data_5497 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5497 _Entry.Title ; 1H, 15N, 13C resonance assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2002-08-08 _Entry.Accession_date 2002-08-08 _Entry.Last_release_date 2002-12-23 _Entry.Original_release_date 2002-12-23 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Mark Bushell . . . 5497 2 Stuart Ferguson . J. . 5497 3 Christina Redfield . . . 5497 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5497 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 719 5497 '13C chemical shifts' 469 5497 '15N chemical shifts' 121 5497 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2002-12-23 2002-08-08 original author . 5497 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5497 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Letter to the Editor: 1H, 15N and 13C assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 24 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 359 _Citation.Page_last 360 _Citation.Year 2002 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 K. Bushell . 'Mark W.' . 5497 1 2 Stuart Ferguson . J. . 5497 1 3 Christina Redfield . . . 5497 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID DsbD 5497 1 DipZ 5497 1 'thiol-disulfide reductase' 5497 1 'electron transfer' 5497 1 periplasm 5497 1 'thioredoxin fold' 5497 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5497 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10760137 _Citation.Full_citation ; Gordon EH, Page MD, Willis AC, Ferguson SI Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function. MolMicrobiol. 2000 Mar:35(6):1360-74 ; _Citation.Title 'Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Mol. Microbiol.' _Citation.Journal_name_full 'Molecular microbiology' _Citation.Journal_volume 35 _Citation.Journal_issue 6 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0950-382X _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1360 _Citation.Page_last 1374 _Citation.Year 2000 _Citation.Details ; DipZ is a bacterial cytoplasmic membrane protein that transfers reducing power from the cytoplasm to the periplasm so as to facilitate the formation of correct disulphide bonds and c-type cytochromes in the latter compartment. Topological analysis using gene fusions between the Escherichia coli dipZ and either E. coli phoA or lacZ shows that DipZ has a highly hydrophobic central domain comprising eight transmembrane alpha-helices plus periplasmic globular N-terminal and C-terminal domains. The previously assigned translational start codon for the E. coli DipZ was shown to be incorrect and the protein to be larger than previously thought. The experimentally determined translational start position indicates that an additional alpha-helix at the N-terminus acts as a cleavable signal peptide so that the N-terminus of the mature protein is located in the periplasm. The newly assigned 5' end of the dipZ gene was shown to be preceded by a functional ribosome-binding site. The hydrophobic central domain and both of the periplasmic globular domains each have a pair of highly conserved cysteine residues, and it was shown by site directed mutagenesis that all six conserved cysteine residues contribute to DipZ function. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 E.H. Gordon E. H. . 5497 2 2 M.D. Page M. D. . 5497 2 3 A.C. Willis A. C. . 5497 2 4 S.J. Ferguson S. J. . 5497 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_DsbD_C-terminal_domain _Assembly.Sf_category assembly _Assembly.Sf_framecode system_DsbD_C-terminal_domain _Assembly.Entry_ID 5497 _Assembly.ID 1 _Assembly.Name 'DsbD C-terminal domain' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5497 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'DsbD C-terminal domain' 1 $DsbD_C_terminal_domain . . . native . . . . . 5497 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . . CYS 62 62 SG . 1 . 1 CYS 65 65 SG . . . . . . . . . . 5497 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'DsbD C-terminal domain' system 5497 1 'DsbD C-terminal domain' abbreviation 5497 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'thiol-disulfide reductase' 5497 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_DsbD_C_terminal_domain _Entity.Sf_category entity _Entity.Sf_framecode DsbD_C_terminal_domain _Entity.Entry_ID 5497 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'E. coli DsbD C-terminal domain' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MDIGINSDPVRPLQDWAFGA THTAQTQTHLNFTQIKTVDE LNQALVEAKGKPVMLDLYAD WCVACKEFEKYTFSDPQVQK ALADTVLLQANVTANDAQDV ALLKHLNVLGLPTILFFDGQ GQEHPQARVTGFMDAETFSA HLRDRQPKLAAALEHHHHHH ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 160 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; The first 9 residues and the last 13 residues are from the expression vector. Residues 10-147 correspond to residues 409 to 546 of the E. coli DsbD sequence. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1UC7 . "Crystal Structure Of Dsbdgamma" . . . . . 78.13 125 100.00 100.00 5.34e-85 . . . . 5497 1 2 no PDB 4IP1 . "C-terminal Domain Of The Thiol:disulfide Interchange Protein Dsbd, Q488k Mutant" . . . . . 77.50 132 98.39 99.19 9.29e-83 . . . . 5497 1 3 no PDB 4IP6 . "C-terminal Domain Of The Thiol:disulfide Interchange Protein Dsbd, Q488a Mutant" . . . . . 77.50 132 98.39 98.39 2.48e-82 . . . . 5497 1 4 no DBJ BAB38540 . "thiol:disulfide interchange protein [Escherichia coli O157:H7 str. Sakai]" . . . . . 86.25 565 100.00 100.00 7.95e-92 . . . . 5497 1 5 no DBJ BAE78138 . "fused thiol:disulfide interchange protein [Escherichia coli str. K-12 substr. W3110]" . . . . . 86.25 565 100.00 100.00 1.03e-91 . . . . 5497 1 6 no DBJ BAG66862 . "fused thiol:disulfide interchange protein: activator of DsbC/conserved protein [Escherichia coli O111:H-]" . . . . . 86.25 565 100.00 100.00 7.54e-92 . . . . 5497 1 7 no DBJ BAG79959 . "thiol:disulfide interchange protein [Escherichia coli SE11]" . . . . . 86.25 565 100.00 100.00 8.04e-92 . . . . 5497 1 8 no DBJ BAI28440 . "fused thiol: disulfide interchange protein: activator of DsbC/conserved protein [Escherichia coli O26:H11 str. 11368]" . . . . . 86.25 565 99.28 99.28 4.23e-91 . . . . 5497 1 9 no EMBL CAA54781 . "disulphide isomerase like protein [Escherichia coli K-12]" . . . . . 86.25 489 100.00 100.00 4.76e-93 . . . . 5497 1 10 no EMBL CAA85375 . "inner membrane copper tolerance protein [Escherichia coli str. K-12 substr. W3110]" . . . . . 86.25 489 100.00 100.00 4.76e-93 . . . . 5497 1 11 no EMBL CAP78654 . "Thiol:disulfide interchange protein dsbD [Escherichia coli LF82]" . . . . . 86.25 565 100.00 100.00 7.07e-92 . . . . 5497 1 12 no EMBL CAQ34485 . "DsbD[reduced] [Escherichia coli BL21(DE3)]" . . . . . 86.25 565 100.00 100.00 8.48e-92 . . . . 5497 1 13 no EMBL CAR01112 . "fused thiol:disulfide interchange protein: activator of DsbC ; conserved hypothetical protein [Escherichia coli IAI1]" . . . . . 86.25 565 100.00 100.00 7.54e-92 . . . . 5497 1 14 no GB AAA97035 . "cycZ [Escherichia coli str. K-12 substr. MG1655]" . . . . . 86.25 565 100.00 100.00 1.03e-91 . . . . 5497 1 15 no GB AAC77096 . "thiol:disulfide interchange protein and activator of DsbC [Escherichia coli str. K-12 substr. MG1655]" . . . . . 86.25 565 100.00 100.00 1.03e-91 . . . . 5497 1 16 no GB AAG59335 . "thiol:disulfide interchange protein; copper tolerance [Escherichia coli O157:H7 str. EDL933]" . . . . . 86.25 565 100.00 100.00 7.95e-92 . . . . 5497 1 17 no GB AAL50628 . "DsbD [Shigella flexneri 2a]" . . . . . 58.13 94 100.00 100.00 1.02e-60 . . . . 5497 1 18 no GB AAN45708 . "thiol:disulfide interchange protein [Shigella flexneri 2a str. 301]" . . . . . 86.25 565 100.00 100.00 8.12e-92 . . . . 5497 1 19 no REF NP_290769 . "thiol:disulfide interchange protein [Escherichia coli O157:H7 str. EDL933]" . . . . . 86.25 565 100.00 100.00 7.95e-92 . . . . 5497 1 20 no REF NP_313144 . "thiol:disulfide interchange protein [Escherichia coli O157:H7 str. Sakai]" . . . . . 86.25 565 100.00 100.00 7.95e-92 . . . . 5497 1 21 no REF NP_418559 . "thiol:disulfide interchange protein and activator of DsbC [Escherichia coli str. K-12 substr. MG1655]" . . . . . 86.25 565 100.00 100.00 1.03e-91 . . . . 5497 1 22 no REF NP_710001 . "thiol:disulfide interchange protein [Shigella flexneri 2a str. 301]" . . . . . 86.25 565 100.00 100.00 8.12e-92 . . . . 5497 1 23 no REF NP_757066 . "thiol:disulfide interchange protein [Escherichia coli CFT073]" . . . . . 86.25 565 99.28 100.00 2.70e-91 . . . . 5497 1 24 no SP P36655 . "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=C-type cytochrome biogenesis protein CycZ; AltName: Full=" . . . . . 86.25 565 100.00 100.00 1.03e-91 . . . . 5497 1 25 no SP P58162 . "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" . . . . . 86.25 565 100.00 100.00 7.95e-92 . . . . 5497 1 26 no SP Q0SXE3 . "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" . . . . . 86.25 565 100.00 100.00 7.54e-92 . . . . 5497 1 27 no SP Q0T9Q5 . "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" . . . . . 86.25 565 99.28 99.28 5.77e-91 . . . . 5497 1 28 no SP Q1R3C4 . "RecName: Full=Thiol:disulfide interchange protein DsbD; AltName: Full=Protein-disulfide reductase; Short=Disulfide reductase; F" . . . . . 86.25 565 99.28 99.28 5.77e-91 . . . . 5497 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'E. coli DsbD C-terminal domain' common 5497 1 'DsbD C-terminal domain' abbreviation 5497 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 MET . 5497 1 2 2 ASP . 5497 1 3 3 ILE . 5497 1 4 4 GLY . 5497 1 5 5 ILE . 5497 1 6 6 ASN . 5497 1 7 7 SER . 5497 1 8 8 ASP . 5497 1 9 9 PRO . 5497 1 10 409 VAL . 5497 1 11 410 ARG . 5497 1 12 411 PRO . 5497 1 13 412 LEU . 5497 1 14 413 GLN . 5497 1 15 414 ASP . 5497 1 16 415 TRP . 5497 1 17 416 ALA . 5497 1 18 417 PHE . 5497 1 19 418 GLY . 5497 1 20 419 ALA . 5497 1 21 420 THR . 5497 1 22 421 HIS . 5497 1 23 422 THR . 5497 1 24 423 ALA . 5497 1 25 424 GLN . 5497 1 26 425 THR . 5497 1 27 426 GLN . 5497 1 28 427 THR . 5497 1 29 428 HIS . 5497 1 30 429 LEU . 5497 1 31 430 ASN . 5497 1 32 431 PHE . 5497 1 33 432 THR . 5497 1 34 433 GLN . 5497 1 35 434 ILE . 5497 1 36 435 LYS . 5497 1 37 436 THR . 5497 1 38 437 VAL . 5497 1 39 438 ASP . 5497 1 40 439 GLU . 5497 1 41 440 LEU . 5497 1 42 441 ASN . 5497 1 43 442 GLN . 5497 1 44 443 ALA . 5497 1 45 444 LEU . 5497 1 46 445 VAL . 5497 1 47 446 GLU . 5497 1 48 447 ALA . 5497 1 49 448 LYS . 5497 1 50 449 GLY . 5497 1 51 450 LYS . 5497 1 52 451 PRO . 5497 1 53 452 VAL . 5497 1 54 453 MET . 5497 1 55 454 LEU . 5497 1 56 455 ASP . 5497 1 57 456 LEU . 5497 1 58 457 TYR . 5497 1 59 458 ALA . 5497 1 60 459 ASP . 5497 1 61 460 TRP . 5497 1 62 461 CYS . 5497 1 63 462 VAL . 5497 1 64 463 ALA . 5497 1 65 464 CYS . 5497 1 66 465 LYS . 5497 1 67 466 GLU . 5497 1 68 467 PHE . 5497 1 69 468 GLU . 5497 1 70 469 LYS . 5497 1 71 470 TYR . 5497 1 72 471 THR . 5497 1 73 472 PHE . 5497 1 74 473 SER . 5497 1 75 474 ASP . 5497 1 76 475 PRO . 5497 1 77 476 GLN . 5497 1 78 477 VAL . 5497 1 79 478 GLN . 5497 1 80 479 LYS . 5497 1 81 480 ALA . 5497 1 82 481 LEU . 5497 1 83 482 ALA . 5497 1 84 483 ASP . 5497 1 85 484 THR . 5497 1 86 485 VAL . 5497 1 87 486 LEU . 5497 1 88 487 LEU . 5497 1 89 488 GLN . 5497 1 90 489 ALA . 5497 1 91 490 ASN . 5497 1 92 491 VAL . 5497 1 93 492 THR . 5497 1 94 493 ALA . 5497 1 95 494 ASN . 5497 1 96 495 ASP . 5497 1 97 496 ALA . 5497 1 98 497 GLN . 5497 1 99 498 ASP . 5497 1 100 499 VAL . 5497 1 101 500 ALA . 5497 1 102 501 LEU . 5497 1 103 502 LEU . 5497 1 104 503 LYS . 5497 1 105 504 HIS . 5497 1 106 505 LEU . 5497 1 107 506 ASN . 5497 1 108 507 VAL . 5497 1 109 508 LEU . 5497 1 110 509 GLY . 5497 1 111 510 LEU . 5497 1 112 511 PRO . 5497 1 113 512 THR . 5497 1 114 513 ILE . 5497 1 115 514 LEU . 5497 1 116 515 PHE . 5497 1 117 516 PHE . 5497 1 118 517 ASP . 5497 1 119 518 GLY . 5497 1 120 519 GLN . 5497 1 121 520 GLY . 5497 1 122 521 GLN . 5497 1 123 522 GLU . 5497 1 124 523 HIS . 5497 1 125 524 PRO . 5497 1 126 525 GLN . 5497 1 127 526 ALA . 5497 1 128 527 ARG . 5497 1 129 528 VAL . 5497 1 130 529 THR . 5497 1 131 530 GLY . 5497 1 132 531 PHE . 5497 1 133 532 MET . 5497 1 134 533 ASP . 5497 1 135 534 ALA . 5497 1 136 535 GLU . 5497 1 137 536 THR . 5497 1 138 537 PHE . 5497 1 139 538 SER . 5497 1 140 539 ALA . 5497 1 141 540 HIS . 5497 1 142 541 LEU . 5497 1 143 542 ARG . 5497 1 144 543 ASP . 5497 1 145 544 ARG . 5497 1 146 545 GLN . 5497 1 147 546 PRO . 5497 1 148 148 LYS . 5497 1 149 149 LEU . 5497 1 150 150 ALA . 5497 1 151 151 ALA . 5497 1 152 152 ALA . 5497 1 153 153 LEU . 5497 1 154 154 GLU . 5497 1 155 155 HIS . 5497 1 156 156 HIS . 5497 1 157 157 HIS . 5497 1 158 158 HIS . 5497 1 159 159 HIS . 5497 1 160 160 HIS . 