data_16367 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR ; _BMRB_accession_number 16367 _BMRB_flat_file_name bmr16367.str _Entry_type original _Submission_date 2009-06-26 _Accession_date 2009-06-26 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Chemical shifts for murine CFTR NBD1 (389-673) G550E/R553M/R555K mutant' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kanelis Voula . . 2 Hudson Rhea P. . 3 Thibodeau Patrick H. . 4 Thomas Phillip J. . 5 Forman-Kay Julie D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 197 "13C chemical shifts" 593 "15N chemical shifts" 197 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-11-06 update BMRB 'switch the chemical shifts of H and N atoms' 2010-01-21 update BMRB 'complete entry citation' 2009-12-11 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19927121 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kanelis Voula . . 2 Hudson Rhea P. . 3 Thibodeau Patrick H. . 4 Thomas Philip J. . 5 Forman-Kay Julie D. . stop_ _Journal_abbreviation 'EMBO J.' _Journal_name_full 'The EMBO journal' _Journal_volume 29 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 263 _Page_last 277 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'CFTR NBD1-RE monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NBD1-RE $entity stop_ _System_molecular_weight 32011.5 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CFTR_NBD1-RE_G550E/R553M/R555K _Molecular_mass 32011.5 _Mol_thiol_state 'all free' loop_ _Biological_function 'chloride channel' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 285 _Mol_residue_sequence ; TTGIIMENVTAFWEEGFGEL LEKVQQSNGDRKHSSDENNV SFSHLCLVGNPVLKNINLNI EKGEMLAITGSTGSGKTSLL MLILGELEASEGIIKHSGRV SFCSQFSWIMPGTIKENIIF GVSYDEYRYKSVVKACQLQQ DITKFAEQDNTVLGEGGVTL SEGQMAKISLARAVYKDADL YLLDSPFGYLDVFTEEQVFE SCVCKLMANKTRILVTSKME HLRKADKILILHQGSSYFYG TFSELQSLRPDFSSKLMGYD TFDQFTEERRSSILTETLRR FSVDD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 389 THR 2 390 THR 3 391 GLY 4 392 ILE 5 393 ILE 6 394 MET 7 395 GLU 8 396 ASN 9 397 VAL 10 398 THR 11 399 ALA 12 400 PHE 13 401 TRP 14 402 GLU 15 403 GLU 16 404 GLY 17 405 PHE 18 406 GLY 19 407 GLU 20 408 LEU 21 409 LEU 22 410 GLU 23 411 LYS 24 412 VAL 25 413 GLN 26 414 GLN 27 415 SER 28 416 ASN 29 417 GLY 30 418 ASP 31 419 ARG 32 420 LYS 33 421 HIS 34 422 SER 35 423 SER 36 424 ASP 37 425 GLU 38 426 ASN 39 427 ASN 40 428 VAL 41 429 SER 42 430 PHE 43 431 SER 44 432 HIS 45 433 LEU 46 434 CYS 47 435 LEU 48 436 VAL 49 437 GLY 50 438 ASN 51 439 PRO 52 440 VAL 53 441 LEU 54 442 LYS 55 443 ASN 56 444 ILE 57 445 ASN 58 446 LEU 59 447 ASN 60 448 ILE 61 449 GLU 62 450 LYS 63 451 GLY 64 452 GLU 65 453 MET 66 454 LEU 67 455 ALA 68 456 ILE 69 457 THR 70 458 GLY 71 459 SER 72 460 THR 73 461 GLY 74 462 SER 75 463 GLY 76 464 LYS 77 465 THR 78 466 SER 79 467 LEU 80 468 LEU 81 469 MET 82 470 LEU 83 471 ILE 84 472 LEU 85 473 GLY 86 474 GLU 87 475 LEU 88 476 GLU 89 477 ALA 90 478 SER 91 479 GLU 92 480 GLY 93 481 ILE 94 482 ILE 95 483 LYS 96 484 HIS 97 485 SER 98 486 GLY 99 487 ARG 100 488 VAL 101 489 SER 102 490 PHE 103 491 CYS 104 492 SER 105 493 GLN 106 494 PHE 107 495 SER 108 496 TRP 109 497 ILE 110 498 MET 111 499 PRO 112 500 GLY 113 501 THR 114 502 ILE 115 503 LYS 116 504 GLU 117 505 ASN 118 506 ILE 119 507 ILE 120 508 PHE 121 509 GLY 122 510 VAL 123 511 SER 124 512 TYR 125 513 ASP 126 514 GLU 127 515 TYR 128 516 ARG 129 517 TYR 130 518 LYS 131 519 SER 132 520 VAL 133 521 VAL 134 522 LYS 135 523 ALA 136 524 CYS 137 525 GLN 138 526 LEU 139 527 GLN 140 528 GLN 141 529 ASP 142 530 ILE 143 531 THR 144 532 LYS 145 533 PHE 146 534 ALA 147 535 GLU 148 536 GLN 149 537 ASP 150 538 ASN 151 539 THR 152 540 VAL 153 541 LEU 154 542 GLY 155 543 GLU 156 544 GLY 157 545 GLY 158 546 VAL 159 547 THR 160 548 LEU 161 549 SER 162 550 GLU 163 551 GLY 164 552 GLN 165 553 MET 166 554 ALA 167 555 LYS 168 556 ILE 169 557 SER 170 558 LEU 171 559 ALA 172 560 ARG 173 561 ALA 174 562 VAL 175 563 TYR 176 564 LYS 177 565 ASP 178 566 ALA 179 567 ASP 180 568 LEU 181 569 TYR 182 570 LEU 183 571 LEU 184 572 ASP 185 573 SER 186 574 PRO 187 575 PHE 188 576 GLY 189 577 TYR 190 578 LEU 191 579 ASP 192 580 VAL 193 581 PHE 194 582 THR 195 583 GLU 196 584 GLU 197 585 GLN 198 586 VAL 199 587 PHE 200 588 GLU 201 589 SER 202 590 CYS 203 591 VAL 204 592 CYS 205 593 LYS 206 594 LEU 207 595 MET 208 596 ALA 209 597 ASN 210 598 LYS 211 599 THR 212 600 ARG 213 601 ILE 214 602 LEU 215 603 VAL 216 604 THR 217 605 SER 218 606 LYS 219 607 MET 220 608 GLU 221 609 HIS 222 610 LEU 223 611 ARG 224 612 LYS 225 613 ALA 226 614 ASP 227 615 LYS 228 616 ILE 229 617 LEU 230 618 ILE 231 619 LEU 232 620 HIS 233 621 GLN 234 622 GLY 235 623 SER 236 624 SER 237 625 TYR 238 626 PHE 239 627 TYR 240 628 GLY 241 629 THR 242 630 PHE 243 631 SER 244 632 GLU 245 633 LEU 246 634 GLN 247 635 SER 248 636 LEU 249 637 ARG 250 638 PRO 251 639 ASP 252 640 PHE 253 641 SER 254 642 SER 255 643 LYS 256 644 LEU 257 645 MET 258 646 GLY 259 647 TYR 260 648 ASP 261 649 THR 262 650 PHE 263 651 ASP 264 652 GLN 265 653 PHE 266 654 THR 267 655 GLU 268 656 GLU 269 657 ARG 270 658 ARG 271 659 SER 272 660 SER 273 