data_16279 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the yeast Hsp90 Middle Domain ; _BMRB_accession_number 16279 _BMRB_flat_file_name bmr16279.str _Entry_type original _Submission_date 2009-05-07 _Accession_date 2009-05-07 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NMR backbone resonance assignment of yeast Hsp90 middle domain' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hagn Franz . . 2 Retzlaff Marco . . 3 Rohrberg Julia . . 4 Buchner Johannes . . 5 Kessler Horst . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 201 "13C chemical shifts" 671 "15N chemical shifts" 201 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-16 update BMRB 'update entry citation' 2011-08-31 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21892170 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hagn Franz . . 2 Lagleder Stephan . . 3 Retzlaff Marco . . 4 Rohrberg Julia . . 5 Demmer Oliver . . 6 Richter Klaus . . 7 Buchner Johannes . . 8 Kessler Horst . . stop_ _Journal_abbreviation 'Nat. Struct. Mol. Biol.' _Journal_name_full 'Nature structural & molecular biology' _Journal_volume 18 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1086 _Page_last 1093 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Hsp90 middle domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Hsp90 middle domain' $Hsp90M stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Hsp90M _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Hsp90M _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function ; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures. ; stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 260 _Mol_residue_sequence ; GSHMKTKPLWTRNPSDITQE EYNAFYKSISNDWEDPLYVK HFSVEGQLEFRAILFIPKRA PFDLFESKKKKNNIKLYVRR VFITDEAEDLIPEWLSFVKG VVDSEDLPLNLSREMLQQNK IMKVIRKNIVKKLIEAFNEI AEDSEQFEKFYSAFSKNIKL GVHEDTQNRAALAKLLRYNS TKSVDELTSLTDYVTRMPEH QKNIYYITGESLKAVEKSPF LDALKAKNFEVLFLTDPIDE YAFTQLKEFEGKTLVDITKD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 268 GLY 2 269 SER 3 270 HIS 4 271 MET 5 272 LYS 6 273 THR 7 274 LYS 8 275 PRO 9 276 LEU 10 277 TRP 11 278 THR 12 279 ARG 13 280 ASN 14 281 PRO 15 282 SER 16 283 ASP 17 284 ILE 18 285 THR 19 286 GLN 20 287 GLU 21 288 GLU 22 289 TYR 23 290 ASN 24 291 ALA 25 292 PHE 26 293 TYR 27 294 LYS 28 295 SER 29 296 ILE 30 297 SER 31 298 ASN 32 299 ASP 33 300 TRP 34 301 GLU 35 302 ASP 36 303 PRO 37 304 LEU 38 305 TYR 39 306 VAL 40 307 LYS 41 308 HIS 42 309 PHE 43 310 SER 44 311 VAL 45 312 GLU 46 313 GLY 47 314 GLN 48 315 LEU 49 316 GLU 50 317 PHE 51 318 ARG 52 319 ALA 53 320 ILE 54 321 LEU 55 322 PHE 56 323 ILE 57 324 PRO 58 325 LYS 59 326 ARG 60 327 ALA 61 328 PRO 62 329 PHE 63 330 ASP 64 331 LEU 65 332 PHE 66 333 GLU 67 334 SER 68 335 LYS 69 336 LYS 70 337 LYS 71 338 LYS 72 339 ASN 73 340 ASN 74 341 ILE 75 342 LYS 76 343 LEU 77 344 TYR 78 345 VAL 79 346 ARG 80 347 ARG 81 348 VAL 82 349 PHE 83 350 ILE 84 351 THR 85 352 ASP 86 353 GLU 87 354 ALA 88 355 GLU 89 356 ASP 90 357 LEU 91 358 ILE 92 359 PRO 93 360 GLU 94 361 TRP 95 362 LEU 96 363 SER 97 364 PHE 98 365 VAL 99 366 LYS 100 367 GLY 101 368 VAL 102 369 VAL 103 370 ASP 104 371 SER 105 372 GLU 106 373 ASP 107 374 LEU 108 375 PRO 109 376 LEU 110 377 ASN 111 378 LEU 112 379 SER 113 380 ARG 114 381 GLU 115 382 MET 116 383 LEU 117 384 GLN 118 385 GLN 119 386 ASN 120 387 LYS 121 388 ILE 122 389 MET 123 390 LYS 124 391 VAL 125 392 ILE 126 393 ARG 127 394 LYS 128 395 ASN 129 396 ILE 130 397 VAL 131 398 LYS 132 399 LYS 133 400 LEU 134 401 ILE 135 402 GLU 136 403 ALA 137 404 PHE 138 405 ASN 139 406 GLU 140 407 ILE 141 408 ALA 142 409 GLU 143 410 ASP 144 411 SER 145 412 GLU 146 413 GLN 147 414 PHE 148 415 GLU 149 416 LYS 150 417 PHE 151 418 TYR 152 419 SER 153 420 ALA 154 421 PHE 155 422 SER 156 423 LYS 157 424 ASN 158 425 ILE 159 426 LYS 160 427 LEU 161 428 GLY 162 429 VAL 163 430 HIS 164 431 GLU 165 432 ASP 166 433 THR 167 434 GLN 168 435 ASN 169 436 ARG 170 437 ALA 171 438 ALA 172 439 LEU 173 440 ALA 174 441 LYS 175 442 LEU 176 443 LEU 177 444 ARG 178 445 TYR 179 446 ASN 180 447 SER 181 448 THR 182 449 LYS 183 450 SER 184 451 VAL 185 452 ASP 186 453 GLU 187 454 LEU 188 455 THR 189 456 SER 190 457 LEU 191 458 THR 192 459 ASP 193 460 TYR 194 461 VAL 195 462 THR 196 463 ARG 197 464 MET 198 465 PRO 199 466 GLU 200 467 HIS 201 468 GLN 202 469 LYS 203 470 ASN 204 471 ILE 205 472 TYR 206 473 TYR 207 474 ILE 208 475 THR 209 476 GLY 210 477 GLU 211 478 SER 212 479 LEU 213 480 LYS 214 481 ALA 215 482 VAL 216 483 GLU 217 484 LYS 218 485 SER 219 486 PRO 220 487 PHE 221 488 LEU 222 489 ASP 223 490 ALA 224 491 LEU 225 492 LYS 226 493 ALA 227 494 LYS 228 495 ASN 229 496 PHE 230 497 GLU 231 498 VAL 232 499 LEU 233 500 PHE 234 501 LEU 235 502 THR 236 503 ASP 237 504 PRO 238 505 ILE 239 506 ASP 240 507 GLU 241 508 TYR 242 509 ALA 243 510 PHE 244 511 THR 245 512 GLN 246 513 LEU 247 514 LYS 248 515 GLU 249 516 PHE 250 517 GLU 251 518 GLY 252 519 LYS 253 520 THR 254 521 LEU 255 522 VAL 256 523 ASP 257 524 ILE 258 525 THR 259 526 LYS 260 527 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-16 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 1HK7 "Middle Domain Of Hsp90" 98.08 288 100.00 100.00 0.00e+00 PDB 1USU "The Structure Of The Complex Between Aha1 And Hsp90" 98.08 260 99.61 100.00 0.00e+00 PDB 1USV "The Structure Of The Complex Between Aha1 And Hsp90" 98.46 260 100.00 100.00 0.00e+00 PDB 2CG9 "Crystal Structure Of An Hsp90-Sba1 Closed Chaperone Complex" 98.46 677 100.00 100.00 2.51e-180 PDB 2CGE "Crystal Structure Of An Hsp90-Sba1 Closed Chaperone Complex" 98.08 405 100.00 