5497 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 5497 1 . ASP 2 2 5497 1 . ILE 3 3 5497 1 . GLY 4 4 5497 1 . ILE 5 5 5497 1 . ASN 6 6 5497 1 . SER 7 7 5497 1 . ASP 8 8 5497 1 . PRO 9 9 5497 1 . VAL 10 10 5497 1 . ARG 11 11 5497 1 . PRO 12 12 5497 1 . LEU 13 13 5497 1 . GLN 14 14 5497 1 . ASP 15 15 5497 1 . TRP 16 16 5497 1 . ALA 17 17 5497 1 . PHE 18 18 5497 1 . GLY 19 19 5497 1 . ALA 20 20 5497 1 . THR 21 21 5497 1 . HIS 22 22 5497 1 . THR 23 23 5497 1 . ALA 24 24 5497 1 . GLN 25 25 5497 1 . THR 26 26 5497 1 . GLN 27 27 5497 1 . THR 28 28 5497 1 . HIS 29 29 5497 1 . LEU 30 30 5497 1 . ASN 31 31 5497 1 . PHE 32 32 5497 1 . THR 33 33 5497 1 . GLN 34 34 5497 1 . ILE 35 35 5497 1 . LYS 36 36 5497 1 . THR 37 37 5497 1 . VAL 38 38 5497 1 . ASP 39 39 5497 1 . GLU 40 40 5497 1 . LEU 41 41 5497 1 . ASN 42 42 5497 1 . GLN 43 43 5497 1 . ALA 44 44 5497 1 . LEU 45 45 5497 1 . VAL 46 46 5497 1 . GLU 47 47 5497 1 . ALA 48 48 5497 1 . LYS 49 49 5497 1 . GLY 50 50 5497 1 . LYS 51 51 5497 1 . PRO 52 52 5497 1 . VAL 53 53 5497 1 . MET 54 54 5497 1 . LEU 55 55 5497 1 . ASP 56 56 5497 1 . LEU 57 57 5497 1 . TYR 58 58 5497 1 . ALA 59 59 5497 1 . ASP 60 60 5497 1 . TRP 61 61 5497 1 . CYS 62 62 5497 1 . VAL 63 63 5497 1 . ALA 64 64 5497 1 . CYS 65 65 5497 1 . LYS 66 66 5497 1 . GLU 67 67 5497 1 . PHE 68 68 5497 1 . GLU 69 69 5497 1 . LYS 70 70 5497 1 . TYR 71 71 5497 1 . THR 72 72 5497 1 . PHE 73 73 5497 1 . SER 74 74 5497 1 . ASP 75 75 5497 1 . PRO 76 76 5497 1 . GLN 77 77 5497 1 . VAL 78 78 5497 1 . GLN 79 79 5497 1 . LYS 80 80 5497 1 . ALA 81 81 5497 1 . LEU 82 82 5497 1 . ALA 83 83 5497 1 . ASP 84 84 5497 1 . THR 85 85 5497 1 . VAL 86 86 5497 1 . LEU 87 87 5497 1 . LEU 88 88 5497 1 . GLN 89 89 5497 1 . ALA 90 90 5497 1 . ASN 91 91 5497 1 . VAL 92 92 5497 1 . THR 93 93 5497 1 . ALA 94 94 5497 1 . ASN 95 95 5497 1 . ASP 96 96 5497 1 . ALA 97 97 5497 1 . GLN 98 98 5497 1 . ASP 99 99 5497 1 . VAL 100 100 5497 1 . ALA 101 101 5497 1 . LEU 102 102 5497 1 . LEU 103 103 5497 1 . LYS 104 104 5497 1 . HIS 105 105 5497 1 . LEU 106 106 5497 1 . ASN 107 107 5497 1 . VAL 108 108 5497 1 . LEU 109 109 5497 1 . GLY 110 110 5497 1 . LEU 111 111 5497 1 . PRO 112 112 5497 1 . THR 113 113 5497 1 . ILE 114 114 5497 1 . LEU 115 115 5497 1 . PHE 116 116 5497 1 . PHE 117 117 5497 1 . ASP 118 118 5497 1 . GLY 119 119 5497 1 . GLN 120 120 5497 1 . GLY 121 121 5497 1 . GLN 122 122 5497 1 . GLU 123 123 5497 1 . HIS 124 124 5497 1 . PRO 125 125 5497 1 . GLN 126 126 5497 1 . ALA 127 127 5497 1 . ARG 128 128 5497 1 . VAL 129 129 5497 1 . THR 130 130 5497 1 . GLY 131 131 5497 1 . PHE 132 132 5497 1 . MET 133 133 5497 1 . ASP 134 134 5497 1 . ALA 135 135 5497 1 . GLU 136 136 5497 1 . THR 137 137 5497 1 . PHE 138 138 5497 1 . SER 139 139 5497 1 . ALA 140 140 5497 1 . HIS 141 141 5497 1 . LEU 142 142 5497 1 . ARG 143 143 5497 1 . ASP 144 144 5497 1 . ARG 145 145 5497 1 . GLN 146 146 5497 1 . PRO 147 147 5497 1 . LYS 148 148 5497 1 . LEU 149 149 5497 1 . ALA 150 150 5497 1 . ALA 151 151 5497 1 . ALA 152 152 5497 1 . LEU 153 153 5497 1 . GLU 154 154 5497 1 . HIS 155 155 5497 1 . HIS 156 156 5497 1 . HIS 157 157 5497 1 . HIS 158 158 5497 1 . HIS 159 159 5497 1 . HIS 160 160 5497 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 5497 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $DsbD_C_terminal_domain . 562 organism . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli K12 . . . . . . . . . . . periplasm . . . DsbD . . . . 5497 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 5497 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $DsbD_C_terminal_domain . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli JM109(DE3) . . . . . . . . . . . . plasmid . . pET22b(+) . . . . . . 5497 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Sample.Sf_category sample _Sample.Sf_framecode sample1 _Sample.Entry_ID 5497 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'E. coli DsbD C-terminal domain' '[U-99% 15N]' . . 1 $DsbD_C_terminal_domain . . 1.5 . . mM . . . . 5497 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5497 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'E. coli DsbD C-terminal domain' '[U-95% 13C; U-99% 15N]' . . 1 $DsbD_C_terminal_domain . . 1.5 . . mM . . . . 5497 2 stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_1 _Sample_condition_list.Entry_ID 5497 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; Sample was in the oxidised state throughout the course of the data collection. ; loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.5 0.1 n/a 5497 1 temperature 298 1 K 5497 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 5497 _Software.ID 1 _Software.Name FELIX _Software.Version 2.3 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 5497 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer1 _NMR_spectrometer.Entry_ID 5497 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer 'home built' _NMR_spectrometer.Model . _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer2 _NMR_spectrometer.Entry_ID 5497 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer 'home built' _NMR_spectrometer.Model . _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5497 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer1 'home built' . . 600 . . . 5497 1 2 NMR_spectrometer2 'home built' . . 750 . . . 5497 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 5497 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 'The home-built spectrometers are equipped with Oxford Instruments' . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 5497 1 2 'Company magnets, Omega software and digital control equipment' . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 5497 1 3 '(Bruker), home-built triple resonance pulsed field gradient probe' . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 5497 1 4 'heads and home-built linear amplifiers.' . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 5497 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5497 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5497 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5497 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5497 1 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5497 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details ; ALA 458 and MET 532 have very upfield shifted H resonances. ; _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 2 $sample_2 . 5497 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 25 25 GLN C C 13 175.341 0.1 . 1 . . . . . . . . 5497 1 2 . 1 1 26 26 THR H H 1 8.250 0.01 . 1 . . . . . . . . 5497 1 3 . 1 1 26 26 THR HA H 1 4.32 0.01 . 1 . . . . . . . . 5497 1 4 . 1 1 26 26 THR HB H 1 4.23 0.01 . 1 . . . . . . . . 5497 1 5 . 1 1 26 26 THR HG21 H 1 1.18 0.01 . 1 . . . . . . . . 5497 1 6 . 1 1 26 26 THR HG22 H 1 1.18 0.01 . 1 . . . . . . . . 5497 1 7 . 1 1 26 26 THR HG23 H 1 1.18 0.01 . 1 . . . . . . . . 5497 1 8 . 1 1 26 26 THR C C 13 173.702 0.1 . 1 . . . . . . . . 5497 1 9 . 1 1 26 26 THR CA C 13 61.43 0.1 . 1 . . . . . . . . 5497 1 10 . 1 1 26 26 THR CB C 13 69.10 0.1 . 1 . . . . . . . . 5497 1 11 . 1 1 26 26 THR CG2 C 13 21.10 0.1 . 1 . . . . . . . . 5497 1 12 . 1 1 26 26 THR N N 15 115.364 0.1 . 1 . . . . . . . . 5497 1 13 . 1 1 27 27 GLN H H 1 8.457 0.01 . 1 . . . . . . . . 5497 1 14 . 1 1 27 27 GLN HA H 1 4.44 0.01 . 1 . . . . . . . . 5497 1 15 . 1 1 27 27 GLN HB2 H 1 2.10 0.01 . 2 . . . . . . . . 5497 1 16 . 1 1 27 27 GLN HB3 H 1 1.99 0.01 . 2 . . . . . . . . 5497 1 17 . 1 1 27 27 GLN HG2 H 1 2.34 0.01 . 2 . . . . . . . . 5497 1 18 . 1 1 27 27 GLN C C 13 175.226 0.1 . 1 . . . . . . . . 5497 1 19 . 1 1 27 27 GLN CA C 13 55.22 0.1 . 1 . . . . . . . . 5497 1 20 . 1 1 27 27 GLN CB C 13 29.08 0.1 . 1 . . . . . . . . 5497 1 21 . 1 1 27 27 GLN CG C 13 33.26 0.1 . 1 . . . . . . . . 5497 1 22 . 1 1 27 27 GLN N N 15 123.325 0.1 . 1 . . . . . . . . 5497 1 23 . 1 1 28 28 THR H H 1 8.260 0.01 . 1 . . . . . . . . 5497 1 24 . 1 1 28 28 THR HA H 1 4.32 0.01 . 1 . . . . . . . . 5497 1 25 . 1 1 28 28 THR HB H 1 4.23 0.01 . 1 . . . . . . . . 5497 1 26 . 1 1 28 28 THR HG21 H 1 1.13 0.01 . 1 . . . . . . . . 5497 1 27 . 1 1 28 28 THR HG22 H 1 1.13 0.01 . 1 . . . . . . . . 5497 1 28 . 1 1 28 28 THR HG23 H 1 1.13 0.01 . 1 . . . . . . . . 5497 1 29 . 1 1 28 28 THR C C 13 173.149 0.1 . 1 . . . . . . . . 5497 1 30 . 1 1 28 28 THR CA C 13 61.00 0.1 . 1 . . . . . . . . 5497 1 31 . 1 1 28 28 THR CB C 13 69.28 0.1 . 1 . . . . . . . . 5497 1 32 . 1 1 28 28 THR CG2 C 13 20.99 0.1 . 1 . . . . . . . . 5497 1 33 . 1 1 28 28 THR N N 15 115.846 0.1 . 1 . . . . . . . . 5497 1 34 . 1 1 29 29 HIS H H 1 8.270 0.01 . 1 . . . . . . . . 5497 1 35 . 1 1 29 29 HIS HA H 1 4.71 0.01 . 1 . . . . . . . . 5497 1 36 . 1 1 29 29 HIS HB2 H 1 3.06 0.01 . 2 . . . . . . . . 5497 1 37 . 1 1 29 29 HIS HB3 H 1 3.21 0.01 . 2 . . . . . . . . 5497 1 38 . 1 1 29 29 HIS C C 13 173.803 0.1 . 1 . . . . . . . . 5497 1 39 . 1 1 29 29 HIS CA C 13 54.45 0.1 . 1 . . . . . . . . 5497 1 40 . 1 1 29 29 HIS CB C 13 30.15 0.1 . 1 . . . . . . . . 5497 1 41 . 1 1 29 29 HIS N N 15 120.008 0.1 . 1 . . . . . . . . 5497 1 42 . 1 1 30 30 LEU H H 1 8.475 0.01 . 1 . . . . . . . . 5497 1 43 . 1 1 30 30 LEU HA H 1 4.04 0.01 . 1 . . . . . . . . 5497 1 44 . 1 1 30 30 LEU HB2 H 1 1.21 0.01 . 2 . . . . . . . . 5497 1 45 . 1 1 30 30 LEU HB3 H 1 0.62 0.01 . 2 . . . . . . . . 5497 1 46 . 1 1 30 30 LEU HG H 1 1.58 0.01 . 1 . . . . . . . . 5497 1 47 . 1 1 30 30 LEU HD11 H 1 0.34 0.01 . 2 . . . . . . . . 5497 1 48 . 1 1 30 30 LEU HD12 H 1 0.34 0.01 . 2 . . . . . . . . 5497 1 49 . 1 1 30 30 LEU HD13 H 1 0.34 0.01 . 2 . . . . . . . . 5497 1 50 . 1 1 30 30 LEU HD21 H 1 0.62 0.01 . 2 . . . . . . . . 5497 1 51 . 1 1 30 30 LEU HD22 H 1 0.62 0.01 . 2 . . . . . . . . 5497 1 52 . 1 1 30 30 LEU HD23 H 1 0.62 0.01 . 2 . . . . . . . . 5497 1 53 . 1 1 30 30 LEU C C 13 175.598 0.1 . 1 . . . . . . . . 5497 1 54 . 1 1 30 30 LEU CA C 13 53.84 0.1 . 1 . . . . . . . . 5497 1 55 . 1 1 30 30 LEU CB C 13 41.03 0.1 . 1 . . . . . . . . 5497 1 56 . 1 1 30 30 LEU CG C 13 25.94 0.1 . 1 . . . . . . . . 5497 1 57 . 1 1 30 30 LEU CD1 C 13 25.40 0.1 . 2 . . . . . . . . 5497 1 58 . 1 1 30 30 LEU CD2 C 13 22.85 0.1 . 2 . . . . . . . . 5497 1 59 . 1 1 30 30 LEU N N 15 122.169 0.1 . 1 . . . . . . . . 5497 1 60 . 1 1 31 31 ASN H H 1 8.422 0.01 . 1 . . . . . . . . 5497 1 61 . 1 1 31 31 ASN HA H 1 4.80 0.01 . 1 . . . . . . . . 5497 1 62 . 1 1 31 31 ASN HB2 H 1 2.72 0.01 . 2 . . . . . . . . 5497 1 63 . 1 1 31 31 ASN HB3 H 1 2.56 0.01 . 2 . . . . . . . . 5497 1 64 . 1 1 31 31 ASN HD21 H 1 7.459 0.01 . 2 . . . . . . . . 5497 1 65 . 1 1 31 31 ASN HD22 H 1 6.762 0.01 . 2 . . . . . . . . 5497 1 66 . 1 1 31 31 ASN C C 13 173.377 0.1 . 1 . . . . . . . . 5497 1 67 . 1 1 31 31 ASN CA C 13 51.54 0.1 . 1 . . . . . . . . 5497 1 68 . 1 1 31 31 ASN CB C 13 37.57 0.1 . 1 . . . . . . . . 5497 1 69 . 1 1 31 31 ASN CG C 13 176.405 0.1 . 1 . . . . . . . . 5497 1 70 . 1 1 31 31 ASN N N 15 122.063 0.1 . 1 . . . . . . . . 5497 1 71 . 1 1 31 31 ASN ND2 N 15 113.075 0.1 . 1 . . . . . . . . 5497 1 72 . 1 1 32 32 PHE H H 1 8.165 0.01 . 1 . . . . . . . . 5497 1 73 . 1 1 32 32 PHE HA H 1 4.29 0.01 . 1 . . . . . . . . 5497 1 74 . 1 1 32 32 PHE HB2 H 1 2.47 0.01 . 1 . . . . . . . . 5497 1 75 . 1 1 32 32 PHE HB3 H 1 2.47 0.01 . 1 . . . . . . . . 5497 1 76 . 1 1 32 32 PHE C C 13 176.557 0.1 . 1 . . . . . . . . 5497 1 77 . 1 1 32 32 PHE CA C 13 57.38 0.1 . 1 . . . . . . . . 5497 1 78 . 1 1 32 32 PHE CB C 13 40.98 0.1 . 1 . . . . . . . . 5497 1 79 . 1 1 32 32 PHE N N 15 121.703 0.1 . 1 . . . . . . . . 5497 1 80 . 1 1 33 33 THR H H 1 8.804 0.01 . 1 . . . . . . . . 5497 1 81 . 1 1 33 33 THR HA H 1 4.38 0.01 . 1 . . . . . . . . 5497 1 82 . 1 1 33 33 THR HB H 1 4.13 0.01 . 1 . . . . . . . . 5497 1 83 . 1 1 33 33 THR C C 13 172.874 0.1 . 1 . . . . . . . . 5497 1 84 . 1 1 33 33 THR CA C 13 62.51 0.1 . 1 . . . . . . . . 5497 1 85 . 1 1 33 33 THR CB C 13 68.91 0.1 . 1 . . . . . . . . 5497 1 86 . 1 1 33 33 THR N N 15 122.127 0.1 . 1 . . . . . . . . 5497 1 87 . 1 1 34 34 GLN H H 1 8.809 0.01 . 1 . . . . . . . . 5497 1 88 . 1 1 34 34 GLN HA H 1 5.00 0.01 . 1 . . . . . . . . 5497 1 89 . 1 1 34 34 GLN HB2 H 1 2.06 0.01 . 2 . . . . . . . . 5497 1 90 . 1 1 34 34 GLN HB3 H 1 1.94 0.01 . 2 . . . . . . . . 5497 1 91 . 1 1 34 34 GLN HG2 H 1 2.36 0.01 . 2 . . . . . . . . 5497 1 92 . 1 1 34 34 GLN C C 13 175.618 0.1 . 1 . . . . . . . . 5497 1 93 . 1 1 34 34 GLN CA C 13 54.67 0.1 . 1 . . . . . . . . 5497 1 94 . 1 1 34 34 GLN CB C 13 28.67 0.1 . 1 . . . . . . . . 5497 1 95 . 1 1 34 34 GLN CG C 13 33.24 0.1 . 1 . . . . . . . . 5497 1 96 . 1 1 34 34 GLN N N 15 127.939 0.1 . 1 . . . . . . . . 5497 1 97 . 1 1 35 35 ILE H H 1 8.619 0.01 . 1 . . . . . . . . 5497 1 98 . 1 1 35 35 ILE HA H 1 4.55 0.01 . 1 . . . . . . . . 5497 1 99 . 1 1 35 35 ILE HB H 1 1.71 0.01 . 1 . . . . . . . . 5497 1 100 . 1 1 35 35 ILE HG12 H 1 0.89 0.01 . 2 . . . . . . . . 5497 1 101 . 1 1 35 35 ILE HG13 H 1 1.23 0.01 . 2 . . . . . . . . 5497 1 102 . 1 1 35 35 ILE HG21 H 1 0.75 0.01 . 1 . . . . . . . . 5497 1 103 . 1 1 35 35 ILE HG22 H 1 0.75 0.01 . 1 . . . . . . . . 5497 1 104 . 1 1 35 35 ILE HG23 H 1 0.75 0.01 . 1 . . . . . . . . 5497 1 105 . 1 1 35 35 ILE HD11 H 1 0.66 0.01 . 1 . . . . . . . . 5497 1 106 . 1 1 35 35 ILE HD12 H 1 0.66 0.01 . 1 . . . . . . . . 5497 1 107 . 1 1 35 35 ILE HD13 H 1 0.66 0.01 . 1 . . . . . . . . 5497 1 108 . 1 1 35 35 ILE C C 13 173.995 0.1 . 1 . . . . . . . . 5497 1 109 . 1 1 35 35 ILE CA C 13 58.12 0.1 . 1 . . . . . . . . 5497 1 110 . 1 1 35 35 ILE CB C 13 41.73 0.1 . 1 . . . . . . . . 5497 1 111 . 1 1 35 35 ILE CG1 C 13 25.64 0.1 . 1 . . . . . . . . 5497 1 112 . 1 1 35 35 ILE CG2 C 13 18.82 0.1 . 1 . . . . . . . . 5497 1 113 . 1 1 35 35 ILE CD1 C 13 14.16 0.1 . 1 . . . . . . . . 5497 1 114 . 