data_26546 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Type III Secretion Protein ; _BMRB_accession_number 26546 _BMRB_flat_file_name bmr26546.str _Entry_type original _Submission_date 2015-03-20 _Accession_date 2015-03-20 _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 Notti Ryan Q. . 2 Bhattacharya Shibani . . 3 Stebbins Charles E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 151 "13C chemical shifts" 432 "15N chemical shifts" 151 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-07-13 update BMRB 'update entry citation' 2015-05-22 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 26543 SpaO stop_ _Original_release_date 2015-05-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A common assembly module in injectisome and flagellar type III secretion sorting platforms ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25994170 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Notti Ryan Q. . 2 Bhattacharya Shibani . . 3 Lilic Mirjana Q. . 4 Stebbins Charles E. . stop_ _Journal_abbreviation 'Nat. Commun.' _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7125 _Page_last 7125 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name SpaO-OrgB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SpaO $SpaO OrgB $OrgB Thioredoxin $Thioredoxin 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_SpaO _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SpaO _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 162 _Mol_residue_sequence ; GPVDVGGGRPKMLRWPLRFV IGSSDTQRSLLGRIGIGDVL LIRTSRAEVYCYAKKLGHFN RVEGGIIVETLDIQHIEEEN NTTETAETLPGLNQLPVKLE FVLYRKNVTLAELEAMGQQQ LLSLPTNAELNVEIMANGVL LGNGELVQMNDTLGVEIHEW LS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 136 GLY 2 137 PRO 3 138 VAL 4 139 ASP 5 140 VAL 6 141 GLY 7 142 GLY 8 143 GLY 9 144 ARG 10 145 PRO 11 146 LYS 12 147 MET 13 148 LEU 14 149 ARG 15 150 TRP 16 151 PRO 17 152 LEU 18 153 ARG 19 154 PHE 20 155 VAL 21 156 ILE 22 157 GLY 23 158 SER 24 159 SER 25 160 ASP 26 161 THR 27 162 GLN 28 163 ARG 29 164 SER 30 165 LEU 31 166 LEU 32 167 GLY 33 168 ARG 34 169 ILE 35 170 GLY 36 171 ILE 37 172 GLY 38 173 ASP 39 174 VAL 40 175 LEU 41 176 LEU 42 177 ILE 43 178 ARG 44 179 THR 45 180 SER 46 181 ARG 47 182 ALA 48 183 GLU 49 184 VAL 50 185 TYR 51 186 CYS 52 187 TYR 53 188 ALA 54 189 LYS 55 190 LYS 56 191 LEU 57 192 GLY 58 193 HIS 59 194 PHE 60 195 ASN 61 196 ARG 62 197 VAL 63 198 GLU 64 199 GLY 65 200 GLY 66 201 ILE 67 202 ILE 68 203 VAL 69 204 GLU 70 205 THR 71 206 LEU 72 207 ASP 73 208 ILE 74 209 GLN 75 210 HIS 76 211 ILE 77 212 GLU 78 213 GLU 79 214 GLU 80 215 ASN 81 216 ASN 82 217 THR 83 218 THR 84 219 GLU 85 220 THR 86 221 ALA 87 222 GLU 88 223 THR 89 224 LEU 90 225 PRO 91 226 GLY 92 227 LEU 93 228 ASN 94 229 GLN 95 230 LEU 96 231 PRO 97 232 VAL 98 233 LYS 99 234 LEU 100 235 GLU 101 236 PHE 102 237 VAL 103 238 LEU 104 239 TYR 105 240 ARG 106 241 LYS 107 242 ASN 108 243 VAL 109 244 THR 110 245 LEU 111 246 ALA 112 247 GLU 113 248 LEU 114 249 GLU 115 250 ALA 116 251 MET 117 252 GLY 118 253 GLN 119 254 GLN 120 255 GLN 121 256 LEU 122 257 LEU 123 258 SER 124 259 LEU 125 260 PRO 126 261 THR 127 262 ASN 128 263 ALA 129 264 GLU 130 265 LEU 131 266 ASN 132 267 VAL 133 268 GLU 134 269 ILE 135 270 MET 136 271 ALA 137 272 ASN 138 273 GLY 139 274 VAL 140 275 LEU 141 276 LEU 142 277 GLY 143 278 ASN 144 279 GLY 145 280 GLU 146 281 LEU 147 282 VAL 148 283 GLN 149 284 MET 150 285 ASN 151 286 ASP 152 287 THR 153 288 LEU 154 289 GLY 155 290 VAL 156 291 GLU 157 292 ILE 158 293 HIS 159 294 GLU 160 295 TRP 161 296 LEU 162 297 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_OrgB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common OrgB _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 33 _Mol_residue_sequence ; GPRSLKNIPIPSPLSPVEGI LIKRKTLERYFSI ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PRO 3 ARG 4 SER 5 LEU 6 LYS 7 ASN 8 ILE 9 PRO 10 ILE 11 PRO 12 SER 13 PRO 14 LEU 15 SER 16 PRO 17 VAL 18 GLU 