data_27502 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for Histidine Kinase NsaS from S. aureus ; _BMRB_accession_number 27502 _BMRB_flat_file_name bmr27502.str _Entry_type original _Submission_date 2018-06-04 _Accession_date 2018-06-04 _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 Bhate Manasi P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 152 "13C chemical shifts" 256 "15N chemical shifts" 83 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-01-24 update BMRB 'update entry citation' 2018-07-02 original author 'original release' stop_ _Original_release_date 2018-06-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and Function of the Transmembrane Domain of NsaS, an Antibiotic Sensing Histidine Kinase in Staphylococcus aureus. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29771498 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhate Manasi P. . 2 Lemmin Thomas . . 3 Kuenze Georg . . 4 Mensa Bruk . . 5 Ganguly Soumya . . 6 Peters Jason M. . 7 Schmidt Nathan . . 8 Pelton Jeffrey G. . 9 Gross Carol A. . 10 Meiler Jens . . 11 DeGrado William F. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 140 _Journal_issue 24 _Journal_ISSN 1520-5126 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7471 _Page_last 7485 _Year 2018 _Details . loop_ _Keyword Bacteria 'Histidine Kinase' Transmembrane stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Nsas _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NsaS $NsaS 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_NsaS _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NsaS _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'Antibiotic stress sensing histidine kinase' 'bacterial signaling' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 90 _Mol_residue_sequence ; MTFLKSIQEIAIVIVIFALF GLMFYLYHLLEAYLLALGVI LLLLIFIGIKYLSFVKTISQ QQQIENLENALYQLKNEQIE YKNGGGCGG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 PHE 4 LEU 5 LYS 6 SER 7 ILE 8 GLN 9 GLU 10 ILE 11 ALA 12 ILE 13 VAL 14 ILE 15 VAL 16 ILE 17 PHE 18 ALA 19 LEU 20 PHE 21 GLY 22 LEU 23 MET 24 PHE 25 TYR 26 LEU 27 TYR 28 HIS 29 LEU 30 LEU 31 GLU 32 ALA 33 TYR 34 LEU 35 LEU 36 ALA 37 LEU 38 GLY 39 VAL 40 ILE 41 LEU 42 LEU 43 LEU 44 LEU 45 ILE 46 PHE 47 ILE 48 GLY 49 ILE 50 LYS 51 TYR 52 