data_27979 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shifts of Bordetella pertussis effector BteA ; _BMRB_accession_number 27979 _BMRB_flat_file_name bmr27979.str _Entry_type original _Submission_date 2019-07-18 _Accession_date 2019-07-18 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Chemical shifts of Bordetella pertussis effector BteA' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yahalom Adi . . 2 Shaked Hadassa . . 3 Chill Jordan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 101 "13C chemical shifts" 283 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-03-31 update BMRB 'update entry citation' 2019-07-30 original author 'original release' stop_ _Original_release_date 2019-07-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and membrane-targeting of a Bordetella pertussis effector N-terminal domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31487494 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yahalom Adi . . 2 Davidov Geula . . 3 Kolusheva Sofiya . . 4 Shaked Hadassa . . 5 Barber-Zucker Shiran . . 6 Zarivach Raz . . 7 Chill Jordan . . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta Biomembr.' _Journal_volume 1861 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 183054 _Page_last 183054 _Year 2019 _Details . loop_ _Keyword Bordetella BteA Effector T3SS stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name BteA131 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BteA131 $BteA131 stop_ _System_molecular_weight 14940.66 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'cytotoxic effector' stop_ _Database_query_date . _Details 'BteA residues 1-131, N-terminal fragment of cytotoxic effector' save_ ######################## # Monomeric polymers # ######################## save_BteA131 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common BteA131 _Molecular_mass 14940.66 _Mol_thiol_state 'not present' loop_ _Biological_function 'cytotoxic effector' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 134 _Mol_residue_sequence ; GSHMLSSNVNPVVGLSYRPL PETPPSGQAAAHPSMRLLEP NNDEFVRSVASPRLHHSSEA LREVKHDVRQFQASGDRSLQ QLRDLEVALNHWEASQPREF AKRGGMVAELRTAIDAYKQQ LHEQAPSHANLDVK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 0 HIS 4 1 MET 5 2 LEU 6 3 SER 7 4 SER 8 5 ASN 9 6 VAL 10 7 ASN 11 8 PRO 12 9 VAL 13 10 VAL 14 11 GLY 15 12 LEU 16 13 SER 17 14 TYR 18 15 ARG 19 16 PRO 20 17 LEU 