data_6646 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C backbone assignment of the firefly luciferase C-terminal 14.3 kDa domain ; _BMRB_accession_number 6646 _BMRB_flat_file_name bmr6646.str _Entry_type original _Submission_date 2005-05-24 _Accession_date 2005-05-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; P. pyralis luciferase consists of a large N-terminal domain (residues 1-436) linked to a small C-terminal domain (residues 440-550) through a short putative hinge region (residues 437-439). Eight stringently conserved residues characterize the adenylate-forming super family that includes the luciferases. The firefly luciferase domain comprised of residues 420-550 contains three of the stringently conserved super family residues Gly446, Glu455 and Lys529 found in the C-terminal domain. The extended polypeptide contains two additional conserved residues Asp422 and Arg437. Furthermore, by extending the C-terminal domain to include residues 420-439, the putative hinge peptide and a small portion of the N-domain has been assigned. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Branchini Bruce R. . 2 Gonzalez Susan A. . 3 Magyar Rachelle A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 242 "13C chemical shifts" 356 "15N chemical shifts" 123 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-10-26 original author . stop_ _Original_release_date 2005-10-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Assignment of the Backbone Resonances of the Firefly Luciferase C-terminal 14.3 kDa Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16222562 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Branchini Bruce R. . 2 Gonzalez Susan A. . 3 Magyar Rachelle A. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 33 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 73 _Page_last 73 _Year 2005 _Details . loop_ _Keyword acyl-adenylate domain firefly luciferase 'NMR assignment' 'P. pyralis' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'firefly luciferase domain residues 420-550' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'firefly luciferase domain residues 420-550' $firefly_luciferase_domain_residues_420-550 stop_ _System_molecular_weight 14333 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_firefly_luciferase_domain_residues_420-550 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'firefly luciferase C-terminal domain (420-550)' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 131 _Mol_residue_sequence ; SGDIAYWDEDEHFFIVDRLK SLIKYKGYQVAPAELESILL QHPNIFDAGVAGLPDDDAGE LPAAVVVLEHGKTMTEKEIV DYVASQVTTAKKLRGGVVFV DEVPKGLTGKLDARKIREIL IKAKKGGKSKL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 420 SER 2 421 GLY 3 422 ASP 4 423 ILE 5 424 ALA 6 425 TYR 7 426 TRP 8 427 ASP 9 428 GLU 10 429 ASP 11 430 GLU 12 431 HIS 13 432 PHE 14 433 PHE 15 434 ILE 16 435 VAL 17 436 ASP 18 437 ARG 19 438 LEU 20 439 LYS 21 440 SER 22 441 LEU 23 442 ILE 24 443 LYS 25 444 TYR 26 445 LYS 27 446 GLY 28 447 TYR 29 448 GLN 30 449 VAL 31 450 ALA 32 451 PRO 33 452 ALA 34 453 GLU 35 454 LEU 36 455 GLU 37 456 SER 38 457 ILE 39 458 LEU 40 459 LEU 41 460 GLN 42 461 HIS 43 462 PRO 44 463 ASN 45 464 ILE 46 465 PHE 47 466 ASP 48 467 ALA 49 468 GLY 50 469 VAL 51 470 ALA 52 471 GLY 53 472 LEU 54 473 PRO 55 474 ASP 56 475 ASP 57 476 ASP 58 477 ALA 59 478 GLY 60 479 GLU 61 480 LEU 62 481 PRO 63 482 ALA 64 483 ALA 65 484 VAL 66 485 VAL 67 486 VAL 68 487 LEU 69 488 GLU 70 489 HIS 71 490 GLY 72 491 LYS 73 492 THR 74 493 MET 75 494 THR 76 495 GLU 77 496 LYS 78 497 GLU 79 498 ILE 80 499 VAL 81 500 ASP 82 501 TYR 83 502 VAL 84 503 ALA 85 504 SER 86 505 GLN 87 506 VAL 88 507 THR 89 508 THR 90 509 ALA 91 510 LYS 92 511 LYS 93 512 LEU 94 513 ARG 95 514 GLY 96 515 GLY 97 516 VAL 98 517 VAL 99 518 PHE 100 519 VAL 101 520 ASP 102 521 GLU 103 522 VAL 104 