALA 95 75 ILE 96 76 LEU 97 77 ASN 98 78 LYS 99 79 PHE 100 80 LEU 101 81 GLU 102 82 TYR 103 83 VAL 104 84 VAL 105 85 PRO 106 86 PHE 107 87 GLU 108 88 LEU 109 89 PRO 110 90 SER 111 91 PRO 112 92 GLN 113 93 LYS 114 94 LEU 115 95 GLN 116 96 LYS 117 97 VAL 118 98 PHE 119 99 LYS 120 100 LYS 121 101 VAL 122 102 LYS 123 103 LYS 124 104 ILE 125 105 LYS 126 106 ILE 127 107 PRO 128 108 GLN 129 109 PHE 130 110 GLU 131 111 GLU 132 112 TYR 133 113 ASP 134 114 LEU 135 115 LYS 136 116 VAL 137 117 SER 138 118 SER 139 119 PHE 140 120 VAL 141 121 GLY 142 122 TRP 143 123 ASN 144 124 GLU 145 125 LEU 146 126 ALA 147 127 SER 148 128 ASN 149 129 ARG 150 130 LYS 151 131 TYR 152 132 ILE 153 133 ILE 154 134 TYR 155 135 TYR 156 136 ASP 157 137 GLU 158 138 LYS 159 139 LYS 160 140 GLN 161 141 LEU 162 142 LYS 163 143 GLY 164 144 LEU 165 145 TYR 166 146 GLY 167 147 GLU 168 148 ILE 169 149 SER 170 150 ASN 171 151 GLN 172 152 VAL 173 153 VAL 174 154 LYS 175 155 GLY 176 156 PHE 177 157 CYS 178 158 THR 179 159 ILE 180 160 CYS 181 161 ASN 182 162 LYS 183 163 GLU 184 164 SER 185 165 ASN 186 166 VAL 187 167 SER 188 168 LEU 189 169 PHE 190 170 MET 191 171 LYS 192 172 LYS 193 173 SER 194 174 LYS 195 175 THR 196 176 ASN 197 177 SER 198 178 ASP 199 179 GLY 200 180 GLN 201 181 TYR 202 182 VAL 203 183 LYS 204 184 LYS 205 185 GLY 206 186 ASP 207 187 TYR 208 188 ILE 209 189 CYS 210 190 ARG 211 191 ASP 212 192 SER 213 193 ILE 214 194 HIS 215 195 CYS 216 196 ASN 217 197 LYS 218 198 GLN 219 199 LEU 220 200 THR 221 201 ASP 222 202 ILE 223 203 ASN 224 204 GLN 225 205 PHE 226 206 TYR 227 207 ASN 228 208 PHE 229 209 ILE 230 210 ASP 231 211 LYS 232 212 LEU 233 213 ASP 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 PDB 4E4B "Structure Of The Fusidic Acid Resistance Protein Fusb" 92.70 216 100.00 100.00 4.06e-153 DBJ BAO09119 "fusidic acid resistance protein [Staphylococcus epidermidis]" 91.42 213 100.00 100.00 2.24e-150 DBJ BAO09144 "fusidic acid resistance protein [Staphylococcus epidermidis]" 91.42 213 100.00 100.00 2.24e-150 EMBL CAJ43426 "fusidic acid resistance protein [Staphylococcus haemolyticus]" 90.13 210 100.00 100.00 6.26e-148 EMBL CAL23838 "FusB protein [Staphylococcus aureus]" 91.42 213 100.00 100.00 2.24e-150 EMBL CQA10371 "Fibronectin-binding protein (FBP) [Mycobacterium abscessus]" 91.42 213 100.00 100.00 2.24e-150 EMBL CQD31768 "Far1 [Staphylococcus capitis]" 91.42 213 100.00 100.00 2.24e-150 EMBL CRI24900 "Far1 [Staphylococcus aureus]" 91.42 213 100.00 100.00 2.24e-150 GB AAL12234 "FusB [Staphylococcus aureus]" 91.42 213 100.00 100.00 2.24e-150 GB AAN07146 "Far1 [Staphylococcus aureus]" 91.42 213 100.00 100.00 2.24e-150 GB ABB82610 "fusidic acid resistance [Staphylococcus aureus]" 91.42 213 100.00 100.00 2.24e-150 GB AEU08355 "fusidic acid resistance protein [Staphylococcus epidermidis]" 91.42 213 99.53 100.00 9.69e-150 GB AEU08384 "fusidic acid resistance protein [Staphylococcus epidermidis]" 91.42 213 100.00 100.00 2.24e-150 REF NP_932197 "Far1 [Staphylococcus aureus]" 91.42 213 100.00 100.00 2.24e-150 REF WP_000855537 "MULTISPECIES: fusidic acid resistance protein FusB [Staphylococcus]" 91.42 213 100.00 100.00 2.24e-150 REF WP_032491632 "fusidic acid resistance protein FusB [Staphylococcus haemolyticus]" 90.13 210 100.00 100.00 6.26e-148 REF YP_009078429 "FusB [Staphylococcus aureus]" 91.42 213 100.00 100.00 2.24e-150 REF YP_009080413 "fusidic acid resistance protein [Staphylococcus haemolyticus]" 90.13 210 100.00 100.00 6.26e-148 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $fusb firmicutes 1280 Bacteria . Staphylococcus aureus fusB 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 $fusb 'recombinant technology' 'Escherichia coli' Escherichia coli 'BL21 (DE3) Rosetta' pET-28a-fusB stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_FusB_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $fusb 0.3 mM '[[U-95% 13C; U-95% 15N; U-95% 2H]]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' Tris-HCl 20 mM 'natural abundance' NaCl 300 mM 'natural abundance' DTT 1 mM 'natural abundance' stop_ save_ save_15N-val-FusB _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $fusb 0.78 mM [U-15N]-Val H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' Tris-HCl 20 mM 'natural abundance' NaCl 300 mM 'natural abundance' DTT 1 mM 'natural abundance' stop_ save_ save_15N-ile-FusB _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $fusb 0.72 mM [U-15N]-Ile H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' Tris-HCl 20 mM 'natural abundance' NaCl 300 mM 'natural abundance' DTT 1 mM 'natural abundance' stop_ save_ save_15N-tyr-FusB _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $fusb 0.68 mM [U-15N]-Tyr H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' Tris-HCl 20 mM 'natural abundance' NaCl 300 mM 'natural abundance' DTT 1 mM 'natural abundance' stop_ save_ save_15N-leu-FusB _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $fusb 0.8 mM [U-15N]-Leu H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' Tris-HCl 20 mM 'natural abundance' NaCl 300 mM 'natural abundance' DTT 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CCPNMR_Analysis_1.0 _Saveframe_category software _Name ANALYSIS _Version 1.0 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task assignment stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_CcpNmr_Analysis_2.1 _Saveframe_category software _Name ANALYSIS _Version 2.1 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task assignment stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_nmrPipe _Saveframe_category software _Name NMRPipe _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Frank Delaglio, Stephan Grzesiek, Guang Zhu, Geerten W. Vuister, John Pfeifer, and Ad Bax' 'Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda MD 20892 USA' http://spin.niddk.nih.gov/NMRPipe/ stop_ loop_ _Task 'processing spectra' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 749 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $FusB_1 save_ save_3D_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $FusB_1 save_ save_hncaco_(H[N[ca[CO]]])_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'hncaco (H[N[ca[CO]]])' _Sample_label $FusB_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $FusB_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $FusB_1 save_ save_hncocacb_(H[N[co[{CA|ca[C]}]]])_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'hncocacb (H[N[co[{CA|ca[C]}]]])' _Sample_label $FusB_1 save_ save_2D_1H-15N_HSQC/HMQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $FusB_1 save_ save_2D_1H-15N_HSQC/HMQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $15N-val-FusB save_ save_2D_1H-15N_HSQC/HMQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $15N-ile-FusB save_ save_2D_1H-15N_HSQC/HMQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $15N-tyr-FusB save_ save_2D_1H-15N_HSQC/HMQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $15N-leu-FusB save_ ####################### # Sample conditions # ####################### save_FusB_buffer _Saveframe_category sample_conditions _Details '20 mM TRis-HCl, 300 mM NaCl, 1 mM DTT' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.300 . M pH 8.000 . pH pressure 1.000 . atm temperature 298.0 . 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 0.0 internal indirect . . . 0.25144953 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.00000000 DSS N 15 'methyl protons' ppm 0.0 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCA' '3D HN(CO)CA' 'hncaco (H[N[ca[CO]]])' '3D HNCO' '3D HNCACB' 'hncocacb (H[N[co[{CA|ca[C]}]]])' '2D 1H-15N HSQC/HMQC' stop_ loop_ _Sample_label $FusB_1 $15N-val-FusB $15N-ile-FusB $15N-tyr-FusB $15N-leu-FusB stop_ _Sample_conditions_label $FusB_buffer _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name fusb _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 -7 13 GLY CA C 44.820 0.037 1 2 -6 14 LEU H H 8.025 0.008 1 3 -6 14 LEU CA C 54.674 0.011 1 4 -6 14 LEU CB C 41.214 0.075 1 5 -6 14 LEU N N 121.257 0.036 1 6 -5 15 VAL H H 8.049 0.023 1 7 -5 15 VAL C C 174.456 0.019 1 8 -5 15 VAL CA C 59.290 0.017 1 9 -5 15 VAL CB C 31.616 0.041 1 10 -5 15 VAL N N 122.179 0.159 1 11 2 22 LYS H H 8.338 0.008 1 12 2 22 LYS C C 177.581 0.044 1 13 2 22 LYS CA C 56.080 0.067 1 14 2 22 LYS CB C 32.684 0.055 1 15 2 22 LYS N N 122.404 0.026 1 16 3 23 THR H H 8.321 0.004 1 17 3 23 THR CA C 61.871 0.009 1 18 3 23 THR CB C 69.012 0.022 1 19 3 23 THR N N 117.992 0.047 1 20 4 24 MET H H 8.092 0.005 1 21 4 24 MET C C 175.343 0.001 1 22 4 24 MET CB C 33.798 0.012 1 23 4 24 MET N N 121.792 0.029 1 24 5 25 ILE H H 8.527 0.008 1 25 5 25 ILE C C 173.883 0.022 1 26 5 25 ILE CA C 58.605 0.007 1 27 5 25 ILE CB C 40.637 0.082 1 28 5 25 ILE N N 114.511 0.014 1 29 6 26 TYR H H 8.612 0.006 1 30 6 26 TYR C C 175.975 0.020 1 31 6 26 TYR CA C 56.951 0.036 1 32 6 26 TYR CB C 37.912 0.050 1 33 6 26 TYR N N 118.544 0.025 1 34 7 27 PRO C C 177.372 0.032 1 35 7 27 PRO CA C 66.727 0.024 1 36 8 28 HIS H H 8.390 0.007 1 37 8 28 HIS C C 176.965 0.008 1 38 8 28 HIS CA C 59.177 0.054 1 39 8 28 HIS CB C 27.863 0.103 1 40 8 28 HIS N N 111.709 0.066 1 41 9 29 GLN H H 6.766 0.006 1 42 9 29 GLN C C 178.435 0.027 