data_6016 #Corrected using PDB structure: 2OHRA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 71 S CA 62.26 56.22 #236 Y CA 50.61 56.82 #364 K CA 62.66 56.65 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted #110 R CB 35.56 30.37 #136 A CB 15.34 20.52 #231 C CB 42.50 36.45 #283 C CB 50.02 42.01 #315 L CB 37.41 42.54 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted #241 V N 110.33 124.04 #314 I N 118.56 128.87 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted #191 G H 8.87 11.16 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A 0.24 0.66 0.03 -0.10 0.10 # #bmr6016.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6016.str file): #HA CA CB CO N HN #N/A +0.45 +0.45 +0.03 -0.10 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.08 +/-0.11 +/-0.08 +/-0.19 +/-0.04 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.961 0.994 0.788 0.876 0.695 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.728 0.895 0.745 1.662 0.351 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments of the 45.3 kDa catalytic domain of human BACE1 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Dingjiang . . 2 Wang Yu-sen . . 3 Gesell Jennifer J. . 4 Wilson Eileen . . 5 Beyer Brian M. . 6 Wyss Daniel . . stop_ _BMRB_accession_number 6016 _BMRB_flat_file_name bmr6016.str _Entry_type new _Submission_date 2003-11-19 _Accession_date 2003-11-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 319 '15N chemical shifts' 324 '13C chemical shifts' 917 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: Backbone resonance assignments of the 45.3 kDa catalytic domain of human BACE1 ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Dingjiang . . 2 Wang Yu-sen . . 3 Gesell Jennifer J. . 4 Wilson Eileen . . 5 Beyer Brian M. . 6 Wyss Daniel F. . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 29 _Journal_issue 3 _Page_first 425 _Page_last 426 _Year 2004 loop_ _Keyword "NMR assignments" "Alzheimer's disease" "BACE" stop_ save_ ################################## # Molecular system description # ################################## save_system_BACE1 _Saveframe_category molecular_system _Mol_system_name "beta-site APP Cleaving Enzyme 1" _Abbreviation_common BACE1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "BACE1 monomer" $BACE1_monomer stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function "membrane-associated aspartic protease" stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1M4H ? "1M4H is a crystal structure of BACE/inhibitor complex." stop_ save_ ######################## # Monomeric polymers # ######################## save_BACE1_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "beta-site APP Cleaving Enzyme 1" _Name_variant . _Abbreviation_common BACE1 _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 407 _Mol_residue_sequence ; DEEPEEPGRRGSFVEMVDNL RGKSGQGYYVEMTVGSPPQT LNILVDTGSSNFAVGAAPHP FLHRYYQRQLSSTYRDLRKG VYVPYTQGKWEGELGTDLVS IPHGPNVTVRANIAAITESD KFFINGSNWEGILGLAYAEI ARPDDSLEPFFDSLVKQTHV PNLFSLQLCGAGFPLNQSEV LASVGGSMIIGGIDHSLYTG SLWYTPIRREWYYEVIIVRV EINGQDLKMDCKEYNYDKSI VDSGTTNLRLPKKVFEAAVK SIKAASSTEKFPDGFWLGEQ LVCWQAGTTPWNIFPVISLY LMGEVTNQSFRITILPQQYL RPVEDVATSQDDCYKFAISQ SSTGTVMGAVIMEGFYVVFD RARKRIGFAVSACHVHDEFR TAAVEGPFVTLDMEDCGYNI PQTDEST ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 48 ASP 2 49 GLU 3 50 GLU 4 51 PRO 5 52 GLU 6 53 GLU 7 54 PRO 8 55 GLY 9 56 ARG 10 57 ARG 11 58 GLY 12 59 SER 13 60 PHE 14 61 VAL 15 62 GLU 16 63 MET 17 64 VAL 18 65 ASP 19 66 ASN 20 67 LEU 21 68 ARG 22 69 GLY 23 70 LYS 24 71 SER 25 72 GLY 26 73 GLN 27 74 GLY 28 75 TYR 29 76 TYR 30 77 VAL 31 78 GLU 32 79 MET 33 80 THR 34 81 VAL 35 82 GLY 36 83 SER 37 84 PRO 38 85 PRO 39 86 GLN 40 87 THR 41 88 LEU 42 89 ASN 43 90 ILE 44 91 LEU 45 92 VAL 46 93 ASP 47 94 THR 48 95 GLY 49 96 SER 50 97 SER 51 98 ASN 52 99 PHE 53 100 ALA 54 101 VAL 55 102 GLY 56 103 ALA 57 104 ALA 58 105 PRO 59 106 HIS 60 107 PRO 61 108 PHE 62 109 LEU 63 110 HIS 64 111 ARG 65 112 TYR 66 113 TYR 67 114 GLN 68 115 ARG 69 116 GLN 70 117 LEU 71 118 SER 72 119 SER 73 120 THR 74 121 TYR 75 122 ARG 76 123 ASP 77 124 LEU 78 125 ARG 79 126 LYS 80 127 GLY 81 128 VAL 82 129 TYR 83 130 VAL 84 131 PRO 85 132 TYR 86 133 THR 87 134 GLN 88 135 GLY 89 136 LYS 90 137 TRP 91 138 GLU 92 139 GLY 93 140 GLU 94 141 LEU 95 142 GLY 96 143 THR 97 144 ASP 98 145 LEU 99 146 VAL 100 147 SER 101 148 ILE 102 149 PRO 103 150 HIS 104 151 GLY 105 152 PRO 106 153 ASN 107 154 VAL 108 155 THR 109 156 VAL 110 157 ARG 111 158 ALA 112 159 ASN 113 160 ILE 114 161 ALA 115 162 ALA 116 163 ILE 117 164 THR 118 165 GLU 119 166 SER 120 167 ASP 121 168 LYS 122 169 PHE 123 170 PHE 124 171 ILE 125 172 ASN 126 173 GLY 127 174 SER 128 175 ASN 129 176 TRP 130 177 GLU 131 178 GLY 132 179 ILE 133 180 LEU 134 181 GLY 135 182 LEU 136 183 ALA 137 184 TYR 138 185 ALA 139 186 GLU 140 187 ILE 141 188 ALA 142 189 ARG 143 190 PRO 144 191 ASP 145 192 ASP 146 193 SER 147 194 LEU 148 195 GLU 149 196 PRO 150 197 PHE 151 198 PHE 152 199 ASP 153 200 SER 154 201 LEU 155 202 VAL 156 203 LYS 157 204 GLN 158 205 THR 159 206 HIS 160 207 VAL 161 208 PRO 162 209 ASN 163 210 LEU 164 211 PHE 165 212 SER 166 213 LEU 167 214 GLN 168 215 LEU 169 216 CYS 170 217 GLY 171 218 ALA 172 219 GLY 173 220 PHE 174 221 PRO 175 222 LEU 176 223 ASN 177 224 GLN 178 225 SER 179 226 GLU 180 227 VAL 181 228 LEU 182 229 ALA 183 230 SER 184 231 VAL 185 232 GLY 186 233 GLY 187 234 SER 188 235 MET 189 236 ILE 190 237 ILE 191 238 GLY 192 239 GLY 193 240 ILE 194 241 ASP 195 242 HIS 196 243 SER 197 244 LEU 198 245 TYR 199 246 THR 200 247 GLY 201 248 SER 202 249 LEU 203 250 TRP 204 251 TYR 205 252 THR 206 253 PRO 207 254 ILE 208 255 ARG 209 256 ARG 210 257 GLU 211 258 TRP 212 259 TYR 213 260 TYR 214 261 GLU 215 262 VAL 216 263 ILE 217 264 ILE 218 265 VAL 219 266 ARG 220 267 VAL 221 268 GLU 222 269 ILE 223 270 ASN 224 271 GLY 225 272 GLN 226 273 ASP 227 274 LEU 228 275 LYS 229 276 MET 230 277 ASP 231 278 CYS 232 279 LYS 233 280 GLU 234 281 TYR 235 282 ASN 236 283 TYR 237 284 ASP 238 285 LYS 239 286 SER 240 287 ILE 241 288 VAL 242 289 ASP 243 290 SER 244 291 GLY 245 292 THR 246 293 THR 247 294 ASN 248 295 LEU 249 296 ARG 250 297 LEU 251 298 PRO 252 299 LYS 253 300 LYS 254 301 VAL 255 302 PHE 256 303 GLU 257 304 ALA 258 305 ALA 259 306 VAL 260 307 LYS 261 308 SER 262 309 ILE 263 310 LYS 264 311 ALA 265 312 ALA 266 313 SER 267 314 SER 268 315 THR 269 316 GLU 270 317 LYS 271 318 PHE 272 319 PRO 273 320 ASP 274 321 GLY 275 322 PHE 276 323 TRP 277 324 LEU 278 325 GLY 279 326 GLU 280 327 GLN 281 328 LEU 282 329 VAL 283 330 CYS 284 331 TRP 285 332 GLN 286 333 ALA 287 