21 18 PRO 22 19 GLU 23 20 THR 24 21 PRO 25 22 PRO 26 23 SER 27 24 GLY 28 25 GLN 29 26 ALA 30 27 ALA 31 28 ALA 32 29 HIS 33 30 PRO 34 31 SER 35 32 MET 36 33 ARG 37 34 LEU 38 35 LEU 39 36 GLU 40 37 PRO 41 38 ASN 42 39 ASN 43 40 ASP 44 41 GLU 45 42 PHE 46 43 VAL 47 44 ARG 48 45 SER 49 46 VAL 50 47 ALA 51 48 SER 52 49 PRO 53 50 ARG 54 51 LEU 55 52 HIS 56 53 HIS 57 54 SER 58 55 SER 59 56 GLU 60 57 ALA 61 58 LEU 62 59 ARG 63 60 GLU 64 61 VAL 65 62 LYS 66 63 HIS 67 64 ASP 68 65 VAL 69 66 ARG 70 67 GLN 71 68 PHE 72 69 GLN 73 70 ALA 74 71 SER 75 72 GLY 76 73 ASP 77 74 ARG 78 75 SER 79 76 LEU 80 77 GLN 81 78 GLN 82 79 LEU 83 80 ARG 84 81 ASP 85 82 LEU 86 83 GLU 87 84 VAL 88 85 ALA 89 86 LEU 90 87 ASN 91 88 HIS 92 89 TRP 93 90 GLU 94 91 ALA 95 92 SER 96 93 GLN 97 94 PRO 98 95 ARG 99 96 GLU 100 97 PHE 101 98 ALA 102 99 LYS 103 100 ARG 104 101 GLY 105 102 GLY 106 103 MET 107 104 VAL 108 105 ALA 109 106 GLU 110 107 LEU 111 108 ARG 112 109 THR 113 110 ALA 114 111 ILE 115 112 ASP 116 113 ALA 117 114 TYR 118 115 LYS 119 116 GLN 120 117 GLN 121 118 LEU 122 119 HIS 123 120 GLU 124 121 GLN 125 122 ALA 126 123 PRO 127 124 SER 128 125 HIS 129 126 ALA 130 127 ASN 131 128 LEU 132 129 ASP 133 130 VAL 134 131 LYS 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 $BteA131 'Bordetella pertussis' 520 Bacteria . Bordetella pertussis 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 $BteA131 'recombinant technology' . Escherichia coli . pET11a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BteA131 . mM . bis-Tris 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 'peak picking' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 700 _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_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.2 0.01 M pH 6.3 0.1 pH pressure 1 . atm temperature 283 0.2 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 carbons' ppm 0.0 internal indirect . . . 0.25144953 water H 1 protons ppm 4.91 internal direct . . . 1 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $TOPSPIN stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name BteA131 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 5 LEU H H 8.22 0.01 . 2 2 5 LEU C C 177.5 0.1 . 3 2 5 LEU CA C 55.3 0.1 . 4 2 5 LEU CB C 42.1 0.1 . 5 2 5 LEU N N 124.2 0.1 . 6 3 6 SER H H 8.18 0.01 . 7 3 6 SER C C 174.6 0.1 . 8 3 6 SER CA C 58.3 0.1 . 9 3 6 SER CB C 63.6 0.1 . 