data_18598 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments for AgrA LytTR domain ; _BMRB_accession_number 18598 _BMRB_flat_file_name bmr18598.str _Entry_type original _Submission_date 2012-07-17 _Accession_date 2012-07-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone resonance assignments for AgrA LytTR domain' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Leonard Paul G. . 2 Sidote David J. . 3 Stock Ann M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 100 "13C chemical shifts" 302 "15N chemical shifts" 100 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-28 original author . stop_ _Original_release_date 2013-02-28 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Identification of a hydrophobic cleft in the LytTR domain of AgrA as a locus for small molecule interactions that inhibit DNA binding.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23181972 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Leonard Paul G. . 2 Bezar Ian F. . 3 Sidote David J. . 4 Stock Ann M. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 51 _Journal_issue 50 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10035 _Page_last 10043 _Year 2012 _Details . loop_ _Keyword 'LytTR domain' 'Quorum sensing' 'response regulator' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'LytTR domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'LytTR domain' $AgrAc stop_ _System_molecular_weight 12336.8 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function DNA-binding stop_ _Database_query_date . _Details Monomer save_ ######################## # Monomeric polymers # ######################## save_AgrAc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common AgrAc _Molecular_mass . _Mol_thiol_state unknown loop_ _Biological_function DNA-binding 'Response regulator' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 103 _Mol_residue_sequence ; MDNSVETIELKRGSNSVYVQ YDDIMFFESSTKSHRLIAHL DNRQIEFYGNLKELSQLDDR FFRCHNSFVVNRHNIESIDS KERIVYFKNKEHCYASVRNV KKI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 136 MET 2 137 ASP 3 138 ASN 4 139 SER 5 140 VAL 6 141 GLU 7 142 THR 8 143 ILE 9 144 GLU 10 145 LEU 11 146 LYS 12 147 ARG 13 148 GLY 14 149 SER 15 150 ASN 16 151 SER 17 152 VAL 18 153 TYR 19 154 VAL 20 155 GLN 21 156 TYR 22 157 ASP 23 158 ASP 24 159 ILE 25 160 MET 26 161 PHE 27 162 PHE 28 163 GLU 29 164 SER 30 165 SER 31 166 THR 32 167 LYS 33 168 SER 34 169 HIS 35 170 ARG 36 171 LEU 37 172 ILE 38 173 ALA 39 174 HIS 40 175 LEU 41 176 ASP 42 177 ASN 43 178 ARG 44 179 GLN 45 180 ILE 46 181 GLU 47 182 PHE 48 183 TYR 49 184 GLY 50 185 ASN 51 186 LEU 52 187 LYS 53 188 GLU 54 189 LEU 55 190 SER 56 191 GLN 57 192 LEU 58 193 ASP 59 194 ASP 60 195 ARG 61 196 PHE 62 197 PHE 63 198 ARG 64 199 CYS 65 200 HIS 66 201 ASN 67 202 SER 68 203 PHE 69 204 VAL 70 205 VAL 71 206 ASN 72 207 ARG 73 208 HIS 74 209 ASN 75 210 ILE 76 