data_25156 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of decorin binding protein A from strain N40 of Borrelia burgdorferi ; _BMRB_accession_number 25156 _BMRB_flat_file_name bmr25156.str _Entry_type original _Submission_date 2014-08-16 _Accession_date 2014-08-16 _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 Wang Xu . . 2 Morgan Ashli . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 517 "13C chemical shifts" 427 "15N chemical shifts" 156 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-09-28 update BMRB 'update entry citation' 2015-03-23 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 25157 'Decorin Binding Protein A' stop_ _Original_release_date 2016-09-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Mechanisms Underlying Sequence-Dependent Variations in GAG Affinities of Decorin Binding Protein A, a Borrelia burgdorferi Adhesin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25695518 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Xu . . 2 Morgan Ashli . . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_volume 467 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 439 _Page_last 451 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Decorin Binding Protein A' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DBPA $DBPA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DBPA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DBPA _Molecular_mass 36566.016 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 166 _Mol_residue_sequence ; GLKGETKIILERSAKDITDE INKIKKDAADNNVNFAAFTD SETGSKVSENSFILEAKVRA TTVAEKFVTAIEGEATKLKK TGSSGEFSAMYNMMLEVSGP LEELGVLRMTKTVTDAAEQH PTTTAEGILEIAKIMKTKLQ RVHTKNYCALEKKKNPNFTD EKCKNN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 29 GLY 2 30 LEU 3 31 LYS 4 32 GLY 5 33 GLU 6 34 THR 7 35 LYS 8 36 ILE 9 37 ILE 10 38 LEU 11 39 GLU 12 40 ARG 13 41 SER 14 42 ALA 15 43 LYS 16 44 ASP 17 45 ILE 18 46 THR 19 47 ASP 20 48 GLU 21 49 ILE 22 50 ASN 23 51 LYS 24 52 ILE 25 53 LYS 26 54 LYS 27 55 ASP 28 56 ALA 29 57 ALA 30 58 ASP 31 59 ASN 32 60 ASN 33 61 VAL 34 62 ASN 35 63 PHE 36 64 ALA 37 65 ALA 38 66 PHE 39 67 THR 40 68 ASP 41 69 SER 42 70 GLU 43 71 THR 44 72 GLY 45 73 SER 46 74 LYS 47 75 VAL 48 76 SER 49 77 GLU 50 78 ASN 51 79 SER 52 80 PHE 53 81 ILE 54 82 LEU 55 83 GLU 56 84 ALA 57 85 LYS 58 86 VAL 59 87 ARG 60 88 ALA 61 89 THR 62 90 THR 63 91 VAL 64 92 ALA 65 93 GLU 66 94 LYS 67 95 PHE 68 96 VAL 69 97 THR 70 98 ALA 71 99 ILE 72 100 GLU 73 101 GLY 74 102 GLU 75 103 ALA 76 104 THR 77 105 LYS 78 106 LEU 79 107 LYS 80 108 LYS 81 109 THR 82 110 GLY 83 111 SER 84 112 SER 85 113 GLY 86 114 GLU 87 115 PHE 88 116 SER 89 117 ALA 90 118 MET 91 119 TYR 92 120 ASN 93 121 MET 94 122 MET 95 123 LEU 96 124 GLU 97 125 VAL 98 126 SER 99 127 GLY 100 128 PRO 101 129 LEU 102 130 GLU 103 131 GLU 104 132 LEU 105 133 GLY 106 134 VAL 107 135 LEU 108 136 ARG 109 137 MET 110 138 THR 111 139 LYS 112 140 THR 113 141 VAL 114 142 THR 115 143 ASP 116 144 ALA 117 145 ALA 118 146 GLU 119 147 GLN 120 148 HIS 121 149 PRO 122 150 THR 123 151 THR 124 152 THR 125 153 ALA 126 154 GLU 127 155 GLY 128 156 ILE 129 157 LEU 130 158 GLU 131 159 ILE 132 160 ALA 133 161 LYS 134 162 ILE 135 163 MET 136 164 LYS 137 165 THR 138 166 LYS 139 167 LEU 140 168 GLN 141 169 ARG 142 170 VAL 143 171 HIS 144 172 THR 145 173 LYS 146 174 ASN 147 175 TYR 148 176 CYS 149 177 ALA 150 178 LEU 151 179 GLU 152 180 LYS 153 181 LYS 154 182 LYS 155 183 ASN 156 184 PRO 157 185 ASN 158 186 PHE 159 187 THR 160 188 ASP 161 189 GLU 162 190 LYS 163 191 CYS 164 192 LYS 165 193 ASN 166 194 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $DBPA 'Lime Disease causing bacterium' 521007 Bacteria . Borrelia burgdorferi N40 dbp 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 $DBPA 'recombinant technology' . Escherichia coli BL21 DE3 pHUE stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DBPA 0.8 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample save_ save_3D_1H-13C_NOESY_aliphatic_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample save_ save_3D_H(CCO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample save_ save_3D_C(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample save_ save_3D_1H-13C_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample save_ save_3D_1H-15N_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.2 . M pH 5.0 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio 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' '3D HNCACB' '3D CBCA(CO)NH' '3D H(CCO)NH' '3D C(CO)NH' stop_ loop_ _Sample_label $sample stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name DBPA _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 29 1 GLY HA2 H 3.48 0.05 2 2 29 1 GLY HA3 H 3.73 0.05 2 3 29 1 GLY CA C 43.2 0.50 1 4 30 2 LEU H H 8.544 0.05 1 5 30 2 LEU HA H 4.36 0.05 1 6 30 2 LEU HG H 0.95 0.05 1 7 30 2 LEU HD1 H 0.87 0.05 2 8 30 2 LEU CA C 54.4 0.50 1 9 30 2 LEU CB C 43.2 0.50 1 10 30 2 LEU CG C 27.6 0.50 1 11 30 2 LEU CD1 C 23.5 0.50 2 12 30 2 LEU N N 118.365 0.50 1 13 31 3 