1 1 35 35 ILE N N 15 119.244 0.1 . 1 . . . . . . . . 5497 1 115 . 1 1 36 36 LYS H H 1 9.104 0.01 . 1 . . . . . . . . 5497 1 116 . 1 1 36 36 LYS HA H 1 4.81 0.01 . 1 . . . . . . . . 5497 1 117 . 1 1 36 36 LYS HB2 H 1 2.21 0.01 . 2 . . . . . . . . 5497 1 118 . 1 1 36 36 LYS HB3 H 1 1.73 0.01 . 2 . . . . . . . . 5497 1 119 . 1 1 36 36 LYS C C 13 174.108 0.1 . 1 . . . . . . . . 5497 1 120 . 1 1 36 36 LYS CA C 13 54.99 0.1 . 1 . . . . . . . . 5497 1 121 . 1 1 36 36 LYS CB C 13 34.63 0.1 . 1 . . . . . . . . 5497 1 122 . 1 1 36 36 LYS N N 15 122.720 0.1 . 1 . . . . . . . . 5497 1 123 . 1 1 37 37 THR H H 1 6.909 0.01 . 1 . . . . . . . . 5497 1 124 . 1 1 37 37 THR HA H 1 5.24 0.01 . 1 . . . . . . . . 5497 1 125 . 1 1 37 37 THR HB H 1 4.65 0.01 . 1 . . . . . . . . 5497 1 126 . 1 1 37 37 THR C C 13 175.245 0.1 . 1 . . . . . . . . 5497 1 127 . 1 1 37 37 THR CA C 13 57.22 0.1 . 1 . . . . . . . . 5497 1 128 . 1 1 37 37 THR CB C 13 72.66 0.1 . 1 . . . . . . . . 5497 1 129 . 1 1 37 37 THR N N 15 102.723 0.1 . 1 . . . . . . . . 5497 1 130 . 1 1 38 38 VAL H H 1 8.349 0.01 . 1 . . . . . . . . 5497 1 131 . 1 1 38 38 VAL HA H 1 3.17 0.01 . 1 . . . . . . . . 5497 1 132 . 1 1 38 38 VAL HB H 1 1.78 0.01 . 1 . . . . . . . . 5497 1 133 . 1 1 38 38 VAL HG11 H 1 0.82 0.01 . 2 . . . . . . . . 5497 1 134 . 1 1 38 38 VAL HG12 H 1 0.82 0.01 . 2 . . . . . . . . 5497 1 135 . 1 1 38 38 VAL HG13 H 1 0.82 0.01 . 2 . . . . . . . . 5497 1 136 . 1 1 38 38 VAL HG21 H 1 0.24 0.01 . 2 . . . . . . . . 5497 1 137 . 1 1 38 38 VAL HG22 H 1 0.24 0.01 . 2 . . . . . . . . 5497 1 138 . 1 1 38 38 VAL HG23 H 1 0.24 0.01 . 2 . . . . . . . . 5497 1 139 . 1 1 38 38 VAL C C 13 176.443 0.1 . 1 . . . . . . . . 5497 1 140 . 1 1 38 38 VAL CA C 13 65.68 0.1 . 1 . . . . . . . . 5497 1 141 . 1 1 38 38 VAL CB C 13 31.34 0.1 . 1 . . . . . . . . 5497 1 142 . 1 1 38 38 VAL CG1 C 13 22.68 0.1 . 2 . . . . . . . . 5497 1 143 . 1 1 38 38 VAL CG2 C 13 19.36 0.1 . 2 . . . . . . . . 5497 1 144 . 1 1 38 38 VAL N N 15 120.368 0.1 . 1 . . . . . . . . 5497 1 145 . 1 1 39 39 ASP H H 1 7.937 0.01 . 1 . . . . . . . . 5497 1 146 . 1 1 39 39 ASP HA H 1 4.35 0.01 . 1 . . . . . . . . 5497 1 147 . 1 1 39 39 ASP HB2 H 1 2.49 0.01 . 2 . . . . . . . . 5497 1 148 . 1 1 39 39 ASP HB3 H 1 2.58 0.01 . 2 . . . . . . . . 5497 1 149 . 1 1 39 39 ASP C C 13 178.606 0.1 . 1 . . . . . . . . 5497 1 150 . 1 1 39 39 ASP CA C 13 56.76 0.1 . 1 . . . . . . . . 5497 1 151 . 1 1 39 39 ASP CB C 13 39.61 0.1 . 1 . . . . . . . . 5497 1 152 . 1 1 39 39 ASP N N 15 117.791 0.1 . 1 . . . . . . . . 5497 1 153 . 1 1 40 40 GLU H H 1 7.974 0.01 . 1 . . . . . . . . 5497 1 154 . 1 1 40 40 GLU HA H 1 3.95 0.01 . 1 . . . . . . . . 5497 1 155 . 1 1 40 40 GLU HB2 H 1 2.00 0.01 . 2 . . . . . . . . 5497 1 156 . 1 1 40 40 GLU HB3 H 1 2.28 0.01 . 2 . . . . . . . . 5497 1 157 . 1 1 40 40 GLU HG2 H 1 2.41 0.01 . 2 . . . . . . . . 5497 1 158 . 1 1 40 40 GLU HG3 H 1 2.28 0.01 . 2 . . . . . . . . 5497 1 159 . 1 1 40 40 GLU C C 13 179.333 0.1 . 1 . . . . . . . . 5497 1 160 . 1 1 40 40 GLU CA C 13 58.84 0.1 . 1 . . . . . . . . 5497 1 161 . 1 1 40 40 GLU CB C 13 29.44 0.1 . 1 . . . . . . . . 5497 1 162 . 1 1 40 40 GLU CG C 13 36.49 0.1 . 1 . . . . . . . . 5497 1 163 . 1 1 40 40 GLU N N 15 120.982 0.1 . 1 . . . . . . . . 5497 1 164 . 1 1 41 41 LEU H H 1 8.267 0.01 . 1 . . . . . . . . 5497 1 165 . 1 1 41 41 LEU HA H 1 3.86 0.01 . 1 . . . . . . . . 5497 1 166 . 1 1 41 41 LEU HB2 H 1 2.17 0.01 . 2 . . . . . . . . 5497 1 167 . 1 1 41 41 LEU HB3 H 1 1.21 0.01 . 2 . . . . . . . . 5497 1 168 . 1 1 41 41 LEU HG H 1 1.38 0.01 . 1 . . . . . . . . 5497 1 169 . 1 1 41 41 LEU HD11 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 170 . 1 1 41 41 LEU HD12 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 171 . 1 1 41 41 LEU HD13 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 172 . 1 1 41 41 LEU HD21 H 1 0.57 0.01 . 2 . . . . . . . . 5497 1 173 . 1 1 41 41 LEU HD22 H 1 0.57 0.01 . 2 . . . . . . . . 5497 1 174 . 1 1 41 41 LEU HD23 H 1 0.57 0.01 . 2 . . . . . . . . 5497 1 175 . 1 1 41 41 LEU C C 13 176.430 0.1 . 1 . . . . . . . . 5497 1 176 . 1 1 41 41 LEU CA C 13 57.63 0.1 . 1 . . . . . . . . 5497 1 177 . 1 1 41 41 LEU CB C 13 39.66 0.1 . 1 . . . . . . . . 5497 1 178 . 1 1 41 41 LEU CG C 13 26.68 0.1 . 1 . . . . . . . . 5497 1 179 . 1 1 41 41 LEU CD1 C 13 26.88 0.1 . 2 . . . . . . . . 5497 1 180 . 1 1 41 41 LEU CD2 C 13 22.33 0.1 . 2 . . . . . . . . 5497 1 181 . 1 1 41 41 LEU N N 15 123.258 0.1 . 1 . . . . . . . . 5497 1 182 . 1 1 42 42 ASN H H 1 8.400 0.01 . 1 . . . . . . . . 5497 1 183 . 1 1 42 42 ASN HA H 1 4.36 0.01 . 1 . . . . . . . . 5497 1 184 . 1 1 42 42 ASN HB2 H 1 2.85 0.01 . 2 . . . . . . . . 5497 1 185 . 1 1 42 42 ASN HB3 H 1 2.74 0.01 . 2 . . . . . . . . 5497 1 186 . 1 1 42 42 ASN HD21 H 1 7.675 0.01 . 2 . . . . . . . . 5497 1 187 . 1 1 42 42 ASN HD22 H 1 6.396 0.01 . 2 . . . . . . . . 5497 1 188 . 1 1 42 42 ASN C C 13 177.787 0.1 . 1 . . . . . . . . 5497 1 189 . 1 1 42 42 ASN CA C 13 55.55 0.1 . 1 . . . . . . . . 5497 1 190 . 1 1 42 42 ASN CB C 13 36.70 0.1 . 1 . . . . . . . . 5497 1 191 . 1 1 42 42 ASN N N 15 117.153 0.1 . 1 . . . . . . . . 5497 1 192 . 1 1 42 42 ASN ND2 N 15 111.547 0.1 . 1 . . . . . . . . 5497 1 193 . 1 1 43 43 GLN H H 1 8.051 0.01 . 1 . . . . . . . . 5497 1 194 . 1 1 43 43 GLN HA H 1 4.03 0.01 . 1 . . . . . . . . 5497 1 195 . 1 1 43 43 GLN HB2 H 1 2.00 0.01 . 2 . . . . . . . . 5497 1 196 . 1 1 43 43 GLN HB3 H 1 2.12 0.01 . 2 . . . . . . . . 5497 1 197 . 1 1 43 43 GLN HG2 H 1 2.40 0.01 . 2 . . . . . . . . 5497 1 198 . 1 1 43 43 GLN C C 13 176.995 0.1 . 1 . . . . . . . . 5497 1 199 . 1 1 43 43 GLN CA C 13 57.88 0.1 . 1 . . . . . . . . 5497 1 200 . 1 1 43 43 GLN CB C 13 27.27 0.1 . 1 . . . . . . . . 5497 1 201 . 1 1 43 43 GLN CG C 13 32.58 0.1 . 1 . . . . . . . . 5497 1 202 . 1 1 43 43 GLN N N 15 120.327 0.1 . 1 . . . . . . . . 5497 1 203 . 1 1 44 44 ALA H H 1 8.104 0.01 . 1 . . . . . . . . 5497 1 204 . 1 1 44 44 ALA HA H 1 4.06 0.01 . 1 . . . . . . . . 5497 1 205 . 1 1 44 44 ALA HB1 H 1 1.39 0.01 . 1 . . . . . . . . 5497 1 206 . 1 1 44 44 ALA HB2 H 1 1.39 0.01 . 1 . . . . . . . . 5497 1 207 . 1 1 44 44 ALA HB3 H 1 1.39 0.01 . 1 . . . . . . . . 5497 1 208 . 1 1 44 44 ALA C C 13 180.361 0.1 . 1 . . . . . . . . 5497 1 209 . 1 1 44 44 ALA CA C 13 54.35 0.1 . 1 . . . . . . . . 5497 1 210 . 1 1 44 44 ALA CB C 13 17.75 0.1 . 1 . . . . . . . . 5497 1 211 . 1 1 44 44 ALA N N 15 123.333 0.1 . 1 . . . . . . . . 5497 1 212 . 1 1 45 45 LEU H H 1 8.257 0.01 . 1 . . . . . . . . 5497 1 213 . 1 1 45 45 LEU HA H 1 3.87 0.01 . 1 . . . . . . . . 5497 1 214 . 1 1 45 45 LEU HB2 H 1 1.92 0.01 . 2 . . . . . . . . 5497 1 215 . 1 1 45 45 LEU HB3 H 1 1.24 0.01 . 2 . . . . . . . . 5497 1 216 . 1 1 45 45 LEU HG H 1 1.49 0.01 . 1 . . . . . . . . 5497 1 217 . 1 1 45 45 LEU HD11 H 1 0.48 0.01 . 2 . . . . . . . . 5497 1 218 . 1 1 45 45 LEU HD12 H 1 0.48 0.01 . 2 . . . . . . . . 5497 1 219 . 1 1 45 45 LEU HD13 H 1 0.48 0.01 . 2 . . . . . . . . 5497 1 220 . 1 1 45 45 LEU HD21 H 1 0.07 0.01 . 2 . . . . . . . . 5497 1 221 . 1 1 45 45 LEU HD22 H 1 0.07 0.01 . 2 . . . . . . . . 5497 1 222 . 1 1 45 45 LEU HD23 H 1 0.07 0.01 . 2 . . . . . . . . 5497 1 223 . 1 1 45 45 LEU C C 13 179.420 0.1 . 1 . . . . . . . . 5497 1 224 . 1 1 45 45 LEU CA C 13 57.23 0.1 . 1 . . . . . . . . 5497 1 225 . 1 1 45 45 LEU CB C 13 40.44 0.1 . 1 . . . . . . . . 5497 1 226 . 1 1 45 45 LEU CG C 13 25.75 0.1 . 1 . . . . . . . . 5497 1 227 . 1 1 45 45 LEU CD1 C 13 24.66 0.1 . 2 . . . . . . . . 5497 1 228 . 1 1 45 45 LEU CD2 C 13 21.13 0.1 . 2 . . . . . . . . 5497 1 229 . 1 1 45 45 LEU N N 15 118.005 0.1 . 1 . . . . . . . . 5497 1 230 . 1 1 46 46 VAL H H 1 7.713 0.01 . 1 . . . . . . . . 5497 1 231 . 1 1 46 46 VAL HA H 1 3.66 0.01 . 1 . . . . . . . . 5497 1 232 . 1 1 46 46 VAL HB H 1 2.26 0.01 . 1 . . . . . . . . 5497 1 233 . 1 1 46 46 VAL HG11 H 1 1.06 0.01 . 2 . . . . . . . . 5497 1 234 . 1 1 46 46 VAL HG12 H 1 1.06 0.01 . 2 . . . . . . . . 5497 1 235 . 1 1 46 46 VAL HG13 H 1 1.06 0.01 . 2 . . . . . . . . 5497 1 236 . 1 1 46 46 VAL HG21 H 1 0.93 0.01 . 2 . . . . . . . . 5497 1 237 . 1 1 46 46 VAL HG22 H 1 0.93 0.01 . 2 . . . . . . . . 5497 1 238 . 1 1 46 46 VAL HG23 H 1 0.93 0.01 . 2 . . . . . . . . 5497 1 239 . 1 1 46 46 VAL C C 13 179.243 0.1 . 1 . . . . . . . . 5497 1 240 . 1 1 46 46 VAL CA C 13 65.91 0.1 . 1 . . . . . . . . 5497 1 241 . 1 1 46 46 VAL CB C 13 30.83 0.1 . 1 . . . . . . . . 5497 1 242 . 1 1 46 46 VAL CG1 C 13 22.23 0.1 . 2 . . . . . . . . 5497 1 243 . 1 1 46 46 VAL CG2 C 13 20.60 0.1 . 2 . . . . . . . . 5497 1 244 . 1 1 46 46 VAL N N 15 121.529 0.1 . 1 . . . . . . . . 5497 1 245 . 1 1 47 47 GLU H H 1 7.849 0.01 . 1 . . . . . . . . 5497 1 246 . 1 1 47 47 GLU HA H 1 4.04 0.01 . 1 . . . . . . . . 5497 1 247 . 1 1 47 47 GLU HB2 H 1 2.12 0.01 . 2 . . . . . . . . 5497 1 248 . 1 1 47 47 GLU HB3 H 1 2.02 0.01 . 2 . . . . . . . . 5497 1 249 . 1 1 47 47 GLU HG2 H 1 2.49 0.01 . 2 . . . . . . . . 5497 1 250 . 1 1 47 47 GLU HG3 H 1 2.30 0.01 . 2 . . . . . . . . 5497 1 251 . 1 1 47 47 GLU C C 13 176.601 0.1 . 1 . . . . . . . . 5497 1 252 . 1 1 47 47 GLU CA C 13 57.68 0.1 . 1 . . . . . . . . 5497 1 253 . 1 1 47 47 GLU CB C 13 28.60 0.1 . 1 . . . . . . . . 5497 1 254 . 1 1 47 47 GLU CG C 13 35.94 0.1 . 1 . . . . . . . . 5497 1 255 . 1 1 47 47 GLU N N 15 119.543 0.1 . 1 . . . . . . . . 5497 1 256 . 1 1 48 48 ALA H H 1 7.622 0.01 . 1 . . . . . . . . 5497 1 257 . 1 1 48 48 ALA HA H 1 4.34 0.01 . 1 . . . . . . . . 5497 1 258 . 1 1 48 48 ALA HB1 H 1 1.41 0.01 . 1 . . . . . . . . 5497 1 259 . 1 1 48 48 ALA HB2 H 1 1.41 0.01 . 1 . . . . . . . . 5497 1 260 . 1 1 48 48 ALA HB3 H 1 1.41 0.01 . 1 . . . . . . . . 5497 1 261 . 1 1 48 48 ALA C C 13 175.232 0.1 . 1 . . . . . . . . 5497 1 262 . 1 1 48 48 ALA CA C 13 51.73 0.1 . 1 . . . . . . . . 5497 1 263 . 1 1 48 48 ALA CB C 13 19.02 0.1 . 1 . . . . . . . . 5497 1 264 . 1 1 48 48 ALA N N 15 121.806 0.1 . 1 . . . . . . . . 5497 1 265 . 1 1 49 49 LYS H H 1 7.030 0.01 . 1 . . . . . . . . 5497 1 266 . 1 1 49 49 LYS HA H 1 4.09 0.01 . 1 . . . . . . . . 5497 1 267 . 1 1 49 49 LYS HB2 H 1 1.87 0.01 . 2 . . . . . . . . 5497 1 268 . 1 1 49 49 LYS HB3 H 1 1.82 0.01 . 2 . . . . . . . . 5497 1 269 . 1 1 49 49 LYS HG2 H 1 1.44 0.01 . 2 . . . . . . . . 5497 1 270 . 1 1 49 49 LYS HG3 H 1 1.57 0.01 . 2 . . . . . . . . 5497 1 271 . 1 1 49 49 LYS HD2 H 1 1.74 0.01 . 2 . . . . . . . . 5497 1 272 . 1 1 49 49 LYS HE2 H 1 3.02 0.01 . 2 . . . . . . . . 5497 1 273 . 1 1 49 49 LYS C C 13 176.864 0.1 . 1 . . . . . . . . 5497 1 274 . 1 1 49 49 LYS CA C 13 57.81 0.1 . 1 . . . . . . . . 5497 1 275 . 1 1 49 49 LYS CB C 13 31.07 0.1 . 1 . . . . . . . . 5497 1 276 . 1 1 49 49 LYS CG C 13 23.75 0.1 . 1 . . . . . . . . 5497 1 277 . 1 1 49 49 LYS CD C 13 28.50 0.1 . 1 . . . . . . . . 5497 1 278 . 1 1 49 49 LYS N N 15 118.084 0.1 . 1 . . . . . . . . 5497 1 279 . 1 1 50 50 GLY H H 1 9.144 0.01 . 1 . . . . . . . . 5497 1 280 . 1 1 50 50 GLY HA2 H 1 4.38 0.01 . 2 . . . . . . . . 5497 1 281 . 1 1 50 50 GLY HA3 H 1 3.75 0.01 . 2 . . . . . . . . 5497 1 282 . 1 1 50 50 GLY C C 13 173.347 0.1 . 1 . . . . . . . . 5497 1 283 . 1 1 50 50 GLY CA C 13 44.39 0.1 . 1 . . . . . . . . 5497 1 284 . 1 1 50 50 GLY N N 15 113.250 0.1 . 1 . . . . . . . . 5497 1 285 . 1 1 51 51 LYS H H 1 8.457 0.01 . 1 . . . . . . . . 5497 1 286 . 1 1 51 51 LYS HA H 1 4.83 0.01 . 1 . . . . . . . . 5497 1 287 . 1 1 51 51 LYS HB2 H 1 1.94 0.01 . 2 . . . . . . . . 5497 1 288 . 1 1 51 51 LYS HB3 H 1 1.79 0.01 . 2 . . . . . . . . 5497 1 289 . 1 1 51 51 LYS HG2 H 1 1.42 0.01 . 2 . . . . . . . . 5497 1 290 . 1 1 51 51 LYS HD2 H 1 1.65 0.01 . 2 . . . . . . . . 5497 1 291 . 1 1 51 51 LYS HD3 H 1 1.57 0.01 . 2 . . . . . . . . 5497 1 292 . 1 1 51 51 LYS HE2 H 1 2.94 0.01 . 1 . . . . . . . . 5497 1 293 . 1 1 51 51 LYS HE3 H 1 2.94 0.01 . 1 . . . . . . . . 5497 1 294 . 1 1 51 51 LYS CA C 13 53.13 0.1 . 1 . . . . . . . . 5497 1 295 . 1 1 51 51 LYS CB C 13 32.56 0.1 . 1 . . . . . . . . 5497 1 296 . 1 1 51 51 LYS CG C 13 24.50 0.1 . 1 . . . . . . . . 5497 1 297 . 1 1 51 51 LYS CD C 13 28.94 0.1 . 1 . . . . . . . . 5497 1 298 . 1 1 51 51 LYS N N 15 123.325 0.1 . 1 . . . . . . . . 5497 1 299 . 1 1 52 52 PRO HA H 1 4.52 0.01 . 1 . . . . . . . . 5497 1 300 . 1 1 52 52 PRO HB2 H 1 2.34 0.01 . 2 . . . . . . . . 5497 1 301 . 1 1 52 52 PRO HB3 H 1 2.07 0.01 . 2 . . . . . . . . 5497 1 302 . 1 1 52 52 PRO HG2 H 1 2.14 0.01 . 2 . . . . . . . . 5497 1 303 . 1 1 52 52 PRO HG3 H 1 1.84 0.01 . 2 . . . . . . . . 5497 1 304 . 1 1 52 52 PRO HD2 H 1 3.78 0.01 . 2 . . . . . . . . 5497 1 305 . 1 1 52 52 PRO HD3 H 1 3.88 0.01 . 2 . . . . . . . . 5497 1 306 . 1 1 52 52 PRO C C 13 174.690 0.1 . 1 . . . . . . . . 5497 1 307 . 1 1 52 52 PRO CA C 13 61.68 0.1 . 1 . . . . . . . . 5497 1 308 . 1 1 52 52 PRO CB C 13 31.49 0.1 . 1 . . . . . . . . 5497 1 309 . 1 1 52 52 PRO CG C 13 26.90 0.1 . 1 . . . . . . . . 5497 1 310 . 1 1 52 52 PRO CD C 13 49.38 0.1 . 1 . . . . . . . . 5497 1 311 . 1 1 53 53 VAL H H 1 8.067 0.01 . 1 . . . . . . . . 5497 1 312 . 1 1 53 53 VAL HA H 1 5.09 0.01 . 1 . . . . . . . . 5497 1 313 . 1 1 53 53 VAL HB H 1 1.80 0.01 . 1 . . . . . . . . 5497 1 314 . 1 1 53 53 VAL HG11 H 1 0.83 0.01 . 2 . . . . . . . . 5497 1 315 . 1 1 53 53 VAL HG12 H 1 0.83 0.01 . 2 . . . . . . . . 5497 1 316 . 1 1 53 53 VAL HG13 H 1 0.83 0.01 . 