211 GLU 77 212 SER 78 213 ILE 79 214 ASP 80 215 SER 81 216 LYS 82 217 GLU 83 218 ARG 84 219 ILE 85 220 VAL 86 221 TYR 87 222 PHE 88 223 LYS 89 224 ASN 90 225 LYS 91 226 GLU 92 227 HIS 93 228 CYS 94 229 TYR 95 230 ALA 96 231 SER 97 232 VAL 98 233 ARG 99 234 ASN 100 235 VAL 101 236 LYS 102 237 LYS 103 238 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 3BS1 "Structure Of The Staphylococcus Aureus Agra Lyttr Domain Bound To Dna Reveals A Beta Fold With A Novel Mode Of Binding" 100.00 103 100.00 100.00 3.95e-67 PDB 4G4K "Structure Of The Staphylococcus Aureus Agra Lyttr Domain" 100.00 103 100.00 100.00 3.95e-67 DBJ BAB43126 "accessory gene regulator A [Staphylococcus aureus subsp. aureus N315]" 99.03 238 100.00 100.00 2.17e-65 DBJ BAB58201 "accessory gene regulator A [Staphylococcus aureus subsp. aureus Mu50]" 98.06 238 100.00 100.00 8.90e-65 DBJ BAB95828 "accessory gene regulator A [Staphylococcus aureus subsp. aureus MW2]" 99.03 238 100.00 100.00 2.17e-65 DBJ BAF68218 "staphylococcal accessory gene regulator A [Staphylococcus aureus subsp. aureus str. Newman]" 99.03 238 100.00 100.00 2.17e-65 DBJ BAF78907 "accessory gene regulator A [Staphylococcus aureus subsp. aureus Mu3]" 98.06 238 100.00 100.00 8.90e-65 EMBL CAA36784 "AgrA protein [Staphylococcus aureus]" 99.03 238 100.00 100.00 2.17e-65 EMBL CAG41107 "autoinducer sensor protein response regulator protein [Staphylococcus aureus subsp. aureus MRSA252]" 99.03 238 100.00 100.00 2.17e-65 EMBL CAG43751 "autoinducer sensor protein response regulator protein [Staphylococcus aureus subsp. aureus MSSA476]" 99.03 238 100.00 100.00 2.17e-65 EMBL CAI81612 "accessory gene regulator A [Staphylococcus aureus RF122]" 99.03 238 99.02 99.02 3.03e-64 EMBL CAQ50464 "accessory gene regulator protein A [Staphylococcus aureus subsp. aureus ST398]" 99.03 238 100.00 100.00 2.17e-65 GB AAA26597 "accessory gene regulator protein [Staphylococcus aureus]" 99.03 238 100.00 100.00 2.17e-65 GB AAW36991 "accessory gene regulator protein A [Staphylococcus aureus subsp. aureus COL]" 99.03 238 100.00 100.00 2.17e-65 GB ABB17358 "AgrA [Staphylococcus aureus]" 99.03 238 100.00 100.00 2.17e-65 GB ABB17371 "AgrA [Staphylococcus aureus]" 99.03 238 100.00 100.00 2.22e-65 GB ABB17378 "AgrA [Staphylococcus aureus]" 99.03 238 100.00 100.00 2.61e-65 REF WP_000688486 "MULTISPECIES: DNA-binding response regulator [Staphylococcus]" 99.03 238 100.00 100.00 2.08e-65 REF WP_000688487 "DNA-binding response regulator [Staphylococcus aureus]" 99.03 238 100.00 100.00 2.15e-65 REF WP_000688488 "DNA-binding response regulator [Staphylococcus aureus]" 99.03 238 100.00 100.00 2.70e-65 REF WP_000688490 "DNA-binding response regulator [Staphylococcus aureus]" 99.03 238 99.02 99.02 5.46e-65 REF WP_000688492 "DNA-binding response regulator [Staphylococcus aureus]" 99.03 238 100.00 100.00 2.17e-65 SP P0A0I5 "RecName: Full=Accessory gene