data_16146 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignment of Staphylococcal Enterotoxin H ; _BMRB_accession_number 16146 _BMRB_flat_file_name bmr16146.str _Entry_type original _Submission_date 2009-01-29 _Accession_date 2009-01-29 _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 Saline Maria . . 2 Orekhov Vladislav . . 3 Lindkvist-Petersson Karin . . 4 Karlsson Goran B. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 207 "13C chemical shifts" 396 "15N chemical shifts" 207 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-20 update BMRB 'complete entry citation' 2009-03-02 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone resonance assignment of Staphylococcal Enterotoxin H.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19888679 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saline Maria . . 2 Orekhov Vladislav . . 3 Lindkvist-Petersson Karin . . 4 Karlsson 'B. Goran' . . 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 1 _Page_last 4 _Year 2010 _Details . loop_ _Keyword 'Backbone assignment' Superantigen 'T-cell activation' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name SEH _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SEH $SEH stop_ _System_molecular_weight 25143.2 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Activation of T-cells' stop_ _Database_query_date . _Details 'STAPHYLOCOCCAL ENTEROTOXIN H, a protein in the Superantigen group.' save_ ######################## # Monomeric polymers # ######################## save_SEH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SEH _Molecular_mass 25143.2 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 217 _Mol_residue_sequence ; EDLHDKSELTDLALANAYGQ YNHPFIKENIKSDEISGEKD LIFRNQGDSGNDLRVKFATA DLAQKFKNKNVDIYGASFYY KCEKISENISECLYGGTTLN SEKLAQERVIGANVWVDGIQ KETELIRTNKKNVTLQELDI KIRKILSDKYKIYYKDSEIS KGLIEFDMKTPRDYSFDIYD LKGENDYEIDKIYEDNKTLK SDDISHIDVNLYTKKKV ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 ASP 3 LEU 4 HIS 5 ASP 6 LYS 7 SER 8 GLU 9 LEU 10 THR 11 ASP 12 LEU 13 ALA 14 LEU 15 ALA 16 ASN 17 ALA 18 TYR 19 GLY 20 GLN 21 TYR 22 ASN 23 HIS 24 PRO 25 PHE 26 ILE 27 LYS 28 GLU 29 ASN 30 ILE 31 LYS 32 SER 33 ASP 34 GLU 35 ILE 36 SER 37 GLY 38 GLU 39 LYS 40 ASP 41 LEU 42 ILE 43 PHE 44 ARG 45 ASN 46 GLN 47 GLY 48 ASP 49 SER 50 GLY 51 ASN 52 ASP 53 LEU 54 ARG 55 VAL 56 LYS 57 PHE 58 ALA 59 THR 60 ALA 61 ASP 62 LEU 63 ALA 64 GLN 65 LYS 66 PHE 67 LYS 68 ASN 69 LYS 70 ASN 71 VAL 72 ASP 73 ILE 74 TYR 75 GLY 76 ALA 77 SER 78 PHE 79 TYR 80 TYR 81 LYS 82 CYS 83 GLU 84 LYS 85 ILE 86 SER 87 GLU 88 ASN 89 ILE 90 SER 91 GLU 92 CYS 93 LEU 94 TYR 95 GLY 96 GLY 97 THR 98 THR 99 LEU 100 ASN 101 SER 102 GLU 103 LYS 104 LEU 105 ALA 106 GLN 107 GLU 108 ARG 109 VAL 110 ILE 111 GLY 112 ALA 113 ASN 114 VAL 115 TRP 116 VAL 117 ASP 118 GLY 119 ILE 120 GLN 121 LYS 122 GLU 123 THR 124 GLU 125 LEU 126 ILE 127 ARG 128 THR 129 ASN 130 LYS 131 LYS 132 ASN 133 VAL 134 THR 135 LEU 136 GLN 137 GLU 138 LEU 139 ASP 140 ILE 141 LYS 142 ILE 143 ARG 144 LYS 145 ILE 146 LEU 147 SER 148 ASP 149 LYS 150 TYR 151 LYS 152 ILE 153 TYR 154 TYR 155 LYS 156 ASP 157 SER 158 GLU 159 ILE 160 SER 161 LYS 162 GLY 163 LEU 164 ILE 165 GLU 166 PHE 167 ASP 168 MET 169 LYS 170 THR 171 PRO 172 ARG 173 ASP 174 TYR 175 SER 176 PHE 177 ASP 178 ILE 179 TYR 180 ASP 181 LEU 182 LYS 183 GLY 184 GLU 185 ASN 186 ASP 187 TYR 188 GLU 189 ILE 190 ASP 191 LYS 192 ILE 193 TYR 194 GLU 195 ASP 196 ASN 197 LYS 198 THR 199 LEU 200 LYS 201 SER 202 ASP 203 ASP 204 ILE 205 SER 206 HIS 207 ILE 208 ASP 209 VAL 210 ASN 211 LEU 212 TYR 213 THR 214 LYS 215 LYS 216 LYS 217 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-21 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 1ENF "Crystal Structure Of Staphylococcal Enterotoxin H Determined To 1.69 A Resolution" 97.70 212 100.00 100.00 7.61e-149 PDB 1EWC "Crystal Structure Of Zn2+ Loaded Staphylococcal Enterotoxin H" 98.62 214 99.53 99.53 4.52e-149 PDB 1F77 "Staphylococcal Enterotoxin H Determined To 2.4 A Resolution" 100.00 217 100.00 100.00 6.30e-152 PDB 1HXY "Crystal Structure Of Staphylococcal Enterotoxin H In Complex With Human Mhc Class Ii" 98.16 213 100.00 100.00 1.88e-149 PDB 2XN9 "Crystal Structure Of The Ternary Complex Between Human T Cell Receptor, Staphylococcal Enterotoxin H And Human Major Histocompa" 100.00 217 100.00 100.00 6.30e-152 PDB 2XNA "Crystal Structure Of The Complex Between Human T Cell Receptor And Staphylococcal