data_18329 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of decorbin-binding protein A from Borrelia burgdorferi ; _BMRB_accession_number 18329 _BMRB_flat_file_name bmr18329.str _Entry_type original _Submission_date 2012-03-14 _Accession_date 2012-03-14 _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 Wang Xu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 residual_dipolar_couplings 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 746 "13C chemical shifts" 633 "15N chemical shifts" 156 "residual dipolar couplings" 215 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-01-15 original author . stop_ _Original_release_date 2013-01-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of decorin-binding protein A from Borrelia burgdorferi' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22985470 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Xu . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 51 _Journal_issue 42 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8353 _Page_last 8362 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name DBPA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DBPA $DBPA stop_ _System_molecular_weight 18525 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Binding cell surface glycosaminoglycans during bacterial infection' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DBPA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DBPA _Molecular_mass 37092.648 _Mol_thiol_state 'all disulfide bound' _Details 'disulfide bond between C173 and C188' ############################## # Polymer residue sequence # ############################## _Residue_count 336 _Mol_residue_sequence ; SAGLTGATKIRLERSAKDIT DEIDAIKKDAALKGVNFDAF KDKKTGSGVSENPFILEAKV RATTVAEKFVIAIEEEATKL KETGSSGEFSAMYDLMFEVS KPLQKLGIQEMTKTVSDAAE ENPPTTAQGVLEIAKKMREK LQRVHTKNYCTLKKKENSTF TDEKCKNNSAGLTGATKIRL ERSAKDITDEIDAIKKDAAL KGVNFDAFKDKKTGSGVSEN PFILEAKVRATTVAEKFVIA IEEEATKLKETGSSGEFSAM YDLMFEVSKPLQKLGIQEMT KTVSDAAEENPPTTAQGVLE IAKKMREKLQRVHTKNYCTL KKKENSTFTDEKCKNN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 24 SER 2 25 ALA 3 26 GLY 4 27 LEU 5 28 THR 6 29 GLY 7 30 ALA 8 31 THR 9 32 LYS 10 33 ILE 11 34 ARG 12 35 LEU 13 36 GLU 14 37 ARG 15 38 SER 16 39 ALA 17 40 LYS 18 41 ASP 19 42 ILE 20 43 THR 21 44 ASP 22 45 GLU 23 46 ILE 24 47 ASP 25 48 ALA 26 49 ILE 27 50 LYS 28 51 LYS 29 52 ASP 30 53 ALA 31 54 ALA 32 55 LEU 33 56 LYS 34 57 GLY 35 58 VAL 36 59 ASN 37 60 PHE 38 61 ASP 39 62 ALA 40 63 PHE 41 64 LYS 42 65 ASP 43 66 LYS 44 67 LYS 45 68 THR 46 69 GLY 47 70 SER 48 71 GLY 49 72 VAL 50 73 SER 51 74 GLU 52 75 ASN 53 76 PRO 54 77 PHE 55 78 ILE 56 79 LEU 57 80 GLU 58 81 ALA 59 82 LYS 60 83 VAL 61 84 ARG 62 85 ALA 63 86 THR 64 87 THR 65 88 VAL 66 89 ALA 67 90 GLU 68 91 LYS 69 92 PHE 70 93 VAL 71 94 ILE 72 95 ALA 73 96 ILE 74 97 GLU 75 98 GLU 76 99 GLU 77 100 ALA 78 101 THR 79 102 LYS 80 103 LEU 81 104 LYS 82 105 GLU 83 106 THR 84 107 GLY 85 108 SER 86 109 SER 87 110 GLY 88 111 GLU 89 112 PHE 90 113 SER 91 114 ALA 92 115 MET 93 116 TYR 94 117 ASP 95 118 LEU 96 119 MET 97 120 PHE 98 121 GLU 99 122 VAL 100 123 SER 101 124 LYS 102 125 PRO 103 126 LEU 104 127 GLN 105 128 LYS 106 129 LEU 107 130 GLY 108 131 ILE 109 132 GLN 110 133 GLU 111 134 MET 112 135 THR 113 136 LYS 114 137 THR 115 138 VAL 116 139 SER 117 140 ASP 118 141 ALA 119 142 ALA 120 143 GLU 121 144 GLU 122 145 ASN 123 146 PRO 124 147 PRO 125 148 THR 126 149 THR 127 150 ALA 128 151 GLN 129 152 GLY 130 153 VAL 131 154 LEU 132 155 GLU 133 156 ILE 134 157 ALA 135 158 LYS 136 159 LYS 137 160 MET 138 161 ARG 139 162 GLU 140 163 LYS 141 164 LEU 142 165 GLN 143 166 ARG 144 167 VAL 145 168 HIS 146 169 THR 147 170 LYS 148 171 ASN 149 172 TYR 150 173 CYS 151 174 THR 152 175 LEU 153 176 LYS 154 177 LYS 155 178 LYS 156 179 GLU 157 180 ASN 158 181 SER 159 182 THR 160 183 PHE 161 184 THR 162 185 ASP 163 186 GLU 164 187 LYS 165 188 CYS 166 189 LYS 167 190 ASN 168 191 ASN 169 192 SER 170 193 ALA 171 194 GLY 172 195 LEU 173 196 THR 174 197 GLY 175 198 ALA 176 199 THR 177 200 LYS 178 201 ILE 179 202 ARG 180 203 LEU 181 204 GLU 182 205 ARG 183 206 SER 184 207 ALA 185 208 LYS 186 209 ASP 187 210 ILE 188 211 THR 189 212 ASP 190 213 GLU 191 214 ILE 192 215 ASP 193 216 ALA 194 217 ILE 195 218 LYS 196 219 LYS 197 220 ASP 198 221 ALA 199 222 ALA 200 223 LEU 201 224 LYS 202 225 GLY 203 226 VAL 204 227 ASN 205 228 PHE 206 229 ASP 207 230 ALA 208 231 PHE 209 232 LYS 210 233 ASP 211 234 LYS 212 235 LYS 213 236 THR 214 237 GLY 215 238 SER 216 239 GLY 217 240 VAL 218 241 SER 219 242 GLU 220 243 ASN 221 244 PRO 222 245 PHE 223 246 ILE 224 247 LEU 225 248 GLU 226 249 ALA 227 250 LYS 228 251 VAL 229 252 ARG 230 253 ALA 231 254 THR 232 255 THR 233 256 VAL 234 257 ALA 235 258 GLU 236 259 LYS 237 260 PHE 238 261 VAL 239 262 ILE 240 263 ALA 241 264 ILE 242 265 GLU 243 266 GLU 244 267 GLU 245 268 ALA 246 269 THR 247 270 LYS 248 271 LEU 249 272 LYS 250 273 GLU 251 274 THR 252 275 GLY 253 276 SER 254 277 SER 255 278 GLY 256 279 GLU 257 280 PHE 258 281 SER 259 282 ALA 260 283 MET 261 284 TYR 262 285 ASP 263 286 LEU 264 287 MET 265 288 PHE 266 289 GLU 267 290 VAL 268 291 SER 269 292 LYS 270 293 PRO 271 294 LEU 272 295 GLN 273 296 LYS 274 297 LEU 275 298 GLY 276 299 ILE 277 300 GLN 278 301 GLU 279 302 MET 280 303 THR 281 304 LYS 282 305 THR 283 306 VAL 284 307 SER 285 308 ASP 286 309 ALA 287 310 ALA 288 311 GLU 289 312 GLU 290 313 ASN 291 314 PRO 292 315 PRO 293 316 THR 294 317 THR 295 318 ALA 296 319 GLN 297 320 GLY 298 321 VAL 299 322 LEU 300 323 GLU 301 324 ILE 302 325 ALA 303 326 LYS 304 327 LYS 305 328 MET 306 329 ARG 307 330 GLU 308 331 LYS 309 332 LEU 310 333 GLN 311 334 ARG 312 335 VAL 313 336 HIS 314 337 THR 315 338 LYS 316 339 ASN 317 340 TYR 318 341 CYS 319 342 THR 320 343 LEU 321 344 LYS 322 345 LYS 323 346 LYS 324 347 GLU 325 348 ASN 326 349 SER 327 350 THR 328 351 PHE 329 352 THR 330 353 ASP 331 354 GLU 332 355 LYS 333 356 CYS 334 357 LYS 335 358 ASN 336 359 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-22 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 2LQU "Structure Of Decorbin-binding Protein A From Borrelia Burgdorferi" 50.00 168 100.00 100.00 2.12e-113 EMBL CAG38080 "decorin binding protein [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 EMBL CAG38331 "decorin binding protein A [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 EMBL CAG38379 "decorin binding protein [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 EMBL CAG38382 "decorin binding protein [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 EMBL CAG38384 "decorin binding protein [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 GB AAC66250 "decorin-binding protein A [Borrelia burgdorferi B31]" 50.00 191 99.40 99.40 1.89e-112 GB AAC70047 "decorin binding protein A [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 GB AAC70053 "decorin binding protein A [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 GB AAC70064 "decorin binding protein A [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 GB AAL35357 "decorin-binding protein A [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 REF NP_045697 "decorin-binding protein A [Borrelia burgdorferi B31]" 50.00 191 99.40 99.40 1.89e-112 REF WP_010890380 "decorin-binding protein A [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 REF YP_009075678 "decorin binding protein A [Borrelia burgdorferi]" 50.00 191 99.40 99.40 1.89e-112 SP O50917 "RecName: Full=Decorin-binding protein A; Flags: Precursor" 50.00 191 99.40 99.40 1.89e-112 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $DBPA 'Borrelia burgdorferi str. B31' 224326 Bacteria . Borrelia burgdorferi B31 DBPA stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name _Details $DBPA 'recombinant technology' . Escherichia coli B21 DE3 pHUE 'expressed as a fusion protein with ubiquitin and cleaved with the enzyme USP2' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'isotropic sample' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DBPA 0.8 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 50 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ save_gel_sample _Saveframe_category sample _Sample_type 'gel solution' _Details 'anisotropic sample in 5% neutral gel' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DBPA 0.8 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 50 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' polyacrylamide 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model 'Inova 800' _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aliphatic_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_J-modulated_15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'J-modulated 15N HSQC' _Sample_label $gel_sample save_ save_JNC-modulated_15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'JNC-modulated 15N HSQC' _Sample_label $gel_sample save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 6.5 . pH pressure 1 . atm temperature 298 . 