334 GLY 288 335 THR 289 336 THR 290 337 PRO 291 338 TRP 292 339 ASN 293 340 ILE 294 341 PHE 295 342 PRO 296 343 VAL 297 344 ILE 298 345 SER 299 346 LEU 300 347 TYR 301 348 LEU 302 349 MET 303 350 GLY 304 351 GLU 305 352 VAL 306 353 THR 307 354 ASN 308 355 GLN 309 356 SER 310 357 PHE 311 358 ARG 312 359 ILE 313 360 THR 314 361 ILE 315 362 LEU 316 363 PRO 317 364 GLN 318 365 GLN 319 366 TYR 320 367 LEU 321 368 ARG 322 369 PRO 323 370 VAL 324 371 GLU 325 372 ASP 326 373 VAL 327 374 ALA 328 375 THR 329 376 SER 330 377 GLN 331 378 ASP 332 379 ASP 333 380 CYS 334 381 TYR 335 382 LYS 336 383 PHE 337 384 ALA 338 385 ILE 339 386 SER 340 387 GLN 341 388 SER 342 389 SER 343 390 THR 344 391 GLY 345 392 THR 346 393 VAL 347 394 MET 348 395 GLY 349 396 ALA 350 397 VAL 351 398 ILE 352 399 MET 353 400 GLU 354 401 GLY 355 402 PHE 356 403 TYR 357 404 VAL 358 405 VAL 359 406 PHE 360 407 ASP 361 408 ARG 362 409 ALA 363 410 ARG 364 411 LYS 365 412 ARG 366 413 ILE 367 414 GLY 368 415 PHE 369 416 ALA 370 417 VAL 371 418 SER 372 419 ALA 373 420 CYS 374 421 HIS 375 422 VAL 376 423 HIS 377 424 ASP 378 425 GLU 379 426 PHE 380 427 ARG 381 428 THR 382 429 ALA 383 430 ALA 384 431 VAL 385 432 GLU 386 433 GLY 387 434 PRO 388 435 PHE 389 436 VAL 390 437 THR 391 438 LEU 392 439 ASP 393 440 MET 394 441 GLU 395 442 ASP 396 443 CYS 397 444 GLY 398 445 TYR 399 446 ASN 400 447 ILE 401 448 PRO 402 449 GLN 403 450 THR 404 451 ASP 405 452 GLU 406 453 SER 407 454 THR stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-24 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 1SGZ "A Chain A, Crystal Structure Of UnboundBeta-Secretase Catalytic Domain." 104.63 389 100 100 0.0 PDB 1FKN "A Chain A, Structure Of Beta-SecretaseComplexed With Inhibitor" 104.09 391 100 100 0.0 PDB 1M4H "A Chain A, Crystal Structure Of Beta-SecretaseComplexed With Inhibitor Om00-3" 104.09 391 100 100 0.0 DBJ BAB29370.1 "unnamed protein product [Mus musculus]" 81.24 501 98 99 0.0 DBJ BAC28156.1 "unnamed protein product [Mus musculus]" 81.24 501 98 99 0.0 DBJ BAC30889.1 "unnamed protein product [Mus musculus]" 81.24 501 98 99 0.0 DBJ BAC33844.1 "unnamed protein product [Mus musculus]" 81.24 501 98 99 0.0 DBJ BAA86463.2 "KIAA1149 protein [Homo sapiens]" 76.50 532 100 100 0.0 GenBank AAF13715.1 "memapsin 2 [Homo sapiens]" 83.40 488 100 100 0.0 GenBank AAF04142.1 "beta-site APP cleaving enzyme [Homosapiens]" 81.24 501 100 100 0.0 GenBank AAF17079.1 "aspartyl protease 2 [Homo sapiens]" 81.24 501 100 100 0.0 GenBank AAF18982.1 "APP beta-secretase [Homo sapiens]" 81.24 501 100 100 0.0 GenBank AAF26367.1 "transmembrane aspartic proteinase Asp 2[Homo sapiens]" 81.24 501 100 100 0.0 PIR A59090 "aspartic proteinase (EC 3.4.23.-) BACEprecursor - human" 81.24 501 100 100 0.0 REF NP_620429.1 "beta-site APP-cleaving enzyme 1isoform D preproprotein; beta-site amyloid beta A4precursor protein-cleaving enzyme; APP beta-secretase;aspartyl protease 2; beta-site amyloid precursor proteincleaving enzyme; memapsin-2; membrane-associatedaspartic protease 2; transmembrane aspartic proteinaseAsp2; beta-secretase [Homo sapiens]" 94.21 432 100 100 1e-138 REF NP_036236.1 "beta-site APP-cleaving enzyme 1 isoformA preproprotein; beta-site amyloid beta A4 precursorprotein-cleaving enzyme; APP beta-secretase; aspartylprotease 2; beta-site amyloid precursor protein cleavingenzyme; memapsin-2; membrane-associated asparticprotease 2; transmembrane aspartic proteinase Asp2;beta-secretase [Homo sapiens]" 81.24 501 100 100 0.0 REF NP_035922.3 "beta-site APP cleaving enzyme 1; APPbeta-secretase [Mus musculus]" 81.24 501 98 99 0.0 REF NP_062077.1 "beta-site APP cleaving enzyme [Rattusnorvegicus]" 81.24 501 98 99 0.0 SWISS-PROT P56817 "BAE1_HUMAN Beta-secretase 1 precursor(Beta-site APP cleaving enzyme 1) (Beta-site amyloidprecursor protein cleaving enzyme 1) (Aspartyl protease2) (Asp 2) (ASP2) (Membrane-associated aspartic protease2) (Memapsin-2)" 81.24 501 100 100 0.0 SWISS-PROT P56818 "BAE1_MOUSE Beta-secretase 1 precursor(Beta-site APP cleaving enzyme 1) (Beta-site amyloidprecursor protein cleaving enzyme 1) (Aspartyl protease2) (Asp 2) (ASP2) (Membrane-associated aspartic protease2) (Memapsin-2)" 81.24 501 98 99 0.0 SWISS-PROT P56819 "BAE1_RAT Beta-secretase 1 precursor (Beta-siteAPP cleaving enzyme 1) (Beta-site amyloid precursorprotein cleaving enzyme 1) (Aspartyl protease 2) (Asp 2)(ASP2) (Membrane-associated aspartic protease 2)(Memapsin-2)" 81.24 501 98 99 0.0 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide "BACE1 monomer" 169 CYS SG "BACE1 monomer" 373 CYS SG single disulfide "BACE1 monomer" 283 CYS SG "BACE1 monomer" 333 CYS SG single disulfide "BACE1 monomer" 231 CYS SG "BACE1 monomer" 396 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BACE1_monomer 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 $BACE1_monomer 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BACE1_monomer 0.9 mM "[U-2H; U-15N; U-13C]" stop_ save_ ############################ # Computer software used # ############################ save_NMRpipe _Saveframe_category software _Name NMRpipe loop_ _Task "data processing" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N TROSY 3D-TROSY-HNCACB 3D-TROSY-HNCACO 3D-TROSY-HNCA 3D-TROSY-HNCO 3D-TROSY-HNCOCA 3D-TROSY-CT-CACB(CO)NH 4D TROSY-HNCOCA 4D TROSY-HNCACO ; save_ ####################### # Sample conditions # ####################### save_condi-1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 n/a temperature 298 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details ; Chemical shift reference was calibrated based on the proton chemical shift of an external standard. ; 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS C 13 'methyl protons' ppm 0.0 external indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.0 external indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condi-1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "BACE1 monomer" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 GLU N N 120.91 0.2 1 2 2 GLU H H 8.12 0.02 1 3 2 GLU CA C 56.46 0.1 1 4 2 GLU CB C 30.53 0.1 1 7 3 GLU H H 8.33 0.02 1 10 5 GLU N N 121.48 0.2 1 14 8 GLY H H 8.46 0.02 1 16 13 PHE C C 176.69 0.1 1 17 14 VAL N N 118.89 0.2 1 18 14 VAL H H 7.42 0.02 1 19 14 VAL CA C 64.94 0.1 1 20 14 VAL C C 177.00 0.1 1 21 15 GLU N N 120.27 0.2 1 22 15 GLU H H 9.04 0.02 1 23 15 GLU CA C 58.23 0.1 1 25 15 GLU C C 177.42 0.1 1 26 16 MET N N 118.29 0.2 1 27 16 MET H H 8.09 0.02 1 28 16 MET CA C 55.87 0.1 1 29 16 MET C C 173.38 0.1 1 30 17 VAL N N 117.42 0.2 1 31 17 VAL H H 6.84 0.02 1 32 17 VAL CA C 63.32 0.1 1 36 18 ASP H H 7.53 