data_4787 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4787 _Entry.Title ; Assignment of 1H, 13C and 15N resonances of domain III of the ectodomain of apical membrane antigen 1 from Plasmodium falciparum ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2000-07-19 _Entry.Accession_date 2000-07-19 _Entry.Last_release_date 2001-02-14 _Entry.Original_release_date 2001-02-14 _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 Margie Nair . . . 4787 2 Anthony Hodder . N. . 4787 3 Mark Hinds . G. . 4787 4 Robin Anders . F. . 4787 5 Raymond Norton . S. . 4787 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4787 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 670 4787 '13C chemical shifts' 358 4787 '15N chemical shifts' 96 4787 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 . . 2001-02-14 2000-07-19 original author . 4787 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4787 _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: Assignment of 1H, 13C and 15N resonances of domain III of the ectodomain of apical membrane antigen 1 from Plasmodium falciparum ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 19 _Citation.Journal_issue 1 _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 85 _Citation.Page_last 86 _Citation.Year 2001 _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 Margie Nair . . . 4787 1 2 Anthony Hodder . N. . 4787 1 3 Mark Hinds . G. . 4787 1 4 Robin Anders . F. . 4787 1 5 Raymond Norton . S. . 4787 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'NMR resonance assignments' 4787 1 antigen 4787 1 malaria 4787 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4787 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8910611 _Citation.Full_citation ; Hodder AN, Crewther PE, Matthew ML, Reid GE, Moritz RL, Simpson RJ, Anders RF. The disulfide bond structure of Plasmodium apical membrane antigen-1. J Biol Chem. 1996 Nov 15;271(46):29446-52. PMID: 8910611; UI: 97067209 ; _Citation.Title 'The disulfide bond structure of Plasmodium apical membrane antigen-1.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 271 _Citation.Journal_issue 46 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0021-9258 _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 29446 _Citation.Page_last 29452 _Citation.Year 1996 _Citation.Details ; Apical membrane antigen-1 (AMA-1) of Plasmodium falciparum is one of the leading asexual blood stage antigens being considered for inclusion in a malaria vaccine. The ability of this molecule to induce a protective immune response has been shown to be dependent upon a conformation stabilized by disulfide bonds. In this study we have utilized the reversed-phase high performance liquid chromatography of dithiothreitol-reduced and nonreduced tryptic digests of Plasmodium chabaudi AMA-1 secreted from baculovirus-infected insect cells, in conjunction with N-terminal sequencing and electrospray-ionization mass spectrometry, to identify and assign disulfide-linked peptides. All 16 cysteine residues that are conserved in all known sequences of AMA-1 are incorporated into intramolecular disulfide bonds. Six of the eight bonds have been assigned unequivocally, whereas the two unassigned disulfide bonds connect two Cys-Xaa-Cys sequences separated by 14 residues. The eight disulfide bonds fall into three nonoverlapping groups that define three possible subdomains within the AMA-1 ectodomain. Although the pattern of disulfide bonds within subdomain III has not been fully elucidated, one of only two possible linkage patterns closely resembles the cystine knot motif found in growth factors. Sites of amino acid substitutions in AMA-1 that are well separated in the primary sequence are clustered by the disulfide bonds in subdomains II and III. These findings are consistent with the conclusion that these amino acid substitutions are defining conformational disulfide bond-dependent epitopes that are recognized by protective immune responses. ; 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 'A. N.' Hodder A. N. . 4787 2 2 'P. E.' Crewther P. E. . 4787 2 3 'M. L.' Matthew M. L. . 4787 2 4 'G. E.' Reid G. E. . 4787 2 5 'R. L.' Moritz R. L. . 4787 2 6 'R. J.' Simpson R. J. . 4787 2 7 'R. F.' Anders R. F. . 4787 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4787 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8589602 _Citation.Full_citation ; Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR. 1995 Sep;6(2):135-40. PMID: 8589602; UI: 96173087 ; _Citation.Title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 135 _Citation.Page_last 140 _Citation.Year 1995 _Citation.Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; 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 'D. S.' Wishart D. S. . 4787 3 2 'C. G.' Bigam C. G. . 4787 3 3 J. Yao J. . . 4787 3 4 F. Abildgaard F. . . 4787 3 5 'H. J.' Dyson H. J. . 4787 3 6 E. Oldfield E. . . 4787 3 7 'J. L.' Markley J. L. . 4787 3 8 'B. D.' Sykes B. D. . 4787 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4787 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Bartels, C., Xia ,T., Billeter, M., Guntert, P. and Wuthrich, K. (1995) J. Biomol. NMR, 6, 1-10. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_Pf_AMA_1 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_Pf_AMA_1 _Assembly.Entry_ID 4787 _Assembly.ID 1 _Assembly.Name 'Apical Membrane Antigen 1' _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 4787 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 'Pf AMA 1 domain III' 1 $Pf_AMA_1 . . . native . . . . . 4787 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 20 20 SG . 1 . 1 CYS 79 79 SG . . . . . . . . . . 4787 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Apical Membrane Antigen 1' system 4787 1 'Pf AMA 1' abbreviation 4787 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'parasite invasion of erythrocytes' 4787 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Pf_AMA_1 _Entity.Sf_category entity _Entity.Sf_framecode Pf_AMA_1 _Entity.Entry_ID 4787 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Apical membrane antigen 1' _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 ; MRGSHHHHHHGSEVENNFPC SLYKDEIMKEIERESKRIKL NDNDDEGNKKIIAPRIFISD DKDSLKCPCDPEMVSNSTCR FFVCKCVERRAEVTSNNEVV VKEEYKDEYADIPEHKPTYD KM ; _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 122 _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 14330 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; There are two unassigned disulphide linkages in the molecule. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-29 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 1HN6 . "Solution Structure Of Plasmodium Falciparum Apical Membrane Antigen 1 (Residues 436-545)" . . . . . 90.16 110 100.00 100.00 1.07e-71 . . . . 4787 1 2 no DBJ BAM85373 . "apical membrane antigen 1 [Plasmodium falciparum]" . . . . . 92.62 622 97.35 97.35 3.67e-67 . . . . 4787 1 3 no DBJ BAM85381 . "apical membrane antigen 1 [Plasmodium falciparum]" . . . . . 92.62 622 97.35 98.23 1.29e-67 . . . . 4787 1 4 no DBJ BAM85383 . "apical membrane antigen 1 [Plasmodium falciparum]" . . . . . 92.62 622 98.23 98.23 3.40e-68 . . . . 4787 1 5 no DBJ BAM85388 . "apical membrane antigen 1 [Plasmodium falciparum]" . . . . . 92.62 622 97.35 97.35 3.52e-67 . . . . 4787 1 6 no DBJ BAM85400 . "apical membrane antigen 1 [Plasmodium falciparum]" . . . . . 92.62 622 97.35 97.35 3.52e-67 . . . . 4787 1 7 no EMBL CAB97182 . "apical membrane antigen 1 [Plasmodium falciparum]" . . . . . 83.61 526 97.06 97.06 6.26e-59 . . . . 4787 1 8 no EMBL CAB97190 . "apical membrane antigen 1 [Plasmodium falciparum]" . . . . . 82.79 526 97.03 98.02 2.69e-58 . . . . 4787 1 9 no EMBL CAB97197 . "apical membrane antigen 1 [Plasmodium falciparum]" . . . . . 83.61 526 97.06 97.06 3.50e-58 . . . . 4787 1 10 no EMBL CAC34760 . "Apical Membrane Antigen 1 [Plasmodium falciparum]" . . . . . 92.62 437 97.35 97.35 8.09e-69 . . . . 4787 1 11 no EMBL CAC34761 . "Apical Membrane Antigen 1 [Plasmodium falciparum]" . . . . . 92.62 437 97.35 97.35 8.01e-69 . . . . 4787 1 12 no GB AAA29476 . "apical membrane antigen 1, partial [Plasmodium falciparum]" . . . . . 92.62 463 97.35 98.23 1.08e-68 . . . . 4787 1 13 no GB AAB36701 . "apical membrane antigen 1 [Plasmodium falciparum]" . . . . . 92.62 622 98.23 98.23 4.37e-68 . . . . 4787 1 14 no GB AAC47104 . "apical membrane antigen-1, partial [Plasmodium falciparum]" . . . . . 92.62 596 98.23 98.23 2.64e-68 . . . . 4787 1 15 no GB AAC47105 . "apical membrane antigen-1, partial [Plasmodium falciparum]" . . . . . 92.62 592 97.35 97.35 1.32e-67 . . . . 4787 1 16 no GB AAG50119 . "apical membrane antigen-1 [Plasmodium falciparum]" . . . . . 92.62 622 98.23 99.12 1.13e-68 . . . . 4787 1 17 no REF XP_001348015 . "apical membrane antigen 1, AMA1 [Plasmodium falciparum 3D7]" . . . . . 92.62 622 98.23 98.23 4.37e-68 . . . . 4787 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Apical membrane antigen 1' common 4787 1 'Pf AMA 1' abbreviation 4787 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 . 4787 1 2 -2 ARG . 4787 1 3 -3 GLY . 4787 1 4 -4 SER . 4787 1 5 -5 HIS . 4787 1 6 -6 HIS . 4787 1 7 -7 HIS . 4787 1 8 -8 HIS . 4787 1 9 -9 HIS . 4787 1 10 -10 HIS . 4787 1 11 -11 GLY . 4787 1 12 -12 SER . 4787 1 13 436 GLU . 4787 1 14 437 VAL . 4787 1 15 438 GLU . 4787 1 16 439 ASN . 4787 1 17 440 ASN . 4787 1 18 441 PHE . 4787 1 19 442 PRO . 4787 1 20 443 CYS . 4787 1 21 444 SER . 4787 1 22 445 LEU . 4787 1 23 446 TYR . 4787 1 24 447 LYS . 4787 1 25 448 ASP . 4787 1 26 449 GLU . 4787 1 27 450 ILE . 4787 1 28 451 MET . 4787 1 29 452 LYS . 4787 1 30 453 GLU . 4787 1 31 454 ILE . 4787 1 32 455 GLU . 4787 1 33 456 ARG . 4787 1 34 457 GLU . 4787 1 35 458 SER . 4787 1 36 459 LYS . 4787 1 37 460 ARG . 4787 1 38 461 ILE . 4787 1 39 462 LYS . 4787 1 40 463 LEU . 4787 1 41 464 ASN . 4787 1 42 465 ASP . 4787 1 43 466 ASN . 4787 1 44 467 ASP . 4787 1 45 468 ASP . 4787 1 46 469 GLU . 4787 1 47 470 GLY . 4787 1 48 471 ASN . 4787 1 49 472 LYS . 4787 1 50 473 LYS . 4787 1 51 474 ILE . 4787 1 52 475 ILE . 4787 1 53 476 ALA . 4787 1 54 477 PRO . 4787 1 55 478 ARG . 4787 1 56 479 ILE . 4787 1 57 480 PHE . 4787 1 58 481 ILE . 4787 1 59 482 SER . 4787 1 60 483 ASP . 4787 1 61 484 ASP . 4787 1 62 485 LYS . 4787 1 63 486 ASP . 4787 1 64 487 SER . 4787 1 65 488 LEU . 4787 1 66 489 LYS . 4787 1 67 490 CYS . 4787 1 68 491 PRO . 4787 1 69 492 CYS . 4787 1 70 493 ASP . 4787 1 71 494 PRO . 4787 1 72 495 GLU . 4787 1 73 496 MET . 4787 1 74 497 VAL . 4787 1 75 498 SER . 4787 1 76 499 ASN . 4787 1 77 500 SER . 4787 1 78 501 THR . 4787 1 79 502 CYS . 4787 1 80 503 ARG . 4787 1 81 504 PHE . 4787 1 82 505 PHE . 4787 1 83 506 VAL . 4787 1 84 507 CYS . 4787 1 85 508 LYS . 4787 1 86 509 CYS . 4787 1 87 510 VAL . 4787 1 88 511 GLU . 4787 1 89 512 ARG . 4787 1 90 513 ARG . 4787 1 91 514 ALA . 4787 1 92 515 GLU . 4787 1 93 516 VAL . 4787 1 94 517 THR . 4787 1 95 518 SER . 4787 1 96 519 ASN . 4787 1 97 520 ASN . 4787 1 98 521 GLU . 4787 1 99 522 VAL . 4787 1 100 523 VAL . 4787 1 101 524 VAL . 4787 1 102 525 LYS . 4787 1 103 526 GLU . 4787 1 104 527 GLU . 4787 1 105 528 TYR . 4787 1 106 529 LYS . 4787 1 107 530 ASP . 4787 1 108 531 GLU . 4787 1 109 532 TYR . 4787 1 110 533 ALA . 4787 1 111 534 ASP . 4787 1 112 535 ILE . 4787 1 113 536 PRO . 4787 1 114 537 GLU . 4787 1 115 538 HIS . 4787 1 116 539 LYS . 4787 1 117 540 PRO . 4787 1 118 541 THR . 4787 1 119 542 TYR . 4787 1 120 543 ASP . 4787 1 121 544 LYS . 4787 1 122 545 MET . 