LYS H H 9.499 0.05 1 14 31 3 LYS HA H 4.66 0.05 1 15 31 3 LYS HB3 H 1.79 0.05 2 16 31 3 LYS HG3 H 1.36 0.05 2 17 31 3 LYS CA C 54.5 0.50 1 18 31 3 LYS CB C 35.7 0.50 1 19 31 3 LYS CG C 23.7 0.50 1 20 31 3 LYS N N 119.962 0.50 1 21 32 4 GLY H H 8.548 0.05 1 22 32 4 GLY HA3 H 3.86 0.05 2 23 32 4 GLY CA C 45.9 0.50 1 24 32 4 GLY N N 107.471 0.50 1 25 33 5 GLU H H 9.049 0.05 1 26 33 5 GLU HA H 4.01 0.05 1 27 33 5 GLU HB3 H 2.1 0.05 2 28 33 5 GLU HG3 H 2.36 0.05 2 29 33 5 GLU CA C 58.4 0.50 1 30 33 5 GLU CB C 28.8 0.50 1 31 33 5 GLU CG C 36.2 0.50 1 32 33 5 GLU N N 124.823 0.50 1 33 34 6 THR H H 7.772 0.05 1 34 34 6 THR HA H 4.15 0.05 1 35 34 6 THR HB H 3.92 0.05 1 36 34 6 THR HG2 H 1.27 0.05 1 37 34 6 THR CA C 66.2 0.50 1 38 34 6 THR CB C 68.5 0.50 1 39 34 6 THR CG2 C 23.6 0.50 1 40 34 6 THR N N 116.008 0.50 1 41 35 7 LYS H H 6.838 0.05 1 42 35 7 LYS HA H 3.65 0.05 1 43 35 7 LYS CA C 59.4 0.50 1 44 35 7 LYS CB C 32.3 0.50 1 45 35 7 LYS N N 119.081 0.50 1 46 36 8 ILE H H 7.02 0.05 1 47 36 8 ILE HA H 3.74 0.05 1 48 36 8 ILE HB H 1.95 0.05 1 49 36 8 ILE HG2 H 0.89 0.05 1 50 36 8 ILE HD1 H 0.82 0.05 1 51 36 8 ILE CA C 63.8 0.50 1 52 36 8 ILE CB C 38.1 0.50 1 53 36 8 ILE CG1 C 28.6 0.50 1 54 36 8 ILE CG2 C 15.2 0.50 1 55 36 8 ILE CD1 C 12.2 0.50 1 56 36 8 ILE N N 116.476 0.50 1 57 37 9 ILE H H 8.507 0.05 1 58 37 9 ILE HA H 3.69 0.05 1 59 37 9 ILE HG2 H 0.9 0.05 1 60 37 9 ILE HD1 H 0.82 0.05 1 61 37 9 ILE CA C 64.5 0.50 1 62 37 9 ILE CB C 39.4 0.50 1 63 37 9 ILE CG1 C 28.6 0.50 1 64 37 9 ILE CG2 C 16.5 0.50 1 65 37 9 ILE CD1 C 12.2 0.50 1 66 37 9 ILE N N 119.272 0.50 1 67 38 10 LEU H H 8.363 0.05 1 68 38 10 LEU HA H 4.27 0.05 1 69 38 10 LEU CA C 57.6 0.50 1 70 38 10 LEU CB C 40.1 0.50 1 71 38 10 LEU CG C 26.6 0.50 1 72 38 10 LEU N N 118.624 0.50 1 73 39 11 GLU H H 8.663 0.05 1 74 39 11 GLU HA H 4.0 0.05 1 75 39 11 GLU CA C 59.9 0.50 1 76 39 11 GLU CB C 28.0 0.50 1 77 39 11 GLU CG C 37.7 0.50 1 78 39 11 GLU N N 118.123 0.50 1 79 40 12 ARG H H 7.977 0.05 1 80 40 12 ARG HA H 4.19 0.05 1 81 40 12 ARG HB2 H 2.04 0.05 2 82 40 12 ARG HB3 H 2.1 0.05 2 83 40 12 ARG HG2 H 1.7 0.05 2 84 40 12 ARG HG3 H 1.76 0.05 2 85 40 12 ARG HD2 H 3.26 0.05 2 86 40 12 ARG HD3 H 3.21 0.05 2 87 40 12 ARG CA C 58.5 0.50 1 88 40 12 ARG CB C 29.5 0.50 1 89 40 12 ARG CG C 26.5 0.50 1 90 40 12 ARG CD C 43.4 0.50 1 91 40 12 ARG N N 120.23 0.50 1 92 41 13 SER H H 7.975 0.05 1 93 41 13 SER HA H 4.21 0.05 1 94 41 13 SER CA C 61.9 0.50 1 95 41 13 SER CB C 63.0 0.50 1 96 41 13 SER N N 114.69 0.50 1 97 42 14 ALA H H 8.578 0.05 1 98 42 14 ALA HA H 3.67 0.05 1 99 42 14 ALA HB H 1.31 0.05 1 100 42 14 ALA CA C 54.7 0.50 1 101 42 14 ALA CB C 17.2 0.50 1 102 42 14 ALA N N 124.202 0.50 1 103 43 15 LYS H H 7.958 0.05 1 104 43 15 LYS HA H 4.06 0.05 1 105 43 15 LYS CA C 58.4 0.50 1 106 43 15 LYS CB C 31.3 0.50 1 107 43 15 LYS CG C 24.8 0.50 1 108 43 15 LYS N N 121.324 0.50 1 109 44 16 ASP H H 8.111 0.05 1 110 44 16 ASP HA H 4.39 0.05 1 111 44 16 ASP HB2 H 2.59 0.05 2 112 44 16 ASP HB3 H 2.97 0.05 2 113 44 16 ASP CA C 57.2 0.50 1 114 44 16 ASP CB C 39.3 0.50 1 115 44 16 ASP N N 118.176 0.50 1 116 45 17 ILE H H 7.417 0.05 1 117 45 17 ILE HA H 3.82 0.05 1 118 45 17 ILE HB H 2.1 0.05 1 119 45 17 ILE HG2 H 0.89 0.05 1 120 45 17 ILE HD1 H 0.8 0.05 1 121 45 17 ILE CA C 64.7 0.50 1 122 45 17 ILE CB C 37.6 0.50 1 123 45 17 ILE CG1 C 29.7 0.50 1 124 45 17 ILE CG2 C 16.8 0.50 1 125 45 17 ILE CD1 C 13.4 0.50 1 126 45 17 ILE N N 117.643 0.50 1 127 46 18 THR H H 7.702 0.05 1 128 46 18 THR HA H 4.16 0.05 1 129 46 18 THR HB H 3.74 0.05 1 130 46 18 THR HG2 H 1.18 0.05 1 131 46 18 THR CA C 66.2 0.50 1 132 46 18 THR CB C 67.5 0.50 1 133 46 18 THR CG2 C 22.0 0.50 1 134 46 18 THR N N 116.31 0.50 1 135 47 19 ASP H H 9.154 0.05 1 136 47 19 ASP HA H 4.46 0.05 1 137 47 19 ASP HB2 H 2.65 0.05 2 138 47 19 ASP HB3 H 2.82 0.05 2 139 47 19 ASP CA C 57.0 0.50 1 140 47 19 ASP CB C 39.4 0.50 1 141 47 19 ASP N N 121.55 0.50 1 142 48 20 GLU H H 7.812 0.05 1 143 48 20 GLU HA H 4.27 0.05 1 144 48 20 GLU CA C 58.5 0.50 1 145 48 20 GLU CB C 29.0 0.50 1 146 48 20 GLU N N 122.105 0.50 1 147 49 21 ILE H H 8.655 0.05 1 148 49 21 ILE HA H 3.58 0.05 1 149 49 21 ILE HB H 2.07 0.05 1 150 49 21 ILE HG2 H 0.83 0.05 1 151 49 21 ILE HD1 H 0.65 0.05 1 152 49 21 ILE CA C 65.7 0.50 1 153 49 21 ILE CB C 36.9 0.50 1 154 49 21 ILE CG1 C 29.3 0.50 1 155 49 21 ILE CG2 C 17.1 0.50 1 156 49 21 ILE CD1 C 13.5 0.50 1 157 49 21 ILE N N 119.77 0.50 1 158 50 22 ASN H H 8.399 0.05 1 159 50 22 ASN HA H 4.46 0.05 1 160 50 22 ASN CA C 55.9 0.50 1 161 50 22 ASN CB C 37.0 0.50 1 162 50 22 ASN N N 118.094 0.50 1 163 51 23 LYS H H 7.949 0.05 1 164 51 23 LYS HA H 4.1 0.05 1 165 51 23 LYS HB3 H 2.03 0.05 2 166 51 23 LYS CA C 59.5 0.50 1 167 51 23 LYS CB C 31.7 0.50 1 168 51 23 LYS CG C 24.9 0.50 1 169 51 23 LYS N N 122.985 0.50 1 170 52 24 ILE H H 8.584 0.05 1 171 52 24 ILE HA H 3.79 0.05 1 172 52 24 ILE HG2 H 0.92 0.05 1 173 52 24 ILE HD1 H 0.95 0.05 1 174 52 24 ILE CA C 65.8 0.50 1 175 52 24 ILE CB C 38.5 0.50 1 176 52 24 ILE CG1 C 30.0 0.50 1 177 52 24 ILE CG2 C 17.4 