19 GLY 20 ILE 21 LEU 22 ILE 23 LYS 24 ARG 25 LYS 26 THR 27 LEU 28 GLU 29 ARG 30 TYR 31 PHE 32 SER 33 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_Thioredoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Thioredoxin _Molecular_mass . _Mol_thiol_state 'all free' _Details . _Residue_count 118 _Mol_residue_sequence ; GPVDMVKQIESKTAFQEALD AAGDKLVVVDFSATWCGPCK MIKPFFHSLSEKYSNVIFLE VDVDDCQDVASECEVKCMPT FQFFKKGQKVGEFSGANKEK LEATINELVGGSLEVLFQ ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PRO 3 VAL 4 ASP 5 MET 6 VAL 7 LYS 8 GLN 9 ILE 10 GLU 11 SER 12 LYS 13 THR 14 ALA 15 PHE 16 GLN 17 GLU 18 ALA 19 LEU 20 ASP 21 ALA 22 ALA 23 GLY 24 ASP 25 LYS 26 LEU 27 VAL 28 VAL 29 VAL 30 ASP 31 PHE 32 SER 33 ALA 34 THR 35 TRP 36 CYS 37 GLY 38 PRO 39 CYS 40 LYS 41 MET 42 ILE 43 LYS 44 PRO 45 PHE 46 PHE 47 HIS 48 SER 49 LEU 50 SER 51 GLU 52 LYS 53 TYR 54 SER 55 ASN 56 VAL 57 ILE 58 PHE 59 LEU 60 GLU 61 VAL 62 ASP 63 VAL 64 ASP 65 ASP 66 CYS 67 GLN 68 ASP 69 VAL 70 ALA 71 SER 72 GLU 73 CYS 74 GLU 75 VAL 76 LYS 77 CYS 78 MET 79 PRO 80 THR 81 PHE 82 GLN 83 PHE 84 PHE 85 LYS 86 LYS 87 GLY 88 GLN 89 LYS 90 VAL 91 GLY 92 GLU 93 PHE 94 SER 95 GLY 96 ALA 97 ASN 98 LYS 99 GLU 100 LYS 101 LEU 102 GLU 103 ALA 104 THR 105 ILE 106 ASN 107 GLU 108 LEU 109 VAL 110 GLY 111 GLY 112 SER 113 LEU 114 GLU 115 VAL 116 LEU 117 PHE 118 GLN 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 $SpaO 'Salmonella enterica' 28901 Bacteria . Salmonella enterica $OrgB 'Salmonella enterica' 28901 Bacteria . Salmonella enterica $Thioredoxin Human 9606 Eukaryota Metazoa Homo sapiens 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 $SpaO 'recombinant technology' . Escherichia coli . pCDFduet $OrgB 'recombinant technology' . Escherichia coli . pCDFduet $Thioredoxin 'recombinant technology' . Escherichia coli . pCDFduet stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'trace amount of Thioredoxin' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SpaO 0.2 mM '[U-13C; U-15N]' $OrgB 0.2 mM 'natural abundance' $Thioredoxin . mM 'natural abundance' 'Sodium Citrate' 10 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' DTT 2 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_900 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_800 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_600 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.6 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_DSS _Saveframe_category chemical_shift_reference _Details '1H DSS Direct 1.000000; C13 DSS Indirect 0.25144953; N15 DSS Indirect 0.101329118' 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 external 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCACB' '3D HNCA' '3D CBCA(CO)NH' '3D HN(CO)CA' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_condition_1 _Chem_shift_reference_set_label $DSS _Mol_system_component_name SpaO _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 PRO C C 176.912 0.50 1 2 137 2 PRO CA C 63.131 0.50 1 3 137 2 PRO CB C 32.398 0.50 1 4 138 3 VAL H H 8.270 0.05 1 5 138 3 VAL C C 175.752 0.50 1 6 138 3 VAL CA C 62.169 0.50 1 7 138 3 VAL CB C 32.609 0.50 1 8 138 3 VAL N N 119.310 0.10 1 9 139 4 ASP H H 8.355 0.05 1 10 139 4 ASP C C 176.363 0.50 1 11 139 4 ASP CA C 54.062 0.50 1 12 139 4 ASP CB C 41.284 0.50 1 13 139 4 ASP N N 123.910 0.10 1 14 140 5 VAL H H 8.176 0.05 1 15 140 5 VAL C C 176.998 0.50 1 16 140 5 VAL CA C 62.424 0.50 1 17 140 5 VAL CB C 32.229 0.50 1 18 140 5 VAL N N 120.277 0.10 1 19 141 6 GLY H H 8.542 0.05 1 20 141 6 GLY C C 174.957 0.50 1 21 141 6 GLY CA C 45.453 0.50 1 22 141 6 GLY N N 111.846 0.10 1 23 142 7 GLY H H 8.310 0.05 1 24 142 7 GLY C C 174.774 0.50 1 25 142 7 GLY CA C 45.292 0.50 1 26 142 7 GLY N N 108.877 0.10 1 27 143 8 GLY H H 8.341 0.05 1 28 143 8 GLY C C 173.885 0.50 1 29 143 8 GLY CA C 45.058 0.50 1 30 143 8 GLY N N 108.681 0.10 1 31 144 9 ARG H H 8.147 0.05 1 32 144 9 ARG C C 174.334 0.50 1 33 144 9 ARG CA C 54.056 0.50 1 34 144 9 ARG CB C 