data_5234 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignment of the 2H,13C,15N labelled 32KDa Central Domain of Escherichia coli TyrR ; _BMRB_accession_number 5234 _BMRB_flat_file_name bmr5234.str _Entry_type original _Submission_date 2001-12-17 _Accession_date 2001-12-17 _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 Swarbrick James D . 2 Bashtannyk Tanya . . 3 Dixon Mathew . . 4 Pau Richard . . 5 Davidson Barrie . . 6 Gooley Paul R . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 247 "13C chemical shifts" 672 "15N chemical shifts" 246 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone resonance assignment of the 2H, 13C, 15N labelled 32kDa Central Domain of Escherichia coli TyrR ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22012552 _PubMed_ID 12018490 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Swarbrick James D . 2 Bashtannyk Tanya . . 3 Dixon Mathew . . 4 Pau Richard . . 5 Davidson Barrie . . 6 Gooley Paul R . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 381 _Page_last 382 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_TyrR _Saveframe_category molecular_system _Mol_system_name 'TyrR transcription factor central domain of E.coli' _Abbreviation_common TyrR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TyrR central domain' $TyrR stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'hexamerisation ATP/Tyrosine binding' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TyrR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'TyrR transcription factor central domain' _Abbreviation_common 'Central Domain of TyrR' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 288 _Mol_residue_sequence ; MGRQLQNVAAQDVSAFSQIV AVSPKMKHVVEQAQKLAMLS APLLITGDTGTGKDLFAYAC HQASPRAGKPYLALNCASIP EDAVESELFGHAPEGKKGFF EQANGGSVLLDEIGEMSPRM QAKLLRFLNDGTFRRVGEDH EVHVDVRVICATQKNLVELV QKGMFREDLYYRLNVLTLNL PPLRDCPQDIMPLTELFVAR FADEQGVPLPKLAADLNTVL TRYAWPGNVRQLKNAIYRAL TQLDGYELRPQDILLPDYDA ATVAVGEDAMEGSLDEITSR LEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 ARG 4 GLN 5 LEU 6 GLN 7 ASN 8 VAL 9 ALA 10 ALA 11 GLN 12 ASP 13 VAL 14 SER 15 ALA 16 PHE 17 SER 18 GLN 19 ILE 20 VAL 21 ALA 22 VAL 23 SER 24 PRO 25 LYS 26 MET 27 LYS 28 HIS 29 VAL 30 VAL 31 GLU 32 GLN 33 ALA 34 GLN 35 LYS 36 LEU 37 ALA 38 MET 39 LEU 40 SER 41 ALA 42 PRO 43 LEU 44 LEU 45 ILE 46 THR 47 GLY 48 ASP 49 THR 50 GLY 51 THR 52 GLY 53 LYS 54 ASP 55 LEU 56 PHE 57 ALA 58 TYR 59 ALA 60 CYS 61 HIS 62 GLN 63 ALA 64 SER 65 PRO 66 ARG 67 ALA 68 GLY 69 LYS 70 PRO 71 TYR 72 LEU 73 ALA 74 LEU 75 ASN 76 CYS 77 ALA 78 SER 79 ILE 80 PRO 81 GLU 82 ASP 83 ALA 84 VAL 85 GLU 86 SER 87 GLU 88 LEU 89 PHE 90 GLY 91 HIS 92 ALA 93 PRO 94 GLU 95 GLY 96 LYS 97 LYS 98 GLY 99 PHE 100 PHE 101 GLU 102 GLN 103 ALA 104 ASN 105 GLY 106 GLY 107 SER 108 VAL 109 LEU 110 LEU 111 ASP 112 GLU 113 ILE 114 GLY 115 GLU 116 MET 117 SER 118 PRO 119 ARG 120 MET 121 GLN 122 ALA 123 LYS 124 LEU 125 LEU 126 ARG 127 PHE 128 LEU 129 ASN 130 ASP 131 GLY 132 THR 133 PHE 134 ARG 135 ARG 136 VAL 137 GLY 138 GLU 139 ASP 140 HIS 141 GLU 142 VAL 143 HIS 144 VAL 145 ASP 146 VAL 147 ARG 148 VAL 149 ILE 150 CYS 151 ALA 152 THR 153 GLN 154 LYS 155 ASN 156 LEU 157 VAL 158 GLU 159 LEU 160 VAL 161 GLN 162 LYS 163 GLY 164 MET 165 PHE 166 ARG 167 GLU 168 ASP 169 LEU 170 TYR 171 TYR 172 ARG 173 LEU 174 ASN 175 VAL 176 LEU 177 THR 178 LEU 179 ASN 180 LEU 181 PRO 182 PRO 183 LEU 184 ARG 185 ASP 186 CYS 187 PRO 188 GLN 189 ASP 190 ILE 191 MET 192 PRO 193 LEU 194 THR 195 GLU 196 LEU 197 PHE 198 VAL 199 ALA 200 ARG 201 PHE 202 ALA 203 ASP 204 GLU 205 GLN 206 GLY 207 VAL 208 PRO 209 LEU 210 PRO 211 LYS 212 LEU 213 ALA 214 ALA 215 ASP 216 LEU 217 ASN 218 THR 219 VAL 220 LEU 221 THR 222 ARG 223 TYR 224 ALA 225 TRP 226 PRO 227 GLY 228 ASN 229 VAL 230 ARG 231 GLN 232 LEU 233 LYS 234 ASN 235 ALA 236 ILE 237 TYR 238 ARG 239 ALA 240 LEU 241 THR 242 GLN 243 LEU 244 ASP 245 GLY 246 TYR 247 GLU 248 LEU 249 ARG 250 PRO 251 GLN 252 ASP 253 ILE 254 LEU 255 LEU 256 PRO 257 ASP 258 TYR 259 ASP 260 ALA 261 ALA 262 THR 263 VAL 264 ALA 265 VAL 266 GLY 267 GLU 268 ASP 269 ALA 270 MET 271 GLU 272 GLY 273 SER 274 LEU 275 ASP 276 GLU 277 ILE 278 THR 279 SER 280 ARG 281 LEU 282 GLU 283 HIS 284 HIS 285 HIS 286 HIS 287 HIS 288 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 DBJ BAA14905 "DNA-binding transcriptional dual regulator, tyrosine-binding [Escherichia coli str. K-12 substr. W3110]" 98.26 513 98.94 98.94 0.00e+00 DBJ BAB35325 "transcription regulator tyrR [Escherichia coli O157:H7 str. Sakai]" 98.26 513 98.59 98.59 0.00e+00 DBJ BAG76899 "transcriptional regulator [Escherichia coli SE11]" 98.26 513 98.94 98.94 0.00e+00 DBJ BAI25172 "DNA-binding transcriptional dual regulator TyrR, tyrosine-binding [Escherichia coli O26:H11 str. 11368]" 98.26 513 98.94 98.94 0.00e+00 DBJ BAI30314 "DNA-binding transcriptional dual regulator TyrR, tyrosine-binding [Escherichia coli O103:H2 str. 12009]" 98.26 513 98.94 98.94 0.00e+00 EMBL CAP75867 "Transcriptional regulatory protein tyrR [Escherichia coli LF82]" 98.26 513 98.23 98.59 0.00e+00 EMBL CAQ31828 "TyrR transcriptional dual regulator [Escherichia coli BL21(DE3)]" 98.26 513 98.94 98.94 0.00e+00 EMBL CAQ98207 "DNA-binding transcriptional dual regulator, tyrosine-binding [Escherichia coli IAI1]" 98.26 513 98.94 98.94 0.00e+00 EMBL CAR02785 "DNA-binding transcriptional dual regulator, tyrosine-binding [Escherichia coli S88]" 98.26 513 98.23 98.59 0.00e+00 EMBL CAR07729 "DNA-binding