data_6051 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 6051 _Entry.Title ; 1H, 13C and 15N resonance assignments for methionine sulfoxide reductase B from Neisseria gonorroeae ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2003-12-16 _Entry.Accession_date 2003-12-16 _Entry.Last_release_date 2004-11-29 _Entry.Original_release_date 2004-11-29 _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 Aurelien Thureau . . . 6051 2 Alexandre Olry . . . 6051 3 Nicolas Coudevylle . . . 6051 4 Said Azza . . . 6051 5 Sandrine Boshi-Muller . . . 6051 6 Guy Branlant . . . 6051 7 'Manh Thong' Cung . . . 6051 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 6051 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 465 6051 '1H chemical shifts' 704 6051 '15N chemical shifts' 127 6051 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 . . 2004-11-29 2003-12-16 original author . 6051 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 6051 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Letter to the Editor: 1H, 13C and 15N resonance assignments of the methionine sulfoxide reductase B from Neisseria meningitidis ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 30 _Citation.Journal_issue 2 _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 223 _Citation.Page_last 224 _Citation.Year 2004 _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 Aurelien Thureau . . . 6051 1 2 Alexandre Olry . . . 6051 1 3 Nicolas Coudevylle . . . 6051 1 4 Said Azza . . . 6051 1 5 Sandrine Boschi-Muller . . . 6051 1 6 Guy Branlant . . . 6051 1 7 'Manh Thong' Cung . . . 6051 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'methionine sulfoxyde reductase B' 6051 1 'NMR assignment' 6051 1 'Neisseria meningitidis' 6051 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 6051 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12954610 _Citation.Full_citation ; Antoine M. et al. (2003) J. Biol. Chem., 278, 45352-45357 ; _Citation.Title 'Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 278 _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 45352 _Citation.Page_last 45357 _Citation.Year 2003 _Citation.Details ; Oxidation of methionine into methionine sulfoxide is associated with many pathologies and is described to exert regulatory effects on protein functions. Two classes of methionine sulfoxide reductases, called MsrA and MsrB, have been described to reduce the S and the R isomers of the sulfoxide of methionine sulfoxide back to methionine, respectively. Although MsrAs and MsrBs display quite different x-ray structures, they share a similar, new catalytic mechanism that proceeds via the sulfenic acid chemistry and that includes at least three chemical steps with 1) the formation of a sulfenic acid intermediate and the concomitant release of methionine; 2) the formation of an intra-disulfide bond; and 3) the reduction of the disulfide bond by thioredoxin. In the present study, it is shown that for the Neisseria meningitidis MsrA, 1) the rate-limiting step is associated with the reduction of the Cys-51/Cys-198 disulfide MsrA bond by thioredoxin; 2) the formation of the sulfenic acid intermediate is very efficient, thus suggesting catalytic assistance via amino acids of the active site; 3) the rate-determining step in the formation of the Cys-51/Cys-198 disulfide bond is that leading to the formation of the sulfenic intermediate on Cys-51; and 4) the apparent affinity constant for methionine sulfoxide in the methionine sulfoxide reductase step is 80-fold higher than the Km value determined under steady-state conditions. ; 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 Mathias Antoine M. . . 6051 2 2 Sandrine Boschi-Muller S. . . 6051 2 3 Guy Branlant G. . . 6051 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 6051 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Bartels C. et al. (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_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 6051 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10964927 _Citation.Full_citation ; Boschi-Muller S. et al. (2000) J. Biol. Chem, 275, 35908-35913 ; _Citation.Title 'A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 275 _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 35908 _Citation.Page_last 35913 _Citation.Year 2000 _Citation.Details ; Methionine oxidation into methionine sulfoxide is known to be involved in many pathologies and to exert regulatory effects on proteins. This oxidation can be reversed by a ubiquitous monomeric enzyme, the peptide methionine sulfoxide reductase (MsrA), whose activity in vivo requires the thioredoxin-regenerating system. The proposed chemical mechanism of Escherichia coli MsrA involves three Cys residues (positions 51, 198, and 206). A fourth Cys (position 86) is not important for catalysis. In the absence of a reducing system, 2 mol of methionine are