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 HNCACB' '3D CBCA(CO)NH' '3D 1H-13C NOESY aliphatic' '3D HCCH-TOCSY' 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 DBPA _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 25 2 ALA H H 8.6900 . 1 2 25 2 ALA HA H 4.3700 . 1 3 25 2 ALA HB H 1.3700 . 1 4 25 2 ALA CA C 52.3000 . 1 5 25 2 ALA CB C 19.7000 . 1 6 25 2 ALA N N 125.0000 . 1 7 26 3 GLY H H 7.9400 . 1 8 26 3 GLY HA2 H 3.7000 . 2 9 26 3 GLY HA3 H 3.7900 . 2 10 26 3 GLY CA C 44.0000 . 1 11 26 3 GLY N N 106.9200 . 1 12 27 4 LEU H H 8.2100 . 1 13 27 4 LEU HA H 4.4100 . 1 14 27 4 LEU HB3 H 2.6900 . 2 15 27 4 LEU HG H 1.6100 . 1 16 27 4 LEU HD1 H 0.8500 . 2 17 27 4 LEU HD2 H 0.9000 . 2 18 27 4 LEU C C 177.1000 . 1 19 27 4 LEU CA C 54.4000 . 1 20 27 4 LEU CB C 42.1000 . 1 21 27 4 LEU CG C 26.8000 . 1 22 27 4 LEU CD1 C 23.5000 . 2 23 27 4 LEU CD2 C 25.0000 . 2 24 27 4 LEU N N 119.1400 . 1 25 28 5 THR H H 9.2200 . 1 26 28 5 THR HA H 4.6500 . 1 27 28 5 THR HB H 4.1500 . 1 28 28 5 THR HG2 H 1.1300 . 1 29 28 5 THR C C 175.5000 . 1 30 28 5 THR CA C 60.1000 . 1 31 28 5 THR CB C 72.6000 . 1 32 28 5 THR CG2 C 21.2000 . 1 33 28 5 THR N N 112.9400 . 1 34 29 6 GLY H H 8.5200 . 1 35 29 6 GLY HA2 H 3.7700 . 2 36 29 6 GLY HA3 H 3.9800 . 2 37 29 6 GLY C C 174.8000 . 1 38 29 6 GLY CA C 46.0000 . 1 39 29 6 GLY N N 108.2300 . 1 40 30 7 ALA HA H 4.0400 . 1 41 30 7 ALA HB H 1.4800 . 1 42 30 7 ALA CA C 54.8000 . 1 43 30 7 ALA CB C 18.2000 . 1 44 31 8 THR H H 8.1100 . 1 45 31 8 THR HA H 3.7400 . 1 46 31 8 THR HB H 4.1600 . 1 47 31 8 THR HG2 H 1.2200 . 1 48 31 8 THR C C 175.3000 . 1 49 31 8 THR CA C 67.0000 . 1 50 31 8 THR CB C 68.7000 . 1 51 31 8 THR CG2 C 23.2000 . 1 52 31 8 THR N N 116.9700 . 1 53 32 9 LYS H H 6.8600 . 1 54 32 9 LYS HA H 3.5900 . 1 55 32 9 LYS HB3 H 1.7600 . 2 56 32 9 LYS HG3 H 1.4100 . 2 57 32 9 LYS C C 176.9000 . 1 58 32 9 LYS CA C 59.8000 . 1 59 32 9 LYS CB C 32.4000 . 1 60 32 9 LYS N N 120.5400 . 1 61 33 10 ILE H H 7.3800 . 1 62 33 10 ILE HA H 3.7100 . 1 63 33 10 ILE HB H 1.7500 . 1 64 33 10 ILE HG12 H 1.1700 . 2 65 33 10 ILE HG13 H 1.5700 . 2 66 33 10 ILE HG2 H 0.8900 . 1 67 33 10 ILE HD1 H 0.8000 . 1 68 33 10 ILE C C 179.0000 . 1 69 33 10 ILE CA C 64.0000 . 1 70 33 10 ILE CB C 38.0000 . 1 71 33 10 ILE CG1 C 28.9000 . 1 72 33 10 ILE CG2 C 17.0000 . 1 73 33 10 ILE CD1 C 12.5000 . 1 74 33 10 ILE N N 115.9400 . 1 75 34 11 ARG H H 8.2500 . 1 76 34 11 ARG HA H 4.0400 . 1 77 34 11 ARG HB2 H 1.6700 . 2 78 34 11 ARG HB3 H 2.0600 . 2 79 34 11 ARG HG2 H 1.7600 . 2 80 34 11 ARG HG3 H 1.4000 . 2 81 34 11 ARG HD3 H 3.1300 . 2 82 34 11 ARG C C 180.0000 . 1 83 34 11 ARG CA C 59.4000 . 1 84 34 11 ARG CB C 30.3000 . 1 85 34 11 ARG CG C 27.7000 . 1 86 34 11 ARG CD C 44.0000 . 1 87 34 11 ARG N N 118.3500 . 1 88 35 12 LEU H H 8.3400 . 1 89 35 12 LEU HA H 4.1700 . 1 90 35 12 LEU HB2 H 1.3300 . 2 91 35 12 LEU HB3 H 1.9100 . 2 92 35 12 LEU HG H 1.3400 . 1 93 35 12 LEU HD1 H 0.6800 . 2 94 35 12 LEU HD2 H 0.8900 . 2 95 35 12 LEU C C 179.0000 . 1 96 35 12 LEU CA C 58.0000 . 1 97 35 12 LEU CB C 40.8000 . 1 98 35 12 LEU CD1 C 22.1000 . 2 99 35 12 LEU CD2 C 26.5000 . 2 100 35 12 LEU N N 117.4200 . 1 101 36 13 GLU H H 8.6100 . 1 102 36 13 GLU HA H 4.0200 . 1 103 36 13 GLU HB2 H 2.1200 . 2 104 36 13 GLU HB3 H 1.9100 . 2 105 36 13 GLU HG2 H 2.1700 . 2 106 36 13 GLU HG3 H 2.6400 . 2 107 36 13 GLU C C 180.1000 . 1 108 36 13 GLU CA C 60.2000 . 1 109 36 13 GLU CB C 28.3000 . 1 110 36 13 GLU CG C 38.0500 . 1 111 36 13 GLU N N 117.8900 . 1 112 37 14 ARG H H 7.9800 . 1 113 37 14 ARG HA H 4.2400 . 1 114 37 14 ARG HB2 H 1.9900 . 2 115 37 14 ARG HB3 H 2.1200 . 2 116 37 14 ARG HG2 H 1.6400 . 2 117 37 14 ARG HG3 H 1.8500 . 2 118 37 14 ARG HD2 H 3.1900 . 2 119 37 14 ARG HD3 H 3.2400 . 2 120 37 14 ARG C C 178.1000 . 1 121 37 14 ARG CA C 58.5000 . 1 122 37 14 ARG CB C 30.2000 . 1 123 37 14 ARG CG C 26.8500 . 1 124 37 14 ARG CD C 43.4000 . 1 125 37 14 ARG N N 121.1000 . 1 126 38 15 SER H H 8.2300 . 1 127 38 15 SER HA H 4.3800 . 1 128 38 15 SER HB2 H 4.1700 . 2 129 38 15 SER HB3 H 4.2100 . 2 130 38 15 SER C C 177.3000 . 1 131 38 15 SER CA C 62.2000 . 1 132 38 15 SER CB C 63.2000 . 1 133 38 15 SER N N 115.4200 . 1 134 39 16 ALA H H 8.2800 . 1 135 39 16 ALA HA H 3.6300 . 1 136 39 16 ALA HB H 1.2500 . 1 137 39 16 ALA C C 179.5000 . 1 138 39 16 ALA CA C 54.7000 . 1 139 39 16 ALA CB C 18.0000 . 1 140 39 16 ALA N N 123.9700 . 1 141 40 17 LYS H H 7.9300 . 1 142 40 17 LYS HA H 4.0900 . 1 143 40 17 LYS HB2 H 1.8300 . 2 144 40 17 LYS HB3 H 2.0000 . 2 145 40 17 LYS HE3 H 2.9600 . 2 146 40 17 LYS C C 178.0000 . 1 147 40 17 LYS CA C 58.4000 . 1 148 40 17 LYS CB C 31.8000 . 1 149 40 17 LYS CE C 42.3000 . 1 150 40 17 LYS N N 121.6900 . 1 151 41 18 ASP H H 8.3200 . 1 152 41 18 ASP HA H 4.3600 . 1 153 41 18 ASP HB2 H 2.5500 . 2 154 41 18 ASP HB3 H 2.9500 . 2 155 41 18 ASP C C 179.9000 . 1 156 41 18 ASP CA C 57.7000 . 1 157 41 18 ASP CB C 39.6000 . 1 158 41 18 ASP N N 118.7300 . 1 159 42 19 ILE H H 7.4200 . 1 160 42 19 ILE HA H 3.6900 . 1 161 42 19 ILE HB H 2.1400 . 1 162 42 19 ILE HG13 H 1.9200 . 2 163 42 19 ILE HG2 H 0.7800 . 1 164 42 19 ILE HD1 H 0.7600 . 1 165 42 19 ILE C C 177.4000 . 1 166 42 19 ILE CA C 65.2000 . 1 167 42 19 ILE CB C 37.9000 . 1 168 42 19 ILE CG1 C 28.6000 . 1 169 42 19 ILE CG2 C 17.2000 . 1 170 42 19 ILE CD1 C 15.4000 . 1 171 42 19 ILE N N 118.1800 . 1 172 43 20 THR H H 7.6100 . 1 173 43 20 THR HA H 3.7700 . 1 174 43 20 THR HB H 4.3700 . 1 175 43 20 THR HG2 H 1.1700 . 1 176 43 20 THR C C 177.8000 . 1 177 43 20 THR CA C 66.4000 . 1 178 43 20 THR CB C 67.4000 . 1 179 43 20 THR CG2 C 22.5000 . 1 180 43 20 THR N N 113.3600 . 1 181 44 21 ASP H H 9.2600 . 1 182 44 21 ASP HA H 4.4100 . 1 183 44 21 ASP HB2 H 2.8100 . 2 184 44 21 ASP HB3 H 2.6500 . 2 185 44 21 ASP C C 179.2000 . 1 186 44 21 ASP CA C 57.2000 . 1 187 44 21 ASP CB C 39.6000 . 1 188 44 21 ASP N N 123.6500 . 1 189 45 22 GLU H H 7.7500 . 1 190 45 22 GLU HA H 4.3700 . 1 191 45 22 GLU HB2 H 2.0400 . 2 192 45 22 GLU HB3 H 2.2800 . 2 193 45 22 GLU HG2 H 2.2600 . 2 194 45 22 GLU HG3 H 2.4300 . 2 195 45 22 GLU C C 178.5000 . 1 196 45 22 GLU CA C 58.2000 . 1 197 45 22 GLU CB C 29.2000 . 1 198 45 22 GLU CG C 36.2000 . 1 199 45 22 GLU N N 123.5600 . 1 200 46 23 ILE H H 8.3600 . 1 201 46 23 ILE HA H 3.6200 . 1 202 46 23 ILE HB H 1.9700 . 1 203 46 23 ILE HG12 H 0.9800 . 2 204 46 23 ILE HG13 H 1.8100 . 2 205 46 23 ILE HG2 H 0.8700 . 1 206 46 23 ILE HD1 H 0.6400 . 1 207 46 23 ILE C C 177.6000 . 1 208 46 23 ILE CA C 65.6000 . 1 209 46 23 ILE CB C 37.0000 . 1 210 46 23 ILE CG1 C 29.2000 . 1 211 46 23 ILE CG2 C 17.5000 . 1 212 46 23 ILE CD1 C 13.3000 . 1 213 46 23 ILE N N 119.9400 . 1 214 47 24 ASP H H 8.2800 . 1 215 47 24 ASP HA H 4.4000 . 1 216 47 24 ASP HB2 H 2.6200 . 2 217 47 24 ASP HB3 H 2.8500 . 2 218 47 24 ASP C C 178.9000 . 1 219 47 24 ASP CA C 57.5000 . 1 220 47 24 ASP CB C 39.9000 . 1 221 47 24 ASP N N 120.7300 . 1 222 48 25 ALA H H 7.8800 . 1 223 48 25 ALA HA H 4.1200 . 1 224 48 25 ALA HB H 1.5400 . 1 225 48 25 ALA C C 180.4000 . 1 226 48 25 ALA CA C 55.5000 . 1 227 48 25 ALA CB C 17.8000 . 1 228 48 25 ALA N N 123.8700 . 1 229 49 26 ILE H H 8.7100 . 1 230 49 26 ILE HA H 3.7300 . 1 231 49 26 ILE HB H 2.1400 . 1 232 49 26 ILE HG2 H 0.9800 . 1 233 49 26 ILE HD1 H 0.9100 . 1 234 49 26 ILE C C 178.4000 . 1 235 49 26 ILE CA C 65.9000 . 1 236 49 26 ILE CB C 37.5000 . 1 237 49 26 ILE CG2 C 18.7000 . 1 238 49 26 ILE CD1 C 15.2000 . 1 239 49 26 ILE N N 121.9700 . 1 240 50 27 LYS H H 8.5400 . 1 241 50 27 LYS HA H 3.8800 . 1 242 50 27 LYS HB3 H 1.8800 . 2 243 50 27 LYS HG2 H 1.5100 . 2 244 50 27 LYS HG3 H 1.0700 . 2 245 50 27 LYS HE3 H 2.7400 . 2 246 50 27 LYS C C 179.9000 . 1 247 50 27 LYS CA C 60.4000 . 1 248 50 27 LYS CB C 31.9000 . 1 249 50 27 LYS CG C 25.8000 . 1 250 50 27 LYS CE C 41.7000 . 1 251 50 27 LYS N N 119.8200 . 1 252 51 28 LYS H H 8.0700 . 1 253 51 28 LYS HA H 4.0900 . 1 254 51 28 LYS C C 179.2000 . 1 255 51 28 LYS CA C 59.3000 . 1 256 51 28 LYS CB C 31.4000 . 1 257 51 28 LYS N N 121.9600 . 1 258 52 29 ASP H H 8.3400 . 1 259 52 29 ASP HA H 4.4700 . 1 260 52 29 ASP HB2 H 2.6800 . 2 261 52 29 ASP HB3 H 2.9800 . 2 262 52 29 ASP C C 178.5000 . 1 263 52 29 ASP CA C 57.0000 . 1 264 52 29 ASP CB C 41.0000 . 1 265 52 29 ASP N N 121.7100 . 1 266 53 30 ALA H H 8.8000 . 1 267 53 30 ALA HA H 3.3400 . 1 268 53 30 ALA HB H 1.5800 . 1 269 53 30 ALA C C 179.5000 . 