transcriptional dual regulator, tyrosine-binding [Escherichia coli ED1a]" 98.26 513 98.23 98.59 0.00e+00 GB AAA24706 "TyrR protein [Escherichia coli]" 98.26 513 98.94 98.94 0.00e+00 GB AAB25766 "TyrR=TyrR regulon repression and activation [Escherichia coli, Peptide, 513 aa]" 98.26 513 98.94 98.94 0.00e+00 GB AAC74405 "aromatic amino acid biosynthesis and transport regulon transcriptional regulator; autorepressor; ATPase; phosphatase [Escherich" 98.26 513 98.94 98.94 0.00e+00 GB AAF28133 "TyrR [Shigella dysenteriae]" 98.26 513 98.59 98.59 0.00e+00 GB AAG56479 "transcriptional regulation of aroF, aroG, tyrA and aromatic amino acid transport [Escherichia coli O157:H7 str. EDL933]" 98.26 513 97.53 97.53 0.00e+00 REF NP_287865 "DNA-binding transcriptional regulator TyrR [Escherichia coli O157:H7 str. EDL933]" 98.26 513 97.53 97.53 0.00e+00 REF NP_309929 "DNA-binding transcriptional regulator TyrR [Escherichia coli O157:H7 str. Sakai]" 98.26 513 98.59 98.59 0.00e+00 REF NP_415839 "aromatic amino acid biosynthesis and transport regulon transcriptional regulator; autorepressor; ATPase; phosphatase [Escherich" 98.26 513 98.94 98.94 0.00e+00 REF NP_707228 "DNA-binding transcriptional regulator TyrR [Shigella flexneri 2a str. 301]" 98.26 513 98.59 98.94 0.00e+00 REF NP_753699 "DNA-binding transcriptional regulator TyrR [Escherichia coli CFT073]" 98.26 522 98.23 98.59 0.00e+00 SP P07604 "RecName: Full=Transcriptional regulatory protein TyrR [Escherichia coli K-12]" 98.26 513 98.94 98.94 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TyrR 'E. coli' 562 Eubacteria . Escherichia coli 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 $TyrR 'recombinant technology' . . . . . 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 $TyrR 0.7 mM '[U-13C; U-2H; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPIPE _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.4 loop_ _Task assignments stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_Trosy_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Trosy HNCA' _Sample_label . save_ save_Trosy_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'Trosy HNCACB' _Sample_label . save_ save_Trosy_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'Trosy HN(CO)CA' _Sample_label . save_ save_Trosy_HN(CO)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'Trosy HN(CO)CB' _Sample_label . save_ save_Trosy_HN(CA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'Trosy HN(CA)CB' _Sample_label . save_ save_1H-15N_NOESY_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY_HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Trosy HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'Trosy HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'Trosy HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'Trosy HN(CO)CB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'Trosy HN(CA)CB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY_HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Deuteration_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 n/a temperature 293 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS H 2 'methyl protons' ppm 0.0 . indirect . . . 0.153506088 DSS N 15 'methyl protons' ppm 0.0 . 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_bb_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Deuteration_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'TyrR central 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 . 8 VAL N N 122.2 0.1 1 2 . 8 VAL H H 7.83 0.01 1 3 . 8 VAL CA C 61.7 0.2 1 4 . 8 VAL CB C 31.9 0.2 1 5 . 8 VAL C C 175.7 0.2 1 6 . 9 ALA N N 129.2 0.1 1 7 . 9 ALA H H 8.10 0.01 1 8 . 9 ALA CA C 51.8 0.2 1 9 . 9 ALA CB C 18.3 0.2 1 10 . 9 ALA C C 177.4 0.2 1 11 . 10 ALA N N 125.1 0.1 1 12 . 10 ALA H H 7.94 0.01 1 13 . 10 ALA CA C 51.9 0.2 1 14 . 10 ALA CB C 18.3 0.2 1 15 . 10 ALA C C 177.6 0.2 1 16 . 11 GLN N N 121.2 0.1 1 17 . 11 GLN H H 8.03 0.01 1 18 . 11 GLN CA C 55.4 0.2 1 19 . 11 GLN CB C 28.5 0.2 1 20 . 11 GLN C C 175.6 0.2 1 21 . 12 ASP N N 123.9 0.1 1 22 . 12 ASP H H 8.19 0.01 1 23 . 12 ASP CA C 53.8 0.2 1 24 . 12 ASP CB C 40.3 0.2 1 25 . 12 ASP C C 176.3 0.2 1 26 . 13 VAL N N 121.4 0.1 1 27 . 13 VAL H H 7.85 0.01 1 28 . 13 VAL CA C 61.4 0.2 1 29 . 13 VAL CB C 31.4 0.2 1 30 . 16 PHE N N 115.5 0.1 1 31 . 16 PHE H H 7.87 0.01 1 32 . 16 PHE CA C 58.8 0.2 1 33 . 16 PHE CB C 37.5 0.2 1 34 . 16 PHE C C 177.0 0.2 1 35 . 17 SER N N 117.3 0.1 1 36 . 17 SER H H 7.51 0.01 1 37 . 17 SER CA C 61.1 0.2 1 38 . 17 SER CB C 62.9 0.2 1 39 . 18 GLN N N 119.6 0.1 1 40 . 18 GLN H H 7.84 0.01 1 41 . 18 GLN CA C 54.9 0.2 1 42 . 19 ILE N N 123.3 0.1 1 43 . 19 ILE H H 7.10 0.01 1 44 . 19 ILE CA C 59.4 0.2 1 45 . 20 VAL N N 111.1 0.1 1 46 . 20 VAL H H 7.83 0.01 1 47 . 20 VAL CA C 63.6 0.2 1 48 . 20 VAL CB C 30.4 0.2 1 49 . 21 ALA N N 113.2 0.1 1 50 . 21 ALA H H 8.33 0.01 1 51 . 21 ALA CA C 50.3 0.2 1 52 . 25 LYS N N 115.9 0.1 1 53 . 25 LYS H H 7.82 0.01 1 54 . 25 LYS CA C 59.5 0.2 1 55 . 25 LYS CB C 32.2 0.2 1 56 . 25 LYS C C 180.0 0.2 1 57 . 26 MET N N 120.5 0.1 1 58 . 26 MET H H 7.66 0.01 1 59 . 26 MET CA C 55.3 0.2 1 60 . 26 MET CB C 29.5 0.2 1 61 . 26 MET C C 178.8 0.2 1 62 . 27 LYS N N 122.3 0.1 1 63 . 27 LYS H H 8.32 0.01 1 64 . 27 LYS CA C 60.2 0.2 1 65 . 27 LYS CB C 31.3 0.2 1 66 . 27 LYS C C 179.4 0.2 1 67 . 28 HIS N N 118.4 0.1 1 68 . 28 HIS H H 7.47 0.01 1 69 . 28 HIS CA C 59.0 0.2 1 70 . 28 HIS CB C 29.8 0.2 1 71 . 28 HIS C C 177.4 0.2 1 72 . 