661 ILE 274 662 LEU 275 663 THR 276 664 GLU 277 665 THR 278 666 LEU 279 667 ARG 280 668 ARG 281 669 PHE 282 670 SER 283 671 VAL 284 672 ASP 285 673 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-05 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 BMRB 16393 "CFTR NBD1-RE" 100.00 285 98.95 99.30 0.00e+00 BMRB 16394 "deltaF508 CFTR NBD1-RE" 100.00 284 98.60 98.95 0.00e+00 PDB 1Q3H "Mouse Cftr Nbd1 With Amp.Pnp" 100.00 286 98.95 99.30 0.00e+00 PDB 1R0W "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) Apo" 100.00 286 98.95 99.30 0.00e+00 PDB 1R0X "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) With Atp" 100.00 286 98.95 99.30 0.00e+00 PDB 1R0Y "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) With Adp" 100.00 286 98.95 99.30 0.00e+00 PDB 1R0Z "Phosphorylated Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide-Binding Domain One (Nbd1) With Atp" 100.00 286 97.54 97.89 0.00e+00 PDB 1R10 "Cystic Fibrosis Transmembrane Conductance Regulator (Cftr) Nucleotide- Binding Domain One (Nbd1) With Atp, I4122 Space Group" 100.00 286 98.95 99.30 0.00e+00 PDB 1XF9 "Structure Of Nbd1 From Murine Cftr- F508s Mutant" 98.95 283 98.58 98.94 0.00e+00 PDB 1XFA "Structure Of Nbd1 From Murine Cftr- F508r Mutant" 98.95 283 98.58 98.94 0.00e+00 PDB 3SI7 "The Crystal Structure Of The Nbd1 Domain Of The Mouse Cftr Protein, Deltaf508 Mutant" 100.00 285 98.60 98.95 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity Mouse 10090 Eukaryota Metazoa Mus musculus 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 $entity 'recombinant technology' . Escherichia coli . pET-His-SUMO 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 $entity 0.6 mM '[U-100% 13C; U-100% 15N; 50% 2H]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCO_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO TROSY' _Sample_label $sample_1 save_ save_3D_HNCA_TROSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA TROSY' _Sample_label $sample_1 save_ save_3D_HNCACB_TROSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB TROSY' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_TROSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA TROSY' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_TROSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB TROSY' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_TROSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO TROSY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_TROSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC TROSY' _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' 0.170 . M pH 7.0 . pH pressure 1 . atm temperature 293 . 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 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0 internal 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_ _Software_label $NMRPipe stop_ loop_ _Experiment_label '3D HNCO TROSY' '3D HNCA TROSY' '3D HNCACB TROSY' '3D HN(CO)CA TROSY' '3D HN(CO)CACB TROSY' '3D HN(CA)CO TROSY' '2D 1H-15N HSQC TROSY' 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 NBD1-RE _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 1 389 1 THR C C 173.98 0.30 1 2 389 1 THR CA C 61.65 0.30 1 3 389 1 THR CB C 44.79 0.30 1 4 390 2 THR H H 8.21 0.02 1 5 390 2 THR C C 174.46 0.30 1 6 390 2 THR CA C 61.59 0.30 1 7 390 2 THR CB C 45.60 0.30 1 8 390 2 THR N N 117.13 0.30 1 9 391 3 GLY H H 8.61 0.02 1 10 391 3 GLY C C 172.76 0.30 1 11 391 3 GLY CA C 44.65 0.30 1 12 391 3 GLY N N 114.22 0.30 1 13 392 4 ILE H H 8.57 0.02 1 14 392 4 ILE C C 172.17 0.30 1 15 392 4 ILE CA C 59.82 0.30 1 16 392 4 ILE CB C 39.26 0.30 1 17 392 4 ILE N N 120.42 0.30 1 18 393 5 ILE H H 8.53 0.02 1 19 393 5 ILE C C 175.28 0.30 1 20 393 5 ILE CA C 59.24 0.30 1 21 393 5 ILE CB C 42.16 0.30 1 22 393 5 ILE N N 126.40 0.30 1 23 394 6 MET H H 8.90 0.02 1 24 394 6 MET C C 175.12 0.30 1 25 394 6 MET CA C 55.13 0.30 1 26 394 6 MET CB C 34.69 0.30 1 27 394 6 MET N N 123.88 0.30 1 28 395 7 GLU H H 9.20 0.02 1 29 395 7 GLU C C 174.21 0.30 1 30 395 7 GLU CA C 54.14 0.30 1 31 395 7 GLU CB C 31.39 0.30 1 32 395 7 GLU N N 124.96 0.30 1 33 396 8 ASN H H 8.89 0.02 1 34 396 8 ASN C C 174.21 0.30 1 35 396 8 ASN CA C 53.72 0.30 1 36 396 8 ASN CB C 37.73 0.30 1 37 396 8 ASN N N 124.80 0.30 1 38 397 9 VAL H H 8.54 0.02 1 39 397 9 VAL C C 176.28 0.30 1 40 397 9 VAL CA C 63.02 0.30 1 41 397 9 VAL CB C 32.06 0.30 1 42 397 9 VAL N N 121.02 0.30 1 43 398 10 THR H H 7.82 0.02 1 44 398 10 THR C C 172.80 0.30 1 45 398 10 THR CA C 60.62 0.30 1 46 398 10 THR CB C 47.30 0.30 1 47 398 10 THR N N 124.47 0.30 1 48 399 11 ALA H H 8.67 0.02 1 49 399 11 ALA C C 173.87 0.30 1 50 399 11 ALA CA C 50.75 0.30 1 51 399 11 ALA CB C 48.06 0.30 1 52 399 11 ALA N N 127.48 0.30 1 53 400 12 PHE H H 9.09 0.02 1 54 400 12 PHE C C 174.93 0.30 1 55 400 12 PHE CA C 56.35 0.30 1 56 400 12 PHE CB C 41.44 0.30 1 57 400 12 PHE N N 120.52 0.30 1 58 401 13 TRP H H 8.76 0.02 1 59 401 13 TRP CA C 58.07 0.30 1 60 401 13 TRP CB C 30.16 0.30 1 61 401 13 TRP N N 122.28 0.30 1 62 422 34 SER C C 174.71 0.30 1 63 422 34 SER CA C 58.11 0.30 1 64 422 34 SER CB C 39.25 0.30 1 65 423 35 SER H H 8.48 