Enterotoxin" 100.00 217 100.00 100.00 6.30e-152 DBJ BAB85990 "enterotoxin H, partial [Staphylococcus aureus]" 100.00 217 100.00 100.00 6.30e-152 DBJ BAB93916 "enterotoxin H [Staphylococcus aureus subsp. aureus MW2]" 100.00 241 100.00 100.00 3.04e-152 EMBL CAG41819 "enterotoxin H [Staphylococcus aureus subsp. aureus MSSA476]" 100.00 241 100.00 100.00 3.04e-152 EMBL CAI77676 "enterotoxin H [Staphylococcus aureus]" 100.00 241 100.00 100.00 3.04e-152 EMBL CAI77677 "enterotoxin H [Staphylococcus aureus]" 100.00 241 100.00 100.00 3.04e-152 EMBL CDR23430 "enterotoxin H [Staphylococcus argenteus]" 100.00 241 99.08 99.54 3.96e-151 GB AAA19777 "enterotoxin H [Staphylococcus aureus]" 100.00 241 100.00 100.00 3.04e-152 GB AAQ63188 "enterotoxin H precursor [Staphylococcus aureus]" 100.00 241 99.54 100.00 1.45e-151 GB ABI98810 "enterotoxin H [Staphylococcus aureus]" 52.53 121 99.12 99.12 1.07e-73 GB AII96788 "enterotoxin H, partial [Staphylococcus aureus]" 53.46 119 100.00 100.00 2.74e-77 GB EFB46156 "enterotoxin type H [Staphylococcus aureus subsp. aureus C427]" 99.08 240 99.53 100.00 4.06e-150 PRF 2023311A exotoxin 100.00 241 100.00 100.00 3.04e-152 REF WP_000608674 "enterotoxin [Staphylococcus aureus]" 100.00 241 100.00 100.00 3.04e-152 REF WP_000608675 "enterotoxin [Staphylococcus aureus]" 100.00 246 98.62 99.54 2.21e-150 REF WP_000608676 "enterotoxin [Staphylococcus aureus]" 99.08 240 99.53 100.00 4.06e-150 REF WP_047431826 "enterotoxin [Staphylococcus aureus]" 100.00 241 99.08 99.54 3.96e-151 SP P0A0L9 "RecName: Full=Enterotoxin type H; AltName: Full=SEH; Flags: Precursor" 100.00 241 100.00 100.00 3.04e-152 SP P0A0M0 "RecName: Full=Enterotoxin type H; AltName: Full=SEH; Flags: Precursor" 100.00 241 100.00 100.00 3.04e-152 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $SEH 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus UL635 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 $SEH 'recombinant technology' . Escherichia coli UL635 PLR16 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '3 mm shigemi tube; 100 uL' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SEH 0.8 mM '[U-100% 13C; U-100% 15N; 80% 2H]' 'ammonium acetate' 300 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SEH 1.6 mM '[U-100% 13C; U-100% 15N]' TRIS 20 uM 'natural abundance' 'sodium chloride' 150 uM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CCPN _Saveframe_category software _Name CCPN _Version . loop_ _Vendor _Address _Electronic_address CCPN . http://www.ccpn.ac.uk/ stop_ loop_ _Task 'chemical shift assignment' stop_ _Details CCPN save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . http://spin.niddk.nih.gov/NMRPipe/ 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 900 _Details 'with a coldprobe' 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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_1H-15N_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_HNCA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2 save_ save_3D_HNCACB_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_HN(CO)CA_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_2 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' 150 . mM pH 6.8 . pH pressure 1 . atm temperature 313 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 150 . mM pH 7.0 . pH temperature 313 . 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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_ _Software_label $CCPN stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name SEH _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 3 3 LEU H H 8.071 0.005 1 2 3 3 LEU CB C 41.505 0.05 1 3 3 3 LEU N N 121.723 0.033 1 4 4 4 HIS H H 10.641 0.001 1 5 4 4 HIS CA C 56.723 0.001 1 6 4 4 HIS N N 122.350 0.019 1 7 5 5 ASP H H 8.590 0.001 1 8 5 5 ASP CA C 52.356 0.064 1 9 5 5 ASP CB C 45.938 0.05 1 10 5 5 ASP N N 122.198 0.019 1 11 6 6 LYS H H 9.212 0.002 1 12 6 6 LYS CA C 59.691 0.05 1 13 6 6 LYS CB C 31.736 0.05 1 14 6 6 LYS N N 128.956 0.022 1 15 7 7 SER H H 9.181 0.001 1 16 7 7 SER CA C 60.520 0.05 1 17 7 7 SER CB C 62.528 0.05 1 18 7 7 SER N N 112.548 0.042 1 19 8 8 GLU H H 8.128 0.002 1 20 8 8 GLU CA C 56.917 0.05 1 21 8 8 GLU CB C 32.847 0.05 1 22 8 8 GLU N N 120.412 0.014 1 23 9 9 LEU H H 7.625 0.001 1 24 9 9 LEU CA C 53.815 0.05 1 25 9 9 LEU CB C 42.259 0.05 1 26 9 9 LEU N N 118.912 0.008 1 27 10 10 THR H H 8.185 0.002 1 28 10 10 THR CA C 60.483 0.065 1 29 10 10 THR CB C 70.518 