29 VAL N N 120.4 0.1 1 73 . 29 VAL H H 7.40 0.01 1 74 . 29 VAL CA C 65.6 0.2 1 75 . 29 VAL CB C 30.5 0.2 1 76 . 29 VAL C C 177.9 0.2 1 77 . 30 VAL H H 8.09 0.01 1 78 . 30 VAL CA C 67.1 0.2 1 79 . 30 VAL CB C 30.4 0.2 1 80 . 30 VAL C C 177.4 0.2 1 81 . 31 GLU N N 121.4 0.1 1 82 . 31 GLU H H 7.51 0.01 1 83 . 31 GLU CA C 59.0 0.2 1 84 . 31 GLU CB C 28.3 0.2 1 85 . 31 GLU C C 180.1 0.2 1 86 . 32 GLN N N 119.7 0.1 1 87 . 32 GLN H H 7.83 0.01 1 88 . 32 GLN CA C 57.8 0.2 1 89 . 32 GLN CB C 28.2 0.2 1 90 . 32 GLN C C 178.6 0.2 1 91 . 33 ALA N N 124.8 0.1 1 92 . 33 ALA H H 8.73 0.01 1 93 . 33 ALA CA C 55.1 0.2 1 94 . 33 ALA CB C 18.6 0.2 1 95 . 33 ALA C C 177.5 0.2 1 96 . 34 GLN N N 116.7 0.1 1 97 . 34 GLN H H 7.60 0.01 1 98 . 34 GLN CA C 58.8 0.2 1 99 . 34 GLN CB C 27.7 0.2 1 100 . 34 GLN C C 178.1 0.2 1 101 . 35 LYS N N 118.5 0.1 1 102 . 35 LYS H H 6.87 0.01 1 103 . 35 LYS CA C 58.3 0.2 1 104 . 35 LYS CB C 31.5 0.2 1 105 . 35 LYS C C 179.9 0.2 1 106 . 36 LEU N N 120.8 0.1 1 107 . 36 LEU H H 8.23 0.01 1 108 . 36 LEU CA C 56.7 0.2 1 109 . 36 LEU CB C 40.4 0.2 1 110 . 36 LEU C C 180.3 0.2 1 111 . 37 ALA N N 123.5 0.1 1 112 . 37 ALA H H 8.61 0.01 1 113 . 37 ALA CA C 54.7 0.2 1 114 . 37 ALA CB C 18.7 0.2 1 115 . 37 ALA C C 177.8 0.2 1 116 . 38 MET N N 110.5 0.1 1 117 . 38 MET H H 6.72 0.01 1 118 . 38 MET CA C 54.8 0.2 1 119 . 38 MET CB C 30.9 0.2 1 120 . 38 MET C C 176.5 0.2 1 121 . 39 LEU N N 120.5 0.1 1 122 . 39 LEU H H 6.84 0.01 1 123 . 39 LEU CA C 53.7 0.2 1 124 . 39 LEU CB C 41.7 0.2 1 125 . 39 LEU C C 174.4 0.2 1 126 . 41 ALA N N 127.3 0.1 1 127 . 41 ALA H H 6.76 0.01 1 128 . 41 ALA CA C 50.4 0.2 1 129 . 41 ALA CB C 16.9 0.2 1 130 . 43 LEU N N 123.6 0.1 1 131 . 43 LEU H H 7.77 0.01 1 132 . 43 LEU CA C 52.6 0.2 1 133 . 43 LEU CB C 45.6 0.2 1 134 . 43 LEU C C 173.7 0.2 1 135 . 44 LEU N N 128.8 0.1 1 136 . 44 LEU H H 8.44 0.01 1 137 . 44 LEU CA C 53.0 0.2 1 138 . 44 LEU CB C 43.3 0.2 1 139 . 44 LEU C C 174.5 0.2 1 140 . 45 ILE N N 129.8 0.1 1 141 . 45 ILE H H 9.23 0.01 1 142 . 45 ILE CA C 59.5 0.2 1 143 . 45 ILE CB C 38.9 0.2 1 144 . 45 ILE C C 175.4 0.2 1 145 . 46 THR N N 120.7 0.1 1 146 . 46 THR H H 8.78 0.01 1 147 . 46 THR CA C 58.8 0.2 1 148 . 46 THR CB C 70.3 0.2 1 149 . 46 THR C C 174.0 0.2 1 150 . 47 GLY N N 110.1 0.1 1 151 . 47 GLY H H 7.58 0.01 1 152 . 47 GLY CA C 45.2 0.2 1 153 . 47 GLY C C 173.4 0.2 1 154 . 48 ASP N N 125.1 0.1 1 155 . 48 ASP H H 9.18 0.01 1 156 . 48 ASP CA C 53.7 0.2 1 157 . 48 ASP CB C 41.1 0.2 1 158 . 49 THR N N 119.4 0.1 1 159 . 49 THR H H 8.72 0.01 1 160 . 49 THR CA C 63.3 0.2 1 161 . 49 THR CB C 68.5 0.2 1 162 . 51 THR N N 112.8 0.1 1 163 . 51 THR H H 7.77 0.01 1 164 . 51 THR CA C 62.3 0.2 1 165 . 51 THR CB C 70.1 0.2 1 166 . 54 ASP N N 117.4 0.1 1 167 . 54 ASP H H 8.48 0.01 1 168 . 55 LEU N N 125.2 0.1 1 169 . 55 LEU H H 7.41 0.01 1 170 . 56 PHE N N 121.2 0.1 1 171 . 56 PHE H H 8.22 0.01 1 172 . 56 PHE CA C 62.4 0.2 1 173 . 57 ALA N N 124.1 0.1 1 174 . 57 ALA H H 8.33 0.01 1 175 . 57 ALA CA C 55.8 0.2 1 176 . 57 ALA CB C 19.7 0.2 1 177 . 57 ALA C C 177.9 0.2 1 178 . 58 TYR N N 118.3 0.1 1 179 . 58 TYR H H 7.10 0.01 1 180 . 58 TYR CA C 59.4 0.2 1 181 . 58 TYR CB C 36.7 0.2 1 182 . 58 TYR C C 177.4 0.2 1 183 . 59 ALA N N 123.2 0.1 1 184 . 59 ALA H H 7.64 0.01 1 185 . 59 ALA CA C 54.4 0.2 1 186 . 59 ALA CB C 16.8 0.2 1 187 . 59 ALA C C 180.5 0.2 1 188 . 60 CYS N N 118.9 0.1 1 189 . 60 CYS H H 8.19 0.01 1 190 . 60 CYS CA C 64.1 0.2 1 191 . 60 CYS CB C 26.7 0.2 1 192 . 60 CYS C C 176.3 0.2 1 193 . 61 HIS N N 120.4 0.1 1 194 . 61 HIS H H 7.34 0.01 1 195 . 61 HIS CA C 60.0 0.2 1 196 . 61 HIS CB C 30.7 0.2 1 197 . 61 HIS C C 179.7 0.2 1 198 . 62 GLN N N 119.8 0.1 1 199 . 62 GLN H H 8.04 0.01 1 200 . 62 GLN CA C 57.5 0.2 1 201 . 62 GLN CB C 28.6 0.2 1 202 . 62 GLN C C 176.0 0.2 1 203 . 63 ALA N N 122.2 0.1 1 204 . 63 ALA H H 7.49 0.01 1 205 . 63 ALA CA C 51.2 0.2 1 206 . 63 ALA CB C 18.7 0.2 1 207 . 63 ALA C C 176.0 0.2 1 208 . 64 SER N N 118.2 0.1 1 209 . 64 SER H H 7.23 0.01 1 210 . 64 SER CA C 57.2 0.2 1 211 . 64 SER CB C 64.8 0.2 1 212 . 66 ARG N N 118.2 0.1 1 213 . 66 ARG H H 7.60 0.01 1 214 . 67 ALA N N 123.4 0.1 1 215 . 67 ALA H H 6.68 0.01 1 216 . 67 ALA CB C 18.5 0.2 1 217 . 69 LYS N N 124.6 0.1 1 218 . 69 LYS H H 8.12 0.01 1 219 . 69 LYS CA C 53.4 0.2 1 220 . 69 LYS CB C 29.6 0.2 1 221 . 71 TYR N N 121.5 0.1 1 222 . 71 TYR H H 7.34 0.01 1 223 . 71 TYR CA C 56.0 0.2 1 224 . 71 TYR CB C 39.7 0.2 1 225 . 71 TYR C C 174.7 0.2 1 226 . 72 LEU N N 129.3 0.1 1 227 . 72 LEU H H 6.85 0.01 1 228 . 72 LEU CA C 52.5 0.2 1 229 . 72 LEU CB C 45.5 0.2 1 230 . 72 LEU C C 173.0 0.2 1 231 . 73 ALA N N 122.2 0.1 1 232 . 73 ALA H H 7.72 0.01 1 233 . 73 ALA CA C 50.0 0.2 1 234 . 73 ALA CB C 22.1 0.2 1 235 . 73 ALA C C 175.7 0.2 1 236 . 74 LEU N N 124.3 0.1 1 237 . 74 LEU H H 8.79 0.01 1 238 . 74 LEU CA C 53.4 0.2 1 239 . 74 LEU CB C 44.5 0.2 1 240 . 74 LEU C C 174.1 0.2 1 241 . 75 ASN N N 124.6 0.1 1 242 . 75 ASN H H 8.47 0.01 1 243 . 75 ASN CA C 51.8 0.2 1 244 . 75 ASN CB C 38.1 0.2 1 245 . 75 ASN C C 176.3 0.2 1 246 . 76 CYS N N 125.7 0.1 1 247 . 76 CYS H H 8.60 0.01 1 248 . 76 CYS CA C 62.4 0.2 1 249 . 76 CYS CB C 26.6 0.2 1 250 . 76 CYS C C 174.5 0.2 1 251 . 77 ALA N N 120.0 0.1 1 252 . 77 ALA H H 8.12 0.01 1 253 . 77 ALA CA C 52.4 0.2 1 254 . 77 ALA CB C 18.6 0.2 1 255 . 77 ALA C C 178.5 0.2 1 256 . 78 SER N N 113.3 0.1 1 257 . 78 SER H H 7.34 0.01 1 258 . 78 SER CA C 58.5 0.2 1 259 . 78 SER CB C 63.8 0.2 1 260 . 78 SER C C 173.5 0.2 1 261 . 