4787 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 4787 1 . ARG 2 2 4787 1 . GLY 3 3 4787 1 . SER 4 4 4787 1 . HIS 5 5 4787 1 . HIS 6 6 4787 1 . HIS 7 7 4787 1 . HIS 8 8 4787 1 . HIS 9 9 4787 1 . HIS 10 10 4787 1 . GLY 11 11 4787 1 . SER 12 12 4787 1 . GLU 13 13 4787 1 . VAL 14 14 4787 1 . GLU 15 15 4787 1 . ASN 16 16 4787 1 . ASN 17 17 4787 1 . PHE 18 18 4787 1 . PRO 19 19 4787 1 . CYS 20 20 4787 1 . SER 21 21 4787 1 . LEU 22 22 4787 1 . TYR 23 23 4787 1 . LYS 24 24 4787 1 . ASP 25 25 4787 1 . GLU 26 26 4787 1 . ILE 27 27 4787 1 . MET 28 28 4787 1 . LYS 29 29 4787 1 . GLU 30 30 4787 1 . ILE 31 31 4787 1 . GLU 32 32 4787 1 . ARG 33 33 4787 1 . GLU 34 34 4787 1 . SER 35 35 4787 1 . LYS 36 36 4787 1 . ARG 37 37 4787 1 . ILE 38 38 4787 1 . LYS 39 39 4787 1 . LEU 40 40 4787 1 . ASN 41 41 4787 1 . ASP 42 42 4787 1 . ASN 43 43 4787 1 . ASP 44 44 4787 1 . ASP 45 45 4787 1 . GLU 46 46 4787 1 . GLY 47 47 4787 1 . ASN 48 48 4787 1 . LYS 49 49 4787 1 . LYS 50 50 4787 1 . ILE 51 51 4787 1 . ILE 52 52 4787 1 . ALA 53 53 4787 1 . PRO 54 54 4787 1 . ARG 55 55 4787 1 . ILE 56 56 4787 1 . PHE 57 57 4787 1 . ILE 58 58 4787 1 . SER 59 59 4787 1 . ASP 60 60 4787 1 . ASP 61 61 4787 1 . LYS 62 62 4787 1 . ASP 63 63 4787 1 . SER 64 64 4787 1 . LEU 65 65 4787 1 . LYS 66 66 4787 1 . CYS 67 67 4787 1 . PRO 68 68 4787 1 . CYS 69 69 4787 1 . ASP 70 70 4787 1 . PRO 71 71 4787 1 . GLU 72 72 4787 1 . MET 73 73 4787 1 . VAL 74 74 4787 1 . SER 75 75 4787 1 . ASN 76 76 4787 1 . SER 77 77 4787 1 . THR 78 78 4787 1 . CYS 79 79 4787 1 . ARG 80 80 4787 1 . PHE 81 81 4787 1 . PHE 82 82 4787 1 . VAL 83 83 4787 1 . CYS 84 84 4787 1 . LYS 85 85 4787 1 . CYS 86 86 4787 1 . VAL 87 87 4787 1 . GLU 88 88 4787 1 . ARG 89 89 4787 1 . ARG 90 90 4787 1 . ALA 91 91 4787 1 . GLU 92 92 4787 1 . VAL 93 93 4787 1 . THR 94 94 4787 1 . SER 95 95 4787 1 . ASN 96 96 4787 1 . ASN 97 97 4787 1 . GLU 98 98 4787 1 . VAL 99 99 4787 1 . VAL 100 100 4787 1 . VAL 101 101 4787 1 . LYS 102 102 4787 1 . GLU 103 103 4787 1 . GLU 104 104 4787 1 . TYR 105 105 4787 1 . LYS 106 106 4787 1 . ASP 107 107 4787 1 . GLU 108 108 4787 1 . TYR 109 109 4787 1 . ALA 110 110 4787 1 . ASP 111 111 4787 1 . ILE 112 112 4787 1 . PRO 113 113 4787 1 . GLU 114 114 4787 1 . HIS 115 115 4787 1 . LYS 116 116 4787 1 . PRO 117 117 4787 1 . THR 118 118 4787 1 . TYR 119 119 4787 1 . ASP 120 120 4787 1 . LYS 121 121 4787 1 . MET 122 122 4787 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 4787 _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 $Pf_AMA_1 . 5833 organism . 'Plasmodium falciparum' 'malaria parasite' . . Eukaryota . Plasmodium falciparum . . . . . . . . . . . . 'Type I membrane Protein' . . . . . . . . 4787 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 4787 _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 $Pf_AMA_1 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . . . . . . . . . . . . . . . 4787 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N_sample _Sample.Sf_category sample _Sample.Sf_framecode 15N_sample _Sample.Entry_ID 4787 _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 'Apical membrane antigen 1' '[U-90% 15N]' . . 1 $Pf_AMA_1 . . . 0.5 1 mM . . . . 4787 1 stop_ save_ save_13C_sample _Sample.Sf_category sample _Sample.Sf_framecode 13C_sample _Sample.Entry_ID 4787 _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 'Apical membrane antigen 1' '[U-95% 13C[' . . 1 $Pf_AMA_1 . . . 0.5 1 mM . . . . 4787 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_set_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_set_1 _Sample_condition_list.Entry_ID 4787 _Sample_condition_list.ID 1 _Sample_condition_list.Details . 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 3.4 0.1 n/a 4787 1 temperature 303 0.2 K 4787 1 stop_ save_ save_sample_conditions_set_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_set_2 _Sample_condition_list.Entry_ID 4787 _Sample_condition_list.ID 2 _Sample_condition_list.Details . 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 3.4 0.1 n/a 4787 2 temperature 283 0.2 K 4787 2 stop_ save_ save_sample_conditions_set_3 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_set_3 _Sample_condition_list.Entry_ID 4787 _Sample_condition_list.ID 3 _Sample_condition_list.Details . 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 2.8 0.1 n/a 4787 3 temperature 303 0.2 K 4787 3 stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Software.Sf_category software _Software.Sf_framecode UXNMR _Software.Entry_ID 4787 _Software.ID 1 _Software.Name UXNMR _Software.Version 1.3 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Data processing' 4787 1 stop_ save_ save_XEASY _Software.Sf_category software _Software.Sf_framecode XEASY _Software.Entry_ID 4787 _Software.ID 2 _Software.Name XEASY _Software.Version 1.3.13 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Peak assignment and analysis' 4787 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $ref_3 4787 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 4787 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4787 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4787 _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_spectrometer_1 Bruker DRX . 600 . . . 4787 1 2 NMR_spectrometer_2 Bruker AMX . 500 . . . 4787 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 4787 _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 '3D 1H-1H-15N NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4787 1 2 '3D 1H-1H-13C NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4787 1 3 '3D 1H-1H-15N TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4787 1 4 '3D HNCA' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4787 1 5 '3D HNCO' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4787 1 6 '3D CBCA(CO)NH' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4787 1 7 '3D CCCONH' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4787 1 8 '3D 1H-13C-1H HCCH-TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4787 1 9 '3D HNHA' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4787 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4787 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '3D 1H-1H-15N NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4787 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '3D 1H-1H-13C NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4787 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '3D 1H-1H-15N TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4787 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '3D HNCA' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4787 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '3D HNCO' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 4787 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name '3D CBCA(CO)NH' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 4787 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name '3D CCCONH' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 4787 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name '3D 1H-13C-1H HCCH-TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 4787 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name '3D HNHA' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_one _Chem_shift_reference.Entry_ID 4787 _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 . . . . . . . . . . 4787 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4787 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4787 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 4787 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_set_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_one _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 . _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 . . 1 $15N_sample . 4787 1 . . 2 $13C_sample . 4787 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 13 13 GLU N N 15 122.8 0.1 . 1 . . . . . . . . 4787 1 2 . 1 1 13 13 GLU H H 1 8.64 0.02 . 1 . . . . . . . . 4787 1 3 . 1 1 13 13 GLU CA C 13 56.2 0.1 . 1 . . . . . . . . 4787 1 4 . 1 1 13 13 GLU HA H 1 4.54 0.02 . 1 . . . . . . . . 4787 1 5 . 1 1 13 13 GLU CB C 13 29.6 0.1 . 1 . . . . . . . . 4787 1 6 . 1 1 13 13 GLU HB2 H 1 2.06 0.02 . 1 . . . . . . . . 4787 1 7 . 1 1 13 13 GLU HB3 H 1 2.06 0.02 . 1 . . . . . . . . 4787 1 8 . 1 1 13 13 GLU CG C 13 32.9 0.1 . 1 . . . . . . . . 4787 1 9 . 1 1 13 13 GLU HG2 H 1 2.48 0.02 . 1 . . . . . . . . 4787 1 10 . 1 1 13 13 GLU HG3 H 1 2.48 0.02 . 1 . . . . . . . . 4787 1 11 . 1 1 13 13 GLU C C 13 176.0 0.1 . 1 . . . . . . . . 4787 1 12 . 1 1 14 14 VAL N N 15 121.8 0.1 . 1 . . . . . . . . 4787 1 13 . 1 1 14 14 VAL H H 1 8.20 0.02 . 1 . . . . . . . . 4787 1 14 . 1 1 14 14 VAL CA C 13 62.5 0.1 . 1 . . . . . . . . 4787 1 15 . 1 1 14 14 VAL HA H 1 4.17 0.02 . 1 . . . . . . . . 4787 1 16 . 1 1 14 14 VAL CB C 13 33.1 0.1 . 1 . . . . . . . . 4787 1 17 . 1 1 14 14 VAL HB H 1 2.13 0.02 . 1 . . . . . . . . 4787 1 18 . 1 1 14 14 VAL HG11 H 1 1.02 0.02 . 2 . . . . . . . . 4787 1 19 . 1 1 14 14 VAL HG12 H 1 1.02 0.02 . 2 . . . . . . . . 4787 1 20 . 1 1 14 14 VAL HG13 H 1 1.02 0.02 . 2 . . . . . . . . 4787 1 21 . 1 1 14 14 VAL HG21 H 1 1.00 0.02 . 2 . . . . . . . . 4787 1 22 . 1 1 14 14 VAL HG22 H 1 1.00 0.02 . 2 . . . . . . . . 4787 1 23 . 1 1 14 14 VAL HG23 H 1 1.00 0.02 . 2 . . . . . . . . 4787 1 24 . 1 1 14 14 VAL CG1 C 13 20.2 0.1 . 1 . . . . . . . . 4787 1 25 . 1 1 14 14 VAL C C 13 176.1 0.1 . 1 . . . . . . . . 4787 1 26 . 1 1 15 15 GLU N N 15 124.1 0.1 . 1 . . . . . . . . 4787 1 27 . 1 1 15 15 GLU H H 1 8.49 0.02 . 1 . . . . . . . . 4787 1 28 . 1 1 15 15 GLU CA C 13 55.8 0.1 . 1 . . . . . . . . 4787 1 29 . 1 1 15 15 GLU HA H 1 4.43 0.02 . 1 . . . . . . . . 4787 1 30 . 1 1 15 15 GLU CB C 13 29.7 0.1 . 1 . . . . . . . . 4787 1 31 . 1 1 15 15 GLU HB2 H 1 2.08 0.02 . 1 . . . . . . . . 4787 1 32 . 1 1 15 15 GLU HB3 H 1 2.08 0.02 . 1 . . . . . . . . 4787 1 33 . 1 1 15 15 GLU CG C 13 33.2 0.1 . 1 . . . . . . . . 4787 1 34 . 1 1 15 15 GLU HG2 H 1 2.46 0.02 . 1 . . . . . . . . 4787 1 35 . 1 1 15 15 GLU HG3 H 1 2.46 0.02 . 1 . . . . . . . . 4787 1 36 . 1 1 15 15 GLU C C 13 175.7 0.1 . 1 . . . . . . . . 4787 1 37 . 1 1 16 16 ASN N N 15 120.1 0.1 . 1 . . . . . . . . 4787 1 38 . 1 1 16 16 ASN H H 1 8.47 0.02 . 1 . . . . . . . . 4787 1 39 . 1 1 16 16 ASN CA C 13 53.2 0.1 . 1 . . . . . . . . 4787 1 40 . 1 1 16 16 ASN HA H 1 4.77 0.02 . 1 . . . . . . . . 4787 1 41 . 1 1 16 16 ASN CB C 13 39.3 0.1 . 1 . . . . . . . . 4787 1 42 . 1 1 16 16 ASN HB2 H 1 2.81 0.02 . 1 . . . . . . . . 4787 1 43 . 1 1 16 16 ASN HB3 H 1 2.81 0.02 . 1 . . . . . . . . 4787 1 44 . 1 1 16 16 ASN HD21 H 1 6.89 0.02 . 2 . . . . . . . . 4787 1 45 . 1 1 16 16 ASN HD22 H 1 7.62 0.02 . 2 . . . . . . . . 4787 1 46 . 1 1 16 16 ASN C C 13 175.0 0.1 . 1 . . . . . . . . 4787 1 47 . 1 1 17 17 ASN N N 15 118.9 0.1 . 1 . . . . . . . . 4787 1 48 . 1 1 17 17 ASN H H 1 8.49 0.02 . 1 . . . . . . . . 4787 1 49 . 1 1 17 17 ASN CA C 13 53.7 0.1 . 1 . . . . . . . . 4787 1 50 . 1 1 17 17 ASN HA H 1 4.78 0.02 . 1 . . . . . . . . 4787 1 51 . 1 1 17 17 ASN CB C 13 39.1 0.1 . 1 . . . . . . . . 4787 1 52 . 1 1 17 17 ASN HB2 H 1 2.87 0.02 . 1 . . . . . . . . 4787 1 53 . 1 1 17 17 ASN HB3 H 1 2.87 0.02 . 1 . . . . . . . . 4787 1 54 . 1 1 17 17 ASN HD21 H 1 6.97 0.02 . 2 . . . . . . . . 4787 1 55 . 1 1 17 17 ASN HD22 H 1 7.62 0.02 . 2 . . . . . . . . 4787 1 56 . 1 1 17 17 ASN C C 13 175.5 0.1 . 1 . . . . . . . . 4787 1 57 . 1 1 18 18 PHE N N 15 120.7 0.1 . 1 . . . . . . . . 4787 1 58 . 1 1 18 18 PHE H H 1 8.25 0.02 . 1 . . . . . . . . 4787 1 59 . 1 1 18 18 PHE CA C 13 56.6 0.1 . 