LEU 53 SER 54 PHE 55 VAL 56 LYS 57 THR 58 ILE 59 SER 60 GLN 61 GLN 62 GLN 63 GLN 64 ILE 65 GLU 66 ASN 67 LEU 68 GLU 69 ASN 70 ALA 71 LEU 72 TYR 73 GLN 74 LEU 75 LYS 76 ASN 77 GLU 78 GLN 79 ILE 80 GLU 81 TYR 82 LYS 83 ASN 84 GLY 85 GLY 86 GLY 87 CYS 88 GLY 89 GLY 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 $NsaS 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $NsaS 'recombinant technology' . Escherichia coli . pEXP5 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 $NsaS 750 uM '[U-100% 13C; U-100% 15N; U-80% 2H]' D2O 10 % [U-2H] DSS 1 % 'natural abundance' 'C14 betaine' 100 mM [U-2H] MES 40 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 900 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 800 _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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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' 40 . mM pH 6 . pH pressure 1 . atm temperature 273 . 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 CBCA(CO)NH' '3D HNCO' '3D HNCA' '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 NsaS _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 1 1 MET H H 8.54 0.01 . 2 1 1 MET HA H 4.58 0.01 . 3 1 1 MET C C 176.9 0.05 . 4 1 1 MET CA C 54.4 0.05 . 5 1 1 MET CB C 31.8 0.05 . 6 1 1 MET N N 127.5 0.1 . 7 2 2 THR H H 8.16 0.01 . 8 2 2 THR HA H 4.59 0.01 . 9 2 2 THR C C 175.7 0.05 . 10 2 2 THR CA C 64.0 0.05 . 11 2 2 THR CB C 68.2 0.05 . 12 2 2 THR N N 114.9 0.1 . 13 3 3 PHE H H 7.94 0.01 . 14 3 3 PHE HA H 4.58 0.01 . 15 3 3 PHE C C 176.1 0.05 . 16 3 3 PHE CA C 59.1 0.05 . 17 3 3 PHE CB C 38.1 0.05 . 18 3 3 PHE N N 120.7 0.1 . 19 4 4 LEU H H 7.59 0.01 . 20 4 4 LEU HA H 3.94 0.01 . 21 4 4 LEU C C 177.4 0.05 . 22 4 4 LEU CA C 56.0 0.05 . 23 4 4 LEU CB C 40.7 0.05 . 24 4 4 LEU N N 119.1 0.1 . 25 5 5 LYS H H 7.69 0.01 . 26 5 5 LYS HA H 3.95 0.01 . 27 5 5 LYS C C 177 0.05 . 28 5 5 LYS CA C 57.7 0.05 . 29 5 5 LYS CB C 31.7 0.05 . 30 5 5 LYS N N 117.2 0.1 . 31 6 6 SER H H 7.75 0.01 . 32 6 6 SER HA H 4.59 0.01 . 33 6 6 SER C C 173.8 0.05 . 34 6 6 SER CA C 58.7 0.05 . 35 6 6 SER CB C 63.4 0.05 . 36 6 6 SER N N 113 0.1 . 37 7 7 ILE H H 7.56 0.01 . 38 7 7 ILE HA H 4.01 0.01 . 39 7 7 ILE C C 174.6 0.05 . 40 7 7 ILE CA C 61.0 0.05 . 41 7 7 ILE CB C 37.0 0.05 . 