formed per mole of enzyme for wild type and Cys-86 --> Ser mutant MsrA, whereas only 1 mol is formed for mutants in which either Cys-198 or Cys-206 is mutated. Reduction of methionine sulfoxide is shown to proceed through the formation of a sulfenic acid intermediate. This intermediate has been characterized by chemical probes and mass spectrometry analyses. Together, the results support a three-step chemical mechanism in vivo: 1) Cys-51 attacks the sulfur atom of the sulfoxide substrate leading, via a rearrangement, to the formation of a sulfenic acid intermediate on Cys-51 and release of 1 mol of methionine/mol of enzyme; 2) the sulfenic acid is then reduced via a double displacement mechanism involving formation of a disulfide bond between Cys-51 and Cys-198, followed by formation of a disulfide bond between Cys-198 and Cys-206, which liberates Cys-51, and 3) the disulfide bond between Cys-198 and Cys-206 is reduced by thioredoxin-dependent recycling system process. ; 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 S. Boschi-Muller S. . . 6051 4 2 S. Azza S. . . 6051 4 3 S. Sanglier-Cianferani S. . . 6051 4 4 F. Talfournier F. . . 6051 4 5 A. 'Van Dorsselear' A. . . 6051 4 6 G. Branlant G. . . 6051 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 6051 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10212987 _Citation.Full_citation ; Cornilescu G. et al. (1999) J. Biomol. NMR, 13, 289-302 ; _Citation.Title 'Protein backbone angle restraints from searching a database for chemical shift and sequence homology.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 13 _Citation.Journal_issue 3 _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 289 _Citation.Page_last 302 _Citation.Year 1999 _Citation.Details ; Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error. ; 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 G Cornilescu G. . . 6051 5 2 F Delaglio F. . . 6051 5 3 A Bax A. . . 6051 5 stop_ save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 6051 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11677230 _Citation.Full_citation ; Grimaud et al. (2001) J. Biol. Chem, 276, 48915-48920 ; _Citation.Title 'Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 276 _Citation.Journal_issue 52 _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 48915 _Citation.Page_last 48920 _Citation.Year 2001 _Citation.Details ; Oxidation of methionine residues to methionine sulfoxide can lead to inactivation of proteins. Methionine sulfoxide reductase (MsrA) has been known for a long time, and its repairing function well characterized. Here we identify a new methionine sulfoxide reductase, which we referred to as MsrB, the gene of which is present in genomes of eubacteria, archaebacteria, and eucaryotes. The msrA and msrB genes exhibit no sequence similarity and, in some genomes, are fused. The Escherichia coli MsrB protein (currently predicted to be encoded by an open reading frame of unknown function named yeaA) was used for genetic, enzymatic, and mass spectrometric investigations. Our in vivo study revealed that msrB is required for cadmium resistance of E. coli, a carcinogenic compound that induces oxidative stress. Our in vitro studies, showed that (i) MsrB and MsrA enzymes reduce free methionine sulfoxide with turn-over rates of 0.6 min(-1) and 20 min(-1), respectively, (ii) MsrA and MsrB act on oxidized calmodulin, each by repairing four to six of the eight methionine sulfoxide residues initially present, and (iii) simultaneous action of both MsrA and MsrB allowed full reduction of oxidized calmodulin. A possibility is that these two ubiquitous methionine sulfoxide reductases exhibit different substrate specificity. ; 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 R. Grimaud R. . . 6051 6 2 B. Ezraty B. . . 6051 6 3 'J. K.' Mitchell J. K. . 6051 6 4 D. Lafitte D. . . 6051 6 5 C. Briand C. . . 6051 6 6 'P. J.' Derrick P. J. . 6051 6 7 F. Barras F. . . 6051 6 stop_ save_ save_ref_6 _Citation.Sf_category citations _Citation.Sf_framecode ref_6 _Citation.Entry_ID 6051 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11938352 _Citation.Full_citation ; Lowther, W.T. et al. (2002) Nat. Struct. Biol., 9, 348-352 ; _Citation.Title 'The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Struct. Biol.' _Citation.Journal_name_full 'Nature structural biology' _Citation.Journal_volume 9 _Citation.Journal_issue 5 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1072-8368 _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 348 _Citation.Page_last 352 _Citation.Year 2002 _Citation.Details ; Methionine sulfoxide reductases (Msr) protect against oxidative damage that can contribute to cell death. The tandem Msr domains (MsrA and MsrB) of the pilB protein from Neisseria gonorrhoeae each reduce different epimeric forms of methionine sulfoxide. The overall fold of the MsrB domain revealed