1 . . . . . . . . 4787 1 60 . 1 1 18 18 PHE HA H 1 4.77 0.02 . 1 . . . . . . . . 4787 1 61 . 1 1 18 18 PHE CB C 13 38.7 0.1 . 1 . . . . . . . . 4787 1 62 . 1 1 18 18 PHE HB2 H 1 3.05 0.02 . 1 . . . . . . . . 4787 1 63 . 1 1 18 18 PHE HB3 H 1 3.05 0.02 . 1 . . . . . . . . 4787 1 64 . 1 1 18 18 PHE HE1 H 1 7.17 0.02 . 1 . . . . . . . . 4787 1 65 . 1 1 18 18 PHE HE2 H 1 7.17 0.02 . 1 . . . . . . . . 4787 1 66 . 1 1 19 19 PRO CA C 13 63.9 0.1 . 1 . . . . . . . . 4787 1 67 . 1 1 19 19 PRO HA H 1 4.59 0.02 . 1 . . . . . . . . 4787 1 68 . 1 1 19 19 PRO CB C 13 31.8 0.1 . 1 . . . . . . . . 4787 1 69 . 1 1 19 19 PRO HB2 H 1 2.42 0.02 . 1 . . . . . . . . 4787 1 70 . 1 1 19 19 PRO HB3 H 1 2.42 0.02 . 1 . . . . . . . . 4787 1 71 . 1 1 19 19 PRO HG2 H 1 2.12 0.02 . 1 . . . . . . . . 4787 1 72 . 1 1 19 19 PRO HG3 H 1 2.12 0.02 . 1 . . . . . . . . 4787 1 73 . 1 1 19 19 PRO HD2 H 1 4.04 0.02 . 2 . . . . . . . . 4787 1 74 . 1 1 19 19 PRO HD3 H 1 3.87 0.02 . 2 . . . . . . . . 4787 1 75 . 1 1 19 19 PRO C C 13 178.4 0.1 . 1 . . . . . . . . 4787 1 76 . 1 1 20 20 CYS N N 15 118.9 0.1 . 1 . . . . . . . . 4787 1 77 . 1 1 20 20 CYS H H 1 8.81 0.02 . 1 . . . . . . . . 4787 1 78 . 1 1 20 20 CYS CA C 13 56.8 0.1 . 1 . . . . . . . . 4787 1 79 . 1 1 20 20 CYS HA H 1 5.00 0.02 . 1 . . . . . . . . 4787 1 80 . 1 1 20 20 CYS CB C 13 38.1 0.1 . 1 . . . . . . . . 4787 1 81 . 1 1 20 20 CYS HB2 H 1 3.43 0.02 . 2 . . . . . . . . 4787 1 82 . 1 1 20 20 CYS HB3 H 1 3.25 0.02 . 2 . . . . . . . . 4787 1 83 . 1 1 20 20 CYS C C 13 176.7 0.1 . 1 . . . . . . . . 4787 1 84 . 1 1 21 21 SER N N 15 116.7 0.1 . 1 . . . . . . . . 4787 1 85 . 1 1 21 21 SER H H 1 8.50 0.02 . 1 . . . . . . . . 4787 1 86 . 1 1 21 21 SER CA C 13 61.7 0.1 . 1 . . . . . . . . 4787 1 87 . 1 1 21 21 SER HA H 1 4.16 0.02 . 1 . . . . . . . . 4787 1 88 . 1 1 21 21 SER CB C 13 61.6 0.1 . 1 . . . . . . . . 4787 1 89 . 1 1 21 21 SER HB2 H 1 4.09 0.02 . 1 . . . . . . . . 4787 1 90 . 1 1 21 21 SER HB3 H 1 4.09 0.02 . 1 . . . . . . . . 4787 1 91 . 1 1 21 21 SER C C 13 176.3 0.1 . 1 . . . . . . . . 4787 1 92 . 1 1 22 22 LEU N N 15 123.1 0.1 . 1 . . . . . . . . 4787 1 93 . 1 1 22 22 LEU H H 1 7.63 0.02 . 1 . . . . . . . . 4787 1 94 . 1 1 22 22 LEU CA C 13 57.7 0.1 . 1 . . . . . . . . 4787 1 95 . 1 1 22 22 LEU HA H 1 4.28 0.02 . 1 . . . . . . . . 4787 1 96 . 1 1 22 22 LEU CB C 13 41.6 0.1 . 1 . . . . . . . . 4787 1 97 . 1 1 22 22 LEU HB2 H 1 1.69 0.02 . 1 . . . . . . . . 4787 1 98 . 1 1 22 22 LEU HB3 H 1 1.69 0.02 . 1 . . . . . . . . 4787 1 99 . 1 1 22 22 LEU CG C 13 26.4 0.1 . 1 . . . . . . . . 4787 1 100 . 1 1 22 22 LEU HG H 1 1.64 0.02 . 1 . . . . . . . . 4787 1 101 . 1 1 22 22 LEU HD11 H 1 0.91 0.02 . 2 . . . . . . . . 4787 1 102 . 1 1 22 22 LEU HD12 H 1 0.91 0.02 . 2 . . . . . . . . 4787 1 103 . 1 1 22 22 LEU HD13 H 1 0.91 0.02 . 2 . . . . . . . . 4787 1 104 . 1 1 22 22 LEU HD21 H 1 0.89 0.02 . 2 . . . . . . . . 4787 1 105 . 1 1 22 22 LEU HD22 H 1 0.89 0.02 . 2 . . . . . . . . 4787 1 106 . 1 1 22 22 LEU HD23 H 1 0.89 0.02 . 2 . . . . . . . . 4787 1 107 . 1 1 22 22 LEU CD1 C 13 23.9 0.1 . 1 . . . . . . . . 4787 1 108 . 1 1 22 22 LEU CD2 C 13 23.6 0.1 . 1 . . . . . . . . 4787 1 109 . 1 1 22 22 LEU C C 13 179.4 0.1 . 1 . . . . . . . . 4787 1 110 . 1 1 23 23 TYR N N 15 120.7 0.1 . 1 . . . . . . . . 4787 1 111 . 1 1 23 23 TYR H H 1 7.69 0.02 . 1 . . . . . . . . 4787 1 112 . 1 1 23 23 TYR CA C 13 60.1 0.1 . 1 . . . . . . . . 4787 1 113 . 1 1 23 23 TYR HA H 1 4.55 0.02 . 1 . . . . . . . . 4787 1 114 . 1 1 23 23 TYR CB C 13 38.7 0.1 . 1 . . . . . . . . 4787 1 115 . 1 1 23 23 TYR HB2 H 1 3.31 0.02 . 1 . . . . . . . . 4787 1 116 . 1 1 23 23 TYR HB3 H 1 3.31 0.02 . 1 . . . . . . . . 4787 1 117 . 1 1 23 23 TYR HD1 H 1 7.26 0.02 . 1 . . . . . . . . 4787 1 118 . 1 1 23 23 TYR HD2 H 1 7.26 0.02 . 1 . . . . . . . . 4787 1 119 . 1 1 23 23 TYR HE1 H 1 6.72 0.02 . 1 . . . . . . . . 4787 1 120 . 1 1 23 23 TYR HE2 H 1 6.72 0.02 . 1 . . . . . . . . 4787 1 121 . 1 1 23 23 TYR C C 13 177.3 0.1 . 1 . . . . . . . . 4787 1 122 . 1 1 24 24 LYS N N 15 118.8 0.1 . 1 . . . . . . . . 4787 1 123 . 1 1 24 24 LYS H H 1 8.13 0.02 . 1 . . . . . . . . 4787 1 124 . 1 1 24 24 LYS CA C 13 60.0 0.1 . 1 . . . . . . . . 4787 1 125 . 1 1 24 24 LYS HA H 1 4.17 0.02 . 1 . . . . . . . . 4787 1 126 . 1 1 24 24 LYS CB C 13 32.3 0.1 . 1 . . . . . . . . 4787 1 127 . 1 1 24 24 LYS HB2 H 1 1.65 0.02 . 1 . . . . . . . . 4787 1 128 . 1 1 24 24 LYS HB3 H 1 1.65 0.02 . 1 . . . . . . . . 4787 1 129 . 1 1 24 24 LYS HG2 H 1 0.64 0.02 . 1 . . . . . . . . 4787 1 130 . 1 1 24 24 LYS HG3 H 1 0.64 0.02 . 1 . . . . . . . . 4787 1 131 . 1 1 24 24 LYS HE2 H 1 3.22 0.02 . 1 . . . . . . . . 4787 1 132 . 1 1 24 24 LYS HE3 H 1 3.22 0.02 . 1 . . . . . . . . 4787 1 133 . 1 1 24 24 LYS C C 13 177.9 0.1 . 1 . . . . . . . . 4787 1 134 . 1 1 25 25 ASP N N 15 116.9 0.1 . 1 . . . . . . . . 4787 1 135 . 1 1 25 25 ASP H H 1 7.78 0.02 . 1 . . . . . . . . 4787 1 136 . 1 1 25 25 ASP CA C 13 56.8 0.1 . 1 . . . . . . . . 4787 1 137 . 1 1 25 25 ASP HA H 1 4.34 0.02 . 1 . . . . . . . . 4787 1 138 . 1 1 25 25 ASP CB C 13 39.5 0.1 . 1 . . . . . . . . 4787 1 139 . 1 1 25 25 ASP HB2 H 1 3.00 0.02 . 2 . . . . . . . . 4787 1 140 . 1 1 25 25 ASP HB3 H 1 2.82 0.02 . 2 . . . . . . . . 4787 1 141 . 1 1 25 25 ASP C C 13 177.0 0.1 . 1 . . . . . . . . 4787 1 142 . 1 1 26 26 GLU N N 15 120.2 0.1 . 1 . . . . . . . . 4787 1 143 . 1 1 26 26 GLU H H 1 8.01 0.02 . 1 . . . . . . . . 4787 1 144 . 1 1 26 26 GLU CA C 13 58.9 0.1 . 1 . . . . . . . . 4787 1 145 . 1 1 26 26 GLU HA H 1 4.36 0.02 . 1 . . . . . . . . 4787 1 146 . 1 1 26 26 GLU CB C 13 29.8 0.1 . 1 . . . . . . . . 4787 1 147 . 1 1 26 26 GLU HB2 H 1 1.92 0.02 . 2 . . . . . . . . 4787 1 148 . 1 1 26 26 GLU HB3 H 1 1.75 0.02 . 2 . . . . . . . . 4787 1 149 . 1 1 26 26 GLU CG C 13 33.4 0.1 . 1 . . . . . . . . 4787 1 150 . 1 1 26 26 GLU HG2 H 1 2.27 0.02 . 2 . . . . . . . . 4787 1 151 . 1 1 26 26 GLU HG3 H 1 2.39 0.02 . 2 . . . . . . . . 4787 1 152 . 1 1 26 26 GLU C C 13 176.9 0.1 . 1 . . . . . . . . 4787 1 153 . 1 1 27 27 ILE N N 15 120.5 0.1 . 1 . . . . . . . . 4787 1 154 . 1 1 27 27 ILE H H 1 8.42 0.02 . 1 . . . . . . . . 4787 1 155 . 1 1 27 27 ILE CA C 13 58.8 0.1 . 1 . . . . . . . . 4787 1 156 . 1 1 27 27 ILE HB H 1 1.97 0.02 . 1 . . . . . . . . 4787 1 157 . 1 1 27 27 ILE HG21 H 1 0.78 0.02 . 1 . . . . . . . . 4787 1 158 . 1 1 27 27 ILE HG22 H 1 0.78 0.02 . 1 . . . . . . . . 4787 1 159 . 1 1 27 27 ILE HG23 H 1 0.78 0.02 . 1 . . . . . . . . 4787 1 160 . 1 1 27 27 ILE HG12 H 1 1.20 0.02 . 2 . . . . . . . . 4787 1 161 . 1 1 27 27 ILE HD11 H 1 0.95 0.02 . 1 . . . . . . . . 4787 1 162 . 1 1 27 27 ILE HD12 H 1 0.95 0.02 . 1 . . . . . . . . 4787 1 163 . 1 1 27 27 ILE HD13 H 1 0.95 0.02 . 1 . . . . . . . . 4787 1 164 . 1 1 27 27 ILE C C 13 179.4 0.1 . 1 . . . . . . . . 4787 1 165 . 1 1 28 28 MET N N 15 120.1 0.1 . 1 . . . . . . . . 4787 1 166 . 1 1 28 28 MET H H 1 7.90 0.02 . 1 . . . . . . . . 4787 1 167 . 1 1 28 28 MET CA C 13 59.2 0.1 . 1 . . . . . . . . 4787 1 168 . 1 1 28 28 MET HA H 1 4.15 0.02 . 1 . . . . . . . . 4787 1 169 . 1 1 28 28 MET CB C 13 32.4 0.1 . 1 . . . . . . . . 4787 1 170 . 1 1 28 28 MET HB2 H 1 2.29 0.02 . 1 . . . . . . . . 4787 1 171 . 1 1 28 28 MET HB3 H 1 2.29 0.02 . 1 . . . . . . . . 4787 1 172 . 1 1 28 28 MET CG C 13 31.3 0.1 . 1 . . . . . . . . 4787 1 173 . 1 1 28 28 MET HG2 H 1 2.59 0.02 . 1 . . . . . . . . 4787 1 174 . 1 1 28 28 MET HG3 H 1 2.59 0.02 . 1 . . . . . . . . 4787 1 175 . 1 1 28 28 MET C C 13 178.5 0.1 . 1 . . . . . . . . 4787 1 176 . 1 1 29 29 LYS N N 15 118.5 0.1 . 1 . . . . . . . . 4787 1 177 . 1 1 29 29 LYS H H 1 8.04 0.02 . 1 . . . . . . . . 4787 1 178 . 1 1 29 29 LYS CA C 13 59.6 0.1 . 1 . . . . . . . . 4787 1 179 . 1 1 29 29 LYS HA H 1 4.09 0.02 . 1 . . . . . . . . 4787 1 180 . 1 1 29 29 LYS CB C 13 32.4 0.1 . 1 . . . . . . . . 4787 1 181 . 1 1 29 29 LYS HB2 H 1 2.22 0.02 . 2 . . . . . . . . 4787 1 182 . 1 1 29 29 LYS HB3 H 1 1.98 0.02 . 2 . . . . . . . . 4787 1 183 . 1 1 29 29 LYS HG2 H 1 1.51 0.02 . 1 . . . . . . . . 4787 1 184 . 1 1 29 29 LYS HG3 H 1 1.51 0.02 . 1 . . . . . . . . 4787 1 185 . 1 1 29 29 LYS CD C 13 29.4 0.1 . 1 . . . . . . . . 4787 1 186 . 1 1 29 29 LYS HD2 H 1 1.68 0.02 . 1 . . . . . . . . 4787 1 187 . 1 1 29 29 LYS HD3 H 1 1.68 0.02 . 1 . . . . . . . . 4787 1 188 . 1 1 29 29 LYS C C 13 178.5 0.1 . 1 . . . . . . . . 4787 1 189 . 1 1 30 30 GLU N N 15 118.6 0.1 . 1 . . . . . . . . 4787 1 190 . 1 1 30 30 GLU H H 1 8.10 0.02 . 1 . . . . . . . . 4787 1 191 . 1 1 30 30 GLU CA C 13 58.6 0.1 . 1 . . . . . . . . 4787 1 192 . 1 1 30 30 GLU CB C 13 29.3 0.1 . 1 . . . . . . . . 4787 1 193 . 1 1 30 30 GLU HB2 H 1 2.03 0.02 . 1 . . . . . . . . 4787 1 194 . 1 1 30 30 GLU HB3 H 1 2.03 0.02 . 1 . . . . . . . . 4787 1 195 . 1 1 30 30 GLU CG C 13 34.4 0.1 . 1 . . . . . . . . 4787 1 196 . 1 1 30 30 GLU HG2 H 1 2.67 0.02 . 1 . . . . . . . . 4787 1 197 . 1 1 30 30 GLU HG3 H 1 2.67 0.02 . 1 . . . . . . . . 4787 1 198 . 1 1 30 30 GLU C C 13 178.4 0.1 . 1 . . . . . . . . 4787 1 199 . 1 1 31 31 ILE N N 15 119.0 0.1 . 1 . . . . . . . . 4787 1 200 . 1 1 31 31 ILE H H 1 8.29 0.02 . 1 . . . . . . . . 4787 1 201 . 1 1 31 31 ILE CA C 13 58.8 0.1 . 1 . . . . . . . . 4787 1 202 . 1 1 31 31 ILE HA H 1 4.11 0.02 . 1 . . . . . . . . 4787 1 203 . 1 1 31 31 ILE CB C 13 39.4 0.1 . 1 . . . . . . . . 4787 1 204 . 1 1 31 31 ILE HB H 1 1.85 0.02 . 1 . . . . . . . . 4787 1 205 . 1 1 31 31 ILE HG21 H 1 0.61 0.02 . 1 . . . . . . . . 4787 1 206 . 1 1 31 31 ILE HG22 H 1 0.61 0.02 . 1 . . . . . . . . 4787 1 207 . 1 1 31 31 ILE HG23 H 1 0.61 0.02 . 1 . . . . . . . . 4787 1 208 . 1 1 31 31 ILE CG1 C 13 31.9 0.1 . 1 . . . . . . . . 4787 1 209 . 1 1 31 31 ILE HD11 H 1 0.81 0.02 . 1 . . . . . . . . 4787 1 210 . 1 1 31 31 ILE HD12 H 1 0.81 0.02 . 1 . . . . . . . . 4787 1 211 . 1 1 31 31 ILE HD13 H 1 0.81 0.02 . 1 . . . . . . . . 4787 1 212 . 1 1 31 31 ILE C C 13 177.0 0.1 . 1 . . . . . . . . 4787 1 213 . 1 1 32 32 GLU N N 15 120.1 0.1 . 1 . . . . . . . . 4787 1 214 . 1 1 32 32 GLU H H 1 8.00 0.02 . 1 . . . . . . . . 4787 1 215 . 1 1 32 32 GLU CA C 13 56.9 0.1 . 1 . . . . . . . . 4787 1 216 . 1 1 32 32 GLU HA H 1 4.36 0.02 . 1 . . . . . . . . 4787 1 217 . 1 1 32 32 GLU CB C 13 28.8 0.1 . 1 . . . . . . . . 4787 1 218 . 1 1 32 32 GLU HB2 H 1 1.91 0.02 . 2 . . . . . . . . 4787 1 219 . 1 1 32 32 GLU HB3 H 1 1.75 0.02 . 2 . . . . . . . . 4787 1 220 . 1 1 32 32 GLU CG C 13 33.7 0.1 . 1 . . . . . . . . 4787 1 221 . 1 1 32 32 GLU HG2 H 1 2.26 0.02 . 2 . . . . . . . . 4787 1 222 . 1 1 32 32 GLU HG3 H 1 2.38 0.02 . 2 . . . . . . . . 4787 1 223 . 1 1 32 32 GLU C C 13 177.0 0.1 . 1 . . . . . . . . 4787 1 224 . 1 1 33 33 ARG N N 15 119.5 0.1 . 1 . . . . . . . . 4787 1 225 . 1 1 33 33 ARG H H 1 8.03 0.02 . 1 . . . . . . . . 4787 1 226 . 1 1 33 33 ARG CA C 13 59.1 0.1 . 1 . . . . . . . . 4787 1 227 . 1 1 33 33 ARG HA H 1 4.17 0.02 . 1 . . . . . . . . 4787 1 228 . 1 1 33 33 ARG CB C 13 30.6 0.1 . 1 . . . . . . . . 4787 1 229 . 1 1 33 33 ARG HB2 H 1 1.74 0.02 . 2 . . . . . . . . 4787 1 230 . 1 1 33 33 ARG HB3 H 1 1.92 0.02 . 2 . . . . . . . . 4787 1 231 . 1 1 33 33 ARG CG C 13 26.9 0.1 . 1 . . . . . . . . 4787 1 232 . 1 1 33 33 ARG HG2 H 1 2.21 0.02 . 2 . . . . . . . . 4787 1 233 . 1 1 33 33 ARG HG3 H 1 2.06 0.02 . 2 . . . . . . . . 4787 1 234 . 1 1 33 33 ARG CD C 13 43.1 0.1 . 1 . . . . . . . . 4787 1 235 . 1 1 33 33 ARG HD2 H 1 3.32 0.02 . 1 . . . . . . . . 4787 1 236 . 1 1 33 33 ARG HD3 H 1 3.32 0.02 . 1 . . . . . . . . 4787 1 237 . 1 1 33 33 ARG HE H 1 7.15 0.02 . 1 . . . . . . . . 4787 1 238 . 1 1 33 33 ARG C C 13 178.7 0.1 . 1 . . . . . . . . 4787 1 239 . 