0.50 1 178 52 24 ILE CD1 C 14.3 0.50 1 179 52 24 ILE N N 121.342 0.50 1 180 53 25 LYS H H 8.548 0.05 1 181 53 25 LYS HA H 3.92 0.05 1 182 53 25 LYS CA C 60.4 0.50 1 183 53 25 LYS CB C 32.1 0.50 1 184 53 25 LYS CG C 26.7 0.50 1 185 53 25 LYS N N 118.268 0.50 1 186 54 26 LYS H H 7.855 0.05 1 187 54 26 LYS HA H 4.16 0.05 1 188 54 26 LYS HB3 H 2.11 0.05 2 189 54 26 LYS HG3 H 1.54 0.05 2 190 54 26 LYS CA C 58.9 0.50 1 191 54 26 LYS CB C 31.8 0.50 1 192 54 26 LYS CG C 24.7 0.50 1 193 54 26 LYS N N 122.485 0.50 1 194 55 27 ASP H H 8.813 0.05 1 195 55 27 ASP HA H 4.34 0.05 1 196 55 27 ASP CA C 56.9 0.50 1 197 55 27 ASP CB C 39.9 0.50 1 198 55 27 ASP N N 120.775 0.50 1 199 56 28 ALA H H 9.101 0.05 1 200 56 28 ALA HA H 3.52 0.05 1 201 56 28 ALA HB H 1.76 0.05 1 202 56 28 ALA CA C 55.1 0.50 1 203 56 28 ALA CB C 17.1 0.50 1 204 56 28 ALA N N 123.205 0.50 1 205 57 29 ALA H H 7.77 0.05 1 206 57 29 ALA HA H 4.24 0.05 1 207 57 29 ALA HB H 1.6 0.05 1 208 57 29 ALA CA C 54.8 0.50 1 209 57 29 ALA CB C 17.3 0.50 1 210 57 29 ALA N N 121.461 0.50 1 211 58 30 ASP H H 8.443 0.05 1 212 58 30 ASP HA H 4.39 0.05 1 213 58 30 ASP HB3 H 2.77 0.05 2 214 58 30 ASP CA C 56.4 0.50 1 215 58 30 ASP CB C 39.8 0.50 1 216 58 30 ASP N N 119.548 0.50 1 217 59 31 ASN H H 7.5 0.05 1 218 59 31 ASN HA H 4.65 0.05 1 219 59 31 ASN HB2 H 2.05 0.05 2 220 59 31 ASN HB3 H 2.62 0.05 2 221 59 31 ASN CA C 53.0 0.50 1 222 59 31 ASN CB C 39.2 0.50 1 223 59 31 ASN N N 115.622 0.50 1 224 60 32 ASN H H 7.93 0.05 1 225 60 32 ASN HA H 4.33 0.05 1 226 60 32 ASN HB2 H 2.74 0.05 2 227 60 32 ASN HB3 H 3.07 0.05 2 228 60 32 ASN CA C 54.3 0.50 1 229 60 32 ASN CB C 36.7 0.50 1 230 60 32 ASN N N 116.019 0.50 1 231 61 33 VAL H H 8.245 0.05 1 232 61 33 VAL HA H 3.96 0.05 1 233 61 33 VAL HB H 1.68 0.05 1 234 61 33 VAL HG1 H 0.63 0.05 2 235 61 33 VAL HG2 H 0.7 0.05 2 236 61 33 VAL CA C 61.5 0.50 1 237 61 33 VAL CB C 32.6 0.50 1 238 61 33 VAL CG1 C 21.2 0.50 2 239 61 33 VAL CG2 C 20.8 0.50 2 240 61 33 VAL N N 119.072 0.50 1 241 62 34 ASN H H 8.524 0.05 1 242 62 34 ASN HA H 4.64 0.05 1 243 62 34 ASN HB2 H 2.83 0.05 2 244 62 34 ASN HB3 H 2.9 0.05 2 245 62 34 ASN CA C 52.1 0.50 1 246 62 34 ASN CB C 38.6 0.50 1 247 62 34 ASN N N 125.564 0.50 1 248 63 35 PHE H H 8.904 0.05 1 249 63 35 PHE CA C 60.7 0.50 1 250 63 35 PHE CB C 38.3 0.50 1 251 63 35 PHE N N 125.711 0.50 1 252 64 36 ALA H H 8.492 0.05 1 253 64 36 ALA HA H 4.2 0.05 1 254 64 36 ALA HB H 1.44 0.05 1 255 64 36 ALA CA C 53.8 0.50 1 256 64 36 ALA CB C 17.7 0.50 1 257 64 36 ALA N N 121.816 0.50 1 258 65 37 ALA H H 7.984 0.05 1 259 65 37 ALA HA H 4.18 0.05 1 260 65 37 ALA HB H 1.38 0.05 1 261 65 37 ALA CA C 53.4 0.50 1 262 65 37 ALA CB C 18.5 0.50 1 263 65 37 ALA N N 118.873 0.50 1 264 66 38 PHE H H 7.795 0.05 1 265 66 38 PHE HA H 4.06 0.05 1 266 66 38 PHE HB3 H 3.06 0.05 2 267 66 38 PHE CA C 60.7 0.50 1 268 66 38 PHE CB C 38.5 0.50 1 269 66 38 PHE N N 115.587 0.50 1 270 67 39 THR H H 7.563 0.05 1 271 67 39 THR HA H 4.33 0.05 1 272 67 39 THR CA C 61.9 0.50 1 273 67 39 THR CB C 69.0 0.50 1 274 67 39 THR N N 109.477 0.50 1 275 68 40 ASP H H 7.969 0.05 1 276 68 40 ASP HA H 4.65 0.05 1 277 68 40 ASP HB2 H 2.64 0.05 2 278 68 40 ASP HB3 H 2.72 0.05 2 279 68 40 ASP CA C 54.6 0.50 1 280 68 40 ASP CB C 40.9 0.50 1 281 68 40 ASP N N 122.883 0.50 1 282 69 41 SER H H 8.277 0.05 1 283 69 41 SER HA H 4.41 0.05 1 284 69 41 SER HB3 H 3.94 0.05 2 285 69 41 SER CA C 58.5 0.50 1 286 69 41 SER CB C 63.4 0.50 1 287 69 41 SER N N 115.778 0.50 1 288 70 42 GLU H H 8.464 0.05 1 289 70 42 GLU HA H 4.36 0.05 1 290 70 42 GLU HB2 H 2.05 0.05 2 291 70 42 GLU HB3 H 2.26 0.05 2 292 70 42 GLU CA C 56.6 0.50 1 293 70 42 GLU CB C 29.3 0.50 1 294 70 42 GLU CG C 36.0 0.50 1 295 70 42 GLU N N 122.04 0.50 1 296 71 43 THR H H 8.06 0.05 1 297 71 43 THR HA H 4.32 0.05 1 298 71 43 THR HG2 H 1.2 0.05 1 299 71 43 THR CA C 61.9 0.50 1 300 71 43 THR CB C 69.2 0.50 1 301 71 43 THR CG2 C 21.7 0.50 1 302 71 43 THR N N 113.162 0.50 1 303 72 44 GLY H H 8.412 0.05 1 304 72 44 GLY HA3 H 3.96 0.05 2 305 72 44 GLY CA C 45.2 0.50 1 306 72 44 GLY N N 111.14 0.50 1 307 73 45 SER H H 8.237 0.05 1 308 73 45 SER HA H 4.41 0.05 1 309 73 45 SER HB3 H 3.94 0.05 2 310 73 45 SER CA C 58.4 0.50 1 311 73 45 SER CB C 63.4 0.50 1 312 73 45 SER N N 115.757 0.50 1 313 75 47 VAL H H 7.997 0.05 1 314 75 47 VAL HA H 4.15 0.05 1 315 75 47 VAL HB H 2.1 0.05 1 316 75 47 VAL HG1 H 0.93 0.05 2 317 75 47 VAL HG2 H 0.93 0.05 2 318 75 47 VAL CA C 61.9 0.50 1 319 75 47 VAL CB C 32.6 0.50 1 320 75 47 VAL CG1 C 21.1 0.50 2 321 75 47 VAL CG2 C 20.6 0.50 2 322 75 47 VAL N N 118.866 0.50 1 323 76 48 SER H H 8.183 0.05 1 324 76 48 SER HA H 4.28 0.05 1 325 76 48 SER HB2 H 3.71 0.05 2 326 76 48 SER HB3 H 3.93 0.05 2 327 76 48 SER CA C 58.6 0.50 1 328 76 48 SER CB C 63.4 0.50 1 329 76 48 SER N N 117.059 0.50 1 330 77 49 GLU H H 8.302 0.05 1 331 77 49 GLU HA H 4.32 0.05 1 332 77 49 GLU HB2 H 1.94 0.05 2 333 77 49 GLU HB3 H 2.24 0.05 2 334 77 49 GLU CA C 55.9 0.50 1 335 77 49 GLU CB C 29.7 0.50 1 336 77 49 GLU CG C 36.2 0.50 1 337 77 49 GLU N N 121.924 