79 ILE N N 122.0 0.1 1 262 . 79 ILE H H 6.68 0.01 1 263 . 79 ILE CA C 57.1 0.2 1 264 . 79 ILE CB C 38.4 0.2 1 265 . 81 GLU N N 125.2 0.1 1 266 . 81 GLU H H 8.60 0.01 1 267 . 81 GLU CA C 58.8 0.2 1 268 . 81 GLU CB C 28.6 0.2 1 269 . 81 GLU C C 178.1 0.2 1 270 . 82 ASP N N 116.8 0.1 1 271 . 82 ASP H H 8.40 0.01 1 272 . 82 ASP CA C 55.2 0.2 1 273 . 82 ASP CB C 39.2 0.2 1 274 . 82 ASP C C 176.7 0.2 1 275 . 83 ALA N N 123.7 0.1 1 276 . 83 ALA H H 7.52 0.01 1 277 . 83 ALA CA C 51.9 0.2 1 278 . 83 ALA CB C 19.4 0.2 1 279 . 83 ALA C C 178.3 0.2 1 280 . 84 VAL N N 121.4 0.1 1 281 . 84 VAL H H 7.15 0.01 1 282 . 84 VAL CA C 66.4 0.2 1 283 . 84 VAL CB C 30.7 0.2 1 284 . 84 VAL C C 176.0 0.2 1 285 . 85 GLU N N 122.5 0.1 1 286 . 85 GLU H H 8.36 0.01 1 287 . 85 GLU CA C 60.1 0.2 1 288 . 85 GLU CB C 28.9 0.2 1 289 . 85 GLU C C 178.3 0.2 1 290 . 86 SER N N 115.1 0.1 1 291 . 86 SER H H 7.83 0.01 1 292 . 86 SER CA C 60.2 0.2 1 293 . 86 SER CB C 62.4 0.2 1 294 . 86 SER C C 177.4 0.2 1 295 . 87 GLU N N 122.6 0.1 1 296 . 87 GLU H H 7.89 0.01 1 297 . 87 GLU CA C 57.9 0.2 1 298 . 87 GLU CB C 28.5 0.2 1 299 . 87 GLU C C 178.7 0.2 1 300 . 88 LEU N N 116.8 0.1 1 301 . 88 LEU H H 7.68 0.01 1 302 . 88 LEU CA C 57.1 0.2 1 303 . 88 LEU CB C 40.2 0.2 1 304 . 88 LEU C C 177.6 0.2 1 305 . 89 PHE N N 117.3 0.1 1 306 . 89 PHE H H 8.20 0.01 1 307 . 89 PHE CA C 56.1 0.2 1 308 . 89 PHE CB C 38.4 0.2 1 309 . 89 PHE C C 175.9 0.2 1 310 . 90 GLY N N 110.8 0.1 1 311 . 90 GLY H H 7.50 0.01 1 312 . 90 GLY CA C 44.3 0.2 1 313 . 90 GLY C C 172.1 0.2 1 314 . 91 HIS N N 120.5 0.1 1 315 . 91 HIS H H 8.24 0.01 1 316 . 91 HIS CA C 55.9 0.2 1 317 . 91 HIS CB C 33.2 0.2 1 318 . 91 HIS C C 175.4 0.2 1 319 . 92 ALA N N 110.8 0.1 1 320 . 92 ALA H H 8.87 0.01 1 321 . 92 ALA CA C 55.7 0.2 1 322 . 92 ALA CB C 15.5 0.2 1 323 . 94 GLU N N 114.6 0.1 1 324 . 94 GLU H H 7.79 0.01 1 325 . 94 GLU CA C 55.8 0.2 1 326 . 94 GLU CB C 29.3 0.2 1 327 . 94 GLU C C 177.0 0.2 1 328 . 95 GLY N N 112.5 0.1 1 329 . 95 GLY H H 8.03 0.01 1 330 . 95 GLY CA C 46.0 0.2 1 331 . 95 GLY C C 174.4 0.2 1 332 . 96 LYS N N 121.8 0.1 1 333 . 96 LYS H H 7.68 0.01 1 334 . 96 LYS CA C 54.7 0.2 1 335 . 96 LYS CB C 33.6 0.2 1 336 . 97 LYS N N 110.4 0.1 1 337 . 97 LYS H H 8.77 0.01 1 338 . 97 LYS CB C 32.6 0.2 1 339 . 98 GLY N N 114.4 0.1 1 340 . 98 GLY H H 9.18 0.01 1 341 . 98 GLY CA C 44.2 0.2 1 342 . 98 GLY C C 173.9 0.2 1 343 . 99 PHE N N 122.2 0.1 1 344 . 99 PHE H H 8.73 0.01 1 345 . 99 PHE CA C 59.3 0.2 1 346 . 99 PHE CB C 38.8 0.2 1 347 . 100 PHE N N 115.0 0.1 1 348 . 100 PHE H H 7.48 0.01 1 349 . 101 GLU N N 117.1 0.1 1 350 . 101 GLU H H 7.74 0.01 1 351 . 101 GLU CA C 59.2 0.2 1 352 . 101 GLU CB C 29.5 0.2 1 353 . 102 GLN N N 120.1 0.1 1 354 . 102 GLN H H 8.04 0.01 1 355 . 102 GLN CA C 58.3 0.2 1 356 . 102 GLN CB C 29.3 0.2 1 357 . 102 GLN C C 177.4 0.2 1 358 . 103 ALA N N 120.5 0.1 1 359 . 103 ALA H H 7.49 0.01 1 360 . 103 ALA CA C 50.4 0.2 1 361 . 103 ALA CB C 17.7 0.2 1 362 . 103 ALA C C 175.1 0.2 1 363 . 104 ASN N N 117.6 0.1 1 364 . 104 ASN H H 6.55 0.01 1 365 . 104 ASN CA C 55.6 0.2 1 366 . 104 ASN CB C 37.9 0.2 1 367 . 104 ASN C C 175.8 0.2 1 368 . 105 GLY N N 119.6 0.1 1 369 . 105 GLY H H 8.82 0.01 1 370 . 105 GLY CA C 45.0 0.2 1 371 . 105 GLY C C 173.7 0.2 1 372 . 106 GLY N N 113.0 0.1 1 373 . 106 GLY H H 9.19 0.01 1 374 . 106 GLY CA C 43.7 0.2 1 375 . 106 GLY C C 174.4 0.2 1 376 . 107 SER N N 120.6 0.1 1 377 . 107 SER H H 8.51 0.01 1 378 . 107 SER CA C 56.7 0.2 1 379 . 107 SER CB C 63.4 0.2 1 380 . 107 SER C C 171.3 0.2 1 381 . 108 VAL N N 118.9 0.1 1 382 . 108 VAL H H 7.97 0.01 1 383 . 108 VAL CA C 57.8 0.2 1 384 . 108 VAL CB C 35.4 0.2 1 385 . 108 VAL C C 173.4 0.2 1 386 . 109 LEU N N 126.3 0.1 1 387 . 109 LEU H H 8.10 0.01 1 388 . 109 LEU CA C 52.2 0.2 1 389 . 109 LEU CB C 42.4 0.2 1 390 . 109 LEU C C 175.2 0.2 1 391 . 110 LEU N N 128.5 0.1 1 392 . 110 LEU H H 9.14 0.01 1 393 . 110 LEU CA C 52.3 0.2 1 394 . 110 LEU CB C 40.9 0.2 1 395 . 110 LEU C C 174.5 0.2 1 396 . 111 ASP N N 125.1 0.1 1 397 . 111 ASP H H 8.72 0.01 1 398 . 111 ASP CA C 52.8 0.2 1 399 . 111 ASP CB C 41.5 0.2 1 400 . 111 ASP C C 175.4 0.2 1 401 . 112 GLU N N 126.5 0.1 1 402 . 112 GLU H H 8.23 0.01 1 403 . 112 GLU CA C 56.3 0.2 1 404 . 112 GLU CB C 26.3 0.2 1 405 . 112 GLU C C 176.8 0.2 1 406 . 113 ILE N N 117.9 0.1 1 407 . 113 ILE H H 7.55 0.01 1 408 . 113 ILE CA C 60.6 0.2 1 409 . 113 ILE C C 175.7 0.2 1 410 . 114 GLY N N 109.8 0.1 1 411 . 114 GLY H H 8.53 0.01 1 412 . 114 GLY CA C 45.7 0.2 1 413 . 114 GLY C C 173.8 0.2 1 414 . 115 GLU N N 117.3 0.1 1 415 . 115 GLU H H 7.70 0.01 1 416 . 115 GLU CA C 54.5 0.2 1 417 . 115 GLU CB C 28.0 0.2 1 418 . 115 GLU C C 177.2 0.2 1 419 . 116 MET N N 122.3 0.1 1 420 . 116 MET H H 7.47 0.01 1 421 . 116 MET CA C 56.4 0.2 1 422 . 116 MET CB C 33.9 0.2 1 423 . 116 MET C C 176.7 0.2 1 424 . 117 SER N N 128.0 0.1 1 425 . 117 SER H H 9.45 0.01 1 426 . 117 SER CA C 56.7 0.2 1 427 . 117 SER CB C 61.8 0.2 1 428 . 119 ARG N N 120.7 0.1 1 429 . 119 ARG H H 8.34 0.01 1 430 . 119 ARG CA C 59.0 0.2 1 431 . 119 ARG C C 179.3 0.2 1 432 . 120 MET N N 121.4 0.1 1 433 . 120 MET H H 7.54 0.01 1 434 . 120 MET CA C 55.5 0.2 1 435 . 120 MET CB C 29.4 0.2 1 436 . 120 MET C C 178.7 0.2 1 437 . 121 GLN N N 122.6 0.1 1 438 . 121 GLN H H 8.72 0.01 1 439 . 121 GLN CA C 58.7 0.2 1 440 . 121 GLN CB C 28.3 0.2 1 441 . 121 GLN C C 178.3 0.2 1 442 . 122 ALA N N 120.4 0.1 1 443 . 122 ALA H H 7.24 0.01 1 444 . 122 ALA CA C 54.8 0.2 1 445 . 122 ALA CB C 17.3 0.2 1 446 . 