2 . . . . . . . . 5497 1 317 . 1 1 53 53 VAL HG21 H 1 0.65 0.01 . 2 . . . . . . . . 5497 1 318 . 1 1 53 53 VAL HG22 H 1 0.65 0.01 . 2 . . . . . . . . 5497 1 319 . 1 1 53 53 VAL HG23 H 1 0.65 0.01 . 2 . . . . . . . . 5497 1 320 . 1 1 53 53 VAL C C 13 174.380 0.1 . 1 . . . . . . . . 5497 1 321 . 1 1 53 53 VAL CA C 13 59.72 0.1 . 1 . . . . . . . . 5497 1 322 . 1 1 53 53 VAL CB C 13 35.91 0.1 . 1 . . . . . . . . 5497 1 323 . 1 1 53 53 VAL CG1 C 13 20.93 0.1 . 2 . . . . . . . . 5497 1 324 . 1 1 53 53 VAL CG2 C 13 20.77 0.1 . 2 . . . . . . . . 5497 1 325 . 1 1 53 53 VAL N N 15 119.112 0.1 . 1 . . . . . . . . 5497 1 326 . 1 1 54 54 MET H H 1 9.166 0.01 . 1 . . . . . . . . 5497 1 327 . 1 1 54 54 MET HA H 1 5.10 0.01 . 1 . . . . . . . . 5497 1 328 . 1 1 54 54 MET HB2 H 1 2.08 0.01 . 2 . . . . . . . . 5497 1 329 . 1 1 54 54 MET HB3 H 1 1.57 0.01 . 2 . . . . . . . . 5497 1 330 . 1 1 54 54 MET HG2 H 1 1.79 0.01 . 2 . . . . . . . . 5497 1 331 . 1 1 54 54 MET HG3 H 1 1.55 0.01 . 2 . . . . . . . . 5497 1 332 . 1 1 54 54 MET C C 13 171.770 0.1 . 1 . . . . . . . . 5497 1 333 . 1 1 54 54 MET CA C 13 53.39 0.1 . 1 . . . . . . . . 5497 1 334 . 1 1 54 54 MET CB C 13 37.85 0.1 . 1 . . . . . . . . 5497 1 335 . 1 1 54 54 MET CG C 13 33.12 0.1 . 1 . . . . . . . . 5497 1 336 . 1 1 54 54 MET N N 15 130.404 0.1 . 1 . . . . . . . . 5497 1 337 . 1 1 55 55 LEU H H 1 9.186 0.01 . 1 . . . . . . . . 5497 1 338 . 1 1 55 55 LEU HA H 1 5.27 0.01 . 1 . . . . . . . . 5497 1 339 . 1 1 55 55 LEU HB2 H 1 1.92 0.01 . 2 . . . . . . . . 5497 1 340 . 1 1 55 55 LEU HB3 H 1 1.09 0.01 . 2 . . . . . . . . 5497 1 341 . 1 1 55 55 LEU HG H 1 1.35 0.01 . 1 . . . . . . . . 5497 1 342 . 1 1 55 55 LEU HD11 H 1 0.89 0.01 . 2 . . . . . . . . 5497 1 343 . 1 1 55 55 LEU HD12 H 1 0.89 0.01 . 2 . . . . . . . . 5497 1 344 . 1 1 55 55 LEU HD13 H 1 0.89 0.01 . 2 . . . . . . . . 5497 1 345 . 1 1 55 55 LEU HD21 H 1 0.64 0.01 . 2 . . . . . . . . 5497 1 346 . 1 1 55 55 LEU HD22 H 1 0.64 0.01 . 2 . . . . . . . . 5497 1 347 . 1 1 55 55 LEU HD23 H 1 0.64 0.01 . 2 . . . . . . . . 5497 1 348 . 1 1 55 55 LEU C C 13 172.274 0.1 . 1 . . . . . . . . 5497 1 349 . 1 1 55 55 LEU CA C 13 51.84 0.1 . 1 . . . . . . . . 5497 1 350 . 1 1 55 55 LEU CB C 13 45.07 0.1 . 1 . . . . . . . . 5497 1 351 . 1 1 55 55 LEU CG C 13 27.13 0.1 . 1 . . . . . . . . 5497 1 352 . 1 1 55 55 LEU CD1 C 13 27.56 0.1 . 2 . . . . . . . . 5497 1 353 . 1 1 55 55 LEU CD2 C 13 23.12 0.1 . 2 . . . . . . . . 5497 1 354 . 1 1 55 55 LEU N N 15 128.732 0.1 . 1 . . . . . . . . 5497 1 355 . 1 1 56 56 ASP H H 1 8.926 0.01 . 1 . . . . . . . . 5497 1 356 . 1 1 56 56 ASP HA H 1 4.89 0.01 . 1 . . . . . . . . 5497 1 357 . 1 1 56 56 ASP HB2 H 1 2.23 0.01 . 2 . . . . . . . . 5497 1 358 . 1 1 56 56 ASP HB3 H 1 2.07 0.01 . 2 . . . . . . . . 5497 1 359 . 1 1 56 56 ASP C C 13 172.879 0.1 . 1 . . . . . . . . 5497 1 360 . 1 1 56 56 ASP CA C 13 52.93 0.1 . 1 . . . . . . . . 5497 1 361 . 1 1 56 56 ASP CB C 13 44.06 0.1 . 1 . . . . . . . . 5497 1 362 . 1 1 56 56 ASP N N 15 126.403 0.1 . 1 . . . . . . . . 5497 1 363 . 1 1 57 57 LEU H H 1 7.292 0.01 . 1 . . . . . . . . 5497 1 364 . 1 1 57 57 LEU HA H 1 4.87 0.01 . 1 . . . . . . . . 5497 1 365 . 1 1 57 57 LEU HB2 H 1 0.97 0.01 . 2 . . . . . . . . 5497 1 366 . 1 1 57 57 LEU HB3 H 1 2.06 0.01 . 2 . . . . . . . . 5497 1 367 . 1 1 57 57 LEU HG H 1 1.62 0.01 . 1 . . . . . . . . 5497 1 368 . 1 1 57 57 LEU HD11 H 1 0.71 0.01 . 2 . . . . . . . . 5497 1 369 . 1 1 57 57 LEU HD12 H 1 0.71 0.01 . 2 . . . . . . . . 5497 1 370 . 1 1 57 57 LEU HD13 H 1 0.71 0.01 . 2 . . . . . . . . 5497 1 371 . 1 1 57 57 LEU HD21 H 1 0.83 0.01 . 2 . . . . . . . . 5497 1 372 . 1 1 57 57 LEU HD22 H 1 0.83 0.01 . 2 . . . . . . . . 5497 1 373 . 1 1 57 57 LEU HD23 H 1 0.83 0.01 . 2 . . . . . . . . 5497 1 374 . 1 1 57 57 LEU C C 13 172.470 0.1 . 1 . . . . . . . . 5497 1 375 . 1 1 57 57 LEU CA C 13 53.15 0.1 . 1 . . . . . . . . 5497 1 376 . 1 1 57 57 LEU CB C 13 41.78 0.1 . 1 . . . . . . . . 5497 1 377 . 1 1 57 57 LEU CG C 13 26.44 0.1 . 1 . . . . . . . . 5497 1 378 . 1 1 57 57 LEU CD1 C 13 23.90 0.1 . 2 . . . . . . . . 5497 1 379 . 1 1 57 57 LEU CD2 C 13 27.35 0.1 . 2 . . . . . . . . 5497 1 380 . 1 1 57 57 LEU N N 15 125.412 0.1 . 1 . . . . . . . . 5497 1 381 . 1 1 58 58 TYR H H 1 8.746 0.01 . 1 . . . . . . . . 5497 1 382 . 1 1 58 58 TYR HA H 1 4.27 0.01 . 1 . . . . . . . . 5497 1 383 . 1 1 58 58 TYR HB2 H 1 2.82 0.01 . 2 . . . . . . . . 5497 1 384 . 1 1 58 58 TYR HB3 H 1 2.40 0.01 . 2 . . . . . . . . 5497 1 385 . 1 1 58 58 TYR C C 13 172.399 0.1 . 1 . . . . . . . . 5497 1 386 . 1 1 58 58 TYR CA C 13 56.99 0.1 . 1 . . . . . . . . 5497 1 387 . 1 1 58 58 TYR CB C 13 41.04 0.1 . 1 . . . . . . . . 5497 1 388 . 1 1 58 58 TYR N N 15 124.111 0.1 . 1 . . . . . . . . 5497 1 389 . 1 1 59 59 ALA H H 1 4.884 0.01 . 1 . . . . . . . . 5497 1 390 . 1 1 59 59 ALA HA H 1 3.73 0.01 . 1 . . . . . . . . 5497 1 391 . 1 1 59 59 ALA HB1 H 1 -0.55 0.01 . 1 . . . . . . . . 5497 1 392 . 1 1 59 59 ALA HB2 H 1 -0.55 0.01 . 1 . . . . . . . . 5497 1 393 . 1 1 59 59 ALA HB3 H 1 -0.55 0.01 . 1 . . . . . . . . 5497 1 394 . 1 1 59 59 ALA C C 13 176.982 0.1 . 1 . . . . . . . . 5497 1 395 . 1 1 59 59 ALA CA C 13 50.29 0.1 . 1 . . . . . . . . 5497 1 396 . 1 1 59 59 ALA CB C 13 20.79 0.1 . 1 . . . . . . . . 5497 1 397 . 1 1 59 59 ALA N N 15 121.142 0.1 . 1 . . . . . . . . 5497 1 398 . 1 1 60 60 ASP H H 1 8.431 0.01 . 1 . . . . . . . . 5497 1 399 . 1 1 60 60 ASP HA H 1 4.16 0.01 . 1 . . . . . . . . 5497 1 400 . 1 1 60 60 ASP HB2 H 1 2.70 0.01 . 2 . . . . . . . . 5497 1 401 . 1 1 60 60 ASP HB3 H 1 2.52 0.01 . 2 . . . . . . . . 5497 1 402 . 1 1 60 60 ASP C C 13 174.852 0.1 . 1 . . . . . . . . 5497 1 403 . 1 1 60 60 ASP CA C 13 56.17 0.1 . 1 . . . . . . . . 5497 1 404 . 1 1 60 60 ASP CB C 13 40.58 0.1 . 1 . . . . . . . . 5497 1 405 . 1 1 60 60 ASP N N 15 120.183 0.1 . 1 . . . . . . . . 5497 1 406 . 1 1 61 61 TRP H H 1 5.957 0.01 . 1 . . . . . . . . 5497 1 407 . 1 1 61 61 TRP HA H 1 4.55 0.01 . 1 . . . . . . . . 5497 1 408 . 1 1 61 61 TRP HB2 H 1 3.68 0.01 . 2 . . . . . . . . 5497 1 409 . 1 1 61 61 TRP HB3 H 1 3.17 0.01 . 2 . . . . . . . . 5497 1 410 . 1 1 61 61 TRP HE1 H 1 10.754 0.01 . 1 . . . . . . . . 5497 1 411 . 1 1 61 61 TRP C C 13 174.878 0.1 . 1 . . . . . . . . 5497 1 412 . 1 1 61 61 TRP CA C 13 52.35 0.1 . 1 . . . . . . . . 5497 1 413 . 1 1 61 61 TRP CB C 13 27.91 0.1 . 1 . . . . . . . . 5497 1 414 . 1 1 61 61 TRP N N 15 109.621 0.1 . 1 . . . . . . . . 5497 1 415 . 1 1 61 61 TRP NE1 N 15 132.359 0.1 . 1 . . . . . . . . 5497 1 416 . 1 1 62 62 CYS H H 1 6.916 0.01 . 1 . . . . . . . . 5497 1 417 . 1 1 62 62 CYS HA H 1 4.78 0.01 . 1 . . . . . . . . 5497 1 418 . 1 1 62 62 CYS HB2 H 1 2.94 0.01 . 1 . . . . . . . . 5497 1 419 . 1 1 62 62 CYS HB3 H 1 2.94 0.01 . 1 . . . . . . . . 5497 1 420 . 1 1 62 62 CYS C C 13 172.694 0.1 . 1 . . . . . . . . 5497 1 421 . 1 1 62 62 CYS CA C 13 52.06 0.1 . 1 . . . . . . . . 5497 1 422 . 1 1 62 62 CYS CB C 13 42.32 0.1 . 1 . . . . . . . . 5497 1 423 . 1 1 62 62 CYS N N 15 121.691 0.1 . 1 . . . . . . . . 5497 1 424 . 1 1 63 63 VAL H H 1 8.675 0.01 . 1 . . . . . . . . 5497 1 425 . 1 1 63 63 VAL HA H 1 3.60 0.01 . 1 . . . . . . . . 5497 1 426 . 1 1 63 63 VAL HB H 1 2.06 0.01 . 1 . . . . . . . . 5497 1 427 . 1 1 63 63 VAL HG11 H 1 0.91 0.01 . 2 . . . . . . . . 5497 1 428 . 1 1 63 63 VAL HG12 H 1 0.91 0.01 . 2 . . . . . . . . 5497 1 429 . 1 1 63 63 VAL HG13 H 1 0.91 0.01 . 2 . . . . . . . . 5497 1 430 . 1 1 63 63 VAL HG21 H 1 1.09 0.01 . 2 . . . . . . . . 5497 1 431 . 1 1 63 63 VAL HG22 H 1 1.09 0.01 . 2 . . . . . . . . 5497 1 432 . 1 1 63 63 VAL HG23 H 1 1.09 0.01 . 2 . . . . . . . . 5497 1 433 . 1 1 63 63 VAL C C 13 178.750 0.1 . 1 . . . . . . . . 5497 1 434 . 1 1 63 63 VAL CA C 13 66.74 0.1 . 1 . . . . . . . . 5497 1 435 . 1 1 63 63 VAL CB C 13 30.93 0.1 . 1 . . . . . . . . 5497 1 436 . 1 1 63 63 VAL CG1 C 13 20.20 0.1 . 2 . . . . . . . . 5497 1 437 . 1 1 63 63 VAL CG2 C 13 21.87 0.1 . 2 . . . . . . . . 5497 1 438 . 1 1 63 63 VAL N N 15 133.583 0.1 . 1 . . . . . . . . 5497 1 439 . 1 1 64 64 ALA H H 1 9.316 0.01 . 1 . . . . . . . . 5497 1 440 . 1 1 64 64 ALA HA H 1 4.29 0.01 . 1 . . . . . . . . 5497 1 441 . 1 1 64 64 ALA HB1 H 1 1.50 0.01 . 1 . . . . . . . . 5497 1 442 . 1 1 64 64 ALA HB2 H 1 1.50 0.01 . 1 . . . . . . . . 5497 1 443 . 1 1 64 64 ALA HB3 H 1 1.50 0.01 . 1 . . . . . . . . 5497 1 444 . 1 1 64 64 ALA C C 13 178.750 0.1 . 1 . . . . . . . . 5497 1 445 . 1 1 64 64 ALA CA C 13 53.87 0.1 . 1 . . . . . . . . 5497 1 446 . 1 1 64 64 ALA CB C 13 18.50 0.1 . 1 . . . . . . . . 5497 1 447 . 1 1 64 64 ALA N N 15 121.680 0.1 . 1 . . . . . . . . 5497 1 448 . 1 1 65 65 CYS H H 1 8.516 0.01 . 1 . . . . . . . . 5497 1 449 . 1 1 65 65 CYS HA H 1 4.93 0.01 . 1 . . . . . . . . 5497 1 450 . 1 1 65 65 CYS HB2 H 1 3.81 0.01 . 2 . . . . . . . . 5497 1 451 . 1 1 65 65 CYS HB3 H 1 3.30 0.01 . 2 . . . . . . . . 5497 1 452 . 1 1 65 65 CYS C C 13 176.399 0.1 . 1 . . . . . . . . 5497 1 453 . 1 1 65 65 CYS CA C 13 63.06 0.1 . 1 . . . . . . . . 5497 1 454 . 1 1 65 65 CYS CB C 13 32.27 0.1 . 1 . . . . . . . . 5497 1 455 . 1 1 65 65 CYS N N 15 113.974 0.1 . 1 . . . . . . . . 5497 1 456 . 1 1 66 66 LYS H H 1 7.617 0.01 . 1 . . . . . . . . 5497 1 457 . 1 1 66 66 LYS HA H 1 4.20 0.01 . 1 . . . . . . . . 5497 1 458 . 1 1 66 66 LYS C C 13 178.787 0.1 . 1 . . . . . . . . 5497 1 459 . 1 1 66 66 LYS CA C 13 58.74 0.1 . 1 . . . . . . . . 5497 1 460 . 1 1 66 66 LYS CB C 13 30.90 0.1 . 1 . . . . . . . . 5497 1 461 . 1 1 66 66 LYS N N 15 121.395 0.1 . 1 . . . . . . . . 5497 1 462 . 1 1 67 67 GLU H H 1 8.024 0.01 . 1 . . . . . . . . 5497 1 463 . 1 1 67 67 GLU HA H 1 3.93 0.01 . 1 . . . . . . . . 5497 1 464 . 1 1 67 67 GLU HB2 H 1 1.43 0.01 . 2 . . . . . . . . 5497 1 465 . 1 1 67 67 GLU HB3 H 1 1.89 0.01 . 2 . . . . . . . . 5497 1 466 . 1 1 67 67 GLU HG2 H 1 2.23 0.01 . 2 . . . . . . . . 5497 1 467 . 1 1 67 67 GLU C C 13 178.583 0.1 . 1 . . . . . . . . 5497 1 468 . 1 1 67 67 GLU CA C 13 59.08 0.1 . 1 . . . . . . . . 5497 1 469 . 1 1 67 67 GLU CB C 13 28.43 0.1 . 1 . . . . . . . . 5497 1 470 . 1 1 67 67 GLU CG C 13 36.06 0.1 . 1 . . . . . . . . 5497 1 471 . 1 1 67 67 GLU N N 15 121.592 0.1 . 1 . . . . . . . . 5497 1 472 . 1 1 68 68 PHE H H 1 8.545 0.01 . 1 . . . . . . . . 5497 1 473 . 1 1 68 68 PHE HA H 1 4.06 0.01 . 1 . . . . . . . . 5497 1 474 . 1 1 68 68 PHE HB2 H 1 3.13 0.01 . 2 . . . . . . . . 5497 1 475 . 1 1 68 68 PHE HB3 H 1 1.90 0.01 . 2 . . . . . . . . 5497 1 476 . 1 1 68 68 PHE C C 13 178.624 0.1 . 1 . . . . . . . . 5497 1 477 . 1 1 68 68 PHE CA C 13 62.27 0.1 . 1 . . . . . . . . 5497 1 478 . 1 1 68 68 PHE CB C 13 38.37 0.1 . 1 . . . . . . . . 5497 1 479 . 1 1 68 68 PHE N N 15 121.006 0.1 . 1 . . . . . . . . 5497 1 480 . 1 1 69 69 GLU H H 1 7.368 0.01 . 1 . . . . . . . . 5497 1 481 . 1 1 69 69 GLU HA H 1 4.03 0.01 . 1 . . . . . . . . 5497 1 482 . 1 1 69 69 GLU HB2 H 1 2.26 0.01 . 2 . . . . . . . . 5497 1 483 . 1 1 69 69 GLU HG2 H 1 2.40 0.01 . 2 . . . . . . . . 5497 1 484 . 1 1 69 69 GLU C C 13 176.403 0.1 . 1 . . . . . . . . 5497 1 485 . 1 1 69 69 GLU CA C 13 58.99 0.1 . 1 . . . . . . . . 5497 1 486 . 1 1 69 69 GLU CB C 13 28.76 0.1 . 1 . . . . . . . . 5497 1 487 . 1 1 69 69 GLU CG C 13 34.70 0.1 . 1 . . . . . . . . 5497 1 488 . 1 1 69 69 GLU N N 15 118.228 0.1 . 1 . . . . . . . . 5497 1 489 . 1 1 70 70 LYS H H 1 7.742 0.01 . 1 . . . . . . . . 5497 1 490 . 1 1 70 70 LYS HA H 1 3.95 0.01 . 1 . . . . . . . . 5497 1 491 . 1 1 70 70 LYS HB2 H 1 1.39 0.01 . 2 . . . . . . . . 5497 1 492 . 1 1 70 70 LYS HB3 H 1 1.07 0.01 . 2 . . . . . . . . 5497 1 493 . 1 1 70 70 LYS HG2 H 1 1.08 0.01 . 2 . . . . . . . . 5497 1 494 . 1 1 70 70 LYS HG3 H 1 0.64 0.01 . 2 . . . . . . . . 5497 1 495 . 1 1 70 70 LYS HD2 H 1 1.39 0.01 . 2 . . . . . . . . 5497 1 496 . 1 1 70 70 LYS HD3 H 1 1.48 0.01 . 2 . . . . . . . . 5497 1 497 . 1 1 70 70 LYS HE2 H 1 2.77 0.01 . 1 . . . . . . . . 5497 1 498 . 1 1 70 70 LYS HE3 H 1 2.77 0.01 . 1 . . . . . . . . 5497 1 499 . 1 1 70 70 LYS C C 13 178.782 0.1 . 1 . . . . . . . . 5497 1 500 . 1 1 70 70 LYS CA C 13 58.29 0.1 . 1 . . . . . . . . 5497 1 501 . 1 1 70 70 LYS CB C 13 32.97 0.1 . 1 . . . . . . . . 5497 1 502 . 1 1 70 70 LYS CG C 13 24.10 0.1 . 1 . . . . . . . . 5497 1 503 . 1 1 70 70 LYS CD C 13 28.86 0.1 . 1 . . . . . . . . 5497 1 504 . 1 1 70 70 LYS CE C 13 41.35 0.1 . 1 . . . . . . . . 5497 1 505 . 1 1 70 70 LYS N N 15 116.394 0.1 . 1 . . . . . . . . 5497 1 506 . 1 1 71 71 TYR H H 1 8.485 0.01 . 1 . . . . . . . . 5497 1 507 . 1 1 71 71 TYR HA H 1 4.94 0.01 . 1 . . . . . . . . 5497 1 508 . 1 1 71 71 TYR HB2 H 1 3.43 0.01 . 2 . . . . . . . . 5497 1 509 . 1 1 71 71 TYR HB3 H 1 2.95 0.01 . 2 . . . . . . . . 5497 1 510 . 1 1 71 71 TYR C C 13 175.973 0.1 . 1 . . . . . . . . 5497 1 511 . 1 1 71 71 TYR CA C 13 58.14 0.1 . 1 . . . . . . . . 5497 1 512 . 1 1 71 71 TYR CB C 13 39.34 0.1 . 1 . . . . . . . . 5497 1 513 . 1 1 71 71 TYR N N 15 115.584 0.1 . 1 . . . . . . . . 5497 1 514 . 1 1 72 72 THR H H 1 7.719 0.01 . 1 . . . . . . . . 5497 1 515 . 1 1 72 72 THR HA H 1 4.38 0.01 . 1 . . . . . . . . 5497 1 516 . 1 1 72 72 THR HB H 1 4.12 0.01 . 1 . . . . . . . . 5497 1 517 . 1 1 72 72 THR C C 13 174.551 0.1 . 1 . . . . . . . . 5497 1 518 . 1 1 72 72 THR CA C 13 66.24 0.1 . 1 . . . . . . . . 5497 1 519 . 1 1 72 72 THR CB C 13 67.82 0.1 . 