523 PRO 105 524 LYS 106 525 GLY 107 526 LEU 108 527 THR 109 528 GLY 110 529 LYS 111 530 LEU 112 531 ASP 113 532 ALA 114 533 ARG 115 534 LYS 116 535 ILE 117 536 ARG 118 537 GLU 119 538 ILE 120 539 LEU 121 540 ILE 122 541 LYS 123 542 ALA 124 543 LYS 125 544 LYS 126 545 GLY 127 546 GLY 128 547 LYS 129 548 SER 130 549 LYS 131 550 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1BA3 "Firefly Luciferase In Complex With Bromoform" 100.00 550 100.00 100.00 2.13e-82 PDB 1LCI "Firefly Luciferase" 100.00 550 100.00 100.00 2.13e-82 PDB 3IEP "Firefly Luciferase Apo Structure (P41 Form)" 100.00 551 100.00 100.00 2.16e-82 PDB 3IER "Firefly Luciferase Apo Structure (P41 Form) With Peg 400 Bound" 100.00 551 100.00 100.00 2.16e-82 PDB 3IES "Firefly Luciferase Inhibitor Complex" 100.00 551 100.00 100.00 2.16e-82 PDB 3RIX "1.7a Resolution Structure Of A Firefly Luciferase-Aspulvinone J Inhibitor Complex" 100.00 550 100.00 100.00 2.13e-82 PDB 4E5D "2.2a Resolution Structure Of A Firefly Luciferase-Benzothiazole Inhibitor Complex" 100.00 550 100.00 100.00 2.13e-82 PDB 4G36 "Photinus Pyralis Luciferase In The Adenylate-Forming Conformation Bound To Dlsa" 100.00 555 100.00 100.00 2.47e-82 PDB 4G37 "Structure Of Cross-Linked Firefly Luciferase In Second Catalytic Conformation" 100.00 555 99.24 99.24 3.35e-81 DBJ BAA93575 "luciferase [synthetic construct]" 97.71 553 100.00 100.00 2.64e-80 DBJ BAB32737 "luciferase [Cloning vector pPVLUC441]" 97.71 355 100.00 100.00 5.43e-82 DBJ BAD00047 "Fusion protein, Feo [Hepatitis C virus]" 97.71 832 100.00 100.00 6.10e-78 DBJ BAE33044 "unnamed protein product [Mus musculus]" 97.71 550 100.00 100.00 2.17e-80 DBJ BAE33661 "unnamed protein product [Mus musculus]" 97.71 550 100.00 100.00 2.17e-80 EMBL CAA46407 "luciferase [Cloning vector pGEM-luc]" 100.00 550 100.00 100.00 2.13e-82 EMBL CAA46419 "luciferase [Cloning vector pGL2-Basic]" 100.00 550 100.00 100.00 2.13e-82 EMBL CAA46421 "luciferase [Cloning vector pGL2-Control]" 100.00 550 100.00 100.00 2.13e-82 EMBL CAA46423 "luciferase [Cloning vector pGL2-Enhancer]" 100.00 550 100.00 100.00 2.13e-82 EMBL CAA46425 "luciferase [Cloning vector pGL2-Promoter]" 100.00 550 100.00 100.00 2.13e-82 GB AAA03561 "luciferase [synthetic construct]" 100.00 550 100.00 100.00 2.13e-82 GB AAA29795 "Luciferase [Photinus pyralis]" 100.00 550 100.00 100.00 2.13e-82 GB AAA66377 "luciferase [Cloning vector pLUC/LIC]" 100.00 550 100.00 100.00 2.13e-82 GB AAA72988 "luciferase/kanamycin resistance protein [synthetic construct]" 100.00 821 99.24 99.24 2.20e-79 GB AAA88784 "luciferase [Cloning vector pSP-luc+]" 97.71 550 100.00 100.00 2.17e-80 SP P08659 "RecName: Full=Luciferin 4-monooxygenase; Short=Luciferase [Photinus pyralis]" 100.00 550 100.00 100.00 2.13e-82 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $firefly_luciferase_domain_residues_420-550 'common eastern firefly' 7054 Eukaryota Metazoa Photinus pyralis stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $firefly_luciferase_domain_residues_420-550 'recombinant technology' 'E. coli' Escherichia 'Escherichia coli' BL21 DE3 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '13C, 15N double labeled protein' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $firefly_luciferase_domain_residues_420-550 1.2 mM '[U-95% 13C; U-95% 15N]' 'sodium phosphate' 100 mM . 'sodium azide' 0.05 % . H2O 92 % . D2O 8 % . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name VNMR _Version 6.1C loop_ _Vendor _Address _Electronic_address Varian 'Palo Alto, CA' www.varianinc.com stop_ _Details . save_ save_software_2 _Saveframe_category software _Name SPARKY _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_500_MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY/INOVA _Field_strength '500 MHz' _Details . save_ ############################# # NMR applied experiments # ############################# save_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label $sample_1 save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_NOESY-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HSQC _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 pH temperature 291 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HSQC HNCO HNCA HN(CO)CA HNCACB CBCA(CO)NH HNHA NOESY-HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'firefly luciferase domain residues 420-550' _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 1 420 1 SER H H 8.33 0.02 1 2 420 1 SER HA H 4.41 0.02 1 3 420 1 SER C C 175 0.2 1 4 420 1 SER CA C 58.4 0.2 1 5 420 1 SER CB C 63.8 0.2 1 6 420 1 SER N N 115.7 0.2 1 7 421 2 GLY H H 8.56 0.02 1 8 421 2 GLY HA2 H 3.97 0.02 1 9 421 2 GLY C C 173.6 0.2 1 10 421 2 GLY CA C 45.4 0.2 1 11 421 2 GLY N N 110.8 0.2 1 12 422 3 ASP H H 8.19 0.02 1 13 422 3 ASP HA H 4.62 0.02 1 14 422 3 ASP C C 175.9 0.2 1 15 422 3 ASP CA C 54.4 0.2 1 16 422 3 ASP CB C 41.4 0.2 1 17 422 3 ASP N N 120.5 0.2 1 18 423 4 ILE H H 8.05 0.02 1 19 423 4 ILE HA H 4.06 0.02 1 20 423 4 ILE C C 175.4 0.2 1 21 423 4 ILE CA C 61 0.2 1 22 423 4 ILE CB C 39 0.2 1 23 423 4 ILE N N 120.9 0.2 1 24 424 5 ALA H H 8.32 0.02 1 25 424 5 ALA HA H 4.22 0.02 1 26 424 5 ALA C C 176.8 0.2 1 27 424 5 ALA CA C 52.3 0.2 1 28 424 5 ALA CB C 19.5 0.2 1 29 424 5 ALA N N 127.6 0.2 1 30 425 6 TYR H H 8 0.02 1 31 425 6 TYR C C 174.9 0.2 1 32 425 6 TYR CA C 57.8 0.2 1 33 425 6 TYR CB C 39.3 0.2 1 34 425 6 TYR N N 119.3 0.2 1 35 426 7 TRP H H 7.93 0.02 1 36 426 7 TRP HA H 4.51 0.02 1 37 426 7 TRP C C 176.3 0.2 1 38 426 7 TRP CA C 56.9 0.2 1 39 426 7 TRP CB C 30.1 0.2 1 40 426 7 TRP N N 122.2 0.2 1 41 427 8 ASP H H 8.09 0.02 1 42 427 8 ASP HA H 4.57 0.02 1 43 427 8 ASP C C 175.9 0.2 1 44 427 8 ASP CA C 54.1 0.2 1 45 427 8 ASP CB C 41.5 0.2 1 46 427 8 ASP N N 122.7 0.2 1 47 428 9 GLU H H 8.22 0.02 1 48 428 9 GLU HA H 4.05 0.02 1 49 428 9 GLU C C 176.3 0.2 1 50 428 9 GLU CA C 57.5 0.2 1 51 428 9 GLU CB C 30.3 0.2 1 52 428 9 GLU N N 121.6 0.2 1 53 429 10 ASP H H 8.25 0.02 1 54 429 10 ASP HA H 4.05 0.02 1 55 429 10 ASP CA C 55.2 0.2 1 56 429 10 ASP CB C 41.4 0.2 1 57 429 10 ASP N N 120.3 0.2 1 58 430 11 GLU H H 8.26 0.02 1 59 430 11 GLU C C 176.5 0.2 1 60 430 11 GLU CA C 57.3 0.2 1 61 430 11 GLU CB C 29.9 0.2 1 62 430 11 GLU N N 120 0.2 1 63 431 12 HIS H H 8.26 0.02 1 64 431 12 HIS HA H 4.59 0.02 1 65 431 12 HIS C C 174.8 0.2 1 66 431 12 HIS CA C 56.7 0.2 1 67 431 12 HIS CB C 29.3 0.2 1 68 431 12 HIS N N 118.2 0.2 1 69 432 13 PHE H H 7.93 0.02 1 70 432 13 PHE HA H 4.41 0.02 1 71 432 13 PHE C C 175.2 0.2 1 72 432 13 PHE CA C 58.5 0.2 1 73 432 13 PHE CB C 39 0.2 1 74 432 13 PHE N N 119 0.2 1 75 433 14 PHE H H 8.12 0.02 1 76 433 14 PHE HA H 4.48 0.02 1 77 433 14 PHE C C 175.5 0.2 1 78 433 14 PHE CA C 58 0.2 1 79 433 14 PHE CB C 39.5 0.2 1 80 433 14 PHE N N 120.2 0.2 1 81 434 15 ILE H H 8.06 0.02 1 82 434 15 ILE HA H 4.02 0.02 1 83 434 15 ILE C C 175 0.2 1 84 434 15 ILE CA C 61.9 0.2 1 85 434 15 ILE CB C 32.9 0.2 1 86 434 15 ILE N N 122 0.2 1 87 435 16 VAL H H 8.09 0.02 1 88 435 16 VAL HA H 3.95 0.02 1 89 435 16 VAL C C 176.1 0.2 1 90 435 16 VAL CA C 62 0.2 1 91 435 16 VAL CB C 32.6 0.2 1 92 435 16 VAL N N 122.7 0.2 1 93 436 17 ASP H H 8.32 0.02 1 94 436 17 ASP HA H 4.44 0.02 1 95 436 17 ASP C C 176.9 0.2 1 96 436 17 ASP CA C 55.2 0.2 1 97 436 17 ASP CB C 41.4 0.2 1 98 436 17 ASP N N 122.7 0.2 1 99 437 18 ARG H H 8.27 0.02 1 100 437 18 ARG HA H 4.13 0.02 1 101 437 18 ARG C C 177.2 0.2 1 102 437 18 ARG N N 121.2 0.2 1 103 438 19 LEU H H 8.19 0.02 1 104 438 19 LEU HA H 4.2 0.02 1 105 438 19 LEU C C 178 0.2 1 106 438 19 LEU CA C 55.6 0.2 1 107 438 19 LEU CB C 41.5 0.2 1 108 438 19 LEU N N 120.5 0.2 1 109 439 20 LYS H H 8.01 0.02 1 110 439 20 LYS HA H 4.5 0.02 1 111 439 20 LYS C C 176.6 