1 270 53 30 ALA CA C 55.1000 . 1 271 53 30 ALA CB C 18.1000 . 1 272 53 30 ALA N N 121.9900 . 1 273 54 31 ALA H H 7.7300 . 1 274 54 31 ALA HA H 4.1500 . 1 275 54 31 ALA HB H 1.5300 . 1 276 54 31 ALA C C 181.6000 . 1 277 54 31 ALA CA C 54.7000 . 1 278 54 31 ALA CB C 17.8000 . 1 279 54 31 ALA N N 119.9700 . 1 280 55 32 LEU H H 7.6600 . 1 281 55 32 LEU HA H 4.1400 . 1 282 55 32 LEU HB2 H 1.6500 . 2 283 55 32 LEU HB3 H 1.9300 . 2 284 55 32 LEU HG H 1.7900 . 1 285 55 32 LEU HD1 H 0.9500 . 2 286 55 32 LEU HD2 H 0.8900 . 2 287 55 32 LEU C C 179.1000 . 1 288 55 32 LEU CA C 57.0000 . 1 289 55 32 LEU CB C 41.9000 . 1 290 55 32 LEU CG C 26.8000 . 1 291 55 32 LEU CD1 C 25.0000 . 2 292 55 32 LEU CD2 C 23.4000 . 2 293 55 32 LEU N N 119.6600 . 1 294 56 33 LYS H H 7.6100 . 1 295 56 33 LYS HA H 4.2100 . 1 296 56 33 LYS HB3 H 1.3600 . 2 297 56 33 LYS HG3 H 1.3100 . 2 298 56 33 LYS HD2 H 1.1900 . 2 299 56 33 LYS HD3 H 1.4100 . 2 300 56 33 LYS HE3 H 2.8700 . 2 301 56 33 LYS C C 176.6000 . 1 302 56 33 LYS CA C 56.1000 . 1 303 56 33 LYS CB C 33.2000 . 1 304 56 33 LYS CG C 25.6000 . 1 305 56 33 LYS CD C 28.9000 . 1 306 56 33 LYS N N 117.1600 . 1 307 57 34 GLY H H 7.7100 . 1 308 57 34 GLY HA2 H 3.7600 . 2 309 57 34 GLY HA3 H 4.0100 . 2 310 57 34 GLY C C 174.4000 . 1 311 57 34 GLY CA C 46.2000 . 1 312 57 34 GLY N N 108.6800 . 1 313 58 35 VAL H H 7.9900 . 1 314 58 35 VAL HA H 3.9000 . 1 315 58 35 VAL HB H 1.5400 . 1 316 58 35 VAL HG1 H 0.5400 . 2 317 58 35 VAL HG2 H 0.5900 . 2 318 58 35 VAL C C 174.2000 . 1 319 58 35 VAL CA C 61.5000 . 1 320 58 35 VAL CB C 32.8000 . 1 321 58 35 VAL CG1 C 20.8000 . 2 322 58 35 VAL CG2 C 21.0000 . 2 323 58 35 VAL N N 121.0000 . 1 324 59 36 ASN H H 8.4600 . 1 325 59 36 ASN HA H 4.6700 . 1 326 59 36 ASN HB2 H 2.8500 . 2 327 59 36 ASN HB3 H 2.7200 . 2 328 59 36 ASN C C 175.7000 . 1 329 59 36 ASN CA C 51.6000 . 1 330 59 36 ASN CB C 39.1000 . 1 331 59 36 ASN N N 124.9600 . 1 332 60 37 PHE H H 8.7800 . 1 333 60 37 PHE HA H 4.1400 . 1 334 60 37 PHE HB2 H 2.9800 . 2 335 60 37 PHE HB3 H 3.2000 . 2 336 60 37 PHE HD1 H 7.2500 . 3 337 60 37 PHE HE1 H 7.1500 . 3 338 60 37 PHE HZ H 7.0100 . 1 339 60 37 PHE C C 177.0000 . 1 340 60 37 PHE CA C 60.4000 . 1 341 60 37 PHE CB C 39.2000 . 1 342 60 37 PHE CD1 C 131.8000 . 3 343 60 37 PHE CE1 C 131.1000 . 3 344 60 37 PHE CZ C 128.9000 . 1 345 60 37 PHE N N 124.4600 . 1 346 61 38 ASP H H 8.4000 . 1 347 61 38 ASP HA H 4.4900 . 1 348 61 38 ASP HB2 H 2.6200 . 2 349 61 38 ASP HB3 H 2.7300 . 2 350 61 38 ASP C C 177.0000 . 1 351 61 38 ASP CA C 55.5000 . 1 352 61 38 ASP CB C 40.0000 . 1 353 61 38 ASP N N 119.2700 . 1 354 62 39 ALA H H 7.7400 . 1 355 62 39 ALA HA H 4.2000 . 1 356 62 39 ALA HB H 1.2900 . 1 357 62 39 ALA C C 178.3000 . 1 358 62 39 ALA CA C 52.9000 . 1 359 62 39 ALA CB C 18.5000 . 1 360 62 39 ALA N N 122.0200 . 1 361 63 40 PHE H H 7.7300 . 1 362 63 40 PHE HA H 4.3800 . 1 363 63 40 PHE HB2 H 3.1500 . 2 364 63 40 PHE HB3 H 2.9600 . 2 365 63 40 PHE HD2 H 7.2500 . 3 366 63 40 PHE HE2 H 7.1600 . 3 367 63 40 PHE HZ H 7.1000 . 1 368 63 40 PHE C C 176.1000 . 1 369 63 40 PHE CA C 58.3000 . 1 370 63 40 PHE CB C 38.8000 . 1 371 63 40 PHE CD2 C 131.8000 . 3 372 63 40 PHE CZ C 129.1000 . 1 373 63 40 PHE N N 116.9400 . 1 374 64 41 LYS H H 7.6500 . 1 375 64 41 LYS HA H 4.2200 . 1 376 64 41 LYS HB3 H 1.8000 . 2 377 64 41 LYS HG3 H 1.4000 . 2 378 64 41 LYS HE3 H 2.9800 . 2 379 64 41 LYS C C 176.1000 . 1 380 64 41 LYS CA C 56.6000 . 1 381 64 41 LYS CB C 32.9000 . 1 382 64 41 LYS CG C 24.6000 . 1 383 64 41 LYS CE C 42.2000 . 1 384 64 41 LYS N N 119.8400 . 1 385 65 42 ASP H H 8.0300 . 1 386 65 42 ASP HA H 4.5700 . 1 387 65 42 ASP HB2 H 2.6000 . 2 388 65 42 ASP HB3 H 2.7200 . 2 389 65 42 ASP C C 176.1000 . 1 390 65 42 ASP CA C 54.2000 . 1 391 65 42 ASP CB C 40.9000 . 1 392 65 42 ASP N N 120.7700 . 1 393 66 43 LYS H H 8.1800 . 1 394 66 43 LYS HA H 4.2800 . 1 395 66 43 LYS HB3 H 1.8200 . 2 396 66 43 LYS HG3 H 1.4200 . 2 397 66 43 LYS HE3 H 2.9700 . 2 398 66 43 LYS C C 176.8000 . 1 399 66 43 LYS CA C 56.5000 . 1 400 66 43 LYS CB C 32.8000 . 1 401 66 43 LYS CE C 42.1000 . 1 402 66 43 LYS N N 122.0700 . 1 403 67 44 LYS H H 8.4600 . 1 404 67 44 LYS HA H 4.3500 . 1 405 67 44 LYS HB2 H 1.8000 . 2 406 67 44 LYS HB3 H 1.8500 . 2 407 67 44 LYS HG3 H 1.4100 . 2 408 67 44 LYS HD3 H 1.5400 . 2 409 67 44 LYS HE3 H 2.6700 . 2 410 67 44 LYS C C 177.0000 . 1 411 67 44 LYS CA C 56.6000 . 1 412 67 44 LYS CB C 32.8000 . 1 413 67 44 LYS CG C 23.6000 . 1 414 67 44 LYS CD C 29.5000 . 1 415 67 44 LYS CE C 41.4000 . 1 416 67 44 LYS N N 122.1700 . 1 417 68 45 THR H H 8.1200 . 1 418 68 45 THR HA H 4.3300 . 1 419 68 45 THR HB H 4.2300 . 1 420 68 45 THR HG2 H 1.1800 . 1 421 68 45 THR C C 175.2000 . 1 422 68 45 THR CA C 62.0000 . 1 423 68 45 THR CB C 69.9000 . 1 424 68 45 THR CG2 C 21.7000 . 1 425 68 45 THR N N 114.3900 . 1 426 69 46 GLY H H 8.4500 . 1 427 69 46 GLY CA C 45.2000 . 1 428 69 46 GLY N N 111.2000 . 1 429 70 47 SER CA C 58.4000 . 1 430 70 47 SER CB C 64.0000 . 1 431 71 48 GLY H H 8.5800 . 1 432 71 48 GLY HA2 H 2.8300 . 2 433 71 48 GLY HA3 H 3.3600 . 2 434 71 48 GLY CA C 45.0000 . 1 435 71 48 GLY N N 111.2000 . 1 436 72 49 VAL H H 7.8600 . 1 437 72 49 VAL HA H 4.1300 . 1 438 72 49 VAL HB H 2.0800 . 1 439 72 49 VAL HG1 H 0.8900 . 2 440 72 49 VAL HG2 H 0.9200 . 2 441 72 49 VAL C C 176.1000 . 1 442 72 49 VAL CA C 62.1000 . 1 443 72 49 VAL CB C 32.5000 . 1 444 72 49 VAL CG1 C 20.7000 . 2 445 72 49 VAL CG2 C 21.3000 . 2 446 72 49 VAL N N 118.9100 . 1 447 73 50 SER H H 8.3000 . 1 448 73 50 SER HB2 H 3.8000 . 2 449 73 50 SER HB3 H 3.8900 . 2 450 73 50 SER C C 176.1000 . 1 451 73 50 SER CA C 58.3000 . 1 452 73 50 SER CB C 63.8000 . 1 453 73 50 SER N N 118.5000 . 1 454 74 51 GLU H H 8.3600 . 1 455 74 51 GLU HA H 4.2700 . 1 456 74 51 GLU HB2 H 1.9700 . 2 457 74 51 GLU HB3 H 1.8500 . 2 458 74 51 GLU HG2 H 2.1600 . 2 459 74 51 GLU HG3 H 2.2700 . 2 460 74 51 GLU CA C 55.7000 . 1 461 74 51 GLU CB C 30.5000 . 1 462 74 51 GLU CG C 36.6000 . 1 463 74 51 GLU N N 122.5600 . 1 464 75 52 ASN H H 8.4500 . 1 465 75 52 ASN HA H 4.8200 . 1 466 75 52 ASN HB2 H 2.8300 . 2 467 75 52 ASN HB3 H 2.7200 . 2 468 75 52 ASN C C 174.8000 . 1 469 75 52 ASN CA C 51.4000 . 1 470 75 52 ASN CB C 39.2000 . 1 471 75 52 ASN N N 122.8300 . 1 472 76 53 PRO HA H 4.1800 . 1 473 76 53 PRO HB2 H 2.2400 . 2 474 76 53 PRO HG2 H 2.1000 . 2 475 76 53 PRO HG3 H 1.9500 . 2 476 76 53 PRO HD2 H 3.9800 . 2 477 76 53 PRO HD3 H 3.8100 . 2 478 76 53 PRO CA C 65.2000 . 1 479 76 53 PRO CB C 32.0000 . 1 480 76 53 PRO CG C 27.6500 . 1 481 76 53 PRO CD C 51.4000 . 1 482 77 54 PHE H H 8.4300 . 1 483 77 54 PHE HA H 4.2700 . 1 484 77 54 PHE HB2 H 2.7800 . 2 485 77 54 PHE HB3 H 3.2300 . 2 486 77 54 PHE HD1 H 7.1500 . 3 487 77 54 PHE HE1 H 7.3200 . 3 488 77 54 PHE HZ H 7.2600 . 1 489 77 54 PHE C C 177.5000 . 1 490 77 54 PHE CA C 61.5000 . 1 491 77 54 PHE CB C 39.4000 . 1 492 77 54 PHE CD1 C 132.1000 . 3 493 77 54 PHE CE1 C 130.8000 . 3 494 77 54 PHE N N 118.0600 . 1 495 78 55 ILE H H 7.5400 . 1 496 78 55 ILE HA H 3.5000 . 1 497 78 55 ILE HB H 2.0000 . 1 498 78 55 ILE HG12 H 0.9200 . 2 499 78 55 ILE HG13 H 1.3500 . 2 500 78 55 ILE HG2 H 0.8400 . 1 501 78 55 ILE HD1 H 0.5900 . 1 502 78 55 ILE C C 177.4000 . 1 503 78 55 ILE CA C 63.5000 . 1 504 78 55 ILE CB C 37.0000 . 1 505 78 55 ILE CG1 C 28.8000 . 1 506 78 55 ILE CG2 C 17.4000 . 1 507 78 55 ILE CD1 C 12.0000 . 1 508 78 55 ILE N N 119.3500 . 1 509 79 56 LEU H H 7.2600 . 1 510 79 56 LEU HA H 4.1500 . 1 511 79 56 LEU HD1 H 0.7600 . 2 512 79 56 LEU HD2 H 1.0000 . 2 513 79 56 LEU C C 179.2000 . 1 514 79 56 LEU CA C 57.8000 . 1 515 79 56 LEU CB C 41.1000 . 1 516 79 56 LEU CD1 C 26.1000 . 2 517 79 56 LEU CD2 C 23.7000 . 2 518 79 56 LEU N N 118.4500 . 1 519 80 57 GLU H H 7.8900 . 1 520 80 57 GLU HA H 3.6500 . 1 521 80 57 GLU HB2 H 1.9900 . 2 522 80 57 GLU HB3 H 1.8700 . 2 523 80 57 GLU HG2 H 2.0400 . 2 524 80 57 GLU HG3 H 2.2600 . 2 525 80 57 GLU C C 178.7000 . 1 526 80 57 GLU CA C 59.3000 . 1 527 80 57 GLU CB C 29.5000 . 1 528 80 57 GLU CG C 36.5000 . 1 529 80 57 GLU N N 117.9800 . 1 530 81 58 ALA H H 8.4000 . 1 531 81 58 ALA HA H 3.8000 . 1 532 81 58 ALA HB H 1.4200 . 1 533 81 58 ALA C C 179.5000 . 1 534 81 58 ALA CA C 55.2000 . 1 535 81 58 ALA CB C 18.8000 . 1 536 81 58 ALA N N 122.0400 . 1 537 82 59 LYS H H 8.0000 . 1 538 82 59 LYS HA H 3.8500 . 1 539 82 59 LYS HB3 H 2.0100 . 2 540 82 59 LYS HG3 H 1.2800 . 2 541 82 59 LYS HD3 H 1.6700 . 2 542 82 59 LYS HE3 H 2.8800 . 2 543 82 59 LYS C C 180.3000 . 1 544 82 59 LYS CA C 61.1000 . 1 545 82 59 LYS CB C 32.2000 . 1 546 82 59 LYS CG C 24.7000 . 1 547 82 59 LYS CD C 29.7000 . 1 548 82 59 LYS CE C 41.7500 . 1 549 82 59 LYS N N 116.0000 . 1 550 83 60 VAL H H 8.1100 . 