1 1 34 34 GLU N N 15 118.5 0.1 . 1 . . . . . . . . 4787 1 240 . 1 1 34 34 GLU H H 1 8.09 0.02 . 1 . . . . . . . . 4787 1 241 . 1 1 34 34 GLU CA C 13 57.7 0.1 . 1 . . . . . . . . 4787 1 242 . 1 1 34 34 GLU HA H 1 4.22 0.02 . 1 . . . . . . . . 4787 1 243 . 1 1 34 34 GLU CB C 13 29.3 0.1 . 1 . . . . . . . . 4787 1 244 . 1 1 34 34 GLU HB2 H 1 2.20 0.02 . 2 . . . . . . . . 4787 1 245 . 1 1 34 34 GLU HB3 H 1 1.98 0.02 . 2 . . . . . . . . 4787 1 246 . 1 1 34 34 GLU CG C 13 33.6 0.1 . 1 . . . . . . . . 4787 1 247 . 1 1 34 34 GLU HG2 H 1 2.71 0.02 . 2 . . . . . . . . 4787 1 248 . 1 1 34 34 GLU HG3 H 1 2.52 0.02 . 2 . . . . . . . . 4787 1 249 . 1 1 34 34 GLU C C 13 177.8 0.1 . 1 . . . . . . . . 4787 1 250 . 1 1 35 35 SER N N 15 115.0 0.1 . 1 . . . . . . . . 4787 1 251 . 1 1 35 35 SER H H 1 8.08 0.02 . 1 . . . . . . . . 4787 1 252 . 1 1 35 35 SER CA C 13 60.1 0.1 . 1 . . . . . . . . 4787 1 253 . 1 1 35 35 SER HA H 1 4.42 0.02 . 1 . . . . . . . . 4787 1 254 . 1 1 35 35 SER CB C 13 63.0 0.1 . 1 . . . . . . . . 4787 1 255 . 1 1 35 35 SER HB2 H 1 4.01 0.02 . 1 . . . . . . . . 4787 1 256 . 1 1 35 35 SER HB3 H 1 4.01 0.02 . 1 . . . . . . . . 4787 1 257 . 1 1 35 35 SER C C 13 175.0 0.1 . 1 . . . . . . . . 4787 1 258 . 1 1 36 36 LYS N N 15 121.4 0.1 . 1 . . . . . . . . 4787 1 259 . 1 1 36 36 LYS H H 1 7.87 0.02 . 1 . . . . . . . . 4787 1 260 . 1 1 36 36 LYS CA C 13 57.2 0.1 . 1 . . . . . . . . 4787 1 261 . 1 1 36 36 LYS HA H 1 4.39 0.02 . 1 . . . . . . . . 4787 1 262 . 1 1 36 36 LYS CB C 13 33.2 0.1 . 1 . . . . . . . . 4787 1 263 . 1 1 36 36 LYS HB2 H 1 1.95 0.02 . 1 . . . . . . . . 4787 1 264 . 1 1 36 36 LYS HB3 H 1 1.95 0.02 . 1 . . . . . . . . 4787 1 265 . 1 1 36 36 LYS CG C 13 23.9 0.1 . 1 . . . . . . . . 4787 1 266 . 1 1 36 36 LYS HG2 H 1 1.59 0.02 . 1 . . . . . . . . 4787 1 267 . 1 1 36 36 LYS HG3 H 1 1.59 0.02 . 1 . . . . . . . . 4787 1 268 . 1 1 36 36 LYS CD C 13 28.9 0.1 . 1 . . . . . . . . 4787 1 269 . 1 1 36 36 LYS HD2 H 1 1.84 0.02 . 1 . . . . . . . . 4787 1 270 . 1 1 36 36 LYS HD3 H 1 1.84 0.02 . 1 . . . . . . . . 4787 1 271 . 1 1 38 38 ILE N N 15 120.6 0.1 . 1 . . . . . . . . 4787 1 272 . 1 1 38 38 ILE H H 1 7.96 0.02 . 1 . . . . . . . . 4787 1 273 . 1 1 38 38 ILE CA C 13 61.4 0.1 . 1 . . . . . . . . 4787 1 274 . 1 1 38 38 ILE HA H 1 4.20 0.02 . 1 . . . . . . . . 4787 1 275 . 1 1 38 38 ILE CB C 13 39.0 0.1 . 1 . . . . . . . . 4787 1 276 . 1 1 38 38 ILE HB H 1 1.94 0.02 . 1 . . . . . . . . 4787 1 277 . 1 1 38 38 ILE HG21 H 1 0.93 0.02 . 1 . . . . . . . . 4787 1 278 . 1 1 38 38 ILE HG22 H 1 0.93 0.02 . 1 . . . . . . . . 4787 1 279 . 1 1 38 38 ILE HG23 H 1 0.93 0.02 . 1 . . . . . . . . 4787 1 280 . 1 1 38 38 ILE CG2 C 13 17.0 0.1 . 1 . . . . . . . . 4787 1 281 . 1 1 38 38 ILE CG1 C 13 26.7 0.1 . 1 . . . . . . . . 4787 1 282 . 1 1 38 38 ILE HG12 H 1 1.26 0.02 . 2 . . . . . . . . 4787 1 283 . 1 1 38 38 ILE HG13 H 1 1.57 0.02 . 2 . . . . . . . . 4787 1 284 . 1 1 38 38 ILE HD11 H 1 0.98 0.02 . 1 . . . . . . . . 4787 1 285 . 1 1 38 38 ILE HD12 H 1 0.98 0.02 . 1 . . . . . . . . 4787 1 286 . 1 1 38 38 ILE HD13 H 1 0.98 0.02 . 1 . . . . . . . . 4787 1 287 . 1 1 38 38 ILE C C 13 176.1 0.1 . 1 . . . . . . . . 4787 1 288 . 1 1 39 39 LYS N N 15 124.5 0.1 . 1 . . . . . . . . 4787 1 289 . 1 1 39 39 LYS H H 1 8.29 0.02 . 1 . . . . . . . . 4787 1 290 . 1 1 39 39 LYS CA C 13 56.4 0.1 . 1 . . . . . . . . 4787 1 291 . 1 1 39 39 LYS HA H 1 4.41 0.02 . 1 . . . . . . . . 4787 1 292 . 1 1 39 39 LYS CB C 13 33.1 0.1 . 1 . . . . . . . . 4787 1 293 . 1 1 39 39 LYS HB2 H 1 1.92 0.02 . 1 . . . . . . . . 4787 1 294 . 1 1 39 39 LYS HB3 H 1 1.92 0.02 . 1 . . . . . . . . 4787 1 295 . 1 1 39 39 LYS CG C 13 24.2 0.1 . 1 . . . . . . . . 4787 1 296 . 1 1 39 39 LYS HG2 H 1 1.51 0.02 . 1 . . . . . . . . 4787 1 297 . 1 1 39 39 LYS HG3 H 1 1.51 0.02 . 1 . . . . . . . . 4787 1 298 . 1 1 39 39 LYS CD C 13 29.0 0.1 . 1 . . . . . . . . 4787 1 299 . 1 1 39 39 LYS HD2 H 1 1.85 0.02 . 1 . . . . . . . . 4787 1 300 . 1 1 39 39 LYS HD3 H 1 1.85 0.02 . 1 . . . . . . . . 4787 1 301 . 1 1 39 39 LYS CE C 13 41.7 0.1 . 1 . . . . . . . . 4787 1 302 . 1 1 39 39 LYS HE2 H 1 2.90 0.02 . 1 . . . . . . . . 4787 1 303 . 1 1 39 39 LYS HE3 H 1 2.90 0.02 . 1 . . . . . . . . 4787 1 304 . 1 1 39 39 LYS C C 13 176.4 0.1 . 1 . . . . . . . . 4787 1 305 . 1 1 40 40 LEU N N 15 123.5 0.1 . 1 . . . . . . . . 4787 1 306 . 1 1 40 40 LEU H H 1 8.35 0.02 . 1 . . . . . . . . 4787 1 307 . 1 1 40 40 LEU CA C 13 55.4 0.1 . 1 . . . . . . . . 4787 1 308 . 1 1 40 40 LEU HA H 1 4.39 0.02 . 1 . . . . . . . . 4787 1 309 . 1 1 40 40 LEU CB C 13 42.6 0.1 . 1 . . . . . . . . 4787 1 310 . 1 1 40 40 LEU HB2 H 1 1.72 0.02 . 1 . . . . . . . . 4787 1 311 . 1 1 40 40 LEU HB3 H 1 1.72 0.02 . 1 . . . . . . . . 4787 1 312 . 1 1 40 40 LEU CG C 13 26.2 0.1 . 1 . . . . . . . . 4787 1 313 . 1 1 40 40 LEU HG H 1 1.63 0.02 . 1 . . . . . . . . 4787 1 314 . 1 1 40 40 LEU HD11 H 1 0.96 0.02 . 2 . . . . . . . . 4787 1 315 . 1 1 40 40 LEU HD12 H 1 0.96 0.02 . 2 . . . . . . . . 4787 1 316 . 1 1 40 40 LEU HD13 H 1 0.96 0.02 . 2 . . . . . . . . 4787 1 317 . 1 1 40 40 LEU HD21 H 1 0.93 0.02 . 2 . . . . . . . . 4787 1 318 . 1 1 40 40 LEU HD22 H 1 0.93 0.02 . 2 . . . . . . . . 4787 1 319 . 1 1 40 40 LEU HD23 H 1 0.93 0.02 . 2 . . . . . . . . 4787 1 320 . 1 1 40 40 LEU CD1 C 13 23.9 0.1 . 1 . . . . . . . . 4787 1 321 . 1 1 40 40 LEU CD2 C 13 23.9 0.1 . 1 . . . . . . . . 4787 1 322 . 1 1 40 40 LEU C C 13 177.1 0.1 . 1 . . . . . . . . 4787 1 323 . 1 1 41 41 ASN N N 15 118.4 0.1 . 1 . . . . . . . . 4787 1 324 . 1 1 41 41 ASN H H 1 8.43 0.02 . 1 . . . . . . . . 4787 1 325 . 1 1 41 41 ASN CA C 13 53.2 0.1 . 1 . . . . . . . . 4787 1 326 . 1 1 41 41 ASN HA H 1 4.79 0.02 . 1 . . . . . . . . 4787 1 327 . 1 1 41 41 ASN CB C 13 39.0 0.1 . 1 . . . . . . . . 4787 1 328 . 1 1 41 41 ASN HB2 H 1 2.88 0.02 . 1 . . . . . . . . 4787 1 329 . 1 1 41 41 ASN HB3 H 1 2.88 0.02 . 1 . . . . . . . . 4787 1 330 . 1 1 41 41 ASN HD21 H 1 6.97 0.02 . 2 . . . . . . . . 4787 1 331 . 1 1 41 41 ASN HD22 H 1 7.67 0.02 . 2 . . . . . . . . 4787 1 332 . 1 1 46 46 GLU N N 15 120.1 0.1 . 1 . . . . . . . . 4787 1 333 . 1 1 46 46 GLU H H 1 8.41 0.02 . 1 . . . . . . . . 4787 1 334 . 1 1 46 46 GLU CA C 13 56.5 0.1 . 1 . . . . . . . . 4787 1 335 . 1 1 46 46 GLU HA H 1 4.75 0.02 . 1 . . . . . . . . 4787 1 336 . 1 1 46 46 GLU CB C 13 29.1 0.1 . 1 . . . . . . . . 4787 1 337 . 1 1 46 46 GLU HB2 H 1 2.13 0.02 . 1 . . . . . . . . 4787 1 338 . 1 1 46 46 GLU HB3 H 1 2.13 0.02 . 1 . . . . . . . . 4787 1 339 . 1 1 46 46 GLU CG C 13 33.1 0.1 . 1 . . . . . . . . 4787 1 340 . 1 1 46 46 GLU HG2 H 1 2.50 0.02 . 2 . . . . . . . . 4787 1 341 . 1 1 46 46 GLU HG3 H 1 2.27 0.02 . 2 . . . . . . . . 4787 1 342 . 1 1 46 46 GLU C C 13 177.0 0.1 . 1 . . . . . . . . 4787 1 343 . 1 1 47 47 GLY N N 15 109.1 0.1 . 1 . . . . . . . . 4787 1 344 . 1 1 47 47 GLY H H 1 8.49 0.02 . 1 . . . . . . . . 4787 1 345 . 1 1 47 47 GLY CA C 13 45.8 0.1 . 1 . . . . . . . . 4787 1 346 . 1 1 47 47 GLY HA3 H 1 4.39 0.02 . 2 . . . . . . . . 4787 1 347 . 1 1 47 47 GLY HA2 H 1 4.00 0.02 . 2 . . . . . . . . 4787 1 348 . 1 1 47 47 GLY C C 13 174.3 0.1 . 1 . . . . . . . . 4787 1 349 . 1 1 48 48 ASN N N 15 118.6 0.1 . 1 . . . . . . . . 4787 1 350 . 1 1 48 48 ASN H H 1 8.29 0.02 . 1 . . . . . . . . 4787 1 351 . 1 1 48 48 ASN CA C 13 53.5 0.1 . 1 . . . . . . . . 4787 1 352 . 1 1 48 48 ASN HA H 1 4.79 0.02 . 1 . . . . . . . . 4787 1 353 . 1 1 48 48 ASN CB C 13 39.0 0.1 . 1 . . . . . . . . 4787 1 354 . 1 1 48 48 ASN HB2 H 1 2.91 0.02 . 1 . . . . . . . . 4787 1 355 . 1 1 48 48 ASN HB3 H 1 2.91 0.02 . 1 . . . . . . . . 4787 1 356 . 1 1 48 48 ASN HD21 H 1 6.06 0.02 . 2 . . . . . . . . 4787 1 357 . 1 1 48 48 ASN HD22 H 1 7.67 0.02 . 2 . . . . . . . . 4787 1 358 . 1 1 48 48 ASN C C 13 175.8 0.1 . 1 . . . . . . . . 4787 1 359 . 1 1 49 49 LYS N N 15 120.8 0.1 . 1 . . . . . . . . 4787 1 360 . 1 1 49 49 LYS H H 1 8.22 0.02 . 1 . . . . . . . . 4787 1 361 . 1 1 49 49 LYS CA C 13 56.5 0.1 . 1 . . . . . . . . 4787 1 362 . 1 1 49 49 LYS HA H 1 4.37 0.02 . 1 . . . . . . . . 4787 1 363 . 1 1 49 49 LYS CB C 13 33.2 0.1 . 1 . . . . . . . . 4787 1 364 . 1 1 49 49 LYS HB2 H 1 2.02 0.02 . 1 . . . . . . . . 4787 1 365 . 1 1 49 49 LYS HB3 H 1 2.02 0.02 . 1 . . . . . . . . 4787 1 366 . 1 1 49 49 LYS CG C 13 23.9 0.1 . 1 . . . . . . . . 4787 1 367 . 1 1 49 49 LYS HG2 H 1 1.50 0.02 . 1 . . . . . . . . 4787 1 368 . 1 1 49 49 LYS HG3 H 1 1.50 0.02 . 1 . . . . . . . . 4787 1 369 . 1 1 49 49 LYS CD C 13 29.1 0.1 . 1 . . . . . . . . 4787 1 370 . 1 1 49 49 LYS HD2 H 1 1.87 0.02 . 1 . . . . . . . . 4787 1 371 . 1 1 49 49 LYS HD3 H 1 1.87 0.02 . 1 . . . . . . . . 4787 1 372 . 1 1 49 49 LYS C C 13 176.2 0.1 . 1 . . . . . . . . 4787 1 373 . 1 1 50 50 LYS N N 15 121.4 0.1 . 1 . . . . . . . . 4787 1 374 . 1 1 50 50 LYS H H 1 8.27 0.02 . 1 . . . . . . . . 4787 1 375 . 1 1 50 50 LYS CA C 13 56.2 0.1 . 1 . . . . . . . . 4787 1 376 . 1 1 50 50 LYS HA H 1 4.41 0.02 . 1 . . . . . . . . 4787 1 377 . 1 1 50 50 LYS CB C 13 33.1 0.1 . 1 . . . . . . . . 4787 1 378 . 1 1 50 50 LYS HB2 H 1 1.83 0.02 . 1 . . . . . . . . 4787 1 379 . 1 1 50 50 LYS HB3 H 1 1.83 0.02 . 1 . . . . . . . . 4787 1 380 . 1 1 50 50 LYS CG C 13 24.1 0.1 . 1 . . . . . . . . 4787 1 381 . 1 1 50 50 LYS HG2 H 1 1.48 0.02 . 1 . . . . . . . . 4787 1 382 . 1 1 50 50 LYS HG3 H 1 1.48 0.02 . 1 . . . . . . . . 4787 1 383 . 1 1 50 50 LYS CD C 13 29.1 0.1 . 1 . . . . . . . . 4787 1 384 . 1 1 50 50 LYS HD2 H 1 1.83 0.02 . 1 . . . . . . . . 4787 1 385 . 1 1 50 50 LYS HD3 H 1 1.83 0.02 . 1 . . . . . . . . 4787 1 386 . 1 1 50 50 LYS C C 13 176.1 0.1 . 1 . . . . . . . . 4787 1 387 . 1 1 51 51 ILE N N 15 122.4 0.1 . 1 . . . . . . . . 4787 1 388 . 1 1 51 51 ILE H H 1 8.12 0.02 . 1 . . . . . . . . 4787 1 389 . 1 1 51 51 ILE CA C 13 60.5 0.1 . 1 . . . . . . . . 4787 1 390 . 1 1 51 51 ILE HA H 1 4.38 0.02 . 1 . . . . . . . . 4787 1 391 . 1 1 51 51 ILE CB C 13 38.8 0.1 . 1 . . . . . . . . 4787 1 392 . 1 1 51 51 ILE HB H 1 1.90 0.02 . 1 . . . . . . . . 4787 1 393 . 1 1 51 51 ILE HG21 H 1 0.90 0.02 . 1 . . . . . . . . 4787 1 394 . 1 1 51 51 ILE HG22 H 1 0.90 0.02 . 1 . . . . . . . . 4787 1 395 . 1 1 51 51 ILE HG23 H 1 0.90 0.02 . 1 . . . . . . . . 4787 1 396 . 1 1 51 51 ILE CG2 C 13 17.2 0.1 . 1 . . . . . . . . 4787 1 397 . 1 1 51 51 ILE CG1 C 13 26.7 0.1 . 1 . . . . . . . . 4787 1 398 . 1 1 51 51 ILE HG12 H 1 1.53 0.02 . 2 . . . . . . . . 4787 1 399 . 1 1 51 51 ILE HG13 H 1 1.26 0.02 . 2 . . . . . . . . 4787 1 400 . 1 1 51 51 ILE HD11 H 1 0.93 0.02 . 1 . . . . . . . . 4787 1 401 . 1 1 51 51 ILE HD12 H 1 0.93 0.02 . 1 . . . . . . . . 4787 1 402 . 1 1 51 51 ILE HD13 H 1 0.93 0.02 . 1 . . . . . . . . 4787 1 403 . 1 1 51 51 ILE C C 13 175.8 0.1 . 1 . . . . . . . . 4787 1 404 . 1 1 52 52 ILE N N 15 126.0 0.1 . 1 . . . . . . . . 4787 1 405 . 1 1 52 52 ILE H H 1 8.37 0.02 . 1 . . . . . . . . 4787 1 406 . 1 1 52 52 ILE CA C 13 60.5 0.1 . 1 . . . . . . . . 4787 1 407 . 1 1 52 52 ILE HA H 1 4.28 0.02 . 1 . . . . . . . . 4787 1 408 . 1 1 52 52 ILE CB C 13 38.9 0.1 . 1 . . . . . . . . 4787 1 409 . 1 1 52 52 ILE HB H 1 1.90 0.02 . 1 . . . . . . . . 4787 1 410 . 1 1 52 52 ILE HG21 H 1 0.91 0.02 . 1 . . . . . . . . 4787 1 411 . 1 1 52 52 ILE HG22 H 1 0.91 0.02 . 1 . . . . . . . . 4787 1 412 . 1 1 52 52 ILE HG23 H 1 0.91 0.02 . 1 . . . . . . . . 4787 1 413 . 1 1 52 52 ILE CG2 C 13 17.2 0.1 . 1 . . . . . . . . 4787 1 414 . 1 1 52 52 ILE CG1 C 13 26.5 0.1 . 1 . . . . . . . . 4787 1 415 . 1 1 52 52 ILE HG12 H 1 1.51 0.02 . 2 . . . . . . . . 4787 1 416 . 1 1 52 52 ILE HG13 H 1 1.23 0.02 . 2 . . . . . . . . 4787 1 417 . 1 1 52 52 ILE HD11 H 1 0.93 0.02 . 