0.05 1 30 10 10 THR N N 111.944 0.033 1 31 11 11 ASP H H 8.652 0.001 1 32 11 11 ASP CA C 57.241 0.05 1 33 11 11 ASP CB C 39.140 0.05 1 34 11 11 ASP N N 120.024 0.024 1 35 12 12 LEU H H 8.088 0.002 1 36 12 12 LEU CA C 57.339 0.05 1 37 12 12 LEU CB C 41.095 0.05 1 38 12 12 LEU N N 120.892 0.030 1 39 13 13 ALA H H 7.899 0.001 1 40 13 13 ALA CA C 54.940 0.05 1 41 13 13 ALA CB C 18.357 0.05 1 42 13 13 ALA N N 121.715 0.022 1 43 14 14 LEU H H 7.864 0.001 1 44 14 14 LEU CA C 57.916 0.05 1 45 14 14 LEU CB C 41.199 0.05 1 46 14 14 LEU N N 115.020 0.012 1 47 15 15 ALA H H 8.069 0.002 1 48 15 15 ALA CA C 54.603 0.052 1 49 15 15 ALA CB C 17.455 0.05 1 50 15 15 ALA N N 120.492 0.003 1 51 16 16 ASN H H 8.956 0.001 1 52 16 16 ASN CA C 54.703 0.05 1 53 16 16 ASN CB C 36.003 0.05 1 54 16 16 ASN N N 120.016 0.036 1 55 17 17 ALA H H 8.844 0.009 1 56 17 17 ALA CA C 55.720 0.172 1 57 17 17 ALA CB C 15.511 0.05 1 58 17 17 ALA N N 125.825 0.188 1 59 18 18 TYR H H 8.541 0.001 1 60 18 18 TYR CA C 62.493 0.027 1 61 18 18 TYR CB C 37.289 0.05 1 62 18 18 TYR N N 116.021 0.011 1 63 19 19 GLY H H 8.406 0.002 1 64 19 19 GLY CA C 47.271 0.05 1 65 19 19 GLY N N 105.212 0.03 1 66 20 20 GLN H H 8.349 0.002 1 67 20 20 GLN CA C 57.150 0.05 1 68 20 20 GLN CB C 28.188 0.05 1 69 20 20 GLN N N 119.197 0.03 1 70 21 21 TYR H H 7.606 0.001 1 71 21 21 TYR CA C 61.079 0.05 1 72 21 21 TYR CB C 36.231 0.05 1 73 21 21 TYR N N 112.707 0.003 1 74 22 22 ASN H H 7.207 0.002 1 75 22 22 ASN CA C 54.077 0.05 1 76 22 22 ASN CB C 39.865 0.05 1 77 22 22 ASN N N 110.793 0.031 1 78 23 23 HIS H H 7.274 0.001 1 79 23 23 HIS CA C 53.585 0.05 1 80 23 23 HIS CB C 28.706 0.05 1 81 23 23 HIS N N 115.731 0.010 1 82 24 24 PRO CA C 62.834 0.05 1 83 24 24 PRO CB C 31.446 0.05 1 84 25 25 PHE H H 9.387 0.002 1 85 25 25 PHE CA C 58.055 0.05 1 86 25 25 PHE CB C 38.929 0.05 1 87 25 25 PHE N N 124.644 0.018 1 88 26 26 ILE H H 6.841 0.001 1 89 26 26 ILE CA C 59.223 0.05 1 90 26 26 ILE CB C 40.458 0.05 1 91 26 26 ILE N N 125.021 0.013 1 92 27 27 LYS H H 8.471 0.001 1 93 27 27 LYS CA C 56.003 0.05 1 94 27 27 LYS CB C 35.711 0.05 1 95 27 27 LYS N N 127.076 0.012 1 96 28 28 GLU H H 8.304 0.001 1 97 28 28 GLU CA C 54.849 0.05 1 98 28 28 GLU CB C 31.752 0.05 1 99 28 28 GLU N N 122.501 0.004 1 100 29 29 ASN H H 9.058 0.001 1 101 29 29 ASN CA C 53.327 0.05 1 102 29 29 ASN CB C 36.468 0.05 1 103 29 29 ASN N N 121.774 0.021 1 104 30 30 ILE H H 8.839 0.001 1 105 30 30 ILE CA C 60.167 0.05 1 106 30 30 ILE CB C 40.949 0.001 1 107 30 30 ILE N N 114.296 0.015 1 108 31 31 LYS H H 8.338 0.002 1 109 31 31 LYS CA C 56.061 0.031 1 110 31 31 LYS CB C 35.215 0.05 1 111 31 31 LYS N N 118.732 0.136 1 112 32 32 SER H H 9.844 0.001 1 113 32 32 SER CA C 56.063 0.05 1 114 32 32 SER CB C 63.360 0.05 1 115 32 32 SER N N 122.726 0.021 1 116 33 33 ASP H H 8.653 0.002 1 117 33 33 ASP CA C 52.540 0.05 1 118 33 33 ASP N N 127.289 0.004 1 119 34 34 GLU H H 8.614 0.002 1 120 34 34 GLU CA C 55.710 0.05 1 121 34 34 GLU CB C 31.730 0.05 1 122 34 34 GLU N N 123.273 0.015 1 123 35 35 ILE H H 8.147 0.002 1 124 35 35 ILE CA C 58.656 0.05 1 125 35 35 ILE CB C 38.599 0.05 1 126 35 35 ILE N N 125.712 0.016 1 127 36 36 SER H H 9.094 0.001 1 128 36 36 SER CA C 55.754 0.05 1 129 36 36 SER CB C 63.844 0.05 1 130 36 36 SER N N 122.345 0.015 1 131 37 37 GLY H H 8.819 0.002 1 132 37 37 GLY CA C 46.754 0.05 1 133 37 37 GLY N N 116.556 0.03 1 134 38 38 GLU H H 8.497 0.001 1 135 38 38 GLU CA C 59.731 0.05 1 136 38 38 GLU CB C 29.936 0.05 1 137 38 38 GLU N N 114.905 0.020 1 138 39 39 LYS H H 7.859 0.001 1 139 39 39 LYS CA C 56.264 0.05 1 140 39 39 LYS CB C 33.446 0.05 1 141 39 39 LYS N N 115.393 0.009 1 142 40 40 ASP H H 7.471 0.001 1 143 40 40 ASP CA C 51.795 0.05 1 144 40 40 ASP CB C 40.739 0.05 1 145 40 40 ASP N N 116.777 0.020 1 146 41 41 LEU H H 9.662 0.002 1 147 41 41 LEU CA C 53.577 0.05 1 148 41 41 LEU CB C 45.390 0.05 1 149 41 41 LEU N N 124.132 0.012 1 150 42 42 ILE H H 8.183 0.001 1 151 42 42 ILE CA C 57.121 0.05 1 152 42 42 ILE CB C 36.673 0.05 1 153 42 42 ILE N N 119.925 0.007 1 154 43 43 PHE H H 9.955 0.001 1 155 43 43 PHE CA C 54.809 0.05 1 156 43 43 PHE CB C 37.869 0.05 1 157 43 43 PHE N N 130.460 0.014 1 158 44 44 ARG H H 8.832 0.006 1 159 44 44 ARG CA C 58.115 0.05 1 160 44 44 ARG CB C 28.274 0.05 1 161 44 44 ARG N N 125.976 0.018 1 162 45 45 ASN H H 9.653 0.001 1 163 45 45 ASN CA C 55.149 0.05 1 164 45 45 ASN CB C 37.746 0.05 1 165 45 45 ASN N N 114.852 0.021 1 166 