0.02 1 66 423 35 SER C C 174.40 0.30 1 67 423 35 SER CA C 58.39 0.30 1 68 423 35 SER CB C 39.32 0.30 1 69 423 35 SER N N 118.67 0.30 1 70 424 36 ASP H H 8.28 0.02 1 71 424 36 ASP C C 176.55 0.30 1 72 424 36 ASP CA C 54.26 0.30 1 73 424 36 ASP CB C 40.78 0.30 1 74 424 36 ASP N N 122.75 0.30 1 75 425 37 GLU H H 8.29 0.02 1 76 425 37 GLU C C 176.42 0.30 1 77 425 37 GLU CA C 56.72 0.30 1 78 425 37 GLU CB C 29.36 0.30 1 79 425 37 GLU N N 121.41 0.30 1 80 426 38 ASN H H 8.36 0.02 1 81 426 38 ASN C C 174.91 0.30 1 82 426 38 ASN CA C 53.16 0.30 1 83 426 38 ASN CB C 38.61 0.30 1 84 426 38 ASN N N 119.15 0.30 1 85 427 39 ASN H H 8.21 0.02 1 86 427 39 ASN C C 175.25 0.30 1 87 427 39 ASN CA C 53.15 0.30 1 88 427 39 ASN CB C 38.53 0.30 1 89 427 39 ASN N N 119.82 0.30 1 90 428 40 VAL H H 8.04 0.02 1 91 428 40 VAL C C 176.18 0.30 1 92 428 40 VAL CA C 62.16 0.30 1 93 428 40 VAL CB C 32.04 0.30 1 94 428 40 VAL N N 120.83 0.30 1 95 429 41 SER H H 8.26 0.02 1 96 429 41 SER C C 174.34 0.30 1 97 429 41 SER CA C 58.06 0.30 1 98 429 41 SER CB C 39.30 0.30 1 99 429 41 SER N N 119.53 0.30 1 100 430 42 PHE H H 8.21 0.02 1 101 430 42 PHE C C 175.97 0.30 1 102 430 42 PHE CA C 57.71 0.30 1 103 430 42 PHE CB C 39.16 0.30 1 104 430 42 PHE N N 122.76 0.30 1 105 431 43 SER H H 8.17 0.02 1 106 431 43 SER C C 174.47 0.30 1 107 431 43 SER CA C 58.51 0.30 1 108 431 43 SER CB C 39.10 0.30 1 109 431 43 SER N N 117.34 0.30 1 110 433 45 LEU C C 177.19 0.30 1 111 433 45 LEU CA C 55.05 0.30 1 112 434 46 CYS H H 8.30 0.02 1 113 434 46 CYS C C 175.87 0.30 1 114 434 46 CYS CA C 58.69 0.30 1 115 434 46 CYS CB C 27.48 0.30 1 116 434 46 CYS N N 120.55 0.30 1 117 435 47 LEU H H 8.09 0.02 1 118 435 47 LEU C C 177.19 0.30 1 119 435 47 LEU CA C 54.55 0.30 1 120 435 47 LEU CB C 41.45 0.30 1 121 435 47 LEU N N 124.64 0.30 1 122 436 48 VAL H H 7.97 0.02 1 123 436 48 VAL C C 176.43 0.30 1 124 436 48 VAL CA C 62.25 0.30 1 125 436 48 VAL CB C 32.22 0.30 1 126 436 48 VAL N N 120.02 0.30 1 127 437 49 GLY H H 8.38 0.02 1 128 437 49 GLY C C 173.20 0.30 1 129 437 49 GLY CA C 44.61 0.30 1 130 437 49 GLY N N 112.50 0.30 1 131 438 50 ASN H H 8.43 0.02 1 132 438 50 ASN C C 172.78 0.30 1 133 438 50 ASN CA C 50.49 0.30 1 134 438 50 ASN CB C 38.72 0.30 1 135 438 50 ASN N N 119.88 0.30 1 136 440 52 VAL C C 173.22 0.30 1 137 440 52 VAL CA C 61.43 0.30 1 138 441 53 LEU H H 6.91 0.02 1 139 441 53 LEU C C 175.64 0.30 1 140 441 53 LEU CA C 52.72 0.30 1 141 441 53 LEU CB C 46.24 0.30 1 142 441 53 LEU N N 119.68 0.30 1 143 442 54 LYS H H 8.55 0.02 1 144 442 54 LYS C C 173.31 0.30 1 145 442 54 LYS CA C 54.56 0.30 1 146 442 54 LYS CB C 34.80 0.30 1 147 442 54 LYS N N 121.36 0.30 1 148 443 55 ASN H H 7.84 0.02 1 149 443 55 ASN C C 172.74 0.30 1 150 443 55 ASN CA C 53.88 0.30 1 151 443 55 ASN CB C 37.34 0.30 1 152 443 55 ASN N N 122.40 0.30 1 153 444 56 ILE H H 9.37 0.02 1 154 444 56 ILE C C 175.52 0.30 1 155 444 56 ILE CA C 59.49 0.30 1 156 444 56 ILE CB C 35.37 0.30 1 157 444 56 ILE N N 120.16 0.30 1 158 445 57 ASN H H 7.40 0.02 1 159 445 57 ASN C C 173.23 0.30 1 160 445 57 ASN CA C 51.71 0.30 1 161 445 57 ASN CB C 42.40 0.30 1 162 445 57 ASN N N 123.12 0.30 1 163 446 58 LEU H H 8.69 0.02 1 164 446 58 LEU C C 175.61 0.30 1 165 446 58 LEU CA C 55.20 0.30 1 166 446 58 LEU CB C 45.04 0.30 1 167 446 58 LEU N N 116.79 0.30 1 168 447 59 ASN H H 7.95 0.02 1 169 447 59 ASN C C 172.35 0.30 1 170 447 59 ASN CA C 53.93 0.30 1 171 447 59 ASN CB C 38.76 0.30 1 172 447 59 ASN N N 119.74 0.30 1 173 448 60 ILE H H 8.89 0.02 1 174 448 60 ILE C C 176.20 0.30 1 175 448 60 ILE CA C 57.69 0.30 1 176 448 60 ILE CB C 37.20 0.30 1 177 448 60 ILE N N 124.80 0.30 1 178 449 61 GLU H H 9.05 0.02 1 179 449 61 GLU C C 175.65 0.30 1 180 449 61 GLU CA C 54.73 0.30 1 181 449 61 GLU CB C 30.19 0.30 1 182 449 61 GLU N N 128.53 0.30 1 183 450 62 LYS H H 8.31 0.02 1 184 450 62 LYS C C 178.39 0.30 1 185 450 62 LYS CA C 57.45 0.30 1 186 450 62 LYS CB C 31.48 0.30 1 187 450 62 LYS N N 120.50 0.30 1 188 451 63 GLY H H 8.81 0.02 1 189 451 63 GLY C C 173.87 0.30 1 190 451 63 GLY CA C 44.55 0.30 1 191 451 63 GLY N N 114.77 0.30 1 192 452 64 GLU H H 7.96 0.02 1 193 452 64 GLU C C 174.83 0.30 1 194 452 64 GLU CA C 56.09 0.30 1 195 452 64 GLU CB C 31.34 0.30 1 196 452 64 GLU N N 120.53 0.30 1 197 453 65 MET H H 9.70 0.02 1 198 453 65 MET C C 175.34 0.30 1 199 453 65 MET CA C 53.62 0.30 1 200 453 65 MET N N 118.94 0.30 1 201 454 66 LEU H H 9.06 0.02 1 202 454 66 LEU C C 174.54 0.30 1 203 454 66 LEU CA C 52.12 0.30 1 204 454 66 LEU CB C 43.43 0.30 1 205 454 66 LEU N N 130.84 0.30 1 206 455 67 ALA H H 8.95 0.02 1 207 455 67 ALA C C 175.61 0.30 1 208 455 67 ALA CA C 49.33 0.30 1 209 455 67 ALA CB C 45.20 0.30 1 210 455 67 ALA N N 130.04 0.30 1 211 456 68 ILE H H 9.31 0.02 1 212 456 68 ILE C C 175.49 0.30 1 213 456 68 ILE CA C 59.14 0.30 1 214 456 68 ILE CB C 40.06 0.30 1 215 456 68 ILE N N 122.64 0.30 1 216 457 69 THR H H 9.08 0.02 1 217 457 69 THR CA C 62.23 0.30 1 218 457 69 THR CB C 45.27 0.30 1 219 457 69 THR N N 120.78 0.30 1 220 466 78 SER C C 174.14 0.30 1 221 466 78 SER CA C 64.58 0.30 1 222 467 79 LEU H H 8.15 0.02 1 223 467 79 LEU C C 178.89 0.30 