0.50 1 338 78 50 ASN H H 8.308 0.05 1 339 78 50 ASN HA H 4.76 0.05 1 340 78 50 ASN HB2 H 2.71 0.05 2 341 78 50 ASN HB3 H 2.88 0.05 2 342 78 50 ASN CA C 52.9 0.50 1 343 78 50 ASN CB C 39.1 0.50 1 344 78 50 ASN N N 120.401 0.50 1 345 79 51 SER CA C 58.3 0.50 1 346 79 51 SER CB C 62.3 0.50 1 347 80 52 PHE H H 8.28 0.05 1 348 80 52 PHE HA H 4.22 0.05 1 349 80 52 PHE HB3 H 1.89 0.05 2 350 80 52 PHE CA C 61.2 0.50 1 351 80 52 PHE CB C 38.2 0.50 1 352 80 52 PHE N N 121.812 0.50 1 353 81 53 ILE H H 7.483 0.05 1 354 81 53 ILE HA H 3.23 0.05 1 355 81 53 ILE HB H 1.98 0.05 1 356 81 53 ILE HG2 H 0.58 0.05 1 357 81 53 ILE HD1 H 0.35 0.05 1 358 81 53 ILE CA C 63.6 0.50 1 359 81 53 ILE CB C 36.7 0.50 1 360 81 53 ILE CG1 C 28.2 0.50 1 361 81 53 ILE CG2 C 17.2 0.50 1 362 81 53 ILE CD1 C 11.8 0.50 1 363 81 53 ILE N N 119.199 0.50 1 364 82 54 LEU H H 7.464 0.05 1 365 82 54 LEU HA H 4.12 0.05 1 366 82 54 LEU HD1 H 1.03 0.05 2 367 82 54 LEU CA C 57.6 0.50 1 368 82 54 LEU CB C 42.7 0.50 1 369 82 54 LEU CG C 26.8 0.50 1 370 82 54 LEU CD1 C 23.7 0.50 2 371 82 54 LEU N N 117.108 0.50 1 372 83 55 GLU H H 8.093 0.05 1 373 83 55 GLU HA H 3.67 0.05 1 374 83 55 GLU HB3 H 1.59 0.05 2 375 83 55 GLU CA C 58.9 0.50 1 376 83 55 GLU CB C 29.1 0.50 1 377 83 55 GLU CG C 36.5 0.50 1 378 83 55 GLU N N 117.3 0.50 1 379 84 56 ALA H H 8.431 0.05 1 380 84 56 ALA HA H 3.85 0.05 1 381 84 56 ALA HB H 1.39 0.05 1 382 84 56 ALA CA C 55.0 0.50 1 383 84 56 ALA CB C 18.4 0.50 1 384 84 56 ALA N N 122.149 0.50 1 385 85 57 LYS H H 8.122 0.05 1 386 85 57 LYS HA H 3.96 0.05 1 387 85 57 LYS CA C 60.7 0.50 1 388 85 57 LYS CB C 31.8 0.50 1 389 85 57 LYS N N 116.458 0.50 1 390 86 58 VAL H H 8.116 0.05 1 391 86 58 VAL HA H 3.34 0.05 1 392 86 58 VAL HB H 2.33 0.05 1 393 86 58 VAL HG1 H 1.01 0.05 2 394 86 58 VAL HG2 H 0.86 0.05 2 395 86 58 VAL CA C 67.6 0.50 1 396 86 58 VAL CB C 31.4 0.50 1 397 86 58 VAL CG1 C 23.4 0.50 2 398 86 58 VAL CG2 C 21.5 0.50 2 399 86 58 VAL N N 122.206 0.50 1 400 87 59 ARG H H 8.768 0.05 1 401 87 59 ARG HA H 4.03 0.05 1 402 87 59 ARG CA C 59.4 0.50 1 403 87 59 ARG CB C 30.8 0.50 1 404 87 59 ARG N N 122.354 0.50 1 405 88 60 ALA H H 8.789 0.05 1 406 88 60 ALA HA H 3.9 0.05 1 407 88 60 ALA HB H 1.32 0.05 1 408 88 60 ALA CA C 54.8 0.50 1 409 88 60 ALA CB C 18.2 0.50 1 410 88 60 ALA N N 119.659 0.50 1 411 89 61 THR H H 8.063 0.05 1 412 89 61 THR HA H 4.31 0.05 1 413 89 61 THR CA C 65.6 0.50 1 414 89 61 THR CB C 67.9 0.50 1 415 89 61 THR N N 105.646 0.50 1 416 90 62 THR H H 8.021 0.05 1 417 90 62 THR HA H 4.37 0.05 1 418 90 62 THR CA C 67.0 0.50 1 419 90 62 THR CB C 68.2 0.50 1 420 90 62 THR N N 120.262 0.50 1 421 91 63 VAL H H 7.653 0.05 1 422 91 63 VAL HA H 4.02 0.05 1 423 91 63 VAL HB H 2.17 0.05 1 424 91 63 VAL HG2 H 1.12 0.05 2 425 91 63 VAL CA C 65.3 0.50 1 426 91 63 VAL CB C 30.9 0.50 1 427 91 63 VAL CG2 C 21.6 0.50 2 428 91 63 VAL N N 119.1 0.50 1 429 92 64 ALA H H 8.189 0.05 1 430 92 64 ALA HA H 4.3 0.05 1 431 92 64 ALA HB H 1.57 0.05 1 432 92 64 ALA CA C 54.6 0.50 1 433 92 64 ALA CB C 19.5 0.50 1 434 92 64 ALA N N 124.8 0.50 1 435 93 65 GLU H H 8.71 0.05 1 436 93 65 GLU HA H 3.78 0.05 1 437 93 65 GLU HB3 H 2.19 0.05 2 438 93 65 GLU CA C 60.2 0.50 1 439 93 65 GLU CB C 28.7 0.50 1 440 93 65 GLU CG C 37.0 0.50 1 441 93 65 GLU N N 120.3 0.50 1 442 94 66 LYS H H 7.575 0.05 1 443 94 66 LYS HA H 4.1 0.05 1 444 94 66 LYS HB3 H 2.08 0.05 2 445 94 66 LYS CA C 59.5 0.50 1 446 94 66 LYS CB C 31.5 0.50 1 447 94 66 LYS CG C 25.0 0.50 1 448 94 66 LYS N N 119.247 0.50 1 449 95 67 PHE H H 7.467 0.05 1 450 95 67 PHE HA H 4.61 0.05 1 451 95 67 PHE HB3 H 3.3 0.05 2 452 95 67 PHE CA C 59.7 0.50 1 453 95 67 PHE CB C 39.0 0.50 1 454 95 67 PHE N N 121.711 0.50 1 455 96 68 VAL H H 8.186 0.05 1 456 96 68 VAL HA H 3.13 0.05 1 457 96 68 VAL HB H 2.29 0.05 1 458 96 68 VAL HG1 H 1.04 0.05 2 459 96 68 VAL HG2 H 1.15 0.05 2 460 96 68 VAL CA C 66.9 0.50 1 461 96 68 VAL CB C 31.0 0.50 1 462 96 68 VAL CG1 C 24.5 0.50 2 463 96 68 VAL CG2 C 23.5 0.50 2 464 96 68 VAL N N 119.674 0.50 1 465 97 69 THR H H 8.47 0.05 1 466 97 69 THR HA H 4.3 0.05 1 467 97 69 THR HG2 H 1.24 0.05 1 468 97 69 THR CA C 65.6 0.50 1 469 97 69 THR CB C 68.3 0.50 1 470 97 69 THR CG2 C 21.9 0.50 1 471 97 69 THR N N 117.086 0.50 1 472 98 70 ALA H H 7.842 0.05 1 473 98 70 ALA HA H 4.17 0.05 1 474 98 70 ALA HB H 1.5 0.05 1 475 98 70 ALA CA C 55.1 0.50 1 476 98 70 ALA CB C 16.7 0.50 1 477 98 70 ALA N N 126.429 0.50 1 478 99 71 ILE H H 7.937 0.05 1 479 99 71 ILE HA H 3.48 0.05 1 480 99 71 ILE HB H 2.25 0.05 1 481 99 71 ILE HG2 H 0.75 0.05 1 482 99 71 ILE HD1 H 0.58 0.05 1 483 99 71 ILE CA C 64.0 0.50 1 484 99 71 ILE CB C 35.2 0.50 1 485 99 71 ILE CG1 C 27.4 0.50 1 486 99 71 ILE CG2 C 16.7 0.50 1 487 99 71 ILE CD1 C 11.8 0.50 1 488 99 71 ILE N N 121.241 0.50 1 489 100 72 GLU H H 8.458 0.05 1 490 100 72 GLU HA H 3.72 0.05 1 491 100 72 GLU CA C 59.0 0.50 1 492 100 72 GLU CB C 29.3 0.50 1 493 100 72 GLU N N 118.069 0.50 1 494 101 73 GLY H H 8.411 0.05 1 495 101 73 GLY HA2 H 3.85 0.05 2 496 101 73 GLY HA3 H 4.11 0.05 2 497 101 73 GLY CA C 46.9 