0.02 1 38 25 GLY C C 174.54 0.1 1 39 26 GLN N N 117.64 0.2 1 40 26 GLN H H 8.07 0.02 1 41 26 GLN CA C 55.13 0.1 1 43 26 GLN C C 176.15 0.1 1 44 27 GLY N N 109.99 0.2 1 45 27 GLY H H 7.76 0.02 1 46 27 GLY CA C 45.02 0.1 1 47 27 GLY C C 172.05 0.1 1 48 28 TYR N N 119.81 0.2 1 49 28 TYR H H 8.64 0.02 1 50 28 TYR CA C 56.85 0.1 1 51 28 TYR CB C 40.90 0.1 1 52 28 TYR C C 174.61 0.1 1 53 29 TYR N N 117.65 0.2 1 54 29 TYR H H 9.18 0.02 1 55 29 TYR CA C 54.62 0.1 1 56 29 TYR CB C 42.73 0.1 1 57 29 TYR C C 172.07 0.1 1 58 30 VAL N N 122.45 0.2 1 59 30 VAL H H 9.23 0.02 1 60 30 VAL CA C 58.82 0.1 1 61 30 VAL CB C 36.83 0.1 1 62 30 VAL C C 172.96 0.1 1 63 31 GLU N N 129.06 0.2 1 64 31 GLU H H 8.46 0.02 1 65 31 GLU CA C 57.49 0.1 1 66 31 GLU CB C 30.76 0.1 1 67 31 GLU C C 176.62 0.1 1 68 32 MET N N 123.94 0.2 1 69 32 MET H H 9.35 0.02 1 70 32 MET CA C 55.49 0.1 1 71 32 MET CB C 37.82 0.1 1 72 32 MET C C 174.19 0.1 1 73 33 THR N N 109.04 0.2 1 74 33 THR H H 8.80 0.02 1 75 33 THR CA C 59.18 0.1 1 76 33 THR CB C 70.98 0.1 1 77 33 THR C C 173.74 0.1 1 78 34 VAL N N 119.59 0.2 1 79 34 VAL H H 8.80 0.02 1 80 34 VAL CA C 59.72 0.1 1 82 34 VAL C C 177.00 0.1 1 83 35 GLY N N 110.98 0.2 1 84 35 GLY H H 8.63 0.02 1 85 35 GLY CA C 43.68 0.1 1 88 36 SER H H 7.45 0.02 1 91 38 PRO C C 177.82 0.1 1 92 39 GLN N N 126.37 0.2 1 93 39 GLN H H 8.66 0.02 1 94 39 GLN CA C 55.04 0.1 1 95 39 GLN CB C 28.84 0.1 1 96 39 GLN C C 175.48 0.1 1 97 40 THR N N 121.68 0.2 1 98 40 THR H H 8.21 0.02 1 99 40 THR CA C 63.94 0.1 1 100 40 THR CB C 69.02 0.1 1 101 40 THR C C 173.59 0.1 1 102 41 LEU N N 125.92 0.2 1 103 41 LEU H H 8.85 0.02 1 104 41 LEU CA C 53.99 0.1 1 105 41 LEU CB C 47.86 0.1 1 106 41 LEU C C 174.23 0.1 1 107 42 ASN N N 120.26 0.2 1 108 42 ASN H H 9.20 0.02 1 109 42 ASN CA C 51.75 0.1 1 110 42 ASN CB C 40.41 0.1 1 111 42 ASN C C 175.79 0.1 1 112 43 ILE N N 124.85 0.2 1 113 43 ILE H H 9.22 0.02 1 114 43 ILE CA C 57.73 0.1 1 115 43 ILE CB C 37.55 0.1 1 116 43 ILE C C 174.88 0.1 1 117 44 LEU N N 130.25 0.2 1 118 44 LEU H H 8.63 0.02 1 119 44 LEU CA C 55.95 0.1 1 120 44 LEU CB C 41.81 0.1 1 121 44 LEU C C 175.80 0.1 1 122 45 VAL N N 125.82 0.2 1 123 45 VAL H H 8.90 0.02 1 124 45 VAL CA C 63.38 0.1 1 125 45 VAL CB C 31.55 0.1 1 126 45 VAL C C 176.06 0.1 1 127 46 ASP N N 130.45 0.2 1 128 46 ASP H H 8.24 0.02 1 129 46 ASP CA C 53.16 0.1 1 130 46 ASP CB C 43.69 0.1 1 131 46 ASP C C 175.16 0.1 1 132 47 THR N N 116.02 0.2 1 133 47 THR H H 8.46 0.02 1 134 47 THR CA C 64.17 0.1 1 136 47 THR C C 173.59 0.1 1 137 48 GLY N N 113.61 0.2 1 138 48 GLY H H 9.01 0.02 1 139 48 GLY CA C 45.28 0.1 1 142 49 SER H H 7.29 0.02 1 145 51 ASN C C 174.96 0.1 1 146 52 PHE N N 127.29 0.2 1 147 52 PHE H H 8.99 0.02 1 148 52 PHE CA C 54.70 0.1 1 149 52 PHE C C 173.93 0.1 1 150 53 ALA N N 134.64 0.2 1 151 53 ALA H H 8.97 0.02 1 152 53 ALA CA C 50.55 0.1 1 153 53 ALA CB C 22.94 0.1 1 154 53 ALA C C 174.85 0.1 1 155 54 VAL N N 113.99 0.2 1 156 54 VAL H H 8.49 0.02 1 157 54 VAL CA C 58.35 0.1 1 159 54 VAL C C 175.22 0.1 1 160 55 GLY N N 112.51 0.2 1 161 55 GLY H H 9.63 0.02 1 162 55 GLY CA C 48.96 0.1 1 163 55 GLY C C 173.96 0.1 1 164 56 ALA N N 128.97 0.2 1 165 56 ALA H H 8.60 0.02 1 166 56 ALA CA C 51.87 0.1 1 167 56 ALA CB C 19.59 0.1 1 170 57 ALA H H 7.33 0.02 1 173 62 LEU C C 177.55 0.1 1 174 63 HIS N N 122.25 0.2 1 175 63 HIS H H 9.72 0.02 1 176 63 HIS CA C 56.92 0.1 1 177 63 HIS CB C 30.51 0.1 1 178 63 HIS C C 174.87 0.1 1 179 64 ARG N N 115.63 0.2 1 180 64 ARG H H 7.46 0.02 1 181 64 ARG CA C 54.41 0.1 1 182 64 ARG CB C 32.81 0.1 1 183 64 ARG C C 171.78 0.1 1 184 65 TYR N N 109.79 0.2 1 185 65 TYR H H 7.33 0.02 1 186 65 TYR CA C 56.20 0.1 1 187 65 TYR CB C 38.69 0.1 1 188 65 TYR C C 173.40 0.1 1 189 66 TYR N N 121.45 0.2 1 190 66 TYR H H 9.04 0.02 1 191 66 TYR CA C 55.26 0.1 1 192 66 TYR CB C 39.16 0.1 1 193 66 TYR C C 173.95 0.1 1 194 67 GLN N N 128.82 0.2 1 195 67 GLN H H 9.25 0.02 1 196 67 GLN CA C 54.06 0.1 1 197 67 GLN CB C 28.72 0.1 1 198 67 GLN C C 177.14 0.1 1 199 68 ARG N N 127.65 0.2 1 200 68 ARG H H 8.55 0.02 1 201 68 ARG CA C 59.69 0.1 1 202 68 ARG CB C 29.17 0.1 1 203 68 ARG C C 178.17 0.1 1 204 69 GLN N N 116.31 0.2 1 205 69 GLN H H 8.83 0.02 1 206 69 GLN CA C 57.33 0.1 1 207 69 GLN CB C 26.50 0.1 1 208 69 GLN C C 176.46 0.1 1 209 70 LEU N N 116.56 0.2 1 210 70 LEU H H 6.90 0.02 1 211 70 LEU CA C 54.09 0.1 1 212 70 LEU CB C 41.42 0.1 1 213 70 LEU C C 177.72 0.1 1 214 71 SER N N 115.14 0.2 1 215 71 SER H H 7.50 0.02 1 216 71 SER CA C 62.47 0.1 1 217 71 SER CB C 63.03 0.1 1 218 71 SER C C 176.18 0.1 1 219 72 SER N N 124.31 0.2 1 220 72 SER H H 9.26 0.02 1 221 72 SER CA C 60.29 0.1 1 222 72 SER CB C 63.02 0.1 1 223 72 SER C C 176.02 0.1 1 224 73 THR N N 109.08 0.2 1 225 73 THR H H 7.90 0.02 1 226 73 THR CA C 60.97 0.1 1 227 73 THR CB C 68.93 0.1 1 228 73 THR C C 174.34 0.1 1 229 74 TYR N N 124.75 0.2 1 230 74 TYR H H 6.90 0.02 1 231 74 TYR CA C 59.20 0.1 1 232 74 TYR CB C 38.42 0.1 1 233 74 TYR C C 175.74 0.1 1 234 75 ARG N N 130.31 0.2 1 235 75 ARG H H 8.41 0.02 1 236 75 ARG CA C 54.26 0.1 1 237 75 ARG CB C 31.50 0.1 1 238 75 ARG C C 173.16 0.1 1 239 76 ASP N N 123.65 0.2 1 240 76 ASP H H 8.25 0.02 1 241 76 ASP CA C 54.52 0.1 1 242 76 ASP CB C 42.31 0.1 1 243 76 ASP C C 177.90 0.1 1 244 77 LEU N N 126.73 0.2 1 245 77 LEU H H 8.34 0.02 1 246 77 LEU CA C 55.42 0.1 1 247 77 LEU CB C 42.08 0.1 1 248 77 LEU C C 176.24 0.1 1 249 78 ARG N N 119.79 0.2 1 250 78 ARG H H 9.09 0.02 1 251 78 ARG CA C 56.51 0.1 1 252 78 ARG CB C 27.12 0.1 1 253 78 ARG C C 175.15 0.1 1 254 79 LYS N N 118.29 0.2 1 255 79 LYS H H 7.98 0.02 1 256 79 LYS CA C 56.28 0.1 1 258 79 LYS C C 174.33 0.1 1 259 80 GLY N N 112.51 0.2 1 260 80 GLY H H 8.48 0.02 1 261 80 GLY CA C 44.20 0.1 1 262 80 GLY C C 172.33 0.1 1 263 81 VAL N N 115.84 0.2 1 264 81 VAL H H 8.02 0.02 1 265 81 VAL CA C 60.34 0.1 1 266 81 VAL CB C 34.32 0.1 1 267 81 VAL C C 171.12 0.1 1 268 82 TYR N N 127.70 0.2 1 269 82 TYR H H 7.93 0.02 1 270 82 TYR CA C 56.82 0.1 1 271 82 TYR CB C 40.43 0.1 1 274 83 VAL H H 7.99 0.02 1 279 85 TYR H H 8.19 0.02 1 282 87 GLN C C 175.04 0.1 1 283 88 GLY N N 109.92 0.2 1 284 88 GLY H H 7.93 0.02 1 285 88 GLY CA C 45.32 0.1 1 286 88 GLY C C 172.94 0.1 1 287 89 LYS N N 116.71 0.2 1 288 89 LYS H H 8.66 0.02 1 289 89 LYS CA C 55.57 0.1 1 290 89 LYS CB C 34.84 0.1 1 291 89 LYS C C 174.29 0.1 1 292 90 TRP N N 115.78 0.2 1 293 90 TRP H H 7.97 0.02 1 294 90 TRP CA C 56.26 0.1 1 295 90 TRP CB C 33.20 0.1 1 296 90 TRP C C 172.94 0.1 1 297 91 GLU N N 118.75 0.2 1 298 91 GLU H H 8.86 0.02 1 299 91 GLU CA C 54.71 0.1 1 301 91 GLU C C 175.73 0.1 1 302 92 GLY N N 107.71 0.2 