100.00 0.00e+00 DBJ GAA25634 "K7_Hsc82p [Saccharomyces cerevisiae Kyokai no. 7]" 98.46 705 99.22 100.00 3.76e-179 DBJ GAA26739 "K7_Hsp82p [Saccharomyces cerevisiae Kyokai no. 7]" 98.46 709 99.61 99.61 2.67e-179 EMBL CAA89919 "Hsc82p [Saccharomyces cerevisiae]" 98.46 705 99.22 100.00 3.76e-179 EMBL CAA91604 "HSP90/HSP82? [Saccharomyces cerevisiae]" 98.46 709 100.00 100.00 3.51e-180 EMBL CAA97961 "HSP82 [Saccharomyces cerevisiae]" 98.46 709 100.00 100.00 3.51e-180 EMBL CAY82016 "Hsc82p [Saccharomyces cerevisiae EC1118]" 98.46 705 99.22 100.00 3.72e-179 EMBL CAY86720 "Hsp82p [Saccharomyces cerevisiae EC1118]" 98.46 709 100.00 100.00 3.47e-180 GB AAA02743 "hsp82 protein [Saccharomyces cerevisiae]" 98.46 709 100.00 100.00 3.51e-180 GB AAA02813 "hsc82 protein [Saccharomyces cerevisiae]" 98.46 705 99.22 100.00 4.52e-179 GB AHY76639 "Hsc82p [Saccharomyces cerevisiae YJM993]" 98.46 705 100.00 100.00 4.43e-180 GB AHY77944 "Hsp82p [Saccharomyces cerevisiae YJM993]" 98.46 705 100.00 100.00 5.81e-180 GB AJP40879 "Hsc82p [Saccharomyces cerevisiae YJM1078]" 98.46 705 99.22 100.00 4.19e-179 REF NP_013911 "Hsp90 family chaperone HSC82 [Saccharomyces cerevisiae S288c]" 98.46 705 99.22 100.00 3.76e-179 REF NP_015084 "Hsp90 family chaperone HSP82 [Saccharomyces cerevisiae S288c]" 98.46 709 100.00 100.00 3.51e-180 SP P02829 "RecName: Full=ATP-dependent molecular chaperone HSP82; AltName: Full=82 kDa heat shock protein; AltName: Full=Heat shock protei" 98.46 709 100.00 100.00 3.51e-180 SP P15108 "RecName: Full=ATP-dependent molecular chaperone HSC82; AltName: Full=82 kDa heat shock cognate protein; AltName: Full=Heat shoc" 98.46 705 99.22 100.00 3.76e-179 TPG DAA10084 "TPA: Hsp90 family chaperone HSC82 [Saccharomyces cerevisiae S288c]" 98.46 705 99.22 100.00 3.76e-179 TPG DAA11197 "TPA: Hsp90 family chaperone HSP82 [Saccharomyces cerevisiae S288c]" 98.46 709 100.00 100.00 3.51e-180 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Hsp90M 'baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae 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 _Details $Hsp90M 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pET28a 'cleavable N-terminal hexahistidine tag' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hsp90M 1.2 mM '[U-99% 13C; U-99% 15N; U-95% 2H]' 'potassium phosphate' 50 mM 'natural abundance' 'potassium chloride' 50 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' 'Rheinstetten, Germany' . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 2 loop_ _Vendor _Address _Electronic_address Goddard 'UCSF, San Francisco' . stop_ loop_ _Task 'data analysis' 'peak picking' stop_ _Details . save_ save_PASTA _Saveframe_category software _Name PASTA _Version 0.1 loop_ _Vendor _Address _Electronic_address Kessler 'TUM, Munich' . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_DMX750 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 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' 0.15 0.02 M pH 7.5 0.1 pH pressure 1 . atm temperature 298 1 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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' '2D 1H-13C HSQC' '3D HN(CO)CA' '3D HNCACB' '3D HNCO' '3D HNCA' '3D HN(CA)CO' '3D HN(CO)CACB' 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 'Hsp90 middle domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 276 9 LEU C C 176.81 0.05 1 2 276 9 LEU CA C 57.95 0.05 1 3 276 9 LEU CB C 41.29 0.05 1 4 277 10 TRP H H 6.21 0.02 1 5 277 10 TRP CA C 58.84 0.05 1 6 277 10 TRP CB C 26.36 0.05 1 7 277 10 TRP N N 106.57 0.05 1 8 278 11 THR H H 7.07 0.02 1 9 278 11 THR C C 174.14 0.05 1 10 278 11 THR CA C 61.98 0.05 1 11 278 11 THR CB C 68.61 0.05 1 12 278 11 THR N N 112.32 0.05 1 13 279 12 ARG H H 6.96 0.02 1 14 279 12 ARG C C 174.86 0.05 1 15 279 12 ARG CA C 54.86 0.05 1 16 279 12 ARG CB C 30.16 0.05 1 17 279 12 ARG N N 122.78 0.05 1 18 280 13 ASN H H 8.56 0.02 1 19 280 13 ASN C C 174.80 0.05 1 20 280 13 ASN CA C 50.67 0.05 1 21 280 13 ASN CB C 37.64 0.05 1 22 280 13 ASN N N 120.91 0.05 1 23 281 14 PRO CA C 64.89 0.05 1 24 281 14 PRO CB C 31.21 0.05 1 25 282 15 SER H H 7.86 0.02 1 26 282 15 SER C C 174.90 0.05 1 27 282 15 SER CA C 59.94 0.05 1 28 282 15 SER CB C 62.06 0.05 1 29 282 15 SER N N 109.28 0.05 1 30 283 16 ASP H H 8.05 0.02 1 31 283 16 ASP C C 175.00 0.05 1 32 283 16 ASP CA C 53.66 0.05 1 33 283 16 ASP CB C 42.07 0.05 1 34 283 16 ASP N N 120.46 0.05 1 35 284 17 ILE H H 7.06 0.02 1 36 284 17 ILE C C 176.11 0.05 1 37 284 17 ILE CA C 60.76 0.05 1 38 284 17 ILE CB C 38.55 0.05 1 39 284 17 ILE N N 122.65 0.05 1 40 285 18 THR H H 8.39 0.02 1 41 285 18 THR C C 175.68 0.05 1 42 285 18 THR CA C 60.27 0.05 1 43 285 18 THR CB C 70.67 0.05 1 44 285 18 THR N N 118.43 0.05 1 45 286 19 GLN H H 8.95 0.02 1 46 286 19 GLN C C 178.10 0.05 1 47 286 19 GLN CA C 58.84 0.05 1 48 286 19 GLN CB C 27.31 0.05 1 49 286 19 GLN N N 121.83 0.05 1 50 287 20 GLU H H 8.67 0.02 1 51 287 20 GLU C C 179.59 0.05 1 52 287 20 GLU CA C 59.56 0.05 1 53 287 20 GLU CB C 27.77 0.05 1 54 287 20 GLU N N 117.20 0.05 1 55 288 21 GLU H H 7.64 0.02 1 56 288 21 GLU C C 180.78 0.05 1 57 288 21 GLU CA C 59.32 0.05 1 58 288 21 GLU CB C 29.45 0.05 1 59 288 21 GLU N N 120.70 0.05 1 60 289 22 TYR H H 7.85 0.02 1 61 289 22 TYR C C 178.38 0.05 1 62 289 22 TYR CA C 62.00 0.05 1 63 289 22 TYR CB C 37.60 0.05 1 64 289 22 TYR N N 120.40 0.05 1 65 290 23 ASN H H 8.85 0.02 1 66 290 23 ASN C C 177.62 0.05 1 67 290 23 ASN CA C 55.67 0.05 1 68 290 23 ASN CB C 36.25 0.05 1 69 290 23 ASN N N 119.90 0.05 1 70 291 24 ALA H H 8.11 0.02 1 71 291 24 ALA C C 180.72 0.05 1 72 291 24 ALA