0.50 1 498 101 73 GLY N N 107.21 0.50 1 499 102 74 GLU H H 8.344 0.05 1 500 102 74 GLU HA H 4.18 0.05 1 501 102 74 GLU CA C 57.8 0.50 1 502 102 74 GLU CB C 28.7 0.50 1 503 102 74 GLU N N 121.134 0.50 1 504 103 75 ALA H H 9.325 0.05 1 505 103 75 ALA HA H 4.05 0.05 1 506 103 75 ALA HB H 1.49 0.05 1 507 103 75 ALA CA C 56.0 0.50 1 508 103 75 ALA CB C 16.5 0.50 1 509 103 75 ALA N N 121.862 0.50 1 510 104 76 THR H H 7.796 0.05 1 511 104 76 THR HA H 4.33 0.05 1 512 104 76 THR HB H 3.75 0.05 1 513 104 76 THR CA C 67.0 0.50 1 514 104 76 THR CB C 68.1 0.50 1 515 104 76 THR N N 110.782 0.50 1 516 105 77 LYS H H 7.728 0.05 1 517 105 77 LYS HA H 4.05 0.05 1 518 105 77 LYS HB3 H 1.98 0.05 2 519 105 77 LYS CA C 59.2 0.50 1 520 105 77 LYS CB C 32.2 0.50 1 521 105 77 LYS CG C 24.5 0.50 1 522 105 77 LYS N N 123.041 0.50 1 523 106 78 LEU H H 7.768 0.05 1 524 106 78 LEU HA H 4.51 0.05 1 525 106 78 LEU HB3 H 1.79 0.05 2 526 106 78 LEU HD1 H 0.69 0.05 2 527 106 78 LEU HD2 H 0.69 0.05 2 528 106 78 LEU CA C 54.2 0.50 1 529 106 78 LEU CB C 42.3 0.50 1 530 106 78 LEU CG C 26.6 0.50 1 531 106 78 LEU CD1 C 22.8 0.50 2 532 106 78 LEU CD2 C 25.0 0.50 2 533 106 78 LEU N N 117.015 0.50 1 534 107 79 LYS H H 7.452 0.05 1 535 107 79 LYS HA H 3.92 0.05 1 536 107 79 LYS HB3 H 2.0 0.05 2 537 107 79 LYS CA C 60.9 0.50 1 538 107 79 LYS CB C 32.5 0.50 1 539 107 79 LYS CG C 25.4 0.50 1 540 107 79 LYS N N 122.173 0.50 1 541 108 80 LYS H H 8.735 0.05 1 542 108 80 LYS HA H 4.6 0.05 1 543 108 80 LYS HB2 H 1.51 0.05 2 544 108 80 LYS HB3 H 2.01 0.05 2 545 108 80 LYS CA C 56.8 0.50 1 546 108 80 LYS CB C 32.8 0.50 1 547 108 80 LYS CG C 25.1 0.50 1 548 108 80 LYS N N 114.243 0.50 1 549 109 81 THR H H 7.53 0.05 1 550 109 81 THR HA H 4.41 0.05 1 551 109 81 THR CA C 61.5 0.50 1 552 109 81 THR CB C 69.7 0.50 1 553 109 81 THR N N 106.918 0.50 1 554 110 82 GLY H H 9.066 0.05 1 555 110 82 GLY HA2 H 3.52 0.05 2 556 110 82 GLY HA3 H 4.12 0.05 2 557 110 82 GLY CA C 45.2 0.50 1 558 110 82 GLY N N 111.753 0.50 1 559 111 83 SER H H 8.709 0.05 1 560 111 83 SER HA H 4.93 0.05 1 561 111 83 SER HB2 H 4.07 0.05 2 562 111 83 SER HB3 H 4.25 0.05 2 563 111 83 SER CA C 56.6 0.50 1 564 111 83 SER CB C 66.4 0.50 1 565 111 83 SER N N 118.638 0.50 1 566 112 84 SER H H 9.082 0.05 1 567 112 84 SER CA C 61.2 0.50 1 568 112 84 SER CB C 62.5 0.50 1 569 112 84 SER N N 116.928 0.50 1 570 113 85 GLY HA3 H 3.97 0.05 2 571 113 85 GLY CA C 46.3 0.50 1 572 114 86 GLU H H 7.628 0.05 1 573 114 86 GLU HA H 3.75 0.05 1 574 114 86 GLU HB3 H 1.82 0.05 2 575 114 86 GLU CA C 59.0 0.50 1 576 114 86 GLU CB C 28.9 0.50 1 577 114 86 GLU N N 122.746 0.50 1 578 115 87 PHE H H 7.102 0.05 1 579 115 87 PHE HA H 4.42 0.05 1 580 115 87 PHE CA C 61.5 0.50 1 581 115 87 PHE CB C 36.9 0.50 1 582 115 87 PHE N N 118.328 0.50 1 583 116 88 SER H H 8.94 0.05 1 584 116 88 SER HA H 4.51 0.05 1 585 116 88 SER HB3 H 4.37 0.05 2 586 116 88 SER CA C 61.7 0.50 1 587 116 88 SER CB C 62.8 0.50 1 588 116 88 SER N N 115.349 0.50 1 589 117 89 ALA H H 7.501 0.05 1 590 117 89 ALA HA H 4.27 0.05 1 591 117 89 ALA HB H 1.56 0.05 1 592 117 89 ALA CA C 54.8 0.50 1 593 117 89 ALA CB C 17.4 0.50 1 594 117 89 ALA N N 122.73 0.50 1 595 118 90 MET H H 7.812 0.05 1 596 118 90 MET HA H 3.95 0.05 1 597 118 90 MET CA C 60.3 0.50 1 598 118 90 MET CB C 31.5 0.50 1 599 118 90 MET N N 118.754 0.50 1 600 119 91 TYR H H 8.213 0.05 1 601 119 91 TYR HA H 4.35 0.05 1 602 119 91 TYR HB3 H 3.23 0.05 2 603 119 91 TYR CA C 61.3 0.50 1 604 119 91 TYR CB C 37.2 0.50 1 605 119 91 TYR N N 119.385 0.50 1 606 120 92 ASN H H 8.592 0.05 1 607 120 92 ASN HA H 4.15 0.05 1 608 120 92 ASN HB2 H 2.82 0.05 2 609 120 92 ASN HB3 H 2.84 0.05 2 610 120 92 ASN CA C 56.2 0.50 1 611 120 92 ASN CB C 37.5 0.50 1 612 120 92 ASN N N 116.665 0.50 1 613 121 93 MET H H 7.9 0.05 1 614 121 93 MET HA H 4.25 0.05 1 615 121 93 MET CA C 59.5 0.50 1 616 121 93 MET CB C 33.8 0.50 1 617 121 93 MET CG C 32.6 0.50 1 618 121 93 MET N N 118.788 0.50 1 619 122 94 MET H H 7.813 0.05 1 620 122 94 MET HA H 3.95 0.05 1 621 122 94 MET CA C 60.3 0.50 1 622 122 94 MET CB C 33.4 0.50 1 623 122 94 MET N N 118.67 0.50 1 624 123 95 LEU H H 7.941 0.05 1 625 123 95 LEU HA H 3.91 0.05 1 626 123 95 LEU HB3 H 1.36 0.05 2 627 123 95 LEU HG H 1.25 0.05 1 628 123 95 LEU HD1 H 0.81 0.05 2 629 123 95 LEU HD2 H 0.82 0.05 2 630 123 95 LEU CA C 57.5 0.50 1 631 123 95 LEU CB C 41.5 0.50 1 632 123 95 LEU CG C 26.5 0.50 1 633 123 95 LEU CD1 C 24.5 0.50 2 634 123 95 LEU CD2 C 26.4 0.50 2 635 123 95 LEU N N 118.865 0.50 1 636 124 96 GLU H H 8.398 0.05 1 637 124 96 GLU HA H 3.95 0.05 1 638 124 96 GLU HB2 H 2.02 0.05 2 639 124 96 GLU HB3 H 2.19 0.05 2 640 124 96 GLU CA C 59.3 0.50 1 641 124 96 GLU CB C 29.0 0.50 1 642 124 96 GLU CG C 37.1 0.50 1 643 124 96 GLU N N 121.088 0.50 1 644 125 97 VAL H H 7.682 0.05 1 645 125 97 VAL HA H 4.0 0.05 1 646 125 97 VAL HG1 H 0.65 0.05 2 647 125 97 VAL HG2 H 0.7 0.05 2 648 125 97 VAL CA C 63.1 0.50 1 649 125 97 VAL CB C 31.2 0.50 1 650 125 97 VAL CG1 C 20.5 0.50 2 651 125 97 VAL CG2 C 20.1 0.50 2 652 125 97 VAL N N 112.092 