regulator protein A" 99.03 238 100.00 100.00 2.17e-65 SP P0A0I6 "RecName: Full=Accessory gene regulator protein A" 99.03 238 100.00 100.00 2.17e-65 SP P0A0I7 "RecName: Full=Accessory gene regulator protein A" 99.03 238 100.00 100.00 2.17e-65 SP Q5HEG2 "RecName: Full=Accessory gene regulator A" 99.03 238 100.00 100.00 2.17e-65 SP Q6G7R8 "RecName: Full=Accessory gene regulator protein A" 99.03 238 100.00 100.00 2.17e-65 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $AgrAc 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus agrA 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 $AgrAc 'recombinant technology' . Escherichia coli 'BL21 (DE3) pLysS' pET9a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM AgrA LytTR domain (residues Asp137-Ile238)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AgrAc 1 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ 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_CcpNMR_Analysis _Saveframe_category software _Name ANALYSIS _Version 2.0 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '20 mM sodium phosphate, 100 mM NaCl and 5% D2O at pH 5.8' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 . M pH 5.8 . pH pressure 1 . atm temperature 293.15 . 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 HNCA' '3D HN(CO)CA' '3D HNCACB' '3D HBHA(CO)NH' '3D HNCO' 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 'LytTR domain' _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 1 137 2 ASP CA C 54.42 0.2 1 2 137 2 ASP CB C 41.27 0.2 1 3 138 3 ASN H H 8.59 0.02 1 4 138 3 ASN C C 175.39 0.2 1 5 138 3 ASN CA C 53.41 0.2 1 6 138 3 ASN CB C 38.79 0.2 1 7 138 3 ASN N N 120.11 0.2 1 8 139 4 SER H H 8.46 0.02 1 9 139 4 SER C C 175.44 0.2 1 10 139 4 SER CA C 58.96 0.2 1 11 139 4 SER CB C 63.73 0.2 1 12 139 4 SER N N 116.80 0.2 1 13 140 5 VAL H H 8.04 0.02 1 14 140 5 VAL C C 175.99 0.2 1 15 140 5 VAL CA C 62.78 0.2 1 16 140 5 VAL CB C 32.46 0.2 1 17 140 5 VAL N N 120.93 0.2 1 18 141 6 GLU H H 8.29 0.02 1 19 141 6 GLU C C 174.98 0.2 1 20 141 6 GLU CA C 55.24 0.2 1 21 141 6 GLU CB C 28.92 0.2 1 22 141 6 GLU N N 122.58 0.2 1 23 142 7 THR H H 7.35 0.02 1 24 142 7 THR C C 176.49 0.2 1 25 142 7 THR CA C 61.14 0.2 1 26 142 7 THR CB C 71.41 0.2 1 27 142 7 THR N N 113.53 0.2 1 28 143 8 ILE H H 9.48 0.02 1 29 143 8 ILE C C 177.36 0.2 1 30 143 8 ILE CA C 59.12 0.2 1 31 143 8 ILE CB C 42.26 0.2 1 32 143 8 ILE N N 125.38 0.2 1 33 144 9 GLU H H 8.37 0.02 1 34 144 9 GLU C C 178.76 0.2 1 35 144 9 GLU CA C 54.68 0.2 1 36 144 9 GLU CB C 30.55 0.2 1 37 144 9 GLU N N 127.56 0.2 1 38 145 10 LEU H H 9.03 0.02 1 39 145 10 LEU C C 173.43 0.2 1 40 145 10 LEU CA C 52.73 0.2 1 41 145 10 LEU CB C 38.95 0.2 1 42 145 10 LEU N N 128.60 0.2 1 43 146 11 LYS H H 8.77 0.02 1 44 146 11 LYS C C 175.35 0.2 1 45 146 11 LYS CA C 57.51 0.2 1 46 146 11 LYS CB C 33.17 0.2 1 47 146 11 LYS N N 125.99 0.2 1 48 147 12 ARG H H 