122 ALA C C 180.2 0.2 1 447 . 123 LYS N N 120.4 0.1 1 448 . 123 LYS H H 7.27 0.01 1 449 . 123 LYS CA C 59.0 0.2 1 450 . 123 LYS CB C 32.0 0.2 1 451 . 123 LYS C C 180.0 0.2 1 452 . 124 LEU N N 124.2 0.1 1 453 . 124 LEU H H 8.95 0.01 1 454 . 124 LEU CA C 57.3 0.2 1 455 . 124 LEU CB C 40.5 0.2 1 456 . 124 LEU C C 177.8 0.2 1 457 . 125 LEU N N 121.3 0.1 1 458 . 125 LEU H H 8.00 0.01 1 459 . 125 LEU CA C 57.7 0.2 1 460 . 125 LEU CB C 40.5 0.2 1 461 . 125 LEU C C 177.6 0.2 1 462 . 126 ARG N N 118.7 0.1 1 463 . 126 ARG H H 7.24 0.01 1 464 . 126 ARG CA C 59.0 0.2 1 465 . 126 ARG CB C 28.4 0.2 1 466 . 126 ARG C C 178.1 0.2 1 467 . 127 PHE N N 120.8 0.1 1 468 . 127 PHE H H 7.64 0.01 1 469 . 127 PHE CA C 60.7 0.2 1 470 . 127 PHE CB C 38.2 0.2 1 471 . 127 PHE C C 178.9 0.2 1 472 . 128 LEU N N 122.3 0.1 1 473 . 128 LEU H H 8.57 0.01 1 474 . 128 LEU CA C 56.7 0.2 1 475 . 128 LEU CB C 40.2 0.2 1 476 . 128 LEU C C 178.3 0.2 1 477 . 129 ASN N N 118.7 0.1 1 478 . 129 ASN H H 7.84 0.01 1 479 . 129 ASN CA C 54.8 0.2 1 480 . 129 ASN CB C 38.0 0.2 1 481 . 129 ASN C C 176.9 0.2 1 482 . 130 ASP N N 119.0 0.1 1 483 . 130 ASP H H 8.24 0.01 1 484 . 130 ASP CA C 54.5 0.2 1 485 . 130 ASP CB C 41.8 0.2 1 486 . 130 ASP C C 177.4 0.2 1 487 . 131 GLY N N 111.7 0.1 1 488 . 131 GLY H H 8.29 0.01 1 489 . 131 GLY CA C 45.8 0.2 1 490 . 131 GLY C C 172.6 0.2 1 491 . 132 THR N N 128.3 0.1 1 492 . 132 THR H H 6.99 0.01 1 493 . 132 THR CA C 58.1 0.2 1 494 . 132 THR CB C 72.5 0.2 1 495 . 132 THR C C 173.9 0.2 1 496 . 133 PHE N N 116.3 0.1 1 497 . 133 PHE H H 7.86 0.01 1 498 . 133 PHE CA C 55.4 0.2 1 499 . 133 PHE CB C 41.0 0.2 1 500 . 133 PHE C C 172.0 0.2 1 501 . 134 ARG N N 118.8 0.1 1 502 . 134 ARG H H 7.54 0.01 1 503 . 134 ARG CA C 53.9 0.2 1 504 . 134 ARG CB C 31.4 0.2 1 505 . 134 ARG C C 176.7 0.2 1 506 . 135 ARG N N 126.6 0.1 1 507 . 135 ARG H H 9.55 0.01 1 508 . 135 ARG CA C 55.4 0.2 1 509 . 135 ARG CB C 30.1 0.2 1 510 . 135 ARG C C 177.3 0.2 1 511 . 136 VAL N N 123.5 0.1 1 512 . 136 VAL H H 7.79 0.01 1 513 . 136 VAL CA C 65.0 0.2 1 514 . 136 VAL CB C 30.1 0.2 1 515 . 136 VAL C C 177.6 0.2 1 516 . 137 GLY N N 115.1 0.1 1 517 . 137 GLY H H 8.35 0.01 1 518 . 137 GLY CA C 44.7 0.2 1 519 . 137 GLY C C 173.9 0.2 1 520 . 138 GLU N N 121.8 0.1 1 521 . 138 GLU H H 7.65 0.01 1 522 . 138 GLU CA C 54.7 0.2 1 523 . 138 GLU CB C 32.9 0.2 1 524 . 140 HIS N N 118.6 0.1 1 525 . 140 HIS H H 6.81 0.01 1 526 . 140 HIS CA C 54.7 0.2 1 527 . 140 HIS CB C 31.3 0.2 1 528 . 140 HIS C C 173.8 0.2 1 529 . 141 GLU N N 122.8 0.1 1 530 . 141 GLU H H 8.18 0.01 1 531 . 141 GLU CA C 55.6 0.2 1 532 . 141 GLU CB C 30.3 0.2 1 533 . 141 GLU C C 175.7 0.2 1 534 . 142 VAL N N 126.0 0.1 1 535 . 142 VAL H H 8.52 0.01 1 536 . 142 VAL CA C 60.8 0.2 1 537 . 142 VAL CB C 32.2 0.2 1 538 . 142 VAL C C 173.9 0.2 1 539 . 143 HIS N N 124.5 0.1 1 540 . 143 HIS H H 8.01 0.01 1 541 . 143 HIS CA C 54.5 0.2 1 542 . 143 HIS CB C 30.7 0.2 1 543 . 143 HIS C C 175.4 0.2 1 544 . 144 VAL N N 118.3 0.1 1 545 . 144 VAL H H 7.72 0.01 1 546 . 144 VAL CA C 59.2 0.2 1 547 . 144 VAL CB C 35.8 0.2 1 548 . 144 VAL C C 173.3 0.2 1 549 . 145 ASP N N 123.1 0.1 1 550 . 145 ASP H H 8.03 0.01 1 551 . 145 ASP CA C 51.8 0.2 1 552 . 145 ASP CB C 40.8 0.2 1 553 . 145 ASP C C 175.7 0.2 1 554 . 146 VAL N N 126.1 0.1 1 555 . 146 VAL H H 8.35 0.01 1 556 . 146 VAL CA C 59.9 0.2 1 557 . 146 VAL CB C 36.2 0.2 1 558 . 146 VAL C C 173.5 0.2 1 559 . 147 ARG N N 111.6 0.1 1 560 . 147 ARG H H 8.54 0.01 1 561 . 147 ARG CA C 55.9 0.2 1 562 . 147 ARG CB C 29.2 0.2 1 563 . 147 ARG C C 175.3 0.2 1 564 . 148 VAL N N 110.7 0.1 1 565 . 148 VAL H H 8.96 0.01 1 566 . 148 VAL CA C 62.5 0.2 1 567 . 148 VAL CB C 32.1 0.2 1 568 . 148 VAL C C 173.4 0.2 1 569 . 149 ILE N N 110.3 0.1 1 570 . 149 ILE H H 8.97 0.01 1 571 . 149 ILE CA C 59.3 0.2 1 572 . 149 ILE CB C 39.0 0.2 1 573 . 149 ILE C C 175.1 0.2 1 574 . 150 CYS N N 124.9 0.1 1 575 . 150 CYS H H 9.45 0.01 1 576 . 150 CYS CA C 56.3 0.2 1 577 . 150 CYS CB C 31.3 0.2 1 578 . 150 CYS C C 172.8 0.2 1 579 . 151 ALA N N 124.5 0.1 1 580 . 151 ALA H H 8.35 0.01 1 581 . 151 ALA CA C 49.7 0.2 1 582 . 151 ALA CB C 22.0 0.2 1 583 . 151 ALA C C 176.1 0.2 1 584 . 152 THR N N 114.4 0.1 1 585 . 152 THR H H 8.04 0.01 1 586 . 152 THR CA C 60.0 0.2 1 587 . 152 THR CB C 70.3 0.2 1 588 . 152 THR C C 171.6 0.2 1 589 . 153 GLN N N 127.6 0.1 1 590 . 153 GLN H H 8.73 0.01 1 591 . 153 GLN CA C 54.9 0.2 1 592 . 153 GLN CB C 29.5 0.2 1 593 . 153 GLN C C 176.7 0.2 1 594 . 154 LYS N N 123.4 0.1 1 595 . 154 LYS H H 8.28 0.01 1 596 . 154 LYS CA C 54.6 0.2 1 597 . 154 LYS CB C 33.1 0.2 1 598 . 156 LEU N N 128.1 0.1 1 599 . 156 LEU H H 8.54 0.01 1 600 . 156 LEU CA C 57.1 0.2 1 601 . 156 LEU CB C 40.6 0.2 1 602 . 156 LEU C C 178.1 0.2 1 603 . 157 VAL N N 119.8 0.1 1 604 . 157 VAL H H 7.61 0.01 1 605 . 157 VAL CA C 65.4 0.2 1 606 . 157 VAL CB C 30.0 0.2 1 607 . 157 VAL C C 177.8 0.2 1 608 . 158 GLU N N 121.7 0.1 1 609 . 158 GLU H H 6.80 0.01 1 610 . 158 GLU CA C 58.2 0.2 1 611 . 158 GLU CB C 28.6 0.2 1 612 . 158 GLU C C 178.8 0.2 1 613 . 159 LEU N N 119.1 0.1 1 614 . 159 LEU H H 6.83 0.01 1 615 . 159 LEU CA C 57.3 0.2 1 616 . 159 LEU CB C 40.9 0.2 1 617 . 159 LEU C C 180.0 0.2 1 618 . 160 VAL N N 124.1 0.1 1 619 . 160 VAL H H 8.03 0.01 1 620 . 160 VAL CA C 64.5 0.2 1 621 . 160 VAL CB C 30.8 0.2 1 622 . 160 VAL C C 181.1 0.2 1 623 . 161 GLN N N 122.7 0.1 1 624 . 161 GLN H H 7.92 0.01 1 625 . 161 GLN CA C 58.3 0.2 1 626 . 161 GLN CB C 27.2 0.2 1 627 . 