10 3 6 SER N N 117 0.1 . 11 4 7 SER H H 8.17 0.01 . 12 4 7 SER CA C 58.3 0.1 . 13 4 7 SER CB C 63.6 0.1 . 14 4 7 SER N N 117.8 0.1 . 15 6 9 VAL H H 7.77 0.01 . 16 6 9 VAL C C 174.6 0.1 . 17 6 9 VAL CA C 61.8 0.1 . 18 6 9 VAL CB C 32.6 0.1 . 19 6 9 VAL N N 119.7 0.1 . 20 7 10 ASN H H 8.32 0.01 . 21 7 10 ASN CA C 50.9 0.1 . 22 7 10 ASN CB C 38.6 0.1 . 23 7 10 ASN N N 123.8 0.1 . 24 9 12 VAL H H 8.01 0.01 . 25 9 12 VAL C C 176.5 0.1 . 26 9 12 VAL CA C 62.6 0.1 . 27 9 12 VAL CB C 32.1 0.1 . 28 9 12 VAL N N 120.6 0.1 . 29 10 13 VAL H H 8.04 0.01 . 30 10 13 VAL C C 176.6 0.1 . 31 10 13 VAL CA C 62.2 0.1 . 32 10 13 VAL CB C 32.5 0.1 . 33 10 13 VAL N N 124.9 0.1 . 34 11 14 GLY H H 8.27 0.01 . 35 11 14 GLY C C 174.1 0.1 . 36 11 14 GLY CA C 45.1 0.1 . 37 11 14 GLY N N 112.7 0.1 . 38 12 15 LEU H H 7.96 0.01 . 39 12 15 LEU C C 177.5 0.1 . 40 12 15 LEU CA C 55.2 0.1 . 41 12 15 LEU CB C 42.1 0.1 . 42 12 15 LEU N N 122.1 0.1 . 43 13 16 SER H H 8.15 0.01 . 44 13 16 SER C C 173.9 0.1 . 45 13 16 SER CA C 58.3 0.1 . 46 13 16 SER CB C 63.6 0.1 . 47 13 16 SER N N 116.7 0.1 . 48 14 17 TYR H H 7.96 0.01 . 49 14 17 TYR C C 175 0.1 . 50 14 17 TYR CA C 57.9 0.1 . 51 14 17 TYR CB C 38.6 0.1 . 52 14 17 TYR N N 122.8 0.1 . 53 15 18 ARG H H 7.9 0.01 . 54 15 18 ARG CA C 53 0.1 . 55 15 18 ARG CB C 30.3 0.1 . 56 15 18 ARG N N 125.5 0.1 . 57 17 20 LEU H H 8.15 0.01 . 58 17 20 LEU CA C 53.1 0.1 . 59 17 20 LEU CB C 41.3 0.1 . 60 17 20 LEU N N 124 0.1 . 61 19 22 GLU H H 8.33 0.01 . 62 19 22 GLU C C 175.6 0.1 . 63 19 22 GLU CA C 56.6 0.1 . 64 19 22 GLU CB C 30.3 0.1 . 65 19 22 GLU N N 122.1 0.1 . 66 20 23 THR H H 7.91 0.01 . 67 20 23 THR CA C 58.3 0.1 . 68 20 23 THR CB C 71 0.1 . 69 20 23 THR N N 116.3 0.1 . 70 23 26 SER H H 8.25 0.01 . 71 23 26 SER C C 175.4 0.1 . 72 23 26 SER CA C 58.3 0.1 . 73 23 26 SER CB C 64 0.1 . 74 23 26 SER N N 116.1 0.1 . 75 24 27 GLY H H 8.35 0.01 . 76 24 27 GLY C C 174.3 0.1 . 77 24 27 GLY CA C 45.1 0.1 . 78 24 27 GLY N N 111.2 0.1 . 79 25 28 GLN H H 8.1 0.01 . 80 25 28 GLN C C 175.6 0.1 . 81 25 28 GLN CA C 55.6 0.1 . 82 25 28 GLN CB C 29.4 0.1 . 83 25 28 GLN N N 120.6 0.1 . 84 26 29 ALA H H 8.02 0.01 . 85 26 29 ALA CA C 50.4 0.1 . 86 26 29 ALA CB C 17.6 0.1 . 87 26 29 ALA N N 126.6 0.1 . 88 28 31 ALA H H 8.02 0.01 . 89 28 31 ALA CA C 52.2 0.1 . 90 28 31 ALA CB C 18.9 0.1 . 91 28 31 ALA N N 123.4 0.1 . 92 31 34 SER H H 9.48 0.01 . 93 31 34 SER C C 176.4 0.1 . 