1 303 92 GLY H H 8.91 0.02 1 304 92 GLY CA C 46.49 0.1 1 305 92 GLY C C 172.79 0.1 1 306 93 GLU N N 121.40 0.2 1 307 93 GLU H H 8.49 0.02 1 308 93 GLU CA C 55.18 0.1 1 309 93 GLU CB C 32.47 0.1 1 310 93 GLU C C 176.73 0.1 1 311 94 LEU N N 123.66 0.2 1 312 94 LEU H H 9.04 0.02 1 313 94 LEU CA C 55.23 0.1 1 315 94 LEU C C 177.02 0.1 1 316 95 GLY N N 111.76 0.2 1 317 95 GLY H H 8.68 0.02 1 318 95 GLY CA C 45.95 0.1 1 319 95 GLY C C 171.11 0.1 1 320 96 THR N N 109.06 0.2 1 321 96 THR H H 9.06 0.02 1 322 96 THR CA C 59.30 0.1 1 323 96 THR CB C 72.79 0.1 1 324 96 THR C C 173.34 0.1 1 325 97 ASP N N 116.84 0.2 1 326 97 ASP H H 8.42 0.02 1 327 97 ASP CA C 52.63 0.1 1 328 97 ASP CB C 43.70 0.1 1 329 97 ASP C C 174.20 0.1 1 330 98 LEU N N 119.96 0.2 1 331 98 LEU H H 9.79 0.02 1 332 98 LEU CA C 54.12 0.1 1 333 98 LEU CB C 41.40 0.1 1 334 98 LEU C C 177.58 0.1 1 335 99 VAL N N 124.25 0.2 1 336 99 VAL H H 9.42 0.02 1 337 99 VAL CA C 60.70 0.1 1 338 99 VAL CB C 35.71 0.1 1 339 99 VAL C C 174.63 0.1 1 340 100 SER N N 119.73 0.2 1 341 100 SER H H 8.66 0.02 1 342 100 SER CA C 57.00 0.1 1 343 100 SER CB C 66.86 0.1 1 346 101 ILE H H 9.23 0.02 1 349 102 PRO C C 178.25 0.1 1 350 103 HIS N N 118.27 0.2 1 351 103 HIS H H 9.14 0.02 1 352 103 HIS CA C 54.05 0.1 1 356 104 GLY H H 7.12 0.02 1 358 106 ASN C C 174.58 0.1 1 359 107 VAL N N 113.54 0.2 1 360 107 VAL H H 7.62 0.02 1 361 107 VAL CA C 59.17 0.1 1 362 107 VAL CB C 35.32 0.1 1 363 107 VAL C C 174.83 0.1 1 364 108 THR N N 119.91 0.2 1 365 108 THR H H 8.33 0.02 1 366 108 THR CA C 62.09 0.1 1 367 108 THR CB C 70.95 0.1 1 368 108 THR C C 173.03 0.1 1 369 109 VAL N N 121.38 0.2 1 370 109 VAL H H 8.54 0.02 1 371 109 VAL CA C 59.15 0.1 1 372 109 VAL CB C 35.21 0.1 1 373 109 VAL C C 174.24 0.1 1 374 110 ARG N N 125.81 0.2 1 375 110 ARG H H 9.00 0.02 1 376 110 ARG CA C 55.97 0.1 1 377 110 ARG CB C 35.35 0.1 1 378 110 ARG C C 174.54 0.1 1 379 111 ALA N N 131.02 0.2 1 380 111 ALA H H 8.67 0.02 1 381 111 ALA CA C 49.56 0.1 1 382 111 ALA CB C 23.06 0.1 1 383 111 ALA C C 175.71 0.1 1 384 112 ASN N N 116.57 0.2 1 385 112 ASN H H 8.59 0.02 1 386 112 ASN CA C 54.44 0.1 1 387 112 ASN CB C 39.68 0.1 1 388 112 ASN C C 175.11 0.1 1 389 113 ILE N N 121.39 0.2 1 390 113 ILE H H 9.41 0.02 1 391 113 ILE CA C 60.80 0.1 1 392 113 ILE CB C 42.30 0.1 1 393 113 ILE C C 174.60 0.1 1 394 114 ALA N N 128.98 0.2 1 395 114 ALA H H 8.55 0.02 1 396 114 ALA CA C 50.54 0.1 1 397 114 ALA CB C 19.59 0.1 1 398 114 ALA C C 173.93 0.1 1 399 115 ALA N N 129.66 0.2 1 400 115 ALA H H 9.03 0.02 1 401 115 ALA CA C 50.78 0.1 1 402 115 ALA CB C 16.75 0.1 1 403 115 ALA C C 175.71 0.1 1 404 116 ILE N N 125.38 0.2 1 405 116 ILE H H 9.05 0.02 1 406 116 ILE CA C 63.57 0.1 1 407 116 ILE CB C 38.45 0.1 1 408 116 ILE C C 177.09 0.1 1 409 117 THR N N 122.45 0.2 1 410 117 THR H H 9.04 0.02 1 411 117 THR CA C 61.98 0.1 1 412 117 THR CB C 68.63 0.1 1 413 117 THR C C 174.63 0.1 1 414 118 GLU N N 123.19 0.2 1 415 118 GLU H H 7.81 0.02 1 416 118 GLU CA C 56.42 0.1 1 417 118 GLU CB C 33.03 0.1 1 418 118 GLU C C 173.98 0.1 1 419 119 SER N N 115.39 0.2 1 420 119 SER H H 8.64 0.02 1 421 119 SER CA C 59.14 0.1 1 422 119 SER CB C 65.72 0.1 1 423 119 SER C C 172.67 0.1 1 424 120 ASP N N 119.93 0.2 1 425 120 ASP H H 8.77 0.02 1 426 120 ASP CA C 54.67 0.1 1 427 120 ASP CB C 44.50 0.1 1 428 120 ASP C C 174.24 0.1 1 429 121 LYS N N 120.62 0.2 1 430 121 LYS H H 8.67 0.02 1 431 121 LYS CA C 57.87 0.1 1 432 121 LYS CB C 29.47 0.1 1 433 121 LYS C C 173.63 0.1 1 434 122 PHE N N 119.59 0.2 1 435 122 PHE H H 8.38 0.02 1 436 122 PHE CA C 59.10 0.1 1 437 122 PHE CB C 42.11 0.1 1 438 122 PHE C C 174.60 0.1 1 439 123 PHE N N 116.87 0.2 1 440 123 PHE H H 8.14 0.02 1 441 123 PHE CA C 58.07 0.1 1 442 123 PHE CB C 38.54 0.1 1 445 124 ILE H H 7.93 0.02 1 448 129 TRP C C 173.56 0.1 1 449 130 GLU H H 11.14 0.02 1 450 130 GLU C C 174.93 0.1 1 451 131 GLY N N 106.69 0.2 1 452 131 GLY H H 8.26 0.02 1 453 131 GLY CA C 46.36 0.1 1 454 131 GLY C C 169.32 0.1 1 455 132 ILE N N 119.36 0.2 1 456 132 ILE H H 9.83 0.02 1 457 132 ILE CA C 60.71 0.1 1 458 132 ILE CB C 42.65 0.1 1 459 132 ILE C C 171.07 0.1 1 460 133 LEU N N 127.64 0.2 1 461 133 LEU H H 9.38 0.02 1 462 133 LEU CA C 53.12 0.1 1 464 133 LEU C C 173.63 0.1 1 465 134 GLY N N 113.22 0.2 1 466 134 GLY H H 7.26 0.02 1 467 134 GLY CA C 47.90 0.1 1 468 134 GLY C C 176.13 0.1 1 469 135 LEU N N 128.62 0.2 1 470 135 LEU H H 8.24 0.02 1 471 135 LEU CA C 55.19 0.1 1 472 135 LEU CB C 43.36 0.1 1 473 135 LEU C C 175.66 0.1 1 474 136 ALA N N 125.49 0.2 1 475 136 ALA H H 8.58 0.02 1 476 136 ALA CA C 51.98 0.1 1 477 136 ALA CB C 15.13 0.1 1 478 136 ALA C C 175.21 0.1 1 479 137 TYR N N 112.08 0.2 1 480 137 TYR H H 7.28 0.02 1 481 137 TYR CA C 58.85 0.1 1 482 137 TYR CB C 38.77 0.1 1 483 137 TYR C C 178.41 0.1 1 484 138 ALA N N 124.47 0.2 1 485 138 ALA H H 9.86 0.02 1 486 138 ALA CA C 55.50 0.1 1 487 138 ALA CB C 17.66 0.1 1 488 138 ALA C C 178.24 0.1 1 489 139 GLU N N 114.62 0.2 1 490 139 GLU H H 8.10 0.02 1 491 139 GLU CA C 59.80 0.1 1 492 139 GLU CB C 30.75 0.1 1 493 139 GLU C C 177.69 0.1 1 494 140 ILE N N 105.01 0.2 1 495 140 ILE H H 6.71 0.02 1 496 140 ILE CA C 60.17 0.1 1 497 140 ILE CB C 37.00 0.1 1 498 140 ILE C C 176.51 0.1 1 499 141 ALA N N 127.67 0.2 1 500 141 ALA H H 7.92 0.02 1 501 141 ALA CA C 53.38 0.1 1 502 141 ALA CB C 19.21 0.1 1 505 142 ARG H H 8.59 0.02 1 508 143 PRO C C 175.87 0.1 1 509 144 ASP N N 115.80 0.2 1 510 144 ASP H H 7.32 0.02 1 511 144 ASP CA C 53.34 0.1 1 512 144 ASP CB C 41.78 0.1 1 513 144 ASP C C 173.52 0.1 1 514 145 ASP N N 113.65 0.2 1 515 145 ASP H H 8.05 0.02 1 516 145 ASP CA C 54.61 0.1 1 517 145 ASP CB C 41.03 0.1 1 518 145 ASP C C 176.38 0.1 1 519 146 SER N N 116.41 0.2 1 520 146 SER H H 8.72 0.02 1 521 146 SER CA C 60.24 0.1 1 522 146 SER CB C 63.69 0.1 1 523 146 SER C C 174.85 0.1 1 524 147 LEU N N 127.51 0.2 1 525 147 LEU H H 7.41 0.02 1 526 147 LEU CA C 53.54 0.1 1 527 147 LEU CB C 39.96 0.1 1 530 148 GLU H H 7.51 0.02 1 533 149 PRO C C 175.52 0.1 1 534 150 PHE N N 122.27 0.2 1 535 150 PHE H H 9.10 0.02 1 536 150 PHE CA C 62.56 0.1 1 537 150 PHE CB C 40.41 0.1 1 538 150 PHE C C 176.47 0.1 1 539 151 PHE N N 119.99 0.2 1 540 151 PHE H H 9.95 0.02 1 541 151 PHE CA C 62.54 0.1 1 542 151 PHE CB C 39.87 0.1 1 543 151 PHE C C 176.98 0.1 1 544 152 ASP N N 114.87 0.2 1 545 152 ASP H H 7.02 0.02 1 546 152 ASP CA C 57.47 0.1 1 548 152 ASP C C 178.62 0.1 1 549 153 SER N N 116.70 0.2 1 550 153 SER H H 7.75 0.02 1 551 153 SER CA C 61.66 0.1 1 552 153 SER C C 174.91 0.1 1 553 154 LEU N N 121.76 0.2 1 554 154 LEU H H 7.92 0.02 1 555 154 LEU CA C 58.23 0.1 1 556 