161 GLN C C 178.0 0.2 1 628 . 162 LYS N N 117.2 0.1 1 629 . 162 LYS H H 7.33 0.01 1 630 . 162 LYS CA C 56.0 0.2 1 631 . 162 LYS CB C 32.7 0.2 1 632 . 162 LYS C C 176.7 0.2 1 633 . 163 GLY N N 107.8 0.1 1 634 . 163 GLY H H 7.74 0.01 1 635 . 163 GLY CA C 45.4 0.2 1 636 . 163 GLY C C 175.0 0.2 1 637 . 164 MET N N 118.1 0.1 1 638 . 164 MET H H 7.89 0.01 1 639 . 164 MET CA C 55.2 0.2 1 640 . 164 MET CB C 33.7 0.2 1 641 . 164 MET C C 174.5 0.2 1 642 . 165 PHE N N 122.8 0.1 1 643 . 165 PHE H H 6.87 0.01 1 644 . 165 PHE CA C 55.7 0.2 1 645 . 165 PHE CB C 42.9 0.2 1 646 . 165 PHE C C 174.1 0.2 1 647 . 166 ARG N N 128.6 0.1 1 648 . 166 ARG H H 7.68 0.01 1 649 . 166 ARG CA C 56.8 0.2 1 650 . 166 ARG CB C 31.9 0.2 1 651 . 166 ARG C C 176.9 0.2 1 652 . 167 GLU N N 127.2 0.1 1 653 . 167 GLU H H 8.73 0.01 1 654 . 167 GLU CA C 59.3 0.2 1 655 . 167 GLU CB C 29.3 0.2 1 656 . 167 GLU C C 176.8 0.2 1 657 . 168 ASP N N 118.7 0.1 1 658 . 168 ASP H H 8.26 0.01 1 659 . 168 ASP CA C 55.7 0.2 1 660 . 168 ASP CB C 37.2 0.2 1 661 . 168 ASP C C 179.8 0.2 1 662 . 169 LEU N N 126.1 0.1 1 663 . 169 LEU H H 7.82 0.01 1 664 . 169 LEU CA C 56.7 0.2 1 665 . 169 LEU CB C 41.2 0.2 1 666 . 169 LEU C C 177.3 0.2 1 667 . 170 TYR N N 121.9 0.1 1 668 . 170 TYR H H 8.11 0.01 1 669 . 170 TYR CA C 61.8 0.2 1 670 . 170 TYR CB C 37.4 0.2 1 671 . 170 TYR C C 176.5 0.2 1 672 . 171 TYR N N 117.8 0.1 1 673 . 171 TYR H H 8.16 0.01 1 674 . 171 TYR CA C 60.2 0.2 1 675 . 171 TYR CB C 36.5 0.2 1 676 . 171 TYR C C 178.6 0.2 1 677 . 172 ARG N N 119.6 0.1 1 678 . 172 ARG H H 7.34 0.01 1 679 . 172 ARG CA C 56.2 0.2 1 680 . 172 ARG CB C 29.2 0.2 1 681 . 172 ARG C C 177.4 0.2 1 682 . 173 LEU N N 117.7 0.1 1 683 . 173 LEU H H 7.53 0.01 1 684 . 173 LEU CA C 55.1 0.2 1 685 . 173 LEU CB C 41.9 0.2 1 686 . 173 LEU C C 176.5 0.2 1 687 . 174 ASN N N 116.1 0.1 1 688 . 174 ASN H H 7.43 0.01 1 689 . 174 ASN CA C 52.5 0.2 1 690 . 174 ASN CB C 37.9 0.2 1 691 . 174 ASN C C 175.6 0.2 1 692 . 175 VAL N N 121.4 0.1 1 693 . 175 VAL H H 6.70 0.01 1 694 . 175 VAL CA C 65.3 0.2 1 695 . 175 VAL CB C 31.2 0.2 1 696 . 175 VAL C C 176.3 0.2 1 697 . 176 LEU N N 122.5 0.1 1 698 . 176 LEU H H 8.05 0.01 1 699 . 176 LEU CA C 52.9 0.2 1 700 . 176 LEU CB C 40.8 0.2 1 701 . 176 LEU C C 174.0 0.2 1 702 . 177 THR N N 115.7 0.1 1 703 . 177 THR H H 7.65 0.01 1 704 . 177 THR CA C 59.1 0.2 1 705 . 177 THR CB C 71.3 0.2 1 706 . 177 THR C C 173.1 0.2 1 707 . 178 LEU N N 126.4 0.1 1 708 . 178 LEU H H 8.61 0.01 1 709 . 178 LEU CA C 52.8 0.2 1 710 . 178 LEU CB C 44.5 0.2 1 711 . 178 LEU C C 173.8 0.2 1 712 . 179 ASN N N 124.8 0.1 1 713 . 179 ASN H H 8.51 0.01 1 714 . 179 ASN CA C 50.9 0.2 1 715 . 179 ASN CB C 39.2 0.2 1 716 . 179 ASN C C 174.0 0.2 1 717 . 180 LEU N N 127.1 0.1 1 718 . 180 LEU H H 8.67 0.01 1 719 . 180 LEU CA C 51.8 0.2 1 720 . 180 LEU CB C 38.7 0.2 1 721 . 183 LEU N N 127.4 0.1 1 722 . 183 LEU H H 8.83 0.01 1 723 . 183 LEU CA C 57.6 0.2 1 724 . 183 LEU CB C 41.7 0.2 1 725 . 183 LEU C C 179.5 0.2 1 726 . 184 ARG N N 116.7 0.1 1 727 . 184 ARG H H 8.97 0.01 1 728 . 184 ARG CA C 57.0 0.2 1 729 . 184 ARG CB C 26.8 0.2 1 730 . 184 ARG C C 177.0 0.2 1 731 . 185 ASP N N 121.3 0.1 1 732 . 185 ASP H H 7.32 0.01 1 733 . 185 ASP CA C 54.0 0.2 1 734 . 185 ASP CB C 41.1 0.2 1 735 . 186 CYS N N 122.6 0.1 1 736 . 186 CYS H H 7.97 0.01 1 737 . 186 CYS CA C 56.2 0.2 1 738 . 188 GLN N N 118.4 0.1 1 739 . 188 GLN H H 8.71 0.01 1 740 . 188 GLN CA C 58.2 0.2 1 741 . 188 GLN CB C 27.0 0.2 1 742 . 188 GLN C C 176.1 0.2 1 743 . 189 ASP N N 116.5 0.1 1 744 . 189 ASP H H 7.88 0.01 1 745 . 189 ASP CA C 55.2 0.2 1 746 . 189 ASP CB C 40.9 0.2 1 747 . 189 ASP C C 177.5 0.2 1 748 . 190 ILE N N 121.5 0.1 1 749 . 190 ILE H H 7.09 0.01 1 750 . 190 ILE CA C 66.5 0.2 1 751 . 190 ILE CB C 36.6 0.2 1 752 . 190 ILE C C 178.3 0.2 1 753 . 191 MET N N 122.0 0.1 1 754 . 191 MET H H 9.26 0.01 1 755 . 191 MET CA C 56.8 0.2 1 756 . 191 MET CB C 24.9 0.2 1 757 . 194 THR N N 119.6 0.1 1 758 . 194 THR H H 7.96 0.01 1 759 . 194 THR CA C 68.4 0.2 1 760 . 194 THR CB C 67.2 0.2 1 761 . 194 THR C C 176.2 0.2 1 762 . 195 GLU N N 120.7 0.1 1 763 . 195 GLU H H 8.39 0.01 1 764 . 195 GLU CA C 59.8 0.2 1 765 . 195 GLU CB C 29.0 0.2 1 766 . 195 GLU C C 179.3 0.2 1 767 . 196 LEU N N 123.5 0.1 1 768 . 196 LEU H H 7.39 0.01 1 769 . 196 LEU CA C 57.7 0.2 1 770 . 196 LEU CB C 40.9 0.2 1 771 . 196 LEU C C 179.6 0.2 1 772 . 197 PHE N N 120.7 0.1 1 773 . 197 PHE H H 8.40 0.01 1 774 . 197 PHE CA C 59.0 0.2 1 775 . 197 PHE CB C 37.2 0.2 1 776 . 197 PHE C C 178.1 0.2 1 777 . 198 VAL N N 121.6 0.1 1 778 . 198 VAL H H 8.59 0.01 1 779 . 198 VAL CA C 66.1 0.2 1 780 . 198 VAL CB C 30.5 0.2 1 781 . 198 VAL C C 177.0 0.2 1 782 . 199 ALA N N 122.1 0.1 1 783 . 199 ALA H H 7.53 0.01 1 784 . 199 ALA CA C 54.9 0.2 1 785 . 199 ALA CB C 16.9 0.2 1 786 . 199 ALA C C 179.8 0.2 1 787 . 200 ARG N N 119.8 0.1 1 788 . 200 ARG H H 8.25 0.01 1 789 . 200 ARG CA C 58.7 0.2 1 790 . 200 ARG CB C 29.5 0.2 1 791 . 200 ARG C C 178.7 0.2 1 792 . 201 PHE N N 121.9 0.1 1 793 . 201 PHE H H 8.39 0.01 1 794 . 201 PHE CA C 60.4 0.2 1 795 . 201 PHE CB C 38.5 0.2 1 796 . 201 PHE C C 177.6 0.2 1 797 . 202 ALA N N 123.2 0.1 1 798 . 202 ALA H H 8.06 0.01 1 799 . 202 ALA CA C 54.9 0.2 1 800 . 202 ALA CB C 17.1 0.2 1 801 . 202 ALA C C 179.8 0.2 1 802 . 203 ASP N N 119.3 0.1 1 803 . 203 ASP H H 7.84 0.01 1 804 . 203 ASP CA C 56.6 0.2 1 805 . 203 ASP CB C 40.0 0.2 1 806 . 203 ASP C C 179.4 0.2 1 807 . 204 GLU N N 121.4 0.1 1 808 . 204 GLU H H 8.22 0.01 1 809 . 