1 43 9 29 GLN CA C 57.241 0.029 1 44 9 29 GLN CB C 28.120 0.058 1 45 9 29 GLN N N 118.562 0.027 1 46 10 30 TYR H H 7.911 0.01 1 47 10 30 TYR C C 176.677 0.041 1 48 10 30 TYR CA C 61.716 0.059 1 49 10 30 TYR CB C 37.073 0.006 1 50 10 30 TYR N N 120.945 0.031 1 51 11 31 ASN H H 8.658 0.007 1 52 11 31 ASN C C 179.171 0.02 1 53 11 31 ASN CA C 55.382 0.009 1 54 11 31 ASN CB C 36.106 0.034 1 55 11 31 ASN N N 117.947 0.02 1 56 12 32 TYR H H 8.344 0.006 1 57 12 32 TYR C C 177.520 0.01 1 58 12 32 TYR CA C 61.927 0.032 1 59 12 32 TYR CB C 36.993 0.186 1 60 12 32 TYR N N 122.949 0.027 1 61 13 33 ILE H H 8.519 0.004 1 62 13 33 ILE C C 177.029 0.013 1 63 13 33 ILE CA C 64.861 0.059 1 64 13 33 ILE CB C 36.026 0.040 1 65 13 33 ILE N N 121.909 0.029 1 66 14 34 ARG H H 8.579 0.007 1 67 14 34 ARG C C 177.226 0.001 1 68 14 34 ARG CA C 59.757 0.016 1 69 14 34 ARG CB C 28.217 0.06 1 70 14 34 ARG N N 119.460 0.026 1 71 15 35 SER H H 7.710 0.01 1 72 15 35 SER C C 177.360 0.011 1 73 15 35 SER CA C 61.370 00.015 1 74 15 35 SER CB C 62.048 0.067 1 75 15 35 SER N N 113.473 0.023 1 76 16 36 VAL H H 7.941 0.018 1 77 16 36 VAL C C 179.004 0.019 1 78 16 36 VAL CA C 64.986 0.017 1 79 16 36 VAL CB C 30.367 0.041 1 80 16 36 VAL N N 120.975 0.249 1 81 17 37 ILE C C 176.941 0.021 1 82 17 37 ILE CA C 65.771 0.021 1 83 17 37 ILE CB C 36.237 0.040 1 84 18 38 LEU H H 8.265 0.008 1 85 18 38 LEU C C 180.360 0.001 1 86 18 38 LEU CA C 57.516 0.028 1 87 18 38 LEU CB C 39.112 0.014 1 88 18 38 LEU N N 119.417 0.026 1 89 19 39 ARG H H 7.797 0.006 1 90 19 39 ARG C C 178.204 0.014 1 91 19 39 ARG CA C 58.874 0.004 1 92 19 39 ARG CB C 28.893 0.062 1 93 19 39 ARG N N 120.723 0.021 1 94 20 40 LEU H H 7.754 0.008 1 95 20 40 LEU C C 176.852 0.035 1 96 20 40 LEU CA C 57.307 0.014 1 97 20 40 LEU CB C 40.171 0.056 1 98 20 40 LEU N N 122.020 0.034 1 99 21 41 LYS H H 7.982 0.008 1 100 21 41 LYS C C 178.095 0.026 1 101 21 41 LYS CA C 58.218 0.014 1 102 21 41 LYS CB C 30.734 0.079 1 103 21 41 LYS N N 116.527 0.07 1 104 22 42 ASN H H 7.650 0.009 1 105 22 42 ASN C C 178.959 0.017 1 106 22 42 ASN CA C 56.357 0.019 1 107 22 42 ASN CB C 38.188 0.049 1 108 22 42 ASN N N 116.116 0.066 1 109 23 43 VAL H H 8.391 0.015 1 110 23 43 VAL C C 177.845 0.007 1 111 23 43 VAL CA C 66.280 0.03 1 112 23 43 VAL CB C 30.004 0.046 1 113 23 43 VAL N N 125.156 0.218 1 114 24 44 TYR H H 8.440 0.007 1 115 24 44 TYR C C 178.987 0.015 1 116 24 44 TYR CA C 56.384 0.039 1 117 24 44 TYR CB C 35.482 0.024 1 118 24 44 TYR N N 118.178 0.015 1 119 25 45 LYS H H 7.731 0.007 1 120 25 45 LYS C C 178.094 0.028 1 121 25 45 LYS CA C 57.465 0.028 1 122 25 45 LYS CB C 32.638 0.03 1 123 25 45 LYS N N 115.963 0.033 1 124 26 46 THR H H 7.808 0.007 1 125 26 46 THR C C 174.957 0.014 1 126 26 46 THR CA C 62.327 0.011 1 127 26 46 THR CB C 71.299 0.063 1 128 26 46 THR N N 106.894 0.029 1 129 27 47 VAL H H 8.601 0.024 1 130 27 47 VAL C C 174.918 0.019 1 131 27 47 VAL CA C 62.589 0.017 1 132 27 47 VAL CB C 30.704 0.041 1 133 27 47 VAL N N 124.854 0.227 1 134 31 51 GLU H H 8.518 0.007 1 135 31 51 GLU C C 179.041 0.054 1 136 31 51 GLU CA C 58.735 0.054 1 137 31 51 GLU CB C 27.694 0.051 1 138 31 51 GLU N N 118.872 0.023 1 139 32 52 THR H H 7.741 0.007 1 140 32 52 THR C C 176.293 0.007 1 141 32 52 THR CA C 66.159 0.025 1 142 32 52 THR CB C 67.428 0.115 1 143 32 52 THR N N 117.530 0.029 1 144 33 53 VAL H H 7.722 0.018 1 145 33 53 VAL C C 177.159 0.033 1 146 33 53 VAL CA C 67.055 0.018 1 147 33 53 VAL CB C 30.561 0.047 1 148 33 53 VAL N N 120.071 0.25 1 149 34 54 LYS H H 7.758 0.007 1 150 34 54 LYS C C 179.875 0.026 1 151 34 54 LYS CA C 59.000 0.025 1 152 34 54 LYS CB C 31.244 0.054 1 153 34 54 LYS N N 118.253 0.058 1 154 35 55 VAL H H 7.768 0.02 1 155 35 55 VAL C C 178.704 0.024 1 156 35 55 VAL CA C 66.134 0.017 1 157 35 55 VAL CB C 30.846 0.041 1 158 35 55 VAL N N 120.474 0.235 1 159 36 56 ILE H H 7.980 0.006 1 160 36 56 ILE C C 180.808 0.011 1 161 36 56 ILE CA C 63.703 0.053 1 162 36 56 ILE CB C 36.308 0.018 1 163 36 56 ILE N N 120.926 0.025 1 164 37 57 GLN H H 9.287 0.005 1 165 37 57 GLN C C 177.918 0.06 1 166 37 57 GLN CA C 60.308 0.011 1 167 37 57 GLN CB C 28.370 0.067 1 168 37 57 GLN N N 123.710 0.032 1 169 38 58 SER H H 8.131 0.008 1 170 38 58 SER C C 176.874 0.009 1 171 38 58 SER CA C 61.520 0.02 1 172 38 58 SER CB C 62.082 0.078 1 173 38 58 SER N N 114.695 0.022 1 174 39 59 GLU H H 8.498 0.009 1 175 39 59 GLU C C 178.952 0.024 1 176 39 59 GLU CA C 59.117 0.034 1 177 39 59 GLU CB C 29.140 0.146 1 178 39 59 GLU N N 121.782 0.066 1 179 40 60 THR H H 8.278 0.007 1 180 40 60 THR C C 175.295 0.023 1 181 40 60 THR CA