0.2 1 112 439 20 LYS CA C 56.9 0.2 1 113 439 20 LYS CB C 32.5 0.2 1 114 439 20 LYS N N 119.6 0.2 1 115 440 21 SER H H 8.06 0.02 1 116 440 21 SER HA H 4.43 0.02 1 117 440 21 SER C C 173.6 0.2 1 118 440 21 SER CA C 58.6 0.2 1 119 440 21 SER CB C 63.4 0.2 1 120 440 21 SER N N 114.8 0.2 1 121 441 22 LEU H H 7.64 0.02 1 122 441 22 LEU HA H 4.03 0.02 1 123 441 22 LEU C C 174 0.2 1 124 441 22 LEU CA C 55.1 0.2 1 125 441 22 LEU CB C 43.3 0.2 1 126 441 22 LEU N N 121.1 0.2 1 127 442 23 ILE H H 8.98 0.02 1 128 442 23 ILE C C 175.2 0.2 1 129 442 23 ILE CA C 60.9 0.2 1 130 442 23 ILE N N 123.9 0.2 1 131 443 24 LYS H H 8.82 0.02 1 132 443 24 LYS HA H 4.95 0.02 1 133 443 24 LYS CA C 55.3 0.2 1 134 443 24 LYS CB C 30 0.2 1 135 443 24 LYS N N 129.2 0.2 1 136 444 25 TYR H H 7.83 0.02 1 137 444 25 TYR HA H 4.13 0.02 1 138 444 25 TYR CA C 56.1 0.2 1 139 444 25 TYR CB C 40.4 0.2 1 140 444 25 TYR N N 126.6 0.2 1 141 445 26 LYS H H 9.27 0.02 1 142 445 26 LYS C C 176.1 0.2 1 143 445 26 LYS CA C 57.4 0.2 1 144 445 26 LYS CB C 30.5 0.2 1 145 445 26 LYS N N 124.9 0.2 1 146 446 27 GLY H H 8.06 0.02 1 147 446 27 GLY HA2 H 3.75 0.02 1 148 446 27 GLY C C 176.1 0.2 1 149 446 27 GLY N N 107.3 0.2 1 150 447 28 TYR H H 8.88 0.02 1 151 447 28 TYR C C 175.2 0.2 1 152 447 28 TYR CA C 57.5 0.2 1 153 447 28 TYR CB C 39.9 0.2 1 154 447 28 TYR N N 122.2 0.2 1 155 448 29 GLN H H 8.51 0.02 1 156 448 29 GLN HA H 4.97 0.02 1 157 448 29 GLN C C 175.2 0.2 1 158 448 29 GLN CA C 55.1 0.2 1 159 448 29 GLN CB C 30.3 0.2 1 160 448 29 GLN N N 120.7 0.2 1 161 449 30 VAL H H 9.4 0.02 1 162 449 30 VAL HA H 4.94 0.02 1 163 449 30 VAL C C 173.9 0.2 1 164 449 30 VAL CA C 61.6 0.2 1 165 449 30 VAL CB C 34.6 0.2 1 166 449 30 VAL N N 125.7 0.2 1 167 450 31 ALA H H 9.36 0.02 1 168 450 31 ALA HA H 4.17 0.02 1 169 450 31 ALA CA C 49.7 0.2 1 170 450 31 ALA CB C 18.9 0.2 1 171 450 31 ALA N N 132.8 0.2 1 172 451 32 PRO C C 177.7 0.2 1 173 451 32 PRO CA C 65.3 0.2 1 174 451 32 PRO CB C 32.5 0.2 1 175 452 33 ALA H H 8.53 0.02 1 176 452 33 ALA HA H 4.39 0.02 1 177 452 33 ALA C C 180.4 0.2 1 178 452 33 ALA CB C 18.7 0.2 1 179 452 33 ALA N N 116.6 0.2 1 180 453 34 GLU H H 7.31 0.02 1 181 453 34 GLU HA H 4.38 0.02 1 182 453 34 GLU C C 178.6 0.2 1 183 453 34 GLU CA C 58.8 0.2 1 184 453 34 GLU CB C 29.8 0.2 1 185 453 34 GLU N N 117.4 0.2 1 186 454 35 LEU H H 6.72 0.02 1 187 454 35 LEU C C 178.6 0.2 1 188 454 35 LEU CA C 57.3 0.2 1 189 454 35 LEU CB C 43.9 0.2 1 190 454 35 LEU N N 118.1 0.2 1 191 455 36 GLU H H 8.89 0.02 1 192 455 36 GLU C C 177.5 0.2 1 193 455 36 GLU CA C 60.6 0.2 1 194 455 36 GLU CB C 28.8 0.2 1 195 455 36 GLU N N 119.1 0.2 1 196 456 37 SER H H 7.83 0.02 1 197 456 37 SER HA H 4.14 0.02 1 198 456 37 SER C C 176.7 0.2 1 199 456 37 SER CA C 61.9 0.2 1 200 456 37 SER N N 111.7 0.2 1 201 457 38 ILE H H 7.09 0.02 1 202 457 38 ILE HA H 3.8 0.02 1 203 457 38 ILE C C 173.8 0.2 1 204 457 38 ILE CA C 64.1 0.2 1 205 457 38 ILE CB C 38.8 0.2 1 206 457 38 ILE N N 120.2 0.2 1 207 458 39 LEU H H 8.18 0.02 1 208 458 39 LEU HA H 4.06 0.02 1 209 458 39 LEU C C 177.4 0.2 1 210 458 39 LEU CA C 58.8 0.2 1 211 458 39 LEU CB C 41.9 0.2 1 212 458 39 LEU N N 121.4 0.2 1 213 459 40 LEU H H 8.48 0.02 1 214 459 40 LEU HA H 3.77 0.02 1 215 459 40 LEU C C 178.5 0.2 1 216 459 40 LEU CA C 57.3 0.2 1 217 459 40 LEU CB C 41.7 0.2 1 218 459 40 LEU N N 116.1 0.2 1 219 460 41 GLN H H 7.31 0.02 1 220 460 41 GLN HA H 4.09 0.02 1 221 460 41 GLN C C 177 0.2 1 222 460 41 GLN CA C 56.5 0.2 1 223 460 41 GLN CB C 29 0.2 1 224 460 41 GLN N N 113.7 0.2 1 225 461 42 HIS H H 8.05 0.02 1 226 461 42 HIS HA H 4.16 0.02 1 227 461 42 HIS CA C 57.4 0.2 1 228 461 42 HIS CB C 31.5 0.2 1 229 461 42 HIS N N 124.5 0.2 1 230 462 43 PRO C C 178.2 0.2 1 231 462 43 PRO CA C 64.3 0.2 1 232 462 43 PRO CB C 32.2 0.2 1 233 463 44 ASN H H 11.31 0.02 1 234 463 44 ASN HA H 4.8 0.02 1 235 