1 551 83 60 VAL HA H 3.3300 . 1 552 83 60 VAL HB H 2.2900 . 1 553 83 60 VAL HG1 H 0.9500 . 2 554 83 60 VAL HG2 H 0.8700 . 2 555 83 60 VAL C C 178.3000 . 1 556 83 60 VAL CA C 67.9000 . 1 557 83 60 VAL CB C 31.2000 . 1 558 83 60 VAL CG1 C 23.3000 . 2 559 83 60 VAL CG2 C 21.5000 . 2 560 83 60 VAL N N 122.9200 . 1 561 84 61 ARG H H 8.7100 . 1 562 84 61 ARG C C 179.5000 . 1 563 84 61 ARG CA C 59.2000 . 1 564 84 61 ARG CB C 30.8000 . 1 565 84 61 ARG N N 121.7700 . 1 566 85 62 ALA H H 8.7000 . 1 567 85 62 ALA HA H 3.8900 . 1 568 85 62 ALA HB H 1.2600 . 1 569 85 62 ALA C C 179.5000 . 1 570 85 62 ALA CA C 55.0000 . 1 571 85 62 ALA CB C 19.0000 . 1 572 85 62 ALA N N 119.4500 . 1 573 86 63 THR H H 8.1500 . 1 574 86 63 THR HA H 3.9700 . 1 575 86 63 THR HG2 H 1.4200 . 1 576 86 63 THR C C 177.7000 . 1 577 86 63 THR CA C 66.0000 . 1 578 86 63 THR CB C 68.2000 . 1 579 86 63 THR CG2 C 23.5000 . 1 580 86 63 THR N N 106.6500 . 1 581 87 64 THR H H 7.9200 . 1 582 87 64 THR HA H 4.0500 . 1 583 87 64 THR HB H 4.3500 . 1 584 87 64 THR HG2 H 1.2000 . 1 585 87 64 THR C C 176.8000 . 1 586 87 64 THR CA C 67.3000 . 1 587 87 64 THR CB C 68.6000 . 1 588 87 64 THR N N 120.4300 . 1 589 88 65 VAL H H 7.3800 . 1 590 88 65 VAL HA H 3.9800 . 1 591 88 65 VAL HB H 2.1100 . 1 592 88 65 VAL HG1 H 1.1000 . 2 593 88 65 VAL HG2 H 1.1000 . 2 594 88 65 VAL C C 178.5000 . 1 595 88 65 VAL CA C 65.6000 . 1 596 88 65 VAL CB C 31.7000 . 1 597 88 65 VAL CG1 C 22.5000 . 2 598 88 65 VAL CG2 C 21.7000 . 2 599 88 65 VAL N N 119.2300 . 1 600 89 66 ALA H H 8.3900 . 1 601 89 66 ALA HA H 4.2500 . 1 602 89 66 ALA HB H 1.4900 . 1 603 89 66 ALA C C 179.9000 . 1 604 89 66 ALA CA C 54.9000 . 1 605 89 66 ALA CB C 19.5000 . 1 606 89 66 ALA N N 124.2600 . 1 607 90 67 GLU H H 8.5200 . 1 608 90 67 GLU HA H 3.7200 . 1 609 90 67 GLU HB3 H 2.3100 . 2 610 90 67 GLU C C 177.6000 . 1 611 90 67 GLU CA C 59.9000 . 1 612 90 67 GLU CB C 28.3000 . 1 613 90 67 GLU N N 120.1800 . 1 614 91 68 LYS H H 7.2100 . 1 615 91 68 LYS HA H 3.9600 . 1 616 91 68 LYS HB3 H 2.0700 . 2 617 91 68 LYS HG2 H 1.5100 . 2 618 91 68 LYS HG3 H 1.7300 . 2 619 91 68 LYS HE3 H 2.9500 . 2 620 91 68 LYS C C 179.2000 . 1 621 91 68 LYS CA C 59.8000 . 1 622 91 68 LYS CB C 32.0000 . 1 623 91 68 LYS CG C 25.4000 . 1 624 91 68 LYS CE C 42.1000 . 1 625 91 68 LYS N N 116.3400 . 1 626 92 69 PHE H H 7.1800 . 1 627 92 69 PHE HA H 4.5100 . 1 628 92 69 PHE HB2 H 3.4600 . 2 629 92 69 PHE HB3 H 3.3100 . 2 630 92 69 PHE HD1 H 7.1500 . 3 631 92 69 PHE C C 175.1000 . 1 632 92 69 PHE CA C 59.8000 . 1 633 92 69 PHE CB C 39.2000 . 1 634 92 69 PHE CD1 C 132.3000 . 3 635 92 69 PHE N N 120.9900 . 1 636 93 70 VAL H H 7.9300 . 1 637 93 70 VAL HA H 3.0900 . 1 638 93 70 VAL HB H 2.0100 . 1 639 93 70 VAL HG1 H 1.0600 . 2 640 93 70 VAL HG2 H 1.1500 . 2 641 93 70 VAL C C 177.5000 . 1 642 93 70 VAL CA C 66.9000 . 1 643 93 70 VAL CB C 31.4000 . 1 644 93 70 VAL CG1 C 24.7300 . 2 645 93 70 VAL CG2 C 23.8200 . 2 646 93 70 VAL N N 120.3300 . 1 647 94 71 ILE H H 8.1800 . 1 648 94 71 ILE HA H 3.8300 . 1 649 94 71 ILE HB H 1.7000 . 1 650 94 71 ILE HG13 H 1.0000 . 2 651 94 71 ILE HG2 H 0.8300 . 1 652 94 71 ILE HD1 H 0.8100 . 1 653 94 71 ILE C C 177.7000 . 1 654 94 71 ILE CA C 65.0000 . 1 655 94 71 ILE CB C 37.3000 . 1 656 94 71 ILE CG1 C 29.7000 . 1 657 94 71 ILE CG2 C 17.2000 . 1 658 94 71 ILE CD1 C 13.8000 . 1 659 94 71 ILE N N 120.4100 . 1 660 95 72 ALA H H 7.3400 . 1 661 95 72 ALA HA H 3.9600 . 1 662 95 72 ALA HB H 1.3900 . 1 663 95 72 ALA C C 179.6000 . 1 664 95 72 ALA CA C 55.9000 . 1 665 95 72 ALA CB C 17.2000 . 1 666 95 72 ALA N N 122.4400 . 1 667 96 73 ILE H H 7.8200 . 1 668 96 73 ILE HA H 3.4400 . 1 669 96 73 ILE HB H 2.3700 . 1 670 96 73 ILE HG2 H 0.7500 . 1 671 96 73 ILE HD1 H 0.6600 . 1 672 96 73 ILE C C 177.4000 . 1 673 96 73 ILE CA C 62.8000 . 1 674 96 73 ILE CB C 34.4000 . 1 675 96 73 ILE CG1 C 25.8000 . 1 676 96 73 ILE CG2 C 16.4500 . 1 677 96 73 ILE CD1 C 10.6000 . 1 678 96 73 ILE N N 119.3300 . 1 679 97 74 GLU H H 8.3800 . 1 680 97 74 GLU HA H 3.6900 . 1 681 97 74 GLU HB2 H 1.8700 . 2 682 97 74 GLU HB3 H 2.3700 . 2 683 97 74 GLU HG2 H 1.9300 . 2 684 97 74 GLU HG3 H 2.5300 . 2 685 97 74 GLU C C 180.5000 . 1 686 97 74 GLU CA C 59.7000 . 1 687 97 74 GLU CB C 29.7000 . 1 688 97 74 GLU CG C 37.5000 . 1 689 97 74 GLU N N 118.4400 . 1 690 98 75 GLU H H 8.8000 . 1 691 98 75 GLU HA H 3.9400 . 1 692 98 75 GLU HB2 H 2.2400 . 2 693 98 75 GLU HB3 H 1.9300 . 2 694 98 75 GLU HG3 H 2.7000 . 2 695 98 75 GLU C C 180.6000 . 1 696 98 75 GLU CA C 59.7000 . 1 697 98 75 GLU CB C 30.2000 . 1 698 98 75 GLU CG C 36.5000 . 1 699 98 75 GLU N N 120.4700 . 1 700 99 76 GLU H H 8.8400 . 1 701 99 76 GLU HA H 4.1400 . 1 702 99 76 GLU HB3 H 1.9800 . 2 703 99 76 GLU C C 178.9000 . 1 704 99 76 GLU CA C 58.6000 . 1 705 99 76 GLU CB C 29.3000 . 1 706 99 76 GLU N N 119.2300 . 1 707 100 77 ALA H H 9.4000 . 1 708 100 77 ALA HA H 4.0000 . 1 709 100 77 ALA HB H 1.4700 . 1 710 100 77 ALA C C 179.0000 . 1 711 100 77 ALA CA C 56.3000 . 1 712 100 77 ALA CB C 16.8000 . 1 713 100 77 ALA N N 121.9500 . 1 714 101 78 THR H H 7.7700 . 1 715 101 78 THR HA H 3.7500 . 1 716 101 78 THR HB H 4.3200 . 1 717 101 78 THR HG2 H 1.2200 . 1 718 101 78 THR CA C 67.5000 . 1 719 101 78 THR CB C 68.6000 . 1 720 101 78 THR CG2 C 21.0000 . 1 721 101 78 THR N N 111.8200 . 1 722 102 79 LYS H H 7.8700 . 1 723 102 79 LYS HA H 4.0900 . 1 724 102 79 LYS HB3 H 1.9800 . 2 725 102 79 LYS HE3 H 2.9500 . 2 726 102 79 LYS CA C 59.2000 . 1 727 102 79 LYS CB C 32.5000 . 1 728 102 79 LYS CE C 42.1000 . 1 729 102 79 LYS N N 122.9400 . 1 730 103 80 LEU H H 7.5500 . 1 731 103 80 LEU HA H 4.4900 . 1 732 103 80 LEU HB3 H 1.6800 . 2 733 103 80 LEU HG H 1.7300 . 1 734 103 80 LEU HD1 H 0.6900 . 2 735 103 80 LEU HD2 H 0.6800 . 2 736 103 80 LEU C C 178.1400 . 1 737 103 80 LEU CA C 54.0000 . 1 738 103 80 LEU CB C 43.1000 . 1 739 103 80 LEU CG C 27.3000 . 1 740 103 80 LEU CD1 C 22.9000 . 2 741 103 80 LEU CD2 C 24.8000 . 2 742 103 80 LEU N N 117.6900 . 1 743 104 81 LYS H H 7.5000 . 1 744 104 81 LYS HA H 3.9300 . 1 745 104 81 LYS HB2 H 2.0300 . 2 746 104 81 LYS HB3 H 1.9400 . 2 747 104 81 LYS HE3 H 2.9900 . 2 748 104 81 LYS C C 178.0000 . 1 749 104 81 LYS CA C 61.3000 . 1 750 104 81 LYS CB C 32.8000 . 1 751 104 81 LYS N N 122.2100 . 1 752 105 82 GLU H H 8.7800 . 1 753 105 82 GLU HA H 4.5600 . 1 754 105 82 GLU HB2 H 2.0600 . 2 755 105 82 GLU HB3 H 2.2500 . 2 756 105 82 GLU HG3 H 2.3300 . 2 757 105 82 GLU C C 177.9000 . 1 758 105 82 GLU CA C 57.6600 . 1 759 105 82 GLU CB C 30.4000 . 1 760 105 82 GLU CG C 36.8000 . 1 761 105 82 GLU N N 114.9200 . 1 762 106 83 THR H H 7.5700 . 1 763 106 83 THR HA H 4.5500 . 1 764 106 83 THR HB H 4.3600 . 1 765 106 83 THR HG2 H 1.1900 . 1 766 106 83 THR C C 176.3000 . 1 767 106 83 THR CA C 61.9000 . 1 768 106 83 THR CB C 70.4000 . 1 769 106 83 THR CG2 C 21.9000 . 1 770 106 83 THR N N 107.2600 . 1 771 107 84 GLY H H 9.0000 . 1 772 107 84 GLY HA2 H 3.4300 . 2 773 107 84 GLY HA3 H 4.1500 . 2 774 107 84 GLY C C 172.8000 . 1 775 107 84 GLY CA C 45.4000 . 1 776 107 84 GLY N N 112.1100 . 1 777 108 85 SER H H 8.9500 . 1 778 108 85 SER CA C 56.3000 . 1 779 108 85 SER CB C 66.3000 . 1 780 108 85 SER N N 119.0300 . 1 781 109 86 SER HA H 4.4800 . 1 782 109 86 SER HB2 H 4.0100 . 2 783 109 86 SER HB3 H 4.1100 . 2 784 109 86 SER C C 177.0000 . 1 785 109 86 SER CA C 61.6000 . 1 786 109 86 SER CB C 62.9000 . 1 787 110 87 GLY H H 8.4800 . 1 788 110 87 GLY HA2 H 3.8400 . 2 789 110 87 GLY HA3 H 3.9800 . 2 790 110 87 GLY C C 177.1000 . 1 791 110 87 GLY CA C 46.2000 . 1 792 110 87 GLY N N 108.1000 . 1 793 111 88 GLU H H 7.5600 . 1 794 111 88 GLU HA H 3.6900 . 1 795 111 88 GLU C C 177.7000 . 1 796 111 88 GLU CA C 59.5000 . 1 797 111 88 GLU CB C 28.7000 . 1 798 111 88 GLU N N 123.0400 . 1 799 112 89 PHE H H 7.2000 . 1 800 112 89 PHE HA H 4.4200 . 1 801 112 89 PHE HB2 H 2.6100 . 2 802 112 89 PHE HB3 H 3.0000 . 2 803 112 89 PHE HD2 H 7.0400 . 3 804 112 89 PHE HE2 H 6.8700 . 3 805 112 89 PHE HZ H 7.3400 . 1 806 112 89 PHE C C 178.6000 . 1 807 112 89 PHE CA C 61.1000 . 1 808 112 89 PHE CB C 37.9000 . 1 809 112 89 PHE CD2 C 132.3000 . 3 810 112 89 PHE N N 118.2700 . 1 811 113 90 SER H H 8.8300 . 1 812 113 90 SER HA H 4.2900 . 1 813 113 90 SER HB2 H 3.9700 . 2 814 113 90 SER HB3 H 4.0300 . 2 815 113 90 SER C C 178.6000 . 1 816 113 90 SER CA C 62.7000 . 1 817 113 90 SER CB C 62.8000 . 1 818 113 90 SER N N 115.9800 . 1 819 114 91 ALA H H 7.5800 . 1 820 114 91 ALA HA H 4.3800 . 1 821 114 91 ALA HB H 1.6100 . 1 822 114 91 ALA C C 181.3000 . 1 823 114 91 ALA CA C 54.7000 . 1 824 114 91 ALA CB C 18.4000 . 1 825 114 91 ALA N N 123.1300 . 1 826 115 92 MET H H 7.8800 . 1 827 115 92 MET HA H 3.9800 . 