1 . . . . . . . . 4787 1 418 . 1 1 52 52 ILE HD12 H 1 0.93 0.02 . 1 . . . . . . . . 4787 1 419 . 1 1 52 52 ILE HD13 H 1 0.93 0.02 . 1 . . . . . . . . 4787 1 420 . 1 1 52 52 ILE C C 13 175.3 0.1 . 1 . . . . . . . . 4787 1 421 . 1 1 53 53 ALA N N 15 129.6 0.1 . 1 . . . . . . . . 4787 1 422 . 1 1 53 53 ALA H H 1 8.37 0.02 . 1 . . . . . . . . 4787 1 423 . 1 1 53 53 ALA CA C 13 50.2 0.1 . 1 . . . . . . . . 4787 1 424 . 1 1 53 53 ALA HA H 1 4.71 0.02 . 1 . . . . . . . . 4787 1 425 . 1 1 53 53 ALA HB1 H 1 1.41 0.02 . 1 . . . . . . . . 4787 1 426 . 1 1 53 53 ALA HB2 H 1 1.41 0.02 . 1 . . . . . . . . 4787 1 427 . 1 1 53 53 ALA HB3 H 1 1.41 0.02 . 1 . . . . . . . . 4787 1 428 . 1 1 53 53 ALA CB C 13 18.2 0.1 . 1 . . . . . . . . 4787 1 429 . 1 1 54 54 PRO CA C 13 62.8 0.1 . 1 . . . . . . . . 4787 1 430 . 1 1 54 54 PRO CB C 13 32.5 0.1 . 1 . . . . . . . . 4787 1 431 . 1 1 54 54 PRO HB2 H 1 2.34 0.02 . 1 . . . . . . . . 4787 1 432 . 1 1 54 54 PRO HB3 H 1 2.34 0.02 . 1 . . . . . . . . 4787 1 433 . 1 1 54 54 PRO CG C 13 26.6 0.1 . 1 . . . . . . . . 4787 1 434 . 1 1 54 54 PRO HD2 H 1 3.80 0.02 . 1 . . . . . . . . 4787 1 435 . 1 1 54 54 PRO HD3 H 1 3.80 0.02 . 1 . . . . . . . . 4787 1 436 . 1 1 54 54 PRO C C 13 175.4 0.1 . 1 . . . . . . . . 4787 1 437 . 1 1 55 55 ARG N N 15 121.1 0.1 . 1 . . . . . . . . 4787 1 438 . 1 1 55 55 ARG H H 1 8.37 0.02 . 1 . . . . . . . . 4787 1 439 . 1 1 55 55 ARG CA C 13 56.2 0.1 . 1 . . . . . . . . 4787 1 440 . 1 1 55 55 ARG HA H 1 4.51 0.02 . 1 . . . . . . . . 4787 1 441 . 1 1 55 55 ARG CB C 13 31.4 0.1 . 1 . . . . . . . . 4787 1 442 . 1 1 55 55 ARG HB2 H 1 1.78 0.02 . 1 . . . . . . . . 4787 1 443 . 1 1 55 55 ARG HB3 H 1 1.78 0.02 . 1 . . . . . . . . 4787 1 444 . 1 1 55 55 ARG CG C 13 26.8 0.1 . 1 . . . . . . . . 4787 1 445 . 1 1 55 55 ARG HG2 H 1 1.61 0.02 . 1 . . . . . . . . 4787 1 446 . 1 1 55 55 ARG HG3 H 1 1.61 0.02 . 1 . . . . . . . . 4787 1 447 . 1 1 55 55 ARG CD C 13 43.3 0.1 . 1 . . . . . . . . 4787 1 448 . 1 1 55 55 ARG HD2 H 1 3.26 0.02 . 1 . . . . . . . . 4787 1 449 . 1 1 55 55 ARG HD3 H 1 3.26 0.02 . 1 . . . . . . . . 4787 1 450 . 1 1 55 55 ARG C C 13 175.6 0.1 . 1 . . . . . . . . 4787 1 451 . 1 1 56 56 ILE N N 15 121.1 0.1 . 1 . . . . . . . . 4787 1 452 . 1 1 56 56 ILE H H 1 8.04 0.02 . 1 . . . . . . . . 4787 1 453 . 1 1 56 56 ILE CA C 13 60.4 0.1 . 1 . . . . . . . . 4787 1 454 . 1 1 56 56 ILE HA H 1 4.34 0.02 . 1 . . . . . . . . 4787 1 455 . 1 1 56 56 ILE CB C 13 39.0 0.1 . 1 . . . . . . . . 4787 1 456 . 1 1 56 56 ILE HB H 1 1.83 0.02 . 1 . . . . . . . . 4787 1 457 . 1 1 56 56 ILE HG21 H 1 0.89 0.02 . 1 . . . . . . . . 4787 1 458 . 1 1 56 56 ILE HG22 H 1 0.89 0.02 . 1 . . . . . . . . 4787 1 459 . 1 1 56 56 ILE HG23 H 1 0.89 0.02 . 1 . . . . . . . . 4787 1 460 . 1 1 56 56 ILE CG2 C 13 12.6 0.1 . 1 . . . . . . . . 4787 1 461 . 1 1 56 56 ILE CG1 C 13 26.9 0.1 . 1 . . . . . . . . 4787 1 462 . 1 1 56 56 ILE HG12 H 1 1.55 0.02 . 2 . . . . . . . . 4787 1 463 . 1 1 56 56 ILE HG13 H 1 1.17 0.02 . 2 . . . . . . . . 4787 1 464 . 1 1 56 56 ILE CD1 C 13 17.0 0.1 . 1 . . . . . . . . 4787 1 465 . 1 1 56 56 ILE C C 13 175.2 0.1 . 1 . . . . . . . . 4787 1 466 . 1 1 57 57 PHE N N 15 122.4 0.1 . 1 . . . . . . . . 4787 1 467 . 1 1 57 57 PHE H H 1 8.37 0.02 . 1 . . . . . . . . 4787 1 468 . 1 1 57 57 PHE CA C 13 57.2 0.1 . 1 . . . . . . . . 4787 1 469 . 1 1 57 57 PHE HA H 1 4.97 0.02 . 1 . . . . . . . . 4787 1 470 . 1 1 57 57 PHE CB C 13 38.4 0.1 . 1 . . . . . . . . 4787 1 471 . 1 1 57 57 PHE HB2 H 1 3.19 0.02 . 2 . . . . . . . . 4787 1 472 . 1 1 57 57 PHE HB3 H 1 2.83 0.02 . 2 . . . . . . . . 4787 1 473 . 1 1 57 57 PHE HD1 H 1 7.01 0.02 . 1 . . . . . . . . 4787 1 474 . 1 1 57 57 PHE HD2 H 1 7.01 0.02 . 1 . . . . . . . . 4787 1 475 . 1 1 57 57 PHE HE1 H 1 7.35 0.02 . 1 . . . . . . . . 4787 1 476 . 1 1 57 57 PHE HE2 H 1 7.35 0.02 . 1 . . . . . . . . 4787 1 477 . 1 1 59 59 SER N N 15 118.0 0.1 . 1 . . . . . . . . 4787 1 478 . 1 1 59 59 SER H H 1 9.07 0.02 . 1 . . . . . . . . 4787 1 479 . 1 1 59 59 SER CA C 13 56.9 0.1 . 1 . . . . . . . . 4787 1 480 . 1 1 59 59 SER HA H 1 4.90 0.02 . 1 . . . . . . . . 4787 1 481 . 1 1 59 59 SER CB C 13 64.4 0.1 . 1 . . . . . . . . 4787 1 482 . 1 1 59 59 SER HB2 H 1 4.03 0.02 . 2 . . . . . . . . 4787 1 483 . 1 1 59 59 SER HB3 H 1 3.63 0.02 . 2 . . . . . . . . 4787 1 484 . 1 1 59 59 SER C C 13 174.0 0.1 . 1 . . . . . . . . 4787 1 485 . 1 1 60 60 ASP N N 15 124.0 0.1 . 1 . . . . . . . . 4787 1 486 . 1 1 60 60 ASP H H 1 9.07 0.02 . 1 . . . . . . . . 4787 1 487 . 1 1 60 60 ASP CA C 13 55.2 0.1 . 1 . . . . . . . . 4787 1 488 . 1 1 60 60 ASP HA H 1 4.91 0.02 . 1 . . . . . . . . 4787 1 489 . 1 1 60 60 ASP CB C 13 39.8 0.1 . 1 . . . . . . . . 4787 1 490 . 1 1 60 60 ASP HB2 H 1 3.01 0.02 . 1 . . . . . . . . 4787 1 491 . 1 1 60 60 ASP HB3 H 1 3.01 0.02 . 1 . . . . . . . . 4787 1 492 . 1 1 60 60 ASP C C 13 174.9 0.1 . 1 . . . . . . . . 4787 1 493 . 1 1 61 61 ASP N N 15 118.8 0.1 . 1 . . . . . . . . 4787 1 494 . 1 1 61 61 ASP H H 1 8.50 0.02 . 1 . . . . . . . . 4787 1 495 . 1 1 61 61 ASP CA C 13 52.3 0.1 . 1 . . . . . . . . 4787 1 496 . 1 1 61 61 ASP HA H 1 4.96 0.02 . 1 . . . . . . . . 4787 1 497 . 1 1 61 61 ASP CB C 13 38.7 0.1 . 1 . . . . . . . . 4787 1 498 . 1 1 61 61 ASP HB2 H 1 2.91 0.02 . 2 . . . . . . . . 4787 1 499 . 1 1 61 61 ASP HB3 H 1 2.77 0.02 . 2 . . . . . . . . 4787 1 500 . 1 1 61 61 ASP C C 13 175.3 0.1 . 1 . . . . . . . . 4787 1 501 . 1 1 62 62 LYS N N 15 125.6 0.1 . 1 . . . . . . . . 4787 1 502 . 1 1 62 62 LYS H H 1 8.37 0.02 . 1 . . . . . . . . 4787 1 503 . 1 1 62 62 LYS CA C 13 59.7 0.1 . 1 . . . . . . . . 4787 1 504 . 1 1 62 62 LYS HA H 1 5.00 0.02 . 1 . . . . . . . . 4787 1 505 . 1 1 62 62 LYS CB C 13 32.3 0.1 . 1 . . . . . . . . 4787 1 506 . 1 1 62 62 LYS HB2 H 1 1.06 0.02 . 1 . . . . . . . . 4787 1 507 . 1 1 62 62 LYS HB3 H 1 1.06 0.02 . 1 . . . . . . . . 4787 1 508 . 1 1 62 62 LYS CG C 13 24.1 0.1 . 1 . . . . . . . . 4787 1 509 . 1 1 62 62 LYS HG2 H 1 0.68 0.02 . 2 . . . . . . . . 4787 1 510 . 1 1 62 62 LYS HG3 H 1 0.75 0.02 . 2 . . . . . . . . 4787 1 511 . 1 1 62 62 LYS HE2 H 1 3.33 0.02 . 1 . . . . . . . . 4787 1 512 . 1 1 62 62 LYS HE3 H 1 3.33 0.02 . 1 . . . . . . . . 4787 1 513 . 1 1 62 62 LYS HZ1 H 1 7.42 0.02 . 3 . . . . . . . . 4787 1 514 . 1 1 62 62 LYS HZ2 H 1 7.42 0.02 . 3 . . . . . . . . 4787 1 515 . 1 1 62 62 LYS HZ3 H 1 7.42 0.02 . 3 . . . . . . . . 4787 1 516 . 1 1 62 62 LYS C C 13 178.1 0.1 . 1 . . . . . . . . 4787 1 517 . 1 1 63 63 ASP N N 15 116.9 0.1 . 1 . . . . . . . . 4787 1 518 . 1 1 63 63 ASP H H 1 8.25 0.02 . 1 . . . . . . . . 4787 1 519 . 1 1 63 63 ASP CA C 13 56.0 0.1 . 1 . . . . . . . . 4787 1 520 . 1 1 63 63 ASP HA H 1 4.48 0.02 . 1 . . . . . . . . 4787 1 521 . 1 1 63 63 ASP CB C 13 39.3 0.1 . 1 . . . . . . . . 4787 1 522 . 1 1 63 63 ASP HB2 H 1 2.83 0.02 . 1 . . . . . . . . 4787 1 523 . 1 1 63 63 ASP HB3 H 1 2.83 0.02 . 1 . . . . . . . . 4787 1 524 . 1 1 63 63 ASP C C 13 177.6 0.1 . 1 . . . . . . . . 4787 1 525 . 1 1 64 64 SER N N 15 114.6 0.1 . 1 . . . . . . . . 4787 1 526 . 1 1 64 64 SER H H 1 7.91 0.02 . 1 . . . . . . . . 4787 1 527 . 1 1 64 64 SER CA C 13 59.8 0.1 . 1 . . . . . . . . 4787 1 528 . 1 1 64 64 SER HA H 1 4.38 0.02 . 1 . . . . . . . . 4787 1 529 . 1 1 64 64 SER CB C 13 62.6 0.1 . 1 . . . . . . . . 4787 1 530 . 1 1 64 64 SER HB2 H 1 3.98 0.02 . 2 . . . . . . . . 4787 1 531 . 1 1 64 64 SER HB3 H 1 4.03 0.02 . 2 . . . . . . . . 4787 1 532 . 1 1 64 64 SER C C 13 174.8 0.1 . 1 . . . . . . . . 4787 1 533 . 1 1 65 65 LEU N N 15 120.5 0.1 . 1 . . . . . . . . 4787 1 534 . 1 1 65 65 LEU H H 1 7.17 0.02 . 1 . . . . . . . . 4787 1 535 . 1 1 65 65 LEU CA C 13 55.4 0.1 . 1 . . . . . . . . 4787 1 536 . 1 1 65 65 LEU HA H 1 4.18 0.02 . 1 . . . . . . . . 4787 1 537 . 1 1 65 65 LEU CB C 13 39.5 0.1 . 1 . . . . . . . . 4787 1 538 . 1 1 65 65 LEU HB2 H 1 1.83 0.02 . 1 . . . . . . . . 4787 1 539 . 1 1 65 65 LEU HB3 H 1 1.83 0.02 . 1 . . . . . . . . 4787 1 540 . 1 1 65 65 LEU CG C 13 27.7 0.1 . 1 . . . . . . . . 4787 1 541 . 1 1 65 65 LEU HG H 1 1.61 0.02 . 1 . . . . . . . . 4787 1 542 . 1 1 65 65 LEU HD11 H 1 0.89 0.02 . 2 . . . . . . . . 4787 1 543 . 1 1 65 65 LEU HD12 H 1 0.89 0.02 . 2 . . . . . . . . 4787 1 544 . 1 1 65 65 LEU HD13 H 1 0.89 0.02 . 2 . . . . . . . . 4787 1 545 . 1 1 65 65 LEU HD21 H 1 0.85 0.02 . 2 . . . . . . . . 4787 1 546 . 1 1 65 65 LEU HD22 H 1 0.85 0.02 . 2 . . . . . . . . 4787 1 547 . 1 1 65 65 LEU HD23 H 1 0.85 0.02 . 2 . . . . . . . . 4787 1 548 . 1 1 65 65 LEU CD1 C 13 23.9 0.1 . 1 . . . . . . . . 4787 1 549 . 1 1 65 65 LEU C C 13 178.1 0.1 . 1 . . . . . . . . 4787 1 550 . 1 1 66 66 LYS N N 15 119.2 0.1 . 1 . . . . . . . . 4787 1 551 . 1 1 66 66 LYS H H 1 8.03 0.02 . 1 . . . . . . . . 4787 1 552 . 1 1 66 66 LYS CA C 13 55.8 0.1 . 1 . . . . . . . . 4787 1 553 . 1 1 66 66 LYS HA H 1 4.18 0.02 . 1 . . . . . . . . 4787 1 554 . 1 1 66 66 LYS CB C 13 33.1 0.1 . 1 . . . . . . . . 4787 1 555 . 1 1 66 66 LYS HB2 H 1 1.85 0.02 . 1 . . . . . . . . 4787 1 556 . 1 1 66 66 LYS HB3 H 1 1.85 0.02 . 1 . . . . . . . . 4787 1 557 . 1 1 66 66 LYS CG C 13 24.1 0.1 . 1 . . . . . . . . 4787 1 558 . 1 1 66 66 LYS HG2 H 1 1.44 0.02 . 1 . . . . . . . . 4787 1 559 . 1 1 66 66 LYS HG3 H 1 1.44 0.02 . 1 . . . . . . . . 4787 1 560 . 1 1 66 66 LYS CD C 13 29.6 0.1 . 1 . . . . . . . . 4787 1 561 . 1 1 66 66 LYS HD2 H 1 1.69 0.02 . 1 . . . . . . . . 4787 1 562 . 1 1 66 66 LYS HD3 H 1 1.69 0.02 . 1 . . . . . . . . 4787 1 563 . 1 1 66 66 LYS C C 13 176.1 0.1 . 1 . . . . . . . . 4787 1 564 . 1 1 67 67 CYS N N 15 121.8 0.1 . 1 . . . . . . . . 4787 1 565 . 1 1 67 67 CYS H H 1 8.78 0.02 . 1 . . . . . . . . 4787 1 566 . 1 1 67 67 CYS CA C 13 52.7 0.1 . 1 . . . . . . . . 4787 1 567 . 1 1 67 67 CYS HA H 1 5.08 0.02 . 1 . . . . . . . . 4787 1 568 . 1 1 67 67 CYS CB C 13 39.4 0.1 . 1 . . . . . . . . 4787 1 569 . 1 1 67 67 CYS HB2 H 1 3.43 0.02 . 2 . . . . . . . . 4787 1 570 . 1 1 67 67 CYS HB3 H 1 2.86 0.02 . 2 . . . . . . . . 4787 1 571 . 1 1 68 68 PRO CA C 13 64.2 0.1 . 1 . . . . . . . . 4787 1 572 . 1 1 68 68 PRO HA H 1 4.65 0.02 . 1 . . . . . . . . 4787 1 573 . 1 1 68 68 PRO CB C 13 31.8 0.1 . 1 . . . . . . . . 4787 1 574 . 1 1 68 68 PRO HB2 H 1 2.36 0.02 . 1 . . . . . . . . 4787 1 575 . 1 1 68 68 PRO HB3 H 1 2.36 0.02 . 1 . . . . . . . . 4787 1 576 . 1 1 68 68 PRO CG C 13 26.8 0.1 . 1 . . . . . . . . 4787 1 577 . 1 1 68 68 PRO HG2 H 1 2.07 0.02 . 1 . . . . . . . . 4787 1 578 . 1 1 68 68 PRO HG3 H 1 2.07 0.02 . 1 . . . . . . . . 4787 1 579 . 1 1 68 68 PRO HD2 H 1 3.77 0.02 . 2 . . . . . . . . 4787 1 580 . 1 1 68 68 PRO HD3 H 1 4.10 0.02 . 2 . . . . . . . . 4787 1 581 . 1 1 68 68 PRO C C 13 174.6 0.1 . 1 . . . . . . . . 4787 1 582 . 1 1 69 69 CYS N N 15 116.2 0.1 . 1 . . . . . . . . 4787 1 583 . 1 1 69 69 CYS H H 1 7.69 0.02 . 1 . . . . . . . . 4787 1 584 . 1 1 69 69 CYS CA C 13 55.2 0.1 . 1 . . . . . . . . 4787 1 585 . 1 1 69 69 CYS HA H 1 5.08 0.02 . 1 . . . . . . . . 4787 1 586 . 1 1 69 69 CYS CB C 13 39.0 0.1 . 1 . . . . . . . . 4787 1 587 . 1 1 69 69 CYS HB2 H 1 3.49 0.02 . 2 . . . . . . . . 4787 1 588 . 1 1 69 69 CYS HB3 H 1 3.19 0.02 . 2 . . . . . . . . 4787 1 589 . 1 1 69 69 CYS C C 13 172.3 0.1 . 1 . . . . . . . . 4787 1 590 . 1 1 70 70 ASP N N 15 119.4 0.1 . 1 . . . . . . . . 4787 1 591 . 1 1 70 70 ASP H H 1 8.39 0.02 . 1 . . . . . . . . 4787 1 592 . 1 1 70 70 ASP CA C 13 53.6 0.1 . 1 . . . . . . . . 4787 1 593 . 1 1 70 70 ASP HA H 1 4.79 0.02 . 1 . . . . . . . . 4787 1 594 . 1 1 70 70 ASP CB C 13 39.0 0.1 . 1 . . . . . . . . 4787 1 595 . 1 1 70 70 ASP HB2 H 1 2.82 0.02 . 1 . . . . . . . . 4787 1 596 . 1 1 70 70 ASP HB3 H 1 2.82 0.02 . 1 . . . . . . . . 