0.50 1 653 126 98 SER H H 7.41 0.05 1 654 126 98 SER CA C 63.3 0.50 1 655 126 98 SER CB C 62.8 0.50 1 656 126 98 SER N N 116.396 0.50 1 657 127 99 GLY H H 7.321 0.05 1 658 127 99 GLY HA2 H 3.82 0.05 2 659 127 99 GLY HA3 H 4.07 0.05 2 660 127 99 GLY CA C 48.1 0.50 1 661 127 99 GLY N N 107.199 0.50 1 662 128 100 PRO HA H 4.31 0.05 1 663 128 100 PRO CA C 64.8 0.50 1 664 128 100 PRO CB C 32.0 0.50 1 665 129 101 LEU H H 6.913 0.05 1 666 129 101 LEU HA H 3.9 0.05 1 667 129 101 LEU HB3 H 2.04 0.05 2 668 129 101 LEU HG H 0.8 0.05 1 669 129 101 LEU CA C 57.4 0.50 1 670 129 101 LEU CB C 41.0 0.50 1 671 129 101 LEU CG C 26.6 0.50 1 672 129 101 LEU CD1 C 22.7 0.50 2 673 129 101 LEU N N 113.172 0.50 1 674 130 102 GLU H H 8.203 0.05 1 675 130 102 GLU HA H 4.12 0.05 1 676 130 102 GLU CA C 59.3 0.50 1 677 130 102 GLU CB C 28.5 0.50 1 678 130 102 GLU N N 121.331 0.50 1 679 131 103 GLU HA H 3.97 0.05 1 680 131 103 GLU CA C 58.5 0.50 1 681 131 103 GLU CB C 29.2 0.50 1 682 131 103 GLU CG C 36.5 0.50 1 683 132 104 LEU H H 6.977 0.05 1 684 132 104 LEU HA H 3.91 0.05 1 685 132 104 LEU HB2 H 1.52 0.05 2 686 132 104 LEU HB3 H 1.7 0.05 2 687 132 104 LEU HG H 0.66 0.05 1 688 132 104 LEU HD1 H 0.4 0.05 2 689 132 104 LEU CA C 53.1 0.50 1 690 132 104 LEU CB C 41.2 0.50 1 691 132 104 LEU CG C 26.4 0.50 1 692 132 104 LEU CD1 C 24.0 0.50 2 693 132 104 LEU N N 115.804 0.50 1 694 133 105 GLY H H 7.484 0.05 1 695 133 105 GLY HA2 H 3.55 0.05 2 696 133 105 GLY HA3 H 4.36 0.05 2 697 133 105 GLY CA C 45.1 0.50 1 698 133 105 GLY N N 105.653 0.50 1 699 134 106 VAL HG1 H 1.0 0.05 2 700 134 106 VAL HG2 H 0.98 0.05 2 701 134 106 VAL CA C 62.9 0.50 1 702 134 106 VAL CB C 31.8 0.50 1 703 134 106 VAL CG1 C 20.5 0.50 2 704 134 106 VAL CG2 C 19.06 0.50 2 705 137 109 MET CA C 58.1 0.50 1 706 138 110 THR H H 9.225 0.05 1 707 138 110 THR CA C 67.1 0.50 1 708 138 110 THR N N 115.359 0.50 1 709 139 111 LYS H H 8.172 0.05 1 710 139 111 LYS HA H 4.2 0.05 1 711 139 111 LYS CA C 57.9 0.50 1 712 139 111 LYS CB C 31.6 0.50 1 713 139 111 LYS N N 123.109 0.50 1 714 140 112 THR H H 8.063 0.05 1 715 140 112 THR HA H 4.0 0.05 1 716 140 112 THR CA C 67.0 0.50 1 717 140 112 THR CB C 68.2 0.50 1 718 140 112 THR N N 115.472 0.50 1 719 141 113 VAL H H 7.753 0.05 1 720 141 113 VAL HA H 3.63 0.05 1 721 141 113 VAL HB H 2.31 0.05 1 722 141 113 VAL HG1 H 0.93 0.05 2 723 141 113 VAL HG2 H 1.08 0.05 2 724 141 113 VAL CA C 67.2 0.50 1 725 141 113 VAL CB C 31.5 0.50 1 726 141 113 VAL CG1 C 23.0 0.50 2 727 141 113 VAL CG2 C 23.6 0.50 2 728 141 113 VAL N N 121.319 0.50 1 729 142 114 THR H H 8.965 0.05 1 730 142 114 THR HA H 4.38 0.05 1 731 142 114 THR HG2 H 1.34 0.05 1 732 142 114 THR CA C 65.9 0.50 1 733 142 114 THR CB C 67.8 0.50 1 734 142 114 THR CG2 C 21.8 0.50 1 735 142 114 THR N N 114.753 0.50 1 736 143 115 ASP H H 9.254 0.05 1 737 143 115 ASP HA H 4.41 0.05 1 738 143 115 ASP HB2 H 2.58 0.05 2 739 143 115 ASP HB3 H 2.97 0.05 2 740 143 115 ASP CA C 56.8 0.50 1 741 143 115 ASP CB C 39.0 0.50 1 742 143 115 ASP N N 123.699 0.50 1 743 144 116 ALA H H 7.668 0.05 1 744 144 116 ALA HA H 4.34 0.05 1 745 144 116 ALA HB H 1.78 0.05 1 746 144 116 ALA CA C 54.7 0.50 1 747 144 116 ALA CB C 19.2 0.50 1 748 144 116 ALA N N 122.856 0.50 1 749 145 117 ALA H H 7.718 0.05 1 750 145 117 ALA HA H 4.54 0.05 1 751 145 117 ALA HB H 1.38 0.05 1 752 145 117 ALA CA C 52.7 0.50 1 753 145 117 ALA CB C 18.2 0.50 1 754 145 117 ALA N N 119.307 0.50 1 755 146 118 GLU H H 7.491 0.05 1 756 146 118 GLU HA H 4.19 0.05 1 757 146 118 GLU HB2 H 2.15 0.05 2 758 146 118 GLU HB3 H 2.22 0.05 2 759 146 118 GLU CA C 57.3 0.50 1 760 146 118 GLU CB C 29.1 0.50 1 761 146 118 GLU CG C 36.1 0.50 1 762 146 118 GLU N N 115.837 0.50 1 763 147 119 GLN H H 7.248 0.05 1 764 147 119 GLN HA H 4.2 0.05 1 765 147 119 GLN HB2 H 1.69 0.05 2 766 147 119 GLN HB3 H 2.1 0.05 2 767 147 119 GLN HE22 H 6.71 0.05 2 768 147 119 GLN CA C 55.3 0.50 1 769 147 119 GLN CB C 30.1 0.50 1 770 147 119 GLN CG C 33.3 0.50 1 771 147 119 GLN N N 115.066 0.50 1 772 147 119 GLN NE2 N 111.5 0.50 1 773 148 120 HIS H H 7.747 0.05 1 774 148 120 HIS HA H 5.0 0.05 1 775 148 120 HIS HB3 H 2.66 0.05 2 776 148 120 HIS CA C 52.5 0.50 1 777 148 120 HIS CB C 31.6 0.50 1 778 148 120 HIS N N 119.398 0.50 1 779 149 121 PRO HA H 4.47 0.05 1 780 149 121 PRO CA C 62.3 0.50 1 781 149 121 PRO CB C 32.3 0.50 1 782 150 122 THR H H 7.864 0.05 1 783 150 122 THR HA H 4.04 0.05 1 784 150 122 THR CA C 60.7 0.50 1 785 150 122 THR CB C 68.4 0.50 1 786 150 122 THR N N 108.042 0.50 1 787 151 123 THR H H 6.9 0.05 1 788 151 123 THR HA H 4.55 0.05 1 789 151 123 THR HB H 4.13 0.05 1 790 151 123 THR HG2 H 0.35 0.05 1 791 151 123 THR CA C 60.4 0.50 1 792 151 123 THR CB C 68.9 0.50 1 793 151 123 THR CG2 C 21.5 0.50 1 794 151 123 THR N N 99.2 0.50 1 795 152 124 THR H H 7.104 0.05 1 796 152 124 THR HA H 4.29 0.05 1 797 152 124 THR HG2 H 1.06 0.05 1 798 152 124 THR CA C 57.7 0.50 1 799 152 124 THR CB C 71.5 0.50 1 800 152 124 THR CG2 C 21.5 0.50 1 801 152 124 THR N N 108.396 0.50 1 802 153 125 ALA H H 7.58 0.05 1 803 153 125 ALA HA H 