154 LEU CB C 40.06 0.1 1 557 154 LEU C C 179.22 0.1 1 558 155 VAL N N 120.30 0.2 1 559 155 VAL H H 7.74 0.02 1 560 155 VAL CA C 65.40 0.1 1 561 155 VAL CB C 31.03 0.1 1 562 155 VAL C C 178.03 0.1 1 563 156 LYS N N 118.29 0.2 1 564 156 LYS H H 7.69 0.02 1 565 156 LYS CA C 59.37 0.1 1 566 156 LYS CB C 32.72 0.1 1 567 156 LYS C C 179.28 0.1 1 568 157 GLN N N 113.58 0.2 1 569 157 GLN H H 7.86 0.02 1 570 157 GLN CA C 57.21 0.1 1 571 157 GLN CB C 30.61 0.1 1 574 158 THR H H 7.26 0.02 1 577 161 PRO C C 176.41 0.1 1 578 162 ASN N N 117.43 0.2 1 579 162 ASN H H 8.30 0.02 1 580 162 ASN CA C 52.24 0.1 1 581 162 ASN CB C 37.13 0.1 1 582 162 ASN C C 173.93 0.1 1 583 163 LEU N N 122.52 0.2 1 584 163 LEU H H 9.13 0.02 1 585 163 LEU CA C 56.53 0.1 1 586 163 LEU CB C 44.79 0.1 1 587 163 LEU C C 174.84 0.1 1 588 164 PHE N N 116.31 0.2 1 589 164 PHE H H 7.80 0.02 1 590 164 PHE CA C 54.27 0.1 1 591 164 PHE CB C 41.23 0.1 1 592 164 PHE C C 171.85 0.1 1 593 165 SER N N 113.60 0.2 1 594 165 SER H H 9.49 0.02 1 595 165 SER CA C 56.25 0.1 1 596 165 SER CB C 67.17 0.1 1 597 165 SER C C 172.06 0.1 1 598 166 LEU N N 121.50 0.2 1 599 166 LEU H H 9.27 0.02 1 600 166 LEU CA C 53.79 0.1 1 601 166 LEU CB C 46.66 0.1 1 604 167 GLN H H 9.47 0.02 1 607 170 GLY C C 173.95 0.1 1 608 171 ALA N N 123.92 0.2 1 609 171 ALA H H 8.48 0.02 1 610 171 ALA CA C 53.01 0.1 1 612 171 ALA C C 178.23 0.1 1 613 172 GLY N N 107.34 0.2 1 614 172 GLY H H 8.29 0.02 1 615 172 GLY CA C 45.54 0.1 1 618 173 PHE H H 7.79 0.02 1 621 179 GLU C C 176.40 0.1 1 622 180 VAL N N 119.46 0.2 1 623 180 VAL H H 7.92 0.02 1 624 180 VAL CA C 62.55 0.1 1 625 180 VAL CB C 32.49 0.1 1 626 180 VAL C C 176.19 0.1 1 627 181 LEU N N 124.85 0.2 1 628 181 LEU H H 8.12 0.02 1 629 181 LEU CA C 55.65 0.1 1 630 181 LEU CB C 41.96 0.1 1 631 181 LEU C C 176.85 0.1 1 632 182 ALA N N 123.38 0.2 1 633 182 ALA H H 8.21 0.02 1 634 182 ALA CA C 52.35 0.1 1 635 182 ALA CB C 19.48 0.1 1 636 182 ALA C C 176.76 0.1 1 637 183 SER N N 114.74 0.2 1 638 183 SER H H 8.02 0.02 1 639 183 SER CA C 58.66 0.1 1 640 183 SER CB C 64.82 0.1 1 642 184 VAL N N 117.14 0.2 1 643 184 VAL H H 7.89 0.02 1 646 185 GLY N N 107.27 0.2 1 647 185 GLY C C 171.34 0.1 1 648 186 GLY N N 107.47 0.2 1 649 186 GLY H H 7.48 0.02 1 650 186 GLY CA C 46.06 0.1 1 651 186 GLY C C 172.88 0.1 1 652 187 SER N N 114.59 0.2 1 653 187 SER H H 9.38 0.02 1 654 187 SER CA C 58.58 0.1 1 655 187 SER CB C 67.12 0.1 1 656 187 SER C C 171.68 0.1 1 657 188 MET N N 128.15 0.2 1 658 188 MET H H 10.53 0.02 1 659 188 MET CA C 54.64 0.1 1 660 188 MET CB C 34.78 0.1 1 661 188 MET C C 173.91 0.1 1 662 189 ILE N N 126.19 0.2 1 663 189 ILE H H 8.72 0.02 1 664 189 ILE CA C 58.51 0.1 1 665 189 ILE CB C 34.68 0.1 1 666 189 ILE C C 176.51 0.1 1 667 190 ILE N N 129.84 0.2 1 668 190 ILE H H 7.94 0.02 1 669 190 ILE CA C 62.25 0.1 1 671 190 ILE C C 174.79 0.1 1 672 191 GLY N N 114.63 0.2 1 673 191 GLY H H 8.77 0.02 1 674 191 GLY CA C 46.25 0.1 1 675 191 GLY C C 173.31 0.1 1 676 192 GLY N N 102.34 0.2 1 677 192 GLY H H 6.36 0.02 1 678 192 GLY CA C 45.77 0.1 1 679 192 GLY C C 169.24 0.1 1 680 193 ILE N N 119.40 0.2 1 681 193 ILE H H 7.82 0.02 1 682 193 ILE CA C 60.16 0.1 1 683 193 ILE CB C 41.80 0.1 1 684 193 ILE C C 173.62 0.1 1 685 194 ASP N N 125.33 0.2 1 686 194 ASP H H 7.74 0.02 1 687 194 ASP CA C 52.84 0.1 1 688 194 ASP CB C 42.30 0.1 1 691 195 HIS H H 8.05 0.02 1 694 196 SER C C 176.40 0.1 1 695 197 LEU N N 119.16 0.2 1 696 197 LEU H H 7.07 0.02 1 697 197 LEU CA C 55.45 0.1 1 698 197 LEU CB C 39.14 0.1 1 699 197 LEU C C 175.71 0.1 1 700 198 TYR N N 115.65 0.2 1 701 198 TYR H H 6.96 0.02 1 702 198 TYR CA C 55.02 0.1 1 703 198 TYR CB C 42.02 0.1 1 704 198 TYR C C 172.90 0.1 1 705 199 THR N N 110.99 0.2 1 706 199 THR H H 8.54 0.02 1 707 199 THR CA C 59.66 0.1 1 709 199 THR C C 174.82 0.1 1 710 200 GLY N N 110.38 0.2 1 711 200 GLY H H 8.59 0.02 1 712 200 GLY CA C 46.14 0.1 1 713 200 GLY C C 173.59 0.1 1 714 201 SER N N 116.80 0.2 1 715 201 SER H H 8.32 0.02 1 716 201 SER CA C 58.42 0.1 1 717 201 SER CB C 65.04 0.1 1 718 201 SER C C 173.71 0.1 1 719 202 LEU N N 123.48 0.2 1 720 202 LEU H H 8.03 0.02 1 721 202 LEU CA C 54.89 0.1 1 722 202 LEU CB C 43.68 0.1 1 723 202 LEU C C 176.38 0.1 1 724 203 TRP N N 125.14 0.2 1 725 203 TRP H H 8.07 0.02 1 726 203 TRP CA C 56.56 0.1 1 727 203 TRP CB C 30.27 0.1 1 728 203 TRP C C 174.27 0.1 1 729 204 TYR N N 117.40 0.2 1 730 204 TYR H H 8.16 0.02 1 731 204 TYR CA C 57.11 0.1 1 732 204 TYR CB C 41.78 0.1 1 735 205 THR H H 9.61 0.02 1 738 206 PRO C C 177.42 0.1 1 739 207 ILE N N 123.91 0.2 1 740 207 ILE H H 8.15 0.02 1 741 207 ILE CA C 61.61 0.1 1 742 207 ILE CB C 38.30 0.1 1 743 207 ILE C C 176.86 0.1 1 744 208 ARG N N 131.35 0.2 1 745 208 ARG H H 8.85 0.02 1 746 208 ARG CA C 59.01 0.1 1 747 208 ARG CB C 31.24 0.1 1 748 208 ARG C C 175.82 0.1 1 749 209 ARG N N 115.69 0.2 1 750 209 ARG H H 7.07 0.02 1 751 209 ARG CA C 55.57 0.1 1 752 209 ARG CB C 33.02 0.1 1 753 209 ARG C C 173.97 0.1 1 754 210 GLU N N 125.46 0.2 1 755 210 GLU H H 8.48 0.02 1 756 210 GLU CA C 55.51 0.1 1 758 210 GLU C C 174.29 0.1 1 759 211 TRP N N 123.27 0.2 1 760 211 TRP H H 8.71 0.02 1 761 211 TRP CA C 58.29 0.1 1 762 211 TRP C C 175.75 0.1 1 763 212 TYR N N 124.45 0.2 1 764 212 TYR H H 6.71 0.02 1 765 212 TYR CA C 59.32 0.1 1 766 212 TYR CB C 41.42 0.1 1 767 212 TYR C C 176.15 0.1 1 768 213 TYR N N 119.39 0.2 1 769 213 TYR H H 9.56 0.02 1 770 213 TYR CA C 59.50 0.1 1 771 213 TYR CB C 35.46 0.1 1 772 213 TYR C C 174.57 0.1 1 773 214 GLU N N 125.17 0.2 1 774 214 GLU H H 7.04 0.02 1 775 214 GLU CA C 55.41 0.1 1 776 214 GLU CB C 31.03 0.1 1 777 214 GLU C C 175.14 0.1 1 778 215 VAL N N 119.98 0.2 1 779 215 VAL H H 8.46 0.02 1 780 215 VAL CA C 58.79 0.1 1 781 215 VAL CB C 35.46 0.1 1 782 215 VAL C C 173.99 0.1 1 783 216 ILE N N 120.00 0.2 1 784 216 ILE H H 9.07 0.02 1 785 216 ILE CA C 60.37 0.1 1 786 216 ILE CB C 39.25 0.1 1 787 216 ILE C C 174.57 0.1 1 788 217 ILE N N 128.21 0.2 1 789 217 ILE H H 9.11 0.02 1 790 217 ILE CA C 60.40 0.1 1 791 217 ILE CB C 38.92 0.1 1 792 217 ILE C C 177.70 0.1 1 793 218 VAL N N 116.60 0.2 1 794 218 VAL H H 8.73 0.02 1 795 218 VAL CA C 60.24 0.1 1 796 218 VAL CB C 32.46 0.1 1 797 218 VAL C C 174.96 0.1 1 798 219 ARG N N 120.01 0.2 1 799 219 ARG H H 7.17 0.02 1 800 219 ARG CA C 56.46 0.1 1 801 219 ARG CB C 32.22 0.1 1 802 219 ARG C C 172.91 0.1 1 803 220 VAL N N 123.89 0.2 1 804 220 VAL H H 7.30 0.02 1 805 220 VAL CA C 61.69 0.1 1 806 220 VAL CB C 34.69 0.1 1 807 220 VAL C C 173.97 0.1 1 808 221 GLU N N 118.05 0.2 1 809 221 GLU H H 8.66 0.02 1 810 221 GLU CA C 53.61 0.1 1 811 221 GLU CB C 34.84 0.1 1 