C 67.113 0.031 1 182 40 60 THR CB C 67.814 0.005 1 183 40 60 THR N N 115.955 0.038 1 184 41 61 TYR H H 8.486 0.005 1 185 41 61 TYR C C 177.751 0.022 1 186 41 61 TYR CA C 61.925 0.029 1 187 41 61 TYR CB C 37.759 0.016 1 188 41 61 TYR N N 121.675 0.05 1 189 42 62 ASN H H 8.507 0.007 1 190 42 62 ASN C C 177.508 0.032 1 191 42 62 ASN CA C 56.194 0.02 1 192 42 62 ASN CB C 37.484 0.007 1 193 42 62 ASN N N 117.091 0.02 1 194 43 63 ASP H H 8.534 0.006 1 195 43 63 ASP C C 178.831 0.014 1 196 43 63 ASP CA C 57.010 0.034 1 197 43 63 ASP CB C 40.373 0.147 1 198 43 63 ASP N N 120.940 0.028 1 199 44 64 ILE H H 7.939 0.008 1 200 44 64 ILE C C 177.591 0.043 1 201 44 64 ILE CA C 65.421 0.022 1 202 44 64 ILE CB C 36.553 0.040 1 203 44 64 ILE N N 117.401 0.024 1 204 45 65 ASN H H 8.314 0.007 1 205 45 65 ASN C C 177.688 0.023 1 206 45 65 ASN CA C 56.558 0.019 1 207 45 65 ASN CB C 38.753 0.033 1 208 45 65 ASN N N 117.700 0.026 1 209 46 66 GLU H H 8.324 0.007 1 210 46 66 GLU C C 178.618 0.033 1 211 46 66 GLU CA C 58.478 0.025 1 212 46 66 GLU CB C 28.648 0.016 1 213 46 66 GLU N N 118.128 0.033 1 214 47 67 ILE H H 7.563 0.008 1 215 47 67 ILE C C 176.994 0.014 1 216 47 67 ILE CA C 63.601 0.038 1 217 47 67 ILE CB C 36.852 0.022 1 218 47 67 ILE N N 119.061 0.02 1 219 48 68 PHE H H 7.600 0.009 1 220 48 68 PHE C C 177.792 0.033 1 221 48 68 PHE CA C 60.701 0.021 1 222 48 68 PHE CB C 39.538 0.026 1 223 48 68 PHE N N 114.852 0.011 1 224 49 69 GLY H H 8.246 0.001 1 225 49 69 GLY C C 173.897 0.007 1 226 49 69 GLY CA C 46.245 0.013 1 227 49 69 GLY N N 109.402 0.028 1 228 50 70 HIS H H 7.888 0.006 1 229 50 70 HIS CA C 55.310 0.011 1 230 50 70 HIS CB C 30.903 0.061 1 231 50 70 HIS N N 120.955 0.008 1 232 51 71 ILE H H 8.044 0.007 1 233 51 71 ILE C C 174.365 0.033 1 234 51 71 ILE CA C 59.501 0.008 1 235 51 71 ILE CB C 37.439 0.115 1 236 51 71 ILE N N 121.235 0.03 1 237 52 72 ASP H H 7.058 0.005 1 238 52 72 ASP C C 175.876 0.041 1 239 52 72 ASP CA C 52.056 0.006 1 240 52 72 ASP CB C 41.273 0.104 1 241 52 72 ASP N N 123.058 0.024 1 242 53 73 ASP H H 8.349 0.008 1 243 53 73 ASP C C 178.265 0.078 1 244 53 73 ASP CA C 57.139 0.032 1 245 53 73 ASP CB C 40.295 0.341 1 246 53 73 ASP N N 117.418 0.04 1 247 54 74 ASP H H 8.218 0.008 1 248 54 74 ASP C C 179.379 0.296 1 249 54 74 ASP CA C 56.599 0.043 1 250 54 74 ASP CB C 39.966 0.072 1 251 54 74 ASP N N 119.672 0.024 1 252 55 75 ILE H H 8.557 0.008 1 253 55 75 ILE C C 177.802 0.035 1 254 55 75 ILE CA C 63.984 0.023 1 255 55 75 ILE CB C 36.469 0.056 1 256 55 75 ILE N N 123.183 0.097 1 257 56 76 GLU H H 8.492 0.007 1 258 56 76 GLU C C 179.005 0.018 1 259 56 76 GLU CA C 59.825 0.004 1 260 56 76 GLU N N 121.201 0.058 1 261 57 77 GLU H H 8.010 0.008 1 262 57 77 GLU C C 179.048 0.325 1 263 57 77 GLU CA C 59.001 0.039 1 264 57 77 GLU CB C 28.292 0.006 1 265 57 77 GLU N N 118.024 0.023 1 266 59 79 LEU H H 8.487 0.007 1 267 59 79 LEU C C 178.492 0.002 1 268 59 79 LEU CA C 57.552 0.034 1 269 59 79 LEU CB C 39.957 0.037 1 270 59 79 LEU N N 120.851 0.11 1 271 60 80 LYS H H 7.853 0.008 1 272 60 80 LYS C C 180.385 0.02 1 273 60 80 LYS CA C 59.558 0.034 1 274 60 80 LYS CB C 31.212 0.037 1 275 60 80 LYS N N 118.217 0.026 1 276 61 81 VAL H H 7.522 0.02 1 277 61 81 VAL C C 178.516 0.017 1 278 61 81 VAL CA C 65.630 0.008 1 279 61 81 VAL CB C 30.679 0.005 1 280 61 81 VAL N N 120.815 0.251 1 281 62 82 LEU H H 7.771 0.007 1 282 62 82 LEU C C 177.527 0.004 1 283 62 82 LEU CA C 56.366 0.008 1 284 62 82 LEU CB C 41.327 0.006 1 285 62 82 LEU N N 116.103 0.03 1 286 63 83 MET H H 7.561 0.007 1 287 63 83 MET C C 174.198 0.018 1 288 63 83 MET CA C 53.634 0.012 1 289 63 83 MET CB C 31.833 0.006 1 290 63 83 MET N N 113.991 0.016 1 291 64 84 ASN H H 7.399 0.009 1 292 64 84 ASN C C 175.245 0.015 1 293 64 84 ASN CA C 51.353 0.003 1 294 64 84 ASN CB C 38.829 0.004 1 295 64 84 ASN N N 120.144 0.015 1 296 65 85 ILE H H 8.036 0.005 1 297 65 85 ILE C C 176.835 0.032 1 298 65 85 ILE CA C 62.574 0.002 1 299 65 85 ILE CB C 36.433 0.025 1 300 65 85 ILE N N 122.177 0.045 1 301 66 86 ARG C C 175.151 0.016 1 302 66 86 ARG CA C 54.939 0.02 1 303 66 86 ARG CB C 27.667 0.058 1 304 66 86 ARG N N 119.311 0.027 1 305 67 87 LEU H H 7.628 0.004 1 306 67 87 LEU C C 175.692 0.01 1 307 67 87 LEU CA C 56.063 0.008 1 308 67 87 LEU CB C 41.913 0.058 1 309 67 87 LEU N N 123.997 0.02 1 310 68 88 SER H H 9.069 0.007 1 311 68 88 SER C C 175.189 0.013 1 312 68 88 SER CA C 55.787 0.015 1 313 68 88 SER CB C 66.374 0.078 1 314 68 88 SER N N 123.884 0.038 1 315 71 91 GLU H H 7.734 0.006 1 316 71 91 GLU C C 179.293 0.024 1 317 71 91 GLU CA C 58.702 0.027 1 318 71 91 GLU