1 . . . . . . . . 5497 1 520 . 1 1 72 72 THR N N 15 117.821 0.1 . 1 . . . . . . . . 5497 1 521 . 1 1 73 73 PHE H H 1 8.931 0.01 . 1 . . . . . . . . 5497 1 522 . 1 1 73 73 PHE HA H 1 4.64 0.01 . 1 . . . . . . . . 5497 1 523 . 1 1 73 73 PHE HB2 H 1 3.56 0.01 . 2 . . . . . . . . 5497 1 524 . 1 1 73 73 PHE HB3 H 1 3.31 0.01 . 2 . . . . . . . . 5497 1 525 . 1 1 73 73 PHE C C 13 174.370 0.1 . 1 . . . . . . . . 5497 1 526 . 1 1 73 73 PHE CA C 13 55.30 0.1 . 1 . . . . . . . . 5497 1 527 . 1 1 73 73 PHE CB C 13 36.67 0.1 . 1 . . . . . . . . 5497 1 528 . 1 1 73 73 PHE N N 15 119.117 0.1 . 1 . . . . . . . . 5497 1 529 . 1 1 74 74 SER H H 1 7.071 0.01 . 1 . . . . . . . . 5497 1 530 . 1 1 74 74 SER HA H 1 4.26 0.01 . 1 . . . . . . . . 5497 1 531 . 1 1 74 74 SER HB2 H 1 4.02 0.01 . 2 . . . . . . . . 5497 1 532 . 1 1 74 74 SER HB3 H 1 3.80 0.01 . 2 . . . . . . . . 5497 1 533 . 1 1 74 74 SER C C 13 172.986 0.1 . 1 . . . . . . . . 5497 1 534 . 1 1 74 74 SER CA C 13 56.71 0.1 . 1 . . . . . . . . 5497 1 535 . 1 1 74 74 SER CB C 13 63.69 0.1 . 1 . . . . . . . . 5497 1 536 . 1 1 74 74 SER N N 15 107.859 0.1 . 1 . . . . . . . . 5497 1 537 . 1 1 75 75 ASP H H 1 7.392 0.01 . 1 . . . . . . . . 5497 1 538 . 1 1 75 75 ASP HA H 1 4.98 0.01 . 1 . . . . . . . . 5497 1 539 . 1 1 75 75 ASP HB2 H 1 3.06 0.01 . 2 . . . . . . . . 5497 1 540 . 1 1 75 75 ASP HB3 H 1 2.69 0.01 . 2 . . . . . . . . 5497 1 541 . 1 1 75 75 ASP CA C 13 51.61 0.1 . 1 . . . . . . . . 5497 1 542 . 1 1 75 75 ASP CB C 13 44.41 0.1 . 1 . . . . . . . . 5497 1 543 . 1 1 75 75 ASP N N 15 125.886 0.1 . 1 . . . . . . . . 5497 1 544 . 1 1 76 76 PRO HA H 1 4.25 0.01 . 1 . . . . . . . . 5497 1 545 . 1 1 76 76 PRO HB2 H 1 2.00 0.01 . 2 . . . . . . . . 5497 1 546 . 1 1 76 76 PRO HB3 H 1 2.41 0.01 . 2 . . . . . . . . 5497 1 547 . 1 1 76 76 PRO HG2 H 1 2.11 0.01 . 2 . . . . . . . . 5497 1 548 . 1 1 76 76 PRO HG3 H 1 2.15 0.01 . 2 . . . . . . . . 5497 1 549 . 1 1 76 76 PRO HD2 H 1 4.10 0.01 . 2 . . . . . . . . 5497 1 550 . 1 1 76 76 PRO HD3 H 1 3.89 0.01 . 2 . . . . . . . . 5497 1 551 . 1 1 76 76 PRO C C 13 178.559 0.1 . 1 . . . . . . . . 5497 1 552 . 1 1 76 76 PRO CA C 13 64.62 0.1 . 1 . . . . . . . . 5497 1 553 . 1 1 76 76 PRO CB C 13 31.72 0.1 . 1 . . . . . . . . 5497 1 554 . 1 1 76 76 PRO CG C 13 27.02 0.1 . 1 . . . . . . . . 5497 1 555 . 1 1 76 76 PRO CD C 13 50.70 0.1 . 1 . . . . . . . . 5497 1 556 . 1 1 77 77 GLN H H 1 8.642 0.01 . 1 . . . . . . . . 5497 1 557 . 1 1 77 77 GLN HA H 1 4.20 0.01 . 1 . . . . . . . . 5497 1 558 . 1 1 77 77 GLN HB2 H 1 2.29 0.01 . 2 . . . . . . . . 5497 1 559 . 1 1 77 77 GLN HB3 H 1 2.17 0.01 . 2 . . . . . . . . 5497 1 560 . 1 1 77 77 GLN HG2 H 1 2.47 0.01 . 2 . . . . . . . . 5497 1 561 . 1 1 77 77 GLN C C 13 179.135 0.1 . 1 . . . . . . . . 5497 1 562 . 1 1 77 77 GLN CA C 13 58.27 0.1 . 1 . . . . . . . . 5497 1 563 . 1 1 77 77 GLN CB C 13 27.37 0.1 . 1 . . . . . . . . 5497 1 564 . 1 1 77 77 GLN CG C 13 33.76 0.1 . 1 . . . . . . . . 5497 1 565 . 1 1 77 77 GLN N N 15 119.082 0.1 . 1 . . . . . . . . 5497 1 566 . 1 1 78 78 VAL H H 1 8.011 0.01 . 1 . . . . . . . . 5497 1 567 . 1 1 78 78 VAL HA H 1 3.59 0.01 . 1 . . . . . . . . 5497 1 568 . 1 1 78 78 VAL HB H 1 2.75 0.01 . 1 . . . . . . . . 5497 1 569 . 1 1 78 78 VAL HG11 H 1 1.22 0.01 . 2 . . . . . . . . 5497 1 570 . 1 1 78 78 VAL HG12 H 1 1.22 0.01 . 2 . . . . . . . . 5497 1 571 . 1 1 78 78 VAL HG13 H 1 1.22 0.01 . 2 . . . . . . . . 5497 1 572 . 1 1 78 78 VAL HG21 H 1 1.44 0.01 . 2 . . . . . . . . 5497 1 573 . 1 1 78 78 VAL HG22 H 1 1.44 0.01 . 2 . . . . . . . . 5497 1 574 . 1 1 78 78 VAL HG23 H 1 1.44 0.01 . 2 . . . . . . . . 5497 1 575 . 1 1 78 78 VAL C C 13 176.551 0.1 . 1 . . . . . . . . 5497 1 576 . 1 1 78 78 VAL CA C 13 65.78 0.1 . 1 . . . . . . . . 5497 1 577 . 1 1 78 78 VAL CB C 13 31.48 0.1 . 1 . . . . . . . . 5497 1 578 . 1 1 78 78 VAL CG1 C 13 21.95 0.1 . 2 . . . . . . . . 5497 1 579 . 1 1 78 78 VAL CG2 C 13 24.10 0.1 . 2 . . . . . . . . 5497 1 580 . 1 1 78 78 VAL N N 15 124.556 0.1 . 1 . . . . . . . . 5497 1 581 . 1 1 79 79 GLN H H 1 7.938 0.01 . 1 . . . . . . . . 5497 1 582 . 1 1 79 79 GLN HA H 1 3.74 0.01 . 1 . . . . . . . . 5497 1 583 . 1 1 79 79 GLN HB2 H 1 1.99 0.01 . 2 . . . . . . . . 5497 1 584 . 1 1 79 79 GLN HG2 H 1 2.20 0.01 . 2 . . . . . . . . 5497 1 585 . 1 1 79 79 GLN HG3 H 1 2.58 0.01 . 2 . . . . . . . . 5497 1 586 . 1 1 79 79 GLN C C 13 178.824 0.1 . 1 . . . . . . . . 5497 1 587 . 1 1 79 79 GLN CA C 13 59.12 0.1 . 1 . . . . . . . . 5497 1 588 . 1 1 79 79 GLN CB C 13 26.78 0.1 . 1 . . . . . . . . 5497 1 589 . 1 1 79 79 GLN CG C 13 33.11 0.1 . 1 . . . . . . . . 5497 1 590 . 1 1 79 79 GLN N N 15 116.622 0.1 . 1 . . . . . . . . 5497 1 591 . 1 1 80 80 LYS H H 1 7.898 0.01 . 1 . . . . . . . . 5497 1 592 . 1 1 80 80 LYS HA H 1 4.06 0.01 . 1 . . . . . . . . 5497 1 593 . 1 1 80 80 LYS HB2 H 1 1.90 0.01 . 2 . . . . . . . . 5497 1 594 . 1 1 80 80 LYS HG2 H 1 1.55 0.01 . 2 . . . . . . . . 5497 1 595 . 1 1 80 80 LYS HG3 H 1 1.45 0.01 . 2 . . . . . . . . 5497 1 596 . 1 1 80 80 LYS HD2 H 1 1.68 0.01 . 2 . . . . . . . . 5497 1 597 . 1 1 80 80 LYS HE2 H 1 2.97 0.01 . 2 . . . . . . . . 5497 1 598 . 1 1 80 80 LYS C C 13 178.780 0.1 . 1 . . . . . . . . 5497 1 599 . 1 1 80 80 LYS CA C 13 58.55 0.1 . 1 . . . . . . . . 5497 1 600 . 1 1 80 80 LYS CB C 13 31.67 0.1 . 1 . . . . . . . . 5497 1 601 . 1 1 80 80 LYS CG C 13 24.45 0.1 . 1 . . . . . . . . 5497 1 602 . 1 1 80 80 LYS CD C 13 28.62 0.1 . 1 . . . . . . . . 5497 1 603 . 1 1 80 80 LYS N N 15 119.273 0.1 . 1 . . . . . . . . 5497 1 604 . 1 1 81 81 ALA H H 1 7.827 0.01 . 1 . . . . . . . . 5497 1 605 . 1 1 81 81 ALA HA H 1 4.17 0.01 . 1 . . . . . . . . 5497 1 606 . 1 1 81 81 ALA HB1 H 1 1.55 0.01 . 1 . . . . . . . . 5497 1 607 . 1 1 81 81 ALA HB2 H 1 1.55 0.01 . 1 . . . . . . . . 5497 1 608 . 1 1 81 81 ALA HB3 H 1 1.55 0.01 . 1 . . . . . . . . 5497 1 609 . 1 1 81 81 ALA C C 13 178.873 0.1 . 1 . . . . . . . . 5497 1 610 . 1 1 81 81 ALA CA C 13 53.87 0.1 . 1 . . . . . . . . 5497 1 611 . 1 1 81 81 ALA CB C 13 18.23 0.1 . 1 . . . . . . . . 5497 1 612 . 1 1 81 81 ALA N N 15 122.586 0.1 . 1 . . . . . . . . 5497 1 613 . 1 1 82 82 LEU H H 1 7.493 0.01 . 1 . . . . . . . . 5497 1 614 . 1 1 82 82 LEU HA H 1 4.40 0.01 . 1 . . . . . . . . 5497 1 615 . 1 1 82 82 LEU HB2 H 1 1.68 0.01 . 2 . . . . . . . . 5497 1 616 . 1 1 82 82 LEU HB3 H 1 1.85 0.01 . 2 . . . . . . . . 5497 1 617 . 1 1 82 82 LEU HG H 1 1.78 0.01 . 1 . . . . . . . . 5497 1 618 . 1 1 82 82 LEU HD11 H 1 0.87 0.01 . 2 . . . . . . . . 5497 1 619 . 1 1 82 82 LEU HD12 H 1 0.87 0.01 . 2 . . . . . . . . 5497 1 620 . 1 1 82 82 LEU HD13 H 1 0.87 0.01 . 2 . . . . . . . . 5497 1 621 . 1 1 82 82 LEU HD21 H 1 1.03 0.01 . 2 . . . . . . . . 5497 1 622 . 1 1 82 82 LEU HD22 H 1 1.03 0.01 . 2 . . . . . . . . 5497 1 623 . 1 1 82 82 LEU HD23 H 1 1.03 0.01 . 2 . . . . . . . . 5497 1 624 . 1 1 82 82 LEU C C 13 176.659 0.1 . 1 . . . . . . . . 5497 1 625 . 1 1 82 82 LEU CA C 13 53.96 0.1 . 1 . . . . . . . . 5497 1 626 . 1 1 82 82 LEU CB C 13 41.83 0.1 . 1 . . . . . . . . 5497 1 627 . 1 1 82 82 LEU CG C 13 26.10 0.1 . 1 . . . . . . . . 5497 1 628 . 1 1 82 82 LEU CD1 C 13 26.38 0.1 . 2 . . . . . . . . 5497 1 629 . 1 1 82 82 LEU CD2 C 13 22.63 0.1 . 2 . . . . . . . . 5497 1 630 . 1 1 82 82 LEU N N 15 117.612 0.1 . 1 . . . . . . . . 5497 1 631 . 1 1 83 83 ALA H H 1 7.333 0.01 . 1 . . . . . . . . 5497 1 632 . 1 1 83 83 ALA HA H 1 4.07 0.01 . 1 . . . . . . . . 5497 1 633 . 1 1 83 83 ALA HB1 H 1 1.50 0.01 . 1 . . . . . . . . 5497 1 634 . 1 1 83 83 ALA HB2 H 1 1.50 0.01 . 1 . . . . . . . . 5497 1 635 . 1 1 83 83 ALA HB3 H 1 1.50 0.01 . 1 . . . . . . . . 5497 1 636 . 1 1 83 83 ALA C C 13 177.090 0.1 . 1 . . . . . . . . 5497 1 637 . 1 1 83 83 ALA CA C 13 54.84 0.1 . 1 . . . . . . . . 5497 1 638 . 1 1 83 83 ALA CB C 13 18.47 0.1 . 1 . . . . . . . . 5497 1 639 . 1 1 83 83 ALA N N 15 122.679 0.1 . 1 . . . . . . . . 5497 1 640 . 1 1 84 84 ASP H H 1 8.158 0.01 . 1 . . . . . . . . 5497 1 641 . 1 1 84 84 ASP HA H 1 4.81 0.01 . 1 . . . . . . . . 5497 1 642 . 1 1 84 84 ASP HB2 H 1 2.84 0.01 . 2 . . . . . . . . 5497 1 643 . 1 1 84 84 ASP HB3 H 1 2.61 0.01 . 2 . . . . . . . . 5497 1 644 . 1 1 84 84 ASP C C 13 174.182 0.1 . 1 . . . . . . . . 5497 1 645 . 1 1 84 84 ASP CA C 13 53.07 0.1 . 1 . . . . . . . . 5497 1 646 . 1 1 84 84 ASP CB C 13 40.56 0.1 . 1 . . . . . . . . 5497 1 647 . 1 1 84 84 ASP N N 15 116.498 0.1 . 1 . . . . . . . . 5497 1 648 . 1 1 85 85 THR H H 1 7.638 0.01 . 1 . . . . . . . . 5497 1 649 . 1 1 85 85 THR HA H 1 4.32 0.01 . 1 . . . . . . . . 5497 1 650 . 1 1 85 85 THR HB H 1 3.99 0.01 . 1 . . . . . . . . 5497 1 651 . 1 1 85 85 THR C C 13 172.674 0.1 . 1 . . . . . . . . 5497 1 652 . 1 1 85 85 THR CA C 13 61.96 0.1 . 1 . . . . . . . . 5497 1 653 . 1 1 85 85 THR CB C 13 69.95 0.1 . 1 . . . . . . . . 5497 1 654 . 1 1 85 85 THR N N 15 117.595 0.1 . 1 . . . . . . . . 5497 1 655 . 1 1 86 86 VAL H H 1 9.049 0.01 . 1 . . . . . . . . 5497 1 656 . 1 1 86 86 VAL HA H 1 3.84 0.01 . 1 . . . . . . . . 5497 1 657 . 1 1 86 86 VAL HB H 1 2.10 0.01 . 1 . . . . . . . . 5497 1 658 . 1 1 86 86 VAL HG11 H 1 0.87 0.01 . 2 . . . . . . . . 5497 1 659 . 1 1 86 86 VAL HG12 H 1 0.87 0.01 . 2 . . . . . . . . 5497 1 660 . 1 1 86 86 VAL HG13 H 1 0.87 0.01 . 2 . . . . . . . . 5497 1 661 . 1 1 86 86 VAL HG21 H 1 1.00 0.01 . 2 . . . . . . . . 5497 1 662 . 1 1 86 86 VAL HG22 H 1 1.00 0.01 . 2 . . . . . . . . 5497 1 663 . 1 1 86 86 VAL HG23 H 1 1.00 0.01 . 2 . . . . . . . . 5497 1 664 . 1 1 86 86 VAL C C 13 173.746 0.1 . 1 . . . . . . . . 5497 1 665 . 1 1 86 86 VAL CA C 13 63.35 0.1 . 1 . . . . . . . . 5497 1 666 . 1 1 86 86 VAL CB C 13 31.04 0.1 . 1 . . . . . . . . 5497 1 667 . 1 1 86 86 VAL CG1 C 13 19.64 0.1 . 2 . . . . . . . . 5497 1 668 . 1 1 86 86 VAL CG2 C 13 21.46 0.1 . 2 . . . . . . . . 5497 1 669 . 1 1 86 86 VAL N N 15 129.198 0.1 . 1 . . . . . . . . 5497 1 670 . 1 1 87 87 LEU H H 1 8.312 0.01 . 1 . . . . . . . . 5497 1 671 . 1 1 87 87 LEU HA H 1 4.92 0.01 . 1 . . . . . . . . 5497 1 672 . 1 1 87 87 LEU HB2 H 1 1.74 0.01 . 2 . . . . . . . . 5497 1 673 . 1 1 87 87 LEU HB3 H 1 0.87 0.01 . 2 . . . . . . . . 5497 1 674 . 1 1 87 87 LEU HG H 1 1.73 0.01 . 1 . . . . . . . . 5497 1 675 . 1 1 87 87 LEU HD11 H 1 0.41 0.01 . 2 . . . . . . . . 5497 1 676 . 1 1 87 87 LEU HD12 H 1 0.41 0.01 . 2 . . . . . . . . 5497 1 677 . 1 1 87 87 LEU HD13 H 1 0.41 0.01 . 2 . . . . . . . . 5497 1 678 . 1 1 87 87 LEU HD21 H 1 0.65 0.01 . 2 . . . . . . . . 5497 1 679 . 1 1 87 87 LEU HD22 H 1 0.65 0.01 . 2 . . . . . . . . 5497 1 680 . 1 1 87 87 LEU HD23 H 1 0.65 0.01 . 2 . . . . . . . . 5497 1 681 . 1 1 87 87 LEU C C 13 174.777 0.1 . 1 . . . . . . . . 5497 1 682 . 1 1 87 87 LEU CA C 13 53.20 0.1 . 1 . . . . . . . . 5497 1 683 . 1 1 87 87 LEU CB C 13 41.16 0.1 . 1 . . . . . . . . 5497 1 684 . 1 1 87 87 LEU CG C 13 25.23 0.1 . 1 . . . . . . . . 5497 1 685 . 1 1 87 87 LEU CD1 C 13 26.72 0.1 . 2 . . . . . . . . 5497 1 686 . 1 1 87 87 LEU CD2 C 13 24.30 0.1 . 2 . . . . . . . . 5497 1 687 . 1 1 87 87 LEU N N 15 128.731 0.1 . 1 . . . . . . . . 5497 1 688 . 1 1 88 88 LEU H H 1 9.372 0.01 . 1 . . . . . . . . 5497 1 689 . 1 1 88 88 LEU HA H 1 5.62 0.01 . 1 . . . . . . . . 5497 1 690 . 1 1 88 88 LEU HB2 H 1 1.76 0.01 . 2 . . . . . . . . 5497 1 691 . 1 1 88 88 LEU HB3 H 1 1.15 0.01 . 2 . . . . . . . . 5497 1 692 . 1 1 88 88 LEU HG H 1 1.50 0.01 . 1 . . . . . . . . 5497 1 693 . 1 1 88 88 LEU HD11 H 1 0.51 0.01 . 2 . . . . . . . . 5497 1 694 . 1 1 88 88 LEU HD12 H 1 0.51 0.01 . 2 . . . . . . . . 5497 1 695 . 1 1 88 88 LEU HD13 H 1 0.51 0.01 . 2 . . . . . . . . 5497 1 696 . 1 1 88 88 LEU HD21 H 1 0.72 0.01 . 2 . . . . . . . . 5497 1 697 . 1 1 88 88 LEU HD22 H 1 0.72 0.01 . 2 . . . . . . . . 5497 1 698 . 1 1 88 88 LEU HD23 H 1 0.72 0.01 . 2 . . . . . . . . 5497 1 699 . 1 1 88 88 LEU C C 13 174.588 0.1 . 1 . . . . . . . . 5497 1 700 . 1 1 88 88 LEU CA C 13 51.76 0.1 . 1 . . . . . . . . 5497 1 701 . 1 1 88 88 LEU CB C 13 46.07 0.1 . 1 . . . . . . . . 5497 1 702 . 1 1 88 88 LEU CG C 13 26.33 0.1 . 1 . . . . . . . . 5497 1 703 . 1 1 88 88 LEU CD1 C 13 21.73 0.1 . 2 . . . . . . . . 5497 1 704 . 1 1 88 88 LEU CD2 C 13 26.51 0.1 . 2 . . . . . . . . 5497 1 705 . 1 1 88 88 LEU N N 15 125.347 0.1 . 1 . . . . . . . . 5497 1 706 . 1 1 89 89 GLN H H 1 8.645 0.01 . 1 . . . . . . . . 5497 1 707 . 1 1 89 89 GLN HA H 1 5.36 0.01 . 1 . . . . . . . . 5497 1 708 . 1 1 89 89 GLN HB2 H 1 1.57 0.01 . 2 . . . . . . . . 5497 1 709 . 1 1 89 89 GLN HB3 H 1 1.01 0.01 . 2 . . . . . . . . 5497 1 710 . 1 1 89 89 GLN HG2 H 1 1.93 0.01 . 2 . . . . . . . . 5497 1 711 . 1 1 89 89 GLN HG3 H 1 1.57 0.01 . 2 . . . . . . . . 5497 1 712 . 1 1 89 89 GLN C C 13 171.873 0.1 . 1 . . . . . . . . 5497 1 713 . 1 1 89 89 GLN CA C 13 53.38 0.1 . 1 . . . . . . . . 5497 1 714 . 1 1 89 89 GLN CB C 13 33.76 0.1 . 1 . . . . . . . . 5497 1 715 . 1 1 89 89 GLN CG C 13 34.34 0.1 . 1 . . . . . . . . 5497 1 716 . 1 1 89 89 GLN N N 15 122.462 0.1 . 1 . . . . . . . . 5497 1 717 . 1 1 90 90 ALA H H 1 8.102 0.01 . 1 . . . . . . . . 5497 1 718 . 1 1 90 90 ALA HA H 1 5.17 0.01 . 1 . . . . . . . . 5497 1 719 . 1 1 90 90 ALA HB1 H 1 1.19 0.01 . 1 . . . . . . . . 5497 1 720 . 1 1 90 90 ALA HB2 H 1 1.19 0.01 . 1 . . . . . . . . 5497 1 721 . 1 1 90 90 ALA HB3 H 1 1.19 0.01 . 1 . . . . . . . . 5497 1 722 . 1 1 90 90 ALA C C 13 174.215 0.1 . 