42 7 7 ILE N N 119.1 0.1 . 43 8 8 GLN C C 175.9 0.05 . 44 8 8 GLN CA C 56.2 0.05 . 45 8 8 GLN CB C 29.4 0.05 . 46 9 9 GLU H H 8.23 0.01 . 47 9 9 GLU C C 175.4 0.05 . 48 9 9 GLU CA C 55.4 0.05 . 49 9 9 GLU CB C 28.5 0.05 . 50 9 9 GLU N N 121.4 0.1 . 51 10 10 ILE H H 7.91 0.01 . 52 10 10 ILE C C 175.5 0.05 . 53 10 10 ILE CA C 60.7 0.05 . 54 10 10 ILE CB C 37.8 0.05 . 55 10 10 ILE N N 122 0.1 . 56 11 11 ALA H H 8.16 0.01 . 57 11 11 ALA C C 178.1 0.05 . 58 11 11 ALA CA C 55.2 0.05 . 59 11 11 ALA CB C 17.6 0.05 . 60 11 11 ALA N N 121.3 0.1 . 61 12 12 ILE H H 7.84 0.01 . 62 12 12 ILE HA H 4.22 0.01 . 63 12 12 ILE C C 176.7 0.05 . 64 12 12 ILE CA C 64.5 0.05 . 65 12 12 ILE CB C 36.7 0.05 . 66 12 12 ILE N N 115.4 0.1 . 67 13 13 VAL H H 7.49 0.01 . 68 13 13 VAL HA H 3.52 0.01 . 69 13 13 VAL C C 176.8 0.05 . 70 13 13 VAL CA C 66.8 0.05 . 71 13 13 VAL CB C 30.3 0.05 . 72 13 13 VAL N N 118.8 0.1 . 73 14 14 ILE H H 8.11 0.01 . 74 14 14 ILE HA H 3.37 0.01 . 75 14 14 ILE C C 177 0.05 . 76 14 14 ILE CA C 65.2 0.05 . 77 14 14 ILE CB C 36.2 0.05 . 78 14 14 ILE N N 118.5 0.1 . 79 15 15 VAL H H 8.07 0.01 . 80 15 15 VAL C C 177 0.05 . 81 15 15 VAL CA C 66.8 0.05 . 82 15 15 VAL CB C 30.3 0.05 . 83 15 15 VAL N N 119.1 0.1 . 84 16 16 ILE H H 8.18 0.01 . 85 16 16 ILE HA H 3.49 0.01 . 86 16 16 ILE C C 177.3 0.05 . 87 16 16 ILE CA C 65.1 0.05 . 88 16 16 ILE CB C 36.0 0.05 . 89 16 16 ILE N N 119.1 0.1 . 90 17 17 PHE H H 8.51 0.01 . 91 17 17 PHE HA H 3.52 0.01 . 92 17 17 PHE C C 177.4 0.05 . 93 17 17 PHE CA C 61.0 0.05 . 94 17 17 PHE CB C 37.8 0.05 . 95 17 17 PHE N N 118.9 0.1 . 96 18 18 ALA H H 8.75 0.01 . 97 18 18 ALA HA H 4.19 0.01 . 98 18 18 ALA C C 178.4 0.05 . 99 18 18 ALA CA C 55.0 0.05 . 100 18 18 ALA CB C 17.2 0.05 . 101 18 18 ALA N N 121.5 0.1 . 102 19 19 LEU H H 8.39 0.01 . 103 19 19 LEU HA H 3.91 0.01 . 104 19 19 LEU C C 178.7 0.05 . 105 19 19 LEU CA C 57.7 0.05 . 106 19 19 LEU CB C 40.5 0.05 . 107 19 19 LEU N N 117.8 0.1 . 108 20 20 PHE H H 8.31 0.01 . 109 20 20 PHE HA H 3.94 0.01 . 110 20 20 PHE C C 177.6 0.05 . 111 20 20 PHE CA C 61.0 0.05 . 112 20 20 PHE CB C 37.6 0.05 . 113 20 20 PHE N N 117.7 0.1 . 114 21 21 GLY H H 8.74 0.01 . 115 21 21 GLY HA2 H 4.11 0.01 . 116 21 21 GLY HA3 H 4.11 0.01 . 117 21 21 GLY C C 174.7 0.05 . 118 21 21 GLY CA C 47.3 0.05 . 