463 44 ASN C C 174.8 0.2 1 236 463 44 ASN CA C 53.3 0.2 1 237 463 44 ASN CB C 38.4 0.2 1 238 463 44 ASN N N 119 0.2 1 239 464 45 ILE H H 7.82 0.02 1 240 464 45 ILE HA H 4.11 0.02 1 241 464 45 ILE C C 173.1 0.2 1 242 464 45 ILE CA C 62.7 0.2 1 243 464 45 ILE CB C 38.2 0.2 1 244 464 45 ILE N N 121.7 0.2 1 245 465 46 PHE H H 8.99 0.02 1 246 465 46 PHE HA H 4.62 0.02 1 247 465 46 PHE C C 174.4 0.2 1 248 465 46 PHE CA C 58.5 0.2 1 249 465 46 PHE CB C 40.7 0.2 1 250 465 46 PHE N N 128.6 0.2 1 251 466 47 ASP H H 8.22 0.02 1 252 466 47 ASP HA H 4.81 0.02 1 253 466 47 ASP C C 173.1 0.2 1 254 466 47 ASP CA C 52.5 0.2 1 255 466 47 ASP CB C 43.7 0.2 1 256 466 47 ASP N N 115.3 0.2 1 257 467 48 ALA H H 8.32 0.02 1 258 467 48 ALA HA H 5.14 0.02 1 259 467 48 ALA C C 174.2 0.2 1 260 467 48 ALA CA C 51.5 0.2 1 261 467 48 ALA CB C 23.9 0.2 1 262 467 48 ALA N N 122.2 0.2 1 263 468 49 GLY H H 8.64 0.02 1 264 468 49 GLY HA2 H 4.63 0.02 1 265 468 49 GLY C C 171.1 0.2 1 266 468 49 GLY CA C 44.9 0.2 1 267 468 49 GLY N N 105 0.2 1 268 469 50 VAL H H 10.37 0.02 1 269 469 50 VAL HA H 5.08 0.02 1 270 469 50 VAL C C 173.9 0.2 1 271 469 50 VAL CA C 60.4 0.2 1 272 469 50 VAL CB C 33.5 0.2 1 273 469 50 VAL N N 127.2 0.2 1 274 470 51 ALA H H 8.62 0.02 1 275 470 51 ALA HA H 4.48 0.02 1 276 470 51 ALA C C 174.2 0.2 1 277 470 51 ALA CA C 50.7 0.2 1 278 470 51 ALA CB C 22.5 0.2 1 279 470 51 ALA N N 125.1 0.2 1 280 471 52 GLY H H 8.71 0.02 1 281 471 52 GLY HA2 H 3.3 0.02 1 282 471 52 GLY HA3 H 4.18 0.02 1 283 471 52 GLY C C 172.1 0.2 1 284 471 52 GLY CA C 44.8 0.2 1 285 471 52 GLY N N 105 0.2 1 286 472 53 LEU H H 9.16 0.02 1 287 472 53 LEU HA H 4.79 0.02 1 288 472 53 LEU CA C 50.9 0.2 1 289 472 53 LEU N N 128.3 0.2 1 290 473 54 PRO C C 175.4 0.2 1 291 473 54 PRO CA C 63.5 0.2 1 292 473 54 PRO CB C 32.5 0.2 1 293 474 55 ASP H H 8.09 0.02 1 294 474 55 ASP HA H 4.8 0.02 1 295 474 55 ASP C C 175.5 0.2 1 296 474 55 ASP CA C 53.6 0.2 1 297 474 55 ASP N N 122.9 0.2 1 298 475 56 ASP H H 8.98 0.02 1 299 475 56 ASP C C 176.3 0.2 1 300 475 56 ASP CA C 57.3 0.2 1 301 475 56 ASP CB C 40.3 0.2 1 302 475 56 ASP N N 126.6 0.2 1 303 476 57 ASP H H 8.02 0.02 1 304 476 57 ASP HA H 4.68 0.02 1 305 476 57 ASP C C 177.3 0.2 1 306 476 57 ASP CA C 56.1 0.2 1 307 476 57 ASP CB C 42.4 0.2 1 308 476 57 ASP N N 117.3 0.2 1 309 477 58 ALA H H 9.14 0.02 1 310 477 58 ALA HA H 4.33 0.02 1 311 477 58 ALA C C 176.9 0.2 1 312 477 58 ALA CA C 52.3 0.2 1 313 477 58 ALA CB C 21.6 0.2 1 314 477 58 ALA N N 120.2 0.2 1 315 478 59 GLY H H 8.04 0.02 1 316 478 59 GLY HA2 H 3.56 0.02 1 317 478 59 GLY HA3 H 4.75 0.02 1 318 478 59 GLY C C 174.8 0.2 1 319 478 59 GLY CA C 46.8 0.2 1 320 478 59 GLY N N 110.8 0.2 1 321 479 60 GLU H H 8.23 0.02 1 322 479 60 GLU HA H 4.32 0.02 1 323 479 60 GLU CA C 55.3 0.2 1 324 479 60 GLU CB C 30.1 0.2 1 325 479 60 GLU N N 122.5 0.2 1 326 481 62 PRO C C 174.3 0.2 1 327 481 62 PRO CA C 63.6 0.2 1 328 481 62 PRO CB C 31.4 0.2 1 329 482 63 ALA H H 8.68 0.02 1 330 482 63 ALA HA H 4.85 0.02 1 331 482 63 ALA C C 173.7 0.2 1 332 482 63 ALA CA C 50.9 0.2 1 333 482 63 ALA CB C 23.9 0.2 1 334 482 63 ALA N N 128.7 0.2 1 335 483 64 ALA H H 8.48 0.02 1 336 483 64 ALA HA H 5.64 0.02 1 337 483 64 ALA C C 176.3 0.2 1 338 483 64 ALA CA C 49.8 0.2 1 339 483 64 ALA CB C 24.4 0.2 1 340 483 64 ALA N N 117.7 0.2 1 341 484 65 VAL H H 9.11 0.02 1 342 484 65 VAL HA H 5.61 0.02 1 343 484 65 VAL C C 175.4 0.2 1 344 484 65 VAL CA C 57.9 0.2 1 345 484 65 VAL CB C 31.9 0.2 1 346 484 65 VAL N N 113.6 0.2 1 347 485 66 VAL H H 8.38 0.02 1 348 485 66 VAL HA H 4.62 0.02 1 349 485 66 VAL C C 173.3 0.2 1 350 485 66 VAL CA C 60.6 0.2 1 351 485 66 VAL CB C 36.8 0.2 1 352 485 66 VAL N N 121.1 0.2 1 353 486 67 VAL H H 8.64 0.02 1 354 486 67 VAL HA H 4.81 0.02 1 355 486 67 VAL C C 177 0.2 1 356 486 67 VAL CA C 59.8 0.2 1 357 486 67 VAL CB C 33.4 0.2 1 358 