29.757 0.50 1 35 144 9 ARG N N 121.504 0.10 1 36 145 10 PRO C C 176.851 0.50 1 37 145 10 PRO CA C 62.625 0.50 1 38 145 10 PRO CB C 31.212 0.50 1 39 146 11 LYS H H 8.430 0.05 1 40 146 11 LYS C C 176.623 0.50 1 41 146 11 LYS CA C 56.474 0.50 1 42 146 11 LYS N N 121.593 0.10 1 43 147 12 MET H H 8.301 0.05 1 44 147 12 MET C C 175.383 0.50 1 45 147 12 MET CA C 55.044 0.50 1 46 147 12 MET CB C 32.715 0.50 1 47 147 12 MET N N 121.466 0.10 1 48 148 13 LEU H H 8.118 0.05 1 49 148 13 LEU C C 176.430 0.50 1 50 148 13 LEU CA C 55.217 0.50 1 51 148 13 LEU CB C 42.539 0.50 1 52 148 13 LEU N N 124.036 0.10 1 53 149 14 ARG H H 7.484 0.05 1 54 149 14 ARG C C 174.932 0.50 1 55 149 14 ARG CA C 54.316 0.50 1 56 149 14 ARG CB C 33.877 0.50 1 57 149 14 ARG N N 118.650 0.10 1 58 150 15 TRP H H 9.402 0.05 1 59 150 15 TRP C C 174.420 0.50 1 60 150 15 TRP CA C 55.463 0.50 1 61 150 15 TRP CB C 30.645 0.50 1 62 150 15 TRP N N 123.946 0.10 1 63 151 16 PRO C C 175.657 0.50 1 64 151 16 PRO CA C 61.971 0.50 1 65 151 16 PRO CB C 30.335 0.50 1 66 152 17 LEU H H 8.913 0.05 1 67 152 17 LEU C C 177.998 0.50 1 68 152 17 LEU CA C 53.734 0.50 1 69 152 17 LEU CB C 44.070 0.50 1 70 152 17 LEU N N 128.103 0.10 1 71 153 18 ARG H H 8.921 0.05 1 72 153 18 ARG C C 173.789 0.50 1 73 153 18 ARG CA C 54.576 0.50 1 74 153 18 ARG CB C 32.765 0.50 1 75 153 18 ARG N N 118.597 0.10 1 76 154 19 PHE H H 8.955 0.05 1 77 154 19 PHE C C 173.950 0.50 1 78 154 19 PHE CA C 57.865 0.50 1 79 154 19 PHE CB C 36.525 0.50 1 80 154 19 PHE N N 123.534 0.10 1 81 155 20 VAL H H 9.494 0.05 1 82 155 20 VAL C C 175.542 0.50 1 83 155 20 VAL CA C 63.420 0.50 1 84 155 20 VAL CB C 33.846 0.50 1 85 155 20 VAL N N 128.339 0.10 1 86 156 21 ILE H H 9.100 0.05 1 87 156 21 ILE C C 176.832 0.50 1 88 156 21 ILE CA C 61.545 0.50 1 89 156 21 ILE CB C 39.054 0.50 1 90 156 21 ILE N N 118.186 0.10 1 91 157 22 GLY H H 7.917 0.05 1 92 157 22 GLY C C 170.568 0.50 1 93 157 22 GLY CA C 46.254 0.50 1 94 157 22 GLY N N 108.254 0.10 1 95 158 23 SER H H 9.132 0.05 1 96 158 23 SER C C 173.080 0.50 1 97 158 23 SER CA C 57.592 0.50 1 98 158 23 SER CB C 66.785 0.50 1 99 158 23 SER N N 113.157 0.10 1 100 159 24 SER H H 8.944 0.05 1 101 159 24 SER C C 171.599 0.50 1 102 159 24 SER CA C 57.748 0.50 1 103 159 24 SER CB C 68.316 0.50 1 104 159 24 SER N N 114.542 0.10 1 105 160 25 ASP H H 8.852 0.05 1 106 160 25 ASP C C 175.802 0.50 1 107 160 25 ASP CA C 54.064 0.50 1 108 160 25 ASP CB C 41.798 0.50 1 109 160 25 ASP N N 125.955 0.10 1 110 161 26 THR H H 9.176 0.05 1 111 161 26 THR C C 173.177 0.50 1 112 161 26 THR CA C 59.829 0.50 1 113 161 26 THR CB C 69.267 0.50 1 114 161 26 THR N N 117.493 0.10 1 115 162 27 GLN H H 8.864 0.05 1 116 162 27 GLN C C 177.476 0.50 1 117 162 27 GLN CA C 54.420 0.50 1 118 162 27 GLN CB C 30.813 0.50 1 119 162 27 GLN N N 121.567 0.10 1 120 163 28 ARG H H 9.205 0.05 1 121 163 28 ARG C C 178.700 0.50 1 122 163 28 ARG CA C 59.911 0.50 1 123 163 28 ARG CB C 29.509 0.50 1 124 163 28 ARG N N 122.913 0.10 1 125 164 29 SER H H 8.522 0.05 1 126 164 29 SER CA C 60.271 0.50 1 127 164 29 SER CB C 61.925 0.50 1 128 164 29 SER N N 113.446 0.10 1 129 165 30 LEU H H 7.533 0.05 1 130 165 30 LEU C C 179.103 0.50 1 131 165 30 LEU CA C 56.748 0.50 1 132 165 30 LEU CB C 41.910 0.50 1 133 165 30 LEU N N 124.118 0.10 1 134 166 31 LEU H H 7.487 0.05 1 135 166 31 LEU C C 178.769 0.50 1 136 166 31 LEU CA C 57.900 0.50 1 137 166 31 LEU CB C 40.110 0.50 1 138 166 31 LEU N N 113.887 0.10 1 139 167 32 GLY H H 7.664 0.05 1 140 167 32 GLY C C 174.792 0.50 1 141 167 32 GLY CA C 45.630 0.50 1 142 167 32 GLY N N 102.697 0.10 1 143 168 33 ARG H H 7.934 0.05 1 144 168 33 ARG C C 174.792 0.50 1 145 168 33 ARG CA C 55.304 0.50 1 146 168 33 ARG CB C 30.761 0.50 1 147 168 33 ARG N N 118.210 0.10 1 148 169 34 ILE H H 6.708 0.05 1 149 169 34 ILE C C 174.422 0.50 1 150 169 34 ILE CA C 61.805 0.50 1 151 169 34 ILE CB C 38.842 0.50 1 152 169 34 ILE N N 120.804 0.10 1 153 170 35 GLY H H 8.739 0.05 1 154 170 35 GLY