119 21 21 GLY N N 106.9 0.1 . 120 22 22 LEU H H 8.50 0.01 . 121 22 22 LEU HA H 3.51 0.01 . 122 22 22 LEU C C 178.4 0.05 . 123 22 22 LEU CA C 57.8 0.05 . 124 22 22 LEU CB C 41.0 0.05 . 125 22 22 LEU N N 121.7 0.1 . 126 23 23 MET H H 8.10 0.01 . 127 23 23 MET HA H 4.11 0.01 . 128 23 23 MET C C 177.5 0.05 . 129 23 23 MET CA C 58.8 0.05 . 130 23 23 MET CB C 32.0 0.05 . 131 23 23 MET N N 117.6 0.1 . 132 24 24 PHE H H 8.33 0.01 . 133 24 24 PHE HA H 4.09 0.01 . 134 24 24 PHE C C 177.1 0.05 . 135 24 24 PHE CA C 56.4 0.05 . 136 24 24 PHE CB C 41.4 0.05 . 137 24 24 PHE N N 120.1 0.1 . 138 25 25 TYR H H 7.71 0.01 . 139 25 25 TYR C C 174.8 0.05 . 140 25 25 TYR CA C 59.0 0.05 . 141 25 25 TYR CB C 38.6 0.05 . 142 25 25 TYR N N 115.1 0.1 . 143 26 26 LEU H H 8.03 0.01 . 144 26 26 LEU C C 177 0.05 . 145 26 26 LEU CA C 55.6 0.05 . 146 26 26 LEU CB C 40.7 0.05 . 147 26 26 LEU N N 119.6 0.1 . 148 27 27 TYR C C 175.5 0.05 . 149 27 27 TYR CA C 57.5 0.05 . 150 27 27 TYR CB C 38.0 0.05 . 151 28 28 HIS H H 8.09 0.01 . 152 28 28 HIS C C 175.9 0.05 . 153 28 28 HIS CA C 56.0 0.05 . 154 28 28 HIS CB C 32.2 0.05 . 155 28 28 HIS N N 122.6 0.1 . 156 29 29 LEU H H 8.17 0.01 . 157 29 29 LEU HA H 4.26 0.01 . 158 29 29 LEU C C 176.4 0.05 . 159 29 29 LEU CA C 54.0 0.05 . 160 29 29 LEU CB C 40.8 0.05 . 161 29 29 LEU N N 121.3 0.1 . 162 30 30 LEU H H 7.87 0.01 . 163 30 30 LEU CA C 55.7 0.05 . 164 30 30 LEU CB C 40.7 0.05 . 165 31 31 GLU H H 7.69 0.01 . 166 31 31 GLU C C 177 0.05 . 167 31 31 GLU CA C 57.9 0.05 . 168 31 31 GLU CB C 31.8 0.05 . 169 31 31 GLU N N 118.3 0.1 . 170 32 32 ALA H H 7.66 0.01 . 171 32 32 ALA C C 176.8 0.05 . 172 32 32 ALA CA C 52.8 0.05 . 173 32 32 ALA CB C 18.7 0.05 . 174 32 32 ALA N N 121.3 0.1 . 175 33 33 TYR H H 7.57 0.01 . 176 33 33 TYR HA H 4.02 0.01 . 177 33 33 TYR C C 174.7 0.05 . 178 33 33 TYR CA C 55.3 0.05 . 179 33 33 TYR CB C 42.2 0.05 . 180 33 33 TYR N N 116.8 0.1 . 181 34 34 LEU H H 7.64 0.01 . 182 34 34 LEU C C 178.1 0.05 . 183 34 34 LEU CA C 57.2 0.05 . 184 34 34 LEU CB C 40.4 0.05 . 185 35 35 LEU H H 7.80 0.01 . 186 35 35 LEU C C 177.6 0.05 . 187 35 35 LEU CA C 57.6 0.05 . 188 35 35 LEU CB C 40.7 0.05 . 189 35 35 LEU N N 118.6 0.1 . 190 36 36 ALA H H 7.94 0.01 . 191 36 36 ALA C C 178.3 0.05 . 192 36 36 ALA CA C 55.0 0.05 . 193 36 36 ALA CB C 17.4 0.05 . 