486 67 VAL N N 125.8 0.2 1 359 487 68 LEU H H 9.07 0.02 1 360 487 68 LEU HA H 4.78 0.02 1 361 487 68 LEU C C 178.2 0.2 1 362 487 68 LEU CA C 54.8 0.2 1 363 487 68 LEU CB C 42.4 0.2 1 364 487 68 LEU N N 128.4 0.2 1 365 488 69 GLU H H 8.35 0.02 1 366 488 69 GLU HA H 4.9 0.02 1 367 488 69 GLU C C 176.1 0.2 1 368 488 69 GLU CA C 56.2 0.2 1 369 488 69 GLU CB C 30.3 0.2 1 370 488 69 GLU N N 121.4 0.2 1 371 489 70 HIS H H 8.75 0.02 1 372 489 70 HIS HA H 4.26 0.02 1 373 489 70 HIS C C 176.8 0.2 1 374 489 70 HIS CA C 57.9 0.2 1 375 489 70 HIS CB C 29.1 0.2 1 376 489 70 HIS N N 121.9 0.2 1 377 490 71 GLY H H 8.68 0.02 1 378 490 71 GLY C C 173.6 0.2 1 379 490 71 GLY CA C 45.1 0.2 1 380 490 71 GLY N N 113.3 0.2 1 381 491 72 LYS H H 7.75 0.02 1 382 491 72 LYS HA H 4.74 0.02 1 383 491 72 LYS C C 175.1 0.2 1 384 491 72 LYS CA C 53.2 0.2 1 385 491 72 LYS CB C 33 0.2 1 386 491 72 LYS N N 118.6 0.2 1 387 492 73 THR H H 8.28 0.02 1 388 492 73 THR HA H 4.45 0.02 1 389 492 73 THR C C 172.8 0.2 1 390 492 73 THR CA C 60.4 0.2 1 391 492 73 THR CB C 70.6 0.2 1 392 492 73 THR N N 112.7 0.2 1 393 493 74 MET H H 7.36 0.02 1 394 493 74 MET HA H 4.68 0.02 1 395 493 74 MET C C 173.7 0.2 1 396 493 74 MET CA C 55.8 0.2 1 397 493 74 MET CB C 37.4 0.2 1 398 493 74 MET N N 122.2 0.2 1 399 494 75 THR H H 8.71 0.02 1 400 494 75 THR HA H 4.66 0.02 1 401 494 75 THR C C 175.3 0.2 1 402 494 75 THR CA C 60 0.2 1 403 494 75 THR CB C 71.6 0.2 1 404 494 75 THR N N 112 0.2 1 405 495 76 GLU H H 9.36 0.02 1 406 495 76 GLU HA H 3.78 0.02 1 407 495 76 GLU C C 177.1 0.2 1 408 495 76 GLU CA C 60.3 0.2 1 409 495 76 GLU CB C 29.8 0.2 1 410 495 76 GLU N N 121.1 0.2 1 411 496 77 LYS H H 8.49 0.02 1 412 496 77 LYS HA H 4.01 0.02 1 413 496 77 LYS C C 177.4 0.2 1 414 496 77 LYS CA C 59 0.2 1 415 496 77 LYS CB C 32.7 0.2 1 416 496 77 LYS N N 118.4 0.2 1 417 497 78 GLU H H 7.86 0.02 1 418 497 78 GLU HA H 4.1 0.02 1 419 497 78 GLU C C 180.4 0.2 1 420 497 78 GLU CA C 59.1 0.2 1 421 497 78 GLU CB C 30.9 0.2 1 422 497 78 GLU N N 116.6 0.2 1 423 498 79 ILE H H 7.84 0.02 1 424 498 79 ILE HA H 3.52 0.02 1 425 498 79 ILE C C 176.9 0.2 1 426 498 79 ILE CA C 66.4 0.2 1 427 498 79 ILE CB C 37.4 0.2 1 428 498 79 ILE N N 120.4 0.2 1 429 499 80 VAL H H 8.81 0.02 1 430 499 80 VAL HA H 3.51 0.02 1 431 499 80 VAL C C 179.5 0.2 1 432 499 80 VAL CA C 67.1 0.2 1 433 499 80 VAL CB C 31.9 0.2 1 434 499 80 VAL N N 121.3 0.2 1 435 500 81 ASP H H 9.08 0.02 1 436 500 81 ASP HA H 4.41 0.02 1 437 500 81 ASP C C 178.8 0.2 1 438 500 81 ASP CA C 57 0.2 1 439 500 81 ASP CB C 39.2 0.2 1 440 500 81 ASP N N 121.8 0.2 1 441 501 82 TYR H H 7.95 0.02 1 442 501 82 TYR HA H 4.51 0.02 1 443 501 82 TYR C C 178.9 0.2 1 444 501 82 TYR CA C 60.3 0.2 1 445 501 82 TYR CB C 37.4 0.2 1 446 501 82 TYR N N 123 0.2 1 447 502 83 VAL H H 8.45 0.02 1 448 502 83 VAL HA H 2.92 0.02 1 449 502 83 VAL C C 177.4 0.2 1 450 502 83 VAL CA C 67.2 0.2 1 451 502 83 VAL CB C 31.3 0.2 1 452 502 83 VAL N N 121.5 0.2 1 453 503 84 ALA H H 8.24 0.02 1 454 503 84 ALA HA H 3.88 0.02 1 455 503 84 ALA C C 178.4 0.2 1 456 503 84 ALA CA C 54.8 0.2 1 457 503 84 ALA CB C 18.2 0.2 1 458 503 84 ALA N N 119.4 0.2 1 459 504 85 SER H H 7.49 0.02 1 460 504 85 SER HA H 4.37 0.02 1 461 504 85 SER C C 174.4 0.2 1 462 504 85 SER CA C 60.1 0.2 1 463 504 85 SER CB C 63.8 0.2 1 464 504 85 SER N N 109.9 0.2 1 465 505 86 GLN H H 7.84 0.02 1 466 505 86 GLN HA H 4.46 0.02 1 467 505 86 GLN C C 175.3 0.2 1 468 505 86 GLN CA C 55.3 0.2 1 469 505 86 GLN CB C 32.3 0.2 1 470 505 86 GLN N N 117.9 0.2 1 471 506 87 VAL H H 7.04 0.02 1 472 506 87 VAL HA H 4.94 0.02 1 473 506 87 VAL C C 175.5 0.2 1 474 506 87 VAL CA C 58.7 0.2 1 475 506 87 VAL CB C 36.2 0.2 1 476 506 87 VAL N N 110.1 0.2 1 477 507 88 THR H H 7.38 0.02 1 478 507 88 THR HA H 4.42 0.02 1 479 507 88 THR C C 175.9 0.2 1 480 507 88 THR CA C 60.8 0.2 1 481 507 88 THR CB