4787 1 597 . 1 1 71 71 PRO CA C 13 62.8 0.1 . 1 . . . . . . . . 4787 1 598 . 1 1 71 71 PRO HA H 1 4.38 0.02 . 1 . . . . . . . . 4787 1 599 . 1 1 71 71 PRO CB C 13 33.7 0.1 . 1 . . . . . . . . 4787 1 600 . 1 1 71 71 PRO HB2 H 1 2.66 0.02 . 1 . . . . . . . . 4787 1 601 . 1 1 71 71 PRO HB3 H 1 2.66 0.02 . 1 . . . . . . . . 4787 1 602 . 1 1 71 71 PRO CG C 13 27.1 0.1 . 1 . . . . . . . . 4787 1 603 . 1 1 71 71 PRO HD2 H 1 3.85 0.02 . 1 . . . . . . . . 4787 1 604 . 1 1 71 71 PRO HD3 H 1 3.85 0.02 . 1 . . . . . . . . 4787 1 605 . 1 1 71 71 PRO C C 13 175.7 0.1 . 1 . . . . . . . . 4787 1 606 . 1 1 72 72 GLU N N 15 122.0 0.1 . 1 . . . . . . . . 4787 1 607 . 1 1 72 72 GLU H H 1 8.91 0.02 . 1 . . . . . . . . 4787 1 608 . 1 1 72 72 GLU CA C 13 54.8 0.1 . 1 . . . . . . . . 4787 1 609 . 1 1 72 72 GLU HA H 1 4.69 0.02 . 1 . . . . . . . . 4787 1 610 . 1 1 72 72 GLU CB C 13 31.0 0.1 . 1 . . . . . . . . 4787 1 611 . 1 1 72 72 GLU HB2 H 1 2.15 0.02 . 1 . . . . . . . . 4787 1 612 . 1 1 72 72 GLU HB3 H 1 2.15 0.02 . 1 . . . . . . . . 4787 1 613 . 1 1 72 72 GLU CG C 13 32.8 0.1 . 1 . . . . . . . . 4787 1 614 . 1 1 72 72 GLU HG2 H 1 2.47 0.02 . 1 . . . . . . . . 4787 1 615 . 1 1 72 72 GLU HG3 H 1 2.47 0.02 . 1 . . . . . . . . 4787 1 616 . 1 1 72 72 GLU C C 13 175.0 0.1 . 1 . . . . . . . . 4787 1 617 . 1 1 73 73 MET N N 15 125.7 0.1 . 1 . . . . . . . . 4787 1 618 . 1 1 73 73 MET H H 1 8.94 0.02 . 1 . . . . . . . . 4787 1 619 . 1 1 73 73 MET CA C 13 55.2 0.1 . 1 . . . . . . . . 4787 1 620 . 1 1 73 73 MET HA H 1 4.67 0.02 . 1 . . . . . . . . 4787 1 621 . 1 1 73 73 MET CB C 13 34.5 0.1 . 1 . . . . . . . . 4787 1 622 . 1 1 73 73 MET HB2 H 1 2.14 0.02 . 1 . . . . . . . . 4787 1 623 . 1 1 73 73 MET HB3 H 1 2.14 0.02 . 1 . . . . . . . . 4787 1 624 . 1 1 73 73 MET CG C 13 33.8 0.1 . 1 . . . . . . . . 4787 1 625 . 1 1 73 73 MET HG2 H 1 2.64 0.02 . 2 . . . . . . . . 4787 1 626 . 1 1 73 73 MET HG3 H 1 2.44 0.02 . 2 . . . . . . . . 4787 1 627 . 1 1 73 73 MET HE1 H 1 1.91 0.02 . 1 . . . . . . . . 4787 1 628 . 1 1 73 73 MET HE2 H 1 1.91 0.02 . 1 . . . . . . . . 4787 1 629 . 1 1 73 73 MET HE3 H 1 1.91 0.02 . 1 . . . . . . . . 4787 1 630 . 1 1 73 73 MET CE C 13 16.1 0.1 . 1 . . . . . . . . 4787 1 631 . 1 1 73 73 MET C C 13 175.4 0.1 . 1 . . . . . . . . 4787 1 632 . 1 1 74 74 VAL N N 15 128.3 0.1 . 1 . . . . . . . . 4787 1 633 . 1 1 74 74 VAL H H 1 8.92 0.02 . 1 . . . . . . . . 4787 1 634 . 1 1 74 74 VAL CA C 13 61.2 0.1 . 1 . . . . . . . . 4787 1 635 . 1 1 74 74 VAL HA H 1 4.30 0.02 . 1 . . . . . . . . 4787 1 636 . 1 1 74 74 VAL CB C 13 33.2 0.1 . 1 . . . . . . . . 4787 1 637 . 1 1 74 74 VAL HB H 1 1.49 0.02 . 1 . . . . . . . . 4787 1 638 . 1 1 74 74 VAL HG11 H 1 0.98 0.02 . 2 . . . . . . . . 4787 1 639 . 1 1 74 74 VAL HG12 H 1 0.98 0.02 . 2 . . . . . . . . 4787 1 640 . 1 1 74 74 VAL HG13 H 1 0.98 0.02 . 2 . . . . . . . . 4787 1 641 . 1 1 74 74 VAL HG21 H 1 0.80 0.02 . 2 . . . . . . . . 4787 1 642 . 1 1 74 74 VAL HG22 H 1 0.80 0.02 . 2 . . . . . . . . 4787 1 643 . 1 1 74 74 VAL HG23 H 1 0.80 0.02 . 2 . . . . . . . . 4787 1 644 . 1 1 74 74 VAL CG1 C 13 20.2 0.1 . 1 . . . . . . . . 4787 1 645 . 1 1 74 74 VAL C C 13 176.4 0.1 . 1 . . . . . . . . 4787 1 646 . 1 1 75 75 SER N N 15 117.8 0.1 . 1 . . . . . . . . 4787 1 647 . 1 1 75 75 SER H H 1 8.40 0.02 . 1 . . . . . . . . 4787 1 648 . 1 1 75 75 SER CA C 13 62.3 0.1 . 1 . . . . . . . . 4787 1 649 . 1 1 75 75 SER HA H 1 5.30 0.02 . 1 . . . . . . . . 4787 1 650 . 1 1 75 75 SER HB2 H 1 3.87 0.02 . 2 . . . . . . . . 4787 1 651 . 1 1 75 75 SER HB3 H 1 3.76 0.02 . 2 . . . . . . . . 4787 1 652 . 1 1 75 75 SER C C 13 173.8 0.1 . 1 . . . . . . . . 4787 1 653 . 1 1 76 76 ASN ND2 N 15 109.5 0.1 . 1 . . . . . . . . 4787 1 654 . 1 1 76 76 ASN HD21 H 1 5.95 0.02 . 2 . . . . . . . . 4787 1 655 . 1 1 76 76 ASN HD22 H 1 7.06 0.02 . 2 . . . . . . . . 4787 1 656 . 1 1 77 77 SER N N 15 114.3 0.1 . 1 . . . . . . . . 4787 1 657 . 1 1 77 77 SER H H 1 8.54 0.02 . 1 . . . . . . . . 4787 1 658 . 1 1 77 77 SER CA C 13 61.2 0.1 . 1 . . . . . . . . 4787 1 659 . 1 1 77 77 SER HA H 1 4.81 0.02 . 1 . . . . . . . . 4787 1 660 . 1 1 77 77 SER CB C 13 62.0 0.1 . 1 . . . . . . . . 4787 1 661 . 1 1 77 77 SER HB2 H 1 4.10 0.02 . 1 . . . . . . . . 4787 1 662 . 1 1 77 77 SER HB3 H 1 4.10 0.02 . 1 . . . . . . . . 4787 1 663 . 1 1 77 77 SER C C 13 175.4 0.1 . 1 . . . . . . . . 4787 1 664 . 1 1 78 78 THR N N 15 112.3 0.1 . 1 . . . . . . . . 4787 1 665 . 1 1 78 78 THR H H 1 7.95 0.02 . 1 . . . . . . . . 4787 1 666 . 1 1 78 78 THR CA C 13 62.8 0.1 . 1 . . . . . . . . 4787 1 667 . 1 1 78 78 THR HA H 1 4.44 0.02 . 1 . . . . . . . . 4787 1 668 . 1 1 78 78 THR CB C 13 69.2 0.1 . 1 . . . . . . . . 4787 1 669 . 1 1 78 78 THR HB H 1 4.40 0.02 . 1 . . . . . . . . 4787 1 670 . 1 1 78 78 THR HG21 H 1 1.26 0.02 . 1 . . . . . . . . 4787 1 671 . 1 1 78 78 THR HG22 H 1 1.26 0.02 . 1 . . . . . . . . 4787 1 672 . 1 1 78 78 THR HG23 H 1 1.26 0.02 . 1 . . . . . . . . 4787 1 673 . 1 1 78 78 THR C C 13 174.2 0.1 . 1 . . . . . . . . 4787 1 674 . 1 1 79 79 CYS N N 15 120.3 0.1 . 1 . . . . . . . . 4787 1 675 . 1 1 79 79 CYS H H 1 8.34 0.02 . 1 . . . . . . . . 4787 1 676 . 1 1 79 79 CYS CA C 13 54.3 0.1 . 1 . . . . . . . . 4787 1 677 . 1 1 79 79 CYS HA H 1 4.95 0.02 . 1 . . . . . . . . 4787 1 678 . 1 1 79 79 CYS CB C 13 39.0 0.1 . 1 . . . . . . . . 4787 1 679 . 1 1 79 79 CYS HB2 H 1 3.13 0.02 . 2 . . . . . . . . 4787 1 680 . 1 1 79 79 CYS HB3 H 1 2.92 0.02 . 2 . . . . . . . . 4787 1 681 . 1 1 79 79 CYS C C 13 172.4 0.1 . 1 . . . . . . . . 4787 1 682 . 1 1 80 80 ARG N N 15 122.4 0.1 . 1 . . . . . . . . 4787 1 683 . 1 1 80 80 ARG H H 1 8.33 0.02 . 1 . . . . . . . . 4787 1 684 . 1 1 80 80 ARG CA C 13 55.4 0.1 . 1 . . . . . . . . 4787 1 685 . 1 1 80 80 ARG HA H 1 4.97 0.02 . 1 . . . . . . . . 4787 1 686 . 1 1 80 80 ARG CB C 13 29.8 0.1 . 1 . . . . . . . . 4787 1 687 . 1 1 80 80 ARG HB2 H 1 1.71 0.02 . 1 . . . . . . . . 4787 1 688 . 1 1 80 80 ARG HB3 H 1 1.71 0.02 . 1 . . . . . . . . 4787 1 689 . 1 1 80 80 ARG CG C 13 26.8 0.1 . 1 . . . . . . . . 4787 1 690 . 1 1 80 80 ARG HG2 H 1 1.49 0.02 . 1 . . . . . . . . 4787 1 691 . 1 1 80 80 ARG HG3 H 1 1.49 0.02 . 1 . . . . . . . . 4787 1 692 . 1 1 80 80 ARG HE H 1 7.25 0.02 . 1 . . . . . . . . 4787 1 693 . 1 1 80 80 ARG C C 13 174.0 0.1 . 1 . . . . . . . . 4787 1 694 . 1 1 81 81 PHE N N 15 121.1 0.1 . 1 . . . . . . . . 4787 1 695 . 1 1 81 81 PHE H H 1 8.78 0.02 . 1 . . . . . . . . 4787 1 696 . 1 1 81 81 PHE CA C 13 56.6 0.1 . 1 . . . . . . . . 4787 1 697 . 1 1 81 81 PHE HA H 1 4.99 0.02 . 1 . . . . . . . . 4787 1 698 . 1 1 81 81 PHE CB C 13 42.3 0.1 . 1 . . . . . . . . 4787 1 699 . 1 1 81 81 PHE HB2 H 1 3.21 0.02 . 2 . . . . . . . . 4787 1 700 . 1 1 81 81 PHE HB3 H 1 2.69 0.02 . 2 . . . . . . . . 4787 1 701 . 1 1 81 81 PHE HD1 H 1 7.01 0.02 . 1 . . . . . . . . 4787 1 702 . 1 1 81 81 PHE HD2 H 1 7.01 0.02 . 1 . . . . . . . . 4787 1 703 . 1 1 81 81 PHE HE1 H 1 7.41 0.02 . 1 . . . . . . . . 4787 1 704 . 1 1 81 81 PHE HE2 H 1 7.41 0.02 . 1 . . . . . . . . 4787 1 705 . 1 1 81 81 PHE C C 13 171.9 0.1 . 1 . . . . . . . . 4787 1 706 . 1 1 82 82 PHE N N 15 117.6 0.1 . 1 . . . . . . . . 4787 1 707 . 1 1 82 82 PHE H H 1 9.23 0.02 . 1 . . . . . . . . 4787 1 708 . 1 1 82 82 PHE CA C 13 56.8 0.1 . 1 . . . . . . . . 4787 1 709 . 1 1 82 82 PHE HA H 1 5.48 0.02 . 1 . . . . . . . . 4787 1 710 . 1 1 82 82 PHE CB C 13 42.4 0.1 . 1 . . . . . . . . 4787 1 711 . 1 1 82 82 PHE HB2 H 1 3.22 0.02 . 2 . . . . . . . . 4787 1 712 . 1 1 82 82 PHE HB3 H 1 2.77 0.02 . 2 . . . . . . . . 4787 1 713 . 1 1 82 82 PHE HD1 H 1 7.01 0.02 . 1 . . . . . . . . 4787 1 714 . 1 1 82 82 PHE HD2 H 1 7.01 0.02 . 1 . . . . . . . . 4787 1 715 . 1 1 82 82 PHE HE1 H 1 7.40 0.02 . 1 . . . . . . . . 4787 1 716 . 1 1 82 82 PHE HE2 H 1 7.40 0.02 . 1 . . . . . . . . 4787 1 717 . 1 1 82 82 PHE HZ H 1 7.44 0.02 . 1 . . . . . . . . 4787 1 718 . 1 1 82 82 PHE C C 13 174.7 0.1 . 1 . . . . . . . . 4787 1 719 . 1 1 83 83 VAL N N 15 119.7 0.1 . 1 . . . . . . . . 4787 1 720 . 1 1 83 83 VAL H H 1 9.40 0.02 . 1 . . . . . . . . 4787 1 721 . 1 1 83 83 VAL CA C 13 60.1 0.1 . 1 . . . . . . . . 4787 1 722 . 1 1 83 83 VAL HA H 1 5.14 0.02 . 1 . . . . . . . . 4787 1 723 . 1 1 83 83 VAL CB C 13 35.4 0.1 . 1 . . . . . . . . 4787 1 724 . 1 1 83 83 VAL HB H 1 2.11 0.02 . 1 . . . . . . . . 4787 1 725 . 1 1 83 83 VAL HG11 H 1 0.97 0.02 . 2 . . . . . . . . 4787 1 726 . 1 1 83 83 VAL HG12 H 1 0.97 0.02 . 2 . . . . . . . . 4787 1 727 . 1 1 83 83 VAL HG13 H 1 0.97 0.02 . 2 . . . . . . . . 4787 1 728 . 1 1 83 83 VAL HG21 H 1 0.81 0.02 . 2 . . . . . . . . 4787 1 729 . 1 1 83 83 VAL HG22 H 1 0.81 0.02 . 2 . . . . . . . . 4787 1 730 . 1 1 83 83 VAL HG23 H 1 0.81 0.02 . 2 . . . . . . . . 4787 1 731 . 1 1 83 83 VAL CG1 C 13 20.8 0.1 . 1 . . . . . . . . 4787 1 732 . 1 1 83 83 VAL C C 13 175.0 0.1 . 1 . . . . . . . . 4787 1 733 . 1 1 84 84 CYS N N 15 125.7 0.1 . 1 . . . . . . . . 4787 1 734 . 1 1 84 84 CYS H H 1 9.35 0.02 . 1 . . . . . . . . 4787 1 735 . 1 1 84 84 CYS CA C 13 54.1 0.1 . 1 . . . . . . . . 4787 1 736 . 1 1 84 84 CYS HA H 1 5.12 0.02 . 1 . . . . . . . . 4787 1 737 . 1 1 84 84 CYS CB C 13 38.6 0.1 . 1 . . . . . . . . 4787 1 738 . 1 1 84 84 CYS HB2 H 1 3.24 0.02 . 2 . . . . . . . . 4787 1 739 . 1 1 84 84 CYS HB3 H 1 2.79 0.02 . 2 . . . . . . . . 4787 1 740 . 1 1 84 84 CYS C C 13 172.6 0.1 . 1 . . . . . . . . 4787 1 741 . 1 1 85 85 LYS N N 15 129.4 0.1 . 1 . . . . . . . . 4787 1 742 . 1 1 85 85 LYS H H 1 8.78 0.02 . 1 . . . . . . . . 4787 1 743 . 1 1 85 85 LYS CA C 13 55.7 0.1 . 1 . . . . . . . . 4787 1 744 . 1 1 85 85 LYS HA H 1 4.71 0.02 . 1 . . . . . . . . 4787 1 745 . 1 1 85 85 LYS CB C 13 31.4 0.1 . 1 . . . . . . . . 4787 1 746 . 1 1 85 85 LYS HB2 H 1 1.90 0.02 . 1 . . . . . . . . 4787 1 747 . 1 1 85 85 LYS HB3 H 1 1.90 0.02 . 1 . . . . . . . . 4787 1 748 . 1 1 85 85 LYS CG C 13 26.5 0.1 . 1 . . . . . . . . 4787 1 749 . 1 1 85 85 LYS HD2 H 1 1.64 0.02 . 1 . . . . . . . . 4787 1 750 . 1 1 85 85 LYS HD3 H 1 1.64 0.02 . 1 . . . . . . . . 4787 1 751 . 1 1 85 85 LYS C C 13 175.0 0.1 . 1 . . . . . . . . 4787 1 752 . 1 1 86 86 CYS N N 15 122.2 0.1 . 1 . . . . . . . . 4787 1 753 . 1 1 86 86 CYS H H 1 8.48 0.02 . 1 . . . . . . . . 4787 1 754 . 1 1 86 86 CYS CA C 13 53.2 0.1 . 1 . . . . . . . . 4787 1 755 . 1 1 86 86 CYS HA H 1 5.13 0.02 . 1 . . . . . . . . 4787 1 756 . 1 1 86 86 CYS CB C 13 38.9 0.1 . 1 . . . . . . . . 4787 1 757 . 1 1 86 86 CYS HB2 H 1 3.30 0.02 . 2 . . . . . . . . 4787 1 758 . 1 1 86 86 CYS HB3 H 1 3.00 0.02 . 2 . . . . . . . . 4787 1 759 . 1 1 86 86 CYS C C 13 172.4 0.1 . 1 . . . . . . . . 4787 1 760 . 1 1 87 87 VAL N N 15 121.6 0.1 . 1 . . . . . . . . 4787 1 761 . 1 1 87 87 VAL H H 1 8.36 0.02 . 1 . . . . . . . . 4787 1 762 . 1 1 87 87 VAL CA C 13 62.2 0.1 . 1 . . . . . . . . 4787 1 763 . 1 1 87 87 VAL HA H 1 4.49 0.02 . 1 . . . . . . . . 4787 1 764 . 1 1 87 87 VAL CB C 13 33.2 0.1 . 1 . . . . . . . . 4787 1 765 . 1 1 87 87 VAL HB H 1 2.17 0.02 . 1 . . . . . . . . 4787 1 766 . 1 1 87 87 VAL HG11 H 1 1.02 0.02 . 2 . . . . . . . . 4787 1 767 . 1 1 87 87 VAL HG12 H 1 1.02 0.02 . 2 . . . . . . . . 4787 1 768 . 1 1 87 87 VAL HG13 H 1 1.02 0.02 . 2 . . . . . . . . 4787 1 769 . 1 1 87 87 VAL HG21 H 1 0.99 0.02 . 2 . . . . . . . . 4787 1 770 . 1 1 87 87 VAL HG22 H 1 0.99 0.02 . 2 . . . . . . . . 4787 1 771 . 1 1 87 87 VAL HG23 H 1 0.99 0.02 . 2 . . . . . . . . 4787 1 772 . 1 1 87 87 VAL CG1 C 13 20.2 0.1 . 1 . . . . . . . . 4787 1 773 . 1 1 87 87 VAL C C 13 175.7 0.1 . 1 . . . . . . . . 4787 1 774 . 1 1 88 88 GLU N N 15 124.3 0.1 . 1 . . . . . . . . 4787 1 775 . 1 1 88 88 GLU H H 1 8.58 0.02 . 1 . . . . . . . . 