CB C 28.998 0.054 1 319 71 91 GLU N N 120.675 0.032 1 320 72 92 ILE H H 8.015 0.008 1 321 72 92 ILE C C 177.125 0.027 1 322 72 92 ILE CA C 65.847 0.006 1 323 72 92 ILE CB C 36.701 0.002 1 324 72 92 ILE N N 119.285 0.013 1 325 73 93 GLU H H 8.018 0.005 1 326 73 93 GLU C C 178.761 0.062 1 327 73 93 GLU CA C 58.932 0.04 1 328 73 93 GLU N N 118.229 0.143 1 329 74 94 ALA H H 7.624 0.008 1 330 74 94 ALA C C 181.284 0.026 1 331 74 94 ALA CA C 54.697 0.015 1 332 74 94 ALA CB C 17.331 0.031 1 333 74 94 ALA N N 120.539 0.028 1 334 75 95 ILE H H 8.241 0.008 1 335 75 95 ILE C C 177.456 0.025 1 336 75 95 ILE CA C 64.542 0.034 1 337 75 95 ILE CB C 36.836 0.016 1 338 75 95 ILE N N 121.534 0.032 1 339 76 96 LEU H H 8.745 0.006 1 340 76 96 LEU C C 180.629 0.039 1 341 76 96 LEU CA C 57.880 0.02 1 342 76 96 LEU CB C 38.843 0.052 1 343 76 96 LEU N N 118.894 0.027 1 344 77 97 ASN H H 8.218 0.008 1 345 77 97 ASN C C 177.781 0.038 1 346 77 97 ASN CA C 55.730 0.047 1 347 77 97 ASN CB C 37.733 0.034 1 348 77 97 ASN N N 118.398 0.021 1 349 78 98 LYS H H 7.936 0.005 1 350 78 98 LYS C C 179.564 0.009 1 351 78 98 LYS CA C 57.877 0.01 1 352 78 98 LYS CB C 29.303 0.055 1 353 78 98 LYS N N 122.309 0.04 1 354 79 99 PHE H H 8.799 0.006 1 355 79 99 PHE C C 178.230 0.022 1 356 79 99 PHE CA C 57.986 0.019 1 357 79 99 PHE CB C 36.401 0.068 1 358 79 99 PHE N N 116.561 0.021 1 359 80 100 LEU H H 8.034 0.008 1 360 80 100 LEU C C 179.830 0.027 1 361 80 100 LEU CA C 56.940 0.024 1 362 80 100 LEU CB C 41.117 0.025 1 363 80 100 LEU N N 119.606 0.025 1 364 81 101 GLU H H 7.740 0.005 1 365 81 101 GLU C C 177.562 0.038 1 366 81 101 GLU CA C 57.950 0.008 1 367 81 101 GLU CB C 28.042 0.008 1 368 81 101 GLU N N 117.464 0.034 1 369 82 102 TYR H H 7.816 0.009 1 370 82 102 TYR C C 174.571 0.012 1 371 82 102 TYR CA C 57.668 0.036 1 372 82 102 TYR CB C 37.842 0.050 1 373 82 102 TYR N N 116.003 0.096 1 374 83 103 VAL H H 7.193 0.023 1 375 83 103 VAL C C 176.636 0.019 1 376 83 103 VAL CA C 61.045 0.023 1 377 83 103 VAL CB C 32.187 0.026 1 378 83 103 VAL N N 119.887 0.242 1 379 84 104 VAL H H 8.423 0.019 1 380 84 104 VAL C C 173.668 0.019 1 381 84 104 VAL CA C 58.616 0.017 1 382 84 104 VAL CB C 31.617 0.041 1 383 84 104 VAL N N 130.128 0.31 1 384 85 105 PRO C C 176.141 0.032 1 385 85 105 PRO CA C 61.377 0.024 1 386 85 105 PRO CB C 31.582 0.069 1 387 86 106 PHE H H 7.874 0.007 1 388 86 106 PHE C C 175.098 0.025 1 389 86 106 PHE CA C 59.272 0.007 1 390 86 106 PHE CB C 38.489 0.079 1 391 86 106 PHE N N 121.581 0.043 1 392 87 107 GLU H H 7.842 0.006 1 393 87 107 GLU C C 174.973 0.019 1 394 87 107 GLU CA C 54.385 0.027 1 395 87 107 GLU CB C 28.675 0.011 1 396 87 107 GLU N N 129.160 0.015 1 397 88 108 LEU H H 8.858 0.006 1 398 88 108 LEU C C 175.038 0.017 1 399 88 108 LEU CA C 52.786 0.021 1 400 88 108 LEU CB C 39.890 0.048 1 401 88 108 LEU N N 131.153 0.032 1 402 89 109 PRO C C 175.251 0.032 1 403 89 109 PRO CA C 61.011 0.024 1 404 89 109 PRO CB C 31.341 0.069 1 405 90 110 SER H H 8.093 0.008 1 406 90 110 SER C C 173.198 0.013 1 407 90 110 SER CA C 55.814 0.015 1 408 90 110 SER CB C 61.973 0.078 1 409 90 110 SER N N 115.311 0.052 1 410 93 113 LYS H H 7.693 0.008 1 411 93 113 LYS C C 179.399 0.011 1 412 93 113 LYS CA C 58.614 0.023 1 413 93 113 LYS CB C 31.373 0.003 1 414 93 113 LYS N N 120.640 0.03 1 415 94 114 LEU H H 8.292 0.006 1 416 94 114 LEU C C 178.435 0.019 1 417 94 114 LEU CA C 57.212 0.01 1 418 94 114 LEU CB C 40.975 0.001 1 419 94 114 LEU N N 119.588 0.023 1 420 95 115 GLN H H 8.033 0.014 1 421 95 115 GLN C C 177.553 0.01 1 422 95 115 GLN CA C 57.580 0.029 1 423 95 115 GLN CB C 27.600 0.008 1 424 95 115 GLN N N 116.300 0.02 1 425 96 116 LYS H H 7.194 0.015 1 426 96 116 LYS C C 178.458 0.004 1 427 96 116 LYS CA C 57.640 0.04 1 428 96 116 LYS CB C 31.406 0.055 1 429 96 116 LYS N N 115.459 0.045 1 430 97 117 VAL H H 7.439 0.017 1 431 97 117 VAL C C 176.697 0.022 1 432 97 117 VAL CA C 64.208 0.005 1 433 97 117 VAL CB C 31.122 0.041 1 434 97 117 VAL N N 117.806 0.292 1 435 98 118 PHE H H 7.565 0.007 1 436 98 118 PHE C C 176.055 0.062 1 437 98 118 PHE CA C 55.637 0.039 1 438 98 118 PHE CB C 37.421 0.068 1 439 98 118 PHE N N 119.404 0.014 1 440 99 119 LYS H H 7.451 0.007 1 441 99 119 LYS C C 175.949 0.028 1 442 99 119 LYS CA C 58.646 0.026 1 443 99 119 LYS CB C 31.401 0.055 1 444 99 119 LYS N N 119.039 0.039 1 445 103 123 LYS H H 8.586 0.008 1 446 103 123 LYS C C 175.073 0.056 1 447 103 123 LYS CA C 55.644 0.021 1 448 103 123 LYS CB C 30.743 0.047 1 449 103 123 LYS N N 124.736 0.029 1 450 104 124 ILE H H 7.960 0.006 1 451 104 124 ILE C C 174.119 0.02 1 452 