46 46 GLN H H 6.954 0.001 1 167 46 46 GLN CA C 55.659 0.05 1 168 46 46 GLN CB C 29.094 0.05 1 169 46 46 GLN N N 114.651 0.015 1 170 47 47 GLY H H 8.869 0.013 1 171 47 47 GLY CA C 43.375 0.05 1 172 47 47 GLY N N 106.510 0.03 1 173 48 48 ASP H H 8.904 0.002 1 174 48 48 ASP CA C 56.203 0.05 1 175 48 48 ASP CB C 41.143 0.05 1 176 48 48 ASP N N 120.774 0.013 1 177 49 49 SER H H 8.884 0.002 1 178 49 49 SER CA C 58.555 0.040 1 179 49 49 SER CB C 61.795 0.05 1 180 49 49 SER N N 113.515 0.017 1 181 50 50 GLY H H 7.717 0.001 1 182 50 50 GLY CA C 44.665 0.05 1 183 50 50 GLY N N 105.263 0.017 1 184 51 51 ASN H H 7.549 0.001 1 185 51 51 ASN CA C 52.854 0.059 1 186 51 51 ASN CB C 38.201 0.05 1 187 51 51 ASN N N 118.556 0.011 1 188 52 52 ASP H H 8.498 0.001 1 189 52 52 ASP CA C 54.990 0.05 1 190 52 52 ASP CB C 41.423 0.05 1 191 52 52 ASP N N 119.313 0.011 1 192 53 53 LEU H H 7.695 0.001 1 193 53 53 LEU CA C 52.985 0.05 1 194 53 53 LEU CB C 44.586 0.05 1 195 53 53 LEU N N 122.632 0.016 1 196 54 54 ARG H H 9.118 0.003 1 197 54 54 ARG CA C 54.417 0.05 1 198 54 54 ARG CB C 31.314 0.05 1 199 54 54 ARG N N 130.726 0.019 1 200 55 55 VAL H H 8.992 0.001 1 201 55 55 VAL CA C 61.398 0.05 1 202 55 55 VAL CB C 31.772 0.05 1 203 55 55 VAL N N 128.080 0.019 1 204 56 56 LYS H H 8.845 0.001 1 205 56 56 LYS CA C 55.892 0.05 1 206 56 56 LYS CB C 32.821 0.05 1 207 56 56 LYS N N 125.495 0.011 1 208 57 57 PHE H H 8.068 0.001 1 209 57 57 PHE CA C 56.370 0.05 1 210 57 57 PHE CB C 42.712 0.05 1 211 57 57 PHE N N 116.801 0.014 1 212 58 58 ALA H H 7.999 0.001 1 213 58 58 ALA CA C 54.443 0.05 1 214 58 58 ALA CB C 19.903 0.05 1 215 58 58 ALA N N 118.082 0.009 1 216 59 59 THR H H 7.192 0.001 1 217 59 59 THR CA C 58.065 0.05 1 218 59 59 THR CB C 72.452 0.05 1 219 59 59 THR N N 100.262 0.011 1 220 60 60 ALA H H 9.017 0.002 1 221 60 60 ALA CA C 54.128 0.05 1 222 60 60 ALA CB C 18.440 0.05 1 223 60 60 ALA N N 124.002 0.014 1 224 61 61 ASP H H 8.139 0.002 1 225 61 61 ASP CA C 56.490 0.05 1 226 61 61 ASP CB C 39.867 0.05 1 227 61 61 ASP N N 114.326 0.025 1 228 62 62 LEU H H 7.352 0.001 1 229 62 62 LEU CA C 57.248 0.05 1 230 62 62 LEU CB C 41.552 0.05 1 231 62 62 LEU N N 120.244 0.019 1 232 63 63 ALA H H 6.620 0.001 1 233 63 63 ALA CA C 55.011 0.05 1 234 63 63 ALA CB C 16.652 0.05 1 235 63 63 ALA N N 118.346 0.011 1 236 64 64 GLN H H 8.090 0.002 1 237 64 64 GLN CA C 57.992 0.05 1 238 64 64 GLN CB C 27.294 0.05 1 239 64 64 GLN N N 111.723 0.013 1 240 65 65 LYS H H 7.391 0.001 1 241 65 65 LYS CA C 58.179 0.05 1 242 65 65 LYS CB C 30.750 0.05 1 243 65 65 LYS N N 118.948 0.003 1 244 66 66 PHE H H 6.792 0.001 1 245 66 66 PHE CA C 57.924 0.05 1 246 66 66 PHE CB C 39.388 0.05 1 247 66 66 PHE N N 113.045 0.009 1 248 67 67 LYS H H 7.300 0.002 1 249 67 67 LYS CA C 57.843 0.05 1 250 67 67 LYS CB C 31.989 0.05 1 251 67 67 LYS N N 123.501 0.006 1 252 68 68 ASN H H 9.753 0.002 1 253 68 68 ASN CA C 54.388 0.05 1 254 68 68 ASN CB C 37.914 0.05 1 255 68 68 ASN N N 121.885 0.040 1 256 69 69 LYS H H 7.631 0.001 1 257 69 69 LYS CA C 53.262 0.05 1 258 69 69 LYS CB C 33.538 0.05 1 259 69 69 LYS N N 115.752 0.017 1 260 70 70 ASN H H 8.794 0.001 1 261 70 70 ASN CA C 59.289 0.05 1 262 70 70 ASN CB C 37.190 0.05 1 263 70 70 ASN N N 119.890 0.010 1 264 71 71 VAL H H 10.158 0.001 1 265 71 71 VAL CA C 59.495 0.05 1 266 71 71 VAL CB C 35.197 0.05 1 267 71 71 VAL N N 123.000 0.027 1 268 72 72 ASP H H 8.996 0.001 1 269 72 72 ASP CA C 52.306 0.05 1 270 72 72 ASP CB C 42.330 0.05 1 271 72 72 ASP N N 118.449 0.016 1 272 73 73 ILE H H 8.864 0.002 1 273 73 73 ILE CA C 58.036 0.05 1 274 73 73 ILE CB C 39.534 0.05 1 275 73 73 ILE N N 119.590 0.014 1 276 74 74 TYR H H 9.054 0.002 1 277 74 74 TYR CA C 56.347 0.05 1 278 74 74 TYR CB C 40.446 0.05 1 279 74 74 TYR N N 133.084 0.012 1 280 75 75 GLY H H 8.495 0.001 1 281 75 75 GLY CA C 45.475 0.05 1 282 75 75 GLY N N 107.924 0.003 1 283 76 76 ALA H H 8.147 0.001 1 284 76 76 ALA CA C 51.406 0.05 1 285 76 76 ALA CB C 17.711 0.05 1 286 76 76 ALA N N 125.226 0.012 1 287 77 77 SER H H 8.241 0.002 1 288 77 77 SER CA C 55.123 0.05 1 289 77 77 SER CB C 66.849 0.05 1 290 77 77 SER N N 115.495 0.029 1 291 78 78 PHE H H 8.742 0.001 1 292 78 78 PHE CA C 55.404 0.05 1 293 78 78 PHE CB C 42.740 0.05 1 294 78 78 PHE N N 116.206 0.014 1 295 79 79 TYR H H 8.864 0.002 1 296 79 79 TYR CA C 58.988 0.041 1 297 79 79 TYR CB C 41.239 0.05 1 298 79 79 TYR N N 116.501 0.009 1 299 80 80 TYR H H 8.974 0.002 1 300 80 80 TYR