94 31 34 SER CA C 61.3 0.1 . 95 31 34 SER CB C 62.6 0.1 . 96 31 34 SER N N 118.2 0.1 . 97 32 35 MET H H 8.05 0.01 . 98 32 35 MET C C 178.3 0.1 . 99 32 35 MET CA C 59.1 0.1 . 100 32 35 MET CB C 32.6 0.1 . 101 32 35 MET N N 119.8 0.1 . 102 33 36 ARG H H 7.44 0.01 . 103 33 36 ARG C C 176 0.1 . 104 33 36 ARG CA C 57.4 0.1 . 105 33 36 ARG CB C 27.2 0.1 . 106 33 36 ARG N N 121.9 0.1 . 107 34 37 LEU H H 7.55 0.01 . 108 34 37 LEU C C 178.4 0.1 . 109 34 37 LEU CA C 55.6 0.1 . 110 34 37 LEU CB C 42.6 0.1 . 111 34 37 LEU N N 116.7 0.1 . 112 35 38 LEU H H 7.16 0.01 . 113 35 38 LEU CA C 53.1 0.1 . 114 35 38 LEU CB C 41.6 0.1 . 115 35 38 LEU N N 113.7 0.1 . 116 38 41 ASN H H 8.36 0.01 . 117 38 41 ASN C C 174 0.1 . 118 38 41 ASN CA C 53.1 0.1 . 119 38 41 ASN CB C 37.8 0.1 . 120 38 41 ASN N N 113.7 0.1 . 121 39 42 ASN H H 7.3 0.01 . 122 39 42 ASN C C 174.7 0.1 . 123 39 42 ASN CA C 54.4 0.1 . 124 39 42 ASN CB C 42.1 0.1 . 125 39 42 ASN N N 121 0.1 . 126 40 43 ASP H H 8.57 0.01 . 127 40 43 ASP C C 176.6 0.1 . 128 40 43 ASP CA C 52.6 0.1 . 129 40 43 ASP CB C 41.2 0.1 . 130 40 43 ASP N N 126.4 0.1 . 131 41 44 GLU H H 8.21 0.01 . 132 41 44 GLU C C 179.9 0.1 . 133 41 44 GLU CA C 60.5 0.1 . 134 41 44 GLU CB C 30.3 0.1 . 135 41 44 GLU N N 118.7 0.1 . 136 42 45 PHE H H 8.78 0.01 . 137 42 45 PHE C C 179.3 0.1 . 138 42 45 PHE CA C 62.6 0.1 . 139 42 45 PHE CB C 37.8 0.1 . 140 42 45 PHE N N 118.5 0.1 . 141 43 46 VAL H H 9.59 0.01 . 142 43 46 VAL CA C 66.6 0.1 . 143 43 46 VAL CB C 30.6 0.1 . 144 43 46 VAL N N 121.2 0.1 . 145 45 48 SER H H 7.73 0.01 . 146 45 48 SER C C 175.4 0.1 . 147 45 48 SER CA C 61.4 0.1 . 148 45 48 SER CB C 62.6 0.1 . 149 45 48 SER N N 117.2 0.1 . 150 46 49 VAL H H 6.65 0.01 . 151 46 49 VAL C C 175.4 0.1 . 152 46 49 VAL CA C 60.1 0.1 . 153 46 49 VAL CB C 30.8 0.1 . 154 46 49 VAL N N 112.3 0.1 . 155 47 50 ALA H H 7.02 0.01 . 156 47 50 ALA C C 177.9 0.1 . 157 47 50 ALA CA C 52.2 0.1 . 158 47 50 ALA CB C 19.4 0.1 . 159 47 50 ALA N N 125.8 0.1 . 160 48 51 SER H H 7.12 0.01 . 161 48 51 SER CA C 59.1 0.1 . 162 48 51 SER CB C 63.6 0.1 . 163 48 51 SER N N 114 0.1 . 164 55 58 SER H H 10.01 0.01 . 165 55 58 SER C C 175.4 0.1 . 166 55 58 SER CA C 59.1 0.1 . 167 55 58 SER CB C 63.7 0.1 . 168 55 58 SER N N 122.3 0.1 . 169 56 59 GLU H H 8.89 0.01 . 170 56 59 GLU C C 179.1 0.1 . 171 56 59 GLU CA C 59.1 0.1 . 172 56 59 GLU CB C 28.6 0.1 . 173 56 59 GLU N N 122.7 0.1 . 174 57 60 ALA H H 8.32 0.01 . 