104 124 ILE CA C 59.864 0.027 1 453 104 124 ILE CB C 38.280 0.041 1 454 104 124 ILE N N 122.738 0.054 1 455 105 125 LYS H H 8.228 0.008 1 456 105 125 LYS C C 174.275 0.009 1 457 105 125 LYS CA C 54.502 0.014 1 458 105 125 LYS CB C 32.805 0.008 1 459 105 125 LYS N N 127.271 0.028 1 460 106 126 ILE H H 8.028 0.008 1 461 106 126 ILE C C 173.843 0.021 1 462 106 126 ILE CA C 57.495 0.024 1 463 106 126 ILE CB C 38.263 0.040 1 464 106 126 ILE N N 125.633 0.024 1 465 112 132 TYR H H 7.757 0.009 1 466 112 132 TYR CA C 62.567 0.036 1 467 112 132 TYR CB C 41.411 0.050 1 468 112 132 TYR N N 115.948 0.022 1 469 118 138 SER C C 171.401 0.013 1 470 118 138 SER CA C 61.275 0.015 1 471 118 138 SER CB C 63.087 0.078 1 472 119 139 PHE H H 8.519 0.006 1 473 119 139 PHE C C 171.843 0.005 1 474 119 139 PHE CA C 54.927 0.001 1 475 119 139 PHE CB C 40.267 0.06 1 476 119 139 PHE N N 118.132 0.029 1 477 120 140 VAL H H 8.546 0.023 1 478 120 140 VAL C C 174.294 0.019 1 479 120 140 VAL CA C 60.836 0.017 1 480 120 140 VAL CB C 32.933 0.041 1 481 120 140 VAL N N 119.446 0.271 1 482 128 148 ASN H H 8.003 0.008 1 483 128 148 ASN C C 173.473 0.041 1 484 128 148 ASN CA C 54.569 0.081 1 485 128 148 ASN CB C 36.755 0.073 1 486 128 148 ASN N N 117.843 0.025 1 487 129 149 ARG H H 7.602 0.006 1 488 129 149 ARG C C 175.745 0.031 1 489 129 149 ARG CA C 54.884 0.03 1 490 129 149 ARG CB C 34.359 0.037 1 491 129 149 ARG N N 115.857 0.016 1 492 130 150 LYS H H 8.503 0.005 1 493 130 150 LYS C C 174.745 0.014 1 494 130 150 LYS CA C 54.770 0.007 1 495 130 150 LYS CB C 33.744 0.055 1 496 130 150 LYS N N 121.818 0.051 1 497 131 151 TYR H H 8.603 0.005 1 498 131 151 TYR C C 174.738 0.017 1 499 131 151 TYR CA C 56.730 0.018 1 500 131 151 TYR CB C 38.612 0.117 1 501 131 151 TYR N N 125.905 0.029 1 502 132 152 ILE H H 9.161 0.006 1 503 132 152 ILE C C 175.650 0.021 1 504 132 152 ILE CA C 60.216 0.024 1 505 132 152 ILE CB C 41.708 0.040 1 506 132 152 ILE N N 119.172 0.068 1 507 134 154 TYR H H 8.803 0.005 1 508 134 154 TYR C C 170.440 0.037 1 509 134 154 TYR CA C 56.120 0.032 1 510 134 154 TYR CB C 38.928 0.006 1 511 134 154 TYR N N 116.987 0.027 1 512 135 155 TYR H H 9.366 0.006 1 513 135 155 TYR C C 176.831 0.019 1 514 135 155 TYR CA C 56.285 0.016 1 515 135 155 TYR CB C 39.848 0.043 1 516 135 155 TYR N N 116.873 0.023 1 517 136 156 ASP H H 8.749 0.006 1 518 136 156 ASP C C 177.966 0.018 1 519 136 156 ASP CA C 52.137 0.073 1 520 136 156 ASP CB C 40.496 0.034 1 521 136 156 ASP N N 123.287 0.018 1 522 137 157 GLU H H 9.182 0.011 1 523 137 157 GLU C C 177.474 0.062 1 524 137 157 GLU CA C 58.624 0.011 1 525 137 157 GLU CB C 27.665 0.051 1 526 137 157 GLU N N 117.961 0.025 1 527 138 158 LYS H H 8.049 0.007 1 528 138 158 LYS C C 175.695 0.021 1 529 138 158 LYS CA C 54.935 0.01 1 530 138 158 LYS CB C 30.590 0.105 1 531 138 158 LYS N N 119.814 0.043 1 532 139 159 LYS H H 8.485 0.005 1 533 139 159 LYS C C 175.209 0.017 1 534 139 159 LYS CA C 57.253 0.019 1 535 139 159 LYS CB C 28.098 0.111 1 536 139 159 LYS N N 115.343 0.022 1 537 140 160 GLN H H 8.662 0.01 1 538 140 160 GLN C C 175.798 0.008 1 539 140 160 GLN CA C 54.064 0.019 1 540 140 160 GLN CB C 28.271 0.046 1 541 140 160 GLN N N 119.033 0.016 1 542 141 161 LEU H H 8.350 0.007 1 543 141 161 LEU C C 175.033 0.017 1 544 141 161 LEU CA C 54.842 0.01 1 545 141 161 LEU CB C 40.445 0.015 1 546 141 161 LEU N N 125.555 0.027 1 547 142 162 LYS H H 8.956 0.008 1 548 142 162 LYS C C 174.176 0.022 1 549 142 162 LYS CA C 52.881 0.021 1 550 142 162 LYS CB C 35.123 0.026 1 551 142 162 LYS N N 127.879 0.099 1 552 143 163 GLY H H 7.869 0.001 1 553 143 163 GLY C C 172.108 0.019 1 554 143 163 GLY CA C 45.508 0.029 1 555 143 163 GLY N N 102.687 0.062 1 556 144 164 LEU H H 9.829 0.005 1 557 144 164 LEU C C 173.552 0.037 1 558 144 164 LEU CA C 54.848 0.008 1 559 144 164 LEU CB C 43.344 0.127 1 560 144 164 LEU N N 120.289 0.025 1 561 145 165 TYR H H 8.292 0.007 1 562 145 165 TYR C C 173.723 0.015 1 563 145 165 TYR CA C 55.181 0.034 1 564 145 165 TYR CB C 41.137 0.021 1 565 145 165 TYR N N 114.523 0.019 1 566 146 166 GLY H H 8.332 0.003 1 567 146 166 GLY C C 171.272 0.029 1 568 146 166 GLY CA C 44.179 0.078 1 569 146 166 GLY N N 106.139 0.032 1 570 147 167 GLU H H 8.013 0.008 1 571 147 167 GLU C C 175.688 0.023 1 572 147 167 GLU CA C 54.757 0.026 1 573 147 167 GLU CB C 30.652 0.086 1 574 147 167 GLU N N 120.629 0.026 1 575 148 168 ILE H H 8.618 0.005 1 576 148 168 ILE C C 175.693 0.01 1 577 148 168 ILE CA C 56.196 0.026 1 578 148 168 ILE CB C 41.586 0.063 1 579 148 168 ILE N N 121.249 0.02 1 580 149 169 SER H H 8.391 0.005 1 581 149 