1 224 467 79 LEU CA C 58.73 0.30 1 225 467 79 LEU CB C 39.71 0.30 1 226 467 79 LEU N N 124.11 0.30 1 227 468 80 LEU H H 7.22 0.02 1 228 468 80 LEU C C 179.07 0.30 1 229 468 80 LEU CA C 57.98 0.30 1 230 468 80 LEU CB C 38.57 0.30 1 231 468 80 LEU N N 118.32 0.30 1 232 469 81 MET H H 8.34 0.02 1 233 469 81 MET C C 179.18 0.30 1 234 469 81 MET CA C 56.55 0.30 1 235 469 81 MET N N 117.88 0.30 1 236 470 82 LEU H H 7.89 0.02 1 237 470 82 LEU C C 179.92 0.30 1 238 470 82 LEU CA C 56.72 0.30 1 239 470 82 LEU CB C 41.32 0.30 1 240 470 82 LEU N N 123.77 0.30 1 241 471 83 ILE H H 7.30 0.02 1 242 471 83 ILE C C 176.68 0.30 1 243 471 83 ILE CA C 64.66 0.30 1 244 471 83 ILE CB C 36.07 0.30 1 245 471 83 ILE N N 122.41 0.30 1 246 472 84 LEU H H 7.76 0.02 1 247 472 84 LEU C C 177.10 0.30 1 248 472 84 LEU CA C 55.72 0.30 1 249 472 84 LEU CB C 42.94 0.30 1 250 472 84 LEU N N 117.17 0.30 1 251 473 85 GLY H H 7.46 0.02 1 252 473 85 GLY C C 174.56 0.30 1 253 473 85 GLY CA C 44.46 0.30 1 254 473 85 GLY N N 105.55 0.30 1 255 474 86 GLU H H 7.57 0.02 1 256 474 86 GLU C C 174.61 0.30 1 257 474 86 GLU CA C 56.66 0.30 1 258 474 86 GLU CB C 29.94 0.30 1 259 474 86 GLU N N 119.45 0.30 1 260 475 87 LEU H H 6.67 0.02 1 261 475 87 LEU C C 174.06 0.30 1 262 475 87 LEU CA C 52.57 0.30 1 263 475 87 LEU CB C 43.28 0.30 1 264 475 87 LEU N N 119.29 0.30 1 265 476 88 GLU H H 8.16 0.02 1 266 476 88 GLU C C 175.49 0.30 1 267 476 88 GLU CA C 54.48 0.30 1 268 476 88 GLU CB C 31.06 0.30 1 269 476 88 GLU N N 123.35 0.30 1 270 477 89 ALA H H 8.78 0.02 1 271 477 89 ALA C C 177.63 0.30 1 272 477 89 ALA CA C 51.57 0.30 1 273 477 89 ALA CB C 42.51 0.30 1 274 477 89 ALA N N 125.87 0.30 1 275 478 90 SER H H 8.87 0.02 1 276 478 90 SER CA C 59.92 0.30 1 277 478 90 SER CB C 39.33 0.30 1 278 478 90 SER N N 120.61 0.30 1 279 479 91 GLU H H 7.82 0.02 1 280 479 91 GLU C C 174.57 0.30 1 281 479 91 GLU CA C 54.88 0.30 1 282 479 91 GLU CB C 33.24 0.30 1 283 479 91 GLU N N 119.79 0.30 1 284 480 92 GLY H H 8.26 0.02 1 285 480 92 GLY C C 173.77 0.30 1 286 480 92 GLY CA C 44.45 0.30 1 287 480 92 GLY N N 108.76 0.30 1 288 481 93 ILE H H 8.01 0.02 1 289 481 93 ILE C C 174.03 0.30 1 290 481 93 ILE CA C 59.29 0.30 1 291 481 93 ILE CB C 41.22 0.30 1 292 481 93 ILE N N 118.08 0.30 1 293 482 94 ILE H H 8.27 0.02 1 294 482 94 ILE C C 175.21 0.30 1 295 482 94 ILE CA C 59.66 0.30 1 296 482 94 ILE CB C 39.96 0.30 1 297 482 94 ILE N N 125.31 0.30 1 298 483 95 LYS H H 9.09 0.02 1 299 483 95 LYS C C 174.68 0.30 1 300 483 95 LYS CA C 54.87 0.30 1 301 483 95 LYS CB C 35.08 0.30 1 302 483 95 LYS N N 127.22 0.30 1 303 484 96 HIS H H 7.91 0.02 1 304 484 96 HIS C C 174.56 0.30 1 305 484 96 HIS CA C 55.96 0.30 1 306 484 96 HIS CB C 31.34 0.30 1 307 484 96 HIS N N 118.66 0.30 1 308 486 98 GLY C C 173.99 0.30 1 309 486 98 GLY CA C 44.94 0.30 1 310 487 99 ARG H H 8.43 0.02 1 311 487 99 ARG C C 175.42 0.30 1 312 487 99 ARG CA C 55.34 0.30 1 313 487 99 ARG CB C 29.17 0.30 1 314 487 99 ARG N N 122.52 0.30 1 315 488 100 VAL H H 8.46 0.02 1 316 488 100 VAL C C 175.12 0.30 1 317 488 100 VAL CA C 59.80 0.30 1 318 488 100 VAL CB C 34.77 0.30 1 319 488 100 VAL N N 124.87 0.30 1 320 489 101 SER H H 8.11 0.02 1 321 489 101 SER C C 172.76 0.30 1 322 489 101 SER CA C 55.50 0.30 1 323 489 101 SER CB C 40.01 0.30 1 324 489 101 SER N N 119.14 0.30 1 325 490 102 PHE H H 8.86 0.02 1 326 490 102 PHE C C 173.22 0.30 1 327 490 102 PHE CA C 54.90 0.30 1 328 490 102 PHE CB C 43.12 0.30 1 329 490 102 PHE N N 130.12 0.30 1 330 491 103 CYS H H 8.78 0.02 1 331 491 103 CYS C C 171.02 0.30 1 332 491 103 CYS CA C 56.67 0.30 1 333 491 103 CYS CB C 28.54 0.30 1 334 491 103 CYS N N 130.58 0.30 1 335 492 104 SER H H 8.00 0.02 1 336 492 104 SER C C 173.41 0.30 1 337 492 104 SER CA C 56.90 0.30 1 338 492 104 SER N N 121.84 0.30 1 339 493 105 GLN H H 9.13 0.02 1 340 493 105 GLN C C 176.19 0.30 1 341 493 105 GLN CA C 57.45 0.30 1 342 493 105 GLN CB C 28.04 0.30 1 343 493 105 GLN N N 123.40 0.30 1 344 494 106 PHE H H 7.85 0.02 1 345 494 106 PHE C C 175.23 0.30 1 346 494 106 PHE CA C 55.33 0.30 1 347 494 106 PHE CB C 38.51 0.30 1 348 494 106 PHE N N 118.48 0.30 1 349 495 107 SER H H 8.38 0.02 1 350 495 107 SER C C 173.19 0.30 1 351 495 107 SER CA C 57.80 0.30 1 352 495 107 SER CB C 39.94 0.30 1 353 495 107 SER N N 121.82 0.30 1 354 496 108 TRP H H 7.49 0.02 1 355 496 108 TRP C C 174.35 0.30 1 356 496 108 TRP CA C 55.23 0.30 1 357 496 108 TRP CB C 30.70 0.30 1 358 496 108 TRP N N 116.85 0.30 1 359 497 109 ILE H H 8.68 0.02 1 360 497 109 ILE C C 174.78 0.30 1 361 497 109 ILE CA C 58.22 0.30 1 362 497 109 ILE CB C 41.27 0.30 1 363 497 109 ILE N N 116.81 0.30 1 364 498 110 MET H H 9.30 0.02 1 365 498 110 MET C C 173.15 0.30 1 366 498 110 MET CA C 51.73 0.30 1 367 498 110 MET CB C 33.13 0.30 1 368 498 110 MET N N 124.77 0.30 1 369 499 111 PRO CA C 63.10 0.30 1 370 499 111 PRO CB C 30.56 0.30 1 371 500 112 GLY H H 7.78 0.02 1 372 500 112 GLY C C 172.98 0.30 1 373 500 112 GLY CA C 43.49 0.30 1 374 500 112 GLY N N 112.97 0.30 1 375 501 113 THR H H 9.05 0.02 1 376 501 113 THR C C 177.94 0.30 1 377 501 113 THR CA C 60.90 0.30 1 378 501 113 THR CB C 46.79 0.30 