1 . . . . . . . . 5497 1 723 . 1 1 90 90 ALA CA C 13 49.78 0.1 . 1 . . . . . . . . 5497 1 724 . 1 1 90 90 ALA CB C 13 21.41 0.1 . 1 . . . . . . . . 5497 1 725 . 1 1 90 90 ALA N N 15 127.594 0.1 . 1 . . . . . . . . 5497 1 726 . 1 1 91 91 ASN H H 1 9.502 0.01 . 1 . . . . . . . . 5497 1 727 . 1 1 91 91 ASN HA H 1 5.23 0.01 . 1 . . . . . . . . 5497 1 728 . 1 1 91 91 ASN HB2 H 1 3.20 0.01 . 2 . . . . . . . . 5497 1 729 . 1 1 91 91 ASN HB3 H 1 2.73 0.01 . 2 . . . . . . . . 5497 1 730 . 1 1 91 91 ASN C C 13 175.783 0.1 . 1 . . . . . . . . 5497 1 731 . 1 1 91 91 ASN CA C 13 50.41 0.1 . 1 . . . . . . . . 5497 1 732 . 1 1 91 91 ASN CB C 13 37.27 0.1 . 1 . . . . . . . . 5497 1 733 . 1 1 91 91 ASN N N 15 122.139 0.1 . 1 . . . . . . . . 5497 1 734 . 1 1 92 92 VAL H H 1 8.669 0.01 . 1 . . . . . . . . 5497 1 735 . 1 1 92 92 VAL HA H 1 4.63 0.01 . 1 . . . . . . . . 5497 1 736 . 1 1 92 92 VAL HB H 1 2.64 0.01 . 1 . . . . . . . . 5497 1 737 . 1 1 92 92 VAL HG11 H 1 0.76 0.01 . 2 . . . . . . . . 5497 1 738 . 1 1 92 92 VAL HG12 H 1 0.76 0.01 . 2 . . . . . . . . 5497 1 739 . 1 1 92 92 VAL HG13 H 1 0.76 0.01 . 2 . . . . . . . . 5497 1 740 . 1 1 92 92 VAL HG21 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 741 . 1 1 92 92 VAL HG22 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 742 . 1 1 92 92 VAL HG23 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 743 . 1 1 92 92 VAL C C 13 175.967 0.1 . 1 . . . . . . . . 5497 1 744 . 1 1 92 92 VAL CA C 13 59.80 0.1 . 1 . . . . . . . . 5497 1 745 . 1 1 92 92 VAL CB C 13 29.68 0.1 . 1 . . . . . . . . 5497 1 746 . 1 1 92 92 VAL CG1 C 13 19.30 0.1 . 2 . . . . . . . . 5497 1 747 . 1 1 92 92 VAL CG2 C 13 20.01 0.1 . 2 . . . . . . . . 5497 1 748 . 1 1 92 92 VAL N N 15 115.721 0.1 . 1 . . . . . . . . 5497 1 749 . 1 1 93 93 THR H H 1 7.891 0.01 . 1 . . . . . . . . 5497 1 750 . 1 1 93 93 THR HA H 1 3.64 0.01 . 1 . . . . . . . . 5497 1 751 . 1 1 93 93 THR HB H 1 4.00 0.01 . 1 . . . . . . . . 5497 1 752 . 1 1 93 93 THR C C 13 174.674 0.1 . 1 . . . . . . . . 5497 1 753 . 1 1 93 93 THR CA C 13 67.11 0.1 . 1 . . . . . . . . 5497 1 754 . 1 1 93 93 THR CB C 13 69.50 0.1 . 1 . . . . . . . . 5497 1 755 . 1 1 93 93 THR N N 15 117.723 0.1 . 1 . . . . . . . . 5497 1 756 . 1 1 94 94 ALA H H 1 8.982 0.01 . 1 . . . . . . . . 5497 1 757 . 1 1 94 94 ALA HA H 1 4.15 0.01 . 1 . . . . . . . . 5497 1 758 . 1 1 94 94 ALA HB1 H 1 1.46 0.01 . 1 . . . . . . . . 5497 1 759 . 1 1 94 94 ALA HB2 H 1 1.46 0.01 . 1 . . . . . . . . 5497 1 760 . 1 1 94 94 ALA HB3 H 1 1.46 0.01 . 1 . . . . . . . . 5497 1 761 . 1 1 94 94 ALA C C 13 176.566 0.1 . 1 . . . . . . . . 5497 1 762 . 1 1 94 94 ALA CA C 13 53.37 0.1 . 1 . . . . . . . . 5497 1 763 . 1 1 94 94 ALA CB C 13 18.06 0.1 . 1 . . . . . . . . 5497 1 764 . 1 1 94 94 ALA N N 15 120.821 0.1 . 1 . . . . . . . . 5497 1 765 . 1 1 95 95 ASN H H 1 8.259 0.01 . 1 . . . . . . . . 5497 1 766 . 1 1 95 95 ASN HA H 1 4.32 0.01 . 1 . . . . . . . . 5497 1 767 . 1 1 95 95 ASN HB2 H 1 3.26 0.01 . 2 . . . . . . . . 5497 1 768 . 1 1 95 95 ASN HB3 H 1 2.53 0.01 . 2 . . . . . . . . 5497 1 769 . 1 1 95 95 ASN HD21 H 1 7.377 0.01 . 2 . . . . . . . . 5497 1 770 . 1 1 95 95 ASN HD22 H 1 6.227 0.01 . 2 . . . . . . . . 5497 1 771 . 1 1 95 95 ASN C C 13 173.985 0.1 . 1 . . . . . . . . 5497 1 772 . 1 1 95 95 ASN CA C 13 53.84 0.1 . 1 . . . . . . . . 5497 1 773 . 1 1 95 95 ASN CB C 13 38.02 0.1 . 1 . . . . . . . . 5497 1 774 . 1 1 95 95 ASN CG C 13 177.132 0.1 . 1 . . . . . . . . 5497 1 775 . 1 1 95 95 ASN N N 15 119.406 0.1 . 1 . . . . . . . . 5497 1 776 . 1 1 95 95 ASN ND2 N 15 110.875 0.1 . 1 . . . . . . . . 5497 1 777 . 1 1 96 96 ASP H H 1 8.993 0.01 . 1 . . . . . . . . 5497 1 778 . 1 1 96 96 ASP HA H 1 4.56 0.01 . 1 . . . . . . . . 5497 1 779 . 1 1 96 96 ASP HB2 H 1 3.25 0.01 . 2 . . . . . . . . 5497 1 780 . 1 1 96 96 ASP HB3 H 1 2.51 0.01 . 2 . . . . . . . . 5497 1 781 . 1 1 96 96 ASP C C 13 174.828 0.1 . 1 . . . . . . . . 5497 1 782 . 1 1 96 96 ASP CA C 13 52.59 0.1 . 1 . . . . . . . . 5497 1 783 . 1 1 96 96 ASP CB C 13 40.64 0.1 . 1 . . . . . . . . 5497 1 784 . 1 1 96 96 ASP N N 15 118.455 0.1 . 1 . . . . . . . . 5497 1 785 . 1 1 97 97 ALA H H 1 8.339 0.01 . 1 . . . . . . . . 5497 1 786 . 1 1 97 97 ALA HA H 1 4.02 0.01 . 1 . . . . . . . . 5497 1 787 . 1 1 97 97 ALA HB1 H 1 1.44 0.01 . 1 . . . . . . . . 5497 1 788 . 1 1 97 97 ALA HB2 H 1 1.44 0.01 . 1 . . . . . . . . 5497 1 789 . 1 1 97 97 ALA HB3 H 1 1.44 0.01 . 1 . . . . . . . . 5497 1 790 . 1 1 97 97 ALA C C 13 181.155 0.1 . 1 . . . . . . . . 5497 1 791 . 1 1 97 97 ALA CA C 13 55.12 0.1 . 1 . . . . . . . . 5497 1 792 . 1 1 97 97 ALA CB C 13 17.93 0.1 . 1 . . . . . . . . 5497 1 793 . 1 1 97 97 ALA N N 15 117.505 0.1 . 1 . . . . . . . . 5497 1 794 . 1 1 98 98 GLN H H 1 8.000 0.01 . 1 . . . . . . . . 5497 1 795 . 1 1 98 98 GLN HA H 1 4.20 0.01 . 1 . . . . . . . . 5497 1 796 . 1 1 98 98 GLN C C 13 177.562 0.1 . 1 . . . . . . . . 5497 1 797 . 1 1 98 98 GLN CA C 13 58.41 0.1 . 1 . . . . . . . . 5497 1 798 . 1 1 98 98 GLN CB C 13 27.63 0.1 . 1 . . . . . . . . 5497 1 799 . 1 1 98 98 GLN N N 15 118.444 0.1 . 1 . . . . . . . . 5497 1 800 . 1 1 99 99 ASP H H 1 8.639 0.01 . 1 . . . . . . . . 5497 1 801 . 1 1 99 99 ASP HA H 1 4.34 0.01 . 1 . . . . . . . . 5497 1 802 . 1 1 99 99 ASP HB2 H 1 3.18 0.01 . 2 . . . . . . . . 5497 1 803 . 1 1 99 99 ASP HB3 H 1 2.56 0.01 . 2 . . . . . . . . 5497 1 804 . 1 1 99 99 ASP C C 13 177.410 0.1 . 1 . . . . . . . . 5497 1 805 . 1 1 99 99 ASP CA C 13 56.85 0.1 . 1 . . . . . . . . 5497 1 806 . 1 1 99 99 ASP CB C 13 39.82 0.1 . 1 . . . . . . . . 5497 1 807 . 1 1 99 99 ASP N N 15 125.062 0.1 . 1 . . . . . . . . 5497 1 808 . 1 1 100 100 VAL H H 1 8.747 0.01 . 1 . . . . . . . . 5497 1 809 . 1 1 100 100 VAL HA H 1 3.56 0.01 . 1 . . . . . . . . 5497 1 810 . 1 1 100 100 VAL HB H 1 1.98 0.01 . 1 . . . . . . . . 5497 1 811 . 1 1 100 100 VAL HG11 H 1 0.94 0.01 . 1 . . . . . . . . 5497 1 812 . 1 1 100 100 VAL HG12 H 1 0.94 0.01 . 1 . . . . . . . . 5497 1 813 . 1 1 100 100 VAL HG13 H 1 0.94 0.01 . 1 . . . . . . . . 5497 1 814 . 1 1 100 100 VAL HG21 H 1 0.94 0.01 . 1 . . . . . . . . 5497 1 815 . 1 1 100 100 VAL HG22 H 1 0.94 0.01 . 1 . . . . . . . . 5497 1 816 . 1 1 100 100 VAL HG23 H 1 0.94 0.01 . 1 . . . . . . . . 5497 1 817 . 1 1 100 100 VAL C C 13 178.142 0.1 . 1 . . . . . . . . 5497 1 818 . 1 1 100 100 VAL CA C 13 65.72 0.1 . 1 . . . . . . . . 5497 1 819 . 1 1 100 100 VAL CB C 13 31.47 0.1 . 1 . . . . . . . . 5497 1 820 . 1 1 100 100 VAL CG1 C 13 20.43 0.1 . 2 . . . . . . . . 5497 1 821 . 1 1 100 100 VAL CG2 C 13 22.30 0.1 . 2 . . . . . . . . 5497 1 822 . 1 1 100 100 VAL N N 15 118.351 0.1 . 1 . . . . . . . . 5497 1 823 . 1 1 101 101 ALA H H 1 7.591 0.01 . 1 . . . . . . . . 5497 1 824 . 1 1 101 101 ALA HA H 1 4.17 0.01 . 1 . . . . . . . . 5497 1 825 . 1 1 101 101 ALA HB1 H 1 1.56 0.01 . 1 . . . . . . . . 5497 1 826 . 1 1 101 101 ALA HB2 H 1 1.56 0.01 . 1 . . . . . . . . 5497 1 827 . 1 1 101 101 ALA HB3 H 1 1.56 0.01 . 1 . . . . . . . . 5497 1 828 . 1 1 101 101 ALA C C 13 180.006 0.1 . 1 . . . . . . . . 5497 1 829 . 1 1 101 101 ALA CA C 13 54.55 0.1 . 1 . . . . . . . . 5497 1 830 . 1 1 101 101 ALA CB C 13 17.50 0.1 . 1 . . . . . . . . 5497 1 831 . 1 1 101 101 ALA N N 15 121.634 0.1 . 1 . . . . . . . . 5497 1 832 . 1 1 102 102 LEU H H 1 8.091 0.01 . 1 . . . . . . . . 5497 1 833 . 1 1 102 102 LEU HA H 1 4.02 0.01 . 1 . . . . . . . . 5497 1 834 . 1 1 102 102 LEU HB2 H 1 1.49 0.01 . 2 . . . . . . . . 5497 1 835 . 1 1 102 102 LEU HB3 H 1 2.21 0.01 . 2 . . . . . . . . 5497 1 836 . 1 1 102 102 LEU HG H 1 1.38 0.01 . 1 . . . . . . . . 5497 1 837 . 1 1 102 102 LEU HD11 H 1 0.67 0.01 . 2 . . . . . . . . 5497 1 838 . 1 1 102 102 LEU HD12 H 1 0.67 0.01 . 2 . . . . . . . . 5497 1 839 . 1 1 102 102 LEU HD13 H 1 0.67 0.01 . 2 . . . . . . . . 5497 1 840 . 1 1 102 102 LEU HD21 H 1 0.61 0.01 . 2 . . . . . . . . 5497 1 841 . 1 1 102 102 LEU HD22 H 1 0.61 0.01 . 2 . . . . . . . . 5497 1 842 . 1 1 102 102 LEU HD23 H 1 0.61 0.01 . 2 . . . . . . . . 5497 1 843 . 1 1 102 102 LEU C C 13 178.896 0.1 . 1 . . . . . . . . 5497 1 844 . 1 1 102 102 LEU CA C 13 57.83 0.1 . 1 . . . . . . . . 5497 1 845 . 1 1 102 102 LEU CB C 13 40.76 0.1 . 1 . . . . . . . . 5497 1 846 . 1 1 102 102 LEU CG C 13 26.60 0.1 . 1 . . . . . . . . 5497 1 847 . 1 1 102 102 LEU CD1 C 13 23.35 0.1 . 2 . . . . . . . . 5497 1 848 . 1 1 102 102 LEU CD2 C 13 25.59 0.1 . 2 . . . . . . . . 5497 1 849 . 1 1 102 102 LEU N N 15 122.907 0.1 . 1 . . . . . . . . 5497 1 850 . 1 1 103 103 LEU H H 1 8.389 0.01 . 1 . . . . . . . . 5497 1 851 . 1 1 103 103 LEU HA H 1 3.81 0.01 . 1 . . . . . . . . 5497 1 852 . 1 1 103 103 LEU HB2 H 1 1.55 0.01 . 2 . . . . . . . . 5497 1 853 . 1 1 103 103 LEU HB3 H 1 1.98 0.01 . 2 . . . . . . . . 5497 1 854 . 1 1 103 103 LEU HG H 1 1.99 0.01 . 1 . . . . . . . . 5497 1 855 . 1 1 103 103 LEU HD11 H 1 0.78 0.01 . 2 . . . . . . . . 5497 1 856 . 1 1 103 103 LEU HD12 H 1 0.78 0.01 . 2 . . . . . . . . 5497 1 857 . 1 1 103 103 LEU HD13 H 1 0.78 0.01 . 2 . . . . . . . . 5497 1 858 . 1 1 103 103 LEU HD21 H 1 0.92 0.01 . 2 . . . . . . . . 5497 1 859 . 1 1 103 103 LEU HD22 H 1 0.92 0.01 . 2 . . . . . . . . 5497 1 860 . 1 1 103 103 LEU HD23 H 1 0.92 0.01 . 2 . . . . . . . . 5497 1 861 . 1 1 103 103 LEU C C 13 177.240 0.1 . 1 . . . . . . . . 5497 1 862 . 1 1 103 103 LEU CA C 13 58.03 0.1 . 1 . . . . . . . . 5497 1 863 . 1 1 103 103 LEU CB C 13 40.27 0.1 . 1 . . . . . . . . 5497 1 864 . 1 1 103 103 LEU CG C 13 26.41 0.1 . 1 . . . . . . . . 5497 1 865 . 1 1 103 103 LEU CD1 C 13 22.82 0.1 . 2 . . . . . . . . 5497 1 866 . 1 1 103 103 LEU CD2 C 13 24.72 0.1 . 2 . . . . . . . . 5497 1 867 . 1 1 103 103 LEU N N 15 118.738 0.1 . 1 . . . . . . . . 5497 1 868 . 1 1 104 104 LYS H H 1 8.389 0.01 . 1 . . . . . . . . 5497 1 869 . 1 1 104 104 LYS HA H 1 4.22 0.01 . 1 . . . . . . . . 5497 1 870 . 1 1 104 104 LYS HB2 H 1 1.92 0.01 . 2 . . . . . . . . 5497 1 871 . 1 1 104 104 LYS HE2 H 1 2.96 0.01 . 2 . . . . . . . . 5497 1 872 . 1 1 104 104 LYS C C 13 179.845 0.1 . 1 . . . . . . . . 5497 1 873 . 1 1 104 104 LYS CA C 13 58.40 0.1 . 1 . . . . . . . . 5497 1 874 . 1 1 104 104 LYS CB C 13 31.83 0.1 . 1 . . . . . . . . 5497 1 875 . 1 1 104 104 LYS N N 15 118.738 0.1 . 1 . . . . . . . . 5497 1 876 . 1 1 105 105 HIS H H 1 8.294 0.01 . 1 . . . . . . . . 5497 1 877 . 1 1 105 105 HIS HA H 1 4.26 0.01 . 1 . . . . . . . . 5497 1 878 . 1 1 105 105 HIS HB2 H 1 3.38 0.01 . 2 . . . . . . . . 5497 1 879 . 1 1 105 105 HIS HB3 H 1 3.26 0.01 . 2 . . . . . . . . 5497 1 880 . 1 1 105 105 HIS C C 13 176.067 0.1 . 1 . . . . . . . . 5497 1 881 . 1 1 105 105 HIS CA C 13 58.97 0.1 . 1 . . . . . . . . 5497 1 882 . 1 1 105 105 HIS CB C 13 30.76 0.1 . 1 . . . . . . . . 5497 1 883 . 1 1 105 105 HIS N N 15 121.880 0.1 . 1 . . . . . . . . 5497 1 884 . 1 1 106 106 LEU H H 1 7.533 0.01 . 1 . . . . . . . . 5497 1 885 . 1 1 106 106 LEU HA H 1 4.13 0.01 . 1 . . . . . . . . 5497 1 886 . 1 1 106 106 LEU HB2 H 1 1.58 0.01 . 2 . . . . . . . . 5497 1 887 . 1 1 106 106 LEU HG H 1 1.93 0.01 . 1 . . . . . . . . 5497 1 888 . 1 1 106 106 LEU HD11 H 1 0.80 0.01 . 2 . . . . . . . . 5497 1 889 . 1 1 106 106 LEU HD12 H 1 0.80 0.01 . 2 . . . . . . . . 5497 1 890 . 1 1 106 106 LEU HD13 H 1 0.80 0.01 . 2 . . . . . . . . 5497 1 891 . 1 1 106 106 LEU HD21 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 892 . 1 1 106 106 LEU HD22 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 893 . 1 1 106 106 LEU HD23 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 894 . 1 1 106 106 LEU C C 13 174.982 0.1 . 1 . . . . . . . . 5497 1 895 . 1 1 106 106 LEU CA C 13 53.39 0.1 . 1 . . . . . . . . 5497 1 896 . 1 1 106 106 LEU CB C 13 42.71 0.1 . 1 . . . . . . . . 5497 1 897 . 1 1 106 106 LEU CG C 13 25.81 0.1 . 1 . . . . . . . . 5497 1 898 . 1 1 106 106 LEU CD1 C 13 26.22 0.1 . 2 . . . . . . . . 5497 1 899 . 1 1 106 106 LEU CD2 C 13 20.75 0.1 . 2 . . . . . . . . 5497 1 900 . 1 1 106 106 LEU N N 15 114.339 0.1 . 1 . . . . . . . . 5497 1 901 . 1 1 107 107 ASN H H 1 8.000 0.01 . 1 . . . . . . . . 5497 1 902 . 1 1 107 107 ASN HA H 1 4.30 0.01 . 1 . . . . . . . . 5497 1 903 . 1 1 107 107 ASN HB2 H 1 3.14 0.01 . 2 . . . . . . . . 5497 1 904 . 1 1 107 107 ASN HB3 H 1 2.65 0.01 . 2 . . . . . . . . 5497 1 905 . 1 1 107 107 ASN HD21 H 1 7.498 0.01 . 2 . . . . . . . . 5497 1 906 . 1 1 107 107 ASN HD22 H 1 6.674 0.01 . 2 . . . . . . . . 5497 1 907 . 1 1 107 107 ASN C C 13 173.566 0.1 . 1 . . . . . . . . 5497 1 908 . 1 1 107 107 ASN CA C 13 53.49 0.1 . 1 . . . . . . . . 5497 1 909 . 1 1 107 107 ASN CB C 13 36.33 0.1 . 1 . . . . . . . . 5497 1 910 . 1 1 107 107 ASN CG C 13 177.416 0.1 . 1 . . . . . . . . 5497 1 911 . 1 1 107 107 ASN N N 15 118.444 0.1 . 1 . . . . . . . . 5497 1 912 . 1 1 107 107 ASN ND2 N 15 112.408 0.1 . 1 . . . . . . . . 5497 1 913 . 1 1 108 108 VAL H H 1 8.100 0.01 . 1 . . . . . . . . 5497 1 914 . 1 1 108 108 VAL HA H 1 3.91 0.01 . 1 . . . . . . . . 5497 1 915 . 1 1 108 108 VAL HB H 1 1.88 0.01 . 1 . . . . . . . . 5497 1 916 . 1 1 108 108 VAL HG11 H 1 0.88 0.01 . 1 . . . . . . . . 5497 1 917 . 1 1 108 108 VAL HG12 H 1 0.88 0.01 . 1 . . . . . . . . 5497 1 918 . 1 1 108 108 VAL HG13 H 1 0.88 0.01 . 1 . . . . . . . . 5497 1 919 . 1 1 108 108 VAL HG21 H 1 0.88 0.01 . 1 . . . . . . . . 5497 1 920 . 1 1 108 108 VAL HG22 H 1 0.88 0.01 . 1 . . . . . . . . 