1 828 115 92 MET HE H 1.8500 . 1 829 115 92 MET C C 178.0000 . 1 830 115 92 MET CA C 61.0000 . 1 831 115 92 MET CB C 31.4000 . 1 832 115 92 MET CE C 19.1000 . 1 833 115 92 MET N N 118.7000 . 1 834 116 93 TYR H H 7.8700 . 1 835 116 93 TYR HA H 4.2800 . 1 836 116 93 TYR HB2 H 3.0000 . 2 837 116 93 TYR HB3 H 3.4200 . 2 838 116 93 TYR HD2 H 7.1400 . 3 839 116 93 TYR HE2 H 6.6500 . 3 840 116 93 TYR C C 176.3000 . 1 841 116 93 TYR CA C 62.1000 . 1 842 116 93 TYR CB C 38.3000 . 1 843 116 93 TYR CD2 C 132.9000 . 3 844 116 93 TYR CE2 C 118.5000 . 3 845 116 93 TYR N N 119.2000 . 1 846 117 94 ASP H H 8.7200 . 1 847 117 94 ASP HA H 4.1900 . 1 848 117 94 ASP HB2 H 2.7300 . 2 849 117 94 ASP HB3 H 2.8300 . 2 850 117 94 ASP C C 179.0000 . 1 851 117 94 ASP CA C 57.7000 . 1 852 117 94 ASP CB C 40.0000 . 1 853 117 94 ASP N N 120.2100 . 1 854 118 95 LEU H H 7.5100 . 1 855 118 95 LEU HA H 4.2100 . 1 856 118 95 LEU HB2 H 1.6700 . 2 857 118 95 LEU HB3 H 2.1500 . 2 858 118 95 LEU HG H 1.9300 . 1 859 118 95 LEU HD1 H 0.9200 . 2 860 118 95 LEU HD2 H 0.9000 . 2 861 118 95 LEU C C 178.6000 . 1 862 118 95 LEU CA C 57.7000 . 1 863 118 95 LEU CB C 43.1000 . 1 864 118 95 LEU CG C 26.8000 . 1 865 118 95 LEU CD1 C 26.2000 . 2 866 118 95 LEU CD2 C 24.2000 . 2 867 118 95 LEU N N 118.4200 . 1 868 119 96 MET H H 7.8200 . 1 869 119 96 MET HA H 3.9900 . 1 870 119 96 MET HB2 H 2.2200 . 2 871 119 96 MET HB3 H 2.5400 . 2 872 119 96 MET HE H 1.9700 . 1 873 119 96 MET C C 177.5000 . 1 874 119 96 MET CA C 60.5000 . 1 875 119 96 MET CB C 33.9000 . 1 876 119 96 MET CE C 17.6000 . 1 877 119 96 MET N N 118.4700 . 1 878 120 97 PHE H H 8.9400 . 1 879 120 97 PHE HA H 3.8100 . 1 880 120 97 PHE HB2 H 2.4100 . 2 881 120 97 PHE HB3 H 2.9400 . 2 882 120 97 PHE HD1 H 7.1300 . 3 883 120 97 PHE C C 178.8000 . 1 884 120 97 PHE CA C 61.8000 . 1 885 120 97 PHE CB C 39.2000 . 1 886 120 97 PHE CD1 C 131.6000 . 3 887 120 97 PHE N N 119.5800 . 1 888 121 98 GLU H H 8.6900 . 1 889 121 98 GLU HA H 3.8800 . 1 890 121 98 GLU HB2 H 2.0400 . 2 891 121 98 GLU HB3 H 2.2000 . 2 892 121 98 GLU HG2 H 2.3000 . 2 893 121 98 GLU HG3 H 2.4600 . 2 894 121 98 GLU C C 180.8000 . 1 895 121 98 GLU CA C 59.8000 . 1 896 121 98 GLU CB C 29.2000 . 1 897 121 98 GLU CG C 35.9000 . 1 898 121 98 GLU N N 119.9400 . 1 899 122 99 VAL H H 8.2100 . 1 900 122 99 VAL HA H 3.7400 . 1 901 122 99 VAL HB H 1.9500 . 1 902 122 99 VAL HG1 H 0.5600 . 2 903 122 99 VAL HG2 H 0.6100 . 2 904 122 99 VAL C C 176.5000 . 1 905 122 99 VAL CA C 64.5000 . 1 906 122 99 VAL CB C 31.3000 . 1 907 122 99 VAL CG1 C 21.2000 . 2 908 122 99 VAL CG2 C 21.1000 . 2 909 122 99 VAL N N 115.3500 . 1 910 123 100 SER H H 7.5200 . 1 911 123 100 SER HA H 4.2700 . 1 912 123 100 SER HB3 H 4.2000 . 2 913 123 100 SER C C 174.7000 . 1 914 123 100 SER CA C 62.0000 . 1 915 123 100 SER N N 115.4500 . 1 916 124 101 LYS H H 6.9300 . 1 917 124 101 LYS HA H 3.9700 . 1 918 124 101 LYS HG2 H 1.2700 . 2 919 124 101 LYS HG3 H 1.1200 . 2 920 124 101 LYS C C 176.6000 . 1 921 124 101 LYS CA C 61.1000 . 1 922 124 101 LYS CB C 28.5000 . 1 923 124 101 LYS CG C 25.2000 . 1 924 124 101 LYS N N 120.3100 . 1 925 125 102 PRO HA H 4.2600 . 1 926 125 102 PRO HB2 H 2.2500 . 2 927 125 102 PRO HB3 H 1.6700 . 2 928 125 102 PRO HG3 H 1.9200 . 2 929 125 102 PRO HD2 H 3.3900 . 2 930 125 102 PRO HD3 H 4.2700 . 2 931 125 102 PRO CA C 65.2000 . 1 932 125 102 PRO CB C 30.6000 . 1 933 125 102 PRO CG C 27.1000 . 1 934 125 102 PRO CD C 50.5000 . 1 935 126 103 LEU H H 6.5200 . 1 936 126 103 LEU HA H 3.8800 . 1 937 126 103 LEU HB3 H 1.9300 . 2 938 126 103 LEU HD1 H 0.7500 . 2 939 126 103 LEU HD2 H 0.6500 . 2 940 126 103 LEU C C 177.9000 . 1 941 126 103 LEU CA C 57.7000 . 1 942 126 103 LEU CB C 41.8000 . 1 943 126 103 LEU CD1 C 26.0000 . 2 944 126 103 LEU CD2 C 22.9000 . 2 945 126 103 LEU N N 116.0200 . 1 946 127 104 GLN H H 8.1600 . 1 947 127 104 GLN HB2 H 2.2300 . 2 948 127 104 GLN HB3 H 2.2900 . 2 949 127 104 GLN C C 180.6000 . 1 950 127 104 GLN CA C 58.3000 . 1 951 127 104 GLN CB C 29.0000 . 1 952 127 104 GLN N N 120.5000 . 1 953 128 105 LYS H H 7.8100 . 1 954 128 105 LYS HA H 4.0500 . 1 955 128 105 LYS HB3 H 1.8900 . 2 956 128 105 LYS C C 177.1000 . 1 957 128 105 LYS CA C 58.5000 . 1 958 128 105 LYS CB C 31.4000 . 1 959 128 105 LYS N N 120.0000 . 1 960 129 106 LEU H H 7.2200 . 1 961 129 106 LEU HA H 3.9700 . 1 962 129 106 LEU HB2 H 1.5500 . 2 963 129 106 LEU HB3 H 1.7000 . 2 964 129 106 LEU HG H 1.7100 . 1 965 129 106 LEU HD1 H 0.4800 . 2 966 129 106 LEU HD2 H 0.6300 . 2 967 129 106 LEU C C 175.2000 . 1 968 129 106 LEU CA C 54.5000 . 1 969 129 106 LEU CB C 42.4000 . 1 970 129 106 LEU CG C 29.4000 . 1 971 129 106 LEU CD1 C 24.8000 . 2 972 129 106 LEU CD2 C 25.6000 . 2 973 129 106 LEU N N 118.5300 . 1 974 130 107 GLY H H 7.5600 . 1 975 130 107 GLY HA2 H 4.3500 . 2 976 130 107 GLY HA3 H 3.6400 . 2 977 130 107 GLY C C 174.8000 . 1 978 130 107 GLY CA C 45.1000 . 1 979 130 107 GLY N N 101.4900 . 1 980 131 108 ILE H H 7.2900 . 1 981 131 108 ILE HA H 4.1500 . 1 982 131 108 ILE HB H 1.6100 . 1 983 131 108 ILE HG12 H 0.9500 . 2 984 131 108 ILE HG13 H 1.4600 . 2 985 131 108 ILE HG2 H 0.8500 . 1 986 131 108 ILE HD1 H 0.7700 . 1 987 131 108 ILE C C 174.3000 . 1 988 131 108 ILE CA C 60.4000 . 1 989 131 108 ILE CB C 35.2000 . 1 990 131 108 ILE CG1 C 27.3000 . 1 991 131 108 ILE CG2 C 18.8000 . 1 992 131 108 ILE CD1 C 13.6000 . 1 993 131 108 ILE N N 121.3400 . 1 994 132 109 GLN H H 8.0800 . 1 995 132 109 GLN HA H 4.0100 . 1 996 132 109 GLN HB2 H 1.9900 . 2 997 132 109 GLN HB3 H 2.0500 . 2 998 132 109 GLN HG2 H 2.4000 . 2 999 132 109 GLN HG3 H 2.4500 . 2 1000 132 109 GLN C C 176.8000 . 1 1001 132 109 GLN CA C 57.6000 . 1 1002 132 109 GLN CB C 29.0000 . 1 1003 132 109 GLN CG C 33.9000 . 1 1004 132 109 GLN N N 125.6500 . 1 1005 133 110 GLU H H 9.2700 . 1 1006 133 110 GLU HA H 4.1500 . 1 1007 133 110 GLU HB2 H 2.0000 . 2 1008 133 110 GLU HB3 H 2.2900 . 2 1009 133 110 GLU HG2 H 2.2200 . 2 1010 133 110 GLU HG3 H 2.1700 . 2 1011 133 110 GLU C C 177.1000 . 1 1012 133 110 GLU CA C 57.1000 . 1 1013 133 110 GLU CB C 27.3000 . 1 1014 133 110 GLU CG C 37.1000 . 1 1015 133 110 GLU N N 114.8900 . 1 1016 134 111 MET H H 7.6200 . 1 1017 134 111 MET HA H 4.3500 . 1 1018 134 111 MET HB2 H 2.8900 . 2 1019 134 111 MET HB3 H 2.2700 . 2 1020 134 111 MET HE H 2.1400 . 1 1021 134 111 MET C C 177.5000 . 1 1022 134 111 MET CA C 57.9000 . 1 1023 134 111 MET CB C 33.3000 . 1 1024 134 111 MET CE C 20.4000 . 1 1025 134 111 MET N N 121.2100 . 1 1026 135 112 THR H H 8.3200 . 1 1027 135 112 THR HA H 3.9200 . 1 1028 135 112 THR HB H 3.8800 . 1 1029 135 112 THR HG2 H 0.9000 . 1 1030 135 112 THR C C 176.4000 . 1 1031 135 112 THR CA C 65.9000 . 1 1032 135 112 THR CB C 68.2000 . 1 1033 135 112 THR CG2 C 23.0000 . 1 1034 135 112 THR N N 113.1700 . 1 1035 136 113 LYS H H 8.0600 . 1 1036 136 113 LYS HA H 3.9300 . 1 1037 136 113 LYS HE3 H 2.8100 . 2 1038 136 113 LYS C C 177.6000 . 1 1039 136 113 LYS CA C 58.3000 . 1 1040 136 113 LYS CB C 32.0000 . 1 1041 136 113 LYS CE C 42.7000 . 1 1042 136 113 LYS N N 123.4400 . 1 1043 137 114 THR H H 7.9500 . 1 1044 137 114 THR HA H 4.0000 . 1 1045 137 114 THR HB H 4.5000 . 1 1046 137 114 THR HG2 H 1.1300 . 1 1047 137 114 THR C C 176.8000 . 1 1048 137 114 THR CA C 67.6000 . 1 1049 137 114 THR CB C 69.2000 . 1 1050 137 114 THR CG2 C 20.7000 . 1 1051 137 114 THR N N 114.5900 . 1 1052 138 115 VAL H H 7.3200 . 1 1053 138 115 VAL HA H 3.8200 . 1 1054 138 115 VAL HB H 2.4700 . 1 1055 138 115 VAL HG1 H 1.1100 . 2 1056 138 115 VAL HG2 H 1.1900 . 2 1057 138 115 VAL C C 176.9000 . 1 1058 138 115 VAL CA C 66.8000 . 1 1059 138 115 VAL CB C 32.5000 . 1 1060 138 115 VAL CG1 C 22.2000 . 2 1061 138 115 VAL CG2 C 22.5000 . 2 1062 138 115 VAL N N 119.0800 . 1 1063 139 116 SER H H 8.9900 . 1 1064 139 116 SER HA H 4.6800 . 1 1065 139 116 SER HB2 H 3.9800 . 2 1066 139 116 SER HB3 H 4.0700 . 2 1067 139 116 SER C C 179.0000 . 1 1068 139 116 SER CA C 61.4000 . 1 1069 139 116 SER CB C 62.8000 . 1 1070 139 116 SER N N 116.6300 . 1 1071 140 117 ASP H H 9.4800 . 1 1072 140 117 ASP HA H 4.3600 . 1 1073 140 117 ASP HB2 H 2.9600 . 2 1074 140 117 ASP HB3 H 2.6000 . 2 1075 140 117 ASP C C 179.9000 . 1 1076 140 117 ASP CA C 57.3000 . 1 1077 140 117 ASP CB C 39.5000 . 1 1078 140 117 ASP N N 124.2200 . 1 1079 141 118 ALA H H 7.3400 . 1 1080 141 118 ALA HA H 4.2800 . 1 1081 141 118 ALA HB H 1.6700 . 1 1082 141 118 ALA C C 179.8000 . 1 1083 141 118 ALA CA C 54.4000 . 1 1084 141 118 ALA CB C 19.0000 . 1 1085 141 118 ALA N N 121.4200 . 1 1086 142 119 ALA H H 7.8900 . 1 1087 142 119 ALA HA H 4.1300 . 1 1088 142 119 ALA HB H 1.1500 . 1 1089 142 119 ALA C C 178.8000 . 1 1090 142 119 ALA CA C 53.2000 . 