175 57 60 ALA C C 180.3 0.1 . 176 57 60 ALA CA C 54.8 0.1 . 177 57 60 ALA CB C 18.1 0.1 . 178 57 60 ALA N N 121.5 0.1 . 179 58 61 LEU H H 8.02 0.01 . 180 58 61 LEU C C 178.3 0.1 . 181 58 61 LEU CA C 57 0.1 . 182 58 61 LEU CB C 39.6 0.1 . 183 58 61 LEU N N 122.8 0.1 . 184 59 62 ARG H H 8.04 0.01 . 185 59 62 ARG C C 179.5 0.1 . 186 59 62 ARG CA C 60.9 0.1 . 187 59 62 ARG CB C 29.1 0.1 . 188 59 62 ARG N N 121.5 0.1 . 189 60 63 GLU H H 7.93 0.01 . 190 60 63 GLU C C 178.4 0.1 . 191 60 63 GLU CA C 59.1 0.1 . 192 60 63 GLU CB C 28.6 0.1 . 193 60 63 GLU N N 121 0.1 . 194 61 64 VAL H H 7.29 0.01 . 195 61 64 VAL C C 177.6 0.1 . 196 61 64 VAL CA C 67.1 0.1 . 197 61 64 VAL CB C 31.2 0.1 . 198 61 64 VAL N N 119.7 0.1 . 199 62 65 LYS H H 8.15 0.01 . 200 62 65 LYS C C 178.4 0.1 . 201 62 65 LYS CA C 60.9 0.1 . 202 62 65 LYS CB C 31.6 0.1 . 203 62 65 LYS N N 117.2 0.1 . 204 63 66 HIS H H 8.08 0.01 . 205 63 66 HIS C C 177.2 0.1 . 206 63 66 HIS CA C 59.3 0.1 . 207 63 66 HIS CB C 29.1 0.1 . 208 63 66 HIS N N 118.3 0.1 . 209 64 67 ASP H H 8.52 0.01 . 210 64 67 ASP C C 179.3 0.1 . 211 64 67 ASP CA C 56.1 0.1 . 212 64 67 ASP CB C 37.8 0.1 . 213 64 67 ASP N N 120.4 0.1 . 214 65 68 VAL H H 8.44 0.01 . 215 65 68 VAL C C 177.1 0.1 . 216 65 68 VAL CA C 67.5 0.1 . 217 65 68 VAL CB C 31.6 0.1 . 218 65 68 VAL N N 124 0.1 . 219 66 69 ARG H H 7.74 0.01 . 220 66 69 ARG C C 179.4 0.1 . 221 66 69 ARG CA C 58.8 0.1 . 222 66 69 ARG CB C 29.1 0.1 . 223 66 69 ARG N N 119.1 0.1 . 224 67 70 GLN H H 8.47 0.01 . 225 67 70 GLN C C 178.2 0.1 . 226 67 70 GLN CA C 58.3 0.1 . 227 67 70 GLN CB C 29 0.1 . 228 67 70 GLN N N 118 0.1 . 229 68 71 PHE H H 7.48 0.01 . 230 68 71 PHE CA C 61.8 0.1 . 231 68 71 PHE CB C 39.1 0.1 . 232 68 71 PHE N N 120 0.1 . 233 75 78 SER H H 7.85 0.01 . 234 75 78 SER CA C 56.2 0.1 . 235 75 78 SER CB C 67.2 0.1 . 236 75 78 SER N N 114.6 0.1 . 237 77 80 GLN H H 8.38 0.01 . 238 77 80 GLN C C 177.6 0.1 . 239 77 80 GLN CA C 58.8 0.1 . 240 77 80 GLN CB C 27.7 0.1 . 241 77 80 GLN N N 119.7 0.1 . 242 78 81 GLN H H 7.57 0.01 . 243 78 81 GLN C C 180.5 0.1 . 244 78 81 GLN CA C 58.8 0.1 . 245 78 81 GLN CB C 29.4 0.1 . 246 78 81 GLN N N 117.8 0.1 . 247 79 82 LEU H H 7.32 0.01 . 248 79 82 LEU C C 178.1 0.1 . 249 79 82 LEU CA C 57.4 0.1 . 250 79 82 LEU CB C 41.7 0.1 . 251 79 82 LEU N N 120.6 0.1 . 252 80 83 ARG H H 8.27 0.01 . 253 80 83 ARG C C 179 0.1 . 254 80 83 ARG CA C 58.9 0.1 . 