8.57 0.02 1 49 147 12 ARG C C 175.12 0.2 1 50 147 12 ARG CA C 55.94 0.2 1 51 147 12 ARG CB C 31.48 0.2 1 52 147 12 ARG N N 124.16 0.2 1 53 148 13 GLY H H 8.63 0.02 1 54 148 13 GLY C C 174.67 0.2 1 55 148 13 GLY CA C 46.94 0.2 1 56 148 13 GLY N N 112.38 0.2 1 57 149 14 SER H H 8.66 0.02 1 58 149 14 SER C C 175.94 0.2 1 59 149 14 SER CA C 58.83 0.2 1 60 149 14 SER CB C 63.64 0.2 1 61 149 14 SER N N 118.97 0.2 1 62 150 15 ASN H H 7.86 0.02 1 63 150 15 ASN C C 177.53 0.2 1 64 150 15 ASN CA C 52.60 0.2 1 65 150 15 ASN CB C 40.51 0.2 1 66 150 15 ASN N N 118.13 0.2 1 67 151 16 SER H H 8.53 0.02 1 68 151 16 SER C C 177.53 0.2 1 69 151 16 SER CA C 58.04 0.2 1 70 151 16 SER CB C 65.88 0.2 1 71 151 16 SER N N 116.28 0.2 1 72 152 17 VAL H H 8.13 0.02 1 73 152 17 VAL C C 178.19 0.2 1 74 152 17 VAL CA C 60.53 0.2 1 75 152 17 VAL CB C 34.98 0.2 1 76 152 17 VAL N N 120.58 0.2 1 77 153 18 TYR H H 8.76 0.02 1 78 153 18 TYR C C 177.45 0.2 1 79 153 18 TYR CA C 57.29 0.2 1 80 153 18 TYR CB C 39.32 0.2 1 81 153 18 TYR N N 125.53 0.2 1 82 154 19 VAL H H 8.59 0.02 1 83 154 19 VAL C C 174.75 0.2 1 84 154 19 VAL CA C 58.94 0.2 1 85 154 19 VAL CB C 35.07 0.2 1 86 154 19 VAL N N 117.67 0.2 1 87 155 20 GLN H H 8.77 0.02 1 88 155 20 GLN C C 176.25 0.2 1 89 155 20 GLN CA C 54.67 0.2 1 90 155 20 GLN CB C 29.75 0.2 1 91 155 20 GLN N N 121.14 0.2 1 92 156 21 TYR H H 8.83 0.02 1 93 156 21 TYR C C 172.04 0.2 1 94 156 21 TYR CA C 58.75 0.2 1 95 156 21 TYR CB C 38.09 0.2 1 96 156 21 TYR N N 120.89 0.2 1 97 157 22 ASP H H 9.01 0.02 1 98 157 22 ASP C C 172.41 0.2 1 99 157 22 ASP CA C 55.07 0.2 1 100 157 22 ASP CB C 37.48 0.2 1 101 157 22 ASP N N 112.82 0.2 1 102 158 23 ASP H H 8.01 0.02 1 103 158 23 ASP C C 173.60 0.2 1 104 158 23 ASP CA C 55.74 0.2 1 105 158 23 ASP CB C 40.87 0.2 1 106 158 23 ASP N N 120.29 0.2 1 107 159 24 ILE H H 7.64 0.02 1 108 159 24 ILE C C 174.88 0.2 1 109 159 24 ILE CA C 60.84 0.2 1 110 159 24 ILE CB C 38.75 0.2 1 111 159 24 ILE N N 117.64 0.2 1 112 160 25 MET H H 9.42 0.02 1 113 160 25 MET C C 175.35 0.2 1 114 160 25 MET CA C 56.20 0.2 1 115 160 25 MET CB C 33.48 0.2 1 116 160 25 MET N N 126.17 0.2 1 117 161 26 PHE H H 6.64 0.02 1 118 161 26 PHE C C 171.71 0.2 1 119 161 26 PHE CA C 55.09 0.2 1 120 161 26 PHE CB C 40.99 0.2 1 121 161 26 PHE N N 107.41 0.2 1 122 162 27 PHE H H 9.92 0.02 1 123 162 27 PHE C C 179.03 0.2 1 124 162 27 PHE CA C 55.95 0.2 1 125 162 27 PHE CB C 43.28 0.2 1 126 162 27 PHE N N 117.53 0.2 1 127 163 28 GLU H H 9.33 0.02 1 128 163 28 GLU C C 176.22 0.2 1 129 163 28 GLU CA C 53.06 0.2 1 130 163 28 GLU CB C 36.23 0.2 1 131 163 28 GLU N N 122.53 0.2 1 132 164 29 SER H H 8.64 0.02 1 133 164 29 SER C C 175.68 0.2 1 134 164 29 SER CA C 58.04 0.2 1 135 164 29 SER CB C 63.97 0.2 1 136 164 29 SER N N 119.43 0.2 1 137 165 30 SER H H 8.18 0.02 1 138 165 30 SER C C 177.18 0.2 1 139 165 30 SER CA C 56.74 0.2 1 140 165 30 SER CB C 64.29 0.2 1 