194 36 36 ALA N N 119.4 0.1 . 195 37 37 LEU H H 8.06 0.01 . 196 37 37 LEU HA H 3.94 0.01 . 197 37 37 LEU C C 178 0.05 . 198 37 37 LEU CA C 57.4 0.05 . 199 37 37 LEU CB C 40.5 0.05 . 200 37 37 LEU N N 116.8 0.1 . 201 38 38 GLY H H 8.31 0.01 . 202 38 38 GLY HA2 H 3.76 0.01 . 203 38 38 GLY HA3 H 3.76 0.01 . 204 38 38 GLY C C 173.9 0.05 . 205 38 38 GLY CA C 47.2 0.05 . 206 38 38 GLY N N 105.8 0.1 . 207 39 39 VAL H H 8.13 0.01 . 208 39 39 VAL HA H 3.87 0.01 . 209 39 39 VAL C C 176.9 0.05 . 210 39 39 VAL CA C 66.7 0.05 . 211 39 39 VAL CB C 30.6 0.05 . 212 39 39 VAL N N 120.5 0.1 . 213 40 40 ILE H H 8.06 0.01 . 214 40 40 ILE C C 177.1 0.05 . 215 40 40 ILE CA C 64.8 0.05 . 216 40 40 ILE CB C 36.2 0.05 . 217 40 40 ILE N N 119.1 0.1 . 218 41 41 LEU H H 8.38 0.01 . 219 41 41 LEU HA H 3.44 0.01 . 220 41 41 LEU C C 177.9 0.05 . 221 41 41 LEU CA C 57.9 0.05 . 222 41 41 LEU CB C 40.4 0.05 . 223 41 41 LEU N N 118.8 0.1 . 224 42 42 LEU H H 8.33 0.01 . 225 42 42 LEU C C 177.2 0.05 . 226 42 42 LEU CA C 56.6 0.05 . 227 42 42 LEU CB C 41.4 0.05 . 228 42 42 LEU N N 119.1 0.1 . 229 43 43 LEU HA H 3.94 0.01 . 230 43 43 LEU CA C 57.9 0.05 . 231 43 43 LEU CB C 40.6 0.05 . 232 44 44 LEU H H 8.36 0.01 . 233 44 44 LEU C C 178.4 0.05 . 234 44 44 LEU CA C 57.9 0.05 . 235 44 44 LEU CB C 40.5 0.05 . 236 44 44 LEU N N 119.1 0.1 . 237 45 45 ILE H H 8.23 0.01 . 238 45 45 ILE C C 176.9 0.05 . 239 45 45 ILE CA C 64.7 0.05 . 240 45 45 ILE CB C 36.8 0.05 . 241 45 45 ILE N N 118.1 0.1 . 242 46 46 PHE H H 8.37 0.01 . 243 46 46 PHE C C 177 0.05 . 244 46 46 PHE CA C 61.0 0.05 . 245 46 46 PHE CB C 38.7 0.05 . 246 46 46 PHE N N 118 0.1 . 247 47 47 ILE H H 8.47 0.01 . 248 47 47 ILE HA H 3.94 0.01 . 249 47 47 ILE C C 177.1 0.05 . 250 47 47 ILE CA C 63.5 0.05 . 251 47 47 ILE CB C 37.2 0.05 . 252 47 47 ILE N N 117.3 0.1 . 253 48 48 GLY H H 8.47 0.01 . 254 48 48 GLY HA2 H 3.90 0.01 . 255 48 48 GLY HA3 H 3.90 0.01 . 256 48 48 GLY C C 174.4 0.05 . 257 48 48 GLY CA C 46.4 0.05 . 258 48 48 GLY N N 108.5 0.1 . 259 49 49 ILE H H 8.24 0.01 . 260 49 49 ILE HA H 4.23 0.01 . 261 49 49 ILE C C 177.2 0.05 . 262 49 49 ILE CA C 63.6 0.05 . 263 49 49 ILE CB C 36.9 0.05 . 264 49 49 ILE N N 119.9 0.1 . 265 50 50 LYS H H 7.98 0.01 . 266 50 50 LYS C C 177.9 0.05 . 267 50 50 LYS CA C 57.9 0.05 . 268 50 50 LYS CB C 31.0 0.05 . 