255 80 83 ARG CB C 28.9 0.1 . 256 80 83 ARG N N 121.2 0.1 . 257 81 84 ASP H H 8.43 0.01 . 258 81 84 ASP C C 179 0.1 . 259 81 84 ASP CA C 57.4 0.1 . 260 81 84 ASP CB C 39.1 0.1 . 261 81 84 ASP N N 119.8 0.1 . 262 82 85 LEU H H 7.35 0.01 . 263 82 85 LEU C C 177.4 0.1 . 264 82 85 LEU CA C 57.4 0.1 . 265 82 85 LEU CB C 40.8 0.1 . 266 82 85 LEU N N 121.9 0.1 . 267 83 86 GLU H H 8.25 0.01 . 268 83 86 GLU C C 179.2 0.1 . 269 83 86 GLU CA C 60.1 0.1 . 270 83 86 GLU CB C 30 0.1 . 271 83 86 GLU N N 121 0.1 . 272 84 87 VAL H H 8.25 0.01 . 273 84 87 VAL C C 178.9 0.1 . 274 84 87 VAL CA C 66.6 0.1 . 275 84 87 VAL CB C 31.2 0.1 . 276 84 87 VAL N N 120 0.1 . 277 85 88 ALA H H 8.29 0.01 . 278 85 88 ALA C C 182.2 0.1 . 279 85 88 ALA CA C 55.3 0.1 . 280 85 88 ALA CB C 17.6 0.1 . 281 85 88 ALA N N 124.7 0.1 . 282 86 89 LEU H H 8.86 0.01 . 283 86 89 LEU C C 178.3 0.1 . 284 86 89 LEU CA C 58.8 0.1 . 285 86 89 LEU CB C 42.6 0.1 . 286 86 89 LEU N N 122.7 0.1 . 287 87 90 ASN H H 8.22 0.01 . 288 87 90 ASN C C 178.4 0.1 . 289 87 90 ASN CA C 55.6 0.1 . 290 87 90 ASN CB C 36.4 0.1 . 291 87 90 ASN N N 119.3 0.1 . 292 88 91 HIS H H 8.8 0.01 . 293 88 91 HIS C C 178.5 0.1 . 294 88 91 HIS CA C 58.3 0.1 . 295 88 91 HIS CB C 29.1 0.1 . 296 88 91 HIS N N 120.2 0.1 . 297 89 92 TRP H H 8.5 0.01 . 298 89 92 TRP C C 174.8 0.1 . 299 89 92 TRP CA C 60 0.1 . 300 89 92 TRP CB C 27.7 0.1 . 301 89 92 TRP N N 125.3 0.1 . 302 90 93 GLU H H 7.76 0.01 . 303 90 93 GLU C C 177.3 0.1 . 304 90 93 GLU CA C 59.2 0.1 . 305 90 93 GLU CB C 29.1 0.1 . 306 90 93 GLU N N 117.8 0.1 . 307 91 94 ALA H H 7.4 0.01 . 308 91 94 ALA C C 179.9 0.1 . 309 91 94 ALA CA C 53.9 0.1 . 310 91 94 ALA CB C 18.9 0.1 . 311 91 94 ALA N N 115.3 0.1 . 312 92 95 SER H H 7.97 0.01 . 313 92 95 SER C C 175.3 0.1 . 314 92 95 SER CA C 59.6 0.1 . 315 92 95 SER CB C 64.9 0.1 . 316 92 95 SER N N 111.2 0.1 . 317 93 96 GLN H H 7.74 0.01 . 318 93 96 GLN CA C 52.1 0.1 . 319 93 96 GLN CB C 27.3 0.1 . 320 93 96 GLN N N 121 0.1 . 321 95 98 ARG H H 7.96 0.01 . 322 95 98 ARG C C 178.6 0.1 . 323 95 98 ARG CA C 59.1 0.1 . 324 95 98 ARG CB C 29.1 0.1 . 325 95 98 ARG N N 118.5 0.1 . 326 96 99 GLU H H 7.94 0.01 . 327 96 99 GLU C C 178.8 0.1 . 328 96 99 GLU CA C 59.1 0.1 . 329 96 99 GLU CB C 32.2 0.1 . 330 96 99 GLU N N 123.6 0.1 . 331 97 100 PHE H H 8.95 0.01 . 332 97 100 PHE C C 178.1 0.1 . 333 97 100 PHE CA C 61.4 0.1 . 334 97 100 PHE CB C 39.1 0.1 . 