812 221 GLU C C 175.39 0.1 1 813 222 ILE N N 120.64 0.2 1 814 222 ILE H H 8.20 0.02 1 815 222 ILE CA C 59.71 0.1 1 816 222 ILE CB C 38.54 0.1 1 817 222 ILE C C 177.33 0.1 1 818 223 ASN N N 130.34 0.2 1 819 223 ASN H H 9.35 0.02 1 820 223 ASN CA C 53.73 0.1 1 822 223 ASN C C 175.40 0.1 1 823 224 GLY N N 103.01 0.2 1 824 224 GLY H H 8.58 0.02 1 825 224 GLY CA C 45.71 0.1 1 828 225 GLN H H 7.55 0.02 1 831 226 ASP C C 177.10 0.1 1 832 227 LEU N N 128.66 0.2 1 833 227 LEU H H 8.45 0.02 1 834 227 LEU CA C 57.18 0.1 1 835 227 LEU CB C 41.75 0.1 1 836 227 LEU C C 178.16 0.1 1 837 228 LYS N N 113.75 0.2 1 838 228 LYS H H 9.13 0.02 1 839 228 LYS CA C 57.29 0.1 1 840 228 LYS CB C 29.20 0.1 1 841 228 LYS C C 175.58 0.1 1 842 229 MET N N 116.08 0.2 1 843 229 MET H H 6.78 0.02 1 844 229 MET CA C 54.56 0.1 1 845 229 MET CB C 33.34 0.1 1 846 229 MET C C 175.16 0.1 1 847 230 ASP N N 122.30 0.2 1 848 230 ASP H H 8.24 0.02 1 849 230 ASP CA C 54.66 0.1 1 850 230 ASP CB C 41.79 0.1 1 851 230 ASP C C 178.64 0.1 1 852 231 CYS N N 123.65 0.2 1 853 231 CYS H H 8.71 0.02 1 854 231 CYS CA C 59.40 0.1 1 855 231 CYS CB C 42.29 0.1 1 856 231 CYS C C 176.44 0.1 1 857 232 LYS N N 122.81 0.2 1 858 232 LYS H H 8.33 0.02 1 859 232 LYS CA C 59.23 0.1 1 860 232 LYS CB C 32.57 0.1 1 861 232 LYS C C 180.83 0.1 1 862 233 GLU N N 114.43 0.2 1 863 233 GLU H H 7.99 0.02 1 864 233 GLU CA C 57.59 0.1 1 865 233 GLU CB C 27.72 0.1 1 866 233 GLU C C 179.86 0.1 1 867 234 TYR N N 113.76 0.2 1 868 234 TYR H H 6.64 0.02 1 869 234 TYR CA C 57.56 0.1 1 870 234 TYR CB C 36.95 0.1 1 871 234 TYR C C 174.30 0.1 1 872 235 ASN N N 111.78 0.2 1 873 235 ASN H H 6.92 0.02 1 874 235 ASN CA C 50.70 0.1 1 875 235 ASN CB C 41.34 0.1 1 876 235 ASN C C 173.28 0.1 1 877 236 TYR N N 119.43 0.2 1 878 236 TYR H H 6.45 0.02 1 879 236 TYR CA C 50.82 0.1 1 880 236 TYR CB C 38.13 0.1 1 881 236 TYR C C 175.87 0.1 1 882 237 ASP N N 123.54 0.2 1 883 237 ASP H H 7.23 0.02 1 884 237 ASP CA C 56.99 0.1 1 885 237 ASP CB C 40.17 0.1 1 886 237 ASP C C 173.85 0.1 1 887 238 LYS N N 115.52 0.2 1 888 238 LYS H H 7.05 0.02 1 889 238 LYS CA C 55.59 0.1 1 890 238 LYS CB C 34.21 0.1 1 891 238 LYS C C 174.52 0.1 1 892 239 SER N N 118.03 0.2 1 893 239 SER H H 8.46 0.02 1 894 239 SER CA C 58.74 0.1 1 895 239 SER CB C 64.10 0.1 1 896 239 SER C C 174.51 0.1 1 897 240 ILE N N 113.86 0.2 1 898 240 ILE H H 8.01 0.02 1 901 240 ILE C C 174.52 0.1 1 902 241 VAL N N 110.33 0.2 1 905 242 ASP H H 8.29 0.02 1 908 243 SER C C 175.18 0.1 1 909 244 GLY N N 114.09 0.2 1 910 244 GLY H H 9.13 0.02 1 911 244 GLY CA C 45.53 0.1 1 914 245 THR H H 7.11 0.02 1 917 246 THR C C 173.61 0.1 1 918 247 ASN N N 118.91 0.2 1 919 247 ASN H H 7.39 0.02 1 920 247 ASN CA C 53.79 0.1 1 921 247 ASN CB C 37.88 0.1 1 922 247 ASN C C 176.29 0.1 1 923 248 LEU N N 116.59 0.2 1 924 248 LEU H H 7.32 0.02 1 925 248 LEU CA C 54.12 0.1 1 926 248 LEU CB C 42.33 0.1 1 927 248 LEU C C 174.68 0.1 1 928 249 ARG N N 125.83 0.2 1 929 249 ARG H H 8.81 0.02 1 930 249 ARG CA C 53.39 0.1 1 931 249 ARG CB C 30.75 0.1 1 934 250 LEU H H 8.72 0.02 1 937 251 PRO C C 177.40 0.1 1 938 252 LYS N N 125.01 0.2 1 939 252 LYS H H 8.46 0.02 1 940 252 LYS CA C 62.45 0.1 1 941 252 LYS CB C 33.54 0.1 1 942 252 LYS C C 177.03 0.1 1 943 253 LYS N N 117.16 0.2 1 944 253 LYS H H 9.37 0.02 1 945 253 LYS CA C 60.32 0.1 1 946 253 LYS CB C 33.09 0.1 1 947 253 LYS C C 179.83 0.1 1 948 254 VAL N N 119.16 0.2 1 949 254 VAL H H 7.29 0.02 1 950 254 VAL CA C 64.64 0.1 1 951 254 VAL CB C 31.02 0.1 1 952 254 VAL C C 177.03 0.1 1 953 255 PHE N N 120.86 0.2 1 954 255 PHE H H 9.15 0.02 1 955 255 PHE CA C 62.51 0.1 1 956 255 PHE CB C 38.42 0.1 1 957 255 PHE C C 176.29 0.1 1 958 256 GLU N N 116.27 0.2 1 959 256 GLU H H 8.35 0.02 1 960 256 GLU CA C 59.59 0.1 1 961 256 GLU CB C 29.19 0.1 1 962 256 GLU C C 179.29 0.1 1 963 257 ALA N N 121.37 0.2 1 964 257 ALA H H 7.08 0.02 1 965 257 ALA CA C 55.12 0.1 1 966 257 ALA CB C 19.22 0.1 1 967 257 ALA C C 180.14 0.1 1 968 258 ALA N N 122.00 0.2 1 969 258 ALA H H 8.99 0.02 1 970 258 ALA CA C 55.19 0.1 1 971 258 ALA CB C 16.49 0.1 1 972 258 ALA C C 179.26 0.1 1 973 259 VAL N N 117.99 0.2 1 974 259 VAL H H 8.51 0.02 1 975 259 VAL CA C 67.03 0.1 1 976 259 VAL CB C 30.59 0.1 1 977 259 VAL C C 177.28 0.1 1 978 260 LYS N N 119.46 0.2 1 979 260 LYS H H 7.24 0.02 1 980 260 LYS CA C 60.44 0.1 1 981 260 LYS CB C 31.95 0.1 1 984 261 SER H H 7.35 0.02 1 987 262 ILE C C 178.92 0.1 1 988 263 LYS N N 122.29 0.2 1 989 263 LYS H H 8.50 0.02 1 990 263 LYS CA C 59.65 0.1 1 991 263 LYS CB C 32.60 0.1 1 992 263 LYS C C 178.93 0.1 1 993 264 ALA N N 119.85 0.2 1 994 264 ALA H H 7.37 0.02 1 995 264 ALA CA C 55.01 0.1 1 996 264 ALA CB C 17.89 0.1 1 997 264 ALA C C 180.51 0.1 1 998 265 ALA N N 119.72 0.2 1 999 265 ALA H H 7.72 0.02 1 1000 265 ALA CA C 54.30 0.1 1 1001 265 ALA CB C 18.22 0.1 1 1002 265 ALA C C 178.01 0.1 1 1003 266 SER N N 110.82 0.2 1 1004 266 SER H H 7.57 0.02 1 1005 266 SER CA C 58.05 0.1 1 1006 266 SER CB C 64.75 0.1 1 1007 266 SER C C 175.45 0.1 1 1008 267 SER N N 114.52 0.2 1 1009 267 SER H H 7.10 0.02 1 1010 267 SER CA C 61.18 0.1 1 1011 267 SER CB C 63.73 0.1 1 1012 267 SER C C 175.19 0.1 1 1013 268 THR N N 114.27 0.2 1 1014 268 THR H H 7.63 0.02 1 1015 268 THR CA C 63.88 0.1 1 1016 268 THR CB C 68.73 0.1 1 1019 269 GLU H H 8.13 0.02 1 1022 274 GLY C C 177.37 0.1 1 1023 275 PHE N N 123.95 0.2 1 1024 275 PHE H H 8.21 0.02 1 1025 275 PHE CA C 60.21 0.1 1 1026 275 PHE CB C 38.54 0.1 1 1027 275 PHE C C 178.31 0.1 1 1028 276 TRP N N 119.42 0.2 1 1029 276 TRP H H 6.79 0.02 1 1030 276 TRP CA C 56.99 0.1 1 1031 276 TRP CB C 28.48 0.1 1 1032 276 TRP C C 176.05 0.1 1 1033 277 LEU N N 114.72 0.2 1 1034 277 LEU H H 7.06 0.02 1 1035 277 LEU CA C 54.49 0.1 1 1037 277 LEU C C 177.70 0.1 1 1038 278 GLY N N 107.82 0.2 1 1039 278 GLY H H 7.91 0.02 1 1040 278 GLY CA C 46.69 0.1 1 1041 278 GLY C C 175.01 0.1 1 1042 279 GLU N N 116.05 0.2 1 1043 279 GLU H H 7.72 0.02 1 1044 279 GLU CA C 56.77 0.1 1 1045 279 GLU CB C 31.47 0.1 1 1046 279 GLU C C 175.89 0.1 1 1047 280 GLN N N 116.03 0.2 1 1048 280 GLN H H 6.88 0.02 1 1049 280 GLN CA C 54.09 0.1 1 1050 280 GLN CB C 32.61 0.1 1 1051 280 GLN C C 174.25 0.1 1 1052 281 LEU N N 122.89 0.2 1 1053 281 LEU H H 8.44 0.02 1 1054 281 LEU CA C 54.14 0.1 1 1055 281 LEU CB C 43.26 0.1 1 1056 281 LEU C C 177.04 0.1 1 1057 282 VAL N N 118.16 0.2 1 1058 282 VAL H H 8.28 0.02 1 1059 282 VAL CA C 60.82 0.1 1 1060 282 VAL CB C 33.82 0.1 1 1061 282 VAL C C 173.55 0.1 1 1062 283 CYS N N 121.97 0.2 1 1063 283 CYS H H 7.70 0.02 1 1064 283 CYS CA C 55.09 0.1 1 1065 283 CYS CB C 49.81 0.1 1 1066 283 CYS C C 173.15 