1 1091 142 119 ALA CB C 18.3000 . 1 1092 142 119 ALA N N 121.6800 . 1 1093 143 120 GLU H H 7.5000 . 1 1094 143 120 GLU HA H 3.9400 . 1 1095 143 120 GLU HB2 H 2.0900 . 2 1096 143 120 GLU HB3 H 2.1400 . 2 1097 143 120 GLU HG2 H 2.2600 . 2 1098 143 120 GLU HG3 H 2.4300 . 2 1099 143 120 GLU C C 178.1000 . 1 1100 143 120 GLU CA C 58.7000 . 1 1101 143 120 GLU CB C 29.5000 . 1 1102 143 120 GLU CG C 36.2000 . 1 1103 143 120 GLU N N 117.6900 . 1 1104 144 121 GLU H H 6.9700 . 1 1105 144 121 GLU HA H 4.1600 . 1 1106 144 121 GLU HB2 H 1.9600 . 2 1107 144 121 GLU HB3 H 2.0300 . 2 1108 144 121 GLU HG2 H 2.1900 . 2 1109 144 121 GLU HG3 H 2.3200 . 2 1110 144 121 GLU C C 176.1000 . 1 1111 144 121 GLU CA C 56.9000 . 1 1112 144 121 GLU CB C 31.1000 . 1 1113 144 121 GLU CG C 36.4000 . 1 1114 144 121 GLU N N 115.6800 . 1 1115 145 122 ASN H H 7.6700 . 1 1116 145 122 ASN HA H 4.9900 . 1 1117 145 122 ASN HB2 H 2.3700 . 2 1118 145 122 ASN HB3 H 2.7700 . 2 1119 145 122 ASN C C 185.3000 . 1 1120 145 122 ASN CA C 50.2000 . 1 1121 145 122 ASN CB C 41.1000 . 1 1122 145 122 ASN N N 117.7500 . 1 1123 146 123 PRO HA H 4.6300 . 1 1124 146 123 PRO HB2 H 2.2700 . 2 1125 146 123 PRO HB3 H 1.7800 . 2 1126 146 123 PRO HG2 H 1.9300 . 2 1127 146 123 PRO HG3 H 2.0600 . 2 1128 146 123 PRO HD2 H 3.3400 . 2 1129 146 123 PRO HD3 H 3.5400 . 2 1130 146 123 PRO CA C 61.0000 . 1 1131 146 123 PRO CB C 31.3000 . 1 1132 146 123 PRO CG C 27.8000 . 1 1133 146 123 PRO CD C 50.5000 . 1 1134 147 124 PRO HA H 4.4400 . 1 1135 147 124 PRO HB2 H 2.5300 . 2 1136 147 124 PRO HG2 H 1.9200 . 2 1137 147 124 PRO HG3 H 2.0600 . 2 1138 147 124 PRO HD2 H 3.5200 . 2 1139 147 124 PRO HD3 H 3.3900 . 2 1140 147 124 PRO CA C 62.9000 . 1 1141 147 124 PRO CB C 28.4000 . 1 1142 147 124 PRO CD C 49.4000 . 1 1143 148 125 THR H H 7.8000 . 1 1144 148 125 THR HA H 4.5300 . 1 1145 148 125 THR HB H 4.5200 . 1 1146 148 125 THR HG2 H 1.0500 . 1 1147 148 125 THR C C 174.3000 . 1 1148 148 125 THR CA C 61.2000 . 1 1149 148 125 THR CB C 68.6000 . 1 1150 148 125 THR CG2 C 22.4000 . 1 1151 148 125 THR N N 106.0900 . 1 1152 149 126 THR H H 7.3500 . 1 1153 149 126 THR HA H 4.1700 . 1 1154 149 126 THR HB H 4.2200 . 1 1155 149 126 THR HG2 H 1.1600 . 1 1156 149 126 THR C C 173.1000 . 1 1157 149 126 THR CA C 58.8000 . 1 1158 149 126 THR CB C 73.1000 . 1 1159 149 126 THR CG2 C 21.4000 . 1 1160 149 126 THR N N 108.6500 . 1 1161 150 127 ALA H H 7.7500 . 1 1162 150 127 ALA HA H 3.0200 . 1 1163 150 127 ALA HB H 1.1100 . 1 1164 150 127 ALA CA C 55.0000 . 1 1165 150 127 ALA CB C 18.7000 . 1 1166 150 127 ALA N N 123.2700 . 1 1167 151 128 GLN H H 8.3000 . 1 1168 151 128 GLN HA H 3.7500 . 1 1169 151 128 GLN HB2 H 1.8800 . 2 1170 151 128 GLN HB3 H 2.0000 . 2 1171 151 128 GLN HG2 H 2.4000 . 2 1172 151 128 GLN HG3 H 2.3400 . 2 1173 151 128 GLN HE22 H 7.0900 . 2 1174 151 128 GLN C C 178.4000 . 1 1175 151 128 GLN CA C 58.8000 . 1 1176 151 128 GLN CB C 27.2000 . 1 1177 151 128 GLN CG C 33.5000 . 1 1178 151 128 GLN N N 114.9200 . 1 1179 152 129 GLY H H 7.9200 . 1 1180 152 129 GLY HA2 H 3.4600 . 2 1181 152 129 GLY HA3 H 3.6900 . 2 1182 152 129 GLY C C 174.9000 . 1 1183 152 129 GLY CA C 47.2000 . 1 1184 152 129 GLY N N 107.2800 . 1 1185 153 130 VAL H H 7.3900 . 1 1186 153 130 VAL HA H 3.4700 . 1 1187 153 130 VAL HB H 2.0000 . 1 1188 153 130 VAL HG1 H 0.9100 . 2 1189 153 130 VAL HG2 H 1.1800 . 2 1190 153 130 VAL C C 177.7000 . 1 1191 153 130 VAL CA C 67.8000 . 1 1192 153 130 VAL CB C 31.7000 . 1 1193 153 130 VAL CG1 C 22.5000 . 2 1194 153 130 VAL CG2 C 25.9000 . 2 1195 153 130 VAL N N 119.4400 . 1 1196 154 131 LEU H H 8.6400 . 1 1197 154 131 LEU HA H 3.9100 . 1 1198 154 131 LEU HB3 H 1.9100 . 2 1199 154 131 LEU HG H 1.6400 . 1 1200 154 131 LEU HD1 H 0.9500 . 2 1201 154 131 LEU HD2 H 0.7000 . 2 1202 154 131 LEU C C 180.4000 . 1 1203 154 131 LEU CA C 58.3000 . 1 1204 154 131 LEU CB C 41.0000 . 1 1205 154 131 LEU CG C 27.3000 . 1 1206 154 131 LEU CD1 C 24.1000 . 2 1207 154 131 LEU CD2 C 24.9000 . 2 1208 154 131 LEU N N 118.9900 . 1 1209 155 132 GLU H H 8.0000 . 1 1210 155 132 GLU HA H 4.1200 . 1 1211 155 132 GLU HB3 H 1.9800 . 2 1212 155 132 GLU HG2 H 2.2000 . 2 1213 155 132 GLU HG3 H 2.5000 . 2 1214 155 132 GLU C C 179.4000 . 1 1215 155 132 GLU CA C 58.9000 . 1 1216 155 132 GLU CB C 29.2000 . 1 1217 155 132 GLU CG C 35.6000 . 1 1218 155 132 GLU N N 120.9800 . 1 1219 156 133 ILE H H 8.0400 . 1 1220 156 133 ILE HA H 3.5800 . 1 1221 156 133 ILE HB H 1.9000 . 1 1222 156 133 ILE HG2 H 1.2800 . 1 1223 156 133 ILE HD1 H 0.9600 . 1 1224 156 133 ILE C C 178.0000 . 1 1225 156 133 ILE CA C 65.5000 . 1 1226 156 133 ILE CB C 39.6000 . 1 1227 156 133 ILE CG2 C 18.0000 . 1 1228 156 133 ILE CD1 C 16.0000 . 1 1229 156 133 ILE N N 121.8300 . 1 1230 157 134 ALA H H 8.9500 . 1 1231 157 134 ALA HA H 3.9000 . 1 1232 157 134 ALA HB H 1.4000 . 1 1233 157 134 ALA C C 178.8000 . 1 1234 157 134 ALA CA C 55.3000 . 1 1235 157 134 ALA CB C 18.1000 . 1 1236 157 134 ALA N N 121.4700 . 1 1237 158 135 LYS H H 8.0000 . 1 1238 158 135 LYS HA H 3.9100 . 1 1239 158 135 LYS C C 179.3000 . 1 1240 158 135 LYS CA C 59.5000 . 1 1241 158 135 LYS CB C 31.4000 . 1 1242 158 135 LYS N N 118.4700 . 1 1243 159 136 LYS H H 7.5300 . 1 1244 159 136 LYS HA H 4.0500 . 1 1245 159 136 LYS C C 180.2000 . 1 1246 159 136 LYS CA C 59.5000 . 1 1247 159 136 LYS CB C 30.9000 . 1 1248 159 136 LYS N N 118.0000 . 1 1249 160 137 MET H H 8.6600 . 1 1250 160 137 MET HA H 3.8000 . 1 1251 160 137 MET HB3 H 1.8200 . 2 1252 160 137 MET HE H 2.1800 . 1 1253 160 137 MET C C 177.4000 . 1 1254 160 137 MET CA C 60.6000 . 1 1255 160 137 MET CB C 31.8000 . 1 1256 160 137 MET CE C 18.4000 . 1 1257 160 137 MET N N 120.9900 . 1 1258 161 138 ARG H H 9.2800 . 1 1259 161 138 ARG HA H 3.8000 . 1 1260 161 138 ARG HB2 H 1.8900 . 2 1261 161 138 ARG HB3 H 2.0700 . 2 1262 161 138 ARG HG3 H 1.6400 . 2 1263 161 138 ARG HD3 H 3.1200 . 2 1264 161 138 ARG C C 177.9000 . 1 1265 161 138 ARG CA C 60.6000 . 1 1266 161 138 ARG CB C 29.8000 . 1 1267 161 138 ARG CG C 27.6000 . 1 1268 161 138 ARG CD C 43.4000 . 1 1269 161 138 ARG N N 119.4800 . 1 1270 162 139 GLU H H 8.4300 . 1 1271 162 139 GLU HA H 4.0000 . 1 1272 162 139 GLU HB2 H 2.0300 . 2 1273 162 139 GLU HB3 H 2.1200 . 2 1274 162 139 GLU C C 179.1000 . 1 1275 162 139 GLU CA C 59.8000 . 1 1276 162 139 GLU CB C 29.5000 . 1 1277 162 139 GLU CG C 34.5000 . 1 1278 162 139 GLU N N 118.7000 . 1 1279 163 140 LYS H H 7.4400 . 1 1280 163 140 LYS HA H 4.2100 . 1 1281 163 140 LYS HB3 H 2.0400 . 2 1282 163 140 LYS HG2 H 1.3000 . 2 1283 163 140 LYS HG3 H 1.5200 . 2 1284 163 140 LYS HD2 H 1.7100 . 2 1285 163 140 LYS HD3 H 1.8600 . 2 1286 163 140 LYS HE3 H 2.8300 . 2 1287 163 140 LYS C C 177.9000 . 1 1288 163 140 LYS CA C 58.9000 . 1 1289 163 140 LYS CB C 31.1000 . 1 1290 163 140 LYS CG C 25.6000 . 1 1291 163 140 LYS CD C 28.8000 . 1 1292 163 140 LYS N N 119.3100 . 1 1293 164 141 LEU H H 8.1800 . 1 1294 164 141 LEU HA H 3.8900 . 1 1295 164 141 LEU HD1 H 0.6500 . 2 1296 164 141 LEU HD2 H 0.8200 . 2 1297 164 141 LEU C C 178.7000 . 1 1298 164 141 LEU CA C 58.0000 . 1 1299 164 141 LEU CB C 41.5000 . 1 1300 164 141 LEU CD1 C 22.9000 . 2 1301 164 141 LEU CD2 C 27.1000 . 2 1302 164 141 LEU N N 117.6300 . 1 1303 165 142 GLN H H 8.7300 . 1 1304 165 142 GLN HA H 4.3100 . 1 1305 165 142 GLN C C 179.2000 . 1 1306 165 142 GLN CA C 58.5000 . 1 1307 165 142 GLN CB C 27.5000 . 1 1308 165 142 GLN N N 117.7100 . 1 1309 166 143 ARG H H 8.0500 . 1 1310 166 143 ARG HA H 4.1900 . 1 1311 166 143 ARG HB2 H 1.9900 . 2 1312 166 143 ARG HB3 H 2.1200 . 2 1313 166 143 ARG HG2 H 1.9300 . 2 1314 166 143 ARG HG3 H 1.7400 . 2 1315 166 143 ARG HD2 H 3.2300 . 2 1316 166 143 ARG HD3 H 3.2900 . 2 1317 166 143 ARG C C 179.7000 . 1 1318 166 143 ARG CA C 59.8000 . 1 1319 166 143 ARG CB C 30.2000 . 1 1320 166 143 ARG CG C 27.8000 . 1 1321 166 143 ARG CD C 43.6000 . 1 1322 166 143 ARG N N 121.4100 . 1 1323 167 144 VAL H H 8.1900 . 1 1324 167 144 VAL HA H 3.7600 . 1 1325 167 144 VAL HB H 2.2700 . 1 1326 167 144 VAL HG1 H 1.1900 . 2 1327 167 144 VAL HG2 H 0.9700 . 2 1328 167 144 VAL C C 179.2000 . 1 1329 167 144 VAL CA C 66.4000 . 1 1330 167 144 VAL CB C 32.1000 . 1 1331 167 144 VAL CG1 C 22.7000 . 2 1332 167 144 VAL CG2 C 22.1000 . 2 1333 167 144 VAL N N 120.9500 . 1 1334 168 145 HIS H H 9.2400 . 1 1335 168 145 HIS HA H 3.9000 . 1 1336 168 145 HIS HB2 H 3.5400 . 2 1337 168 145 HIS HB3 H 3.3600 . 2 1338 168 145 HIS HD2 H 6.9900 . 1 1339 168 145 HIS HE1 H 7.6200 . 1 1340 168 145 HIS C C 177.1000 . 1 1341 168 145 HIS CA C 61.3000 . 1 1342 168 145 HIS CB C 29.9000 . 1 1343 168 145 HIS CD2 C 120.7000 . 1 1344 168 145 HIS CE1 C 137.9000 . 1 1345 168 145 HIS N N 123.5200 . 1 1346 169 146 THR H H 8.7500 . 