C 69.2 0.2 1 482 507 88 THR N N 109.7 0.2 1 483 508 89 THR H H 8.14 0.02 1 484 508 89 THR C C 175.3 0.2 1 485 508 89 THR CA C 65.5 0.2 1 486 508 89 THR CB C 68.6 0.2 1 487 508 89 THR N N 112.9 0.2 1 488 509 90 ALA H H 8.18 0.02 1 489 509 90 ALA HA H 3.88 0.02 1 490 509 90 ALA CA C 54.7 0.2 1 491 509 90 ALA CB C 18.6 0.2 1 492 509 90 ALA N N 122.2 0.2 1 493 511 92 LYS C C 178 0.2 1 494 511 92 LYS CA C 57.3 0.2 1 495 511 92 LYS CB C 33.1 0.2 1 496 512 93 LEU H H 8.71 0.02 1 497 512 93 LEU HA H 4.33 0.02 1 498 512 93 LEU C C 176.4 0.2 1 499 512 93 LEU CA C 53 0.2 1 500 512 93 LEU CB C 41.4 0.2 1 501 512 93 LEU N N 124.8 0.2 1 502 513 94 ARG H H 8.05 0.02 1 503 513 94 ARG HA H 4.07 0.02 1 504 513 94 ARG C C 177 0.2 1 505 513 94 ARG CA C 58.4 0.2 1 506 513 94 ARG CB C 32.4 0.2 1 507 513 94 ARG N N 121.5 0.2 1 508 514 95 GLY H H 9.1 0.02 1 509 514 95 GLY HA2 H 3.19 0.02 1 510 514 95 GLY HA3 H 3.98 0.02 1 511 514 95 GLY C C 172.7 0.2 1 512 514 95 GLY CA C 45.1 0.2 1 513 514 95 GLY N N 106.4 0.2 1 514 515 96 GLY H H 7.29 0.02 1 515 515 96 GLY HA2 H 3.36 0.02 1 516 515 96 GLY HA3 H 4.29 0.02 1 517 515 96 GLY C C 171.1 0.2 1 518 515 96 GLY CA C 44.2 0.2 1 519 515 96 GLY N N 105.6 0.2 1 520 516 97 VAL H H 8.96 0.02 1 521 516 97 VAL HA H 5.11 0.02 1 522 516 97 VAL C C 174.4 0.2 1 523 516 97 VAL CA C 59.5 0.2 1 524 516 97 VAL CB C 36.8 0.2 1 525 516 97 VAL N N 115.8 0.2 1 526 517 98 VAL H H 8.56 0.02 1 527 517 98 VAL HA H 4.05 0.02 1 528 517 98 VAL C C 174.6 0.2 1 529 517 98 VAL CA C 60.5 0.2 1 530 517 98 VAL CB C 35.1 0.2 1 531 517 98 VAL N N 124.5 0.2 1 532 518 99 PHE H H 8.77 0.02 1 533 518 99 PHE HA H 5.21 0.02 1 534 518 99 PHE C C 175.9 0.2 1 535 518 99 PHE CA C 58.3 0.2 1 536 518 99 PHE CB C 39.1 0.2 1 537 518 99 PHE N N 127.1 0.2 1 538 519 100 VAL H H 8.67 0.02 1 539 519 100 VAL HA H 4.86 0.02 1 540 519 100 VAL C C 174.6 0.2 1 541 519 100 VAL CA C 58.4 0.2 1 542 519 100 VAL CB C 36.6 0.2 1 543 519 100 VAL N N 115.6 0.2 1 544 520 101 ASP H H 8.58 0.02 1 545 520 101 ASP HA H 4.87 0.02 1 546 520 101 ASP C C 176.6 0.2 1 547 520 101 ASP CA C 55.2 0.2 1 548 520 101 ASP CB C 41 0.2 1 549 520 101 ASP N N 116.8 0.2 1 550 521 102 GLU H H 7.25 0.02 1 551 521 102 GLU HA H 4.37 0.02 1 552 521 102 GLU C C 173.7 0.2 1 553 521 102 GLU CA C 55 0.2 1 554 521 102 GLU CB C 32.5 0.2 1 555 521 102 GLU N N 117 0.2 1 556 522 103 VAL H H 9.29 0.02 1 557 522 103 VAL HA H 3.88 0.02 1 558 522 103 VAL CA C 60.2 0.2 1 559 522 103 VAL CB C 32.2 0.2 1 560 522 103 VAL N N 127.9 0.2 1 561 523 104 PRO C C 175.2 0.2 1 562 523 104 PRO CA C 63.5 0.2 1 563 523 104 PRO CB C 32.6 0.2 1 564 524 105 LYS H H 8.35 0.02 1 565 524 105 LYS HA H 4.9 0.02 1 566 524 105 LYS C C 177.4 0.2 1 567 524 105 LYS CA C 54.2 0.2 1 568 524 105 LYS CB C 36.7 0.2 1 569 524 105 LYS N N 122.2 0.2 1 570 525 106 GLY H H 8.76 0.02 1 571 525 106 GLY HA2 H 3.96 0.02 1 572 525 106 GLY HA3 H 4.52 0.02 1 573 525 106 GLY C C 175.9 0.2 1 574 525 106 GLY CA C 43.8 0.2 1 575 525 106 GLY N N 107.7 0.2 1 576 526 107 LEU H H 8.77 0.02 1 577 526 107 LEU HA H 4.49 0.02 1 578 526 107 LEU C C 178.8 0.2 1 579 526 107 LEU CA C 57.5 0.2 1 580 526 107 LEU CB C 42.3 0.2 1 581 526 107 LEU N N 120.4 0.2 1 582 527 108 THR H H 8.07 0.02 1 583 527 108 THR HA H 4.46 0.02 1 584 527 108 THR C C 175 0.2 1 585 527 108 THR CA C 60.6 0.2 1 586 527 108 THR CB C 68.9 0.2 1 587 527 108 THR N N 106.1 0.2 1 588 528 109 GLY H H 7.95 0.02 1 589 528 109 GLY HA2 H 3.61 0.02 1 590 528 109 GLY HA3 H 4.31 0.02 1 591 528 109 GLY C C 173.6 0.2 1 592 528 109 GLY CA C 45.2 0.2 1 593 528 109 GLY N N 108.8 0.2 1 594 529 110 LYS H H 7.99 0.02 1 595 529 110 LYS HA H 4.46 0.02 1 596 529 110 LYS C C 176.4 0.2 1 597 529 110 LYS CA C 55 0.2 1 598 529 110 LYS CB C 32.8 0.2 1 599 529 110 LYS N N 120 0.2 1 600 530 111 LEU H H 8.61 0.02 1 601 530 111 LEU HA H 4.16 0.02 1 602 530 111 LEU C C 177 