169 SER C C 174.190 0.013 1 582 149 169 SER CA C 57.672 0.015 1 583 149 169 SER CB C 63.239 0.078 1 584 149 169 SER N N 120.627 0.016 1 585 151 171 GLN H H 8.205 0.007 1 586 151 171 GLN C C 175.940 0.019 1 587 151 171 GLN CA C 55.660 0.073 1 588 151 171 GLN CB C 28.463 0.045 1 589 151 171 GLN N N 118.604 0.037 1 590 152 172 VAL H H 8.727 0.014 1 591 152 172 VAL C C 174.907 0.003 1 592 152 172 VAL CA C 60.673 0.029 1 593 152 172 VAL CB C 32.380 0.04 1 594 152 172 VAL N N 128.414 0.242 1 595 153 173 VAL H H 9.150 0.025 1 596 153 173 VAL C C 174.011 0.018 1 597 153 173 VAL CA C 58.365 0.007 1 598 153 173 VAL CB C 34.609 0.014 1 599 153 173 VAL N N 123.289 0.253 1 600 154 174 LYS H H 8.216 0.005 1 601 154 174 LYS C C 176.947 0.022 1 602 154 174 LYS CA C 54.535 0.028 1 603 154 174 LYS CB C 30.219 0.055 1 604 154 174 LYS N N 122.299 0.021 1 605 155 175 GLY H H 8.540 0.002 1 606 155 175 GLY C C 170.578 0.008 1 607 155 175 GLY CA C 44.386 0.019 1 608 155 175 GLY N N 114.348 0.056 1 609 156 176 PHE H H 8.469 0.008 1 610 156 176 PHE C C 175.073 0.029 1 611 156 176 PHE CA C 57.919 0.007 1 612 156 176 PHE CB C 39.096 0.106 1 613 156 176 PHE N N 120.189 0.01 1 614 157 177 CYS H H 7.856 0.007 1 615 157 177 CYS C C 177.857 0.035 1 616 157 177 CYS CA C 58.076 0.057 1 617 157 177 CYS CB C 32.124 0.031 1 618 157 177 CYS N N 126.631 0.034 1 619 158 178 THR H H 8.802 0.007 1 620 158 178 THR C C 173.642 0.01 1 621 158 178 THR CA C 64.626 0.042 1 622 158 178 THR CB C 68.657 0.063 1 623 158 178 THR N N 123.060 0.023 1 624 159 179 ILE H H 9.712 0.012 1 625 159 179 ILE N N 124.688 0.102 1 626 161 181 ASN H H 7.802 0.006 1 627 161 181 ASN C C 173.469 0.025 1 628 161 181 ASN CA C 53.841 0.009 1 629 161 181 ASN CB C 36.666 0.035 1 630 161 181 ASN N N 117.941 0.033 1 631 162 182 LYS H H 7.514 0.006 1 632 162 182 LYS C C 175.965 0.045 1 633 162 182 LYS CA C 52.961 0.004 1 634 162 182 LYS CB C 33.795 0.023 1 635 162 182 LYS N N 116.154 0.017 1 636 163 183 GLU H H 8.264 0.005 1 637 163 183 GLU C C 176.704 0.062 1 638 163 183 GLU CA C 56.158 0.027 1 639 163 183 GLU CB C 28.279 0.078 1 640 163 183 GLU N N 121.528 0.083 1 641 164 184 SER H H 9.091 0.006 1 642 164 184 SER C C 172.687 0.027 1 643 164 184 SER CA C 54.684 0.002 1 644 164 184 SER CB C 63.557 0.035 1 645 164 184 SER N N 123.071 0.033 1 646 165 185 ASN H H 8.013 0.005 1 647 165 185 ASN C C 174.975 0.023 1 648 165 185 ASN CA C 52.068 0.014 1 649 165 185 ASN CB C 37.385 0.053 1 650 165 185 ASN N N 120.039 0.027 1 651 166 186 VAL H H 9.566 0.023 1 652 166 186 VAL C C 174.160 0.032 1 653 166 186 VAL CA C 58.700 0.027 1 654 166 186 VAL CB C 35.540 0.05 1 655 166 186 VAL N N 120.228 0.193 1 656 167 187 SER H H 8.903 0.009 1 657 167 187 SER C C 172.774 0.004 1 658 167 187 SER CA C 57.028 0.029 1 659 167 187 SER CB C 68.121 0.114 1 660 167 187 SER N N 113.407 0.047 1 661 168 188 LEU H H 8.828 0.008 1 662 168 188 LEU C C 174.771 0.021 1 663 168 188 LEU CA C 55.641 0.031 1 664 168 188 LEU CB C 41.453 0.153 1 665 168 188 LEU N N 125.615 0.127 1 666 169 189 PHE H H 8.850 0.006 1 667 169 189 PHE C C 174.359 0.002 1 668 169 189 PHE CA C 55.710 0.005 1 669 169 189 PHE CB C 41.663 0.068 1 670 169 189 PHE N N 128.374 0.033 1 671 170 190 MET H H 8.464 0.005 1 672 170 190 MET C C 174.100 0.011 1 673 170 190 MET CA C 53.077 0.005 1 674 170 190 MET CB C 34.091 0.024 1 675 170 190 MET N N 126.329 0.031 1 676 171 191 LYS H H 8.871 0.006 1 677 171 191 LYS C C 175.574 0.02 1 678 171 191 LYS CA C 56.013 0.034 1 679 171 191 LYS CB C 33.003 0.027 1 680 171 191 LYS N N 125.631 0.038 1 681 172 192 LYS H H 8.545 0.009 1 682 172 192 LYS CA C 55.675 0.026 1 683 172 192 LYS CB C 30.453 0.055 1 684 172 192 LYS N N 124.728 0.025 1 685 180 200 GLN C C 175.487 0.025 1 686 180 200 GLN CA C 55.196 0.036 1 687 180 200 GLN CB C 28.628 0.041 1 688 181 201 TYR H H 8.206 0.012 1 689 181 201 TYR C C 175.539 0.020 1 690 181 201 TYR CA C 57.190 0.034 1 691 181 201 TYR CB C 38.216 0.035 1 692 181 201 TYR N N 120.359 0.012 1 693 182 202 VAL H H 8.263 0.014 1 694 182 202 VAL C C 175.307 0.019 1 695 182 202 VAL CA C 61.407 0.006 1 696 182 202 VAL CB C 32.096 0.103 1 697 182 202 VAL N N 121.263 0.187 1 698 183 203 LYS H H 8.241 0.007 1 699 183 203 LYS C C 175.850 0.02 1 700 183 203 LYS CA C 55.455 0.084 1 701 183 203 LYS CB C 32.266 0.031 1 702 183 203 LYS N N 124.124 0.099 1 703 184 204 LYS H H 8.281 0.008 1 704 184 204 LYS C C 175.528 0.135 1 705 184 204 LYS CA C 55.347 0.022 1 706 184 204 LYS CB C 33.186 0.193 1 707 184 204 LYS N N 122.467 0.043 1 708 185 205 GLY H H 8.164 0.02 1 709 185 205 GLY C C 172.108 0.004 1 710 185 