C C 172.032 0.50 1 155 170 35 GLY CA C 43.524 0.50 1 156 170 35 GLY N N 114.795 0.10 1 157 171 36 ILE H H 8.151 0.05 1 158 171 36 ILE C C 177.854 0.50 1 159 171 36 ILE CA C 63.183 0.50 1 160 171 36 ILE CB C 37.046 0.50 1 161 171 36 ILE N N 116.614 0.10 1 162 172 37 GLY H H 9.117 0.05 1 163 172 37 GLY C C 173.348 0.50 1 164 172 37 GLY CA C 44.876 0.50 1 165 172 37 GLY N N 116.578 0.10 1 166 173 38 ASP H H 7.502 0.05 1 167 173 38 ASP C C 174.422 0.50 1 168 173 38 ASP CA C 54.238 0.50 1 169 173 38 ASP CB C 41.483 0.50 1 170 173 38 ASP N N 119.569 0.10 1 171 174 39 VAL H H 8.936 0.05 1 172 174 39 VAL C C 174.974 0.50 1 173 174 39 VAL CA C 60.375 0.50 1 174 174 39 VAL N N 117.638 0.10 1 175 175 40 LEU H H 8.506 0.05 1 176 175 40 LEU C C 176.050 0.50 1 177 175 40 LEU CA C 51.767 0.50 1 178 175 40 LEU CB C 44.845 0.50 1 179 175 40 LEU N N 126.075 0.10 1 180 176 41 LEU H H 9.261 0.05 1 181 176 41 LEU CA C 55.158 0.50 1 182 176 41 LEU CB C 42.315 0.50 1 183 176 41 LEU N N 122.780 0.10 1 184 177 42 ILE H H 8.011 0.05 1 185 177 42 ILE C C 175.751 0.50 1 186 177 42 ILE CA C 61.092 0.50 1 187 177 42 ILE N N 121.468 0.10 1 188 178 43 ARG H H 8.703 0.05 1 189 178 43 ARG C C 177.534 0.50 1 190 178 43 ARG CA C 58.081 0.50 1 191 178 43 ARG CB C 30.278 0.50 1 192 178 43 ARG N N 128.241 0.10 1 193 179 44 THR H H 8.695 0.05 1 194 179 44 THR C C 173.700 0.50 1 195 179 44 THR CA C 61.441 0.50 1 196 179 44 THR CB C 69.848 0.50 1 197 179 44 THR N N 116.234 0.10 1 198 180 45 SER H H 8.954 0.05 1 199 180 45 SER C C 173.778 0.50 1 200 180 45 SER CA C 58.320 0.50 1 201 180 45 SER CB C 62.976 0.50 1 202 180 45 SER N N 123.390 0.10 1 203 181 46 ARG H H 7.675 0.05 1 204 181 46 ARG C C 173.467 0.50 1 205 181 46 ARG CA C 55.694 0.50 1 206 181 46 ARG CB C 33.454 0.50 1 207 181 46 ARG N N 125.114 0.10 1 208 182 47 ALA H H 8.316 0.05 1 209 182 47 ALA C C 176.603 0.50 1 210 182 47 ALA CA C 52.107 0.50 1 211 182 47 ALA CB C 17.064 0.50 1 212 182 47 ALA N N 128.509 0.10 1 213 183 48 GLU H H 8.749 0.05 1 214 183 48 GLU C C 174.422 0.50 1 215 183 48 GLU CA C 54.599 0.50 1 216 183 48 GLU CB C 36.374 0.50 1 217 183 48 GLU N N 122.642 0.10 1 218 184 49 VAL H H 8.505 0.05 1 219 184 49 VAL C C 174.710 0.50 1 220 184 49 VAL CA C 60.479 0.50 1 221 184 49 VAL N N 121.572 0.10 1 222 185 50 TYR H H 9.113 0.05 1 223 185 50 TYR C C 175.320 0.50 1 224 185 50 TYR CA C 56.632 0.50 1 225 185 50 TYR CB C 44.432 0.50 1 226 185 50 TYR N N 126.753 0.10 1 227 186 51 CYS H H 8.816 0.05 1 228 186 51 CYS C C 174.725 0.50 1 229 186 51 CYS CA C 58.632 0.50 1 230 186 51 CYS CB C 28.648 0.50 1 231 186 51 CYS N N 120.319 0.10 1 232 187 52 TYR H H 9.211 0.05 1 233 187 52 TYR C C 176.475 0.50 1 234 187 52 TYR CA C 60.598 0.50 1 235 187 52 TYR CB C 35.114 0.50 1 236 187 52 TYR N N 126.687 0.10 1 237 188 53 ALA H H 8.632 0.05 1 238 188 53 ALA C C 177.277 0.50 1 239 188 53 ALA CA C 52.361 0.50 1 240 188 53 ALA CB C 18.872 0.50 1 241 188 53 ALA N N 125.859 0.10 1 242 189 54 LYS H H 8.243 0.05 1 243 189 54 LYS C C 174.678 0.50 1 244 189 54 LYS CA C 55.565 0.50 1 245 189 54 LYS CB C 33.898 0.50 1 246 189 54 LYS N N 120.518 0.10 1 247 190 55 LYS H H 8.625 0.05 1 248 190 55 LYS C C 176.507 0.50 1 249 190 55 LYS CA C 55.895 0.50 1 250 190 55 LYS CB C 31.419 0.50 1 251 190 55 LYS N N 127.472 0.10 1 252 191 56 LEU H H 9.186 0.05 1 253 191 56 LEU CA C 54.802 0.50 1 254 191 56 LEU N N 126.591 0.10 1 255 192 57 GLY H H 7.119 0.05 1 256 192 57 GLY C C 171.567 0.50 1 257 192 57 GLY CA C 45.474 0.50 1 258 192 57 GLY N N 103.435 0.10 1 259 193 58 HIS H H 8.603 0.05 1 260 193 58 HIS C C 173.379 0.50 1 261 193 58 HIS CA C 55.044 0.50 1 262 193 58 HIS CB C 31.870 0.50 1 263 193 58 HIS N N 119.588 0.10 1 264 194 59 PHE H H 7.688 0.05 1 265 194 59 PHE C C 170.909 0.50 1 266 194 59 PHE CA C 55.096 0.50 1 267 194 59 PHE CB C 43.121 0.50 1 268 194 59 PHE N N 116.281 0.10 1 269 195 60 ASN H H 9.161 0.05 1 270 195 60 ASN C C 174.005 0.50 1 271 195 60 ASN CA C 51.845 0.50 1 272 195 