by the 1.85 A crystal structure shows no resemblance to the previously determined MsrA structures from other organisms. Despite the lack of homology, the active sites show approximate mirror symmetry. In each case, conserved amino acid motifs mediate the stereo-specific recognition and reduction of the substrate. Unlike the MsrA domain, the MsrB domain activates the cysteine or selenocysteine nucleophile through a unique Cys-Arg-Asp/Glu catalytic triad. The collapse of the reaction intermediate most likely results in the formation of a sulfenic or selenenic acid moiety. Regeneration of the active site occurs through a series of thiol-disulfide exchange steps involving another active site Cys residue and thioredoxin. These observations have broad implications for modular catalysis, antibiotic drug design and continuing longevity studies in mammals. ; 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 'W. Todd' Lowther W. T. . 6051 7 2 Herbert Weissbach H. . . 6051 7 3 Frantzy Etienne F. . . 6051 7 4 Nathan Brot N. . . 6051 7 5 'Brian W.' Matthews B. W. . 6051 7 stop_ save_ save_ref_7 _Citation.Sf_category citations _Citation.Sf_framecode ref_7 _Citation.Entry_ID 6051 _Citation.ID 8 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10799493 _Citation.Full_citation ; Moskovitz J. et al. (2000) J. Biol. Chem., 275, 14167-14172 ; _Citation.Title 'Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 275 _Citation.Journal_issue 19 _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 14167 _Citation.Page_last 14172 _Citation.Year 2000 _Citation.Details ; Peptide methionine sulfoxide reductases (MsrA) from many different organisms share a consensus amino acid sequence (GCFWG) that could play an important role in their active site. Site-directed single substitution of each of these amino acids except glycines in the yeast MsrA resulted in total loss of enzyme activity. Nevertheless, all the recombinant MsrA mutants and native proteins had a very similar circular dichroism spectrum. The demonstration that either treatment with iodoacetamide or replacement of the motif cysteine with serine leads to inactivation of the enzyme underscores the singular importance of cysteine residues in the activity of MsrA. The recombinant yeast MsrA was used for general characterization of the enzyme. Its K(m) value was similar to the bovine MsrA and appreciably lower than the K(m) of the bacterial enzyme. Also, it was shown that the enzymatic activity increased dramatically with increasing ionic strength. The recombinant yeast MsrA activity and the reduction activity of free methionine sulfoxide(s) were stereoselective toward the L-methionine S-sulfoxide and S-methyl p-tolyl sulfoxide. It was established that a methionine auxotroph yeast strain could grow on either form of L-methionine sulfoxide. ; 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 J. Moskovitz J. . . 6051 8 2 'J. M.' Poston J. M. . 6051 8 3 'B. S.' Berlett B. S. . 6051 8 4 'N. J.' Nosworthy N. J. . 6051 8 5 R. Szczepanowski R. . . 6051 8 6 'E. R.' Stadtman E. R. . 6051 8 stop_ save_ save_ref_8 _Citation.Sf_category citations _Citation.Sf_framecode ref_8 _Citation.Entry_ID 6051 _Citation.ID 9 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11812798 _Citation.Full_citation ; Olry A. et al. (2002) J. Biol. Chem., 277, 12016-12022 ; _Citation.Title 'Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 277 _Citation.Journal_issue 14 _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 12016 _Citation.Page_last 12022 _Citation.Year 2002 _Citation.Details ; PILB has been described as being involved in the virulence of bacteria of Neisseria genus. The PILB protein is composed of three subdomains. In the present study, the central subdomain (PILB-MsrA), the C terminus subdomain (PILB-MsrB), and the fused subdomain (PILB-MsrA/MsrB) of N. meningitidis were produced as folded entities. The central subdomain shows a methionine sulfoxide reductase A (MsrA) activity, whereas PILB-MsrB displays a methionine sulfoxide reductase B (MsrB) activity. The catalytic mechanism of PILB-MsrB can be divided into two steps: 1) an attack of the Cys-494 on the sulfur atom of the sulfoxide substrate, leading to formation of a sulfenic acid intermediate and release of 1 mol of methionine/mol of enzyme and 2) a regeneration of Cys-494 via formation of an intradisulfide bond with Cys-439 followed by reduction with thioredoxin. The study also shows that 1) MsrA and MsrB display opposite stereoselectivities toward the sulfoxide function; 2) the active sites of both Msrs, particularly MsrB, are rather adapted for binding protein-bound MetSO more efficiently than free MetSO; 3) the carbon Calpha is not a determining factor for efficient binding to both Msrs; and 4) the presence of the sulfoxide function is a prerequisite for binding to Msrs. The fact that the two Msrs exhibit opposite stereoselectivities argues for a structure of the active site of MsrBs different from that of MsrAs. This is further supported by the absence of sequence homology between the two Msrs in particular around the cysteine that is involved in formation of the sulfenic acid derivative. The fact that the catalytic mechanism takes place through formation of a sulfenic acid intermediate for both Msrs supports the idea that sulfenic acid chemistry is a general feature in the reduction of sulfoxides by thiols. ; 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 Alexandre Olry A. . . 