141 165 30 SER N N 118.11 0.2 1 142 166 31 THR H H 8.38 0.02 1 143 166 31 THR C C 175.68 0.2 1 144 166 31 THR CA C 63.38 0.2 1 145 166 31 THR CB C 68.92 0.2 1 146 166 31 THR N N 115.20 0.2 1 147 167 32 LYS H H 8.28 0.02 1 148 167 32 LYS C C 175.43 0.2 1 149 167 32 LYS CA C 56.06 0.2 1 150 167 32 LYS CB C 33.17 0.2 1 151 167 32 LYS N N 121.75 0.2 1 152 168 33 SER H H 8.07 0.02 1 153 168 33 SER C C 174.66 0.2 1 154 168 33 SER CA C 58.62 0.2 1 155 168 33 SER CB C 63.90 0.2 1 156 168 33 SER N N 115.64 0.2 1 157 169 34 HIS H H 8.75 0.02 1 158 169 34 HIS C C 176.21 0.2 1 159 169 34 HIS CA C 56.83 0.2 1 160 169 34 HIS CB C 27.86 0.2 1 161 169 34 HIS N N 117.32 0.2 1 162 170 35 ARG H H 7.75 0.02 1 163 170 35 ARG C C 177.11 0.2 1 164 170 35 ARG CA C 55.05 0.2 1 165 170 35 ARG CB C 32.36 0.2 1 166 170 35 ARG N N 117.58 0.2 1 167 171 36 LEU H H 8.61 0.02 1 168 171 36 LEU C C 175.81 0.2 1 169 171 36 LEU CA C 52.45 0.2 1 170 171 36 LEU CB C 45.56 0.2 1 171 171 36 LEU N N 122.14 0.2 1 172 172 37 ILE H H 9.25 0.02 1 173 172 37 ILE C C 176.02 0.2 1 174 172 37 ILE CA C 60.38 0.2 1 175 172 37 ILE CB C 40.89 0.2 1 176 172 37 ILE N N 117.16 0.2 1 177 173 38 ALA H H 9.88 0.02 1 178 173 38 ALA C C 173.57 0.2 1 179 173 38 ALA CA C 51.04 0.2 1 180 173 38 ALA CB C 19.61 0.2 1 181 173 38 ALA N N 130.06 0.2 1 182 174 39 HIS H H 8.65 0.02 1 183 174 39 HIS C C 175.14 0.2 1 184 174 39 HIS CA C 55.77 0.2 1 185 174 39 HIS CB C 26.39 0.2 1 186 174 39 HIS N N 123.47 0.2 1 187 175 40 LEU H H 8.49 0.02 1 188 175 40 LEU C C 177.56 0.2 1 189 175 40 LEU CA C 54.36 0.2 1 190 175 40 LEU CB C 41.68 0.2 1 191 175 40 LEU N N 126.67 0.2 1 192 176 41 ASP H H 8.75 0.02 1 193 176 41 ASP C C 174.76 0.2 1 194 176 41 ASP CA C 58.58 0.2 1 195 176 41 ASP CB C 40.84 0.2 1 196 176 41 ASP N N 118.54 0.2 1 197 177 42 ASN H H 8.65 0.02 1 198 177 42 ASN C C 173.05 0.2 1 199 177 42 ASN CA C 52.10 0.2 1 200 177 42 ASN CB C 39.50 0.2 1 201 177 42 ASN N N 113.67 0.2 1 202 178 43 ARG H H 7.06 0.02 1 203 178 43 ARG C C 176.21 0.2 1 204 178 43 ARG CA C 55.06 0.2 1 205 178 43 ARG CB C 32.12 0.2 1 206 178 43 ARG N N 114.31 0.2 1 207 179 44 GLN H H 8.44 0.02 1 208 179 44 GLN C C 178.26 0.2 1 209 179 44 GLN CA C 54.44 0.2 1 210 179 44 GLN CB C 30.67 0.2 1 211 179 44 GLN N N 118.07 0.2 1 212 180 45 ILE H H 8.56 0.02 1 213 180 45 ILE C C 175.34 0.2 1 214 180 45 ILE CA C 59.75 0.2 1 215 180 45 ILE CB C 42.04 0.2 1 216 180 45 ILE N N 121.24 0.2 1 217 181 46 GLU H H 8.94 0.02 1 218 181 46 GLU C C 176.27 0.2 1 219 181 46 GLU CA C 55.35 0.2 1 220 181 46 GLU CB C 31.14 0.2 1 221 181 46 GLU N N 130.54 0.2 1 222 182 47 PHE H H 9.32 0.02 1 223 182 47 PHE C C 175.10 0.2 1 224 182 47 PHE CA C 55.93 0.2 1 225 182 47 PHE CB C 40.87 0.2 1 226 182 47 PHE N N 123.25 0.2 1 227 183 48 TYR H H 8.89 0.02 1 228 183 48 TYR C C 179.34 0.2 1 229 183 48 TYR CA C 57.26 0.2 1 230 183 48 TYR CB C 39.06 0.2 1 231 183 48 TYR N N 119.23 