0.1 1 1067 284 TRP N N 122.53 0.2 1 1068 284 TRP H H 9.07 0.02 1 1069 284 TRP CA C 59.11 0.1 1 1070 284 TRP CB C 32.68 0.1 1 1071 284 TRP C C 174.82 0.1 1 1072 285 GLN N N 121.07 0.2 1 1073 285 GLN H H 8.46 0.02 1 1074 285 GLN CA C 57.25 0.1 1 1075 285 GLN CB C 28.33 0.1 1 1076 285 GLN C C 177.42 0.1 1 1077 286 ALA N N 128.73 0.2 1 1078 286 ALA H H 8.93 0.02 1 1079 286 ALA CA C 54.36 0.1 1 1081 286 ALA C C 178.73 0.1 1 1082 287 GLY N N 110.78 0.2 1 1083 287 GLY H H 8.80 0.02 1 1084 287 GLY CA C 46.19 0.1 1 1085 287 GLY C C 176.65 0.1 1 1086 288 THR N N 109.82 0.2 1 1087 288 THR H H 8.25 0.02 1 1088 288 THR CA C 61.93 0.1 1 1089 288 THR CB C 70.15 0.1 1 1092 289 THR H H 7.48 0.02 1 1095 290 PRO C C 175.13 0.1 1 1096 291 TRP N N 122.36 0.2 1 1097 291 TRP H H 7.35 0.02 1 1098 291 TRP CA C 60.38 0.1 1 1099 291 TRP C C 177.70 0.1 1 1100 292 ASN N N 108.96 0.2 1 1101 292 ASN H H 8.14 0.02 1 1102 292 ASN CA C 55.60 0.1 1 1103 292 ASN CB C 37.74 0.1 1 1104 292 ASN C C 176.72 0.1 1 1105 293 ILE N N 115.10 0.2 1 1106 293 ILE H H 7.53 0.02 1 1107 293 ILE CA C 62.51 0.1 1 1108 293 ILE CB C 37.37 0.1 1 1111 294 PHE H H 7.54 0.02 1 1114 295 PRO C C 178.31 0.1 1 1115 296 VAL N N 112.42 0.2 1 1116 296 VAL H H 8.13 0.02 1 1117 296 VAL CA C 61.12 0.1 1 1118 296 VAL CB C 31.41 0.1 1 1119 296 VAL C C 176.12 0.1 1 1120 297 ILE N N 121.36 0.2 1 1121 297 ILE H H 8.26 0.02 1 1122 297 ILE CA C 60.74 0.1 1 1123 297 ILE CB C 40.25 0.1 1 1124 297 ILE C C 174.80 0.1 1 1125 298 SER N N 121.26 0.2 1 1126 298 SER H H 9.16 0.02 1 1127 298 SER CA C 57.04 0.1 1 1128 298 SER CB C 64.77 0.1 1 1129 298 SER C C 172.61 0.1 1 1130 299 LEU N N 123.83 0.2 1 1131 299 LEU H H 8.78 0.02 1 1132 299 LEU CA C 53.75 0.1 1 1133 299 LEU CB C 42.35 0.1 1 1134 299 LEU C C 174.62 0.1 1 1135 300 TYR N N 122.13 0.2 1 1136 300 TYR H H 8.69 0.02 1 1137 300 TYR CA C 55.54 0.1 1 1138 300 TYR CB C 38.88 0.1 1 1139 300 TYR C C 175.18 0.1 1 1140 301 LEU N N 125.08 0.2 1 1141 301 LEU H H 8.33 0.02 1 1142 301 LEU CA C 52.57 0.1 1 1143 301 LEU CB C 42.74 0.1 1 1144 301 LEU C C 175.22 0.1 1 1145 302 MET N N 117.92 0.2 1 1146 302 MET H H 7.28 0.02 1 1147 302 MET CA C 57.30 0.1 1 1149 302 MET C C 176.22 0.1 1 1150 303 GLY N N 114.85 0.2 1 1151 303 GLY H H 8.52 0.02 1 1152 303 GLY CA C 44.57 0.1 1 1153 303 GLY C C 174.34 0.1 1 1154 304 GLU N N 115.91 0.2 1 1155 304 GLU H H 8.39 0.02 1 1156 304 GLU CA C 58.75 0.1 1 1157 304 GLU CB C 31.56 0.1 1 1158 304 GLU C C 176.99 0.1 1 1159 305 VAL N N 120.20 0.2 1 1160 305 VAL H H 7.94 0.02 1 1161 305 VAL CA C 61.20 0.1 1 1162 305 VAL CB C 32.95 0.1 1 1163 305 VAL C C 175.80 0.1 1 1164 306 THR N N 122.08 0.2 1 1165 306 THR H H 8.08 0.02 1 1166 306 THR CA C 64.57 0.1 1 1167 306 THR CB C 69.16 0.1 1 1168 306 THR C C 174.51 0.1 1 1169 307 ASN N N 118.33 0.2 1 1170 307 ASN H H 8.70 0.02 1 1171 307 ASN CA C 55.05 0.1 1 1172 307 ASN CB C 36.66 0.1 1 1173 307 ASN C C 174.25 0.1 1 1174 308 GLN N N 118.73 0.2 1 1175 308 GLN H H 7.92 0.02 1 1176 308 GLN CA C 55.42 0.1 1 1177 308 GLN CB C 31.35 0.1 1 1178 308 GLN C C 174.27 0.1 1 1179 309 SER N N 116.88 0.2 1 1180 309 SER H H 9.04 0.02 1 1181 309 SER CA C 57.00 0.1 1 1182 309 SER CB C 68.54 0.1 1 1183 309 SER C C 173.64 0.1 1 1184 310 PHE N N 115.20 0.2 1 1185 310 PHE H H 8.12 0.02 1 1186 310 PHE CA C 56.07 0.1 1 1187 310 PHE CB C 40.73 0.1 1 1188 310 PHE C C 171.37 0.1 1 1189 311 ARG N N 117.95 0.2 1 1190 311 ARG H H 9.30 0.02 1 1191 311 ARG CA C 53.08 0.1 1 1192 311 ARG CB C 32.76 0.1 1 1193 311 ARG C C 174.26 0.1 1 1194 312 ILE N N 118.41 0.2 1 1195 312 ILE H H 8.38 0.02 1 1196 312 ILE CA C 58.70 0.1 1 1197 312 ILE CB C 37.87 0.1 1 1198 312 ILE C C 174.85 0.1 1 1199 313 THR N N 121.50 0.2 1 1200 313 THR H H 8.99 0.02 1 1201 313 THR CA C 61.70 0.1 1 1202 313 THR CB C 71.36 0.1 1 1203 313 THR C C 173.86 0.1 1 1204 314 ILE N N 118.56 0.2 1 1205 314 ILE H H 9.01 0.02 1 1206 314 ILE CA C 59.62 0.1 1 1207 314 ILE CB C 40.68 0.1 1 1210 315 LEU H H 8.01 0.02 1 1213 317 GLN C C 177.57 0.1 1 1214 318 GLN N N 115.18 0.2 1 1215 318 GLN H H 7.70 0.02 1 1216 318 GLN CA C 59.53 0.1 1 1217 318 GLN CB C 29.58 0.1 1 1218 318 GLN C C 176.04 0.1 1 1219 319 TYR N N 111.21 0.2 1 1220 319 TYR H H 6.80 0.02 1 1221 319 TYR CA C 58.29 0.1 1 1222 319 TYR CB C 37.69 0.1 1 1223 319 TYR C C 172.60 0.1 1 1224 320 LEU N N 125.69 0.2 1 1225 320 LEU H H 8.12 0.02 1 1226 320 LEU CA C 54.19 0.1 1 1227 320 LEU CB C 40.42 0.1 1 1230 321 ARG H H 8.98 0.02 1 1233 322 PRO C C 177.10 0.1 1 1234 323 VAL N N 121.22 0.2 1 1235 323 VAL H H 7.86 0.02 1 1236 323 VAL CA C 61.03 0.1 1 1237 323 VAL CB C 34.19 0.1 1 1238 323 VAL C C 175.23 0.1 1 1239 324 GLU N N 124.95 0.2 1 1240 324 GLU H H 8.45 0.02 1 1241 324 GLU CA C 56.58 0.1 1 1242 324 GLU CB C 29.85 0.1 1 1243 324 GLU C C 175.84 0.1 1 1244 325 ASP N N 122.21 0.2 1 1245 325 ASP H H 8.34 0.02 1 1246 325 ASP CA C 54.06 0.1 1 1247 325 ASP CB C 41.80 0.1 1 1248 325 ASP C C 176.34 0.1 1 1249 326 VAL N N 119.47 0.2 1 1250 326 VAL H H 7.96 0.02 1 1251 326 VAL CA C 62.64 0.1 1 1252 326 VAL CB C 32.17 0.1 1 1253 326 VAL C C 176.59 0.1 1 1254 327 ALA N N 124.73 0.2 1 1255 327 ALA H H 8.22 0.02 1 1256 327 ALA CA C 53.42 0.1 1 1257 327 ALA CB C 19.45 0.1 1 1258 327 ALA C C 178.27 0.1 1 1259 328 THR N N 110.68 0.2 1 1260 328 THR H H 7.76 0.02 1 1261 328 THR CA C 61.45 0.1 1 1262 328 THR CB C 69.36 0.1 1 1265 329 SER H H 8.01 0.02 1 1268 330 GLN C C 175.39 0.1 1 1269 331 ASP N N 120.54 0.2 1 1270 331 ASP H H 7.89 0.02 1 1271 331 ASP CA C 54.23 0.1 1 1272 331 ASP CB C 43.36 0.1 1 1273 331 ASP C C 174.83 0.1 1 1274 332 ASP N N 121.40 0.2 1 1275 332 ASP H H 8.84 0.02 1 1276 332 ASP CA C 54.30 0.1 1 1277 332 ASP CB C 42.46 0.1 1 1278 332 ASP C C 174.50 0.1 1 1279 333 CYS N N 121.01 0.2 1 1280 333 CYS H H 8.21 0.02 1 1281 333 CYS CA C 55.00 0.1 1 1282 333 CYS CB C 48.34 0.1 1 1283 333 CYS C C 173.97 0.1 1 1284 334 TYR N N 117.92 0.2 1 1285 334 TYR H H 9.06 0.02 1 1286 334 TYR CA C 57.53 0.1 1 1287 334 TYR CB C 44.17 0.1 1 1288 334 TYR C C 174.53 0.1 1 1289 335 LYS N N 118.58 0.2 1 1290 335 LYS H H 8.95 0.02 1 1291 335 LYS CA C 54.22 0.1 1 1292 335 LYS CB C 36.35 0.1 1 1293 335 LYS C C 175.24 0.1 1 1294 336 PHE N N 126.31 0.2 1 1295 336 PHE H H 8.88 0.02 1 1296 336 PHE CA C 57.84 0.1 1 1297 336 PHE CB C 39.57 0.1 1 1298 336 PHE C C 175.81 0.1 1 1299 337 ALA N N 132.53 0.2 1 1300 337 ALA H H 8.71 0.02 1 1301 337 ALA CA C 52.07 0.1 1 1302 337 ALA CB C 19.58 0.1 1 1303 337 ALA C C 174.12 0.1 1 1304 338 ILE N N 116.02 0.2 1 1305 338 ILE H H 5.50 0.02 1 1306 338 ILE CA C 59.30 0.1 1 1307 338 ILE CB C 37.88 0.1 1 1308 338 ILE C C 175.18 0.1 1 1309 339 SER N N 119.11 0.2 1 