60 ASN CB C 41.959 0.50 1 273 195 60 ASN N N 116.370 0.10 1 274 196 61 ARG H H 8.905 0.05 1 275 196 61 ARG C C 174.983 0.50 1 276 196 61 ARG CA C 55.920 0.50 1 277 196 61 ARG CB C 31.161 0.50 1 278 196 61 ARG N N 126.587 0.10 1 279 197 62 VAL H H 8.622 0.05 1 280 197 62 VAL C C 176.333 0.50 1 281 197 62 VAL CA C 59.178 0.50 1 282 197 62 VAL CB C 34.828 0.50 1 283 197 62 VAL N N 121.024 0.10 1 284 198 63 GLU H H 8.665 0.05 1 285 198 63 GLU C C 177.911 0.50 1 286 198 63 GLU CA C 59.354 0.50 1 287 198 63 GLU CB C 28.571 0.50 1 288 198 63 GLU N N 122.306 0.10 1 289 199 64 GLY H H 8.659 0.05 1 290 199 64 GLY C C 174.980 0.50 1 291 199 64 GLY CA C 45.240 0.50 1 292 199 64 GLY N N 109.791 0.10 1 293 200 65 GLY H H 7.626 0.05 1 294 200 65 GLY C C 170.987 0.50 1 295 200 65 GLY CA C 46.852 0.50 1 296 200 65 GLY N N 107.135 0.10 1 297 201 66 ILE H H 8.956 0.05 1 298 201 66 ILE C C 173.724 0.50 1 299 201 66 ILE CA C 59.461 0.50 1 300 201 66 ILE N N 123.756 0.10 1 301 202 67 ILE H H 8.689 0.05 1 302 202 67 ILE C C 176.107 0.50 1 303 202 67 ILE CA C 59.622 0.50 1 304 202 67 ILE N N 123.731 0.10 1 305 203 68 VAL H H 9.596 0.05 1 306 203 68 VAL C C 174.761 0.50 1 307 203 68 VAL CA C 62.708 0.50 1 308 203 68 VAL CB C 31.523 0.50 1 309 203 68 VAL N N 129.643 0.10 1 310 204 69 GLU H H 8.297 0.05 1 311 204 69 GLU C C 175.802 0.50 1 312 204 69 GLU CA C 57.573 0.50 1 313 204 69 GLU CB C 30.851 0.50 1 314 204 69 GLU N N 125.845 0.10 1 315 205 70 THR H H 7.635 0.05 1 316 205 70 THR C C 172.782 0.50 1 317 205 70 THR CA C 61.545 0.50 1 318 205 70 THR CB C 70.731 0.50 1 319 205 70 THR N N 110.491 0.10 1 320 206 71 LEU H H 8.405 0.05 1 321 206 71 LEU C C 175.593 0.50 1 322 206 71 LEU CA C 53.900 0.50 1 323 206 71 LEU CB C 44.777 0.50 1 324 206 71 LEU N N 123.456 0.10 1 325 207 72 ASP H H 8.774 0.05 1 326 207 72 ASP C C 175.946 0.50 1 327 207 72 ASP CA C 52.982 0.50 1 328 207 72 ASP CB C 40.559 0.50 1 329 207 72 ASP N N 125.361 0.10 1 330 208 73 ILE H H 8.138 0.05 1 331 208 73 ILE C C 176.832 0.50 1 332 208 73 ILE CA C 61.129 0.50 1 333 208 73 ILE CB C 38.103 0.50 1 334 208 73 ILE N N 118.069 0.10 1 335 209 74 GLN H H 8.223 0.05 1 336 209 74 GLN C C 176.703 0.50 1 337 209 74 GLN CA C 57.592 0.50 1 338 209 74 GLN CB C 28.753 0.50 1 339 209 74 GLN N N 121.278 0.10 1 340 210 75 HIS H H 8.339 0.05 1 341 210 75 HIS C C 175.302 0.50 1 342 210 75 HIS CA C 55.564 0.50 1 343 210 75 HIS CB C 27.891 0.50 1 344 210 75 HIS N N 115.372 0.10 1 345 211 76 ILE H H 7.418 0.05 1 346 211 76 ILE C C 175.373 0.50 1 347 211 76 ILE CA C 63.157 0.50 1 348 211 76 ILE CB C 38.261 0.50 1 349 211 76 ILE N N 120.485 0.10 1 350 212 77 GLU H H 8.440 0.05 1 351 212 77 GLU C C 176.623 0.50 1 352 212 77 GLU CA C 56.584 0.50 1 353 212 77 GLU CB C 30.127 0.50 1 354 212 77 GLU N N 121.044 0.10 1 355 213 78 GLU H H 8.052 0.05 1 356 213 78 GLU C C 176.424 0.50 1 357 213 78 GLU CA C 56.630 0.50 1 358 213 78 GLU CB C 30.127 0.50 1 359 213 78 GLU N N 120.390 0.10 1 360 214 79 GLU H H 8.103 0.05 1 361 214 79 GLU C C 175.995 0.50 1 362 214 79 GLU CA C 56.448 0.50 1 363 214 79 GLU CB C 30.074 0.50 1 364 214 79 GLU N N 121.473 0.10 1 365 215 80 ASN H H 8.453 0.05 1 366 215 80 ASN C C 174.739 0.50 1 367 215 80 ASN CA C 53.114 0.50 1 368 215 80 ASN CB C 39.001 0.50 1 369 215 80 ASN N N 120.014 0.10 1 370 216 81 ASN H H 8.438 0.05 1 371 216 81 ASN C C 175.431 0.50 1 372 216 81 ASN CA C 53.041 0.50 1 373 216 81 ASN N N 119.827 0.10 1 374 217 82 THR H H 8.144 0.05 1 375 217 82 THR C C 174.723 0.50 1 376 217 82 THR CA C 61.857 0.50 1 377 217 82 THR CB C 69.479 0.50 1 378 217 82 THR N N 114.368 0.10 1 379 218 83 THR H H 8.159 0.05 1 380 218 83 THR C C 174.610 0.50 1 381 218 83 THR CA C 62.013 0.50 1 382 218 83 THR CB C 69.479 0.50 1 383 218 83 THR N N 116.342 0.10 1 384 219 84 GLU H H 8.434 0.05 1 385 219 84 GLU C C 176.424 0.50 1 386 219 84 GLU CA C 56.533 0.50 1 387 219 84 GLU CB C 30.263 0.50 1 388 219 84 GLU N N 123.654 0.10 1 389 220 85 THR H H 8.198 0.05 1 390 