269 50 50 LYS N N 120.8 0.1 . 270 51 51 TYR H H 8.11 0.01 . 271 51 51 TYR C C 176.3 0.05 . 272 51 51 TYR CA C 59.4 0.05 . 273 51 51 TYR CB C 38.1 0.05 . 274 51 51 TYR N N 117.9 0.1 . 275 52 52 LEU H H 7.82 0.01 . 276 52 52 LEU HA H 3.82 0.01 . 277 52 52 LEU C C 177.3 0.05 . 278 52 52 LEU CA C 55.9 0.05 . 279 52 52 LEU CB C 40.7 0.05 . 280 52 52 LEU N N 118.9 0.1 . 281 53 53 SER H H 7.86 0.01 . 282 53 53 SER HA H 3.94 0.01 . 283 53 53 SER C C 177.2 0.05 . 284 53 53 SER CA C 59.9 0.05 . 285 53 53 SER CB C 62.5 0.05 . 286 53 53 SER N N 113.8 0.1 . 287 54 54 PHE H H 7.81 0.01 . 288 54 54 PHE HA H 3.82 0.01 . 289 54 54 PHE C C 175.9 0.05 . 290 54 54 PHE CA C 58.5 0.05 . 291 54 54 PHE CB C 38.6 0.05 . 292 54 54 PHE N N 120.6 0.1 . 293 55 55 VAL H H 7.74 0.01 . 294 55 55 VAL HA H 4.17 0.01 . 295 55 55 VAL C C 176.1 0.05 . 296 55 55 VAL CA C 63.2 0.05 . 297 55 55 VAL CB C 31.3 0.05 . 298 55 55 VAL N N 118.9 0.1 . 299 56 56 LYS H H 8.00 0.01 . 300 56 56 LYS HA H 4.18 0.01 . 301 56 56 LYS C C 177 0.05 . 302 56 56 LYS CA C 57.3 0.05 . 303 56 56 LYS CB C 31.8 0.05 . 304 56 56 LYS N N 122 0.1 . 305 57 57 THR H H 7.78 0.01 . 306 57 57 THR HA H 4.20 0.01 . 307 57 57 THR C C 174.9 0.05 . 308 57 57 THR CA C 62.7 0.05 . 309 57 57 THR CB C 68.9 0.05 . 310 57 57 THR N N 113.5 0.1 . 311 58 58 ILE H H 7.78 0.01 . 312 58 58 ILE HA H 3.81 0.01 . 313 58 58 ILE C C 175.9 0.05 . 314 58 58 ILE CA C 61.5 0.05 . 315 58 58 ILE CB C 37.6 0.05 . 316 58 58 ILE N N 120.6 0.1 . 317 59 59 SER H H 8.05 0.01 . 318 59 59 SER HA H 3.79 0.01 . 319 59 59 SER C C 174.8 0.05 . 320 59 59 SER CA C 58.5 0.05 . 321 59 59 SER CB C 63.2 0.05 . 322 59 59 SER N N 117.3 0.1 . 323 60 60 GLN H H 8.13 0.01 . 324 60 60 GLN C C 176.8 0.05 . 325 60 60 GLN CA C 57.1 0.05 . 326 60 60 GLN CB C 28.3 0.05 . 327 60 60 GLN N N 121.6 0.1 . 328 61 61 GLN CA C 57.3 0.05 . 329 61 61 GLN CB C 27.7 0.05 . 330 62 62 GLN H H 8.21 0.01 . 331 62 62 GLN HA H 4.09 0.01 . 332 62 62 GLN C C 177 0.05 . 333 62 62 GLN CA C 57.3 0.05 . 334 62 62 GLN CB C 27.9 0.05 . 335 62 62 GLN N N 119.5 0.1 . 336 63 63 GLN H H 8.00 0.01 . 337 63 63 GLN HA H 4.25 0.01 . 338 63 63 GLN C C 177.6 0.05 . 339 63 63 GLN CA C 57.4 0.05 . 340 63 63 GLN CB C 28.0 0.05 . 341 63 63 GLN N N 118.9 0.1 . 342 64 64 ILE H H 7.95 0.01 . 