335 97 100 PHE N N 121.2 0.1 . 336 98 101 ALA H H 7.96 0.01 . 337 98 101 ALA C C 179.8 0.1 . 338 98 101 ALA CA C 54.4 0.1 . 339 98 101 ALA CB C 17.6 0.1 . 340 98 101 ALA N N 121.5 0.1 . 341 99 102 LYS H H 7.4 0.01 . 342 99 102 LYS C C 179.1 0.1 . 343 99 102 LYS CA C 57.9 0.1 . 344 99 102 LYS CB C 33.2 0.1 . 345 99 102 LYS N N 115.3 0.1 . 346 100 103 ARG H H 8.39 0.01 . 347 100 103 ARG C C 176.5 0.1 . 348 100 103 ARG CA C 55.6 0.1 . 349 100 103 ARG CB C 31.6 0.1 . 350 100 103 ARG N N 114.8 0.1 . 351 101 104 GLY H H 7.74 0.01 . 352 101 104 GLY C C 176.4 0.1 . 353 101 104 GLY CA C 46.1 0.1 . 354 101 104 GLY N N 108.2 0.1 . 355 102 105 GLY H H 8.27 0.01 . 356 102 105 GLY C C 175.6 0.1 . 357 102 105 GLY CA C 47.4 0.1 . 358 102 105 GLY N N 111.4 0.1 . 359 103 106 MET H H 9.69 0.01 . 360 103 106 MET C C 177.1 0.1 . 361 103 106 MET CA C 55.9 0.1 . 362 103 106 MET CB C 34 0.1 . 363 103 106 MET N N 119.7 0.1 . 364 104 107 VAL H H 8.05 0.01 . 365 104 107 VAL C C 177 0.1 . 366 104 107 VAL CA C 67.5 0.1 . 367 104 107 VAL CB C 30.3 0.1 . 368 104 107 VAL N N 121.7 0.1 . 369 105 108 ALA H H 8.6 0.01 . 370 105 108 ALA C C 180.9 0.1 . 371 105 108 ALA CA C 56.1 0.1 . 372 105 108 ALA CB C 17.2 0.1 . 373 105 108 ALA N N 123.4 0.1 . 374 106 109 GLU H H 7.99 0.01 . 375 106 109 GLU C C 178.8 0.1 . 376 106 109 GLU CA C 59.6 0.1 . 377 106 109 GLU CB C 29 0.1 . 378 106 109 GLU N N 120.8 0.1 . 379 107 110 LEU H H 8.27 0.01 . 380 107 110 LEU C C 178.7 0.1 . 381 107 110 LEU CA C 57.9 0.1 . 382 107 110 LEU CB C 41.3 0.1 . 383 107 110 LEU N N 122.3 0.1 . 384 108 111 ARG H H 8.99 0.01 . 385 108 111 ARG C C 179.5 0.1 . 386 108 111 ARG CA C 60.9 0.1 . 387 108 111 ARG CB C 29.1 0.1 . 388 108 111 ARG N N 119.3 0.1 . 389 109 112 THR H H 7.85 0.01 . 390 109 112 THR C C 176.4 0.1 . 391 109 112 THR CA C 66.6 0.1 . 392 109 112 THR CB C 68.4 0.1 . 393 109 112 THR N N 119.3 0.1 . 394 110 113 ALA H H 8.11 0.01 . 395 110 113 ALA C C 179.6 0.1 . 396 110 113 ALA CA C 55.3 0.1 . 397 110 113 ALA CB C 18 0.1 . 398 110 113 ALA N N 127.2 0.1 . 399 111 114 ILE H H 8.55 0.01 . 400 111 114 ILE C C 177.8 0.1 . 401 111 114 ILE CA C 66.1 0.1 . 402 111 114 ILE CB C 37.8 0.1 . 403 111 114 ILE N N 119.7 0.1 . 404 112 115 ASP H H 7.65 0.01 . 405 112 115 ASP C C 178.7 0.1 . 406 112 115 ASP CA C 57.9 0.1 . 407 112 115 ASP CB C 40.4 0.1 . 408 112 115 ASP N N 119.7 0.1 . 409 113 116 ALA H H 7.87 0.01 . 410 113 116 ALA C C 181.4 0.1 . 