3.03 0.05 1 804 153 125 ALA HB H 1.13 0.05 1 805 153 125 ALA CA C 54.7 0.50 1 806 153 125 ALA CB C 18.8 0.50 1 807 153 125 ALA N N 122.816 0.50 1 808 154 126 GLU H H 8.544 0.05 1 809 154 126 GLU HA H 3.74 0.05 1 810 154 126 GLU CA C 59.8 0.50 1 811 154 126 GLU CB C 28.3 0.50 1 812 154 126 GLU CG C 37.0 0.50 1 813 154 126 GLU N N 113.788 0.50 1 814 155 127 GLY H H 7.973 0.05 1 815 155 127 GLY HA2 H 3.65 0.05 2 816 155 127 GLY HA3 H 4.67 0.05 2 817 155 127 GLY CA C 46.9 0.50 1 818 155 127 GLY N N 108.136 0.50 1 819 156 128 ILE H H 7.688 0.05 1 820 156 128 ILE HA H 3.7 0.05 1 821 156 128 ILE HB H 2.15 0.05 1 822 156 128 ILE HG2 H 0.83 0.05 1 823 156 128 ILE HD1 H 0.91 0.05 1 824 156 128 ILE CA C 61.4 0.50 1 825 156 128 ILE CB C 34.7 0.50 1 826 156 128 ILE CG1 C 28.6 0.50 1 827 156 128 ILE CG2 C 18.5 0.50 1 828 156 128 ILE CD1 C 9.28 0.50 1 829 156 128 ILE N N 119.992 0.50 1 830 157 129 LEU H H 8.535 0.05 1 831 157 129 LEU HA H 3.89 0.05 1 832 157 129 LEU HB2 H 1.5 0.05 2 833 157 129 LEU HB3 H 1.94 0.05 2 834 157 129 LEU HG H 1.32 0.05 1 835 157 129 LEU HD1 H 0.71 0.05 2 836 157 129 LEU HD2 H 0.97 0.05 2 837 157 129 LEU CA C 58.1 0.50 1 838 157 129 LEU CB C 40.7 0.50 1 839 157 129 LEU CG C 27.0 0.50 1 840 157 129 LEU CD1 C 25.1 0.50 2 841 157 129 LEU CD2 C 24.0 0.50 2 842 157 129 LEU N N 118.638 0.50 1 843 158 130 GLU H H 7.606 0.05 1 844 158 130 GLU HA H 3.96 0.05 1 845 158 130 GLU CA C 58.2 0.50 1 846 158 130 GLU CB C 27.1 0.50 1 847 158 130 GLU CG C 35.1 0.50 1 848 158 130 GLU N N 119.4 0.50 1 849 159 131 ILE H H 8.285 0.05 1 850 159 131 ILE HA H 3.47 0.05 1 851 159 131 ILE HB H 1.97 0.05 1 852 159 131 ILE HG2 H 1.12 0.05 1 853 159 131 ILE HD1 H 0.72 0.05 1 854 159 131 ILE CA C 66.0 0.50 1 855 159 131 ILE CB C 38.5 0.50 1 856 159 131 ILE CG1 C 29.8 0.50 1 857 159 131 ILE CG2 C 17.2 0.50 1 858 159 131 ILE CD1 C 14.2 0.50 1 859 159 131 ILE N N 122.226 0.50 1 860 160 132 ALA H H 9.171 0.05 1 861 160 132 ALA HA H 3.9 0.05 1 862 160 132 ALA HB H 1.38 0.05 1 863 160 132 ALA CA C 55.0 0.50 1 864 160 132 ALA CB C 17.9 0.50 1 865 160 132 ALA N N 121.722 0.50 1 866 161 133 LYS H H 7.661 0.05 1 867 161 133 LYS HA H 3.87 0.05 1 868 161 133 LYS HB3 H 2.01 0.05 2 869 161 133 LYS CA C 59.5 0.50 1 870 161 133 LYS CB C 31.6 0.50 1 871 161 133 LYS CG C 24.5 0.50 1 872 161 133 LYS N N 117.72 0.50 1 873 162 134 ILE H H 7.587 0.05 1 874 162 134 ILE HA H 3.71 0.05 1 875 162 134 ILE HG2 H 0.79 0.05 1 876 162 134 ILE HD1 H 0.77 0.05 1 877 162 134 ILE CA C 65.1 0.50 1 878 162 134 ILE CB C 38.1 0.50 1 879 162 134 ILE CG1 C 28.6 0.50 1 880 162 134 ILE CG2 C 17.3 0.50 1 881 162 134 ILE CD1 C 14.8 0.50 1 882 162 134 ILE N N 122.241 0.50 1 883 163 135 MET H H 8.581 0.05 1 884 163 135 MET HA H 3.79 0.05 1 885 163 135 MET CA C 60.2 0.50 1 886 163 135 MET CB C 32.2 0.50 1 887 163 135 MET N N 120.758 0.50 1 888 164 136 LYS H H 9.221 0.05 1 889 164 136 LYS HA H 3.75 0.05 1 890 164 136 LYS HB3 H 1.98 0.05 2 891 164 136 LYS CA C 60.3 0.50 1 892 164 136 LYS CB C 31.8 0.50 1 893 164 136 LYS N N 118.723 0.50 1 894 165 137 THR H H 8.336 0.05 1 895 165 137 THR HA H 4.27 0.05 1 896 165 137 THR HB H 3.96 0.05 1 897 165 137 THR HG2 H 1.27 0.05 1 898 165 137 THR CA C 66.4 0.50 1 899 165 137 THR CB C 68.2 0.50 1 900 165 137 THR CG2 C 21.4 0.50 1 901 165 137 THR N N 115.639 0.50 1 902 166 138 LYS H H 7.357 0.05 1 903 166 138 LYS HA H 4.17 0.05 1 904 166 138 LYS CA C 58.8 0.50 1 905 166 138 LYS CB C 30.6 0.50 1 906 166 138 LYS N N 121.525 0.50 1 907 167 139 LEU H H 8.09 0.05 1 908 167 139 LEU HA H 3.89 0.05 1 909 167 139 LEU CA C 58.1 0.50 1 910 167 139 LEU CB C 42.0 0.50 1 911 167 139 LEU N N 117.6 0.50 1 912 168 140 GLN H H 8.793 0.05 1 913 168 140 GLN HA H 4.11 0.05 1 914 168 140 GLN HE22 H 6.72 0.05 2 915 168 140 GLN CA C 58.3 0.50 1 916 168 140 GLN CB C 27.6 0.50 1 917 168 140 GLN CG C 33.8 0.50 1 918 168 140 GLN N N 117.484 0.50 1 919 168 140 GLN NE2 N 110.9 0.50 1 920 169 141 ARG H H 8.051 0.05 1 921 169 141 ARG HA H 4.23 0.05 1 922 169 141 ARG CA C 59.4 0.50 1 923 169 141 ARG CB C 29.1 0.50 1 924 169 141 ARG N N 121.344 0.50 1 925 170 142 VAL H H 7.911 0.05 1 926 170 142 VAL HA H 3.76 0.05 1 927 170 142 VAL HG1 H 1.24 0.05 2 928 170 142 VAL HG2 H 0.99 0.05 2 929 170 142 VAL CA C 66.3 0.50 1 930 170 142 VAL CB C 31.6 0.50 1 931 170 142 VAL CG1 C 22.9 0.50 2 932 170 142 VAL CG2 C 21.9 0.50 2 933 170 142 VAL N N 120.397 0.50 1 934 171 143 HIS H H 9.281 0.05 1 935 171 143 HIS HA H 4.01 0.05 1 936 171 143 HIS CA C 60.3 0.50 1 937 171 143 HIS CB C 29.6 0.50 1 938 171 143 HIS N N 122.97 0.50 1 939 172 144 THR H H 8.977 0.05 1 940 172 144 THR HA H 4.36 0.05 1 941 172 144 THR CA C 67.1 0.50 1 942 172 144 THR CB C 68.6 0.50 1 943 172 144 THR N N 115.729 0.50 1 944 173 145 LYS H H 7.959 0.05 1 945 173 145 LYS HA H 4.2 0.05 1 946 173 145 LYS CA C 59.5 0.50 1 947 173 145 LYS CB C 32.1 0.50 1 948 173 145 LYS N N 119.978 0.50 1 949 174 146 ASN H H 7.64 0.05 1 950 174 146 ASN HA H 4.45 0.05 1 951 174 146 ASN HB3 H 2.52 0.05 2 952 174 146 ASN CA C 57.5 0.50 1 953 174 146 ASN CB C 40.0 0.50 1 954 