CA C 54.39 0.05 1 73 291 24 ALA CB C 17.14 0.05 1 74 291 24 ALA N N 121.92 0.05 1 75 292 25 PHE H H 8.00 0.02 1 76 292 25 PHE C C 178.19 0.05 1 77 292 25 PHE CA C 60.55 0.05 1 78 292 25 PHE CB C 38.91 0.05 1 79 292 25 PHE N N 121.39 0.05 1 80 293 26 TYR H H 8.54 0.02 1 81 293 26 TYR C C 178.77 0.05 1 82 293 26 TYR CA C 60.47 0.05 1 83 293 26 TYR CB C 35.70 0.05 1 84 293 26 TYR N N 120.77 0.05 1 85 294 27 LYS H H 7.86 0.02 1 86 294 27 LYS C C 178.22 0.05 1 87 294 27 LYS CA C 59.84 0.05 1 88 294 27 LYS CB C 30.95 0.05 1 89 294 27 LYS N N 121.41 0.05 1 90 295 28 SER H H 7.57 0.02 1 91 295 28 SER C C 176.00 0.05 1 92 295 28 SER CA C 60.35 0.05 1 93 295 28 SER CB C 62.33 0.05 1 94 295 28 SER N N 114.65 0.05 1 95 296 29 ILE H H 7.07 0.02 1 96 296 29 ILE C C 176.06 0.05 1 97 296 29 ILE CA C 61.41 0.05 1 98 296 29 ILE CB C 37.77 0.05 1 99 296 29 ILE N N 112.89 0.05 1 100 297 30 SER H H 7.41 0.02 1 101 297 30 SER C C 174.39 0.05 1 102 297 30 SER CA C 57.90 0.05 1 103 297 30 SER CB C 65.42 0.05 1 104 297 30 SER N N 115.57 0.05 1 105 298 31 ASN C C 178.53 0.05 1 106 298 31 ASN CA C 56.42 0.05 1 107 298 31 ASN CB C 36.14 0.05 1 108 299 32 ASP H H 8.10 0.02 1 109 299 32 ASP C C 178.23 0.05 1 110 299 32 ASP CA C 56.98 0.05 1 111 299 32 ASP CB C 40.34 0.05 1 112 299 32 ASP N N 121.71 0.05 1 113 300 33 TRP H H 7.62 0.02 1 114 300 33 TRP C C 176.72 0.05 1 115 300 33 TRP CA C 57.22 0.05 1 116 300 33 TRP CB C 27.70 0.05 1 117 300 33 TRP N N 116.43 0.05 1 118 301 34 GLU H H 7.51 0.02 1 119 301 34 GLU C C 175.57 0.05 1 120 301 34 GLU CA C 55.04 0.05 1 121 301 34 GLU CB C 27.89 0.05 1 122 301 34 GLU N N 115.54 0.05 1 123 303 36 PRO CA C 62.09 0.05 1 124 303 36 PRO CB C 29.21 0.05 1 125 304 37 LEU H H 8.65 0.02 1 126 304 37 LEU C C 176.80 0.05 1 127 304 37 LEU CA C 56.51 0.05 1 128 304 37 LEU CB C 42.41 0.05 1 129 304 37 LEU N N 122.76 0.05 1 130 305 38 TYR C C 172.29 0.05 1 131 305 38 TYR CA C 57.56 0.05 1 132 305 38 TYR CB C 43.76 0.05 1 133 306 39 VAL H H 6.93 0.02 1 134 306 39 VAL C C 171.97 0.05 1 135 306 39 VAL CA C 59.38 0.05 1 136 306 39 VAL CB C 33.08 0.05 1 137 306 39 VAL N N 125.62 0.05 1 138 307 40 LYS H H 8.76 0.02 1 139 307 40 LYS C C 172.08 0.05 1 140 307 40 LYS CA C 52.30 0.05 1 141 307 40 LYS CB C 32.52 0.05 1 142 307 40 LYS N N 126.96 0.05 1 143 308 41 HIS H H 9.13 0.02 1 144 308 41 HIS C C 173.77 0.05 1 145 308 41 HIS CA C 51.43 0.05 1 146 308 41 HIS CB C 33.52 0.05 1 147 308 41 HIS N N 131.50 0.05 1 148 309 42 PHE H H 8.83 0.02 1 149 309 42 PHE C C 171.05 0.05 1 150 309 42 PHE CA C 54.98 0.05 1 151 309 42 PHE CB C 40.75 0.05 1 152 309 42 PHE N N 122.42 0.05 1 153 310 43 SER H H 8.38 0.02 1 154 310 43 SER C C 172.65 0.05 1 155 310 43 SER CA C 55.64 0.05 1 156 310 43 SER CB C 65.27 0.05 1 157 310 43 SER N N 113.33 0.05 1 158 311 44 VAL H H 8.47 0.02 1 159 311 44 VAL C C 174.00 0.05 1 160 311 44 VAL CA C 61.37 0.05 1 161 311 44 VAL CB C 32.92 0.05 1 162 311 44 VAL N N 124.82 0.05 1 163 312 45 GLU H H 8.17 0.02 1 164 312 45 GLU C C 175.39 0.05 1 165 312 45 GLU CA C 54.47 0.05 1 166 312 45 GLU CB C 31.79 0.05 1 167 312 45 GLU N N 124.96 0.05 1 168 313 46 GLY H H 8.44 0.02 1 169 313 46 GLY C C 173.52 0.05 1 170 313 46 GLY CA C 44.50 0.05 1 171 313 46 GLY N N 110.22 0.05 1 172 314 47 GLN C C 175.24 0.05 1 173 314 47 GLN CA C 57.79 0.05 1 174 314 47 GLN CB C 27.66 0.05 1 175 315 48 LEU H H 7.48 0.02 1 176 315 48 LEU C C 174.36 0.05 1 177 315 48 LEU CA C 53.37 0.05 1 178 315 48 LEU CB C 42.72 0.05 1 179 315 48 LEU N N 118.48 0.05 1 180 316 49 GLU H H 9.03 0.02 1 181 316 49 GLU C C 176.59 0.05 1 182 316 49 GLU CA C 53.84 0.05 1 183 316 49 GLU CB C 30.87 0.05 1 184 316 49 GLU N N 122.16 0.05 1 185 317 50 PHE H H 8.35 0.02 1 186 317 50 PHE C C 171.25 0.05 1 187 317 50 PHE CA C 56.20 0.05 1 188 317 50 PHE CB C 39.88 0.05 1 189 317 50 PHE N N 120.70 0.05 1 190 318 51 ARG H H 8.43 0.02 1 191 318 51 ARG C C 174.15 0.05 1 192 318 51 ARG CA C 53.95 0.05 1 193 318 51 ARG CB C 33.59 0.05 1 194 318 51 ARG N N 117.71 0.05 1 195 319 52 ALA H H 8.32 0.02 1 196 319 52 ALA C C 175.20 0.05 1 197 319 52 ALA CA C 50.30 0.05 1 198 319 52 ALA CB C 22.28 0.05 1 199 319 52 ALA N N 120.92 0.05 1 200 324 57 PRO CA C 62.16 0.05 1 201 324 57 PRO CB C 32.68 0.05 1 202 325 58 LYS H H 9.16 0.02 1 203 325 58 LYS C C 176.07 0.05 1 204 325 58 LYS CA C 58.45 0.05 1 205 325 58 LYS CB C 32.58 0.05 1 206 325 58 LYS N N 115.24 0.05 1 207 326 59 ARG H H 7.38 0.02 1 208 326 59 ARG C C 174.61 0.05 1 209 326 59 ARG CA C 52.73 0.05 1 210 326 59 ARG CB C 31.39 0.05 1 211 326 59 ARG N N 112.39 0.05 1 212 327 60 ALA H H 8.30 0.02 1 213 327 60 ALA C C 175.66 0.05 1 214 327 60 ALA CA C 49.49 0.05 1 215 327 60 ALA CB C 16.88 0.05 1 216 327 60 ALA N N 124.71 0.05 1 217 330 63 ASP C C 176.36 0.05 1 218 330 63 ASP CA C 52.67 0.05 1 219 330 63 ASP CB C 39.95 0.05 1 220 331 64 LEU H H 7.51 0.02 1 221 331 64 LEU C C 177.19 0.05 1 222 331 64 LEU CA C 56.18 0.05 1 223 331 64 LEU CB C 41.08 0.05 1 224 331 64 LEU N N 122.18 0.05 1 225 332 65 PHE H H 8.20 0.02 1 226 332 65 PHE C C 176.02 0.05 1 227 332 65 PHE CA C 57.30 0.05 1 228 332 65 PHE CB C 37.57 0.05 1 229 332 65 PHE N N 116.93 0.05 1 230 333 66 GLU H H 7.77 0.02 1 231 333 66 GLU C C 176.61 0.05 1 232 333 66 GLU CA C 56.13 0.05 1 233 333 66 GLU CB C 28.97 0.05 1 234 333 66 GLU N N 121.07 0.05 1 235 336 69 LYS C C 176.27 0.05 1 236 336 69 LYS CA C 55.80 0.05 1 237 336 69 LYS CB C 32.16 0.05 1 238 337 70 LYS H H 8.15 0.02 1 239 337 70 LYS C C 176.41 0.05 1 240 337 70 LYS CA C 55.62 0.05 1 241 337 70 LYS CB C 31.45 0.05 1 242 337 70 LYS N N 122.97 0.05 1 243 338 71 LYS H H 8.40 0.02 