5497 1 921 . 1 1 108 108 VAL HG23 H 1 0.88 0.01 . 1 . . . . . . . . 5497 1 922 . 1 1 108 108 VAL C C 13 175.087 0.1 . 1 . . . . . . . . 5497 1 923 . 1 1 108 108 VAL CA C 13 62.05 0.1 . 1 . . . . . . . . 5497 1 924 . 1 1 108 108 VAL CB C 13 32.23 0.1 . 1 . . . . . . . . 5497 1 925 . 1 1 108 108 VAL CG1 C 13 22.37 0.1 . 2 . . . . . . . . 5497 1 926 . 1 1 108 108 VAL CG2 C 13 21.03 0.1 . 2 . . . . . . . . 5497 1 927 . 1 1 108 108 VAL N N 15 119.709 0.1 . 1 . . . . . . . . 5497 1 928 . 1 1 109 109 LEU H H 1 8.633 0.01 . 1 . . . . . . . . 5497 1 929 . 1 1 109 109 LEU HA H 1 4.43 0.01 . 1 . . . . . . . . 5497 1 930 . 1 1 109 109 LEU HB2 H 1 1.64 0.01 . 2 . . . . . . . . 5497 1 931 . 1 1 109 109 LEU HG H 1 1.59 0.01 . 1 . . . . . . . . 5497 1 932 . 1 1 109 109 LEU HD11 H 1 0.79 0.01 . 2 . . . . . . . . 5497 1 933 . 1 1 109 109 LEU HD12 H 1 0.79 0.01 . 2 . . . . . . . . 5497 1 934 . 1 1 109 109 LEU HD13 H 1 0.79 0.01 . 2 . . . . . . . . 5497 1 935 . 1 1 109 109 LEU HD21 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 936 . 1 1 109 109 LEU HD22 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 937 . 1 1 109 109 LEU HD23 H 1 0.90 0.01 . 2 . . . . . . . . 5497 1 938 . 1 1 109 109 LEU C C 13 176.217 0.1 . 1 . . . . . . . . 5497 1 939 . 1 1 109 109 LEU CA C 13 54.66 0.1 . 1 . . . . . . . . 5497 1 940 . 1 1 109 109 LEU CB C 13 41.88 0.1 . 1 . . . . . . . . 5497 1 941 . 1 1 109 109 LEU CG C 13 26.65 0.1 . 1 . . . . . . . . 5497 1 942 . 1 1 109 109 LEU CD1 C 13 22.18 0.1 . 2 . . . . . . . . 5497 1 943 . 1 1 109 109 LEU CD2 C 13 24.31 0.1 . 2 . . . . . . . . 5497 1 944 . 1 1 109 109 LEU N N 15 128.878 0.1 . 1 . . . . . . . . 5497 1 945 . 1 1 110 110 GLY H H 1 7.361 0.01 . 1 . . . . . . . . 5497 1 946 . 1 1 110 110 GLY HA2 H 1 4.09 0.01 . 2 . . . . . . . . 5497 1 947 . 1 1 110 110 GLY HA3 H 1 3.95 0.01 . 2 . . . . . . . . 5497 1 948 . 1 1 110 110 GLY C C 13 169.246 0.1 . 1 . . . . . . . . 5497 1 949 . 1 1 110 110 GLY CA C 13 44.22 0.1 . 1 . . . . . . . . 5497 1 950 . 1 1 110 110 GLY N N 15 107.387 0.1 . 1 . . . . . . . . 5497 1 951 . 1 1 111 111 LEU H H 1 8.694 0.01 . 1 . . . . . . . . 5497 1 952 . 1 1 111 111 LEU HA H 1 4.48 0.01 . 1 . . . . . . . . 5497 1 953 . 1 1 111 111 LEU HB2 H 1 1.50 0.01 . 2 . . . . . . . . 5497 1 954 . 1 1 111 111 LEU HB3 H 1 1.59 0.01 . 2 . . . . . . . . 5497 1 955 . 1 1 111 111 LEU HG H 1 1.60 0.01 . 1 . . . . . . . . 5497 1 956 . 1 1 111 111 LEU HD11 H 1 0.54 0.01 . 1 . . . . . . . . 5497 1 957 . 1 1 111 111 LEU HD12 H 1 0.54 0.01 . 1 . . . . . . . . 5497 1 958 . 1 1 111 111 LEU HD13 H 1 0.54 0.01 . 1 . . . . . . . . 5497 1 959 . 1 1 111 111 LEU HD21 H 1 0.54 0.01 . 1 . . . . . . . . 5497 1 960 . 1 1 111 111 LEU HD22 H 1 0.54 0.01 . 1 . . . . . . . . 5497 1 961 . 1 1 111 111 LEU HD23 H 1 0.54 0.01 . 1 . . . . . . . . 5497 1 962 . 1 1 111 111 LEU CA C 13 51.92 0.1 . 1 . . . . . . . . 5497 1 963 . 1 1 111 111 LEU CB C 13 42.40 0.1 . 1 . . . . . . . . 5497 1 964 . 1 1 111 111 LEU CG C 13 28.78 0.1 . 1 . . . . . . . . 5497 1 965 . 1 1 111 111 LEU CD1 C 13 24.59 0.1 . 1 . . . . . . . . 5497 1 966 . 1 1 111 111 LEU CD2 C 13 24.59 0.1 . 1 . . . . . . . . 5497 1 967 . 1 1 111 111 LEU N N 15 120.927 0.1 . 1 . . . . . . . . 5497 1 968 . 1 1 112 112 PRO HA H 1 4.39 0.01 . 1 . . . . . . . . 5497 1 969 . 1 1 112 112 PRO HB2 H 1 2.65 0.01 . 2 . . . . . . . . 5497 1 970 . 1 1 112 112 PRO HB3 H 1 1.85 0.01 . 2 . . . . . . . . 5497 1 971 . 1 1 112 112 PRO HG2 H 1 1.68 0.01 . 2 . . . . . . . . 5497 1 972 . 1 1 112 112 PRO HG3 H 1 1.72 0.01 . 2 . . . . . . . . 5497 1 973 . 1 1 112 112 PRO HD2 H 1 3.47 0.01 . 2 . . . . . . . . 5497 1 974 . 1 1 112 112 PRO HD3 H 1 3.79 0.01 . 2 . . . . . . . . 5497 1 975 . 1 1 112 112 PRO C C 13 175.288 0.1 . 1 . . . . . . . . 5497 1 976 . 1 1 112 112 PRO CA C 13 61.92 0.1 . 1 . . . . . . . . 5497 1 977 . 1 1 112 112 PRO CB C 13 34.69 0.1 . 1 . . . . . . . . 5497 1 978 . 1 1 112 112 PRO CG C 13 23.72 0.1 . 1 . . . . . . . . 5497 1 979 . 1 1 112 112 PRO CD C 13 50.37 0.1 . 1 . . . . . . . . 5497 1 980 . 1 1 113 113 THR H H 1 8.389 0.01 . 1 . . . . . . . . 5497 1 981 . 1 1 113 113 THR HA H 1 5.16 0.01 . 1 . . . . . . . . 5497 1 982 . 1 1 113 113 THR HB H 1 3.91 0.01 . 1 . . . . . . . . 5497 1 983 . 1 1 113 113 THR C C 13 169.875 0.1 . 1 . . . . . . . . 5497 1 984 . 1 1 113 113 THR CA C 13 63.99 0.1 . 1 . . . . . . . . 5497 1 985 . 1 1 113 113 THR CB C 13 72.93 0.1 . 1 . . . . . . . . 5497 1 986 . 1 1 113 113 THR N N 15 118.738 0.1 . 1 . . . . . . . . 5497 1 987 . 1 1 114 114 ILE H H 1 8.750 0.01 . 1 . . . . . . . . 5497 1 988 . 1 1 114 114 ILE HA H 1 4.82 0.01 . 1 . . . . . . . . 5497 1 989 . 1 1 114 114 ILE HB H 1 1.67 0.01 . 1 . . . . . . . . 5497 1 990 . 1 1 114 114 ILE HG12 H 1 1.37 0.01 . 2 . . . . . . . . 5497 1 991 . 1 1 114 114 ILE HG13 H 1 1.23 0.01 . 2 . . . . . . . . 5497 1 992 . 1 1 114 114 ILE HG21 H 1 0.71 0.01 . 1 . . . . . . . . 5497 1 993 . 1 1 114 114 ILE HG22 H 1 0.71 0.01 . 1 . . . . . . . . 5497 1 994 . 1 1 114 114 ILE HG23 H 1 0.71 0.01 . 1 . . . . . . . . 5497 1 995 . 1 1 114 114 ILE HD11 H 1 0.17 0.01 . 1 . . . . . . . . 5497 1 996 . 1 1 114 114 ILE HD12 H 1 0.17 0.01 . 1 . . . . . . . . 5497 1 997 . 1 1 114 114 ILE HD13 H 1 0.17 0.01 . 1 . . . . . . . . 5497 1 998 . 1 1 114 114 ILE C C 13 174.259 0.1 . 1 . . . . . . . . 5497 1 999 . 1 1 114 114 ILE CA C 13 59.82 0.1 . 1 . . . . . . . . 5497 1 1000 . 1 1 114 114 ILE CB C 13 39.74 0.1 . 1 . . . . . . . . 5497 1 1001 . 1 1 114 114 ILE CG1 C 13 26.91 0.1 . 1 . . . . . . . . 5497 1 1002 . 1 1 114 114 ILE CG2 C 13 18.48 0.1 . 1 . . . . . . . . 5497 1 1003 . 1 1 114 114 ILE CD1 C 13 13.86 0.1 . 1 . . . . . . . . 5497 1 1004 . 1 1 114 114 ILE N N 15 126.471 0.1 . 1 . . . . . . . . 5497 1 1005 . 1 1 115 115 LEU H H 1 8.739 0.01 . 1 . . . . . . . . 5497 1 1006 . 1 1 115 115 LEU HA H 1 4.90 0.01 . 1 . . . . . . . . 5497 1 1007 . 1 1 115 115 LEU HB2 H 1 1.29 0.01 . 2 . . . . . . . . 5497 1 1008 . 1 1 115 115 LEU HB3 H 1 1.45 0.01 . 2 . . . . . . . . 5497 1 1009 . 1 1 115 115 LEU HG H 1 1.45 0.01 . 1 . . . . . . . . 5497 1 1010 . 1 1 115 115 LEU HD11 H 1 0.85 0.01 . 2 . . . . . . . . 5497 1 1011 . 1 1 115 115 LEU HD12 H 1 0.85 0.01 . 2 . . . . . . . . 5497 1 1012 . 1 1 115 115 LEU HD13 H 1 0.85 0.01 . 2 . . . . . . . . 5497 1 1013 . 1 1 115 115 LEU HD21 H 1 0.78 0.01 . 2 . . . . . . . . 5497 1 1014 . 1 1 115 115 LEU HD22 H 1 0.78 0.01 . 2 . . . . . . . . 5497 1 1015 . 1 1 115 115 LEU HD23 H 1 0.78 0.01 . 2 . . . . . . . . 5497 1 1016 . 1 1 115 115 LEU C C 13 174.351 0.1 . 1 . . . . . . . . 5497 1 1017 . 1 1 115 115 LEU CA C 13 53.82 0.1 . 1 . . . . . . . . 5497 1 1018 . 1 1 115 115 LEU CB C 13 44.96 0.1 . 1 . . . . . . . . 5497 1 1019 . 1 1 115 115 LEU CG C 13 28.90 0.1 . 1 . . . . . . . . 5497 1 1020 . 1 1 115 115 LEU CD1 C 13 27.15 0.1 . 2 . . . . . . . . 5497 1 1021 . 1 1 115 115 LEU CD2 C 13 27.45 0.1 . 2 . . . . . . . . 5497 1 1022 . 1 1 115 115 LEU N N 15 125.518 0.1 . 1 . . . . . . . . 5497 1 1023 . 1 1 116 116 PHE H H 1 9.963 0.01 . 1 . . . . . . . . 5497 1 1024 . 1 1 116 116 PHE HA H 1 5.30 0.01 . 1 . . . . . . . . 5497 1 1025 . 1 1 116 116 PHE HB2 H 1 3.15 0.01 . 2 . . . . . . . . 5497 1 1026 . 1 1 116 116 PHE HB3 H 1 2.51 0.01 . 2 . . . . . . . . 5497 1 1027 . 1 1 116 116 PHE C C 13 173.359 0.1 . 1 . . . . . . . . 5497 1 1028 . 1 1 116 116 PHE CA C 13 56.50 0.1 . 1 . . . . . . . . 5497 1 1029 . 1 1 116 116 PHE CB C 13 41.91 0.1 . 1 . . . . . . . . 5497 1 1030 . 1 1 116 116 PHE N N 15 118.726 0.1 . 1 . . . . . . . . 5497 1 1031 . 1 1 117 117 PHE H H 1 9.332 0.01 . 1 . . . . . . . . 5497 1 1032 . 1 1 117 117 PHE HA H 1 5.38 0.01 . 1 . . . . . . . . 5497 1 1033 . 1 1 117 117 PHE HB2 H 1 2.89 0.01 . 2 . . . . . . . . 5497 1 1034 . 1 1 117 117 PHE HB3 H 1 2.64 0.01 . 2 . . . . . . . . 5497 1 1035 . 1 1 117 117 PHE C C 13 175.856 0.1 . 1 . . . . . . . . 5497 1 1036 . 1 1 117 117 PHE CA C 13 54.38 0.1 . 1 . . . . . . . . 5497 1 1037 . 1 1 117 117 PHE CB C 13 40.76 0.1 . 1 . . . . . . . . 5497 1 1038 . 1 1 117 117 PHE N N 15 120.081 0.1 . 1 . . . . . . . . 5497 1 1039 . 1 1 118 118 ASP H H 1 8.655 0.01 . 1 . . . . . . . . 5497 1 1040 . 1 1 118 118 ASP HA H 1 4.66 0.01 . 1 . . . . . . . . 5497 1 1041 . 1 1 118 118 ASP HB2 H 1 3.36 0.01 . 2 . . . . . . . . 5497 1 1042 . 1 1 118 118 ASP HB3 H 1 2.55 0.01 . 2 . . . . . . . . 5497 1 1043 . 1 1 118 118 ASP C C 13 176.864 0.1 . 1 . . . . . . . . 5497 1 1044 . 1 1 118 118 ASP CA C 13 51.50 0.1 . 1 . . . . . . . . 5497 1 1045 . 1 1 118 118 ASP CB C 13 41.67 0.1 . 1 . . . . . . . . 5497 1 1046 . 1 1 118 118 ASP N N 15 121.144 0.1 . 1 . . . . . . . . 5497 1 1047 . 1 1 119 119 GLY H H 1 8.544 0.01 . 1 . . . . . . . . 5497 1 1048 . 1 1 119 119 GLY HA2 H 1 4.17 0.01 . 2 . . . . . . . . 5497 1 1049 . 1 1 119 119 GLY HA3 H 1 3.54 0.01 . 2 . . . . . . . . 5497 1 1050 . 1 1 119 119 GLY C C 13 174.219 0.1 . 1 . . . . . . . . 5497 1 1051 . 1 1 119 119 GLY CA C 13 45.72 0.1 . 1 . . . . . . . . 5497 1 1052 . 1 1 119 119 GLY N N 15 104.367 0.1 . 1 . . . . . . . . 5497 1 1053 . 1 1 120 120 GLN H H 1 8.539 0.01 . 1 . . . . . . . . 5497 1 1054 . 1 1 120 120 GLN HA H 1 4.60 0.01 . 1 . . . . . . . . 5497 1 1055 . 1 1 120 120 GLN HB2 H 1 2.17 0.01 . 2 . . . . . . . . 5497 1 1056 . 1 1 120 120 GLN HG2 H 1 2.35 0.01 . 2 . . . . . . . . 5497 1 1057 . 1 1 120 120 GLN C C 13 175.806 0.1 . 1 . . . . . . . . 5497 1 1058 . 1 1 120 120 GLN CA C 13 54.57 0.1 . 1 . . . . . . . . 5497 1 1059 . 1 1 120 120 GLN CB C 13 28.44 0.1 . 1 . . . . . . . . 5497 1 1060 . 1 1 120 120 GLN CG C 13 34.02 0.1 . 1 . . . . . . . . 5497 1 1061 . 1 1 120 120 GLN N N 15 118.703 0.1 . 1 . . . . . . . . 5497 1 1062 . 1 1 121 121 GLY H H 1 8.365 0.01 . 1 . . . . . . . . 5497 1 1063 . 1 1 121 121 GLY HA2 H 1 4.17 0.01 . 2 . . . . . . . . 5497 1 1064 . 1 1 121 121 GLY HA3 H 1 3.54 0.01 . 2 . . . . . . . . 5497 1 1065 . 1 1 121 121 GLY C C 13 172.636 0.1 . 1 . . . . . . . . 5497 1 1066 . 1 1 121 121 GLY CA C 13 45.77 0.1 . 1 . . . . . . . . 5497 1 1067 . 1 1 121 121 GLY N N 15 110.054 0.1 . 1 . . . . . . . . 5497 1 1068 . 1 1 122 122 GLN H H 1 8.317 0.01 . 1 . . . . . . . . 5497 1 1069 . 1 1 122 122 GLN HA H 1 4.59 0.01 . 1 . . . . . . . . 5497 1 1070 . 1 1 122 122 GLN HG2 H 1 2.23 0.01 . 2 . . . . . . . . 5497 1 1071 . 1 1 122 122 GLN HG3 H 1 2.33 0.01 . 2 . . . . . . . . 5497 1 1072 . 1 1 122 122 GLN C C 13 175.482 0.1 . 1 . . . . . . . . 5497 1 1073 . 1 1 122 122 GLN CA C 13 53.66 0.1 . 1 . . . . . . . . 5497 1 1074 . 1 1 122 122 GLN CB C 13 28.83 0.1 . 1 . . . . . . . . 5497 1 1075 . 1 1 122 122 GLN CG C 13 33.05 0.1 . 1 . . . . . . . . 5497 1 1076 . 1 1 122 122 GLN N N 15 120.164 0.1 . 1 . . . . . . . . 5497 1 1077 . 1 1 123 123 GLU H H 1 9.122 0.01 . 1 . . . . . . . . 5497 1 1078 . 1 1 123 123 GLU HA H 1 4.10 0.01 . 1 . . . . . . . . 5497 1 1079 . 1 1 123 123 GLU HG2 H 1 1.74 0.01 . 2 . . . . . . . . 5497 1 1080 . 1 1 123 123 GLU HG3 H 1 1.62 0.01 . 2 . . . . . . . . 5497 1 1081 . 1 1 123 123 GLU C C 13 176.710 0.1 . 1 . . . . . . . . 5497 1 1082 . 1 1 123 123 GLU CA C 13 56.14 0.1 . 1 . . . . . . . . 5497 1 1083 . 1 1 123 123 GLU CG C 13 35.50 0.1 . 1 . . . . . . . . 5497 1 1084 . 1 1 123 123 GLU N N 15 128.752 0.1 . 1 . . . . . . . . 5497 1 1085 . 1 1 124 124 HIS H H 1 8.274 0.01 . 1 . . . . . . . . 5497 1 1086 . 1 1 124 124 HIS HA H 1 5.18 0.01 . 1 . . . . . . . . 5497 1 1087 . 1 1 124 124 HIS HB2 H 1 3.06 0.01 . 2 . . . . . . . . 5497 1 1088 . 1 1 124 124 HIS HB3 H 1 2.86 0.01 . 2 . . . . . . . . 5497 1 1089 . 1 1 124 124 HIS CA C 13 52.93 0.1 . 1 . . . . . . . . 5497 1 1090 . 1 1 124 124 HIS CB C 13 30.54 0.1 . 1 . . . . . . . . 5497 1 1091 . 1 1 124 124 HIS N N 15 126.187 0.1 . 1 . . . . . . . . 5497 1 1092 . 1 1 125 125 PRO HA H 1 4.51 0.01 . 1 . . . . . . . . 5497 1 1093 . 1 1 125 125 PRO HB2 H 1 2.00 0.01 . 2 . . . . . . . . 5497 1 1094 . 1 1 125 125 PRO HB3 H 1 2.36 0.01 . 2 . . . . . . . . 5497 1 1095 . 1 1 125 125 PRO HG2 H 1 2.00 0.01 . 2 . . . . . . . . 5497 1 1096 . 1 1 125 125 PRO HD2 H 1 3.90 0.01 . 2 . . . . . . . . 5497 1 1097 . 1 1 125 125 PRO HD3 H 1 3.73 0.01 . 2 . . . . . . . . 5497 1 1098 . 1 1 125 125 PRO C C 13 178.158 0.1 . 1 . . . . . . . . 5497 1 1099 . 1 1 125 125 PRO CA C 13 64.34 0.1 . 1 . . . . . . . . 5497 1 1100 . 1 1 125 125 PRO CB C 13 31.01 0.1 . 1 . . . . . . . . 5497 1 1101 . 1 1 125 125 PRO CG C 13 26.78 0.1 . 1 . . . . . . . . 5497 1 1102 . 1 1 125 125 PRO CD C 13 51.17 0.1 . 1 . . . . . . . . 5497 1 1103 . 1 1 126 126 GLN H H 1 9.285 0.01 . 1 . . . . . . . . 5497 1 1104 . 1 1 126 126 GLN HA H 1 4.28 0.01 . 1 . . . . . . . . 5497 1 1105 . 1 1 126 126 GLN HB2 H 1 2.07 0.01 . 2 . . . . . . . . 5497 1 1106 . 1 1 126 126 GLN HB3 H 1 2.16 0.01 . 2 . . . . . . . . 5497 1 1107 . 1 1 126 126 GLN HG2 H 1 2.52 0.01 . 2 . . . . . . . . 5497 1 1108 . 1 1 126 126 GLN HG3 H 1 2.45 0.01 . 2 . . . . . . . . 5497 1 1109 . 1 1 126 126 GLN C C 13 175.730 0.1 . 1 . . . . . . . . 5497 1 1110 . 1 1 126 126 GLN CA C 13 57.20 0.1 . 1 . . . . . . . . 5497 1 1111 . 1 1 126 126 GLN CB C 13 26.76 0.1 . 1 . . . . . . . . 5497 1 1112 . 1 1 126 126 GLN CG C 13 33.39 0.1 . 1 . . . . . . . . 5497 1 1113 . 1 1 126 126 GLN N N 15 118.708 0.1 . 1 . . . . . . . . 5497 1 1114 . 1 1 127 127 ALA H H 1 8.175 0.01 . 1 . . . . . . . . 5497 1 1115 . 1 1 127 127 ALA HA H 1 4.42 0.01 . 