411 113 116 ALA CA C 54.8 0.1 . 412 113 116 ALA CB C 17.2 0.1 . 413 113 116 ALA N N 123.2 0.1 . 414 114 117 TYR H H 8.72 0.01 . 415 114 117 TYR C C 179 0.1 . 416 114 117 TYR CA C 63.1 0.1 . 417 114 117 TYR CB C 38.6 0.1 . 418 114 117 TYR N N 120 0.1 . 419 115 118 LYS H H 8.64 0.01 . 420 115 118 LYS C C 179 0.1 . 421 115 118 LYS CA C 60.5 0.1 . 422 115 118 LYS CB C 32.1 0.1 . 423 115 118 LYS N N 120.4 0.1 . 424 116 119 GLN H H 7.48 0.01 . 425 116 119 GLN C C 178.2 0.1 . 426 116 119 GLN CA C 58.3 0.1 . 427 116 119 GLN CB C 27.7 0.1 . 428 116 119 GLN N N 116.8 0.1 . 429 117 120 GLN H H 7.57 0.01 . 430 117 120 GLN C C 177.8 0.1 . 431 117 120 GLN CA C 58.1 0.1 . 432 117 120 GLN CB C 29.1 0.1 . 433 117 120 GLN N N 118.9 0.1 . 434 118 121 LEU H H 7.94 0.01 . 435 118 121 LEU C C 178.3 0.1 . 436 118 121 LEU CA C 56.1 0.1 . 437 118 121 LEU CB C 41.6 0.1 . 438 118 121 LEU N N 119.3 0.1 . 439 119 122 HIS H H 7.91 0.01 . 440 119 122 HIS C C 175.9 0.1 . 441 119 122 HIS CA C 57.4 0.1 . 442 119 122 HIS CB C 29.1 0.1 . 443 119 122 HIS N N 118.2 0.1 . 444 120 123 GLU H H 8.07 0.01 . 445 120 123 GLU C C 178.7 0.1 . 446 120 123 GLU CA C 57 0.1 . 447 120 123 GLU CB C 29.4 0.1 . 448 120 123 GLU N N 120.6 0.1 . 449 121 124 GLN H H 8.02 0.01 . 450 121 124 GLN C C 175.9 0.1 . 451 121 124 GLN CA C 55.6 0.1 . 452 121 124 GLN CB C 29.4 0.1 . 453 121 124 GLN N N 120.2 0.1 . 454 122 125 ALA H H 8.22 0.01 . 455 122 125 ALA CA C 52.2 0.1 . 456 122 125 ALA CB C 18.9 0.1 . 457 122 125 ALA N N 125.7 0.1 . 458 124 127 SER H H 8.38 0.01 . 459 124 127 SER CA C 58.3 0.1 . 460 124 127 SER CB C 64 0.1 . 461 124 127 SER N N 117.2 0.1 . 462 127 130 ASN H H 8.33 0.01 . 463 127 130 ASN C C 175.2 0.1 . 464 127 130 ASN CA C 53.1 0.1 . 465 127 130 ASN CB C 38.2 0.1 . 466 127 130 ASN N N 118.3 0.1 . 467 128 131 LEU H H 8.08 0.01 . 468 128 131 LEU C C 177 0.1 . 469 128 131 LEU CA C 55.3 0.1 . 470 128 131 LEU CB C 42.1 0.1 . 471 128 131 LEU N N 122.8 0.1 . 472 129 132 ASP H H 8.21 0.01 . 473 129 132 ASP C C 175.9 0.1 . 474 129 132 ASP CA C 54.3 0.1 . 475 129 132 ASP CB C 40.9 0.1 . 476 129 132 ASP N N 121.7 0.1 . 477 130 133 VAL H H 7.8 0.01 . 478 130 133 VAL C C 175.3 0.1 . 479 130 133 VAL CA C 62.3 0.1 . 480 130 133 VAL CB C 32.6 0.1 . 481 130 133 VAL N N 120.8 0.1 . 482 131 134 LYS H H 7.82 0.01 . 483 131 134 LYS CA C 57.5 0.1 . 484 131 134 LYS CB C 33.4 0.1 . 485 131 134 LYS N N 130.9 0.1 . stop_ save_