1 244 338 71 LYS C C 175.99 0.05 1 245 338 71 LYS CA C 55.61 0.05 1 246 338 71 LYS CB C 31.57 0.05 1 247 338 71 LYS N N 123.32 0.05 1 248 339 72 ASN H H 8.18 0.02 1 249 339 72 ASN C C 175.05 0.05 1 250 339 72 ASN CA C 52.34 0.05 1 251 339 72 ASN CB C 37.66 0.05 1 252 339 72 ASN N N 119.35 0.05 1 253 340 73 ASN H H 8.43 0.02 1 254 340 73 ASN C C 174.61 0.05 1 255 340 73 ASN CA C 54.38 0.05 1 256 340 73 ASN CB C 38.41 0.05 1 257 340 73 ASN N N 117.86 0.05 1 258 341 74 ILE H H 8.05 0.02 1 259 341 74 ILE C C 174.87 0.05 1 260 341 74 ILE CA C 58.39 0.05 1 261 341 74 ILE CB C 37.22 0.05 1 262 341 74 ILE N N 120.88 0.05 1 263 342 75 LYS H H 8.40 0.02 1 264 342 75 LYS C C 173.45 0.05 1 265 342 75 LYS CA C 55.39 0.05 1 266 342 75 LYS CB C 32.98 0.05 1 267 342 75 LYS N N 125.11 0.05 1 268 343 76 LEU H H 8.61 0.02 1 269 343 76 LEU C C 173.66 0.05 1 270 343 76 LEU CA C 53.62 0.05 1 271 343 76 LEU CB C 42.72 0.05 1 272 343 76 LEU N N 125.66 0.05 1 273 344 77 TYR H H 9.47 0.02 1 274 344 77 TYR C C 174.48 0.05 1 275 344 77 TYR CA C 55.61 0.05 1 276 344 77 TYR CB C 40.68 0.05 1 277 344 77 TYR N N 127.94 0.05 1 278 345 78 VAL H H 8.81 0.02 1 279 345 78 VAL C C 176.44 0.05 1 280 345 78 VAL CA C 60.22 0.05 1 281 345 78 VAL CB C 33.44 0.05 1 282 345 78 VAL N N 119.68 0.05 1 283 346 79 ARG H H 8.75 0.02 1 284 346 79 ARG C C 175.94 0.05 1 285 346 79 ARG CA C 57.36 0.05 1 286 346 79 ARG CB C 26.79 0.05 1 287 346 79 ARG N N 128.27 0.05 1 288 347 80 ARG H H 9.46 0.02 1 289 347 80 ARG C C 175.97 0.05 1 290 347 80 ARG CA C 58.50 0.05 1 291 347 80 ARG CB C 27.03 0.05 1 292 347 80 ARG N N 110.44 0.05 1 293 348 81 VAL H H 8.28 0.02 1 294 348 81 VAL C C 175.45 0.05 1 295 348 81 VAL CA C 61.75 0.05 1 296 348 81 VAL CB C 31.74 0.05 1 297 348 81 VAL N N 124.64 0.05 1 298 349 82 PHE H H 8.72 0.02 1 299 349 82 PHE C C 174.16 0.05 1 300 349 82 PHE CA C 58.81 0.05 1 301 349 82 PHE CB C 37.38 0.05 1 302 349 82 PHE N N 128.80 0.05 1 303 350 83 ILE H H 8.24 0.02 1 304 350 83 ILE C C 175.20 0.05 1 305 350 83 ILE CA C 59.02 0.05 1 306 350 83 ILE CB C 36.67 0.05 1 307 350 83 ILE N N 127.47 0.05 1 308 351 84 THR H H 6.59 0.02 1 309 351 84 THR C C 170.61 0.05 1 310 351 84 THR CA C 60.16 0.05 1 311 351 84 THR CB C 66.81 0.05 1 312 351 84 THR N N 110.61 0.05 1 313 352 85 ASP H H 8.16 0.02 1 314 352 85 ASP C C 175.48 0.05 1 315 352 85 ASP CA C 52.72 0.05 1 316 352 85 ASP CB C 40.72 0.05 1 317 352 85 ASP N N 125.43 0.05 1 318 353 86 GLU H H 8.53 0.02 1 319 353 86 GLU C C 175.88 0.05 1 320 353 86 GLU CA C 54.40 0.05 1 321 353 86 GLU CB C 29.06 0.05 1 322 353 86 GLU N N 120.76 0.05 1 323 354 87 ALA H H 8.26 0.02 1 324 354 87 ALA C C 177.30 0.05 1 325 354 87 ALA CA C 51.02 0.05 1 326 354 87 ALA CB C 16.68 0.05 1 327 354 87 ALA N N 125.95 0.05 1 328 355 88 GLU H H 8.25 0.02 1 329 355 88 GLU C C 176.40 0.05 1 330 355 88 GLU CA C 57.47 0.05 1 331 355 88 GLU CB C 29.07 0.05 1 332 355 88 GLU N N 123.16 0.05 1 333 356 89 ASP H H 8.38 0.02 1 334 356 89 ASP C C 175.98 0.05 1 335 356 89 ASP CA C 54.53 0.05 1 336 356 89 ASP CB C 39.87 0.05 1 337 356 89 ASP N N 116.42 0.05 1 338 357 90 LEU H H 7.48 0.02 1 339 357 90 LEU C C 173.66 0.05 1 340 357 90 LEU CA C 56.54 0.05 1 341 357 90 LEU CB C 41.80 0.05 1 342 357 90 LEU N N 120.58 0.05 1 343 358 91 ILE H H 6.83 0.02 1 344 358 91 ILE C C 172.80 0.05 1 345 358 91 ILE CA C 55.90 0.05 1 346 358 91 ILE CB C 40.09 0.05 1 347 358 91 ILE N N 107.72 0.05 1 348 359 92 PRO CA C 61.42 0.05 1 349 360 93 GLU H H 8.94 0.02 1 350 360 93 GLU C C 179.66 0.05 1 351 360 93 GLU CA C 59.50 0.05 1 352 360 93 GLU CB C 28.19 0.05 1 353 360 93 GLU N N 122.68 0.05 1 354 361 94 TRP H H 7.81 0.02 1 355 361 94 TRP C C 175.80 0.05 1 356 361 94 TRP CA C 57.96 0.05 1 357 361 94 TRP CB C 26.24 0.05 1 358 361 94 TRP N N 116.27 0.05 1 359 362 95 LEU H H 6.67 0.02 1 360 362 95 LEU C C 176.68 0.05 1 361 362 95 LEU CA C 52.61 0.05 1 362 362 95 LEU CB C 41.16 0.05 1 363 362 95 LEU N N 120.40 0.05 1 364 363 96 SER H H 7.43 0.02 1 365 363 96 SER C C 172.73 0.05 1 366 363 96 SER CA C 60.50 0.05 1 367 363 96 SER CB C 62.17 0.05 1 368 363 96 SER N N 113.74 0.05 1 369 364 97 PHE H H 6.53 0.02 1 370 364 97 PHE C C 174.26 0.05 1 371 364 97 PHE CA C 55.56 0.05 1 372 364 97 PHE CB C 38.30 0.05 1 373 364 97 PHE N N 115.77 0.05 1 374 365 98 VAL H H 6.66 0.02 1 375 365 98 VAL C C 174.28 0.05 1 376 365 98 VAL CA C 62.03 0.05 1 377 365 98 VAL CB C 30.99 0.05 1 378 365 98 VAL N N 120.23 0.05 1 379 366 99 LYS C C 176.40 0.05 1 380 366 99 LYS CA C 52.52 0.05 1 381 366 99 LYS CB C 35.65 0.05 1 382 367 100 GLY H H 8.57 0.02 1 383 367 100 GLY C C 170.60 0.05 1 384 367 100 GLY CA C 45.73 0.05 1 385 367 100 GLY N N 106.75 0.05 1 386 370 103 ASP C C 177.08 0.05 1 387 370 103 ASP CA C 51.12 0.05 1 388 370 103 ASP CB C 42.64 0.05 1 389 371 104 SER H H 8.80 0.02 1 390 371 104 SER C C 174.80 0.05 1 391 371 104 SER CA C 56.11 0.05 1 392 371 104 SER CB C 64.78 0.05 1 393 371 104 SER N N 120.89 0.05 1 394 372 105 GLU H H 8.32 0.02 1 395 372 105 GLU C C 177.61 0.05 1 396 372 105 GLU CA C 56.47 0.05 1 397 372 105 GLU CB C 29.77 0.05 1 398 372 105 GLU N N 124.73 0.05 1 399 373 106 ASP H H 7.68 0.02 1 400 373 106 ASP C C 176.06 0.05 1 401 373 106 ASP CA C 54.47 0.05 1 402 373 106 ASP CB C 43.73 0.05 1 403 373 106 ASP N N 114.44 0.05 1 404 374 107 LEU H H 7.03 0.02 1 405 374 107 LEU C C 173.38 0.05 1 406 374 107 LEU CA C 53.28 0.05 1 407 374 107 LEU CB C 41.47 0.05 1 408 374 107 LEU N N 121.65 0.05 1 409 375 108 PRO CA C 61.90 0.05 1 410 375 108 PRO CB C 30.55 0.05 1 411 376 109 LEU H H 7.82 0.02 1 412 376 109 LEU C C 177.31 0.05 1 413 376 109 LEU CA C 54.78 