343 64 64 ILE C C 176.9 0.05 . 344 64 64 ILE CA C 63.1 0.05 . 345 64 64 ILE CB C 36.7 0.05 . 346 64 64 ILE N N 120.1 0.1 . 347 65 65 GLU H H 8.26 0.01 . 348 65 65 GLU HA H 4.09 0.01 . 349 65 65 GLU C C 177.8 0.05 . 350 65 65 GLU CA C 58.6 0.05 . 351 65 65 GLU CB C 28.5 0.05 . 352 65 65 GLU N N 121.8 0.1 . 353 66 66 ASN H H 8.14 0.01 . 354 66 66 ASN HA H 4.15 0.01 . 355 66 66 ASN C C 177.3 0.05 . 356 66 66 ASN CA C 54.9 0.05 . 357 66 66 ASN CB C 37.8 0.05 . 358 66 66 ASN N N 117.6 0.1 . 359 67 67 LEU H H 7.96 0.01 . 360 67 67 LEU HA H 3.80 0.01 . 361 67 67 LEU C C 177.6 0.05 . 362 67 67 LEU CA C 57.4 0.05 . 363 67 67 LEU CB C 40.8 0.05 . 364 67 67 LEU N N 122.3 0.1 . 365 68 68 GLU H H 8.44 0.01 . 366 68 68 GLU HA H 4.05 0.01 . 367 68 68 GLU C C 177.5 0.05 . 368 68 68 GLU CA C 59.2 0.05 . 369 68 68 GLU CB C 28.2 0.05 . 370 68 68 GLU N N 118.4 0.1 . 371 69 69 ASN H H 8.14 0.01 . 372 69 69 ASN HA H 4.05 0.01 . 373 69 69 ASN C C 176.9 0.05 . 374 69 69 ASN CA C 55.2 0.05 . 375 69 69 ASN CB C 37.9 0.05 . 376 69 69 ASN N N 116.4 0.1 . 377 70 70 ALA H H 7.81 0.01 . 378 70 70 ALA HA H 4.07 0.01 . 379 70 70 ALA C C 179 0.05 . 380 70 70 ALA CA C 54.0 0.05 . 381 70 70 ALA CB C 17.7 0.05 . 382 70 70 ALA N N 122.1 0.1 . 383 71 71 LEU H H 7.85 0.01 . 384 71 71 LEU HA H 3.73 0.01 . 385 71 71 LEU C C 177.5 0.05 . 386 71 71 LEU CA C 56.5 0.05 . 387 71 71 LEU CB C 41.0 0.05 . 388 71 71 LEU N N 116.8 0.1 . 389 72 72 TYR H H 7.86 0.01 . 390 72 72 TYR HA H 3.72 0.01 . 391 72 72 TYR C C 176.2 0.05 . 392 72 72 TYR CA C 59.2 0.05 . 393 72 72 TYR CB C 37.7 0.05 . 394 72 72 TYR N N 117.2 0.1 . 395 73 73 GLN H H 7.75 0.01 . 396 73 73 GLN HA H 4.11 0.01 . 397 73 73 GLN C C 176.4 0.05 . 398 73 73 GLN CA C 56.2 0.05 . 399 73 73 GLN CB C 28.0 0.05 . 400 73 73 GLN N N 117 0.1 . 401 74 74 LEU H H 7.72 0.01 . 402 74 74 LEU HA H 4.05 0.01 . 403 74 74 LEU C C 176.7 0.05 . 404 74 74 LEU CA C 55.7 0.05 . 405 74 74 LEU CB C 41.1 0.05 . 406 74 74 LEU N N 121.1 0.1 . 407 75 75 LYS H H 7.87 0.01 . 408 75 75 LYS HA H 4.06 0.01 . 409 75 75 LYS C C 176 0.05 . 410 75 75 LYS CA C 56.3 0.05 . 411 75 75 LYS CB C 32.1 0.05 . 412 75 75 LYS N N 119.3 0.1 . 413 76 76 ASN H H 8.10 0.01 . 414 76 76 ASN HA H 4.16 0.01 . 415 76 76 ASN C C 175.2 0.05 . 416 76 76 ASN CA C 53.5 0.05 . 417 76 76 ASN CB C 38.4 0.05 . 