1 379 501 113 THR N N 111.63 0.30 1 380 502 114 ILE H H 7.77 0.02 1 381 502 114 ILE C C 176.71 0.30 1 382 502 114 ILE CA C 66.97 0.30 1 383 502 114 ILE CB C 37.61 0.30 1 384 502 114 ILE N N 122.99 0.30 1 385 503 115 LYS H H 8.26 0.02 1 386 503 115 LYS C C 178.70 0.30 1 387 503 115 LYS CA C 59.69 0.30 1 388 503 115 LYS CB C 31.97 0.30 1 389 503 115 LYS N N 119.53 0.30 1 390 504 116 GLU H H 8.11 0.02 1 391 504 116 GLU C C 180.18 0.30 1 392 504 116 GLU CA C 58.70 0.30 1 393 504 116 GLU CB C 28.80 0.30 1 394 504 116 GLU N N 117.24 0.30 1 395 505 117 ASN H H 8.24 0.02 1 396 505 117 ASN C C 176.06 0.30 1 397 505 117 ASN CA C 57.48 0.30 1 398 505 117 ASN CB C 40.76 0.30 1 399 505 117 ASN N N 118.25 0.30 1 400 506 118 ILE H H 7.69 0.02 1 401 506 118 ILE C C 175.23 0.30 1 402 506 118 ILE CA C 65.19 0.30 1 403 506 118 ILE CB C 38.12 0.30 1 404 506 118 ILE N N 119.36 0.30 1 405 507 119 ILE H H 7.97 0.02 1 406 507 119 ILE C C 176.11 0.30 1 407 507 119 ILE CA C 62.24 0.30 1 408 507 119 ILE CB C 35.53 0.30 1 409 507 119 ILE N N 111.58 0.30 1 410 508 120 PHE H H 7.58 0.02 1 411 508 120 PHE C C 175.78 0.30 1 412 508 120 PHE CA C 58.90 0.30 1 413 508 120 PHE CB C 39.46 0.30 1 414 508 120 PHE N N 122.26 0.30 1 415 509 121 GLY H H 8.38 0.02 1 416 509 121 GLY C C 174.31 0.30 1 417 509 121 GLY CA C 45.33 0.30 1 418 509 121 GLY N N 109.74 0.30 1 419 510 122 VAL H H 8.21 0.02 1 420 510 122 VAL C C 175.55 0.30 1 421 510 122 VAL CA C 60.62 0.30 1 422 510 122 VAL CB C 32.46 0.30 1 423 510 122 VAL N N 121.83 0.30 1 424 511 123 SER H H 8.20 0.02 1 425 511 123 SER CA C 59.18 0.30 1 426 511 123 SER CB C 63.55 0.30 1 427 511 123 SER N N 117.78 0.30 1 428 523 135 ALA C C 179.12 0.30 1 429 523 135 ALA CA C 54.83 0.30 1 430 524 136 CYS H H 7.85 0.02 1 431 524 136 CYS C C 171.08 0.30 1 432 524 136 CYS CA C 60.73 0.30 1 433 524 136 CYS CB C 26.96 0.30 1 434 524 136 CYS N N 112.27 0.30 1 435 525 137 GLN H H 7.71 0.02 1 436 525 137 GLN C C 176.10 0.30 1 437 525 137 GLN CA C 54.95 0.30 1 438 525 137 GLN CB C 47.71 0.30 1 439 525 137 GLN N N 109.75 0.30 1 440 526 138 LEU H H 8.03 0.02 1 441 526 138 LEU C C 177.69 0.30 1 442 526 138 LEU CA C 54.01 0.30 1 443 526 138 LEU CB C 45.46 0.30 1 444 526 138 LEU N N 117.03 0.30 1 445 527 139 GLN H H 7.88 0.02 1 446 527 139 GLN C C 178.05 0.30 1 447 527 139 GLN CA C 59.67 0.30 1 448 527 139 GLN CB C 27.84 0.30 1 449 527 139 GLN N N 123.20 0.30 1 450 528 140 GLN H H 8.72 0.02 1 451 528 140 GLN C C 177.58 0.30 1 452 528 140 GLN CA C 57.97 0.30 1 453 528 140 GLN CB C 27.25 0.30 1 454 528 140 GLN N N 117.45 0.30 1 455 529 141 ASP H H 7.60 0.02 1 456 529 141 ASP C C 177.76 0.30 1 457 529 141 ASP CA C 56.68 0.30 1 458 529 141 ASP CB C 41.16 0.30 1 459 529 141 ASP N N 118.99 0.30 1 460 530 142 ILE H H 7.91 0.02 1 461 530 142 ILE C C 177.58 0.30 1 462 530 142 ILE CA C 65.75 0.30 1 463 530 142 ILE CB C 37.56 0.30 1 464 530 142 ILE N N 117.32 0.30 1 465 531 143 THR H H 7.64 0.02 1 466 531 143 THR C C 175.05 0.30 1 467 531 143 THR CA C 64.43 0.30 1 468 531 143 THR CB C 44.82 0.30 1 469 531 143 THR N N 109.85 0.30 1 470 532 144 LYS H H 6.99 0.02 1 471 532 144 LYS C C 177.57 0.30 1 472 532 144 LYS CA C 56.60 0.30 1 473 532 144 LYS CB C 31.91 0.30 1 474 532 144 LYS N N 118.77 0.30 1 475 533 145 PHE H H 7.29 0.02 1 476 533 145 PHE C C 178.81 0.30 1 477 533 145 PHE CA C 56.78 0.30 1 478 533 145 PHE CB C 39.84 0.30 1 479 533 145 PHE N N 119.84 0.30 1 480 534 146 ALA H H 9.24 0.02 1 481 534 146 ALA C C 179.49 0.30 1 482 534 146 ALA CA C 55.69 0.30 1 483 534 146 ALA CB C 42.75 0.30 1 484 534 146 ALA N N 128.84 0.30 1 485 535 147 GLU H H 8.13 0.02 1 486 535 147 GLU C C 176.55 0.30 1 487 535 147 GLU CA C 54.66 0.30 1 488 535 147 GLU CB C 28.30 0.30 1 489 535 147 GLU N N 112.61 0.30 1 490 536 148 GLN H H 8.00 0.02 1 491 536 148 GLN C C 177.63 0.30 1 492 536 148 GLN CA C 57.20 0.30 1 493 536 148 GLN CB C 49.59 0.30 1 494 536 148 GLN N N 116.59 0.30 1 495 537 149 ASP H H 9.05 0.02 1 496 537 149 ASP C C 174.33 0.30 1 497 537 149 ASP CA C 55.37 0.30 1 498 537 149 ASP CB C 39.46 0.30 1 499 537 149 ASP N N 122.39 0.30 1 500 538 150 ASN H H 8.12 0.02 1 501 538 150 ASN C C 173.46 0.30 1 502 538 150 ASN CA C 52.40 0.30 1 503 538 150 ASN CB C 37.80 0.30 1 504 538 150 ASN N N 114.18 0.30 1 505 539 151 THR H H 7.33 0.02 1 506 539 151 THR C C 173.24 0.30 1 507 539 151 THR CA C 64.59 0.30 1 508 539 151 THR CB C 44.88 0.30 1 509 539 151 THR N N 119.78 0.30 1 510 540 152 VAL H H 8.43 0.02 1 511 540 152 VAL C C 174.49 0.30 1 512 540 152 VAL CA C 63.80 0.30 1 513 540 152 VAL CB C 31.59 0.30 1 514 540 152 VAL N N 128.85 0.30 1 515 541 153 LEU H H 8.57 0.02 1 516 541 153 LEU C C 177.28 0.30 1 517 541 153 LEU CA C 52.61 0.30 1 518 541 153 LEU CB C 42.56 0.30 1 519 541 153 LEU N N 127.38 0.30 1 520 542 154 GLY H H 8.39 0.02 1 521 542 154 GLY C C 174.42 0.30 1 522 542 154 GLY CA C 43.47 0.30 1 523 542 154 GLY N N 108.48 0.30 1 524 543 155 GLU H H 8.55 0.02 1 525 543 155 GLU C C 178.06 0.30 1 526 543 155 GLU CA C 57.68 0.30 1 527 543 155 GLU CB C 28.69 0.30 1 528 543 155 GLU N N 123.29 0.30 1 529 544 156 GLY H H 8.86 0.02 1 530 544 156 GLY C C 174.34 0.30 1 531 544 156 