4787 1 776 . 1 1 88 88 GLU CA C 13 55.9 0.1 . 1 . . . . . . . . 4787 1 777 . 1 1 88 88 GLU HA H 1 4.28 0.02 . 1 . . . . . . . . 4787 1 778 . 1 1 88 88 GLU CB C 13 30.1 0.1 . 1 . . . . . . . . 4787 1 779 . 1 1 88 88 GLU HB2 H 1 2.10 0.02 . 1 . . . . . . . . 4787 1 780 . 1 1 88 88 GLU HB3 H 1 2.10 0.02 . 1 . . . . . . . . 4787 1 781 . 1 1 88 88 GLU CG C 13 33.4 0.1 . 1 . . . . . . . . 4787 1 782 . 1 1 88 88 GLU HG2 H 1 2.40 0.02 . 1 . . . . . . . . 4787 1 783 . 1 1 88 88 GLU HG3 H 1 2.40 0.02 . 1 . . . . . . . . 4787 1 784 . 1 1 88 88 GLU C C 13 175.8 0.1 . 1 . . . . . . . . 4787 1 785 . 1 1 89 89 ARG N N 15 123.2 0.1 . 1 . . . . . . . . 4787 1 786 . 1 1 89 89 ARG H H 1 8.53 0.02 . 1 . . . . . . . . 4787 1 787 . 1 1 89 89 ARG CA C 13 56.0 0.1 . 1 . . . . . . . . 4787 1 788 . 1 1 89 89 ARG HA H 1 4.48 0.02 . 1 . . . . . . . . 4787 1 789 . 1 1 89 89 ARG CB C 13 30.1 0.1 . 1 . . . . . . . . 4787 1 790 . 1 1 89 89 ARG HB2 H 1 1.87 0.02 . 1 . . . . . . . . 4787 1 791 . 1 1 89 89 ARG HB3 H 1 1.87 0.02 . 1 . . . . . . . . 4787 1 792 . 1 1 89 89 ARG CG C 13 26.4 0.1 . 1 . . . . . . . . 4787 1 793 . 1 1 89 89 ARG HG2 H 1 1.71 0.02 . 1 . . . . . . . . 4787 1 794 . 1 1 89 89 ARG HG3 H 1 1.71 0.02 . 1 . . . . . . . . 4787 1 795 . 1 1 89 89 ARG HD2 H 1 3.29 0.02 . 1 . . . . . . . . 4787 1 796 . 1 1 89 89 ARG HD3 H 1 3.29 0.02 . 1 . . . . . . . . 4787 1 797 . 1 1 89 89 ARG C C 13 176.0 0.1 . 1 . . . . . . . . 4787 1 798 . 1 1 90 90 ARG N N 15 122.9 0.1 . 1 . . . . . . . . 4787 1 799 . 1 1 90 90 ARG H H 1 8.49 0.02 . 1 . . . . . . . . 4787 1 800 . 1 1 90 90 ARG CA C 13 56.1 0.1 . 1 . . . . . . . . 4787 1 801 . 1 1 90 90 ARG HA H 1 4.43 0.02 . 1 . . . . . . . . 4787 1 802 . 1 1 90 90 ARG CB C 13 29.5 0.1 . 1 . . . . . . . . 4787 1 803 . 1 1 90 90 ARG HB2 H 1 1.89 0.02 . 1 . . . . . . . . 4787 1 804 . 1 1 90 90 ARG HB3 H 1 1.89 0.02 . 1 . . . . . . . . 4787 1 805 . 1 1 90 90 ARG CG C 13 26.4 0.1 . 1 . . . . . . . . 4787 1 806 . 1 1 90 90 ARG HG2 H 1 1.72 0.02 . 1 . . . . . . . . 4787 1 807 . 1 1 90 90 ARG HG3 H 1 1.72 0.02 . 1 . . . . . . . . 4787 1 808 . 1 1 90 90 ARG HD2 H 1 3.28 0.02 . 1 . . . . . . . . 4787 1 809 . 1 1 90 90 ARG HD3 H 1 3.28 0.02 . 1 . . . . . . . . 4787 1 810 . 1 1 90 90 ARG C C 13 175.8 0.1 . 1 . . . . . . . . 4787 1 811 . 1 1 91 91 ALA N N 15 125.9 0.1 . 1 . . . . . . . . 4787 1 812 . 1 1 91 91 ALA H H 1 8.47 0.02 . 1 . . . . . . . . 4787 1 813 . 1 1 91 91 ALA CA C 13 52.3 0.1 . 1 . . . . . . . . 4787 1 814 . 1 1 91 91 ALA HA H 1 4.41 0.02 . 1 . . . . . . . . 4787 1 815 . 1 1 91 91 ALA HB1 H 1 1.46 0.02 . 1 . . . . . . . . 4787 1 816 . 1 1 91 91 ALA HB2 H 1 1.46 0.02 . 1 . . . . . . . . 4787 1 817 . 1 1 91 91 ALA HB3 H 1 1.46 0.02 . 1 . . . . . . . . 4787 1 818 . 1 1 91 91 ALA CB C 13 20.3 0.1 . 1 . . . . . . . . 4787 1 819 . 1 1 91 91 ALA C C 13 177.4 0.1 . 1 . . . . . . . . 4787 1 820 . 1 1 92 92 GLU N N 15 120.1 0.1 . 1 . . . . . . . . 4787 1 821 . 1 1 92 92 GLU H H 1 8.42 0.02 . 1 . . . . . . . . 4787 1 822 . 1 1 92 92 GLU CA C 13 56.2 0.1 . 1 . . . . . . . . 4787 1 823 . 1 1 92 92 GLU HA H 1 4.45 0.02 . 1 . . . . . . . . 4787 1 824 . 1 1 92 92 GLU CB C 13 29.8 0.1 . 1 . . . . . . . . 4787 1 825 . 1 1 92 92 GLU HB2 H 1 2.10 0.02 . 1 . . . . . . . . 4787 1 826 . 1 1 92 92 GLU HB3 H 1 2.10 0.02 . 1 . . . . . . . . 4787 1 827 . 1 1 92 92 GLU CG C 13 32.8 0.1 . 1 . . . . . . . . 4787 1 828 . 1 1 92 92 GLU HG2 H 1 2.49 0.02 . 1 . . . . . . . . 4787 1 829 . 1 1 92 92 GLU HG3 H 1 2.49 0.02 . 1 . . . . . . . . 4787 1 830 . 1 1 92 92 GLU C C 13 176.0 0.1 . 1 . . . . . . . . 4787 1 831 . 1 1 93 93 VAL N N 15 121.8 0.1 . 1 . . . . . . . . 4787 1 832 . 1 1 93 93 VAL H H 1 8.20 0.02 . 1 . . . . . . . . 4787 1 833 . 1 1 93 93 VAL CA C 13 62.4 0.1 . 1 . . . . . . . . 4787 1 834 . 1 1 93 93 VAL HA H 1 4.15 0.02 . 1 . . . . . . . . 4787 1 835 . 1 1 93 93 VAL CB C 13 33.2 0.1 . 1 . . . . . . . . 4787 1 836 . 1 1 93 93 VAL HB H 1 2.13 0.02 . 1 . . . . . . . . 4787 1 837 . 1 1 93 93 VAL HG11 H 1 1.00 0.02 . 1 . . . . . . . . 4787 1 838 . 1 1 93 93 VAL HG12 H 1 1.00 0.02 . 1 . . . . . . . . 4787 1 839 . 1 1 93 93 VAL HG13 H 1 1.00 0.02 . 1 . . . . . . . . 4787 1 840 . 1 1 93 93 VAL HG21 H 1 1.00 0.02 . 1 . . . . . . . . 4787 1 841 . 1 1 93 93 VAL HG22 H 1 1.00 0.02 . 1 . . . . . . . . 4787 1 842 . 1 1 93 93 VAL HG23 H 1 1.00 0.02 . 1 . . . . . . . . 4787 1 843 . 1 1 93 93 VAL CG1 C 13 20.1 0.1 . 1 . . . . . . . . 4787 1 844 . 1 1 93 93 VAL C C 13 176.4 0.1 . 1 . . . . . . . . 4787 1 845 . 1 1 94 94 THR N N 15 117.8 0.1 . 1 . . . . . . . . 4787 1 846 . 1 1 94 94 THR H H 1 8.39 0.02 . 1 . . . . . . . . 4787 1 847 . 1 1 94 94 THR CA C 13 61.7 0.1 . 1 . . . . . . . . 4787 1 848 . 1 1 94 94 THR HA H 1 4.55 0.02 . 1 . . . . . . . . 4787 1 849 . 1 1 94 94 THR CB C 13 68.9 0.1 . 1 . . . . . . . . 4787 1 850 . 1 1 94 94 THR HB H 1 4.32 0.02 . 1 . . . . . . . . 4787 1 851 . 1 1 94 94 THR HG21 H 1 1.29 0.02 . 1 . . . . . . . . 4787 1 852 . 1 1 94 94 THR HG22 H 1 1.29 0.02 . 1 . . . . . . . . 4787 1 853 . 1 1 94 94 THR HG23 H 1 1.29 0.02 . 1 . . . . . . . . 4787 1 854 . 1 1 94 94 THR CG2 C 13 21.2 0.1 . 1 . . . . . . . . 4787 1 855 . 1 1 94 94 THR C C 13 174.6 0.1 . 1 . . . . . . . . 4787 1 856 . 1 1 95 95 SER N N 15 117.9 0.1 . 1 . . . . . . . . 4787 1 857 . 1 1 95 95 SER H H 1 8.41 0.02 . 1 . . . . . . . . 4787 1 858 . 1 1 95 95 SER CA C 13 58.3 0.1 . 1 . . . . . . . . 4787 1 859 . 1 1 95 95 SER HA H 1 4.56 0.02 . 1 . . . . . . . . 4787 1 860 . 1 1 95 95 SER CB C 13 63.1 0.1 . 1 . . . . . . . . 4787 1 861 . 1 1 95 95 SER HB2 H 1 3.96 0.02 . 1 . . . . . . . . 4787 1 862 . 1 1 95 95 SER HB3 H 1 3.96 0.02 . 1 . . . . . . . . 4787 1 863 . 1 1 95 95 SER C C 13 174.4 0.1 . 1 . . . . . . . . 4787 1 864 . 1 1 96 96 ASN N N 15 120.9 0.1 . 1 . . . . . . . . 4787 1 865 . 1 1 96 96 ASN H H 1 8.58 0.02 . 1 . . . . . . . . 4787 1 866 . 1 1 96 96 ASN CA C 13 53.6 0.1 . 1 . . . . . . . . 4787 1 867 . 1 1 96 96 ASN HA H 1 4.81 0.02 . 1 . . . . . . . . 4787 1 868 . 1 1 96 96 ASN CB C 13 39.0 0.1 . 1 . . . . . . . . 4787 1 869 . 1 1 96 96 ASN HB2 H 1 2.88 0.02 . 1 . . . . . . . . 4787 1 870 . 1 1 96 96 ASN HB3 H 1 2.88 0.02 . 1 . . . . . . . . 4787 1 871 . 1 1 96 96 ASN HD22 H 1 6.91 0.02 . 2 . . . . . . . . 4787 1 872 . 1 1 96 96 ASN C C 13 174.9 0.1 . 1 . . . . . . . . 4787 1 873 . 1 1 97 97 ASN N N 15 119.7 0.1 . 1 . . . . . . . . 4787 1 874 . 1 1 97 97 ASN H H 1 8.40 0.02 . 1 . . . . . . . . 4787 1 875 . 1 1 97 97 ASN CA C 13 53.6 0.1 . 1 . . . . . . . . 4787 1 876 . 1 1 97 97 ASN HA H 1 4.76 0.02 . 1 . . . . . . . . 4787 1 877 . 1 1 97 97 ASN CB C 13 38.7 0.1 . 1 . . . . . . . . 4787 1 878 . 1 1 97 97 ASN HB2 H 1 2.88 0.02 . 1 . . . . . . . . 4787 1 879 . 1 1 97 97 ASN HB3 H 1 2.88 0.02 . 1 . . . . . . . . 4787 1 880 . 1 1 97 97 ASN HD21 H 1 6.99 0.02 . 2 . . . . . . . . 4787 1 881 . 1 1 97 97 ASN C C 13 175.0 0.1 . 1 . . . . . . . . 4787 1 882 . 1 1 98 98 GLU N N 15 120.4 0.1 . 1 . . . . . . . . 4787 1 883 . 1 1 98 98 GLU H H 1 8.29 0.02 . 1 . . . . . . . . 4787 1 884 . 1 1 98 98 GLU CA C 13 56.2 0.1 . 1 . . . . . . . . 4787 1 885 . 1 1 98 98 GLU HA H 1 4.45 0.02 . 1 . . . . . . . . 4787 1 886 . 1 1 98 98 GLU CB C 13 32.9 0.1 . 1 . . . . . . . . 4787 1 887 . 1 1 98 98 GLU HB2 H 1 2.50 0.02 . 2 . . . . . . . . 4787 1 888 . 1 1 98 98 GLU HB3 H 1 2.10 0.02 . 2 . . . . . . . . 4787 1 889 . 1 1 98 98 GLU CG C 13 37.9 0.1 . 1 . . . . . . . . 4787 1 890 . 1 1 98 98 GLU C C 13 176.1 0.1 . 1 . . . . . . . . 4787 1 891 . 1 1 99 99 VAL N N 15 124.7 0.1 . 1 . . . . . . . . 4787 1 892 . 1 1 99 99 VAL H H 1 8.29 0.02 . 1 . . . . . . . . 4787 1 893 . 1 1 99 99 VAL CA C 13 62.8 0.1 . 1 . . . . . . . . 4787 1 894 . 1 1 99 99 VAL HA H 1 4.16 0.02 . 1 . . . . . . . . 4787 1 895 . 1 1 99 99 VAL CB C 13 33.1 0.1 . 1 . . . . . . . . 4787 1 896 . 1 1 99 99 VAL HB H 1 2.10 0.02 . 1 . . . . . . . . 4787 1 897 . 1 1 99 99 VAL HG11 H 1 0.99 0.02 . 2 . . . . . . . . 4787 1 898 . 1 1 99 99 VAL HG12 H 1 0.99 0.02 . 2 . . . . . . . . 4787 1 899 . 1 1 99 99 VAL HG13 H 1 0.99 0.02 . 2 . . . . . . . . 4787 1 900 . 1 1 99 99 VAL HG21 H 1 0.97 0.02 . 2 . . . . . . . . 4787 1 901 . 1 1 99 99 VAL HG22 H 1 0.97 0.02 . 2 . . . . . . . . 4787 1 902 . 1 1 99 99 VAL HG23 H 1 0.97 0.02 . 2 . . . . . . . . 4787 1 903 . 1 1 99 99 VAL CG1 C 13 20.7 0.1 . 1 . . . . . . . . 4787 1 904 . 1 1 99 99 VAL C C 13 176.0 0.1 . 1 . . . . . . . . 4787 1 905 . 1 1 100 100 VAL N N 15 124.7 0.1 . 1 . . . . . . . . 4787 1 906 . 1 1 100 100 VAL H H 1 8.32 0.02 . 1 . . . . . . . . 4787 1 907 . 1 1 100 100 VAL CA C 13 62.7 0.1 . 1 . . . . . . . . 4787 1 908 . 1 1 100 100 VAL HA H 1 4.18 0.02 . 1 . . . . . . . . 4787 1 909 . 1 1 100 100 VAL CB C 13 33.1 0.1 . 1 . . . . . . . . 4787 1 910 . 1 1 100 100 VAL HB H 1 2.10 0.02 . 1 . . . . . . . . 4787 1 911 . 1 1 100 100 VAL HG11 H 1 0.96 0.02 . 2 . . . . . . . . 4787 1 912 . 1 1 100 100 VAL HG12 H 1 0.96 0.02 . 2 . . . . . . . . 4787 1 913 . 1 1 100 100 VAL HG13 H 1 0.96 0.02 . 2 . . . . . . . . 4787 1 914 . 1 1 100 100 VAL HG21 H 1 0.91 0.02 . 2 . . . . . . . . 4787 1 915 . 1 1 100 100 VAL HG22 H 1 0.91 0.02 . 2 . . . . . . . . 4787 1 916 . 1 1 100 100 VAL HG23 H 1 0.91 0.02 . 2 . . . . . . . . 4787 1 917 . 1 1 100 100 VAL CG1 C 13 20.5 0.1 . 1 . . . . . . . . 4787 1 918 . 1 1 100 100 VAL C C 13 176.0 0.1 . 1 . . . . . . . . 4787 1 919 . 1 1 101 101 VAL N N 15 124.9 0.1 . 1 . . . . . . . . 4787 1 920 . 1 1 101 101 VAL H H 1 8.33 0.02 . 1 . . . . . . . . 4787 1 921 . 1 1 101 101 VAL CA C 13 62.6 0.1 . 1 . . . . . . . . 4787 1 922 . 1 1 101 101 VAL HA H 1 4.18 0.02 . 1 . . . . . . . . 4787 1 923 . 1 1 101 101 VAL CB C 13 33.1 0.1 . 1 . . . . . . . . 4787 1 924 . 1 1 101 101 VAL HB H 1 2.13 0.02 . 1 . . . . . . . . 4787 1 925 . 1 1 101 101 VAL HG11 H 1 0.99 0.02 . 2 . . . . . . . . 4787 1 926 . 1 1 101 101 VAL HG12 H 1 0.99 0.02 . 2 . . . . . . . . 4787 1 927 . 1 1 101 101 VAL HG13 H 1 0.99 0.02 . 2 . . . . . . . . 4787 1 928 . 1 1 101 101 VAL HG21 H 1 0.97 0.02 . 2 . . . . . . . . 4787 1 929 . 1 1 101 101 VAL HG22 H 1 0.97 0.02 . 2 . . . . . . . . 4787 1 930 . 1 1 101 101 VAL HG23 H 1 0.97 0.02 . 2 . . . . . . . . 4787 1 931 . 1 1 101 101 VAL CG1 C 13 20.5 0.1 . 1 . . . . . . . . 4787 1 932 . 1 1 101 101 VAL C C 13 176.1 0.1 . 1 . . . . . . . . 4787 1 933 . 1 1 102 102 LYS N N 15 125.2 0.1 . 1 . . . . . . . . 4787 1 934 . 1 1 102 102 LYS H H 1 8.44 0.02 . 1 . . . . . . . . 4787 1 935 . 1 1 102 102 LYS CA C 13 56.5 0.1 . 1 . . . . . . . . 4787 1 936 . 1 1 102 102 LYS HA H 1 4.39 0.02 . 1 . . . . . . . . 4787 1 937 . 1 1 102 102 LYS CB C 13 33.4 0.1 . 1 . . . . . . . . 4787 1 938 . 1 1 102 102 LYS HB2 H 1 1.85 0.02 . 1 . . . . . . . . 4787 1 939 . 1 1 102 102 LYS HB3 H 1 1.85 0.02 . 1 . . . . . . . . 4787 1 940 . 1 1 102 102 LYS CG C 13 24.2 0.1 . 1 . . . . . . . . 4787 1 941 . 1 1 102 102 LYS HG2 H 1 1.50 0.02 . 1 . . . . . . . . 4787 1 942 . 1 1 102 102 LYS HG3 H 1 1.50 0.02 . 1 . . . . . . . . 4787 1 943 . 1 1 102 102 LYS HD2 H 1 1.80 0.02 . 1 . . . . . . . . 4787 1 944 . 1 1 102 102 LYS HD3 H 1 1.80 0.02 . 1 . . . . . . . . 4787 1 945 . 1 1 102 102 LYS HE2 H 1 3.00 0.02 . 1 . . . . . . . . 4787 1 946 . 1 1 102 102 LYS HE3 H 1 3.00 0.02 . 1 . . . . . . . . 4787 1 947 . 1 1 102 102 LYS C C 13 176.5 0.1 . 1 . . . . . . . . 4787 1 948 . 1 1 103 103 GLU N N 15 121.8 0.1 . 1 . . . . . . . . 4787 1 949 . 1 1 103 103 GLU H H 1 8.40 0.02 . 1 . . . . . . . . 4787 1 950 . 1 1 103 103 GLU CA C 13 55.9 0.1 . 1 . . . . . . . . 4787 1 951 . 1 1 103 103 GLU HA H 1 4.40 0.02 . 1 . . . . . . . . 4787 1 952 . 1 1 103 103 GLU CB C 13 30.0 0.1 . 1 . . . . . . . . 4787 1 953 . 