1 1347 169 146 THR HA H 3.8600 . 1 1348 169 146 THR HB H 4.3000 . 1 1349 169 146 THR HG2 H 1.3400 . 1 1350 169 146 THR C C 175.7000 . 1 1351 169 146 THR CA C 67.2000 . 1 1352 169 146 THR CB C 69.3000 . 1 1353 169 146 THR CG2 C 22.8000 . 1 1354 169 146 THR N N 115.0200 . 1 1355 170 147 LYS H H 8.0200 . 1 1356 170 147 LYS HA H 4.0000 . 1 1357 170 147 LYS HE3 H 2.9400 . 2 1358 170 147 LYS C C 179.3000 . 1 1359 170 147 LYS CA C 59.1000 . 1 1360 170 147 LYS CB C 31.8000 . 1 1361 170 147 LYS N N 120.3000 . 1 1362 171 148 ASN H H 7.8100 . 1 1363 171 148 ASN HA H 4.3200 . 1 1364 171 148 ASN C C 175.4000 . 1 1365 171 148 ASN CA C 57.7000 . 1 1366 171 148 ASN CB C 39.7000 . 1 1367 171 148 ASN N N 117.6000 . 1 1368 172 149 TYR H H 9.0200 . 1 1369 172 149 TYR HA H 3.8900 . 1 1370 172 149 TYR HB2 H 2.6800 . 2 1371 172 149 TYR HB3 H 3.0300 . 2 1372 172 149 TYR HD1 H 7.0500 . 3 1373 172 149 TYR HE1 H 6.8500 . 3 1374 172 149 TYR C C 176.9000 . 1 1375 172 149 TYR CA C 61.5000 . 1 1376 172 149 TYR CB C 38.9200 . 1 1377 172 149 TYR CD1 C 133.4000 . 3 1378 172 149 TYR CE1 C 118.6000 . 3 1379 172 149 TYR N N 121.5600 . 1 1380 173 150 CYS H H 8.8100 . 1 1381 173 150 CYS C C 177.1000 . 1 1382 173 150 CYS CA C 58.4000 . 1 1383 173 150 CYS CB C 38.6000 . 1 1384 173 150 CYS N N 116.0500 . 1 1385 174 151 THR H H 7.7200 . 1 1386 174 151 THR HA H 3.8800 . 1 1387 174 151 THR HB H 4.1800 . 1 1388 174 151 THR HG2 H 1.2000 . 1 1389 174 151 THR C C 176.0000 . 1 1390 174 151 THR CA C 66.9000 . 1 1391 174 151 THR CB C 68.5000 . 1 1392 174 151 THR N N 117.1900 . 1 1393 175 152 LEU H H 7.8700 . 1 1394 175 152 LEU HA H 3.8100 . 1 1395 175 152 LEU HB3 H 1.6900 . 2 1396 175 152 LEU HG H 1.4900 . 1 1397 175 152 LEU HD1 H 0.8100 . 2 1398 175 152 LEU HD2 H 0.8300 . 2 1399 175 152 LEU CA C 58.0000 . 1 1400 175 152 LEU CB C 41.5000 . 1 1401 175 152 LEU CG C 26.9000 . 1 1402 175 152 LEU CD1 C 25.0000 . 2 1403 175 152 LEU CD2 C 24.2000 . 2 1404 175 152 LEU N N 123.1100 . 1 1405 176 153 LYS H H 7.9000 . 1 1406 176 153 LYS HA H 3.7000 . 1 1407 176 153 LYS HB3 H 1.9800 . 2 1408 176 153 LYS HG2 H 1.1600 . 2 1409 176 153 LYS HG3 H 1.2400 . 2 1410 176 153 LYS HE2 H 2.7000 . 2 1411 176 153 LYS HE3 H 2.5200 . 2 1412 176 153 LYS C C 179.1000 . 1 1413 176 153 LYS CA C 56.7000 . 1 1414 176 153 LYS CB C 29.9000 . 1 1415 176 153 LYS CG C 26.9000 . 1 1416 176 153 LYS CE C 42.0000 . 1 1417 176 153 LYS N N 117.2700 . 1 1418 177 154 LYS H H 7.5400 . 1 1419 177 154 LYS HA H 4.2600 . 1 1420 177 154 LYS HB3 H 1.8800 . 2 1421 177 154 LYS HG2 H 1.5900 . 2 1422 177 154 LYS HG3 H 1.5400 . 2 1423 177 154 LYS HE3 H 3.0100 . 2 1424 177 154 LYS C C 178.1000 . 1 1425 177 154 LYS CA C 57.8000 . 1 1426 177 154 LYS CB C 31.8000 . 1 1427 177 154 LYS CG C 25.7000 . 1 1428 177 154 LYS CE C 42.3000 . 1 1429 177 154 LYS N N 119.2900 . 1 1430 178 155 LYS H H 7.6300 . 1 1431 178 155 LYS HA H 4.0500 . 1 1432 178 155 LYS HB3 H 1.8900 . 2 1433 178 155 LYS HG2 H 1.4500 . 2 1434 178 155 LYS HG3 H 1.5500 . 2 1435 178 155 LYS HE3 H 2.9300 . 2 1436 178 155 LYS C C 178.1000 . 1 1437 178 155 LYS CA C 58.0000 . 1 1438 178 155 LYS CB C 32.2000 . 1 1439 178 155 LYS CG C 25.1000 . 1 1440 178 155 LYS N N 118.9100 . 1 1441 179 156 GLU H H 7.5600 . 1 1442 179 156 GLU HA H 4.1100 . 1 1443 179 156 GLU HB3 H 2.0200 . 2 1444 179 156 GLU HG2 H 2.3200 . 2 1445 179 156 GLU HG3 H 2.1500 . 2 1446 179 156 GLU C C 176.7000 . 1 1447 179 156 GLU CA C 57.5000 . 1 1448 179 156 GLU CB C 29.6000 . 1 1449 179 156 GLU CG C 36.3000 . 1 1450 179 156 GLU N N 117.9500 . 1 1451 180 157 ASN H H 7.8200 . 1 1452 180 157 ASN HA H 4.7200 . 1 1453 180 157 ASN HB2 H 2.6900 . 2 1454 180 157 ASN HB3 H 2.8600 . 2 1455 180 157 ASN C C 175.0000 . 1 1456 180 157 ASN CA C 52.7000 . 1 1457 180 157 ASN CB C 38.8000 . 1 1458 180 157 ASN N N 116.5900 . 1 1459 181 158 SER H H 8.0300 . 1 1460 181 158 SER HA H 4.4500 . 1 1461 181 158 SER HB2 H 3.9500 . 2 1462 181 158 SER HB3 H 4.0000 . 2 1463 181 158 SER CA C 60.4000 . 1 1464 181 158 SER CB C 63.5000 . 1 1465 182 159 THR H H 8.0700 . 1 1466 182 159 THR HA H 4.3800 . 1 1467 182 159 THR HB H 4.3800 . 1 1468 182 159 THR HG2 H 1.1600 . 1 1469 182 159 THR C C 174.3000 . 1 1470 182 159 THR CA C 61.8000 . 1 1471 182 159 THR CB C 69.1000 . 1 1472 182 159 THR CG2 C 21.9000 . 1 1473 182 159 THR N N 112.8000 . 1 1474 183 160 PHE H H 7.9000 . 1 1475 183 160 PHE HA H 4.4400 . 1 1476 183 160 PHE HB2 H 2.9000 . 2 1477 183 160 PHE HB3 H 3.1300 . 2 1478 183 160 PHE HD2 H 7.1100 . 3 1479 183 160 PHE HE2 H 7.3300 . 3 1480 183 160 PHE C C 175.1000 . 1 1481 183 160 PHE CA C 58.9000 . 1 1482 183 160 PHE CB C 40.0000 . 1 1483 183 160 PHE CD2 C 131.8000 . 3 1484 183 160 PHE N N 123.1200 . 1 1485 184 161 THR H H 7.8100 . 1 1486 184 161 THR HA H 4.1900 . 1 1487 184 161 THR HB H 3.9500 . 1 1488 184 161 THR HG2 H 1.0700 . 1 1489 184 161 THR CA C 60.7000 . 1 1490 184 161 THR CB C 70.7000 . 1 1491 184 161 THR CG2 C 21.0000 . 1 1492 184 161 THR N N 119.3300 . 1 1493 185 162 ASP H H 8.0000 . 1 1494 185 162 ASP HA H 4.4100 . 1 1495 185 162 ASP HB2 H 2.5700 . 2 1496 185 162 ASP HB3 H 2.6600 . 2 1497 185 162 ASP C C 176.9000 . 1 1498 185 162 ASP CA C 53.9000 . 1 1499 185 162 ASP CB C 44.0000 . 1 1500 185 162 ASP N N 123.1900 . 1 1501 186 163 GLU HA H 4.4800 . 1 1502 186 163 GLU HB2 H 2.0500 . 2 1503 186 163 GLU HB3 H 2.2400 . 2 1504 186 163 GLU HG2 H 2.4000 . 2 1505 186 163 GLU HG3 H 2.5700 . 2 1506 186 163 GLU CA C 58.8000 . 1 1507 186 163 GLU CB C 28.1000 . 1 1508 186 163 GLU CG C 34.6000 . 1 1509 189 166 LYS H H 8.8900 . 1 1510 189 166 LYS HA H 4.2200 . 1 1511 189 166 LYS HB2 H 1.8500 . 2 1512 189 166 LYS HB3 H 1.8900 . 2 1513 189 166 LYS HG3 H 1.4600 . 2 1514 189 166 LYS HE3 H 3.0100 . 2 1515 189 166 LYS C C 177.5000 . 1 1516 189 166 LYS CA C 58.0000 . 1 1517 189 166 LYS CB C 32.6000 . 1 1518 189 166 LYS CG C 25.1000 . 1 1519 189 166 LYS CE C 42.3000 . 1 1520 189 166 LYS N N 118.1500 . 1 1521 190 167 ASN H H 8.0300 . 1 1522 190 167 ASN HA H 4.9600 . 1 1523 190 167 ASN HB2 H 3.4100 . 2 1524 190 167 ASN HB3 H 2.8300 . 2 1525 190 167 ASN C C 174.9000 . 1 1526 190 167 ASN CA C 52.9000 . 1 1527 190 167 ASN CB C 38.4000 . 1 1528 190 167 ASN N N 116.2100 . 1 1529 191 168 ASN H H 7.7900 . 1 1530 191 168 ASN HA H 4.2500 . 1 1531 191 168 ASN HB3 H 3.0000 . 2 1532 191 168 ASN C C 176.3000 . 1 1533 191 168 ASN CA C 57.1000 . 1 1534 191 168 ASN CB C 32.3000 . 1 1535 191 168 ASN N N 122.1400 . 1 stop_ save_ save_RDC_list_1 _Saveframe_category residual_dipolar_couplings loop_ _Sample_label $gel_sample stop_ loop_ _Residual_dipolar_coupling_ID _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Residual_dipolar_coupling_value _Atom_one_mol_system_component_name _Atom_two_mol_system_component_name _Residual_dipolar_coupling_min_value _Residual_dipolar_coupling_max_value _Residual_dipolar_coupling_value_error DNH 3 GLY N 3 GLY H 0.4 ? ? . . 0.36 DNH 4 LEU N 4 LEU H -8.094 ? ? . . 0.122 DNH 5 THR N 5 THR H 5.34 ? ? . . 0.4 DNH 6 GLY N 6 GLY H 0.92 ? ? . . 0.44 DNH 8 THR N 8 THR H -20.18 ? ? . . 0.3 DNH 9 LYS N 9 LYS H -18.62 ? ? . . 0.32 DNH 10 ILE N 10 ILE H -16.76 ? ? . . 0.4 DNH 11 ARG N 11 ARG H -18.278 ? ? . . 0.382 DNH 12 LEU N 12 LEU H -19.96 ? ? . . 0.26 DNH 13 GLU N 13 GLU H -17.08 ? ? . . 0.3 DNH 16 ALA N 16 ALA H -18.4 ? ? . . 0.58 DNH 17 LYS N 17 LYS H -14.692 ? ? . . 0.25 DNH 18 ASP N 18 ASP H -14.024 ? ? . . 0.394 DNH 19 ILE N 19 ILE H -18.94 ? ? . . 0.26 DNH 22 GLU N 22 GLU H -13.46 ? ? . . 0.44 DNH 23 ILE N 23 ILE H -18.2 ? ? . . 0.44 DNH 24 ASP N 24 ASP H -17.38 ? ? . . 0.74 DNH 25 ALA N 25 ALA H -11.36 ? ? . . 0.68 DNH 27 LYS N 27 LYS H -19.652 ? ? . . 0.372 DNH 28 LYS N 28 LYS H -14.08 ? ? . . 0.42 DNH 29 ASP N 29 ASP H -13.16 ? ? . . 0.76 DNH 30 ALA N 30 ALA H -18.3 ? ? . . 0.4 DNH 31 ALA N 31 ALA H -18.46 ? ? . . 0.52 DNH 32 LEU N 32 LEU H -9.84 ? ? . . 0.772 DNH 33 LYS N 33 LYS H -15.08 ? ? . . 0.66 DNH 34 GLY N 34 GLY H -11.05 ? ? . . 0.624 DNH 38 ASP N 38 ASP H 0.428 ? ? . . 0.202 DNH 39 ALA N 39 ALA H 7.66 ? ? . . 0.46 DNH 40 PHE N 40 PHE H 1.36 ? ? . . 0.38 DNH 42 ASP N 42 ASP H 0.042 ? ? . . 0.248 DNH 45 THR N 45 THR H 0.88 ? ? . . 1.26 DNH 49 VAL N 49 VAL H -0.28 ? ? . . 0.26 DNH 51 GLU N 51 GLU H 1.02 ? ? . . 0.82 DNH 52 ASN N 52 ASN H 3.88 ? ? . . 0.46 DNH 54 PHE N 54 PHE H -9.66 ? ? . . 0.34 DNH 56 LEU N 56 LEU H -18.776 ? ? . . 0.452 DNH 57 GLU N 57 GLU H -17.128 ? ? . . 0.286 DNH 58 ALA N 58 ALA H -9 ? ? . . 0.44 DNH 59 LYS N 59 LYS H -18.36 ? ? . . 0.76 DNH 60 VAL N 60 VAL H -17.674 ? ? . . 0.314 DNH 62 ALA N 62 ALA H -16.02 ? ? . . 0.64 DNH 63 THR N 63 THR H -20.82 ? ? . . 0.56 DNH 66 ALA N 66 ALA H -19.08 ? ? . . 0.52 DNH 67 GLU N 67 GLU H -19.04 ? ? . . 0.44 DNH 68 LYS N 68 LYS H -14.9 ? ? . . 