220 85 THR C C 174.256 0.50 1 391 220 85 THR CA C 61.597 0.50 1 392 220 85 THR CB C 69.901 0.50 1 393 220 85 THR N N 115.502 0.10 1 394 221 86 ALA H H 8.371 0.05 1 395 221 86 ALA C C 177.589 0.50 1 396 221 86 ALA CA C 52.565 0.50 1 397 221 86 ALA CB C 19.181 0.50 1 398 221 86 ALA N N 126.567 0.10 1 399 222 87 GLU H H 8.381 0.05 1 400 222 87 GLU C C 176.534 0.50 1 401 222 87 GLU CA C 56.630 0.50 1 402 222 87 GLU CB C 30.180 0.50 1 403 222 87 GLU N N 119.904 0.10 1 404 223 88 THR H H 8.139 0.05 1 405 223 88 THR C C 174.256 0.50 1 406 223 88 THR CA C 61.623 0.50 1 407 223 88 THR CB C 69.584 0.50 1 408 223 88 THR N N 115.066 0.10 1 409 224 89 LEU H H 8.205 0.05 1 410 224 89 LEU C C 175.190 0.50 1 411 224 89 LEU CA C 53.327 0.50 1 412 224 89 LEU CB C 41.747 0.50 1 413 224 89 LEU N N 125.849 0.10 1 414 225 90 PRO C C 177.597 0.50 1 415 225 90 PRO CA C 63.404 0.50 1 416 225 90 PRO CB C 31.923 0.50 1 417 226 91 GLY H H 8.394 0.05 1 418 226 91 GLY C C 174.591 0.50 1 419 226 91 GLY CA C 45.286 0.50 1 420 226 91 GLY N N 108.325 0.10 1 421 227 92 LEU H H 7.944 0.05 1 422 227 92 LEU C C 177.508 0.50 1 423 227 92 LEU CA C 55.590 0.50 1 424 227 92 LEU CB C 41.906 0.50 1 425 227 92 LEU N N 121.317 0.10 1 426 228 93 ASN H H 8.384 0.05 1 427 228 93 ASN C C 175.043 0.50 1 428 228 93 ASN CA C 53.847 0.50 1 429 228 93 ASN CB C 38.472 0.50 1 430 228 93 ASN N N 118.008 0.10 1 431 229 94 GLN H H 8.199 0.05 1 432 229 94 GLN C C 175.624 0.50 1 433 229 94 GLN CA C 55.538 0.50 1 434 229 94 GLN CB C 29.070 0.50 1 435 229 94 GLN N N 118.250 0.10 1 436 230 95 LEU H H 8.033 0.05 1 437 230 95 LEU C C 175.045 0.50 1 438 230 95 LEU CA C 53.712 0.50 1 439 230 95 LEU CB C 41.448 0.50 1 440 230 95 LEU N N 123.219 0.10 1 441 231 96 PRO C C 176.373 0.50 1 442 231 96 PRO CA C 63.183 0.50 1 443 231 96 PRO CB C 32.187 0.50 1 444 232 97 VAL H H 8.563 0.05 1 445 232 97 VAL C C 173.016 0.50 1 446 232 97 VAL CA C 60.765 0.50 1 447 232 97 VAL CB C 34.300 0.50 1 448 232 97 VAL N N 120.554 0.10 1 449 233 98 LYS H H 8.552 0.05 1 450 233 98 LYS C C 175.834 0.50 1 451 233 98 LYS CA C 55.208 0.50 1 452 233 98 LYS CB C 32.504 0.50 1 453 233 98 LYS N N 128.665 0.10 1 454 234 99 LEU H H 8.857 0.05 1 455 234 99 LEU C C 176.118 0.50 1 456 234 99 LEU CA C 53.624 0.50 1 457 234 99 LEU CB C 42.537 0.50 1 458 234 99 LEU N N 127.540 0.10 1 459 235 100 GLU H H 9.160 0.05 1 460 235 100 GLU C C 174.513 0.50 1 461 235 100 GLU CA C 54.732 0.50 1 462 235 100 GLU CB C 33.243 0.50 1 463 235 100 GLU N N 121.517 0.10 1 464 237 102 VAL H H 9.904 0.05 1 465 237 102 VAL C C 175.125 0.50 1 466 237 102 VAL CA C 62.962 0.50 1 467 237 102 VAL CB C 33.898 0.50 1 468 237 102 VAL N N 127.071 0.10 1 469 238 103 LEU H H 9.079 0.05 1 470 238 103 LEU C C 173.853 0.50 1 471 238 103 LEU CA C 56.378 0.50 1 472 238 103 LEU N N 129.532 0.10 1 473 239 104 TYR H H 7.519 0.05 1 474 239 104 TYR C C 172.404 0.50 1 475 239 104 TYR CA C 56.760 0.50 1 476 239 104 TYR CB C 41.589 0.50 1 477 239 104 TYR N N 113.840 0.10 1 478 240 105 ARG H H 7.270 0.05 1 479 240 105 ARG C C 173.186 0.50 1 480 240 105 ARG CA C 55.200 0.50 1 481 240 105 ARG CB C 34.300 0.50 1 482 240 105 ARG N N 125.190 0.10 1 483 241 106 LYS H H 8.022 0.05 1 484 241 106 LYS C C 173.308 0.50 1 485 241 106 LYS CA C 55.902 0.50 1 486 241 106 LYS CB C 37.416 0.50 1 487 241 106 LYS N N 119.453 0.10 1 488 242 107 ASN H H 8.780 0.05 1 489 242 107 ASN C C 175.834 0.50 1 490 242 107 ASN CA C 51.929 0.50 1 491 242 107 ASN CB C 38.081 0.50 1 492 242 107 ASN N N 126.086 0.10 1 493 243 108 VAL H H 8.990 0.05 1 494 243 108 VAL C C 175.753 0.50 1 495 243 108 VAL CA C 59.517 0.50 1 496 243 108 VAL CB C 34.617 0.50 1 497 243 108 VAL N N 118.401 0.10 1 498 244 109 THR H H 8.842 0.05 1 499 244 109 THR C C 175.823 0.50 1 500 244 109 THR CA C 60.505 0.50 1 501 244 109 THR CB C 71.486 0.50 1 502 244 109 THR N N 112.297 0.10 1 503 245 110 LEU H H 9.231 0.05 1 504 245 110 LEU C C 178.684 0.50 1 505 245 110 LEU CA C 58.398 0.50 1 506 245 110 LEU