CA C 59.173 0.05 1 301 80 80 TYR CB C 36.458 0.05 1 302 80 80 TYR N N 124.927 0.008 1 303 81 81 LYS H H 8.475 0.001 1 304 81 81 LYS CA C 57.495 0.05 1 305 81 81 LYS CB C 27.437 0.05 1 306 81 81 LYS N N 118.992 0.007 1 307 82 82 CYS H H 7.698 0.001 1 308 82 82 CYS CA C 54.037 0.05 1 309 82 82 CYS CB C 36.437 0.05 1 310 82 82 CYS N N 117.844 0.013 1 311 83 83 GLU H H 8.816 0.001 1 312 83 83 GLU CA C 58.056 0.05 1 313 83 83 GLU CB C 27.880 0.05 1 314 83 83 GLU N N 131.334 0.020 1 315 84 84 LYS H H 8.475 0.002 1 316 84 84 LYS CA C 57.222 0.05 1 317 84 84 LYS CB C 32.720 0.05 1 318 84 84 LYS N N 125.645 0.008 1 319 85 85 ILE H H 8.731 0.001 1 320 85 85 ILE CA C 60.017 0.05 1 321 85 85 ILE CB C 39.947 0.05 1 322 85 85 ILE N N 120.850 0.015 1 323 86 86 SER H H 8.738 0.001 1 324 86 86 SER CA C 57.053 0.05 1 325 86 86 SER CB C 64.474 0.05 1 326 86 86 SER N N 122.091 0.045 1 327 87 87 GLU H H 8.590 0.001 1 328 87 87 GLU CA C 57.442 0.05 1 329 87 87 GLU CB C 28.507 0.05 1 330 87 87 GLU N N 117.980 0.004 1 331 88 88 ASN H H 8.348 0.001 1 332 88 88 ASN CA C 52.108 0.05 1 333 88 88 ASN CB C 38.486 0.05 1 334 88 88 ASN N N 118.831 0.141 1 335 89 89 ILE H H 7.951 0.001 1 336 89 89 ILE CA C 62.485 0.05 1 337 89 89 ILE CB C 37.590 0.05 1 338 89 89 ILE N N 123.001 0.017 1 339 90 90 SER H H 7.853 0.002 1 340 90 90 SER CA C 56.294 0.05 1 341 90 90 SER CB C 65.517 0.05 1 342 90 90 SER N N 118.427 0.025 1 343 91 91 GLU H H 8.696 0.016 1 344 91 91 GLU CA C 53.571 0.05 1 345 91 91 GLU CB C 31.432 0.05 1 346 91 91 GLU N N 125.041 0.011 1 347 92 92 CYS H H 8.258 0.006 1 348 92 92 CYS CA C 57.028 0.014 1 349 92 92 CYS CB C 37.410 0.05 1 350 92 92 CYS N N 123.558 0.043 1 351 93 93 LEU H H 7.838 0.002 1 352 93 93 LEU CA C 55.167 0.05 1 353 93 93 LEU CB C 45.376 0.05 1 354 93 93 LEU N N 116.348 0.017 1 355 94 94 TYR H H 9.896 0.002 1 356 94 94 TYR CA C 55.816 0.05 1 357 94 94 TYR CB C 39.229 0.05 1 358 94 94 TYR N N 120.740 0.011 1 359 95 95 GLY H H 7.995 0.001 1 360 95 95 GLY CA C 47.379 0.019 1 361 95 95 GLY N N 108.384 0.008 1 362 96 96 GLY H H 8.634 0.001 1 363 96 96 GLY CA C 47.374 0.05 1 364 96 96 GLY N N 110.483 0.016 1 365 97 97 THR H H 8.986 0.001 1 366 97 97 THR CA C 64.280 0.05 1 367 97 97 THR CB C 69.624 0.054 1 368 97 97 THR N N 119.613 0.002 1 369 98 98 THR H H 8.782 0.001 1 370 98 98 THR CA C 59.207 0.05 1 371 98 98 THR CB C 71.158 0.012 1 372 98 98 THR N N 115.854 0.029 1 373 99 99 LEU H H 9.087 0.001 1 374 99 99 LEU CA C 55.300 0.05 1 375 99 99 LEU CB C 40.454 0.05 1 376 99 99 LEU N N 118.683 0.008 1 377 100 100 ASN H H 9.082 0.001 1 378 100 100 ASN CA C 56.394 0.05 1 379 100 100 ASN CB C 40.309 0.05 1 380 100 100 ASN N N 125.814 0.004 1 381 102 102 GLU H H 7.216 0.002 1 382 102 102 GLU CA C 55.577 0.05 1 383 102 102 GLU CB C 27.864 0.05 1 384 102 102 GLU N N 122.043 0.014 1 385 103 103 LYS H H 7.694 0.001 1 386 103 103 LYS CA C 53.912 0.05 1 387 103 103 LYS CB C 34.370 0.05 1 388 103 103 LYS N N 123.531 0.012 1 389 104 104 LEU H H 8.521 0.001 1 390 104 104 LEU CA C 53.341 0.05 1 391 104 104 LEU CB C 43.619 0.05 1 392 104 104 LEU N N 121.934 0.010 1 393 106 106 GLN H H 7.368 0.002 1 394 106 106 GLN CA C 52.663 0.05 1 395 106 106 GLN CB C 30.492 0.05 1 396 106 106 GLN N N 113.466 0.013 1 397 107 107 GLU H H 8.445 0.002 1 398 107 107 GLU CA C 57.181 0.025 1 399 107 107 GLU CB C 29.548 0.05 1 400 107 107 GLU N N 121.061 0.03 1 401 108 108 ARG H H 8.616 0.001 1 402 108 108 ARG CA C 54.004 0.05 1 403 108 108 ARG CB C 29.617 0.05 1 404 108 108 ARG N N 124.233 0.018 1 405 109 109 VAL H H 8.467 0.004 1 406 109 109 VAL CA C 61.148 0.05 1 407 109 109 VAL CB C 31.649 0.05 1 408 109 109 VAL N N 125.580 0.03 1 409 110 110 ILE H H 9.514 0.002 1 410 110 110 ILE CA C 60.014 0.05 1 411 110 110 ILE CB C 39.804 0.05 1 412 110 110 ILE N N 130.378 0.006 1 413 111 111 GLY H H 9.040 0.002 1 414 111 111 GLY CA C 44.721 0.05 1 415 111 111 GLY N N 114.224 0.011 1 416 112 112 ALA H H 9.179 0.010 1 417 112 112 ALA CA C 48.615 0.05 1 418 112 112 ALA N N 126.701 0.006 1 419 113 113 ASN H H 9.145 0.013 1 420 113 113 ASN CA C 52.032 0.05 1 421 113 113 ASN CB C 39.914 0.05 1 422 113 113 ASN N N 123.242 0.154 1 423 114 114 VAL H H 7.900 0.002 1 424 114 114 VAL CA C 61.043 0.05 1 425 114 114 VAL CB C 34.083 0.05 1 426 114 114 VAL N N 122.150 0.033 1 427 115 115 TRP H H 8.926 0.001 1 428 115 115 TRP CA C 56.755 0.05 1 429 115 115 TRP CB C 33.113 0.05 1 430 115 115 TRP N N 126.826 0.003 1 431 116 