1 1 103 103 GLU HB2 H 1 2.03 0.02 . 1 . . . . . . . . 4787 1 954 . 1 1 103 103 GLU HB3 H 1 2.03 0.02 . 1 . . . . . . . . 4787 1 955 . 1 1 103 103 GLU CG C 13 34.4 0.1 . 1 . . . . . . . . 4787 1 956 . 1 1 103 103 GLU HG2 H 1 2.43 0.02 . 1 . . . . . . . . 4787 1 957 . 1 1 103 103 GLU HG3 H 1 2.43 0.02 . 1 . . . . . . . . 4787 1 958 . 1 1 103 103 GLU C C 13 175.4 0.1 . 1 . . . . . . . . 4787 1 959 . 1 1 104 104 GLU N N 15 121.4 0.1 . 1 . . . . . . . . 4787 1 960 . 1 1 104 104 GLU H H 1 8.35 0.02 . 1 . . . . . . . . 4787 1 961 . 1 1 104 104 GLU CA C 13 56.3 0.1 . 1 . . . . . . . . 4787 1 962 . 1 1 104 104 GLU HA H 1 4.69 0.02 . 1 . . . . . . . . 4787 1 963 . 1 1 104 104 GLU CB C 13 29.2 0.1 . 1 . . . . . . . . 4787 1 964 . 1 1 104 104 GLU CG C 13 32.5 0.1 . 1 . . . . . . . . 4787 1 965 . 1 1 104 104 GLU C C 13 175.9 0.1 . 1 . . . . . . . . 4787 1 966 . 1 1 105 105 TYR N N 15 119.7 0.1 . 1 . . . . . . . . 4787 1 967 . 1 1 105 105 TYR H H 1 8.16 0.02 . 1 . . . . . . . . 4787 1 968 . 1 1 105 105 TYR CA C 13 57.6 0.1 . 1 . . . . . . . . 4787 1 969 . 1 1 105 105 TYR HA H 1 4.66 0.02 . 1 . . . . . . . . 4787 1 970 . 1 1 105 105 TYR CB C 13 38.9 0.1 . 1 . . . . . . . . 4787 1 971 . 1 1 105 105 TYR HB2 H 1 3.17 0.02 . 2 . . . . . . . . 4787 1 972 . 1 1 105 105 TYR HB3 H 1 2.94 0.02 . 2 . . . . . . . . 4787 1 973 . 1 1 105 105 TYR HD1 H 1 7.16 0.02 . 1 . . . . . . . . 4787 1 974 . 1 1 105 105 TYR HD2 H 1 7.16 0.02 . 1 . . . . . . . . 4787 1 975 . 1 1 105 105 TYR HE1 H 1 6.84 0.02 . 1 . . . . . . . . 4787 1 976 . 1 1 105 105 TYR HE2 H 1 6.84 0.02 . 1 . . . . . . . . 4787 1 977 . 1 1 105 105 TYR C C 13 175.9 0.1 . 1 . . . . . . . . 4787 1 978 . 1 1 106 106 LYS N N 15 122.5 0.1 . 1 . . . . . . . . 4787 1 979 . 1 1 106 106 LYS H H 1 8.25 0.02 . 1 . . . . . . . . 4787 1 980 . 1 1 106 106 LYS CA C 13 56.5 0.1 . 1 . . . . . . . . 4787 1 981 . 1 1 106 106 LYS HA H 1 4.31 0.02 . 1 . . . . . . . . 4787 1 982 . 1 1 106 106 LYS CB C 13 33.5 0.1 . 1 . . . . . . . . 4787 1 983 . 1 1 106 106 LYS HB2 H 1 1.83 0.02 . 1 . . . . . . . . 4787 1 984 . 1 1 106 106 LYS HB3 H 1 1.83 0.02 . 1 . . . . . . . . 4787 1 985 . 1 1 106 106 LYS CG C 13 24.1 0.1 . 1 . . . . . . . . 4787 1 986 . 1 1 106 106 LYS HG2 H 1 1.43 0.02 . 1 . . . . . . . . 4787 1 987 . 1 1 106 106 LYS HG3 H 1 1.43 0.02 . 1 . . . . . . . . 4787 1 988 . 1 1 106 106 LYS HD2 H 1 1.80 0.02 . 1 . . . . . . . . 4787 1 989 . 1 1 106 106 LYS HD3 H 1 1.80 0.02 . 1 . . . . . . . . 4787 1 990 . 1 1 106 106 LYS HE2 H 1 3.11 0.02 . 1 . . . . . . . . 4787 1 991 . 1 1 106 106 LYS HE3 H 1 3.11 0.02 . 1 . . . . . . . . 4787 1 992 . 1 1 106 106 LYS C C 13 177.4 0.1 . 1 . . . . . . . . 4787 1 993 . 1 1 107 107 ASP N N 15 120.0 0.1 . 1 . . . . . . . . 4787 1 994 . 1 1 107 107 ASP H H 1 8.43 0.02 . 1 . . . . . . . . 4787 1 995 . 1 1 107 107 ASP CA C 13 56.2 0.1 . 1 . . . . . . . . 4787 1 996 . 1 1 107 107 ASP HA H 1 4.71 0.02 . 1 . . . . . . . . 4787 1 997 . 1 1 107 107 ASP CB C 13 38.8 0.1 . 1 . . . . . . . . 4787 1 998 . 1 1 107 107 ASP HB2 H 1 2.89 0.02 . 1 . . . . . . . . 4787 1 999 . 1 1 107 107 ASP HB3 H 1 2.89 0.02 . 1 . . . . . . . . 4787 1 1000 . 1 1 107 107 ASP C C 13 176.2 0.1 . 1 . . . . . . . . 4787 1 1001 . 1 1 108 108 GLU N N 15 120.9 0.1 . 1 . . . . . . . . 4787 1 1002 . 1 1 108 108 GLU H H 1 8.27 0.02 . 1 . . . . . . . . 4787 1 1003 . 1 1 108 108 GLU CA C 13 56.5 0.1 . 1 . . . . . . . . 4787 1 1004 . 1 1 108 108 GLU HA H 1 4.27 0.02 . 1 . . . . . . . . 4787 1 1005 . 1 1 108 108 GLU CB C 13 29.2 0.1 . 1 . . . . . . . . 4787 1 1006 . 1 1 108 108 GLU HB2 H 1 2.25 0.02 . 2 . . . . . . . . 4787 1 1007 . 1 1 108 108 GLU HB3 H 1 1.94 0.02 . 2 . . . . . . . . 4787 1 1008 . 1 1 108 108 GLU CG C 13 32.5 0.1 . 1 . . . . . . . . 4787 1 1009 . 1 1 108 108 GLU C C 13 175.8 0.1 . 1 . . . . . . . . 4787 1 1010 . 1 1 109 109 TYR N N 15 119.7 0.1 . 1 . . . . . . . . 4787 1 1011 . 1 1 109 109 TYR H H 1 8.18 0.02 . 1 . . . . . . . . 4787 1 1012 . 1 1 109 109 TYR CA C 13 57.8 0.1 . 1 . . . . . . . . 4787 1 1013 . 1 1 109 109 TYR HA H 1 4.69 0.02 . 1 . . . . . . . . 4787 1 1014 . 1 1 109 109 TYR CB C 13 38.5 0.1 . 1 . . . . . . . . 4787 1 1015 . 1 1 109 109 TYR HB2 H 1 3.19 0.02 . 2 . . . . . . . . 4787 1 1016 . 1 1 109 109 TYR HB3 H 1 2.96 0.02 . 2 . . . . . . . . 4787 1 1017 . 1 1 109 109 TYR HD1 H 1 7.16 0.02 . 1 . . . . . . . . 4787 1 1018 . 1 1 109 109 TYR HD2 H 1 7.16 0.02 . 1 . . . . . . . . 4787 1 1019 . 1 1 109 109 TYR HE1 H 1 6.83 0.02 . 1 . . . . . . . . 4787 1 1020 . 1 1 109 109 TYR HE2 H 1 6.83 0.02 . 1 . . . . . . . . 4787 1 1021 . 1 1 109 109 TYR C C 13 175.6 0.1 . 1 . . . . . . . . 4787 1 1022 . 1 1 110 110 ALA N N 15 124.1 0.1 . 1 . . . . . . . . 4787 1 1023 . 1 1 110 110 ALA H H 1 8.04 0.02 . 1 . . . . . . . . 4787 1 1024 . 1 1 110 110 ALA CA C 13 52.6 0.1 . 1 . . . . . . . . 4787 1 1025 . 1 1 110 110 ALA HA H 1 4.33 0.02 . 1 . . . . . . . . 4787 1 1026 . 1 1 110 110 ALA HB1 H 1 1.39 0.02 . 1 . . . . . . . . 4787 1 1027 . 1 1 110 110 ALA HB2 H 1 1.39 0.02 . 1 . . . . . . . . 4787 1 1028 . 1 1 110 110 ALA HB3 H 1 1.39 0.02 . 1 . . . . . . . . 4787 1 1029 . 1 1 110 110 ALA CB C 13 20.3 0.1 . 1 . . . . . . . . 4787 1 1030 . 1 1 110 110 ALA C C 13 177.1 0.1 . 1 . . . . . . . . 4787 1 1031 . 1 1 111 111 ASP N N 15 118.0 0.1 . 1 . . . . . . . . 4787 1 1032 . 1 1 111 111 ASP H H 1 8.35 0.02 . 1 . . . . . . . . 4787 1 1033 . 1 1 111 111 ASP CA C 13 53.0 0.1 . 1 . . . . . . . . 4787 1 1034 . 1 1 111 111 ASP HA H 1 4.76 0.02 . 1 . . . . . . . . 4787 1 1035 . 1 1 111 111 ASP CB C 13 39.0 0.1 . 1 . . . . . . . . 4787 1 1036 . 1 1 111 111 ASP HB2 H 1 2.84 0.02 . 1 . . . . . . . . 4787 1 1037 . 1 1 111 111 ASP HB3 H 1 2.84 0.02 . 1 . . . . . . . . 4787 1 1038 . 1 1 111 111 ASP C C 13 175.0 0.1 . 1 . . . . . . . . 4787 1 1039 . 1 1 112 112 ILE N N 15 122.5 0.1 . 1 . . . . . . . . 4787 1 1040 . 1 1 112 112 ILE H H 1 8.04 0.02 . 1 . . . . . . . . 4787 1 1041 . 1 1 112 112 ILE CA C 13 58.9 0.1 . 1 . . . . . . . . 4787 1 1042 . 1 1 112 112 ILE HA H 1 4.49 0.02 . 1 . . . . . . . . 4787 1 1043 . 1 1 112 112 ILE CB C 13 38.2 0.1 . 1 . . . . . . . . 4787 1 1044 . 1 1 112 112 ILE HB H 1 1.95 0.02 . 1 . . . . . . . . 4787 1 1045 . 1 1 112 112 ILE HG21 H 1 0.94 0.02 . 1 . . . . . . . . 4787 1 1046 . 1 1 112 112 ILE HG22 H 1 0.94 0.02 . 1 . . . . . . . . 4787 1 1047 . 1 1 112 112 ILE HG23 H 1 0.94 0.02 . 1 . . . . . . . . 4787 1 1048 . 1 1 112 112 ILE CG2 C 13 16.8 0.1 . 1 . . . . . . . . 4787 1 1049 . 1 1 112 112 ILE CG1 C 13 26.6 0.1 . 1 . . . . . . . . 4787 1 1050 . 1 1 112 112 ILE HG12 H 1 1.56 0.02 . 2 . . . . . . . . 4787 1 1051 . 1 1 112 112 ILE HG13 H 1 1.22 0.02 . 2 . . . . . . . . 4787 1 1052 . 1 1 112 112 ILE HD11 H 1 0.97 0.02 . 1 . . . . . . . . 4787 1 1053 . 1 1 112 112 ILE HD12 H 1 0.97 0.02 . 1 . . . . . . . . 4787 1 1054 . 1 1 112 112 ILE HD13 H 1 0.97 0.02 . 1 . . . . . . . . 4787 1 1055 . 1 1 112 112 ILE CD1 C 13 13.2 0.1 . 1 . . . . . . . . 4787 1 1056 . 1 1 113 113 PRO CB C 13 34.6 0.1 . 1 . . . . . . . . 4787 1 1057 . 1 1 113 113 PRO HB2 H 1 2.06 0.02 . 1 . . . . . . . . 4787 1 1058 . 1 1 113 113 PRO HB3 H 1 2.06 0.02 . 1 . . . . . . . . 4787 1 1059 . 1 1 113 113 PRO HD2 H 1 3.72 0.02 . 2 . . . . . . . . 4787 1 1060 . 1 1 113 113 PRO HD3 H 1 3.93 0.02 . 2 . . . . . . . . 4787 1 1061 . 1 1 113 113 PRO C C 13 175.0 0.1 . 1 . . . . . . . . 4787 1 1062 . 1 1 114 114 GLU N N 15 120.9 0.1 . 1 . . . . . . . . 4787 1 1063 . 1 1 114 114 GLU H H 1 8.65 0.02 . 1 . . . . . . . . 4787 1 1064 . 1 1 114 114 GLU HA H 1 4.31 0.02 . 1 . . . . . . . . 4787 1 1065 . 1 1 114 114 GLU CB C 13 29.7 0.1 . 1 . . . . . . . . 4787 1 1066 . 1 1 114 114 GLU HB2 H 1 2.05 0.02 . 1 . . . . . . . . 4787 1 1067 . 1 1 114 114 GLU HB3 H 1 2.05 0.02 . 1 . . . . . . . . 4787 1 1068 . 1 1 114 114 GLU CG C 13 32.7 0.1 . 1 . . . . . . . . 4787 1 1069 . 1 1 114 114 GLU HG2 H 1 2.48 0.02 . 1 . . . . . . . . 4787 1 1070 . 1 1 114 114 GLU HG3 H 1 2.48 0.02 . 1 . . . . . . . . 4787 1 1071 . 1 1 114 114 GLU C C 13 176.0 0.1 . 1 . . . . . . . . 4787 1 1072 . 1 1 115 115 HIS N N 15 119.5 0.1 . 1 . . . . . . . . 4787 1 1073 . 1 1 115 115 HIS H H 1 8.55 0.02 . 1 . . . . . . . . 4787 1 1074 . 1 1 115 115 HIS CA C 13 54.9 0.1 . 1 . . . . . . . . 4787 1 1075 . 1 1 115 115 HIS HA H 1 4.77 0.02 . 1 . . . . . . . . 4787 1 1076 . 1 1 115 115 HIS CB C 13 29.5 0.1 . 1 . . . . . . . . 4787 1 1077 . 1 1 115 115 HIS HB2 H 1 3.24 0.02 . 1 . . . . . . . . 4787 1 1078 . 1 1 115 115 HIS HB3 H 1 3.24 0.02 . 1 . . . . . . . . 4787 1 1079 . 1 1 115 115 HIS C C 13 174.0 0.1 . 1 . . . . . . . . 4787 1 1080 . 1 1 116 116 LYS N N 15 124.6 0.1 . 1 . . . . . . . . 4787 1 1081 . 1 1 116 116 LYS H H 1 8.46 0.02 . 1 . . . . . . . . 4787 1 1082 . 1 1 116 116 LYS CA C 13 54.4 0.1 . 1 . . . . . . . . 4787 1 1083 . 1 1 116 116 LYS HA H 1 4.78 0.02 . 1 . . . . . . . . 4787 1 1084 . 1 1 116 116 LYS HB2 H 1 1.88 0.02 . 1 . . . . . . . . 4787 1 1085 . 1 1 116 116 LYS HB3 H 1 1.88 0.02 . 1 . . . . . . . . 4787 1 1086 . 1 1 116 116 LYS HG2 H 1 1.56 0.02 . 1 . . . . . . . . 4787 1 1087 . 1 1 116 116 LYS HG3 H 1 1.56 0.02 . 1 . . . . . . . . 4787 1 1088 . 1 1 116 116 LYS HD2 H 1 1.81 0.02 . 1 . . . . . . . . 4787 1 1089 . 1 1 116 116 LYS HD3 H 1 1.81 0.02 . 1 . . . . . . . . 4787 1 1090 . 1 1 117 117 PRO CA C 13 63.2 0.1 . 1 . . . . . . . . 4787 1 1091 . 1 1 117 117 PRO CB C 13 32.3 0.1 . 1 . . . . . . . . 4787 1 1092 . 1 1 117 117 PRO HB2 H 1 2.28 0.02 . 1 . . . . . . . . 4787 1 1093 . 1 1 117 117 PRO HB3 H 1 2.28 0.02 . 1 . . . . . . . . 4787 1 1094 . 1 1 117 117 PRO CG C 13 26.7 0.1 . 1 . . . . . . . . 4787 1 1095 . 1 1 117 117 PRO HG2 H 1 2.08 0.02 . 1 . . . . . . . . 4787 1 1096 . 1 1 117 117 PRO HG3 H 1 2.08 0.02 . 1 . . . . . . . . 4787 1 1097 . 1 1 117 117 PRO HD2 H 1 3.67 0.02 . 2 . . . . . . . . 4787 1 1098 . 1 1 117 117 PRO HD3 H 1 3.91 0.02 . 2 . . . . . . . . 4787 1 1099 . 1 1 118 118 THR N N 15 114.0 0.1 . 1 . . . . . . . . 4787 1 1100 . 1 1 118 118 THR H H 1 8.22 0.02 . 1 . . . . . . . . 4787 1 1101 . 1 1 118 118 THR CA C 13 61.9 0.1 . 1 . . . . . . . . 4787 1 1102 . 1 1 118 118 THR HA H 1 4.28 0.02 . 1 . . . . . . . . 4787 1 1103 . 1 1 118 118 THR CB C 13 68.9 0.1 . 1 . . . . . . . . 4787 1 1104 . 1 1 118 118 THR HB H 1 4.50 0.02 . 1 . . . . . . . . 4787 1 1105 . 1 1 118 118 THR HG21 H 1 1.23 0.02 . 1 . . . . . . . . 4787 1 1106 . 1 1 118 118 THR HG22 H 1 1.23 0.02 . 1 . . . . . . . . 4787 1 1107 . 1 1 118 118 THR HG23 H 1 1.23 0.02 . 1 . . . . . . . . 4787 1 1108 . 1 1 119 119 TYR N N 15 121.8 0.1 . 1 . . . . . . . . 4787 1 1109 . 1 1 119 119 TYR H H 1 8.14 0.02 . 1 . . . . . . . . 4787 1 1110 . 1 1 119 119 TYR CA C 13 57.6 0.1 . 1 . . . . . . . . 4787 1 1111 . 1 1 119 119 TYR HA H 1 4.70 0.02 . 1 . . . . . . . . 4787 1 1112 . 1 1 119 119 TYR CB C 13 38.9 0.1 . 1 . . . . . . . . 4787 1 1113 . 1 1 119 119 TYR HB2 H 1 3.04 0.02 . 1 . . . . . . . . 4787 1 1114 . 1 1 119 119 TYR HB3 H 1 3.04 0.02 . 1 . . . . . . . . 4787 1 1115 . 1 1 119 119 TYR HD1 H 1 7.19 0.02 . 1 . . . . . . . . 4787 1 1116 . 1 1 119 119 TYR HD2 H 1 7.19 0.02 . 1 . . . . . . . . 4787 1 1117 . 1 1 119 119 TYR HE1 H 1 6.91 0.02 . 1 . . . . . . . . 4787 1 1118 . 1 1 119 119 TYR HE2 H 1 6.91 0.02 . 1 . . . . . . . . 4787 1 1119 . 1 1 120 120 ASP N N 15 121.4 0.1 . 1 . . . . . . . . 4787 1 1120 . 1 1 120 120 ASP H H 1 8.37 0.02 . 1 . . . . . . . . 4787 1 1121 . 1 1 120 120 ASP CA C 13 53.3 0.1 . 1 . . . . . . . . 4787 1 1122 . 1 1 120 120 ASP HA H 1 4.71 0.02 . 1 . . . . . . . . 4787 1 1123 . 1 1 120 120 ASP HB2 H 1 2.79 0.02 . 1 . . . . . . . . 4787 1 1124 . 1 1 120 120 ASP HB3 H 1 2.79 0.02 . 1 . . . . . . . . 4787 1 stop_ save_