418 76 76 ASN N N 119 0.1 . 419 77 77 GLU H H 8.23 0.01 . 420 77 77 GLU HA H 4.16 0.01 . 421 77 77 GLU C C 175.9 0.05 . 422 77 77 GLU CA C 56.4 0.05 . 423 77 77 GLU CB C 29.2 0.05 . 424 77 77 GLU N N 120.6 0.1 . 425 78 78 GLN H H 8.15 0.01 . 426 78 78 GLN HA H 4.16 0.01 . 427 78 78 GLN C C 175.4 0.05 . 428 78 78 GLN CA C 55.5 0.05 . 429 78 78 GLN CB C 28.4 0.05 . 430 78 78 GLN N N 120.2 0.1 . 431 79 79 ILE H H 7.86 0.01 . 432 79 79 ILE HA H 4.15 0.01 . 433 79 79 ILE C C 175 0.05 . 434 79 79 ILE CA C 60.7 0.05 . 435 79 79 ILE CB C 37.8 0.05 . 436 79 79 ILE N N 120.7 0.1 . 437 80 80 GLU H H 8.02 0.01 . 438 80 80 GLU HA H 4.20 0.01 . 439 80 80 GLU C C 175.3 0.05 . 440 80 80 GLU CA C 55.5 0.05 . 441 80 80 GLU CB C 29.8 0.05 . 442 80 80 GLU N N 123.4 0.1 . 443 81 81 TYR H H 8.11 0.01 . 444 81 81 TYR HA H 4.21 0.01 . 445 81 81 TYR C C 175 0.05 . 446 81 81 TYR CA C 57.3 0.05 . 447 81 81 TYR CB C 38.1 0.05 . 448 81 81 TYR N N 122.1 0.1 . 449 82 82 LYS H H 8.06 0.01 . 450 82 82 LYS HA H 4.06 0.01 . 451 82 82 LYS C C 174.8 0.05 . 452 82 82 LYS CA C 55.6 0.05 . 453 82 82 LYS CB C 32.4 0.05 . 454 82 82 LYS N N 123.4 0.1 . 455 83 83 ASN H H 7.89 0.01 . 456 83 83 ASN HA H 4.06 0.01 . 457 83 83 ASN C C 178.9 0.05 . 458 83 83 ASN CA C 54.5 0.05 . 459 83 83 ASN CB C 40.5 0.05 . 460 83 83 ASN N N 125.7 0.1 . 461 84 84 GLY H H 8.25 0.01 . 462 84 84 GLY HA2 H 4.38 0.01 . 463 84 84 GLY HA3 H 4.38 0.01 . 464 84 84 GLY C C 174.9 0.05 . 465 84 84 GLY CA C 45.2 0.05 . 466 84 84 GLY N N 114.3 0.1 . 467 85 85 GLY H H 8.35 0.01 . 468 85 85 GLY HA2 H 4.25 0.01 . 469 85 85 GLY HA3 H 4.25 0.01 . 470 85 85 GLY C C 174.6 0.05 . 471 85 85 GLY CA C 45.0 0.05 . 472 85 85 GLY N N 109.1 0.1 . 473 86 86 GLY H H 8.21 0.01 . 474 86 86 GLY HA2 H 4.26 0.01 . 475 86 86 GLY HA3 H 4.26 0.01 . 476 86 86 GLY C C 174.2 0.05 . 477 86 86 GLY CA C 45.0 0.05 . 478 86 86 GLY N N 108.9 0.1 . 479 87 87 CYS H H 8.34 0.01 . 480 87 87 CYS C C 175 0.05 . 481 87 87 CYS CA C 55.3 0.05 . 482 87 87 CYS CB C 40.7 0.05 . 483 87 87 CYS N N 118.8 0.1 . 484 88 88 GLY H H 8.44 0.01 . 485 88 88 GLY C C 174.3 0.05 . 486 88 88 GLY CA C 45.1 0.05 . 487 88 88 GLY N N 110.8 0.1 . 488 89 89 GLY H H 8.08 0.01 . 489 89 89 GLY C C 173.7 0.05 . 490 89 89 GLY CA C 44.9 0.05 . 491 89 89 GLY N N 108.6 0.1 . stop_ save_