0.05 1 414 376 109 LEU CB C 41.75 0.05 1 415 376 109 LEU N N 118.37 0.05 1 416 377 110 ASN H H 8.04 0.02 1 417 377 110 ASN C C 174.69 0.05 1 418 377 110 ASN CA C 52.29 0.05 1 419 377 110 ASN CB C 36.90 0.05 1 420 377 110 ASN N N 115.42 0.05 1 421 378 111 LEU H H 7.76 0.02 1 422 378 111 LEU C C 176.61 0.05 1 423 378 111 LEU CA C 54.31 0.05 1 424 378 111 LEU CB C 41.56 0.05 1 425 378 111 LEU N N 121.13 0.05 1 426 379 112 SER H H 7.80 0.02 1 427 379 112 SER C C 174.70 0.05 1 428 379 112 SER CA C 56.56 0.05 1 429 379 112 SER CB C 64.11 0.05 1 430 379 112 SER N N 117.49 0.05 1 431 380 113 ARG C C 178.18 0.05 1 432 380 113 ARG CA C 58.85 0.05 1 433 380 113 ARG CB C 28.76 0.05 1 434 381 114 GLU H H 8.61 0.02 1 435 381 114 GLU C C 178.29 0.05 1 436 381 114 GLU CA C 58.54 0.05 1 437 381 114 GLU CB C 28.02 0.05 1 438 381 114 GLU N N 118.40 0.05 1 439 382 115 MET H H 7.57 0.02 1 440 382 115 MET C C 178.52 0.05 1 441 382 115 MET CA C 56.47 0.05 1 442 382 115 MET CB C 31.85 0.05 1 443 382 115 MET N N 118.58 0.05 1 444 383 116 LEU C C 173.43 0.05 1 445 383 116 LEU CA C 54.22 0.05 1 446 383 116 LEU CB C 37.15 0.05 1 447 384 117 GLN H H 7.39 0.02 1 448 384 117 GLN C C 174.64 0.05 1 449 384 117 GLN CA C 54.85 0.05 1 450 384 117 GLN CB C 30.32 0.05 1 451 384 117 GLN N N 123.89 0.05 1 452 385 118 GLN H H 7.84 0.02 1 453 385 118 GLN C C 176.43 0.05 1 454 385 118 GLN CA C 56.03 0.05 1 455 385 118 GLN CB C 28.11 0.05 1 456 385 118 GLN N N 123.13 0.05 1 457 386 119 ASN H H 7.57 0.02 1 458 386 119 ASN C C 175.51 0.05 1 459 386 119 ASN CA C 53.15 0.05 1 460 386 119 ASN CB C 40.66 0.05 1 461 386 119 ASN N N 120.52 0.05 1 462 387 120 LYS H H 7.84 0.02 1 463 387 120 LYS C C 178.19 0.05 1 464 387 120 LYS CA C 52.56 0.05 1 465 387 120 LYS CB C 36.62 0.05 1 466 387 120 LYS N N 118.89 0.05 1 467 388 121 ILE H H 7.85 0.02 1 468 388 121 ILE C C 178.19 0.05 1 469 388 121 ILE CA C 63.81 0.05 1 470 388 121 ILE CB C 35.94 0.05 1 471 388 121 ILE N N 120.47 0.05 1 472 389 122 MET H H 7.85 0.02 1 473 389 122 MET C C 178.09 0.05 1 474 389 122 MET CA C 57.08 0.05 1 475 389 122 MET CB C 30.30 0.05 1 476 389 122 MET N N 118.59 0.05 1 477 390 123 LYS H H 7.40 0.02 1 478 390 123 LYS C C 179.16 0.05 1 479 390 123 LYS CA C 59.06 0.05 1 480 390 123 LYS CB C 31.01 0.05 1 481 390 123 LYS N N 116.82 0.05 1 482 391 124 VAL H H 7.37 0.02 1 483 391 124 VAL C C 179.52 0.05 1 484 391 124 VAL CA C 65.56 0.05 1 485 391 124 VAL CB C 30.44 0.05 1 486 391 124 VAL N N 120.91 0.05 1 487 392 125 ILE H H 8.14 0.02 1 488 392 125 ILE C C 177.47 0.05 1 489 392 125 ILE CA C 65.95 0.05 1 490 392 125 ILE CB C 35.92 0.05 1 491 392 125 ILE N N 124.29 0.05 1 492 393 126 ARG H H 8.16 0.02 1 493 393 126 ARG C C 177.62 0.05 1 494 393 126 ARG CA C 59.17 0.05 1 495 393 126 ARG CB C 29.21 0.05 1 496 393 126 ARG N N 120.32 0.05 1 497 394 127 LYS H H 7.71 0.02 1 498 394 127 LYS C C 179.80 0.05 1 499 394 127 LYS CA C 59.16 0.05 1 500 394 127 LYS CB C 31.26 0.05 1 501 394 127 LYS N N 116.72 0.05 1 502 395 128 ASN H H 7.74 0.02 1 503 395 128 ASN C C 176.68 0.05 1 504 395 128 ASN CA C 56.92 0.05 1 505 395 128 ASN CB C 40.54 0.05 1 506 395 128 ASN N N 117.19 0.05 1 507 396 129 ILE H H 8.75 0.02 1 508 396 129 ILE C C 176.81 0.05 1 509 396 129 ILE CA C 66.35 0.05 1 510 396 129 ILE CB C 36.19 0.05 1 511 396 129 ILE N N 121.27 0.05 1 512 397 130 VAL H H 8.14 0.02 1 513 397 130 VAL C C 177.25 0.05 1 514 397 130 VAL CA C 67.28 0.05 1 515 397 130 VAL CB C 30.18 0.05 1 516 397 130 VAL N N 118.60 0.05 1 517 398 131 LYS H H 7.38 0.02 1 518 398 131 LYS C C 179.71 0.05 1 519 398 131 LYS CA C 59.26 0.05 1 520 398 131 LYS CB C 31.35 0.05 1 521 398 131 LYS N N 117.18 0.05 1 522 399 132 LYS H H 7.68 0.02 1 523 399 132 LYS C C 178.62 0.05 1 524 399 132 LYS CA C 56.32 0.05 1 525 399 132 LYS CB C 30.64 0.05 1 526 399 132 LYS N N 118.28 0.05 1 527 401 134 ILE C C 178.09 0.05 1 528 401 134 ILE CA C 65.29 0.05 1 529 401 134 ILE CB C 36.03 0.05 1 530 402 135 GLU H H 7.41 0.02 1 531 402 135 GLU C C 178.60 0.05 1 532 402 135 GLU CA C 59.25 0.05 1 533 402 135 GLU CB C 28.62 0.05 1 534 402 135 GLU N N 119.60 0.05 1 535 403 136 ALA H H 7.62 0.02 1 536 403 136 ALA C C 178.70 0.05 1 537 403 136 ALA CA C 53.78 0.05 1 538 403 136 ALA CB C 16.34 0.05 1 539 403 136 ALA N N 121.44 0.05 1 540 404 137 PHE C C 177.55 0.05 1 541 404 137 PHE CA C 56.37 0.05 1 542 404 137 PHE CB C 36.04 0.05 1 543 405 138 ASN H H 8.06 0.02 1 544 405 138 ASN C C 177.88 0.05 1 545 405 138 ASN CA C 55.41 0.05 1 546 405 138 ASN CB C 37.33 0.05 1 547 405 138 ASN N N 117.04 0.05 1 548 406 139 GLU H H 7.86 0.02 1 549 406 139 GLU C C 180.73 0.05 1 550 406 139 GLU CA C 58.69 0.05 1 551 406 139 GLU CB C 27.41 0.05 1 552 406 139 GLU N N 122.51 0.05 1 553 407 140 ILE C C 177.24 0.05 1 554 407 140 ILE CA C 64.70 0.05 1 555 407 140 ILE CB C 36.30 0.05 1 556 408 141 ALA H H 7.62 0.02 1 557 408 141 ALA C C 177.89 0.05 1 558 408 141 ALA CA C 52.92 0.05 1 559 408 141 ALA CB C 16.36 0.05 1 560 408 141 ALA N N 116.96 0.05 1 561 409 142 GLU H H 7.07 0.02 1 562 409 142 GLU C C 175.72 0.05 1 563 409 142 GLU CA C 56.94 0.05 1 564 409 142 GLU CB C 28.79 0.05 1 565 409 142 GLU N N 116.38 0.05 1 566 410 143 ASP H H 7.95 0.02 1 567 410 143 ASP C C 175.16 0.05 1 568 410 143 ASP CA C 51.95 0.05 1 569 410 143 ASP CB C 42.23 0.05 1 570 410 143 ASP N N 121.56 0.05 1 571 411 144 SER H H 8.73 0.02 1 572 411 144 SER C C 176.72 0.05 1 573 411 144 SER CA C 61.91 0.05 1 574 411 144 SER N N 120.99 0.05 1 575 412 145 GLU H H 8.09 0.02 1 576 412 145 GLU C C 179.41 0.05 1 577 412 145 GLU CA C 58.95 0.05 1 578 412 145 GLU CB C 28.70 0.05 1 579 412 145 