204 GLU CA C 58.7 0.2 1 810 . 204 GLU CB C 29.1 0.2 1 811 . 204 GLU C C 178.9 0.2 1 812 . 205 GLN N N 116.4 0.1 1 813 . 205 GLN H H 7.85 0.01 1 814 . 205 GLN CA C 55.0 0.2 1 815 . 205 GLN CB C 28.5 0.2 1 816 . 205 GLN C C 176.6 0.2 1 817 . 206 GLY N N 111.9 0.1 1 818 . 206 GLY H H 7.66 0.01 1 819 . 206 GLY CA C 46.3 0.2 1 820 . 206 GLY C C 175.0 0.2 1 821 . 207 VAL N N 114.9 0.1 1 822 . 207 VAL H H 7.59 0.01 1 823 . 207 VAL CA C 57.3 0.2 1 824 . 207 VAL CB C 31.5 0.2 1 825 . 209 LEU N N 120.8 0.1 1 826 . 209 LEU H H 7.96 0.01 1 827 . 209 LEU CA C 57.6 0.2 1 828 . 209 LEU CB C 41.9 0.2 1 829 . 211 LYS N N 120.6 0.1 1 830 . 211 LYS H H 7.83 0.01 1 831 . 211 LYS CA C 55.0 0.2 1 832 . 211 LYS CB C 32.9 0.2 1 833 . 211 LYS C C 175.5 0.2 1 834 . 212 LEU N N 124.2 0.1 1 835 . 212 LEU H H 8.47 0.01 1 836 . 212 LEU CA C 53.8 0.2 1 837 . 212 LEU CB C 39.8 0.2 1 838 . 212 LEU C C 176.7 0.2 1 839 . 213 ALA N N 128.5 0.1 1 840 . 213 ALA H H 8.18 0.01 1 841 . 213 ALA CA C 52.1 0.2 1 842 . 213 ALA CB C 20.4 0.2 1 843 . 213 ALA C C 179.1 0.2 1 844 . 214 ALA N N 126.5 0.1 1 845 . 214 ALA H H 8.75 0.01 1 846 . 214 ALA CA C 54.3 0.2 1 847 . 214 ALA CB C 17.3 0.2 1 848 . 214 ALA C C 178.9 0.2 1 849 . 215 ASP N N 114.1 0.1 1 850 . 215 ASP H H 8.44 0.01 1 851 . 215 ASP CA C 53.2 0.2 1 852 . 215 ASP CB C 39.0 0.2 1 853 . 215 ASP C C 177.3 0.2 1 854 . 216 LEU N N 122.5 0.1 1 855 . 216 LEU H H 7.56 0.01 1 856 . 216 LEU CA C 58.0 0.2 1 857 . 216 LEU CB C 41.4 0.2 1 858 . 216 LEU C C 178.0 0.2 1 859 . 217 ASN N N 116.8 0.1 1 860 . 217 ASN H H 8.37 0.01 1 861 . 217 ASN CA C 56.9 0.2 1 862 . 217 ASN CB C 37.4 0.2 1 863 . 217 ASN C C 178.6 0.2 1 864 . 218 THR N N 116.7 0.1 1 865 . 218 THR H H 7.61 0.01 1 866 . 218 THR CA C 65.0 0.2 1 867 . 218 THR CB C 68.3 0.2 1 868 . 218 THR C C 175.3 0.2 1 869 . 219 VAL N N 119.4 0.1 1 870 . 219 VAL H H 7.00 0.01 1 871 . 219 VAL CA C 64.7 0.2 1 872 . 219 VAL CB C 31.8 0.2 1 873 . 219 VAL C C 178.6 0.2 1 874 . 220 LEU N N 117.8 0.1 1 875 . 220 LEU H H 8.05 0.01 1 876 . 220 LEU CA C 57.7 0.2 1 877 . 220 LEU CB C 40.6 0.2 1 878 . 220 LEU C C 179.5 0.2 1 879 . 221 THR N N 128.4 0.1 1 880 . 221 THR H H 7.80 0.01 1 881 . 221 THR CA C 63.8 0.2 1 882 . 221 THR CB C 69.0 0.2 1 883 . 221 THR C C 175.7 0.2 1 884 . 222 ARG N N 121.1 0.1 1 885 . 222 ARG H H 6.93 0.01 1 886 . 222 ARG CA C 55.8 0.2 1 887 . 222 ARG CB C 30.1 0.2 1 888 . 222 ARG C C 175.8 0.2 1 889 . 223 TYR N N 122.5 0.1 1 890 . 223 TYR H H 6.61 0.01 1 891 . 223 TYR CA C 56.5 0.2 1 892 . 223 TYR CB C 38.2 0.2 1 893 . 223 TYR C C 174.5 0.2 1 894 . 224 ALA N N 126.3 0.1 1 895 . 224 ALA H H 6.70 0.01 1 896 . 224 ALA CA C 53.0 0.2 1 897 . 224 ALA CB C 18.6 0.2 1 898 . 224 ALA C C 176.4 0.2 1 899 . 225 TRP N N 111.2 0.1 1 900 . 225 TRP H H 5.16 0.01 1 901 . 225 TRP CA C 55.3 0.2 1 902 . 225 TRP C C 177.5 0.2 1 903 . 227 GLY N N 126.2 0.1 1 904 . 227 GLY H H 8.22 0.01 1 905 . 227 GLY CA C 45.1 0.2 1 906 . 227 GLY C C 175.2 0.2 1 907 . 228 ASN N N 120.5 0.1 1 908 . 228 ASN H H 8.80 0.01 1 909 . 228 ASN CA C 56.4 0.2 1 910 . 228 ASN CB C 38.8 0.2 1 911 . 228 ASN C C 172.7 0.2 1 912 . 229 VAL N N 122.8 0.1 1 913 . 229 VAL H H 7.05 0.01 1 914 . 229 VAL CA C 66.1 0.2 1 915 . 229 VAL CB C 30.7 0.2 1 916 . 229 VAL C C 176.6 0.2 1 917 . 230 ARG N N 121.8 0.1 1 918 . 230 ARG H H 8.02 0.01 1 919 . 230 ARG CA C 59.2 0.2 1 920 . 230 ARG CB C 29.4 0.2 1 921 . 230 ARG C C 177.5 0.2 1 922 . 231 GLN N N 120.6 0.1 1 923 . 231 GLN H H 7.03 0.01 1 924 . 231 GLN CA C 58.3 0.2 1 925 . 231 GLN CB C 26.7 0.2 1 926 . 231 GLN C C 178.4 0.2 1 927 . 232 LEU N N 124.7 0.1 1 928 . 232 LEU H H 7.41 0.01 1 929 . 232 LEU CA C 58.4 0.2 1 930 . 232 LEU CB C 39.7 0.2 1 931 . 232 LEU C C 177.2 0.2 1 932 . 233 LYS N N 121.0 0.1 1 933 . 233 LYS H H 8.22 0.01 1 934 . 233 LYS CA C 59.9 0.2 1 935 . 233 LYS CB C 30.7 0.2 1 936 . 233 LYS C C 178.4 0.2 1 937 . 234 ASN N N 117.1 0.1 1 938 . 234 ASN H H 7.85 0.01 1 939 . 234 ASN CA C 55.5 0.2 1 940 . 234 ASN CB C 37.6 0.2 1 941 . 234 ASN C C 177.9 0.2 1 942 . 235 ALA N N 125.4 0.1 1 943 . 235 ALA H H 8.49 0.01 1 944 . 235 ALA CA C 54.5 0.2 1 945 . 235 ALA CB C 16.7 0.2 1 946 . 235 ALA C C 181.2 0.2 1 947 . 236 ILE N N 121.7 0.1 1 948 . 236 ILE H H 8.28 0.01 1 949 . 236 ILE CA C 62.6 0.2 1 950 . 236 ILE CB C 35.1 0.2 1 951 . 236 ILE C C 177.2 0.2 1 952 . 237 TYR N N 122.8 0.1 1 953 . 237 TYR H H 8.62 0.01 1 954 . 237 TYR CA C 61.6 0.2 1 955 . 237 TYR CB C 36.4 0.2 1 956 . 237 TYR C C 178.8 0.2 1 957 . 238 ARG N N 120.5 0.1 1 958 . 238 ARG H H 8.08 0.01 1 959 . 238 ARG CA C 58.9 0.2 1 960 . 238 ARG CB C 28.9 0.2 1 961 . 238 ARG C C 178.8 0.2 1 962 . 239 ALA N N 122.8 0.1 1 963 . 239 ALA H H 7.48 0.01 1 964 . 239 ALA CA C 54.1 0.2 1 965 . 239 ALA CB C 19.1 0.2 1 966 . 239 ALA C C 180.6 0.2 1 967 . 240 LEU N N 118.1 0.1 1 968 . 240 LEU H H 7.93 0.01 1 969 . 240 LEU CA C 56.6 0.2 1 970 . 240 LEU CB C 38.8 0.2 1 971 . 240 LEU C C 179.0 0.2 1 972 . 241 THR N N 114.9 0.1 1 973 . 241 THR H H 7.44 0.01 1 974 . 241 THR CA C 65.2 0.2 1 975 . 241 THR CB C 69.0 0.2 1 976 . 241 THR C C 175.2 0.2 1 977 . 242 GLN N N 118.5 0.1 1 978 . 242 GLN H H 6.91 0.01 1 979 . 242 GLN CA C 54.2 0.2 1 980 . 242 GLN CB C 28.7 0.2 1 981 . 242 GLN C C 175.1 0.2 1 982 . 243 LEU N N 124.6 0.1 1 983 . 243 LEU H H 6.77 0.01 1 984 . 243 LEU CA C 55.9 0.2 1 985 . 243 LEU CB C 42.1 0.2 1 986 . 243 LEU C C 176.5 0.2 1 987 . 244 ASP N N 128.5 0.1 1 988 . 244 ASP H H 8.45 0.01 1 989 . 244 ASP CA C 53.1 0.2 1 990 . 