0.2 1 232 184 49 GLY H H 7.72 0.02 1 233 184 49 GLY C C 175.63 0.2 1 234 184 49 GLY CA C 45.61 0.2 1 235 184 49 GLY N N 110.25 0.2 1 236 185 50 ASN H H 8.42 0.02 1 237 185 50 ASN C C 180.58 0.2 1 238 185 50 ASN CA C 52.15 0.2 1 239 185 50 ASN CB C 42.09 0.2 1 240 185 50 ASN N N 116.69 0.2 1 241 186 51 LEU H H 9.12 0.02 1 242 186 51 LEU C C 176.44 0.2 1 243 186 51 LEU CA C 58.08 0.2 1 244 186 51 LEU CB C 41.68 0.2 1 245 186 51 LEU N N 124.41 0.2 1 246 187 52 LYS H H 8.25 0.02 1 247 187 52 LYS C C 172.54 0.2 1 248 187 52 LYS CA C 59.52 0.2 1 249 187 52 LYS CB C 31.88 0.2 1 250 187 52 LYS N N 119.32 0.2 1 251 188 53 GLU H H 7.85 0.02 1 252 188 53 GLU C C 171.45 0.2 1 253 188 53 GLU CA C 59.04 0.2 1 254 188 53 GLU CB C 29.56 0.2 1 255 188 53 GLU N N 119.11 0.2 1 256 189 54 LEU H H 7.50 0.02 1 257 189 54 LEU C C 171.25 0.2 1 258 189 54 LEU CA C 57.18 0.2 1 259 189 54 LEU CB C 41.03 0.2 1 260 189 54 LEU N N 119.71 0.2 1 261 190 55 SER H H 7.79 0.02 1 262 190 55 SER C C 172.72 0.2 1 263 190 55 SER CA C 60.78 0.2 1 264 190 55 SER CB C 63.23 0.2 1 265 190 55 SER N N 111.04 0.2 1 266 191 56 GLN H H 7.22 0.02 1 267 191 56 GLN C C 176.77 0.2 1 268 191 56 GLN CA C 55.57 0.2 1 269 191 56 GLN CB C 29.28 0.2 1 270 191 56 GLN N N 117.02 0.2 1 271 192 57 LEU H H 7.53 0.02 1 272 192 57 LEU C C 173.98 0.2 1 273 192 57 LEU CA C 57.80 0.2 1 274 192 57 LEU CB C 43.40 0.2 1 275 192 57 LEU N N 120.15 0.2 1 276 193 58 ASP H H 7.19 0.02 1 277 193 58 ASP C C 173.88 0.2 1 278 193 58 ASP CA C 54.12 0.2 1 279 193 58 ASP CB C 46.23 0.2 1 280 193 58 ASP N N 112.09 0.2 1 281 194 59 ASP H H 8.94 0.02 1 282 194 59 ASP C C 175.38 0.2 1 283 194 59 ASP CA C 56.77 0.2 1 284 194 59 ASP CB C 41.13 0.2 1 285 194 59 ASP N N 125.41 0.2 1 286 195 60 ARG H H 9.20 0.02 1 287 195 60 ARG C C 174.59 0.2 1 288 195 60 ARG CA C 56.77 0.2 1 289 195 60 ARG CB C 28.12 0.2 1 290 195 60 ARG N N 117.89 0.2 1 291 196 61 PHE H H 7.87 0.02 1 292 196 61 PHE C C 175.54 0.2 1 293 196 61 PHE CA C 56.43 0.2 1 294 196 61 PHE CB C 39.37 0.2 1 295 196 61 PHE N N 120.81 0.2 1 296 197 62 PHE H H 8.92 0.02 1 297 197 62 PHE C C 176.30 0.2 1 298 197 62 PHE CA C 56.31 0.2 1 299 197 62 PHE CB C 43.16 0.2 1 300 197 62 PHE N N 121.53 0.2 1 301 198 63 ARG H H 9.00 0.02 1 302 198 63 ARG C C 176.46 0.2 1 303 198 63 ARG CA C 54.97 0.2 1 304 198 63 ARG CB C 29.93 0.2 1 305 198 63 ARG N N 132.79 0.2 1 306 199 64 CYS H H 7.74 0.02 1 307 199 64 CYS C C 178.20 0.2 1 308 199 64 CYS CA C 56.05 0.2 1 309 199 64 CYS CB C 29.73 0.2 1 310 199 64 CYS N N 121.69 0.2 1 311 200 65 HIS H H 8.52 0.02 1 312 200 65 HIS C C 179.04 0.2 1 313 200 65 HIS CA C 56.80 0.2 1 314 200 65 HIS CB C 36.95 0.2 1 315 200 65 HIS N N 125.62 0.2 1 316 201 66 ASN H H 8.72 0.02 1 317 201 66 ASN C C 177.20 0.2 1 318 201 66 ASN CA C 57.33 0.2 1 319 201 66 ASN CB C 38.83 0.2 1 320 201 66 ASN N N 125.50 0.2 1 321 202 67 SER H H 12.10 0.02 1 322 202 67 SER C