GLU N N 122.21 0.05 1 580 413 146 GLN H H 8.11 0.02 1 581 413 146 GLN C C 178.88 0.05 1 582 413 146 GLN CA C 57.91 0.05 1 583 413 146 GLN CB C 28.57 0.05 1 584 413 146 GLN N N 120.80 0.05 1 585 414 147 PHE H H 9.33 0.02 1 586 414 147 PHE C C 176.79 0.05 1 587 414 147 PHE CA C 61.99 0.05 1 588 414 147 PHE CB C 37.44 0.05 1 589 414 147 PHE N N 120.18 0.05 1 590 415 148 GLU H H 7.97 0.02 1 591 415 148 GLU C C 179.59 0.05 1 592 415 148 GLU CA C 59.35 0.05 1 593 415 148 GLU CB C 28.05 0.05 1 594 415 148 GLU N N 118.77 0.05 1 595 416 149 LYS H H 7.02 0.02 1 596 416 149 LYS C C 179.15 0.05 1 597 416 149 LYS CA C 58.75 0.05 1 598 416 149 LYS CB C 31.42 0.05 1 599 416 149 LYS N N 118.81 0.05 1 600 417 150 PHE H H 8.09 0.02 1 601 417 150 PHE C C 175.40 0.05 1 602 417 150 PHE CA C 59.83 0.05 1 603 417 150 PHE CB C 39.09 0.05 1 604 417 150 PHE N N 121.45 0.05 1 605 418 151 TYR H H 9.34 0.02 1 606 418 151 TYR C C 177.59 0.05 1 607 418 151 TYR CA C 61.98 0.05 1 608 418 151 TYR CB C 37.23 0.05 1 609 418 151 TYR N N 122.07 0.05 1 610 419 152 SER H H 7.61 0.02 1 611 419 152 SER C C 175.82 0.05 1 612 419 152 SER CA C 60.68 0.05 1 613 419 152 SER CB C 61.90 0.05 1 614 419 152 SER N N 111.72 0.05 1 615 420 153 ALA H H 6.61 0.02 1 616 420 153 ALA C C 179.58 0.05 1 617 420 153 ALA CA C 53.36 0.05 1 618 420 153 ALA CB C 18.07 0.05 1 619 420 153 ALA N N 120.80 0.05 1 620 421 154 PHE H H 7.59 0.02 1 621 421 154 PHE C C 176.38 0.05 1 622 421 154 PHE CA C 57.17 0.05 1 623 421 154 PHE CB C 37.47 0.05 1 624 421 154 PHE N N 112.94 0.05 1 625 422 155 SER H H 7.58 0.02 1 626 422 155 SER C C 176.41 0.05 1 627 422 155 SER CA C 61.84 0.05 1 628 422 155 SER CB C 59.50 0.05 1 629 422 155 SER N N 117.26 0.05 1 630 423 156 LYS H H 8.01 0.02 1 631 423 156 LYS C C 177.34 0.05 1 632 423 156 LYS CA C 59.51 0.05 1 633 423 156 LYS CB C 30.69 0.05 1 634 423 156 LYS N N 121.33 0.05 1 635 424 157 ASN H H 7.26 0.02 1 636 424 157 ASN C C 176.61 0.05 1 637 424 157 ASN CA C 58.08 0.05 1 638 424 157 ASN CB C 37.50 0.05 1 639 424 157 ASN N N 115.98 0.05 1 640 427 160 LEU C C 179.70 0.05 1 641 427 160 LEU CA C 57.23 0.05 1 642 427 160 LEU CB C 40.07 0.05 1 643 428 161 GLY H H 7.78 0.02 1 644 428 161 GLY C C 174.91 0.05 1 645 428 161 GLY CA C 44.98 0.05 1 646 428 161 GLY N N 110.07 0.05 1 647 429 162 VAL H H 7.78 0.02 1 648 429 162 VAL C C 177.20 0.05 1 649 429 162 VAL CA C 65.44 0.05 1 650 429 162 VAL CB C 29.45 0.05 1 651 429 162 VAL N N 121.23 0.05 1 652 430 163 HIS H H 7.68 0.02 1 653 430 163 HIS C C 177.06 0.05 1 654 430 163 HIS CA C 59.64 0.05 1 655 430 163 HIS CB C 30.24 0.05 1 656 430 163 HIS N N 116.94 0.05 1 657 431 164 GLU H H 7.83 0.02 1 658 431 164 GLU C C 176.89 0.05 1 659 431 164 GLU CA C 57.60 0.05 1 660 431 164 GLU CB C 31.49 0.05 1 661 431 164 GLU N N 115.67 0.05 1 662 432 165 ASP H H 8.62 0.02 1 663 432 165 ASP C C 175.06 0.05 1 664 432 165 ASP CA C 53.22 0.05 1 665 432 165 ASP CB C 40.66 0.05 1 666 432 165 ASP N N 121.81 0.05 1 667 433 166 THR H H 7.85 0.02 1 668 433 166 THR C C 176.53 0.05 1 669 433 166 THR CA C 64.87 0.05 1 670 433 166 THR CB C 68.11 0.05 1 671 433 166 THR N N 118.01 0.05 1 672 434 167 GLN H H 8.08 0.02 1 673 434 167 GLN C C 177.79 0.05 1 674 434 167 GLN CA C 57.78 0.05 1 675 434 167 GLN CB C 28.16 0.05 1 676 434 167 GLN N N 119.53 0.05 1 677 435 168 ASN H H 8.08 0.02 1 678 435 168 ASN C C 175.42 0.05 1 679 435 168 ASN CA C 52.41 0.05 1 680 435 168 ASN CB C 38.95 0.05 1 681 435 168 ASN N N 114.28 0.05 1 682 436 169 ARG H H 7.57 0.02 1 683 436 169 ARG C C 176.42 0.05 1 684 436 169 ARG CA C 60.50 0.05 1 685 436 169 ARG CB C 29.54 0.05 1 686 436 169 ARG N N 120.52 0.05 1 687 437 170 ALA H H 8.41 0.02 1 688 437 170 ALA C C 179.65 0.05 1 689 437 170 ALA CA C 55.03 0.05 1 690 437 170 ALA CB C 16.59 0.05 1 691 437 170 ALA N N 121.58 0.05 1 692 438 171 ALA H H 7.58 0.02 1 693 438 171 ALA C C 181.98 0.05 1 694 438 171 ALA CA C 54.14 0.05 1 695 438 171 ALA CB C 17.56 0.05 1 696 438 171 ALA N N 120.52 0.05 1 697 439 172 LEU H H 8.11 0.02 1 698 439 172 LEU C C 179.02 0.05 1 699 439 172 LEU CA C 56.80 0.05 1 700 439 172 LEU CB C 41.61 0.05 1 701 439 172 LEU N N 118.94 0.05 1 702 440 173 ALA H H 8.43 0.02 1 703 440 173 ALA C C 179.91 0.05 1 704 440 173 ALA CA C 53.65 0.05 1 705 440 173 ALA CB C 17.96 0.05 1 706 440 173 ALA N N 119.75 0.05 1 707 441 174 LYS H H 7.27 0.02 1 708 441 174 LYS C C 176.70 0.05 1 709 441 174 LYS CA C 58.10 0.05 1 710 441 174 LYS CB C 31.37 0.05 1 711 441 174 LYS N N 115.76 0.05 1 712 442 175 LEU C C 180.87 0.05 1 713 442 175 LEU CA C 59.45 0.05 1 714 442 175 LEU CB C 37.10 0.05 1 715 443 176 LEU H H 7.76 0.02 1 716 443 176 LEU C C 178.86 0.05 1 717 443 176 LEU CA C 54.50 0.05 1 718 443 176 LEU CB C 41.41 0.05 1 719 443 176 LEU N N 121.48 0.05 1 720 444 177 ARG H H 7.51 0.02 1 721 444 177 ARG C C 173.20 0.05 1 722 444 177 ARG CA C 52.50 0.05 1 723 444 177 ARG CB C 33.19 0.05 1 724 444 177 ARG N N 121.54 0.05 1 725 445 178 TYR H H 8.53 0.02 1 726 445 178 TYR C C 176.39 0.05 1 727 445 178 TYR CA C 57.73 0.05 1 728 445 178 TYR CB C 44.34 0.05 1 729 445 178 TYR N N 117.62 0.05 1 730 446 179 ASN H H 9.69 0.02 1 731 446 179 ASN C C 173.26 0.05 1 732 446 179 ASN CA C 54.47 0.05 1 733 446 179 ASN CB C 41.28 0.05 1 734 446 179 ASN N N 118.93 0.05 1 735 447 180 SER H H 8.33 0.02 1 736 447 180 SER C C 174.78 0.05 1 737 447 180 SER CA C 56.04 0.05 1 738 447 180 SER CB C 67.81 0.05 1 739 447 180 SER N N 114.99 0.05 1 740 448 181 THR H H 8.02 0.02 1 741 448 181 THR C C 176.29 0.05 1 742 448 181 THR CA C 63.28 0.05 1 743 448 181 THR CB C 68.56 0.05 1 744 448 181 THR N N 107.30 0.05 1 745 