116 VAL H H 8.518 0.001 1 432 116 116 VAL CA C 60.507 0.05 1 433 116 116 VAL CB C 32.449 0.05 1 434 116 116 VAL N N 118.407 0.008 1 435 117 117 ASP H H 9.376 0.002 1 436 117 117 ASP CA C 55.805 0.05 1 437 117 117 ASP CB C 38.757 0.05 1 438 117 117 ASP N N 127.756 0.035 1 439 118 118 GLY H H 9.223 0.001 1 440 118 118 GLY CA C 45.190 0.05 1 441 118 118 GLY N N 102.720 0.016 1 442 119 119 ILE H H 8.098 0.001 1 443 119 119 ILE CA C 59.197 0.05 1 444 119 119 ILE CB C 36.663 0.05 1 445 119 119 ILE N N 123.589 0.022 1 446 120 120 GLN H H 8.833 0.001 1 447 120 120 GLN CA C 57.732 0.05 1 448 120 120 GLN CB C 27.345 0.05 1 449 120 120 GLN N N 129.685 0.009 1 450 121 121 LYS H H 8.913 0.002 1 451 121 121 LYS CA C 51.813 0.05 1 452 121 121 LYS CB C 31.537 0.05 1 453 121 121 LYS N N 127.067 0.018 1 454 122 122 GLU H H 8.369 0.001 1 455 122 122 GLU CA C 57.301 0.05 1 456 122 122 GLU CB C 28.864 0.05 1 457 122 122 GLU N N 121.093 0.009 1 458 123 123 THR H H 8.123 0.001 1 459 123 123 THR CA C 62.881 0.05 1 460 123 123 THR CB C 69.472 0.05 1 461 123 123 THR N N 118.643 0.011 1 462 124 124 GLU H H 8.895 0.001 1 463 124 124 GLU CA C 56.310 0.05 1 464 124 124 GLU CB C 29.788 0.05 1 465 124 124 GLU N N 126.812 0.031 1 466 125 125 LEU H H 8.601 0.001 1 467 125 125 LEU CA C 53.138 0.05 1 468 125 125 LEU CB C 42.808 0.05 1 469 125 125 LEU N N 119.668 0.021 1 470 126 126 ILE H H 8.850 0.002 1 471 126 126 ILE CA C 58.664 0.05 1 472 126 126 ILE CB C 39.245 0.05 1 473 126 126 ILE N N 119.227 0.009 1 474 127 127 ARG H H 8.375 0.001 1 475 127 127 ARG CA C 53.912 0.05 1 476 127 127 ARG CB C 33.445 0.05 1 477 127 127 ARG N N 120.448 0.008 1 478 128 128 THR H H 8.370 0.001 1 479 128 128 THR CA C 60.990 0.016 1 480 128 128 THR CB C 68.843 0.05 1 481 128 128 THR N N 112.074 0.004 1 482 129 129 ASN H H 8.064 0.001 1 483 129 129 ASN CA C 51.818 0.05 1 484 129 129 ASN CB C 37.223 0.05 1 485 129 129 ASN N N 124.136 0.017 1 486 130 130 LYS H H 8.255 0.002 1 487 130 130 LYS CA C 56.674 0.05 1 488 130 130 LYS CB C 33.613 0.05 1 489 130 130 LYS N N 122.620 0.003 1 490 131 131 LYS H H 8.088 0.001 1 491 131 131 LYS CA C 59.201 0.05 1 492 131 131 LYS CB C 32.847 0.05 1 493 131 131 LYS N N 122.537 0.012 1 494 132 132 ASN H H 7.764 0.001 1 495 132 132 ASN CA C 51.749 0.05 1 496 132 132 ASN CB C 40.162 0.05 1 497 132 132 ASN N N 115.629 0.014 1 498 133 133 VAL H H 9.210 0.001 1 499 133 133 VAL CA C 58.097 0.045 1 500 133 133 VAL CB C 34.612 0.05 1 501 133 133 VAL N N 122.196 0.008 1 502 134 134 THR H H 8.953 0.003 1 503 134 134 THR CA C 62.604 0.05 1 504 134 134 THR CB C 69.736 0.05 1 505 134 134 THR N N 118.411 0.034 1 506 135 135 LEU H H 7.884 0.010 1 507 135 135 LEU CA C 57.212 0.013 1 508 135 135 LEU CB C 41.105 0.05 1 509 135 135 LEU N N 121.779 0.085 1 510 136 136 GLN H H 8.128 0.002 1 511 136 136 GLN CA C 58.797 0.032 1 512 136 136 GLN CB C 28.449 0.05 1 513 136 136 GLN N N 115.498 0.017 1 514 137 137 GLU H H 7.935 0.004 1 515 137 137 GLU CA C 58.623 0.059 1 516 137 137 GLU CB C 27.343 0.05 1 517 137 137 GLU N N 118.569 0.069 1 518 138 138 LEU H H 6.921 0.001 1 519 138 138 LEU CA C 57.235 0.05 1 520 138 138 LEU CB C 41.222 0.05 1 521 138 138 LEU N N 113.587 0.010 1 522 139 139 ASP H H 8.786 0.001 1 523 139 139 ASP CA C 56.394 0.05 1 524 139 139 ASP CB C 41.216 0.05 1 525 139 139 ASP N N 117.868 0.017 1 526 140 140 ILE H H 8.886 0.001 1 527 140 140 ILE CA C 66.050 0.05 1 528 140 140 ILE CB C 37.120 0.05 1 529 140 140 ILE N N 117.477 0.005 1 530 141 141 LYS H H 7.945 0.002 1 531 141 141 LYS CA C 60.549 0.05 1 532 141 141 LYS CB C 32.266 0.05 1 533 141 141 LYS N N 115.738 0.016 1 534 142 142 ILE H H 8.352 0.002 1 535 142 142 ILE CA C 60.589 0.05 1 536 142 142 ILE CB C 37.032 0.05 1 537 142 142 ILE N N 116.447 0.009 1 538 143 143 ARG H H 9.433 0.002 1 539 143 143 ARG CA C 61.598 0.05 1 540 143 143 ARG CB C 29.307 0.05 1 541 143 143 ARG N N 122.644 0.029 1 542 144 144 LYS H H 9.166 0.002 1 543 144 144 LYS CA C 59.514 0.05 1 544 144 144 LYS CB C 30.814 0.05 1 545 144 144 LYS N N 121.703 0.007 1 546 145 145 ILE H H 6.962 0.001 1 547 145 145 ILE CA C 64.652 0.05 1 548 145 145 ILE CB C 37.570 0.05 1 549 145 145 ILE N N 119.164 0.007 1 550 146 146 LEU H H 8.547 0.002 1 551 146 146 LEU CA C 57.203 0.05 1 552 146 146 LEU CB C 40.551 0.05 1 553 146 146 LEU N N 116.374 0.014 1 554 147 147 SER H H 9.096 0.002 1 555 147 147 SER CA C 61.621 0.038 1 556 147 147 SER CB C 62.538 0.05 1 557 147 147 SER N N 116.957 