C 172.79 0.2 1 323 202 67 SER CA C 59.56 0.2 1 324 202 67 SER CB C 64.31 0.2 1 325 202 67 SER N N 116.98 0.2 1 326 203 68 PHE H H 7.19 0.02 1 327 203 68 PHE C C 178.02 0.2 1 328 203 68 PHE CA C 56.74 0.2 1 329 203 68 PHE CB C 44.85 0.2 1 330 203 68 PHE N N 112.33 0.2 1 331 204 69 VAL H H 8.69 0.02 1 332 204 69 VAL C C 175.79 0.2 1 333 204 69 VAL CA C 61.16 0.2 1 334 204 69 VAL CB C 35.14 0.2 1 335 204 69 VAL N N 120.60 0.2 1 336 205 70 VAL H H 9.32 0.02 1 337 205 70 VAL C C 175.26 0.2 1 338 205 70 VAL CA C 59.44 0.2 1 339 205 70 VAL CB C 34.28 0.2 1 340 205 70 VAL N N 119.66 0.2 1 341 206 71 ASN H H 8.27 0.02 1 342 206 71 ASN C C 177.10 0.2 1 343 206 71 ASN CA C 51.79 0.2 1 344 206 71 ASN CB C 39.22 0.2 1 345 206 71 ASN N N 117.91 0.2 1 346 207 72 ARG H H 9.97 0.02 1 347 207 72 ARG C C 173.60 0.2 1 348 207 72 ARG CA C 59.85 0.2 1 349 207 72 ARG CB C 32.04 0.2 1 350 207 72 ARG N N 124.50 0.2 1 351 208 73 HIS H H 8.74 0.02 1 352 208 73 HIS C C 171.75 0.2 1 353 208 73 HIS CA C 56.35 0.2 1 354 208 73 HIS CB C 28.19 0.2 1 355 208 73 HIS N N 113.30 0.2 1 356 209 74 ASN H H 8.00 0.02 1 357 209 74 ASN C C 175.31 0.2 1 358 209 74 ASN CA C 52.84 0.2 1 359 209 74 ASN CB C 41.84 0.2 1 360 209 74 ASN N N 114.16 0.2 1 361 210 75 ILE H H 7.04 0.02 1 362 210 75 ILE C C 176.52 0.2 1 363 210 75 ILE CA C 63.33 0.2 1 364 210 75 ILE CB C 39.28 0.2 1 365 210 75 ILE N N 122.22 0.2 1 366 211 76 GLU H H 9.61 0.02 1 367 211 76 GLU C C 175.67 0.2 1 368 211 76 GLU CA C 57.12 0.2 1 369 211 76 GLU CB C 32.64 0.2 1 370 211 76 GLU N N 130.53 0.2 1 371 212 77 SER H H 7.73 0.02 1 372 212 77 SER C C 175.44 0.2 1 373 212 77 SER CA C 58.22 0.2 1 374 212 77 SER CB C 64.74 0.2 1 375 212 77 SER N N 111.44 0.2 1 376 213 78 ILE H H 8.44 0.02 1 377 213 78 ILE C C 179.86 0.2 1 378 213 78 ILE CA C 60.44 0.2 1 379 213 78 ILE CB C 42.10 0.2 1 380 213 78 ILE N N 119.00 0.2 1 381 214 79 ASP H H 9.30 0.02 1 382 214 79 ASP C C 175.35 0.2 1 383 214 79 ASP CA C 52.16 0.2 1 384 214 79 ASP CB C 41.80 0.2 1 385 214 79 ASP N N 127.57 0.2 1 386 215 80 SER H H 8.91 0.02 1 387 215 80 SER C C 173.60 0.2 1 388 215 80 SER CA C 61.01 0.2 1 389 215 80 SER CB C 62.97 0.2 1 390 215 80 SER N N 120.99 0.2 1 391 216 81 LYS H H 8.28 0.02 1 392 216 81 LYS C C 176.34 0.2 1 393 216 81 LYS CA C 58.97 0.2 1 394 216 81 LYS CB C 32.56 0.2 1 395 216 81 LYS N N 123.04 0.2 1 396 217 82 GLU H H 7.78 0.02 1 397 217 82 GLU C C 172.71 0.2 1 398 217 82 GLU CA C 55.59 0.2 1 399 217 82 GLU CB C 30.33 0.2 1 400 217 82 GLU N N 116.10 0.2 1 401 218 83 ARG H H 7.83 0.02 1 402 218 83 ARG C C 175.51 0.2 1 403 218 83 ARG CA C 57.63 0.2 1 404 218 83 ARG CB C 26.27 0.2 1 405 218 83 ARG N N 115.08 0.2 1 406 219 84 ILE H H 7.51 0.02 1 407 219 84 ILE C C 177.24 0.2 1 408 219 84 ILE CA C 60.06 0.2 1 409 219 84 ILE CB C 40.96 0.2 1 410 219 84 ILE N N 116.69 0.2 1 411 220 85 VAL H H 8.19 0.02 1 412 220 85 VAL C C 177.54 0.2 1 413 220 