1310 339 SER H H 8.77 0.02 1 1311 339 SER CA C 57.30 0.1 1 1312 339 SER CB C 65.91 0.1 1 1313 339 SER C C 172.32 0.1 1 1314 340 GLN N N 119.75 0.2 1 1315 340 GLN H H 7.76 0.02 1 1316 340 GLN CA C 55.68 0.1 1 1317 340 GLN CB C 30.25 0.1 1 1320 341 SER H H 8.15 0.02 1 1323 342 SER C C 175.16 0.1 1 1324 343 THR N N 114.89 0.2 1 1325 343 THR H H 8.46 0.02 1 1326 343 THR CA C 60.30 0.1 1 1328 343 THR C C 174.58 0.1 1 1329 344 GLY N N 110.90 0.2 1 1330 344 GLY H H 8.08 0.02 1 1331 344 GLY CA C 43.75 0.1 1 1332 344 GLY C C 174.58 0.1 1 1333 345 THR N N 119.08 0.2 1 1334 345 THR H H 8.60 0.02 1 1335 345 THR CA C 63.53 0.1 1 1336 345 THR CB C 67.52 0.1 1 1337 345 THR C C 176.55 0.1 1 1338 346 VAL N N 128.87 0.2 1 1339 346 VAL H H 9.44 0.02 1 1340 346 VAL CA C 61.87 0.1 1 1341 346 VAL CB C 33.65 0.1 1 1342 346 VAL C C 175.61 0.1 1 1343 347 MET N N 126.89 0.2 1 1344 347 MET H H 9.11 0.02 1 1345 347 MET CA C 55.52 0.1 1 1347 347 MET C C 174.40 0.1 1 1348 348 GLY N N 110.17 0.2 1 1349 348 GLY H H 6.58 0.02 1 1350 348 GLY CA C 44.00 0.1 1 1353 349 ALA H H 9.39 0.02 1 1356 353 GLU C C 177.93 0.1 1 1357 354 GLY N N 104.71 0.2 1 1358 354 GLY H H 7.79 0.02 1 1359 354 GLY CA C 44.56 0.1 1 1360 354 GLY C C 172.65 0.1 1 1361 355 PHE N N 113.48 0.2 1 1362 355 PHE H H 7.46 0.02 1 1363 355 PHE CA C 58.01 0.1 1 1364 355 PHE CB C 43.19 0.1 1 1365 355 PHE C C 174.79 0.1 1 1366 356 TYR N N 125.36 0.2 1 1367 356 TYR H H 9.45 0.02 1 1368 356 TYR CA C 55.54 0.1 1 1369 356 TYR CB C 42.95 0.1 1 1370 356 TYR C C 173.90 0.1 1 1371 357 VAL N N 125.99 0.2 1 1372 357 VAL H H 7.83 0.02 1 1373 357 VAL CA C 60.02 0.1 1 1374 357 VAL CB C 32.77 0.1 1 1375 357 VAL C C 174.75 0.1 1 1376 358 VAL N N 127.06 0.2 1 1377 358 VAL H H 8.79 0.02 1 1378 358 VAL CA C 60.83 0.1 1 1379 358 VAL CB C 33.64 0.1 1 1380 358 VAL C C 173.92 0.1 1 1381 359 PHE N N 128.91 0.2 1 1382 359 PHE H H 8.93 0.02 1 1383 359 PHE CA C 56.61 0.1 1 1384 359 PHE CB C 36.25 0.1 1 1385 359 PHE C C 173.69 0.1 1 1386 360 ASP N N 124.62 0.2 1 1387 360 ASP H H 7.97 0.02 1 1388 360 ASP CA C 51.98 0.1 1 1389 360 ASP CB C 40.09 0.1 1 1390 360 ASP C C 176.19 0.1 1 1391 361 ARG N N 124.29 0.2 1 1392 361 ARG H H 7.27 0.02 1 1393 361 ARG CA C 58.95 0.1 1 1394 361 ARG CB C 29.64 0.1 1 1395 361 ARG C C 180.37 0.1 1 1396 362 ALA N N 123.38 0.2 1 1397 362 ALA H H 8.20 0.02 1 1398 362 ALA CA C 55.08 0.1 1 1399 362 ALA CB C 19.48 0.1 1 1400 362 ALA C C 179.05 0.1 1 1401 363 ARG N N 114.83 0.2 1 1402 363 ARG H H 7.19 0.02 1 1403 363 ARG CA C 54.99 0.1 1 1405 363 ARG C C 174.60 0.1 1 1406 364 LYS N N 120.63 0.2 1 1407 364 LYS H H 7.72 0.02 1 1408 364 LYS CA C 62.87 0.1 1 1409 364 LYS C C 175.40 0.1 1 1410 365 ARG N N 116.90 0.2 1 1411 365 ARG H H 8.53 0.02 1 1412 365 ARG CA C 55.54 0.1 1 1413 365 ARG CB C 32.39 0.1 1 1414 365 ARG C C 172.64 0.1 1 1415 366 ILE N N 120.47 0.2 1 1416 366 ILE H H 9.35 0.02 1 1417 366 ILE CA C 58.40 0.1 1 1419 366 ILE C C 175.53 0.1 1 1420 367 GLY N N 115.63 0.2 1 1421 367 GLY H H 9.53 0.02 1 1422 367 GLY CA C 44.21 0.1 1 1423 367 GLY C C 171.15 0.1 1 1424 368 PHE N N 119.14 0.2 1 1425 368 PHE H H 8.85 0.02 1 1426 368 PHE CA C 57.40 0.1 1 1427 368 PHE C C 174.52 0.1 1 1428 369 ALA N N 120.06 0.2 1 1429 369 ALA H H 8.26 0.02 1 1430 369 ALA CA C 51.27 0.1 1 1431 369 ALA CB C 25.50 0.1 1 1432 369 ALA C C 176.74 0.1 1 1433 370 VAL N N 123.91 0.2 1 1434 370 VAL H H 9.12 0.02 1 1435 370 VAL CA C 65.83 0.1 1 1436 370 VAL CB C 31.08 0.1 1 1438 371 SER N N 119.08 0.2 1 1439 371 SER H H 7.93 0.02 1 1442 372 ALA N N 130.39 0.2 1 1444 378 GLU C C 176.08 0.1 1 1445 379 PHE N N 117.87 0.2 1 1446 379 PHE H H 8.84 0.02 1 1447 379 PHE CA C 58.71 0.1 1 1448 379 PHE CB C 40.63 0.1 1 1449 379 PHE C C 176.13 0.1 1 1450 380 ARG N N 119.45 0.2 1 1451 380 ARG H H 8.49 0.02 1 1452 380 ARG CA C 55.93 0.1 1 1453 380 ARG CB C 34.37 0.1 1 1454 380 ARG C C 173.44 0.1 1 1455 381 THR N N 109.20 0.2 1 1456 381 THR H H 7.56 0.02 1 1457 381 THR CA C 60.17 0.1 1 1459 381 THR C C 173.95 0.1 1 1460 382 ALA N N 127.47 0.2 1 1461 382 ALA H H 9.44 0.02 1 1462 382 ALA CA C 53.39 0.1 1 1463 382 ALA C C 176.70 0.1 1 1464 383 ALA N N 118.65 0.2 1 1465 383 ALA H H 7.89 0.02 1 1466 383 ALA CA C 52.39 0.1 1 1467 383 ALA CB C 23.58 0.1 1 1468 383 ALA C C 175.48 0.1 1 1469 384 VAL N N 120.85 0.2 1 1470 384 VAL H H 8.03 0.02 1 1471 384 VAL CA C 62.60 0.1 1 1472 384 VAL CB C 33.12 0.1 1 1473 384 VAL C C 175.81 0.1 1 1474 385 GLU N N 123.36 0.2 1 1475 385 GLU H H 8.65 0.02 1 1476 385 GLU CA C 54.88 0.1 1 1480 386 GLY H H 7.73 0.02 1 1482 389 VAL C C 177.28 0.1 1 1483 390 THR N N 126.47 0.2 1 1484 390 THR H H 8.14 0.02 1 1485 390 THR CA C 61.86 0.1 1 1486 390 THR CB C 71.99 0.1 1 1487 390 THR C C 172.02 0.1 1 1488 391 LEU N N 124.19 0.2 1 1489 391 LEU H H 8.26 0.02 1 1490 391 LEU CA C 54.52 0.1 1 1491 391 LEU CB C 42.31 0.1 1 1492 391 LEU C C 177.28 0.1 1 1493 392 ASP N N 117.37 0.2 1 1494 392 ASP H H 8.63 0.02 1 1495 392 ASP CA C 55.50 0.1 1 1496 392 ASP CB C 39.42 0.1 1 1497 392 ASP C C 177.34 0.1 1 1498 393 MET N N 118.30 0.2 1 1499 393 MET H H 8.58 0.02 1 1500 393 MET CA C 59.37 0.1 1 1501 393 MET CB C 33.50 0.1 1 1502 393 MET C C 178.32 0.1 1 1503 394 GLU N N 117.61 0.2 1 1504 394 GLU H H 8.91 0.02 1 1505 394 GLU CA C 59.24 0.1 1 1506 394 GLU CB C 28.75 0.1 1 1507 394 GLU C C 178.60 0.1 1 1508 395 ASP N N 119.17 0.2 1 1509 395 ASP H H 7.63 0.02 1 1510 395 ASP CA C 55.45 0.1 1 1511 395 ASP CB C 40.46 0.1 1 1512 395 ASP C C 176.61 0.1 1 1513 396 CYS N N 116.37 0.2 1 1514 396 CYS H H 7.79 0.02 1 1515 396 CYS CA C 56.61 0.1 1 1517 396 CYS C C 175.53 0.1 1 1518 397 GLY N N 105.06 0.2 1 1519 397 GLY H H 7.63 0.02 1 1520 397 GLY CA C 44.87 0.1 1 1521 397 GLY C C 172.59 0.1 1 1522 398 TYR N N 125.67 0.2 1 1523 398 TYR H H 9.48 0.02 1 1524 398 TYR CA C 58.87 0.1 1 1525 398 TYR CB C 39.67 0.1 1 1526 398 TYR C C 175.83 0.1 1 1527 399 ASN N N 126.78 0.2 1 1528 399 ASN H H 7.62 0.02 1 1529 399 ASN CA C 52.28 0.1 1 1530 399 ASN CB C 40.83 0.1 1 1533 400 ILE H H 8.12 0.02 1 1536 401 PRO C C 176.81 0.1 1 1537 402 GLN N N 121.79 0.2 1 1538 402 GLN H H 8.41 0.02 1 1539 402 GLN CA C 55.80 0.1 1 1540 402 GLN CB C 29.23 0.1 1 1541 402 GLN C C 176.29 0.1 1 1542 403 THR N N 115.87 0.2 1 1543 403 THR H H 8.13 0.02 1 1544 403 THR CA C 61.67 0.1 1 1545 403 THR CB C 69.90 0.1 1 1546 403 THR C C 174.21 0.1 1 1547 404 ASP N N 122.99 0.2 1 1548 404 ASP H H 8.33 0.02 1 1549 404 ASP CA C 54.29 0.1 1 1550 404 ASP CB C 41.20 0.1 1 1551 404 ASP C C 176.28 0.1 1 1552 405 GLU N N 121.77 0.2 1 1553 405 GLU H H 8.30 0.02 1 1554 405 GLU CA C 56.71 0.1 1 1555 405 GLU CB C 30.13 0.1 1 1558 406 SER H H 8.32 0.02 1 stop_ save_