0.019 1 558 148 148 ASP H H 8.476 0.001 1 559 148 148 ASP CA C 57.174 0.05 1 560 148 148 ASP CB C 40.129 0.05 1 561 148 148 ASP N N 120.849 0.016 1 562 149 149 LYS H H 8.421 0.001 1 563 149 149 LYS CA C 58.530 0.05 1 564 149 149 LYS CB C 32.813 0.05 1 565 149 149 LYS N N 115.707 0.014 1 566 150 150 TYR H H 7.913 0.002 1 567 150 150 TYR CA C 57.537 0.05 1 568 150 150 TYR CB C 38.723 0.05 1 569 150 150 TYR N N 113.926 0.024 1 570 151 151 LYS H H 7.610 0.001 1 571 151 151 LYS CA C 56.572 0.05 1 572 151 151 LYS CB C 27.786 0.05 1 573 151 151 LYS N N 115.048 0.013 1 574 152 152 ILE H H 6.499 0.001 1 575 152 152 ILE CA C 65.364 0.05 1 576 152 152 ILE CB C 36.512 0.05 1 577 152 152 ILE N N 106.995 0.003 1 578 153 153 TYR H H 8.812 0.001 1 579 153 153 TYR CA C 56.438 0.05 1 580 153 153 TYR CB C 36.851 0.05 1 581 153 153 TYR N N 118.268 0.016 1 582 154 154 TYR H H 7.267 0.001 1 583 154 154 TYR CA C 54.600 0.05 1 584 154 154 TYR CB C 38.380 0.05 1 585 154 154 TYR N N 116.229 0.012 1 586 155 155 LYS H H 9.394 0.001 1 587 155 155 LYS CA C 59.961 0.05 1 588 155 155 LYS CB C 31.845 0.05 1 589 155 155 LYS N N 128.778 0.018 1 590 156 156 ASP H H 7.353 0.002 1 591 156 156 ASP CA C 53.713 0.05 1 592 156 156 ASP CB C 39.886 0.05 1 593 156 156 ASP N N 112.197 0.021 1 594 157 157 SER H H 7.248 0.001 1 595 157 157 SER CA C 57.314 0.05 1 596 157 157 SER CB C 65.308 0.05 1 597 157 157 SER N N 114.388 0.014 1 598 158 158 GLU H H 9.367 0.009 1 599 158 158 GLU CA C 57.487 0.05 1 600 158 158 GLU CB C 29.326 0.05 1 601 158 158 GLU N N 119.868 0.021 1 602 159 159 ILE H H 7.082 0.001 1 603 159 159 ILE CA C 60.065 0.05 1 604 159 159 ILE CB C 34.918 0.05 1 605 159 159 ILE N N 116.683 0.021 1 606 160 160 SER H H 9.435 0.002 1 607 160 160 SER CA C 58.824 0.05 1 608 160 160 SER CB C 66.652 0.05 1 609 160 160 SER N N 121.060 0.010 1 610 161 161 LYS H H 8.183 0.001 1 611 161 161 LYS CA C 55.052 0.05 1 612 161 161 LYS CB C 39.101 0.05 1 613 161 161 LYS N N 117.856 0.026 1 614 162 162 GLY H H 10.877 0.001 1 615 162 162 GLY CA C 47.349 0.05 1 616 162 162 GLY N N 109.175 0.017 1 617 163 163 LEU H H 9.005 0.002 1 618 163 163 LEU CA C 53.433 0.05 1 619 163 163 LEU CB C 46.336 0.05 1 620 163 163 LEU N N 124.767 0.015 1 621 164 164 ILE H H 9.118 0.002 1 622 164 164 ILE CA C 60.373 0.05 1 623 164 164 ILE N N 125.882 0.03 1 624 165 165 GLU H H 9.386 0.002 1 625 165 165 GLU CA C 54.895 0.05 1 626 165 165 GLU N N 125.573 0.158 1 627 166 166 PHE H H 9.119 0.006 1 628 166 166 PHE CA C 56.844 0.05 1 629 166 166 PHE N N 123.232 0.129 1 630 170 170 THR H H 7.382 0.002 1 631 170 170 THR CA C 58.905 0.05 1 632 170 170 THR CB C 67.999 0.05 1 633 170 170 THR N N 109.447 0.03 1 634 171 171 PRO CA C 64.942 0.05 1 635 172 172 ARG H H 7.970 0.002 1 636 172 172 ARG CA C 55.605 0.05 1 637 172 172 ARG CB C 31.374 0.05 1 638 172 172 ARG N N 121.361 0.230 1 639 173 173 ASP H H 7.933 0.004 1 640 173 173 ASP CA C 53.235 0.05 1 641 173 173 ASP CB C 42.215 0.05 1 642 173 173 ASP N N 122.919 0.001 1 643 174 174 TYR H H 7.937 0.002 1 644 174 174 TYR CA C 56.493 0.05 1 645 174 174 TYR CB C 41.310 0.05 1 646 174 174 TYR N N 116.876 0.067 1 647 175 175 SER H H 8.222 0.003 1 648 175 175 SER CA C 56.815 0.05 1 649 175 175 SER CB C 65.796 0.05 1 650 175 175 SER N N 115.969 0.032 1 651 176 176 PHE H H 9.295 0.002 1 652 176 176 PHE CA C 57.522 0.05 1 653 176 176 PHE CB C 43.038 0.05 1 654 176 176 PHE N N 117.571 0.023 1 655 177 177 ASP H H 8.718 0.001 1 656 177 177 ASP CA C 52.590 0.056 1 657 177 177 ASP CB C 41.526 0.05 1 658 177 177 ASP N N 123.825 0.014 1 659 178 178 ILE H H 7.921 0.002 1 660 178 178 ILE CA C 64.001 0.05 1 661 178 178 ILE CB C 36.078 0.05 1 662 178 178 ILE N N 120.763 0.018 1 663 179 179 TYR H H 8.605 0.001 1 664 179 179 TYR CA C 56.783 0.05 1 665 179 179 TYR CB C 35.986 0.05 1 666 179 179 TYR N N 116.560 0.013 1 667 180 180 ASP H H 7.367 0.002 1 668 180 180 ASP CA C 51.394 0.004 1 669 180 180 ASP CB C 39.038 0.05 1 670 180 180 ASP N N 122.861 0.008 1 671 181 181 LEU H H 7.145 0.002 1 672 181 181 LEU CA C 54.145 0.002 1 673 181 181 LEU CB C 41.250 0.05 1 674 181 181 LEU N N 120.517 0.012 1 675 182 182 LYS H H 8.545 0.002 1 676 182 182 LYS N N 118.285 0.03 1 677 183 183 GLY H H 7.168 0.001 1 678 183 183 GLY CA C 44.015 0.05 1 679 183 183 GLY N N 103.897 0.03 1 680 184 184 GLU H H 8.084 0.001 1 681 184 184 GLU CA C 55.964 0.05 1 682 184 184 GLU CB C 31.733 0.05 1 683 184 184 GLU N N 113.951 0.013 1 684 185 185 