244 ASP CB C 40.9 0.2 1 991 . 244 ASP C C 175.8 0.2 1 992 . 245 GLY N N 111.3 0.1 1 993 . 245 GLY H H 7.45 0.01 1 994 . 245 GLY CA C 44.1 0.2 1 995 . 245 GLY C C 173.1 0.2 1 996 . 246 TYR N N 118.0 0.1 1 997 . 246 TYR H H 7.87 0.01 1 998 . 246 TYR CA C 56.9 0.2 1 999 . 246 TYR CB C 38.0 0.2 1 1000 . 246 TYR C C 174.7 0.2 1 1001 . 247 GLU N N 121.6 0.1 1 1002 . 247 GLU H H 7.50 0.01 1 1003 . 247 GLU CA C 53.7 0.2 1 1004 . 247 GLU CB C 32.9 0.2 1 1005 . 247 GLU C C 173.7 0.2 1 1006 . 248 LEU N N 128.7 0.1 1 1007 . 248 LEU H H 8.78 0.01 1 1008 . 248 LEU CA C 53.9 0.2 1 1009 . 248 LEU CB C 41.4 0.2 1 1010 . 248 LEU C C 174.0 0.2 1 1011 . 249 ARG N N 129.3 0.1 1 1012 . 249 ARG H H 9.19 0.01 1 1013 . 249 ARG CA C 53.2 0.2 1 1014 . 249 ARG CB C 29.0 0.2 1 1015 . 251 GLN N N 114.0 0.1 1 1016 . 251 GLN H H 8.40 0.01 1 1017 . 251 GLN CA C 57.1 0.2 1 1018 . 251 GLN CB C 27.2 0.2 1 1019 . 251 GLN C C 176.0 0.2 1 1020 . 252 ASP N N 119.5 0.1 1 1021 . 252 ASP H H 7.56 0.01 1 1022 . 252 ASP CA C 55.3 0.2 1 1023 . 252 ASP CB C 42.1 0.2 1 1024 . 252 ASP C C 175.0 0.2 1 1025 . 253 ILE N N 120.5 0.1 1 1026 . 253 ILE H H 7.06 0.01 1 1027 . 253 ILE CA C 59.5 0.2 1 1028 . 253 ILE CB C 37.6 0.2 1 1029 . 253 ILE C C 173.9 0.2 1 1030 . 254 LEU N N 129.1 0.1 1 1031 . 254 LEU H H 7.72 0.01 1 1032 . 254 LEU CA C 53.7 0.2 1 1033 . 254 LEU CB C 40.6 0.2 1 1034 . 254 LEU C C 175.4 0.2 1 1035 . 255 LEU N N 128.3 0.1 1 1036 . 255 LEU H H 7.94 0.01 1 1037 . 255 LEU CA C 51.0 0.2 1 1038 . 255 LEU CB C 40.2 0.2 1 1039 . 257 ASP N N 122.3 0.1 1 1040 . 257 ASP H H 8.24 0.01 1 1041 . 257 ASP CA C 54.0 0.2 1 1042 . 257 ASP CB C 40.0 0.2 1 1043 . 257 ASP C C 175.9 0.2 1 1044 . 258 TYR N N 122.7 0.1 1 1045 . 258 TYR H H 7.79 0.01 1 1046 . 258 TYR CA C 57.7 0.2 1 1047 . 258 TYR CB C 38.4 0.2 1 1048 . 258 TYR C C 175.1 0.2 1 1049 . 259 ASP N N 124.4 0.1 1 1050 . 259 ASP H H 7.99 0.01 1 1051 . 259 ASP CA C 53.5 0.2 1 1052 . 259 ASP CB C 40.6 0.2 1 1053 . 259 ASP C C 175.8 0.2 1 1054 . 260 ALA N N 126.8 0.1 1 1055 . 260 ALA H H 7.81 0.01 1 1056 . 260 ALA CA C 52.5 0.2 1 1057 . 260 ALA CB C 18.2 0.2 1 1058 . 260 ALA C C 177.7 0.2 1 1059 . 261 ALA N N 123.3 0.1 1 1060 . 261 ALA H H 7.95 0.01 1 1061 . 261 ALA CA C 52.4 0.2 1 1062 . 261 ALA CB C 18.1 0.2 1 1063 . 261 ALA C C 178.1 0.2 1 1064 . 262 THR N N 114.7 0.1 1 1065 . 262 THR H H 7.67 0.01 1 1066 . 262 THR CA C 61.7 0.2 1 1067 . 262 THR CB C 69.3 0.2 1 1068 . 262 THR C C 174.6 0.2 1 1069 . 263 VAL N N 124.2 0.1 1 1070 . 263 VAL H H 7.70 0.01 1 1071 . 263 VAL CA C 61.7 0.2 1 1072 . 263 VAL CB C 31.9 0.2 1 1073 . 263 VAL C C 175.5 0.2 1 1074 . 264 ALA N N 129.6 0.1 1 1075 . 264 ALA H H 8.06 0.01 1 1076 . 264 ALA CA C 51.7 0.2 1 1077 . 264 ALA CB C 18.4 0.2 1 1078 . 264 ALA C C 177.4 0.2 1 1079 . 265 VAL N N 121.4 0.1 1 1080 . 265 VAL H H 7.88 0.01 1 1081 . 265 VAL CA C 61.8 0.2 1 1082 . 265 VAL CB C 32.1 0.2 1 1083 . 265 VAL C C 176.7 0.2 1 1084 . 266 GLY N N 114.1 0.1 1 1085 . 266 GLY H H 8.20 0.01 1 1086 . 266 GLY CA C 44.7 0.2 1 1087 . 266 GLY C C 174.2 0.2 1 1088 . 267 GLU N N 122.6 0.1 1 1089 . 267 GLU H H 8.09 0.01 1 1090 . 267 GLU CA C 56.3 0.2 1 1091 . 267 GLU CB C 29.6 0.2 1 1092 . 267 GLU C C 176.4 0.2 1 1093 . 268 ASP N N 122.5 0.1 1 1094 . 268 ASP H H 8.18 0.01 1 1095 . 268 ASP CA C 54.0 0.2 1 1096 . 268 ASP CB C 40.5 0.2 1 1097 . 268 ASP C C 176.1 0.2 1 1098 . 269 ALA N N 125.9 0.1 1 1099 . 269 ALA H H 7.91 0.01 1 1100 . 269 ALA CA C 52.1 0.2 1 1101 . 269 ALA CB C 18.3 0.2 1 1102 . 269 ALA C C 177.8 0.2 1 1103 . 270 MET N N 121.0 0.1 1 1104 . 270 MET H H 8.06 0.01 1 1105 . 270 MET CA C 55.0 0.2 1 1106 . 270 MET CB C 31.9 0.2 1 1107 . 270 MET C C 176.4 0.2 1 1108 . 271 GLU N N 124.0 0.1 1 1109 . 271 GLU H H 8.15 0.01 1 1110 . 271 GLU CA C 56.4 0.2 1 1111 . 271 GLU CB C 29.2 0.2 1 1112 . 271 GLU C C 177.0 0.2 1 1113 . 272 GLY N N 112.0 0.1 1 1114 . 272 GLY H H 8.20 0.01 1 1115 . 272 GLY CA C 44.7 0.2 1 1116 . 272 GLY C C 174.1 0.2 1 1117 . 273 SER N N 117.4 0.1 1 1118 . 273 SER H H 7.96 0.01 1 1119 . 273 SER CA C 57.8 0.2 1 1120 . 273 SER CB C 63.4 0.2 1 1121 . 273 SER C C 174.9 0.2 1 1122 . 274 LEU N N 125.8 0.1 1 1123 . 274 LEU H H 8.18 0.01 1 1124 . 274 LEU CA C 55.2 0.2 1 1125 . 274 LEU CB C 41.0 0.2 1 1126 . 274 LEU C C 177.5 0.2 1 1127 . 275 ASP N N 122.2 0.1 1 1128 . 275 ASP H H 8.01 0.01 1 1129 . 275 ASP CA C 54.5 0.2 1 1130 . 275 ASP CB C 40.5 0.2 1 1131 . 275 ASP C C 176.5 0.2 1 1132 . 276 GLU N N 122.7 0.1 1 1133 . 276 GLU H H 7.98 0.01 1 1134 . 276 GLU CA C 56.7 0.2 1 1135 . 276 GLU CB C 29.1 0.2 1 1136 . 276 GLU C C 177.2 0.2 1 1137 . 277 ILE N N 122.9 0.1 1 1138 . 277 ILE H H 7.94 0.01 1 1139 . 277 ILE CA C 61.8 0.2 1 1140 . 277 ILE CB C 37.3 0.2 1 1141 . 277 ILE C C 177.3 0.2 1 1142 . 278 THR N N 118.2 0.1 1 1143 . 278 THR H H 7.92 0.01 1 1144 . 278 THR CA C 62.7 0.2 1 1145 . 278 THR CB C 68.9 0.2 1 1146 . 278 THR C C 175.3 0.2 1 1147 . 279 SER N N 119.2 0.1 1 1148 . 279 SER H H 7.91 0.01 1 1149 . 279 SER CA C 58.6 0.2 1 1150 . 279 SER CB C 63.5 0.2 1 1151 . 279 SER C C 174.8 0.2 1 1152 . 280 ARG N N 124.1 0.1 1 1153 . 280 ARG H H 7.85 0.01 1 1154 . 280 ARG CA C 56.0 0.2 1 1155 . 280 ARG CB C 29.5 0.2 1 1156 . 280 ARG C C 176.5 0.2 1 1157 . 281 LEU N N 123.9 0.1 1 1158 . 281 LEU H H 7.84 0.01 1 1159 . 281 LEU CA C 54.9 0.2 1 1160 . 281 LEU CB C 41.0 0.2 1 1161 . 281 LEU C C 177.5 0.2 1 1162 . 282 GLU N N 122.5 0.1 1 1163 . 282 GLU H H 8.02 0.01 1 1164 . 282 GLU CA C 56.2 0.2 1 1165 . 282 GLU CB C 29.3 0.2 1 stop_ save_