GLY CA C 44.94 0.30 1 532 544 156 GLY N N 114.22 0.30 1 533 545 157 GLY H H 8.18 0.02 1 534 545 157 GLY C C 173.99 0.30 1 535 545 157 GLY CA C 44.12 0.30 1 536 545 157 GLY N N 111.19 0.30 1 537 546 158 VAL H H 8.21 0.02 1 538 546 158 VAL C C 175.71 0.30 1 539 546 158 VAL CA C 61.39 0.30 1 540 546 158 VAL CB C 32.92 0.30 1 541 546 158 VAL N N 121.83 0.30 1 542 547 159 THR H H 8.43 0.02 1 543 547 159 THR C C 174.05 0.30 1 544 547 159 THR CA C 61.44 0.30 1 545 547 159 THR CB C 45.16 0.30 1 546 547 159 THR N N 121.06 0.30 1 547 548 160 LEU H H 8.63 0.02 1 548 548 160 LEU C C 176.84 0.30 1 549 548 160 LEU CA C 53.02 0.30 1 550 548 160 LEU CB C 43.05 0.30 1 551 548 160 LEU N N 126.69 0.30 1 552 549 161 SER H H 8.69 0.02 1 553 549 161 SER C C 175.25 0.30 1 554 549 161 SER CA C 56.66 0.30 1 555 549 161 SER CB C 40.92 0.30 1 556 549 161 SER N N 116.79 0.30 1 557 550 162 GLU H H 9.32 0.02 1 558 550 162 GLU C C 180.36 0.30 1 559 550 162 GLU CA C 59.86 0.30 1 560 550 162 GLU CB C 28.11 0.30 1 561 550 162 GLU N N 121.50 0.30 1 562 551 163 GLY H H 8.93 0.02 1 563 551 163 GLY C C 175.96 0.30 1 564 551 163 GLY CA C 46.70 0.30 1 565 551 163 GLY N N 108.93 0.30 1 566 552 164 GLN H H 7.72 0.02 1 567 552 164 GLN C C 178.78 0.30 1 568 552 164 GLN CA C 59.06 0.30 1 569 552 164 GLN CB C 28.48 0.30 1 570 552 164 GLN N N 121.30 0.30 1 571 553 165 MET H H 8.53 0.02 1 572 553 165 MET C C 178.62 0.30 1 573 553 165 MET CA C 59.20 0.30 1 574 553 165 MET CB C 32.09 0.30 1 575 553 165 MET N N 118.21 0.30 1 576 554 166 ALA H H 8.01 0.02 1 577 554 166 ALA C C 181.29 0.30 1 578 554 166 ALA CA C 54.73 0.30 1 579 554 166 ALA CB C 42.73 0.30 1 580 554 166 ALA N N 124.18 0.30 1 581 555 167 LYS H H 8.12 0.02 1 582 555 167 LYS C C 178.51 0.30 1 583 555 167 LYS CA C 60.90 0.30 1 584 555 167 LYS N N 119.98 0.30 1 585 556 168 ILE H H 8.15 0.02 1 586 556 168 ILE C C 176.29 0.30 1 587 556 168 ILE CA C 64.61 0.30 1 588 556 168 ILE CB C 37.39 0.30 1 589 556 168 ILE N N 119.02 0.30 1 590 557 169 SER H H 7.88 0.02 1 591 557 169 SER C C 177.11 0.30 1 592 557 169 SER CA C 61.44 0.30 1 593 557 169 SER CB C 38.68 0.30 1 594 557 169 SER N N 116.09 0.30 1 595 558 170 LEU H H 7.82 0.02 1 596 558 170 LEU C C 177.15 0.30 1 597 558 170 LEU CA C 57.68 0.30 1 598 558 170 LEU CB C 40.35 0.30 1 599 558 170 LEU N N 124.47 0.30 1 600 559 171 ALA H H 8.40 0.02 1 601 559 171 ALA C C 178.46 0.30 1 602 559 171 ALA CA C 54.89 0.30 1 603 559 171 ALA CB C 42.14 0.30 1 604 559 171 ALA N N 122.11 0.30 1 605 560 172 ARG H H 8.27 0.02 1 606 560 172 ARG C C 176.31 0.30 1 607 560 172 ARG CA C 57.59 0.30 1 608 560 172 ARG CB C 30.15 0.30 1 609 560 172 ARG N N 118.23 0.30 1 610 561 173 ALA H H 7.29 0.02 1 611 561 173 ALA C C 180.65 0.30 1 612 561 173 ALA CA C 53.92 0.30 1 613 561 173 ALA CB C 42.73 0.30 1 614 561 173 ALA N N 119.87 0.30 1 615 562 174 VAL H H 8.34 0.02 1 616 562 174 VAL C C 176.04 0.30 1 617 562 174 VAL CA C 63.76 0.30 1 618 562 174 VAL CB C 30.97 0.30 1 619 562 174 VAL N N 115.93 0.30 1 620 563 175 TYR H H 8.74 0.02 1 621 563 175 TYR C C 177.08 0.30 1 622 563 175 TYR CA C 61.64 0.30 1 623 563 175 TYR CB C 37.95 0.30 1 624 563 175 TYR N N 121.27 0.30 1 625 564 176 LYS H H 6.81 0.02 1 626 564 176 LYS C C 175.35 0.30 1 627 564 176 LYS CA C 56.79 0.30 1 628 564 176 LYS CB C 32.34 0.30 1 629 564 176 LYS N N 118.90 0.30 1 630 565 177 ASP H H 8.80 0.02 1 631 565 177 ASP C C 173.73 0.30 1 632 565 177 ASP CA C 54.53 0.30 1 633 565 177 ASP CB C 40.56 0.30 1 634 565 177 ASP N N 127.51 0.30 1 635 566 178 ALA H H 7.80 0.02 1 636 566 178 ALA C C 174.06 0.30 1 637 566 178 ALA CA C 49.85 0.30 1 638 566 178 ALA CB C 45.05 0.30 1 639 566 178 ALA N N 128.30 0.30 1 640 567 179 ASP H H 7.78 0.02 1 641 567 179 ASP CB C 42.50 0.30 1 642 567 179 ASP N N 117.16 0.30 1 643 569 181 TYR C C 173.63 0.30 1 644 569 181 TYR CA C 56.85 0.30 1 645 569 181 TYR CB C 40.21 0.30 1 646 570 182 LEU H H 9.18 0.02 1 647 570 182 LEU C C 174.13 0.30 1 648 570 182 LEU CA C 52.41 0.30 1 649 570 182 LEU CB C 41.97 0.30 1 650 570 182 LEU N N 123.65 0.30 1 651 571 183 LEU H H 9.48 0.02 1 652 571 183 LEU C C 173.66 0.30 1 653 571 183 LEU CA C 52.74 0.30 1 654 571 183 LEU CB C 42.34 0.30 1 655 571 183 LEU N N 125.13 0.30 1 656 572 184 ASP H H 8.52 0.02 1 657 572 184 ASP C C 172.85 0.30 1 658 572 184 ASP CA C 52.10 0.30 1 659 572 184 ASP CB C 40.04 0.30 1 660 572 184 ASP N N 126.91 0.30 1 661 573 185 SER H H 7.39 0.02 1 662 573 185 SER CA C 57.15 0.30 1 663 573 185 SER CB C 37.78 0.30 1 664 573 185 SER N N 115.15 0.30 1 665 577 189 TYR C C 175.52 0.30 1 666 577 189 TYR CA C 58.46 0.30 1 667 578 190 LEU H H 7.78 0.02 1 668 578 190 LEU C C 176.86 0.30 1 669 578 190 LEU CA C 53.31 0.30 1 670 578 190 LEU CB C 42.63 0.30 1 671 578 190 LEU N N 119.58 0.30 1 672 579 191 ASP H H 8.14 0.02 1 673 579 191 ASP C C 175.70 0.30 1 674 579 191 ASP CA C 52.95 0.30 1 675 579 191 ASP CB C 40.88 0.30 1 676 579 191 ASP N N 120.48 0.30 1 677 580 192 VAL H H 8.37 0.02 1 678 580 192 VAL C C 177.54 0.30 1 679 580 192 VAL CA C 65.58 0.30 1 680 580 192 VAL CB C 31.13 0.30 1 681 580 192 VAL N N 119.28 0.30 1 682 581 193 PHE H H 7.99 0.02 1 683 581 193 PHE C C 