85 VAL CA C 61.09 0.2 1 414 220 85 VAL CB C 32.31 0.2 1 415 220 85 VAL N N 127.07 0.2 1 416 221 86 TYR H H 8.71 0.02 1 417 221 86 TYR C C 177.28 0.2 1 418 221 86 TYR CA C 57.94 0.2 1 419 221 86 TYR CB C 39.74 0.2 1 420 221 86 TYR N N 123.10 0.2 1 421 222 87 PHE H H 8.82 0.02 1 422 222 87 PHE C C 174.03 0.2 1 423 222 87 PHE CA C 58.36 0.2 1 424 222 87 PHE CB C 42.85 0.2 1 425 222 87 PHE N N 119.33 0.2 1 426 223 88 LYS H H 8.56 0.02 1 427 223 88 LYS C C 172.32 0.2 1 428 223 88 LYS CA C 59.43 0.2 1 429 223 88 LYS CB C 33.31 0.2 1 430 223 88 LYS N N 120.60 0.2 1 431 224 89 ASN H H 7.62 0.02 1 432 224 89 ASN C C 175.39 0.2 1 433 224 89 ASN CA C 52.91 0.2 1 434 224 89 ASN CB C 38.54 0.2 1 435 224 89 ASN N N 116.96 0.2 1 436 225 90 LYS H H 8.25 0.02 1 437 225 90 LYS C C 174.59 0.2 1 438 225 90 LYS CA C 58.39 0.2 1 439 225 90 LYS CB C 29.00 0.2 1 440 225 90 LYS N N 110.68 0.2 1 441 226 91 GLU H H 7.80 0.02 1 442 226 91 GLU C C 173.55 0.2 1 443 226 91 GLU CA C 57.80 0.2 1 444 226 91 GLU CB C 33.59 0.2 1 445 226 91 GLU N N 118.19 0.2 1 446 227 92 HIS H H 8.43 0.02 1 447 227 92 HIS C C 176.17 0.2 1 448 227 92 HIS CA C 54.35 0.2 1 449 227 92 HIS CB C 32.36 0.2 1 450 227 92 HIS N N 113.61 0.2 1 451 228 93 CYS H H 8.46 0.02 1 452 228 93 CYS C C 178.83 0.2 1 453 228 93 CYS CA C 55.50 0.2 1 454 228 93 CYS CB C 28.57 0.2 1 455 228 93 CYS N N 114.11 0.2 1 456 229 94 TYR CA C 57.00 0.2 1 457 229 94 TYR CB C 41.75 0.2 1 458 230 95 ALA H H 8.11 0.02 1 459 230 95 ALA C C 177.78 0.2 1 460 230 95 ALA CA C 49.75 0.2 1 461 230 95 ALA CB C 22.70 0.2 1 462 230 95 ALA N N 117.12 0.2 1 463 231 96 SER H H 9.26 0.02 1 464 231 96 SER C C 174.37 0.2 1 465 231 96 SER CA C 57.04 0.2 1 466 231 96 SER CB C 65.17 0.2 1 467 231 96 SER N N 117.01 0.2 1 468 232 97 VAL H H 8.74 0.02 1 469 232 97 VAL C C 175.68 0.2 1 470 232 97 VAL CA C 65.82 0.2 1 471 232 97 VAL CB C 32.18 0.2 1 472 232 97 VAL N N 121.65 0.2 1 473 233 98 ARG H H 8.20 0.02 1 474 233 98 ARG C C 173.37 0.2 1 475 233 98 ARG CA C 58.15 0.2 1 476 233 98 ARG CB C 30.53 0.2 1 477 233 98 ARG N N 117.30 0.2 1 478 234 99 ASN H H 7.70 0.02 1 479 234 99 ASN C C 173.38 0.2 1 480 234 99 ASN CA C 53.89 0.2 1 481 234 99 ASN CB C 40.20 0.2 1 482 234 99 ASN N N 114.34 0.2 1 483 235 100 VAL H H 8.15 0.02 1 484 235 100 VAL C C 173.18 0.2 1 485 235 100 VAL CA C 65.50 0.2 1 486 235 100 VAL CB C 31.22 0.2 1 487 235 100 VAL N N 121.77 0.2 1 488 236 101 LYS H H 8.05 0.02 1 489 236 101 LYS C C 175.52 0.2 1 490 236 101 LYS CA C 56.86 0.2 1 491 236 101 LYS CB C 32.04 0.2 1 492 236 101 LYS N N 117.96 0.2 1 493 237 102 LYS H H 7.69 0.02 1 494 237 102 LYS C C 174.36 0.2 1 495 237 102 LYS CA C 55.51 0.2 1 496 237 102 LYS CB C 34.00 0.2 1 497 237 102 LYS N N 118.12 0.2 1 498 238 103 ILE H H 6.83 0.02 1 499 238 103 ILE C C 175.54 0.2 1 500 238 103 ILE CA C 65.83 0.2 1 501 238 103 ILE CB C 38.70 0.2 1 502 238 103 ILE N N 124.63 0.2 1 stop_ save_