CB C 41.272 0.50 1 507 245 110 LEU N N 121.822 0.10 1 508 246 111 ALA H H 8.351 0.05 1 509 246 111 ALA C C 181.695 0.50 1 510 246 111 ALA CA C 54.992 0.50 1 511 246 111 ALA CB C 18.031 0.50 1 512 246 111 ALA N N 119.797 0.10 1 513 247 112 GLU H H 7.700 0.05 1 514 247 112 GLU C C 179.613 0.50 1 515 247 112 GLU CA C 59.100 0.50 1 516 247 112 GLU CB C 30.074 0.50 1 517 247 112 GLU N N 119.088 0.10 1 518 248 113 LEU H H 8.439 0.05 1 519 248 113 LEU C C 179.038 0.50 1 520 248 113 LEU CA C 58.172 0.50 1 521 248 113 LEU CB C 42.048 0.50 1 522 248 113 LEU N N 122.950 0.10 1 523 249 114 GLU H H 8.559 0.05 1 524 249 114 GLU C C 179.430 0.50 1 525 249 114 GLU CA C 59.282 0.50 1 526 249 114 GLU CB C 29.123 0.50 1 527 249 114 GLU N N 118.275 0.10 1 528 250 115 ALA H H 7.603 0.05 1 529 250 115 ALA C C 180.309 0.50 1 530 250 115 ALA CA C 54.472 0.50 1 531 250 115 ALA CB C 17.767 0.50 1 532 250 115 ALA N N 121.129 0.10 1 533 251 116 MET H H 8.130 0.05 1 534 251 116 MET C C 179.148 0.50 1 535 251 116 MET CA C 58.918 0.50 1 536 251 116 MET CB C 32.873 0.50 1 537 251 116 MET N N 118.923 0.10 1 538 252 117 GLY H H 8.188 0.05 1 539 252 117 GLY C C 173.982 0.50 1 540 252 117 GLY CA C 46.124 0.50 1 541 252 117 GLY N N 106.485 0.10 1 542 253 118 GLN H H 7.507 0.05 1 543 253 118 GLN C C 175.447 0.50 1 544 253 118 GLN CA C 55.278 0.50 1 545 253 118 GLN CB C 28.120 0.50 1 546 253 118 GLN N N 118.622 0.10 1 547 254 119 GLN H H 8.045 0.05 1 548 254 119 GLN C C 174.803 0.50 1 549 254 119 GLN CA C 57.722 0.50 1 550 254 119 GLN CB C 25.426 0.50 1 551 254 119 GLN N N 113.659 0.10 1 552 255 120 GLN H H 7.407 0.05 1 553 255 120 GLN C C 175.850 0.50 1 554 255 120 GLN CA C 56.058 0.50 1 555 255 120 GLN CB C 29.334 0.50 1 556 255 120 GLN N N 116.500 0.10 1 557 256 121 LEU H H 8.363 0.05 1 558 256 121 LEU CA C 55.996 0.50 1 559 256 121 LEU CB C 42.955 0.50 1 560 256 121 LEU N N 126.794 0.10 1 561 257 122 LEU H H 9.091 0.05 1 562 257 122 LEU C C 175.440 0.50 1 563 257 122 LEU CA C 53.429 0.50 1 564 257 122 LEU CB C 42.414 0.50 1 565 257 122 LEU N N 130.536 0.10 1 566 258 123 SER H H 8.495 0.05 1 567 258 123 SER C C 173.708 0.50 1 568 258 123 SER CA C 59.386 0.50 1 569 258 123 SER N N 121.461 0.10 1 570 259 124 LEU H H 7.754 0.05 1 571 259 124 LEU C C 174.652 0.50 1 572 259 124 LEU CA C 51.644 0.50 1 573 259 124 LEU CB C 44.231 0.50 1 574 259 124 LEU N N 123.495 0.10 1 575 260 125 PRO C C 177.616 0.50 1 576 260 125 PRO CA C 62.585 0.50 1 577 260 125 PRO CB C 32.187 0.50 1 578 261 126 THR H H 8.582 0.05 1 579 261 126 THR C C 177.734 0.50 1 580 261 126 THR CA C 64.457 0.50 1 581 261 126 THR CB C 68.845 0.50 1 582 261 126 THR N N 116.488 0.10 1 583 262 127 ASN CA C 52.085 0.50 1 584 263 128 ALA H H 7.536 0.05 1 585 263 128 ALA C C 179.075 0.50 1 586 263 128 ALA CA C 56.345 0.50 1 587 263 128 ALA CB C 17.931 0.50 1 588 263 128 ALA N N 124.014 0.10 1 589 264 129 GLU H H 9.263 0.05 1 590 264 129 GLU C C 175.222 0.50 1 591 264 129 GLU CA C 60.661 0.50 1 592 264 129 GLU CB C 28.331 0.50 1 593 264 129 GLU N N 115.085 0.10 1 594 265 130 LEU H H 7.822 0.05 1 595 265 130 LEU C C 175.947 0.50 1 596 265 130 LEU CA C 55.668 0.50 1 597 265 130 LEU CB C 41.378 0.50 1 598 265 130 LEU N N 116.305 0.10 1 599 266 131 ASN H H 8.065 0.05 1 600 266 131 ASN C C 173.748 0.50 1 601 266 131 ASN CA C 52.677 0.50 1 602 266 131 ASN CB C 40.677 0.50 1 603 266 131 ASN N N 119.911 0.10 1 604 267 132 VAL H H 8.739 0.05 1 605 267 132 VAL C C 176.204 0.50 1 606 267 132 VAL CA C 63.275 0.50 1 607 267 132 VAL CB C 32.391 0.50 1 608 267 132 VAL N N 121.944 0.10 1 609 268 133 GLU H H 8.705 0.05 1 610 268 133 GLU C C 175.544 0.50 1 611 268 133 GLU CA C 55.754 0.50 1 612 268 133 GLU CB C 32.445 0.50 1 613 268 133 GLU N N 124.914 0.10 1 614 269 134 ILE H H 8.546 0.05 1 615 269 134 ILE C C 174.868 0.50 1 616 269 134 ILE CA C 60.401 0.50 1 617 269 134 ILE CB C 38.938 0.50 1 618 269 134 ILE N N 122.647 0.10 1 619 270 135 MET H H 8.948 0.05 1 620 270 135 MET C C 174.304 