178.22 0.30 1 684 581 193 PHE CA C 60.33 0.30 1 685 581 193 PHE CB C 38.13 0.30 1 686 581 193 PHE N N 121.70 0.30 1 687 586 198 VAL H H 8.68 0.02 1 688 586 198 VAL C C 179.21 0.30 1 689 586 198 VAL CA C 65.04 0.30 1 690 586 198 VAL CB C 31.10 0.30 1 691 586 198 VAL N N 120.45 0.30 1 692 587 199 PHE H H 9.16 0.02 1 693 587 199 PHE C C 176.75 0.30 1 694 587 199 PHE CA C 62.37 0.30 1 695 587 199 PHE CB C 38.04 0.30 1 696 587 199 PHE N N 124.21 0.30 1 697 588 200 GLU H H 7.85 0.02 1 698 588 200 GLU C C 177.79 0.30 1 699 588 200 GLU CA C 59.22 0.30 1 700 588 200 GLU CB C 29.00 0.30 1 701 588 200 GLU N N 117.56 0.30 1 702 589 201 SER H H 8.70 0.02 1 703 589 201 SER C C 176.13 0.30 1 704 589 201 SER CA C 61.70 0.30 1 705 589 201 SER CB C 38.73 0.30 1 706 589 201 SER N N 112.24 0.30 1 707 590 202 CYS H H 9.02 0.02 1 708 590 202 CYS C C 173.94 0.30 1 709 590 202 CYS CA C 60.57 0.30 1 710 590 202 CYS CB C 27.16 0.30 1 711 590 202 CYS N N 121.97 0.30 1 712 591 203 VAL H H 6.99 0.02 1 713 591 203 VAL C C 176.19 0.30 1 714 591 203 VAL CA C 66.18 0.30 1 715 591 203 VAL CB C 29.62 0.30 1 716 591 203 VAL N N 116.75 0.30 1 717 592 204 CYS H H 7.30 0.02 1 718 592 204 CYS C C 175.55 0.30 1 719 592 204 CYS CA C 61.15 0.30 1 720 592 204 CYS CB C 27.29 0.30 1 721 592 204 CYS N N 112.90 0.30 1 722 593 205 LYS H H 6.75 0.02 1 723 593 205 LYS C C 177.69 0.30 1 724 593 205 LYS CA C 58.07 0.30 1 725 593 205 LYS CB C 31.86 0.30 1 726 593 205 LYS N N 117.33 0.30 1 727 594 206 LEU H H 7.88 0.02 1 728 594 206 LEU C C 179.08 0.30 1 729 594 206 LEU CA C 58.72 0.30 1 730 594 206 LEU CB C 41.23 0.30 1 731 594 206 LEU N N 123.20 0.30 1 732 595 207 MET H H 7.22 0.02 1 733 595 207 MET C C 174.39 0.30 1 734 595 207 MET CA C 54.53 0.30 1 735 595 207 MET CB C 32.45 0.30 1 736 595 207 MET N N 112.53 0.30 1 737 596 208 ALA H H 6.73 0.02 1 738 596 208 ALA C C 177.47 0.30 1 739 596 208 ALA CA C 54.58 0.30 1 740 596 208 ALA CB C 43.08 0.30 1 741 596 208 ALA N N 119.59 0.30 1 742 597 209 ASN H H 8.45 0.02 1 743 597 209 ASN C C 175.01 0.30 1 744 597 209 ASN CA C 52.77 0.30 1 745 597 209 ASN CB C 38.09 0.30 1 746 597 209 ASN N N 111.29 0.30 1 747 598 210 LYS H H 7.88 0.02 1 748 598 210 LYS C C 176.10 0.30 1 749 598 210 LYS CA C 52.49 0.30 1 750 598 210 LYS CB C 33.73 0.30 1 751 598 210 LYS N N 118.92 0.30 1 752 599 211 THR H H 7.88 0.02 1 753 599 211 THR C C 174.51 0.30 1 754 599 211 THR CA C 63.30 0.30 1 755 599 211 THR CB C 42.89 0.30 1 756 599 211 THR N N 118.92 0.30 1 757 600 212 ARG H H 8.98 0.02 1 758 600 212 ARG CA C 54.05 0.30 1 759 600 212 ARG CB C 33.77 0.30 1 760 600 212 ARG N N 127.19 0.30 1 761 601 213 ILE H H 9.10 0.02 1 762 601 213 ILE C C 173.07 0.30 1 763 601 213 ILE CA C 59.81 0.30 1 764 601 213 ILE CB C 38.28 0.30 1 765 601 213 ILE N N 122.43 0.30 1 766 602 214 LEU H H 9.21 0.02 1 767 602 214 LEU C C 175.02 0.30 1 768 602 214 LEU CA C 52.38 0.30 1 769 602 214 LEU CB C 45.73 0.30 1 770 602 214 LEU N N 130.43 0.30 1 771 603 215 VAL H H 8.97 0.02 1 772 603 215 VAL C C 175.76 0.30 1 773 603 215 VAL CA C 61.24 0.30 1 774 603 215 VAL CB C 31.63 0.30 1 775 603 215 VAL N N 129.68 0.30 1 776 604 216 THR H H 8.88 0.02 1 777 604 216 THR CA C 58.96 0.30 1 778 604 216 THR CB C 43.91 0.30 1 779 604 216 THR N N 122.22 0.30 1 780 610 222 LEU C C 178.21 0.30 1 781 610 222 LEU CA C 57.73 0.30 1 782 610 222 LEU CB C 40.27 0.30 1 783 611 223 ARG H H 7.74 0.02 1 784 611 223 ARG C C 178.04 0.30 1 785 611 223 ARG CA C 58.39 0.30 1 786 611 223 ARG CB C 29.79 0.30 1 787 611 223 ARG N N 115.52 0.30 1 788 612 224 LYS H H 7.23 0.02 1 789 612 224 LYS C C 176.55 0.30 1 790 612 224 LYS CA C 55.63 0.30 1 791 612 224 LYS CB C 32.63 0.30 1 792 612 224 LYS N N 116.94 0.30 1 793 613 225 ALA H H 7.33 0.02 1 794 613 225 ALA C C 176.43 0.30 1 795 613 225 ALA CA C 52.22 0.30 1 796 613 225 ALA CB C 44.20 0.30 1 797 613 225 ALA N N 122.91 0.30 1 798 614 226 ASP H H 8.75 0.02 1 799 614 226 ASP C C 177.11 0.30 1 800 614 226 ASP CA C 57.68 0.30 1 801 614 226 ASP CB C 42.06 0.30 1 802 614 226 ASP N N 120.83 0.30 1 803 615 227 LYS H H 8.05 0.02 1 804 615 227 LYS C C 173.59 0.30 1 805 615 227 LYS CA C 53.57 0.30 1 806 615 227 LYS CB C 38.52 0.30 1 807 615 227 LYS N N 116.10 0.30 1 808 616 228 ILE H H 8.40 0.02 1 809 616 228 ILE CA C 56.86 0.30 1 810 616 228 ILE N N 123.69 0.30 1 811 617 229 LEU C C 174.28 0.30 1 812 617 229 LEU CA C 53.13 0.30 1 813 618 230 ILE H H 9.38 0.02 1 814 618 230 ILE C C 175.32 0.30 1 815 618 230 ILE CA C 59.23 0.30 1 816 618 230 ILE CB C 38.15 0.30 1 817 618 230 ILE N N 124.62 0.30 1 818 619 231 LEU H H 9.18 0.02 1 819 619 231 LEU C C 176.17 0.30 1 820 619 231 LEU CA C 53.13 0.30 1 821 619 231 LEU CB C 43.96 0.30 1 822 619 231 LEU N N 129.03 0.30 1 823 620 232 HIS H H 8.84 0.02 1 824 620 232 HIS C C 175.77 0.30 1 825 620 232 HIS CA C 56.71 0.30 1 826 620 232 HIS N N 116.41 0.30 1 827 621 233 GLN H H 8.69 0.02 1 828 621 233 GLN C C 175.88 0.30 1 829 621 233 GLN CA C 56.08 0.30 1 830 621 233 GLN CB C 50.00 0.30 1 831 621 233 GLN N N 126.30 0.30 1 832 622 234 GLY H H 7.74 0.02 1 833 622 234 GLY C C 172.32 0.30 1 834 622 234 GLY CA C 46.78 0.30 1 835 622 234 GLY N N 105.89 0.30 1 