ASN H H 8.062 0.001 1 685 185 185 ASN CA C 52.636 0.05 1 686 185 185 ASN CB C 41.261 0.05 1 687 185 185 ASN N N 113.479 0.017 1 688 186 186 ASP H H 8.856 0.001 1 689 186 186 ASP CA C 58.085 0.05 1 690 186 186 ASP CB C 39.689 0.05 1 691 186 186 ASP N N 124.927 0.009 1 692 187 187 TYR H H 8.684 0.002 1 693 187 187 TYR CA C 58.424 0.05 1 694 187 187 TYR CB C 36.824 0.05 1 695 187 187 TYR N N 113.477 0.008 1 696 188 188 GLU H H 6.687 0.002 1 697 188 188 GLU CA C 57.100 0.05 1 698 188 188 GLU CB C 30.321 0.05 1 699 188 188 GLU N N 118.805 0.011 1 700 189 189 ILE H H 7.745 0.002 1 701 189 189 ILE CA C 64.324 0.05 1 702 189 189 ILE CB C 38.399 0.05 1 703 189 189 ILE N N 119.827 0.010 1 704 190 190 ASP H H 7.631 0.002 1 705 190 190 ASP CA C 53.707 0.05 1 706 190 190 ASP CB C 36.896 0.05 1 707 190 190 ASP N N 112.740 0.006 1 708 191 191 LYS H H 6.741 0.001 1 709 191 191 LYS CA C 57.698 0.05 1 710 191 191 LYS CB C 31.557 0.05 1 711 191 191 LYS N N 119.932 0.012 1 712 192 192 ILE H H 6.409 0.002 1 713 192 192 ILE CA C 62.793 0.030 1 714 192 192 ILE CB C 36.931 0.05 1 715 192 192 ILE N N 110.341 0.03 1 716 193 193 TYR H H 7.570 0.001 1 717 193 193 TYR CA C 56.298 0.05 1 718 193 193 TYR CB C 37.940 0.05 1 719 193 193 TYR N N 120.314 0.012 1 720 194 194 GLU H H 7.846 0.002 1 721 194 194 GLU CA C 58.881 0.05 1 722 194 194 GLU CB C 28.535 0.05 1 723 194 194 GLU N N 120.190 0.003 1 724 195 195 ASP H H 7.937 0.010 1 725 195 195 ASP CA C 53.918 0.05 1 726 195 195 ASP CB C 39.239 0.05 1 727 195 195 ASP N N 118.457 0.012 1 728 196 196 ASN H H 8.666 0.002 1 729 196 196 ASN CA C 54.364 0.05 1 730 196 196 ASN CB C 42.428 0.05 1 731 196 196 ASN N N 119.772 0.016 1 732 197 197 LYS H H 7.823 0.002 1 733 197 197 LYS CA C 58.358 0.034 1 734 197 197 LYS CB C 30.857 0.05 1 735 197 197 LYS N N 118.186 0.026 1 736 198 198 THR CA C 61.384 0.05 1 737 199 199 LEU H H 9.200 0.007 1 738 199 199 LEU CA C 52.566 0.05 1 739 199 199 LEU CB C 43.681 0.05 1 740 199 199 LEU N N 124.583 0.115 1 741 200 200 LYS H H 8.547 0.001 1 742 200 200 LYS CA C 55.805 0.05 1 743 200 200 LYS CB C 30.990 0.05 1 744 200 200 LYS N N 122.882 0.013 1 745 201 201 SER H H 8.711 0.005 1 746 201 201 SER CA C 61.879 0.05 1 747 201 201 SER CB C 65.585 0.05 1 748 201 201 SER N N 124.977 0.043 1 749 202 202 ASP H H 8.7922 0.002 1 750 202 202 ASP CA C 55.609 0.05 1 751 202 202 ASP CB C 40.516 0.05 1 752 202 202 ASP N N 118.371 0.083 1 753 203 203 ASP H H 7.912 0.002 1 754 203 203 ASP CA C 54.411 0.05 1 755 203 203 ASP CB C 41.239 0.05 1 756 203 203 ASP N N 116.639 0.03 1 757 204 204 ILE H H 7.205 0.007 1 758 204 204 ILE CA C 61.441 0.05 1 759 204 204 ILE CB C 39.350 0.05 1 760 204 204 ILE N N 120.417 0.023 1 761 205 205 SER H H 9.557 0.004 1 762 205 205 SER CA C 59.862 0.05 1 763 205 205 SER CB C 63.681 0.05 1 764 205 205 SER N N 123.653 0.03 1 765 206 206 HIS H H 7.989 0.009 1 766 206 206 HIS CA C 55.913 0.05 1 767 206 206 HIS CB C 30.050 0.05 1 768 206 206 HIS N N 112.964 0.050 1 769 207 207 ILE H H 8.773 0.002 1 770 207 207 ILE CA C 59.223 0.05 1 771 207 207 ILE N N 120.157 0.005 1 772 208 208 ASP H H 9.252 0.005 1 773 208 208 ASP CA C 53.686 0.05 1 774 208 208 ASP N N 127.158 0.024 1 775 209 209 VAL H H 9.763 0.003 1 776 209 209 VAL CA C 60.609 0.05 1 777 209 209 VAL CB C 32.858 0.05 1 778 209 209 VAL N N 124.726 0.014 1 779 210 210 ASN H H 8.973 0.001 1 780 210 210 ASN CA C 52.492 0.05 1 781 210 210 ASN CB C 42.251 0.05 1 782 210 210 ASN N N 126.407 0.013 1 783 211 211 LEU H H 8.726 0.001 1 784 211 211 LEU CA C 52.432 0.05 1 785 211 211 LEU CB C 42.792 0.05 1 786 211 211 LEU N N 120.071 0.017 1 787 212 212 TYR H H 8.946 0.002 1 788 212 212 TYR CA C 56.468 0.05 1 789 212 212 TYR CB C 40.973 0.05 1 790 212 212 TYR N N 118.429 0.019 1 791 213 213 THR H H 10.398 0.001 1 792 213 213 THR CA C 60.636 0.05 1 793 213 213 THR CB C 71.189 0.05 1 794 213 213 THR N N 116.692 0.038 1 795 214 214 LYS H H 8.322 0.002 1 796 214 214 LYS CA C 56.350 0.05 1 797 214 214 LYS CB C 32.29 0.05 1 798 214 214 LYS N N 120.28 0.03 1 799 215 215 LYS H H 8.311 0.002 1 800 215 215 LYS CA C 56.34 0.05 1 801 215 215 LYS CB C 32.10 0.05 1 802 215 215 LYS N N 123.66 0.03 1 803 216 216 LYS H H 8.319 0.002 1 804 216 216 LYS CA C 56.180 0.05 1 805 216 216 LYS CB C 32.870 0.05 1 806 216 216 LYS N N 123.90 0.03 1 807 217 217 VAL H H 7.627 0.002 1 808 217 217 VAL CA C 63.15 0.05 1 809 217 217 VAL CB C 32.87 0.05 1 810 217 217 VAL N N 125.74 0.03 1 stop_ save_