1 . . . . . . . . 5497 1 1116 . 1 1 127 127 ALA HB1 H 1 1.41 0.01 . 1 . . . . . . . . 5497 1 1117 . 1 1 127 127 ALA HB2 H 1 1.41 0.01 . 1 . . . . . . . . 5497 1 1118 . 1 1 127 127 ALA HB3 H 1 1.41 0.01 . 1 . . . . . . . . 5497 1 1119 . 1 1 127 127 ALA C C 13 175.279 0.1 . 1 . . . . . . . . 5497 1 1120 . 1 1 127 127 ALA CA C 13 50.38 0.1 . 1 . . . . . . . . 5497 1 1121 . 1 1 127 127 ALA CB C 13 19.17 0.1 . 1 . . . . . . . . 5497 1 1122 . 1 1 127 127 ALA N N 15 120.406 0.1 . 1 . . . . . . . . 5497 1 1123 . 1 1 128 128 ARG H H 1 7.448 0.01 . 1 . . . . . . . . 5497 1 1124 . 1 1 128 128 ARG HA H 1 4.94 0.01 . 1 . . . . . . . . 5497 1 1125 . 1 1 128 128 ARG HB2 H 1 1.66 0.01 . 2 . . . . . . . . 5497 1 1126 . 1 1 128 128 ARG HB3 H 1 2.03 0.01 . 2 . . . . . . . . 5497 1 1127 . 1 1 128 128 ARG HG2 H 1 1.84 0.01 . 2 . . . . . . . . 5497 1 1128 . 1 1 128 128 ARG HG3 H 1 2.33 0.01 . 2 . . . . . . . . 5497 1 1129 . 1 1 128 128 ARG HD2 H 1 3.19 0.01 . 2 . . . . . . . . 5497 1 1130 . 1 1 128 128 ARG HD3 H 1 3.00 0.01 . 2 . . . . . . . . 5497 1 1131 . 1 1 128 128 ARG C C 13 176.874 0.1 . 1 . . . . . . . . 5497 1 1132 . 1 1 128 128 ARG CA C 13 57.88 0.1 . 1 . . . . . . . . 5497 1 1133 . 1 1 128 128 ARG CB C 13 31.67 0.1 . 1 . . . . . . . . 5497 1 1134 . 1 1 128 128 ARG CG C 13 28.68 0.1 . 1 . . . . . . . . 5497 1 1135 . 1 1 128 128 ARG CD C 13 43.64 0.1 . 1 . . . . . . . . 5497 1 1136 . 1 1 128 128 ARG N N 15 118.617 0.1 . 1 . . . . . . . . 5497 1 1137 . 1 1 129 129 VAL H H 1 8.814 0.01 . 1 . . . . . . . . 5497 1 1138 . 1 1 129 129 VAL HA H 1 4.43 0.01 . 1 . . . . . . . . 5497 1 1139 . 1 1 129 129 VAL HB H 1 2.19 0.01 . 1 . . . . . . . . 5497 1 1140 . 1 1 129 129 VAL HG11 H 1 0.97 0.01 . 2 . . . . . . . . 5497 1 1141 . 1 1 129 129 VAL HG12 H 1 0.97 0.01 . 2 . . . . . . . . 5497 1 1142 . 1 1 129 129 VAL HG13 H 1 0.97 0.01 . 2 . . . . . . . . 5497 1 1143 . 1 1 129 129 VAL HG21 H 1 1.41 0.01 . 2 . . . . . . . . 5497 1 1144 . 1 1 129 129 VAL HG22 H 1 1.41 0.01 . 2 . . . . . . . . 5497 1 1145 . 1 1 129 129 VAL HG23 H 1 1.41 0.01 . 2 . . . . . . . . 5497 1 1146 . 1 1 129 129 VAL C C 13 176.094 0.1 . 1 . . . . . . . . 5497 1 1147 . 1 1 129 129 VAL CA C 13 61.56 0.1 . 1 . . . . . . . . 5497 1 1148 . 1 1 129 129 VAL CB C 13 33.65 0.1 . 1 . . . . . . . . 5497 1 1149 . 1 1 129 129 VAL CG1 C 13 20.34 0.1 . 2 . . . . . . . . 5497 1 1150 . 1 1 129 129 VAL CG2 C 13 21.93 0.1 . 2 . . . . . . . . 5497 1 1151 . 1 1 129 129 VAL N N 15 125.623 0.1 . 1 . . . . . . . . 5497 1 1152 . 1 1 130 130 THR H H 1 8.887 0.01 . 1 . . . . . . . . 5497 1 1153 . 1 1 130 130 THR HA H 1 5.17 0.01 . 1 . . . . . . . . 5497 1 1154 . 1 1 130 130 THR HB H 1 4.75 0.01 . 1 . . . . . . . . 5497 1 1155 . 1 1 130 130 THR C C 13 173.171 0.1 . 1 . . . . . . . . 5497 1 1156 . 1 1 130 130 THR CA C 13 59.82 0.1 . 1 . . . . . . . . 5497 1 1157 . 1 1 130 130 THR CB C 13 68.65 0.1 . 1 . . . . . . . . 5497 1 1158 . 1 1 130 130 THR N N 15 115.721 0.1 . 1 . . . . . . . . 5497 1 1159 . 1 1 131 131 GLY H H 1 7.456 0.01 . 1 . . . . . . . . 5497 1 1160 . 1 1 131 131 GLY HA2 H 1 4.17 0.01 . 2 . . . . . . . . 5497 1 1161 . 1 1 131 131 GLY HA3 H 1 3.92 0.01 . 2 . . . . . . . . 5497 1 1162 . 1 1 131 131 GLY C C 13 170.329 0.1 . 1 . . . . . . . . 5497 1 1163 . 1 1 131 131 GLY CA C 13 43.65 0.1 . 1 . . . . . . . . 5497 1 1164 . 1 1 131 131 GLY N N 15 108.629 0.1 . 1 . . . . . . . . 5497 1 1165 . 1 1 132 132 PHE H H 1 8.787 0.01 . 1 . . . . . . . . 5497 1 1166 . 1 1 132 132 PHE HA H 1 3.70 0.01 . 1 . . . . . . . . 5497 1 1167 . 1 1 132 132 PHE HB2 H 1 2.90 0.01 . 2 . . . . . . . . 5497 1 1168 . 1 1 132 132 PHE HB3 H 1 2.58 0.01 . 2 . . . . . . . . 5497 1 1169 . 1 1 132 132 PHE C C 13 173.941 0.1 . 1 . . . . . . . . 5497 1 1170 . 1 1 132 132 PHE CA C 13 59.92 0.1 . 1 . . . . . . . . 5497 1 1171 . 1 1 132 132 PHE CB C 13 38.48 0.1 . 1 . . . . . . . . 5497 1 1172 . 1 1 132 132 PHE N N 15 117.518 0.1 . 1 . . . . . . . . 5497 1 1173 . 1 1 133 133 MET H H 1 4.865 0.01 . 1 . . . . . . . . 5497 1 1174 . 1 1 133 133 MET HA H 1 4.12 0.01 . 1 . . . . . . . . 5497 1 1175 . 1 1 133 133 MET HB2 H 1 1.86 0.01 . 2 . . . . . . . . 5497 1 1176 . 1 1 133 133 MET HB3 H 1 1.58 0.01 . 2 . . . . . . . . 5497 1 1177 . 1 1 133 133 MET HG2 H 1 2.71 0.01 . 2 . . . . . . . . 5497 1 1178 . 1 1 133 133 MET HG3 H 1 2.34 0.01 . 2 . . . . . . . . 5497 1 1179 . 1 1 133 133 MET C C 13 171.523 0.1 . 1 . . . . . . . . 5497 1 1180 . 1 1 133 133 MET CA C 13 54.20 0.1 . 1 . . . . . . . . 5497 1 1181 . 1 1 133 133 MET CB C 13 37.64 0.1 . 1 . . . . . . . . 5497 1 1182 . 1 1 133 133 MET CG C 13 32.33 0.1 . 1 . . . . . . . . 5497 1 1183 . 1 1 133 133 MET N N 15 127.224 0.1 . 1 . . . . . . . . 5497 1 1184 . 1 1 134 134 ASP H H 1 7.886 0.01 . 1 . . . . . . . . 5497 1 1185 . 1 1 134 134 ASP HA H 1 3.94 0.01 . 1 . . . . . . . . 5497 1 1186 . 1 1 134 134 ASP HB2 H 1 3.20 0.01 . 2 . . . . . . . . 5497 1 1187 . 1 1 134 134 ASP HB3 H 1 2.63 0.01 . 2 . . . . . . . . 5497 1 1188 . 1 1 134 134 ASP C C 13 173.914 0.1 . 1 . . . . . . . . 5497 1 1189 . 1 1 134 134 ASP CA C 13 51.67 0.1 . 1 . . . . . . . . 5497 1 1190 . 1 1 134 134 ASP CB C 13 39.44 0.1 . 1 . . . . . . . . 5497 1 1191 . 1 1 134 134 ASP N N 15 119.273 0.1 . 1 . . . . . . . . 5497 1 1192 . 1 1 135 135 ALA H H 1 8.705 0.01 . 1 . . . . . . . . 5497 1 1193 . 1 1 135 135 ALA HA H 1 4.08 0.01 . 1 . . . . . . . . 5497 1 1194 . 1 1 135 135 ALA HB1 H 1 1.67 0.01 . 1 . . . . . . . . 5497 1 1195 . 1 1 135 135 ALA HB2 H 1 1.67 0.01 . 1 . . . . . . . . 5497 1 1196 . 1 1 135 135 ALA HB3 H 1 1.67 0.01 . 1 . . . . . . . . 5497 1 1197 . 1 1 135 135 ALA C C 13 179.400 0.1 . 1 . . . . . . . . 5497 1 1198 . 1 1 135 135 ALA CA C 13 56.18 0.1 . 1 . . . . . . . . 5497 1 1199 . 1 1 135 135 ALA CB C 13 18.56 0.1 . 1 . . . . . . . . 5497 1 1200 . 1 1 135 135 ALA N N 15 120.309 0.1 . 1 . . . . . . . . 5497 1 1201 . 1 1 136 136 GLU H H 1 8.593 0.01 . 1 . . . . . . . . 5497 1 1202 . 1 1 136 136 GLU HA H 1 4.01 0.01 . 1 . . . . . . . . 5497 1 1203 . 1 1 136 136 GLU HB2 H 1 2.11 0.01 . 2 . . . . . . . . 5497 1 1204 . 1 1 136 136 GLU HB3 H 1 2.02 0.01 . 2 . . . . . . . . 5497 1 1205 . 1 1 136 136 GLU HG2 H 1 2.32 0.01 . 2 . . . . . . . . 5497 1 1206 . 1 1 136 136 GLU C C 13 178.953 0.1 . 1 . . . . . . . . 5497 1 1207 . 1 1 136 136 GLU CA C 13 59.30 0.1 . 1 . . . . . . . . 5497 1 1208 . 1 1 136 136 GLU CB C 13 29.06 0.1 . 1 . . . . . . . . 5497 1 1209 . 1 1 136 136 GLU CG C 13 35.82 0.1 . 1 . . . . . . . . 5497 1 1210 . 1 1 136 136 GLU N N 15 120.054 0.1 . 1 . . . . . . . . 5497 1 1211 . 1 1 137 137 THR H H 1 8.604 0.01 . 1 . . . . . . . . 5497 1 1212 . 1 1 137 137 THR HA H 1 3.95 0.01 . 1 . . . . . . . . 5497 1 1213 . 1 1 137 137 THR HB H 1 4.06 0.01 . 1 . . . . . . . . 5497 1 1214 . 1 1 137 137 THR C C 13 176.471 0.1 . 1 . . . . . . . . 5497 1 1215 . 1 1 137 137 THR CA C 13 66.25 0.1 . 1 . . . . . . . . 5497 1 1216 . 1 1 137 137 THR CB C 13 67.74 0.1 . 1 . . . . . . . . 5497 1 1217 . 1 1 137 137 THR N N 15 119.752 0.1 . 1 . . . . . . . . 5497 1 1218 . 1 1 138 138 PHE H H 1 9.669 0.01 . 1 . . . . . . . . 5497 1 1219 . 1 1 138 138 PHE HA H 1 4.69 0.01 . 1 . . . . . . . . 5497 1 1220 . 1 1 138 138 PHE HB2 H 1 3.13 0.01 . 2 . . . . . . . . 5497 1 1221 . 1 1 138 138 PHE HB3 H 1 2.84 0.01 . 2 . . . . . . . . 5497 1 1222 . 1 1 138 138 PHE C C 13 176.911 0.1 . 1 . . . . . . . . 5497 1 1223 . 1 1 138 138 PHE CA C 13 60.23 0.1 . 1 . . . . . . . . 5497 1 1224 . 1 1 138 138 PHE CB C 13 39.34 0.1 . 1 . . . . . . . . 5497 1 1225 . 1 1 138 138 PHE N N 15 125.227 0.1 . 1 . . . . . . . . 5497 1 1226 . 1 1 139 139 SER H H 1 8.666 0.01 . 1 . . . . . . . . 5497 1 1227 . 1 1 139 139 SER HA H 1 3.93 0.01 . 1 . . . . . . . . 5497 1 1228 . 1 1 139 139 SER HB2 H 1 4.01 0.01 . 2 . . . . . . . . 5497 1 1229 . 1 1 139 139 SER HB3 H 1 3.79 0.01 . 2 . . . . . . . . 5497 1 1230 . 1 1 139 139 SER C C 13 176.116 0.1 . 1 . . . . . . . . 5497 1 1231 . 1 1 139 139 SER CA C 13 62.71 0.1 . 1 . . . . . . . . 5497 1 1232 . 1 1 139 139 SER CB C 13 61.91 0.1 . 1 . . . . . . . . 5497 1 1233 . 1 1 139 139 SER N N 15 114.955 0.1 . 1 . . . . . . . . 5497 1 1234 . 1 1 140 140 ALA H H 1 7.615 0.01 . 1 . . . . . . . . 5497 1 1235 . 1 1 140 140 ALA HA H 1 3.98 0.01 . 1 . . . . . . . . 5497 1 1236 . 1 1 140 140 ALA HB1 H 1 1.53 0.01 . 1 . . . . . . . . 5497 1 1237 . 1 1 140 140 ALA HB2 H 1 1.53 0.01 . 1 . . . . . . . . 5497 1 1238 . 1 1 140 140 ALA HB3 H 1 1.53 0.01 . 1 . . . . . . . . 5497 1 1239 . 1 1 140 140 ALA C C 13 177.787 0.1 . 1 . . . . . . . . 5497 1 1240 . 1 1 140 140 ALA CA C 13 54.63 0.1 . 1 . . . . . . . . 5497 1 1241 . 1 1 140 140 ALA CB C 13 17.16 0.1 . 1 . . . . . . . . 5497 1 1242 . 1 1 140 140 ALA N N 15 125.403 0.1 . 1 . . . . . . . . 5497 1 1243 . 1 1 141 141 HIS H H 1 8.043 0.01 . 1 . . . . . . . . 5497 1 1244 . 1 1 141 141 HIS HA H 1 4.01 0.01 . 1 . . . . . . . . 5497 1 1245 . 1 1 141 141 HIS HB2 H 1 3.33 0.01 . 2 . . . . . . . . 5497 1 1246 . 1 1 141 141 HIS HB3 H 1 3.03 0.01 . 2 . . . . . . . . 5497 1 1247 . 1 1 141 141 HIS C C 13 177.090 0.1 . 1 . . . . . . . . 5497 1 1248 . 1 1 141 141 HIS CA C 13 59.98 0.1 . 1 . . . . . . . . 5497 1 1249 . 1 1 141 141 HIS CB C 13 30.60 0.1 . 1 . . . . . . . . 5497 1 1250 . 1 1 141 141 HIS N N 15 120.982 0.1 . 1 . . . . . . . . 5497 1 1251 . 1 1 142 142 LEU H H 1 8.185 0.01 . 1 . . . . . . . . 5497 1 1252 . 1 1 142 142 LEU HA H 1 3.47 0.01 . 1 . . . . . . . . 5497 1 1253 . 1 1 142 142 LEU HB2 H 1 1.78 0.01 . 2 . . . . . . . . 5497 1 1254 . 1 1 142 142 LEU HB3 H 1 1.26 0.01 . 2 . . . . . . . . 5497 1 1255 . 1 1 142 142 LEU HG H 1 1.29 0.01 . 1 . . . . . . . . 5497 1 1256 . 1 1 142 142 LEU HD11 H 1 0.63 0.01 . 2 . . . . . . . . 5497 1 1257 . 1 1 142 142 LEU HD12 H 1 0.63 0.01 . 2 . . . . . . . . 5497 1 1258 . 1 1 142 142 LEU HD13 H 1 0.63 0.01 . 2 . . . . . . . . 5497 1 1259 . 1 1 142 142 LEU HD21 H 1 0.52 0.01 . 2 . . . . . . . . 5497 1 1260 . 1 1 142 142 LEU HD22 H 1 0.52 0.01 . 2 . . . . . . . . 5497 1 1261 . 1 1 142 142 LEU HD23 H 1 0.52 0.01 . 2 . . . . . . . . 5497 1 1262 . 1 1 142 142 LEU C C 13 178.726 0.1 . 1 . . . . . . . . 5497 1 1263 . 1 1 142 142 LEU CA C 13 56.55 0.1 . 1 . . . . . . . . 5497 1 1264 . 1 1 142 142 LEU CB C 13 40.25 0.1 . 1 . . . . . . . . 5497 1 1265 . 1 1 142 142 LEU CG C 13 25.14 0.1 . 1 . . . . . . . . 5497 1 1266 . 1 1 142 142 LEU CD1 C 13 26.26 0.1 . 2 . . . . . . . . 5497 1 1267 . 1 1 142 142 LEU CD2 C 13 22.55 0.1 . 2 . . . . . . . . 5497 1 1268 . 1 1 142 142 LEU N N 15 117.799 0.1 . 1 . . . . . . . . 5497 1 1269 . 1 1 143 143 ARG H H 1 7.736 0.01 . 1 . . . . . . . . 5497 1 1270 . 1 1 143 143 ARG HA H 1 3.86 0.01 . 1 . . . . . . . . 5497 1 1271 . 1 1 143 143 ARG HB2 H 1 1.88 0.01 . 2 . . . . . . . . 5497 1 1272 . 1 1 143 143 ARG HG2 H 1 1.76 0.01 . 2 . . . . . . . . 5497 1 1273 . 1 1 143 143 ARG HG3 H 1 1.45 0.01 . 2 . . . . . . . . 5497 1 1274 . 1 1 143 143 ARG HD2 H 1 3.18 0.01 . 2 . . . . . . . . 5497 1 1275 . 1 1 143 143 ARG C C 13 177.665 0.1 . 1 . . . . . . . . 5497 1 1276 . 1 1 143 143 ARG CA C 13 58.58 0.1 . 1 . . . . . . . . 5497 1 1277 . 1 1 143 143 ARG CB C 13 29.63 0.1 . 1 . . . . . . . . 5497 1 1278 . 1 1 143 143 ARG CG C 13 26.38 0.1 . 1 . . . . . . . . 5497 1 1279 . 1 1 143 143 ARG CD C 13 42.90 0.1 . 1 . . . . . . . . 5497 1 1280 . 1 1 143 143 ARG N N 15 119.241 0.1 . 1 . . . . . . . . 5497 1 1281 . 1 1 144 144 ASP H H 1 7.882 0.01 . 1 . . . . . . . . 5497 1 1282 . 1 1 144 144 ASP HA H 1 4.53 0.01 . 1 . . . . . . . . 5497 1 1283 . 1 1 144 144 ASP HB2 H 1 2.55 0.01 . 2 . . . . . . . . 5497 1 1284 . 1 1 144 144 ASP C C 13 177.229 0.1 . 1 . . . . . . . . 5497 1 1285 . 1 1 144 144 ASP CA C 13 55.64 0.1 . 1 . . . . . . . . 5497 1 1286 . 1 1 144 144 ASP CB C 13 41.32 0.1 . 1 . . . . . . . . 5497 1 1287 . 1 1 144 144 ASP N N 15 116.073 0.1 . 1 . . . . . . . . 5497 1 1288 . 1 1 145 145 ARG H H 1 8.198 0.01 . 1 . . . . . . . . 5497 1 1289 . 1 1 145 145 ARG HA H 1 4.23 0.01 . 1 . . . . . . . . 5497 1 1290 . 1 1 145 145 ARG HB2 H 1 0.96 0.01 . 2 . . . . . . . . 5497 1 1291 . 1 1 145 145 ARG HB3 H 1 1.27 0.01 . 2 . . . . . . . . 5497 1 1292 . 1 1 145 145 ARG HG2 H 1 1.18 0.01 . 2 . . . . . . . . 5497 1 1293 . 1 1 145 145 ARG HD2 H 1 2.83 0.01 . 2 . . . . . . . . 5497 1 1294 . 1 1 145 145 ARG HD3 H 1 2.95 0.01 . 2 . . . . . . . . 5497 1 1295 . 1 1 145 145 ARG CA C 13 54.67 0.1 . 1 . . . . . . . . 5497 1 1296 . 1 1 145 145 ARG CB C 13 30.79 0.1 . 1 . . . . . . . . 5497 1 1297 . 1 1 145 145 ARG CD C 13 42.26 0.1 . 1 . . . . . . . . 5497 1 1298 . 1 1 145 145 ARG N N 15 115.647 0.1 . 1 . . . . . . . . 5497 1 1299 . 1 1 147 147 PRO HA H 1 4.38 0.01 . 1 . . . . . . . . 5497 1 1300 . 1 1 147 147 PRO HB2 H 1 2.28 0.01 . 2 . . . . . . . . 5497 1 1301 . 1 1 147 147 PRO HB3 H 1 1.90 0.01 . 2 . . . . . . . . 5497 1 1302 . 1 1 147 147 PRO HG2 H 1 2.01 0.01 . 2 . . . . . . . . 5497 1 1303 . 1 1 147 147 PRO HG3 H 1 1.99 0.01 . 2 . . . . . . . . 5497 1 1304 . 1 1 147 147 PRO HD2 H 1 3.77 0.01 . 2 . . . . . . . . 5497 1 1305 . 1 1 147 147 PRO HD3 H 1 3.65 0.01 . 2 . . . . . . . . 5497 1 1306 . 1 1 147 147 PRO CA C 13 62.52 0.1 . 1 . . . . . . . . 5497 1 1307 . 1 1 147 147 PRO CB C 13 31.43 0.1 . 1 . . . . . . . . 5497 1 1308 . 1 1 147 147 PRO CG C 13 26.85 0.1 . 1 . . . . . . . . 5497 1 1309 . 1 1 147 147 PRO CD C 13 50.07 0.1 . 1 . . . . . . . . 5497 1 stop_ save_