0.2 1 603 530 111 LEU CA C 56.7 0.2 1 604 530 111 LEU CB C 41.9 0.2 1 605 530 111 LEU N N 124.2 0.2 1 606 531 112 ASP H H 8.23 0.02 1 607 531 112 ASP HA H 4.75 0.02 1 608 531 112 ASP C C 174.8 0.2 1 609 531 112 ASP CA C 52 0.2 1 610 531 112 ASP CB C 40.2 0.2 1 611 531 112 ASP N N 122.9 0.2 1 612 532 113 ALA H H 8.2 0.02 1 613 532 113 ALA HA H 3.94 0.02 1 614 532 113 ALA C C 179.4 0.2 1 615 532 113 ALA CA C 55.3 0.2 1 616 532 113 ALA CB C 18.9 0.2 1 617 532 113 ALA N N 126.9 0.2 1 618 533 114 ARG H H 8.16 0.02 1 619 533 114 ARG HA H 3.98 0.02 1 620 533 114 ARG C C 178.9 0.2 1 621 533 114 ARG CA C 59.3 0.2 1 622 533 114 ARG CB C 29.6 0.2 1 623 533 114 ARG N N 118.3 0.2 1 624 534 115 LYS H H 7.67 0.02 1 625 534 115 LYS HA H 4.02 0.02 1 626 534 115 LYS C C 179.1 0.2 1 627 534 115 LYS CA C 58.3 0.2 1 628 534 115 LYS CB C 32.5 0.2 1 629 534 115 LYS N N 120.3 0.2 1 630 535 116 ILE H H 8.17 0.02 1 631 535 116 ILE HA H 3.43 0.02 1 632 535 116 ILE C C 176.5 0.2 1 633 535 116 ILE CA C 66 0.2 1 634 535 116 ILE CB C 37.6 0.2 1 635 535 116 ILE N N 119.2 0.2 1 636 536 117 ARG H H 7.99 0.02 1 637 536 117 ARG HA H 3.74 0.02 1 638 536 117 ARG C C 177.2 0.2 1 639 536 117 ARG CA C 60.3 0.2 1 640 536 117 ARG CB C 30.2 0.2 1 641 536 117 ARG N N 118.7 0.2 1 642 537 118 GLU H H 7.76 0.02 1 643 537 118 GLU HA H 3.97 0.02 1 644 537 118 GLU C C 178.9 0.2 1 645 537 118 GLU CA C 59.7 0.2 1 646 537 118 GLU CB C 29.7 0.2 1 647 537 118 GLU N N 117.5 0.2 1 648 538 119 ILE H H 8.02 0.02 1 649 538 119 ILE HA H 3.63 0.02 1 650 538 119 ILE C C 178.7 0.2 1 651 538 119 ILE CA C 65.2 0.2 1 652 538 119 ILE N N 120.4 0.2 1 653 539 120 LEU H H 7.99 0.02 1 654 539 120 LEU HA H 4.45 0.02 1 655 539 120 LEU C C 178.2 0.2 1 656 539 120 LEU CA C 58.1 0.2 1 657 539 120 LEU CB C 42.5 0.2 1 658 539 120 LEU N N 119.7 0.2 1 659 540 121 ILE H H 8.6 0.02 1 660 540 121 ILE HA H 3.47 0.02 1 661 540 121 ILE C C 178.6 0.2 1 662 540 121 ILE CA C 65.4 0.2 1 663 540 121 ILE CB C 38.2 0.2 1 664 540 121 ILE N N 119 0.2 1 665 541 122 LYS H H 8.06 0.02 1 666 541 122 LYS HA H 3.98 0.02 1 667 541 122 LYS C C 178.4 0.2 1 668 541 122 LYS CA C 59.2 0.2 1 669 541 122 LYS CB C 32.6 0.2 1 670 541 122 LYS N N 119.6 0.2 1 671 542 123 ALA H H 7.84 0.02 1 672 542 123 ALA HA H 4.32 0.02 1 673 542 123 ALA C C 179.8 0.2 1 674 542 123 ALA CA C 54.3 0.2 1 675 542 123 ALA CB C 20.9 0.2 1 676 542 123 ALA N N 118.4 0.2 1 677 543 124 LYS H H 8.25 0.02 1 678 543 124 LYS HA H 4.48 0.02 1 679 543 124 LYS C C 177.8 0.2 1 680 543 124 LYS CA C 56 0.2 1 681 543 124 LYS CB C 33.8 0.2 1 682 543 124 LYS N N 114.3 0.2 1 683 544 125 LYS H H 8.15 0.02 1 684 544 125 LYS HA H 4.6 0.02 1 685 544 125 LYS C C 177.2 0.2 1 686 544 125 LYS CA C 55.8 0.2 1 687 544 125 LYS CB C 32.1 0.2 1 688 544 125 LYS N N 118.7 0.2 1 689 545 126 GLY H H 8.14 0.02 1 690 545 126 GLY HA2 H 4.04 0.02 1 691 545 126 GLY C C 174.7 0.2 1 692 545 126 GLY CA C 45.2 0.2 1 693 545 126 GLY N N 108.6 0.2 1 694 546 127 GLY H H 8.3 0.02 1 695 546 127 GLY HA2 H 4 0.02 1 696 546 127 GLY C C 174.1 0.2 1 697 546 127 GLY CA C 45.4 0.2 1 698 546 127 GLY N N 108.5 0.2 1 699 547 128 LYS H H 8.28 0.02 1 700 547 128 LYS HA H 4.45 0.02 1 701 547 128 LYS C C 176.6 0.2 1 702 547 128 LYS CA C 56 0.2 1 703 547 128 LYS CB C 33.1 0.2 1 704 547 128 LYS N N 120.7 0.2 1 705 548 129 SER H H 8.43 0.02 1 706 548 129 SER HA H 4.45 0.02 1 707 548 129 SER C C 174.1 0.2 1 708 548 129 SER CA C 58.3 0.2 1 709 548 129 SER CB C 63.6 0.2 1 710 548 129 SER N N 117.2 0.2 1 711 549 130 LYS H H 8.38 0.02 1 712 549 130 LYS HA H 4.43 0.02 1 713 549 130 LYS C C 175.2 0.2 1 714 549 130 LYS CA C 56.2 0.2 1 715 549 130 LYS CB C 32.8 0.2 1 716 549 130 LYS N N 123.8 0.2 1 717 550 131 LEU H H 7.97 0.02 1 718 550 131 LEU HA H 4.18 0.02 1 719 550 131 LEU CA C 56.8 0.2 1 720 550 131 LEU CB C 43.1 0.2 1 721 550 131 LEU N N 129.2 0.2 1 stop_ save_