0.50 1 621 270 135 MET CA C 53.659 0.50 1 622 270 135 MET CB C 36.974 0.50 1 623 270 135 MET N N 125.002 0.10 1 624 271 136 ALA H H 8.624 0.05 1 625 271 136 ALA C C 177.412 0.50 1 626 271 136 ALA CA C 51.351 0.50 1 627 271 136 ALA CB C 21.623 0.50 1 628 271 136 ALA N N 120.501 0.10 1 629 272 137 ASN H H 9.696 0.05 1 630 272 137 ASN C C 174.945 0.50 1 631 272 137 ASN CA C 53.861 0.50 1 632 272 137 ASN CB C 37.461 0.50 1 633 272 137 ASN N N 124.475 0.10 1 634 273 138 GLY H H 8.674 0.05 1 635 273 138 GLY C C 173.531 0.50 1 636 273 138 GLY CA C 45.370 0.50 1 637 273 138 GLY N N 102.578 0.10 1 638 274 139 VAL H H 7.877 0.05 1 639 274 139 VAL C C 175.222 0.50 1 640 274 139 VAL CA C 61.315 0.50 1 641 274 139 VAL CB C 33.264 0.50 1 642 274 139 VAL N N 122.174 0.10 1 643 275 140 LEU H H 8.473 0.05 1 644 275 140 LEU C C 175.318 0.50 1 645 275 140 LEU CA C 55.895 0.50 1 646 275 140 LEU CB C 42.263 0.50 1 647 275 140 LEU N N 127.969 0.10 1 648 276 141 LEU H H 9.019 0.05 1 649 276 141 LEU CA C 54.649 0.50 1 650 276 141 LEU N N 126.282 0.10 1 651 277 142 GLY H H 7.341 0.05 1 652 277 142 GLY C C 171.276 0.50 1 653 277 142 GLY CA C 45.552 0.50 1 654 277 142 GLY N N 101.773 0.10 1 655 278 143 ASN H H 8.997 0.05 1 656 278 143 ASN C C 175.254 0.50 1 657 278 143 ASN CA C 52.573 0.50 1 658 278 143 ASN CB C 42.593 0.50 1 659 278 143 ASN N N 114.107 0.10 1 660 279 144 GLY H H 9.194 0.05 1 661 279 144 GLY C C 169.398 0.50 1 662 279 144 GLY CA C 46.904 0.50 1 663 279 144 GLY N N 108.037 0.10 1 664 280 145 GLU H H 7.921 0.05 1 665 280 145 GLU CA C 53.093 0.50 1 666 280 145 GLU CB C 34.506 0.50 1 667 280 145 GLU N N 118.706 0.10 1 668 281 146 LEU H H 8.710 0.05 1 669 281 146 LEU C C 174.030 0.50 1 670 281 146 LEU CA C 55.412 0.50 1 671 281 146 LEU CB C 43.547 0.50 1 672 281 146 LEU N N 128.589 0.10 1 673 282 147 VAL H H 9.128 0.05 1 674 282 147 VAL C C 173.305 0.50 1 675 282 147 VAL CA C 58.918 0.50 1 676 282 147 VAL N N 119.034 0.10 1 677 283 148 GLN H H 8.678 0.05 1 678 283 148 GLN C C 174.449 0.50 1 679 283 148 GLN CA C 54.446 0.50 1 680 283 148 GLN CB C 31.500 0.50 1 681 283 148 GLN N N 119.095 0.10 1 682 285 150 ASN H H 9.130 0.05 1 683 285 150 ASN C C 174.320 0.50 1 684 285 150 ASN CA C 55.819 0.50 1 685 285 150 ASN CB C 36.635 0.50 1 686 285 150 ASN N N 122.099 0.10 1 687 286 151 ASP H H 8.549 0.05 1 688 286 151 ASP CA C 54.524 0.50 1 689 286 151 ASP CB C 40.638 0.50 1 690 286 151 ASP N N 121.064 0.10 1 691 287 152 THR H H 8.041 0.05 1 692 287 152 THR CA C 61.779 0.50 1 693 287 152 THR CB C 70.958 0.50 1 694 287 152 THR N N 117.145 0.10 1 695 288 153 LEU H H 8.730 0.05 1 696 288 153 LEU C C 176.107 0.50 1 697 288 153 LEU CA C 53.836 0.50 1 698 288 153 LEU CB C 45.000 0.50 1 699 288 153 LEU N N 125.435 0.10 1 700 289 154 GLY H H 8.632 0.05 1 701 289 154 GLY CA C 44.857 0.50 1 702 289 154 GLY N N 106.946 0.10 1 703 290 155 VAL H H 9.029 0.05 1 704 290 155 VAL C C 174.481 0.50 1 705 290 155 VAL CA C 60.271 0.50 1 706 290 155 VAL CB C 34.881 0.50 1 707 290 155 VAL N N 117.800 0.10 1 708 291 156 GLU H H 9.349 0.05 1 709 291 156 GLU CA C 54.598 0.50 1 710 291 156 GLU CB C 31.451 0.50 1 711 291 156 GLU N N 129.328 0.10 1 712 292 157 ILE H H 9.261 0.05 1 713 292 157 ILE C C 177.508 0.50 1 714 292 157 ILE CA C 62.098 0.50 1 715 292 157 ILE N N 129.234 0.10 1 716 293 158 HIS H H 9.801 0.05 1 717 293 158 HIS CA C 54.802 0.50 1 718 293 158 HIS CB C 31.264 0.50 1 719 293 158 HIS N N 127.352 0.10 1 720 295 160 TRP H H 8.832 0.05 1 721 295 160 TRP C C 175.221 0.50 1 722 295 160 TRP CA C 57.064 0.50 1 723 295 160 TRP CB C 32.814 0.50 1 724 295 160 TRP N N 125.928 0.10 1 725 296 161 LEU H H 8.010 0.05 1 726 296 161 LEU C C 176.002 0.50 1 727 296 161 LEU CA C 55.590 0.50 1 728 296 161 LEU CB C 41.179 0.50 1 729 296 161 LEU N N 128.121 0.10 1 730 297 162 SER H H 7.307 0.05 1 731 297 162 SER C C 178.732 0.50 1 732 297 162 SER CA C 59.334 0.50 1 733 297 162 SER CB C 65.094 0.50 1 734 297 162 SER N N 120.905 0.10 1 stop_ save_