174 146 ASN N N 116.606 0.50 1 955 175 147 TYR H H 9.079 0.05 1 956 175 147 TYR HA H 4.03 0.05 1 957 175 147 TYR HB2 H 2.83 0.05 2 958 175 147 TYR HB3 H 3.12 0.05 2 959 175 147 TYR CA C 61.1 0.50 1 960 175 147 TYR CB C 38.0 0.50 1 961 175 147 TYR N N 122.163 0.50 1 962 176 148 CYS H H 8.799 0.05 1 963 176 148 CYS HA H 4.74 0.05 1 964 176 148 CYS HB2 H 3.13 0.05 2 965 176 148 CYS CA C 58.8 0.50 1 966 176 148 CYS CB C 39.3 0.50 1 967 176 148 CYS N N 116.655 0.50 1 968 177 149 ALA H H 7.337 0.05 1 969 177 149 ALA HA H 4.08 0.05 1 970 177 149 ALA HB H 1.52 0.05 1 971 177 149 ALA CA C 54.5 0.50 1 972 177 149 ALA CB C 18.8 0.50 1 973 177 149 ALA N N 120.661 0.50 1 974 178 150 LEU H H 8.075 0.05 1 975 178 150 LEU HA H 3.85 0.05 1 976 178 150 LEU HB2 H 1.57 0.05 2 977 178 150 LEU HB3 H 1.87 0.05 2 978 178 150 LEU HG H 1.44 0.05 1 979 178 150 LEU HD1 H 0.87 0.05 2 980 178 150 LEU HD2 H 0.91 0.05 2 981 178 150 LEU CA C 57.5 0.50 1 982 178 150 LEU CB C 41.7 0.50 1 983 178 150 LEU CG C 27.1 0.50 1 984 178 150 LEU CD1 C 25.6 0.50 2 985 178 150 LEU CD2 C 23.3 0.50 2 986 178 150 LEU N N 120.82 0.50 1 987 179 151 GLU H H 8.066 0.05 1 988 179 151 GLU HA H 3.51 0.05 1 989 179 151 GLU CA C 57.9 0.50 1 990 179 151 GLU CB C 26.4 0.50 1 991 179 151 GLU N N 117.503 0.50 1 992 180 152 LYS H H 7.424 0.05 1 993 180 152 LYS HA H 4.27 0.05 1 994 180 152 LYS HB3 H 1.88 0.05 2 995 180 152 LYS CA C 57.3 0.50 1 996 180 152 LYS CB C 32.0 0.50 1 997 180 152 LYS CG C 25.6 0.50 1 998 180 152 LYS CD C 29.3 0.50 1 999 180 152 LYS N N 118.823 0.50 1 1000 181 153 LYS H H 7.381 0.05 1 1001 181 153 LYS HA H 3.99 0.05 1 1002 181 153 LYS HB3 H 1.93 0.05 2 1003 181 153 LYS CA C 57.9 0.50 1 1004 181 153 LYS CB C 31.6 0.50 1 1005 181 153 LYS CG C 24.5 0.50 1 1006 181 153 LYS CD C 28.9 0.50 1 1007 181 153 LYS N N 118.403 0.50 1 1008 182 154 LYS H H 7.374 0.05 1 1009 182 154 LYS HA H 4.03 0.05 1 1010 182 154 LYS HB3 H 1.73 0.05 2 1011 182 154 LYS CA C 57.9 0.50 1 1012 182 154 LYS CB C 32.7 0.50 1 1013 182 154 LYS CG C 25.0 0.50 1 1014 182 154 LYS N N 116.472 0.50 1 1015 183 155 ASN H H 7.643 0.05 1 1016 183 155 ASN HA H 5.05 0.05 1 1017 183 155 ASN HB2 H 2.82 0.05 2 1018 183 155 ASN HB3 H 2.98 0.05 2 1019 183 155 ASN CA C 49.7 0.50 1 1020 183 155 ASN CB C 39.1 0.50 1 1021 183 155 ASN N N 114.082 0.50 1 1022 184 156 PRO HA H 4.6 0.05 1 1023 184 156 PRO HB2 H 2.45 0.05 2 1024 184 156 PRO CA C 64.1 0.50 1 1025 184 156 PRO CB C 31.9 0.50 1 1026 185 157 ASN H H 7.866 0.05 1 1027 185 157 ASN HA H 4.82 0.05 1 1028 185 157 ASN HB2 H 2.68 0.05 2 1029 185 157 ASN HB3 H 2.97 0.05 2 1030 185 157 ASN CA C 52.6 0.50 1 1031 185 157 ASN CB C 38.3 0.50 1 1032 185 157 ASN N N 114.209 0.50 1 1033 186 158 PHE H H 8.035 0.05 1 1034 186 158 PHE HA H 4.35 0.05 1 1035 186 158 PHE HB2 H 2.86 0.05 2 1036 186 158 PHE HB3 H 3.35 0.05 2 1037 186 158 PHE CA C 58.8 0.50 1 1038 186 158 PHE CB C 39.6 0.50 1 1039 186 158 PHE N N 122.429 0.50 1 1040 187 159 THR H H 7.687 0.05 1 1041 187 159 THR HA H 4.11 0.05 1 1042 187 159 THR HB H 3.86 0.05 1 1043 187 159 THR HG2 H 1.02 0.05 1 1044 187 159 THR CA C 59.7 0.50 1 1045 187 159 THR CB C 70.4 0.50 1 1046 187 159 THR CG2 C 20.4 0.50 1 1047 187 159 THR N N 120.308 0.50 1 1048 188 160 ASP H H 7.732 0.05 1 1049 188 160 ASP HA H 4.38 0.05 1 1050 188 160 ASP HB2 H 2.47 0.05 2 1051 188 160 ASP HB3 H 2.64 0.05 2 1052 188 160 ASP CA C 54.0 0.50 1 1053 188 160 ASP CB C 45.0 0.50 1 1054 188 160 ASP N N 122.01 0.50 1 1055 189 161 GLU H H 9.002 0.05 1 1056 189 161 GLU HA H 4.0 0.05 1 1057 189 161 GLU HB2 H 2.07 0.05 2 1058 189 161 GLU HB3 H 2.34 0.05 2 1059 189 161 GLU CA C 58.9 0.50 1 1060 189 161 GLU CB C 28.9 0.50 1 1061 189 161 GLU CG C 35.6 0.50 1 1062 189 161 GLU N N 127.772 0.50 1 1063 190 162 LYS H H 9.144 0.05 1 1064 190 162 LYS HA H 4.23 0.05 1 1065 190 162 LYS HB2 H 1.87 0.05 2 1066 190 162 LYS HB3 H 1.93 0.05 2 1067 190 162 LYS CA C 57.6 0.50 1 1068 190 162 LYS CB C 31.9 0.50 1 1069 190 162 LYS CG C 24.6 0.50 1 1070 190 162 LYS N N 117.753 0.50 1 1071 191 163 CYS H H 7.999 0.05 1 1072 191 163 CYS HA H 4.97 0.05 1 1073 191 163 CYS HB2 H 3.49 0.05 2 1074 191 163 CYS HB3 H 2.9 0.05 2 1075 191 163 CYS CA C 52.8 0.50 1 1076 191 163 CYS CB C 38.3 0.50 1 1077 191 163 CYS N N 115.894 0.50 1 1078 192 164 LYS H H 7.718 0.05 1 1079 192 164 LYS HA H 4.29 0.05 1 1080 192 164 LYS HB2 H 1.43 0.05 2 1081 192 164 LYS HB3 H 1.83 0.05 2 1082 192 164 LYS CA C 56.6 0.50 1 1083 192 164 LYS CB C 32.6 0.50 1 1084 192 164 LYS CG C 24.4 0.50 1 1085 192 164 LYS CD C 28.7 0.50 1 1086 192 164 LYS N N 121.894 0.50 1 1087 193 165 ASN H H 8.497 0.05 1 1088 193 165 ASN HA H 4.79 0.05 1 1089 193 165 ASN HB2 H 2.68 0.05 2 1090 193 165 ASN HB3 H 2.94 0.05 2 1091 193 165 ASN CA C 53.0 0.50 1 1092 193 165 ASN CB C 38.5 0.50 1 1093 193 165 ASN N N 118.976 0.50 1 1094 194 166 ASN H H 7.913 0.05 1 1095 194 166 ASN HA H 4.48 0.05 1 1096 194 166 ASN HB2 H 2.64 0.05 2 1097 194 166 ASN HB3 H 2.71 0.05 2 1098 194 166 ASN CA C 54.6 0.50 1 1099 194 166 ASN CB C 40.2 0.50 1 1100 194 166 ASN N N 124.0 0.50 1 stop_ save_