836 623 235 SER H H 7.75 0.02 1 837 623 235 SER C C 173.34 0.30 1 838 623 235 SER CA C 56.51 0.30 1 839 623 235 SER CB C 41.37 0.30 1 840 623 235 SER N N 113.81 0.30 1 841 624 236 SER H H 9.11 0.02 1 842 624 236 SER C C 174.60 0.30 1 843 624 236 SER CA C 56.85 0.30 1 844 624 236 SER CB C 38.00 0.30 1 845 624 236 SER N N 116.88 0.30 1 846 625 237 TYR H H 9.46 0.02 1 847 625 237 TYR C C 176.44 0.30 1 848 625 237 TYR CA C 59.66 0.30 1 849 625 237 TYR CB C 38.54 0.30 1 850 625 237 TYR N N 133.93 0.30 1 851 626 238 PHE H H 7.78 0.02 1 852 626 238 PHE C C 170.96 0.30 1 853 626 238 PHE CA C 58.72 0.30 1 854 626 238 PHE CB C 42.70 0.30 1 855 626 238 PHE N N 117.16 0.30 1 856 627 239 TYR H H 7.00 0.02 1 857 627 239 TYR C C 173.31 0.30 1 858 627 239 TYR CA C 55.30 0.30 1 859 627 239 TYR CB C 40.61 0.30 1 860 627 239 TYR N N 128.71 0.30 1 861 628 240 GLY H H 7.83 0.02 1 862 628 240 GLY C C 171.79 0.30 1 863 628 240 GLY CA C 44.91 0.30 1 864 628 240 GLY N N 115.74 0.30 1 865 629 241 THR H H 8.86 0.02 1 866 629 241 THR C C 175.61 0.30 1 867 629 241 THR CA C 60.30 0.30 1 868 629 241 THR CB C 46.58 0.30 1 869 629 241 THR N N 114.22 0.30 1 870 630 242 PHE H H 9.28 0.02 1 871 630 242 PHE C C 177.62 0.30 1 872 630 242 PHE CA C 62.26 0.30 1 873 630 242 PHE CB C 38.79 0.30 1 874 630 242 PHE N N 122.68 0.30 1 875 631 243 SER H H 8.64 0.02 1 876 631 243 SER C C 177.58 0.30 1 877 631 243 SER CA C 61.43 0.30 1 878 631 243 SER CB C 38.05 0.30 1 879 631 243 SER N N 113.76 0.30 1 880 632 244 GLU H H 7.66 0.02 1 881 632 244 GLU C C 177.64 0.30 1 882 632 244 GLU CA C 58.06 0.30 1 883 632 244 GLU CB C 29.66 0.30 1 884 632 244 GLU N N 122.67 0.30 1 885 633 245 LEU H H 7.95 0.02 1 886 633 245 LEU C C 177.75 0.30 1 887 633 245 LEU CA C 57.73 0.30 1 888 633 245 LEU CB C 39.62 0.30 1 889 633 245 LEU N N 124.19 0.30 1 890 639 251 ASP C C 177.52 0.30 1 891 639 251 ASP CA C 56.77 0.30 1 892 639 251 ASP CB C 29.64 0.30 1 893 640 252 PHE H H 7.97 0.02 1 894 640 252 PHE C C 176.08 0.30 1 895 640 252 PHE CA C 60.86 0.30 1 896 640 252 PHE CB C 39.49 0.30 1 897 640 252 PHE N N 123.27 0.30 1 898 641 253 SER H H 8.26 0.02 1 899 641 253 SER C C 176.23 0.30 1 900 641 253 SER CA C 61.99 0.30 1 901 641 253 SER N N 113.08 0.30 1 902 642 254 SER H H 8.11 0.02 1 903 642 254 SER C C 177.20 0.30 1 904 642 254 SER CA C 61.07 0.30 1 905 642 254 SER CB C 38.18 0.30 1 906 642 254 SER N N 116.47 0.30 1 907 643 255 LYS H H 7.34 0.02 1 908 643 255 LYS C C 178.74 0.30 1 909 643 255 LYS CA C 56.92 0.30 1 910 643 255 LYS CB C 30.44 0.30 1 911 643 255 LYS N N 121.84 0.30 1 912 644 256 LEU H H 7.42 0.02 1 913 644 256 LEU C C 178.99 0.30 1 914 644 256 LEU CA C 56.91 0.30 1 915 644 256 LEU CB C 40.30 0.30 1 916 644 256 LEU N N 119.23 0.30 1 917 645 257 MET H H 8.16 0.02 1 918 645 257 MET C C 177.50 0.30 1 919 645 257 MET CA C 56.31 0.30 1 920 645 257 MET CB C 30.89 0.30 1 921 645 257 MET N N 114.81 0.30 1 922 646 258 GLY H H 7.43 0.02 1 923 646 258 GLY C C 174.50 0.30 1 924 646 258 GLY CA C 45.28 0.30 1 925 646 258 GLY N N 106.46 0.30 1 926 647 259 TYR H H 7.23 0.02 1 927 647 259 TYR CA C 57.28 0.30 1 928 647 259 TYR N N 120.22 0.30 1 929 651 263 ASP C C 176.88 0.30 1 930 651 263 ASP CA C 55.88 0.30 1 931 651 263 ASP CB C 39.65 0.30 1 932 652 264 GLN H H 7.81 0.02 1 933 652 264 GLN C C 177.45 0.30 1 934 652 264 GLN CA C 55.34 0.30 1 935 652 264 GLN CB C 28.04 0.30 1 936 652 264 GLN N N 116.30 0.30 1 937 653 265 PHE H H 7.32 0.02 1 938 653 265 PHE C C 176.19 0.30 1 939 653 265 PHE CA C 53.87 0.30 1 940 653 265 PHE CB C 38.26 0.30 1 941 653 265 PHE N N 120.88 0.30 1 942 654 266 THR H H 8.21 0.02 1 943 654 266 THR C C 175.26 0.30 1 944 654 266 THR CA C 61.03 0.30 1 945 654 266 THR CB C 45.79 0.30 1 946 654 266 THR N N 110.83 0.30 1 947 655 267 GLU H H 8.90 0.02 1 948 655 267 GLU C C 178.48 0.30 1 949 655 267 GLU CA C 59.65 0.30 1 950 655 267 GLU CB C 28.82 0.30 1 951 655 267 GLU N N 122.79 0.30 1 952 656 268 GLU H H 8.65 0.02 1 953 656 268 GLU C C 178.80 0.30 1 954 656 268 GLU CA C 59.16 0.30 1 955 656 268 GLU CB C 28.66 0.30 1 956 656 268 GLU N N 118.84 0.30 1 957 657 269 ARG H H 7.58 0.02 1 958 657 269 ARG CA C 58.02 0.30 1 959 657 269 ARG CB C 29.15 0.30 1 960 657 269 ARG N N 122.77 0.30 1 961 668 280 ARG C C 177.66 0.30 1 962 668 280 ARG CA C 57.62 0.30 1 963 669 281 PHE H H 7.57 0.02 1 964 669 281 PHE C C 175.91 0.30 1 965 669 281 PHE CA C 58.04 0.30 1 966 669 281 PHE CB C 38.60 0.30 1 967 669 281 PHE N N 116.18 0.30 1 968 670 282 SER H H 7.79 0.02 1 969 670 282 SER C C 174.35 0.30 1 970 670 282 SER CA C 58.45 0.30 1 971 670 282 SER CB C 39.28 0.30 1 972 670 282 SER N N 117.07 0.30 1 973 671 283 VAL H H 8.16 0.02 1 974 671 283 VAL C C 175.84 0.30 1 975 671 283 VAL CA C 61.66 0.30 1 976 671 283 VAL CB C 32.66 0.30 1 977 671 283 VAL N N 121.86 0.30 1 978 672 284 ASP H H 8.39 0.02 1 979 672 284 ASP C C 175.10 0.30 1 980 672 284 ASP CA C 54.15 0.30 1 981 672 284 ASP CB C 41.10 0.30 1 982 672 284 ASP N N 124.93 0.30 1 983 673 285 ASP H H 7.94 0.02 1 984 673 285 ASP C C 181.01 0.30 1 985 673 285 ASP CA C 55.59 0.30 1 986 673 285 ASP CB C 41.92 0.30 1 987 673 285 ASP N N 127.06 0.30 1 stop_ save_