1.28 DNH 69 PHE N 69 PHE H -16.9 ? ? . . 0.58 DNH 71 ILE N 71 ILE H -17.58 ? ? . . 0.4 DNH 72 ALA N 72 ALA H -15.02 ? ? . . 0.58 DNH 74 GLU N 74 GLU H -19.74 ? ? . . 0.36 DNH 75 GLU N 75 GLU H -16.34 ? ? . . 0.58 DNH 76 GLU N 76 GLU H -16.176 ? ? . . 0.256 DNH 80 LEU N 80 LEU H -18.474 ? ? . . 0.472 DNH 81 LYS N 81 LYS H -2.08 ? ? . . 0.38 DNH 82 GLU N 82 GLU H 9.54 ? ? . . 0.52 DNH 83 THR N 83 THR H -7.546 ? ? . . 0.264 DNH 84 GLY N 84 GLY H -0.94 ? ? . . 0.52 DNH 85 SER N 85 SER H 3.02 ? ? . . 0.3 DNH 92 MET N 92 MET H -11.76 ? ? . . 1.66 DNH 93 TYR N 93 TYR H -17.088 ? ? . . 0.252 DNH 94 ASP N 94 ASP H -20.14 ? ? . . 0.62 DNH 95 LEU N 95 LEU H -14.56 ? ? . . 0.44 DNH 96 MET N 96 MET H -17.826 ? ? . . 0.236 DNH 97 PHE N 97 PHE H -20.096 ? ? . . 0.398 DNH 98 GLU N 98 GLU H -17.328 ? ? . . 0.344 DNH 100 SER N 100 SER H -18.24 ? ? . . 0.56 DNH 101 LYS N 101 LYS H -17.32 ? ? . . 0.36 DNH 103 LEU N 103 LEU H -20 ? ? . . 0.48 DNH 104 GLN N 104 GLN H -17.4 ? ? . . 0.48 DNH 105 LYS N 105 LYS H -17.47 ? ? . . 0.434 DNH 106 LEU N 106 LEU H -16.7 ? ? . . 0.42 DNH 108 ILE N 108 ILE H -1.7 ? ? . . 0.48 DNH 109 GLN N 109 GLN H -9.58 ? ? . . 0.46 DNH 110 GLU N 110 GLU H 4.36 ? ? . . 0.34 DNH 111 MET N 111 MET H -10.78 ? ? . . 0.34 DNH 112 THR N 112 THR H -12.54 ? ? . . 0.3 DNH 113 LYS N 113 LYS H -10.68 ? ? . . 0.44 DNH 114 THR N 114 THR H -11.18 ? ? . . 0.22 DNH 115 VAL N 115 VAL H -8.52 ? ? . . 0.52 DNH 116 SER N 116 SER H -17.32 ? ? . . 0.48 DNH 118 ALA N 118 ALA H -2.38 ? ? . . 0.58 DNH 119 ALA N 119 ALA H -8.28 ? ? . . 0.3 DNH 120 GLU N 120 GLU H -19.92 ? ? . . 0.32 DNH 121 GLU N 121 GLU H -9.546 ? ? . . 0.626 DNH 122 ASN N 122 ASN H -7.598 ? ? . . 0.4 DNH 125 THR N 125 THR H 7.06 ? ? . . 0.52 DNH 126 THR N 126 THR H -19.76 ? ? . . 0.66 DNH 127 ALA N 127 ALA H -19.78 ? ? . . 0.4 DNH 128 GLN N 128 GLN H -17.88 ? ? . . 0.5 DNH 129 GLY N 129 GLY H -18.39 ? ? . . 0.22 DNH 133 ILE N 133 ILE H -17.46 ? ? . . 0.28 DNH 134 ALA N 134 ALA H -20.4 ? ? . . 0.68 DNH 135 LYS N 135 LYS H -16.74 ? ? . . 0.4 DNH 136 LYS N 136 LYS H -16.8 ? ? . . 0.28 DNH 137 MET N 137 MET H -19.52 ? ? . . 0.62 DNH 138 ARG N 138 ARG H -19.842 ? ? . . 0.384 DNH 139 GLU N 139 GLU H -14.606 ? ? . . 0.214 DNH 140 LYS N 140 LYS H -17.156 ? ? . . 0.368 DNH 141 LEU N 141 LEU H -19.98 ? ? . . 0.86 DNH 142 GLN N 142 GLN H -13.966 ? ? . . 0.26 DNH 143 ARG N 143 ARG H -10.98 ? ? . . 0.36 DNH 144 VAL N 144 VAL H -23.34 ? ? . . 0.66 DNH 146 THR N 146 THR H -6.32 ? ? . . 1.18 DNH 147 LYS N 147 LYS H -9.62 ? ? . . 0.36 DNH 148 ASN N 148 ASN H -18.84 ? ? . . 0.86 DNH 149 TYR N 149 TYR H -14.7 ? ? . . 0.5 DNH 153 LYS N 153 LYS H -12.08 ? ? . . 0.66 DNH 155 LYS N 155 LYS H -13.16 ? ? . . 0.38 DNH 157 ASN N 157 ASN H -1.08 ? ? . . 1.7 DNH 160 PHE N 160 PHE H -2.3 ? ? . . 0.76 DNH 162 ASP N 162 ASP H 7.76 ? ? . . 0.6 DNH 166 LYS N 166 LYS H 7.38 ? ? . . 0.42 DNH 167 ASN N 167 ASN H 9.06 ? ? . . 0.48 DNH 168 ASN N 168 ASN H -0.36 ? ? . . 0.42 stop_ _Details . _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 800 _Text_data_format . _Text_data . save_ save_NCO_RDC _Saveframe_category residual_dipolar_couplings loop_ _Sample_label $gel_sample stop_ loop_ _Residual_dipolar_coupling_ID _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Residual_dipolar_coupling_value _Atom_one_mol_system_component_name _Atom_two_mol_system_component_name _Residual_dipolar_coupling_min_value _Residual_dipolar_coupling_max_value _Residual_dipolar_coupling_value_error DNC 3 GLY N 2 ALA C 0.203787 ? ? . . 0.0385305 DNC 4 LEU N 3 GLY C -1.17829 ? ? . . 0.0136674 DNC 5 THR N 4 LEU C 0.859979 ? ? . . 0.0358193 DNC 6 GLY N 5 THR C 0.947649 ? ? . . 0.059066 DNC 8 THR N 7 ALA C 0.687712 ? ? . . 0.032589 DNC 9 LYS N 8 THR C 0.0551074 ? ? . . 0.030521 DNC 10 ILE N 9 LYS C 1.47774 ? ? . . 0.0226577 DNC 11 ARG N 10 ILE C 0.566824 ? ? . . 0.0271282 DNC 12 LEU N 11 ARG C 0.975992 ? ? . . 0.0332807 DNC 13 GLU N 12 LEU C -0.00398949 ? ? . . 0.0163571 DNC 16 ALA N 15 SER C 0.549888 ? ? . . 0.0322398 DNC 17 LYS N 16 ALA C 0.66066 ? ? . . 0.0315596 DNC 18 ASP N 17 LYS C 1.04478 ? ? . . 0.0179673 DNC 19 ILE N 18 ASP C 1.28132 ? ? . . 0.0292668 DNC 20 THR N 19 ILE C -0.165494 ? ? . . 0.0137799 DNC 21 ASP N 20 THR C 1.28518 ? ? . . 0.0508445 DNC 23 ILE N 22 GLU C 1.07243 ? ? . . 0.0536103 DNC 24 ASP N 23 ILE C -0.394413 ? ? . . 0.0233324 DNC 25 ALA N 24 ASP C 1.38283 ? ? . . 0.0377059 DNC 27 LYS N 26 ILE C 0.0486371 ? ? . . 0.0383873 DNC 28 LYS N 27 LYS C 0.844932 ? ? . . 0.0336926 DNC 29 ASP N 28 LYS C 0.850535 ? ? . . 0.0401382 DNC 30 ALA N 29 ASP C 1.12451 ? ? . . 0.0576243 DNC 31 ALA N 30 ALA C 0.322982 ? ? . . 0.0626324 DNC 33 LYS N 32 LEU C 0.755898 ? ? . . 0.0228146 DNC 34 GLY N 33 LYS C 0.77881 ? ? . . 0.036721 DNC 36 ASN N 35 VAL C 1.22222 ? ? . . 0.0683309 DNC 37 PHE N 36 ASN C -1.36836 ? ? . . 0.0619729 DNC 38 ASP N 37 PHE C 0.433095 ? ? . . 0.0301799 DNC 39 ALA N 38 ASP C -0.373819 ? ? . . 0.0156953 DNC 42 ASP N 41 LYS C -0.0170128 ? ? . . 0.0866303 DNC 44 LYS N 43 LYS C 0.0374311 ? ? . . 0.101571 DNC 49 VAL N 48 GLY C -0.394768 ? ? . . 0.0141448 DNC 51 GLU N 50 SER C -0.842598 ? ? . . 0.051987 DNC 52 ASN N 51 GLU C -0.133584 ? ? . . 0.0845949 DNC 54 PHE N 53 PRO C 0.602421 ? ? . . 0.0595774 DNC 56 LEU N 55 ILE C -0.284893 ? ? . . 0.0540099 DNC 57 GLU N 56 LEU C 0.653353 ? ? . . 0.0385609 DNC 58 ALA N 57 GLU C 0.937612 ? ? . . 0.0428115 DNC 60 VAL N 59 LYS C 0.314928 ? ? . . 0.0482967 DNC 62 ALA N 61 ARG C 1.69638 ? ? . . 0.0457887 DNC 63 THR N 62 ALA C 0.0419067 ? ? . . 0.0622341 DNC 67 GLU N 66 ALA C 0.147964 ? ? . . 0.0300283 DNC 68 LYS N 67 GLU C 0.611872 ? ? . . 0.0935716 DNC 69 PHE N 68 LYS C 1.43554 ? ? . . 0.0576986 DNC 72 ALA N 71 ILE C 0.634299 ? ? . . 0.0422478 DNC 74 GLU N 73 ILE C -0.339809 ? ? . . 0.0389612 DNC 75 GLU N 74 GLU C 1.39 ? ? . . 0.0644649 DNC 76 GLU N 75 GLU C 1.04533 ? ? . . 0.0341728 DNC 77 ALA N 76 GLU C 0.570496 ? ? . . 0.0604585 DNC 78 THR N 77 ALA C 0.634445 ? ? . . 0.0393835 DNC 81 LYS N 80 LEU C 0.485407 ? ? . . 0.027728 DNC 82 GLU N 81 LYS C -0.151692 ? ? . . 0.0393666 DNC 83 THR N 82 GLU C 0.248248 ? ? . . 0.0618709 DNC 84 GLY N 83 THR C -2.16753 ? ? . . 0.0921575 DNC 85 SER N 84 GLY C 0.751491 ? ? . . 0.0367227 DNC 94 ASP N 93 TYR C -0.361972 ? ? . . 0.0444275 DNC 95 LEU N 94 ASP C 1.51669 ? ? . . 0.0544415 DNC 96 MET N 95 LEU C 0.786554 ? ? . . 0.0539679 DNC 98 GLU N 97 PHE C 0.232127 ? ? . . 0.0925414 DNC 100 SER N 99 VAL C 1.128 ? ? . . 0.0840968 DNC 103 LEU N 102 PRO C -0.0908655 ? ? . . 0.0297324 DNC 104 GLN N 103 LEU C 0.858269 ? ? . . 0.0253854 DNC 105 LYS N 104 GLN C 0.676325 ? ? . . 0.0426469 DNC 107 GLY N 106 LEU C 1.24125 ? ? . . 0.0457782 DNC 108 ILE N 107 GLY C -2.00972 ? ? . . 0.0362437 DNC 109 GLN N 108 ILE C 0.223162 ? ? . . 0.028754 DNC 110 GLU N 109 GLN C 0.429436 ? ? . . 0.0306226 DNC 111 MET N 110 GLU C 1.28514 ? ? . . 0.0311182 DNC 112 THR N 111 MET C 1.13824 ? ? . . 0.0431577 DNC 113 LYS N 112 THR C 0.230102 ? ? . . 0.077473 DNC 114 THR N 113 LYS C 0.88314 ? ? . . 0.0336207 DNC 115 VAL N 114 THR C 0.49624 ? ? . . 0.0449065 DNC 116 SER N 115 VAL C 1.09367 ? ? . . 0.0496562 DNC 117 ASP N 116 SER C -1.21812 ? ? . . 0.046106 DNC 118 ALA N 117 ASP C 1.52255 ? ? . . 0.0600344 DNC 119 ALA N 118 ALA C 0.644506 ? ? . . 0.0258133 DNC 120 GLU N 119 ALA C 0.0412841 ? ? . . 0.0273399 DNC 121 GLU N 120 GLU C 0.493223 ? ? . . 0.0427779 DNC 122 ASN N 121 GLU C 1.24411 ? ? . . 0.0380176 DNC 125 THR N 124 PRO C -1.08502 ? ? . . 0.0523805 DNC 126 THR N 125 THR C 0.0315974 ? ? . . 0.0558445 DNC 128 GLN N 127 ALA C 0.475374 ? ? . . 0.0216917 DNC 129 GLY N 128 GLN C 0.987954 ? ? . . 0.0657987 DNC 133 ILE N 132 GLU C 0.631229 ? ? . . 0.0464463 DNC 134 ALA N 133 ILE C 0.883263 ? ? . . 0.0336989 DNC 135 LYS N 134 ALA C 0.383567 ? ? . . 0.0229454 DNC 137 MET N 136 LYS C 0.0667499 ? ? . . 0.060859 DNC 138 ARG N 137 MET C 0.48918 ? ? . . 0.060934 DNC 139 GLU N 138 ARG C 0.986072 ? ? . . 0.040754 DNC 140 LYS N 139 GLU C 1.1086 ? ? . . 0.0368916 DNC 141 LEU N 140 LYS C 0.0428809 ? ? . . 0.0496642 DNC 142 GLN N 141 LEU C 0.0679817 ? ? . . 0.0532241 DNC 146 THR N 145 HIS C 0.333995 ? ? . . 0.0356481 DNC 148 ASN N 147 LYS C 0.0449345 ? ? . . 0.0503374 DNC 149 TYR N 148 ASN C -0.417218 ? ? . . 0.0940526 DNC 153 LYS N 152 LEU C -0.0977222 ? ? . . 0.0324297 DNC 155 LYS N 154 LYS C 0.528756 ? ? . . 0.0372817 DNC 157 ASN N 156 GLU C 0.186622 ? ? . . 0.0397867 DNC 162 ASP N 161 THR C 0.0260645 ? ? . . 0.0471415 DNC 166 LYS N 165 CYS C 0.222541 ? ? . . 0.0359503 DNC 168 ASN N 167 ASN C 0.3129 ? ? . . 0.0373979 stop_ _Details . _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 800 _Text_data_format . _Text_data . save_