205 GLY CA C 44.698 0.044 1 711 185 205 GLY N N 107.877 0.023 1 712 186 206 ASP H H 8.393 0.005 1 713 186 206 ASP C C 175.466 0.007 1 714 186 206 ASP CA C 52.718 0.014 1 715 186 206 ASP CB C 45.159 0.007 1 716 186 206 ASP N N 116.986 0.029 1 717 187 207 TYR H H 9.572 0.006 1 718 187 207 TYR C C 176.363 0.008 1 719 187 207 TYR CA C 59.530 0.02 1 720 187 207 TYR CB C 37.964 0.022 1 721 187 207 TYR N N 121.375 0.025 1 722 188 208 ILE H H 8.599 0.007 1 723 188 208 ILE C C 175.692 0.021 1 724 188 208 ILE CA C 58.249 0.024 1 725 188 208 ILE N N 116.010 0.018 1 726 189 209 CYS H H 9.818 0.006 1 727 189 209 CYS C C 177.519 0.033 1 728 189 209 CYS CA C 63.086 0.050 1 729 189 209 CYS CB C 30.486 0.077 1 730 189 209 CYS N N 124.732 0.027 1 731 190 210 ARG H H 8.094 0.005 1 732 190 210 ARG C C 177.625 0.016 1 733 190 210 ARG CA C 59.281 0.005 1 734 190 210 ARG CB C 28.961 0.089 1 735 190 210 ARG N N 123.586 0.032 1 736 191 211 ASP H H 8.902 0.006 1 737 191 211 ASP C C 176.493 0.014 1 738 191 211 ASP CA C 51.834 0.036 1 739 191 211 ASP CB C 39.663 0.104 1 740 191 211 ASP N N 119.919 0.019 1 741 192 212 SER H H 9.385 0.009 1 742 192 212 SER C C 176.043 0.013 1 743 192 212 SER CA C 61.274 0.008 1 744 192 212 SER CB C 63.232 0.095 1 745 192 212 SER N N 120.193 0.083 1 746 193 213 ILE H H 8.434 0.004 1 747 193 213 ILE C C 177.213 0.012 1 748 193 213 ILE CA C 64.876 0.016 1 749 193 213 ILE CB C 35.361 0.004 1 750 193 213 ILE N N 126.092 0.025 1 751 194 214 HIS H H 6.991 0.007 1 752 194 214 HIS C C 176.907 0.008 1 753 194 214 HIS CA C 59.517 0.033 1 754 194 214 HIS CB C 29.952 0.144 1 755 194 214 HIS N N 120.481 0.027 1 756 195 215 CYS H H 7.554 0.007 1 757 195 215 CYS C C 177.749 0.031 1 758 195 215 CYS CA C 64.150 0.042 1 759 195 215 CYS CB C 31.843 0.054 1 760 195 215 CYS N N 121.204 0.058 1 761 196 216 ASN H H 7.581 0.002 1 762 196 216 ASN C C 178.710 0.023 1 763 196 216 ASN N N 114.185 0.026 1 764 198 218 GLN H H 7.482 0.007 1 765 198 218 GLN C C 175.141 0.007 1 766 198 218 GLN CA C 53.843 0.053 1 767 198 218 GLN CB C 28.179 0.024 1 768 198 218 GLN N N 113.770 0.024 1 769 199 219 LEU H H 7.617 0.004 1 770 199 219 LEU C C 176.221 0.008 1 771 199 219 LEU CA C 55.085 0.095 1 772 199 219 LEU N N 124.178 0.03 1 773 200 220 THR H H 8.731 0.006 1 774 200 220 THR C C 173.734 0.015 1 775 200 220 THR CA C 61.096 0.024 1 776 200 220 THR CB C 68.954 0.11 1 777 200 220 THR N N 114.010 0.025 1 778 201 221 ASP H H 7.097 0.007 1 779 201 221 ASP C C 176.778 0.015 1 780 201 221 ASP CA C 52.966 0.035 1 781 201 221 ASP CB C 41.653 0.03 1 782 201 221 ASP N N 118.668 0.035 1 783 202 222 ILE H H 6.683 0.003 1 784 202 222 ILE C C 175.741 0.01 1 785 202 222 ILE CA C 61.564 0.002 1 786 202 222 ILE N N 125.580 0.031 1 787 203 223 ASN H H 8.309 0.007 1 788 203 223 ASN C C 177.718 0.003 1 789 203 223 ASN CB C 36.968 0.013 1 790 203 223 ASN N N 120.124 0.026 1 791 204 224 GLN H H 7.650 0.007 1 792 204 224 GLN C C 179.190 0.046 1 793 204 224 GLN CA C 58.176 0.036 1 794 204 224 GLN N N 117.795 0.028 1 795 205 225 PHE H H 7.039 0.007 1 796 205 225 PHE C C 176.228 0.022 1 797 205 225 PHE CA C 60.701 0.046 1 798 205 225 PHE CB C 37.484 0.068 1 799 205 225 PHE N N 118.870 0.032 1 800 206 226 TYR H H 7.705 0.005 1 801 206 226 TYR C C 178.170 0.024 1 802 206 226 TYR CA C 58.648 0.079 1 803 206 226 TYR CB C 34.906 0.050 1 804 206 226 TYR N N 117.907 0.029 1 805 207 227 ASN H H 8.389 0.008 1 806 207 227 ASN C C 176.753 0.017 1 807 207 227 ASN CA C 55.605 0.006 1 808 207 227 ASN CB C 37.632 0.029 1 809 207 227 ASN N N 117.042 0.025 1 810 208 228 PHE H H 7.119 0.002 1 811 208 228 PHE C C 176.052 0.027 1 812 208 228 PHE CA C 59.702 0.01 1 813 208 228 PHE N N 120.391 0.026 1 814 209 229 ILE H H 7.259 0.008 1 815 209 229 ILE C C 179.211 0.007 1 816 209 229 ILE CA C 60.827 0.047 1 817 209 229 ILE CB C 34.447 0.040 1 818 209 229 ILE N N 117.654 0.038 1 819 210 230 ASP H H 7.932 0.006 1 820 210 230 ASP C C 177.718 0.017 1 821 210 230 ASP CA C 56.068 0.016 1 822 210 230 ASP CB C 40.398 0.095 1 823 210 230 ASP N N 118.848 0.037 1 824 211 231 LYS H H 7.295 0.008 1 825 211 231 LYS C C 177.245 0.012 1 826 211 231 LYS CA C 56.443 0.005 1 827 211 231 LYS CB C 31.111 0.052 1 828 211 231 LYS N N 117.283 0.028 1 829 212 232 LEU H H 7.313 0.006 1 830 212 232 LEU C C 176.319 0.006 1 831 212 232 LEU CA C 54.862 0.007 1 832 212 232 LEU CB C 41.160 0.011 1 833 212 232 LEU N N 119.737 0.03 1 834 213 233 ASP H H 7.458 0.007 1 835 213 233 ASP C C 180.868 0.056 1 836 213 233 ASP CA C 55.717 0.032 1 837 213 233 ASP CB C 41.638 0.104 1 838 213 233 ASP N N 123.582 0.024 1 stop_ save_