449 182 LYS H H 7.57 0.02 1 746 449 182 LYS C C 174.51 0.05 1 747 449 182 LYS CA C 55.68 0.05 1 748 449 182 LYS CB C 31.91 0.05 1 749 449 182 LYS N N 118.91 0.05 1 750 450 183 SER H H 7.45 0.02 1 751 450 183 SER C C 174.66 0.05 1 752 450 183 SER CA C 56.83 0.05 1 753 450 183 SER CB C 61.51 0.05 1 754 450 183 SER N N 119.21 0.05 1 755 451 184 VAL H H 8.52 0.02 1 756 451 184 VAL C C 176.00 0.05 1 757 451 184 VAL CA C 64.14 0.05 1 758 451 184 VAL CB C 31.36 0.05 1 759 451 184 VAL N N 124.65 0.05 1 760 452 185 ASP H H 8.18 0.02 1 761 452 185 ASP C C 175.31 0.05 1 762 452 185 ASP CA C 53.93 0.05 1 763 452 185 ASP CB C 41.11 0.05 1 764 452 185 ASP N N 117.88 0.05 1 765 453 186 GLU H H 7.45 0.02 1 766 453 186 GLU C C 175.53 0.05 1 767 453 186 GLU CA C 54.09 0.05 1 768 453 186 GLU CB C 31.23 0.05 1 769 453 186 GLU N N 118.17 0.05 1 770 454 187 LEU H H 8.58 0.02 1 771 454 187 LEU C C 176.65 0.05 1 772 454 187 LEU CA C 54.42 0.05 1 773 454 187 LEU CB C 42.09 0.05 1 774 454 187 LEU N N 123.32 0.05 1 775 455 188 THR H H 9.19 0.02 1 776 455 188 THR C C 171.62 0.05 1 777 455 188 THR CA C 58.91 0.05 1 778 455 188 THR CB C 69.97 0.05 1 779 455 188 THR N N 117.27 0.05 1 780 456 189 SER H H 8.49 0.02 1 781 456 189 SER C C 174.97 0.05 1 782 456 189 SER CA C 55.09 0.05 1 783 456 189 SER CB C 66.22 0.05 1 784 456 189 SER N N 119.19 0.05 1 785 457 190 LEU H H 9.16 0.02 1 786 457 190 LEU C C 178.25 0.05 1 787 457 190 LEU CA C 57.72 0.05 1 788 457 190 LEU CB C 38.36 0.05 1 789 457 190 LEU N N 121.16 0.05 1 790 458 191 THR H H 7.81 0.02 1 791 458 191 THR C C 176.44 0.05 1 792 458 191 THR CA C 66.83 0.05 1 793 458 191 THR CB C 68.07 0.05 1 794 458 191 THR N N 115.58 0.05 1 795 459 192 ASP H H 7.85 0.02 1 796 459 192 ASP C C 178.27 0.05 1 797 459 192 ASP CA C 56.74 0.05 1 798 459 192 ASP CB C 38.48 0.05 1 799 459 192 ASP N N 123.15 0.05 1 800 461 194 VAL C C 179.38 0.05 1 801 461 194 VAL CA C 66.14 0.05 1 802 461 194 VAL CB C 30.30 0.05 1 803 462 195 THR H H 7.96 0.02 1 804 462 195 THR C C 175.36 0.05 1 805 462 195 THR CA C 65.20 0.05 1 806 462 195 THR CB C 68.38 0.05 1 807 462 195 THR N N 115.81 0.05 1 808 463 196 ARG H H 7.09 0.02 1 809 463 196 ARG C C 176.77 0.05 1 810 463 196 ARG CA C 56.77 0.05 1 811 463 196 ARG CB C 31.88 0.05 1 812 463 196 ARG N N 118.94 0.05 1 813 464 197 MET H H 7.38 0.02 1 814 464 197 MET C C 174.52 0.05 1 815 464 197 MET CA C 54.89 0.05 1 816 464 197 MET CB C 32.67 0.05 1 817 464 197 MET N N 122.22 0.05 1 818 465 198 PRO CA C 58.76 0.05 1 819 465 198 PRO CB C 28.88 0.05 1 820 466 199 GLU H H 7.88 0.02 1 821 466 199 GLU C C 175.00 0.05 1 822 466 199 GLU CA C 55.55 0.05 1 823 466 199 GLU CB C 29.09 0.05 1 824 466 199 GLU N N 111.18 0.05 1 825 467 200 HIS H H 7.42 0.02 1 826 467 200 HIS C C 168.74 0.05 1 827 467 200 HIS CA C 55.04 0.05 1 828 467 200 HIS CB C 29.14 0.05 1 829 467 200 HIS N N 125.12 0.05 1 830 474 207 ILE C C 171.74 0.05 1 831 474 207 ILE CA C 58.92 0.05 1 832 474 207 ILE CB C 41.21 0.05 1 833 475 208 THR H H 8.24 0.02 1 834 475 208 THR C C 174.22 0.05 1 835 475 208 THR CA C 58.61 0.05 1 836 475 208 THR CB C 69.84 0.05 1 837 475 208 THR N N 118.34 0.05 1 838 476 209 GLY H H 7.78 0.02 1 839 476 209 GLY C C 172.63 0.05 1 840 476 209 GLY CA C 44.69 0.05 1 841 476 209 GLY N N 106.51 0.05 1 842 477 210 GLU H H 8.63 0.02 1 843 477 210 GLU C C 175.95 0.05 1 844 477 210 GLU CA C 57.37 0.05 1 845 477 210 GLU CB C 29.36 0.05 1 846 477 210 GLU N N 116.77 0.05 1 847 478 211 SER H H 7.30 0.02 1 848 478 211 SER C C 173.60 0.05 1 849 478 211 SER CA C 56.25 0.05 1 850 478 211 SER CB C 64.22 0.05 1 851 478 211 SER N N 109.35 0.05 1 852 479 212 LEU H H 8.75 0.02 1 853 479 212 LEU C C 177.98 0.05 1 854 479 212 LEU CA C 57.48 0.05 1 855 479 212 LEU CB C 39.88 0.05 1 856 479 212 LEU N N 123.90 0.05 1 857 480 213 LYS H H 7.88 0.02 1 858 480 213 LYS C C 178.46 0.05 1 859 480 213 LYS CA C 57.64 0.05 1 860 480 213 LYS CB C 30.59 0.05 1 861 480 213 LYS N N 116.91 0.05 1 862 481 214 ALA H H 7.44 0.02 1 863 481 214 ALA C C 180.10 0.05 1 864 481 214 ALA CA C 53.59 0.05 1 865 481 214 ALA CB C 18.26 0.05 1 866 481 214 ALA N N 119.22 0.05 1 867 482 215 VAL H H 7.42 0.02 1 868 482 215 VAL C C 177.09 0.05 1 869 482 215 VAL CA C 62.81 0.05 1 870 482 215 VAL CB C 31.12 0.05 1 871 482 215 VAL N N 112.99 0.05 1 872 483 216 GLU H H 7.63 0.02 1 873 483 216 GLU C C 176.54 0.05 1 874 483 216 GLU CA C 58.09 0.05 1 875 483 216 GLU CB C 28.08 0.05 1 876 483 216 GLU N N 118.49 0.05 1 877 484 217 LYS H H 7.27 0.02 1 878 484 217 LYS C C 176.27 0.05 1 879 484 217 LYS CA C 53.78 0.05 1 880 484 217 LYS CB C 30.95 0.05 1 881 484 217 LYS N N 116.07 0.05 1 882 485 218 SER H H 7.40 0.02 1 883 485 218 SER C C 176.63 0.05 1 884 485 218 SER CA C 56.25 0.05 1 885 485 218 SER CB C 63.65 0.05 1 886 485 218 SER N N 116.64 0.05 1 887 486 219 PRO CA C 63.62 0.05 1 888 486 219 PRO CB C 30.51 0.05 1 889 487 220 PHE H H 7.67 0.02 1 890 487 220 PHE C C 176.97 0.05 1 891 487 220 PHE CA C 60.06 0.05 1 892 487 220 PHE CB C 38.06 0.05 1 893 487 220 PHE N N 116.00 0.05 1 894 488 221 LEU H H 7.53 0.02 1 895 488 221 LEU C C 179.26 0.05 1 896 488 221 LEU CA C 56.12 0.05 1 897 488 221 LEU CB C 41.34 0.05 1 898 488 221 LEU N N 114.79 0.05 1 899 489 222 ASP H H 7.49 0.02 1 900 489 222 ASP C C 178.76 0.05 1 901 489 222 ASP CA C 58.41 0.05 1 902 489 222 ASP CB C 38.83 0.05 1 903 489 222 ASP N N 120.63 0.05 1 904 490 223 ALA H H 8.46 0.02 1 905 490 223 ALA C C 179.11 0.05 1 906 490 223 ALA CA C 53.89 0.05 1 907 490 223 ALA CB C 16.95 0.05 1 908 490 223 ALA N N 121.06 0.05 1 909 491 224 LEU H H 6.80 0.02 1 910 491 224 LEU C C 179.15 0.05 1 911 491 224 LEU CA C 54.91 0.05 1 912 491 224 LEU CB C 38.09 0.05 1 913 491 224 LEU N N 120.64 0.05 1 914 492 225 LYS H H 8.29 0.02 1 915 492 225 LYS C C 180.88 0.05 1 916 492 225 LYS CA C 59.47 0.05 1 917 492 225 LYS CB C 30.87 0.05 1 918 492 225 LYS N N 121.34 0.05 1 919 493 226 ALA H H 7.76 0.02 1 920 493 226 ALA C C 178.82 0.05 1 921 493 226 ALA CA C 54.13 0.05 1 922 493 226 ALA CB C 16.97 0.05 1 923 493 226 ALA N N 121.41 0.05 1 924 494 227 LYS H H 6.66 0.02 1 925 494 227 LYS C C 174.63 0.05 1 926 494 227 LYS CA C 55.25 0.05 1 927 494 227 LYS CB C 31.40 0.05 1 928 494 227 LYS N N 115.95 0.05 1 929 495 228 ASN H H 7.76 0.02 1 930 495 228 ASN C C 174.19 0.05 1 931 495 228 ASN CA C 53.19 0.05 1 932 495 228 ASN CB C 36.57 0.05 1 933 495 228 ASN N N 115.06 0.05 1 934 496 229 PHE H H 7.57 0.02 1 935 496 229 PHE C C 174.99 0.05 1 936 496 229 PHE CA C 51.66 0.05 1 937 496 229 PHE CB C 37.84 0.05 1 938 496 229 PHE N N 116.33 0.05 1 939 497 230 GLU H H 9.58 0.02 1 940 497 230 GLU C C 176.11 0.05 1 941 497 230 GLU CA C 55.37 0.05 1 942 497 230 GLU CB C 28.79 0.05 1 943 497 230 GLU N N 127.01 0.05 1 944 498 231 VAL H H 8.26 0.02 1 945 498 231 VAL C C 175.20 0.05 1 946 498 231 VAL CA C 60.95 0.05 1 947 498 231 VAL CB C 33.76 0.05 1 948 498 231 VAL N N 128.35 0.05 1 949 501 234 LEU C C 177.29 0.05 1 950 501 234 LEU CA C 54.12 0.05 1 951 501 234 LEU CB C 40.68 0.05 1 952 502 235 THR H H 7.83 0.02 1 953 502 235 THR C C 172.98 0.05 1 954 502 235 THR CA C 60.23 0.05 1 955 502 235 THR CB C 68.28 0.05 1 956 502 235 THR N N 111.18 0.05 1 957 503 236 ASP H H 8.07 0.02 1 958 503 236 ASP C C 176.03 0.05 1 959 503 236 ASP CA C 50.79 0.05 1 960 503 236 ASP CB C 43.88 0.05 1 961 503 236 ASP N N 123.34 0.05 1 962 504 237 PRO CA C 64.87 0.05 1 963 504 237 PRO CB C 31.11 0.05 1 964 505 238 ILE H H 8.76 0.02 1 965 505 238 ILE C C 177.78 0.05 1 966 505 238 ILE CA C 62.19 0.05 1 967 505 238 ILE CB C 36.45 0.05 1 968 505 238 ILE N N 116.37 0.05 1 969 506 239 ASP H H 7.98 0.02 1 970 506 239 ASP C C 177.54 0.05 1 971 506 239 ASP CA C 57.80 0.05 1 972 506 239 ASP CB C 41.59 0.05 1 973 506 239 ASP N N 122.08 0.05 1 974 507 240 GLU H H 7.33 0.02 1 975 507 240 GLU C C 178.12 0.05 1 976 507 240 GLU CA C 59.26 0.05 1 977 507 240 GLU CB C 28.11 0.05 1 978 507 240 GLU N N 119.15 0.05 1 979 508 241 TYR H H 7.57 0.02 1 980 508 241 TYR C C 174.51 0.05 1 981 508 241 TYR CA C 59.47 0.05 1 982 508 241 TYR CB C 36.50 0.05 1 983 508 241 TYR N N 119.07 0.05 1 984 509 242 ALA C C 178.62 0.05 1 985 509 242 ALA CA C 55.13 0.05 1 986 509 242 ALA CB C 15.85 0.05 1 987 510 243 PHE H H 8.35 0.02 1 988 510 243 PHE C C 178.42 0.05 1 989 510 243 PHE CA C 60.47 0.05 1 990 510 243 PHE CB C 36.16 0.05 1 991 510 243 PHE N N 118.80 0.05 1 992 511 244 THR H H 8.12 0.02 1 993 511 244 THR C C 176.00 0.05 1 994 511 244 THR CA C 65.04 0.05 1 995 511 244 THR CB C 68.31 0.05 1 996 511 244 THR N N 113.29 0.05 1 997 512 245 GLN H H 7.08 0.02 1 998 512 245 GLN C C 176.86 0.05 1 999 512 245 GLN CA C 55.35 0.05 1 1000 512 245 GLN CB C 28.24 0.05 1 1001 512 245 GLN N N 117.35 0.05 1 1002 513 246 LEU H H 7.73 0.02 1 1003 513 246 LEU C C 178.16 0.05 1 1004 513 246 LEU CA C 56.82 0.05 1 1005 513 246 LEU CB C 41.66 0.05 1 1006 513 246 LEU N N 120.87 0.05 1 1007 514 247 LYS C C 177.10 0.05 1 1008 514 247 LYS CA C 61.30 0.05 1 1009 514 247 LYS CB C 30.28 0.05 1 1010 515 248 GLU H H 8.88 0.02 1 1011 515 248 GLU C C 173.21 0.05 1 1012 515 248 GLU CA C 54.00 0.05 1 1013 515 248 GLU CB C 32.39 0.05 1 1014 515 248 GLU N N 120.80 0.05 1 1015 516 249 PHE H H 8.52 0.02 1 1016 516 249 PHE C C 173.65 0.05 1 1017 516 249 PHE CA C 57.19 0.05 1 1018 516 249 PHE CB C 40.95 0.05 1 1019 516 249 PHE N N 120.47 0.05 1 1020 517 250 GLU H H 8.71 0.02 1 1021 517 250 GLU C C 176.10 0.05 1 1022 517 250 GLU CA C 56.22 0.05 1 1023 517 250 GLU CB C 25.82 0.05 1 1024 517 250 GLU N N 126.20 0.05 1 1025 518 251 GLY H H 8.29 0.02 1 1026 518 251 GLY C C 174.04 0.05 1 1027 518 251 GLY CA C 44.59 0.05 1 1028 518 251 GLY N N 103.21 0.05 1 1029 519 252 LYS H H 7.81 0.02 1 1030 519 252 LYS C C 175.75 0.05 1 1031 519 252 LYS CA C 53.09 0.05 1 1032 519 252 LYS CB C 31.27 0.05 1 1033 519 252 LYS N N 120.94 0.05 1 1034 520 253 THR H H 8.23 0.02 1 1035 520 253 THR C C 173.71 0.05 1 1036 520 253 THR CA C 63.00 0.05 1 1037 520 253 THR CB C 68.63 0.05 1 1038 520 253 THR N N 118.35 0.05 1 1039 521 254 LEU H H 7.66 0.02 1 1040 521 254 LEU C C 177.22 0.05 1 1041 521 254 LEU CA C 55.24 0.05 1 1042 521 254 LEU CB C 40.37 0.05 1 1043 521 254 LEU N N 125.64 0.05 1 1044 522 255 VAL H H 7.72 0.02 1 1045 522 255 VAL C C 172.48 0.05 1 1046 522 255 VAL CA C 61.44 0.05 1 1047 522 255 VAL CB C 34.91 0.05 1 1048 522 255 VAL N N 113.00 0.05 1 1049 523 256 ASP H H 8.11 0.02 1 1050 523 256 ASP C C 178.56 0.05 1 1051 523 256 ASP CA C 51.16 0.05 1 1052 523 256 ASP CB C 39.81 0.05 1 1053 523 256 ASP N N 129.58 0.05 1 1054 524 257 ILE H H 8.06 0.02 1 1055 524 257 ILE C C 175.72 0.05 1 1056 524 257 ILE CA C 63.26 0.05 1 1057 524 257 ILE CB C 36.22 0.05 1 1058 524 257 ILE N N 119.66 0.05 1 1059 525 258 THR H H 8.72 0.02 1 1060 525 258 THR C C 174.16 0.05 1 1061 525 258 THR CA C 61.76 0.05 1 1062 525 258 THR CB C 68.50 0.05 1 1063 525 258 THR N N 113.18 0.05 1 1064 526 259 LYS H H 6.76 0.02 1 1065 526 259 LYS C C 175.55 0.05 1 1066 526 259 LYS CA C 54.47 0.05 1 1067 526 259 LYS CB C 32.81 0.05 1 1068 526 259 LYS N N 121.68 0.05 1 1069 527 260 ASP H H 8.02 0.02 1 1070 527 260 ASP C C 181.00 0.05 1 1071 527 260 ASP CA C 56.11 0.05 1 1072 527 260 ASP CB C 41.41 0.05 1 1073 527 260 ASP N N 127.40 0.05 1 stop_ save_