6051 9 2 Sandrine Boschi-Muller S. . . 6051 9 3 Michel Marraud M. . . 6051 9 4 Sarah Sanglier-Cianferani S. . . 6051 9 5 Alain 'Van Dorsselear' A. . . 6051 9 6 Guy Branlant G. . . 6051 9 stop_ save_ save_ref_9 _Citation.Sf_category citations _Citation.Sf_framecode ref_9 _Citation.Entry_ID 6051 _Citation.ID 10 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10437782 _Citation.Full_citation ; Sharov V.S. et al (1999) FEBS lett., 455, 247-250 ; _Citation.Title 'Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'FEBS Lett.' _Citation.Journal_name_full 'FEBS letters' _Citation.Journal_volume 455 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-5793 _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 247 _Citation.Page_last 250 _Citation.Year 1999 _Citation.Details ; Methionine sulfoxide (MetSO) in calmodulin (CaM) was previously shown to be a substrate for bovine liver peptide methionine sulfoxide reductase (pMSR, EC 1.8.4.6), which can partially recover protein structure and function of oxidized CaM in vitro. Here, we report for the first time that pMSR selectively reduces the D-sulfoxide diastereomer of CaM-bound L-MetSO (L-Met-D-SO). After exhaustive reduction by pMSR, the ratio of L-Met-D-SO to L-Met-L-SO decreased to about 1:25 for hydrogen peroxide-oxidized CaM, and to about 1:10 for free MetSO. The accumulation of MetSO upon oxidative stress and aging in vivo may be related to incomplete, diastereoselective, repair by pMSR. ; 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 'V. S.' Sharov V. S. . 6051 10 2 'D. A.' Ferrington D. A. . 6051 10 3 'T. C.' Squier T. C. . 6051 10 4 C. Schneich C. . . 6051 10 stop_ save_ save_ref_10 _Citation.Sf_category citations _Citation.Sf_framecode ref_10 _Citation.Entry_ID 6051 _Citation.ID 11 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12913416 _Citation.Full_citation ; Zheng D. et al. (2003) J. Biomol. NMR, 27, 183-184 ; _Citation.Title '1H, 13C and 15N resonance assignments for methionine sulfoxide reductase B from Bacillus subtilis.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 27 _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 183 _Citation.Page_last 184 _Citation.Year 2003 _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 Deyou Zheng D. . . 6051 11 2 'John R.' Cort J. R. . 6051 11 3 YiWen Chiang Y. . . 6051 11 4 Thomas Acton T. . . 6051 11 5 'Michael A.' Kennedy M. A. . 6051 11 6 'Gaetano T.' Montelione G. T. . 6051 11 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_msrB _Assembly.Sf_category assembly _Assembly.Sf_framecode system_msrB _Assembly.Entry_ID 6051 _Assembly.ID 1 _Assembly.Name 'methionine sulfoxide reductase B' _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 free' _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 6051 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 msrB 1 $MsrB . . . reduced . . . . . 6051 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'methionine sulfoxide reductase B' system 6051 1 msrB abbreviation 6051 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_MsrB _Entity.Sf_category entity _Entity.Sf_framecode MsrB _Entity.Entry_ID 6051 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'methionine sulfoxide reductase B' _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 ; TYKKPSDAELKRTLTEEQYQ VTQNSATEYAFSHEYDHLFK PGIYVDVVSGEPLFSSADKY DSGCGWPSFTRPIDAKSVTE HDDFSYNMRRTEVRSHAADS HLGHVFPDGPRDKGGLRYCI NGASLKFIPLEQMDAAGYGA LKSKVK ; _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 146 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; We work on N. meningitidis MsrB protein but the numbering of amino acid residues is based on those of the E. coli MsrB for alignment. So the first residue of the N. meningitidis MsrB protein is the number 0. We have also a gap at the residue 113 (Glycine) which leads to the two residue numbers Gly 113 and Gly 113a. All these facts will be outlined in the publication. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 3HCG . "Structure Of The C-terminal Domain (msrb) Of Neisseria Meningitidis Pilb (reduced Form)" . . . . . 100.00 146 98.63 98.63 1.20e-101 . . . . 6051 1 2 no PDB 3HCH . "Structure Of The C-terminal Domain (msrb) Of Neisseria Meningitidis Pilb (complex With Substrate)" . . . . . 100.00 146 98.63 98.63 9.22e-102 . . . . 6051 1 3 no EMBL CAM07595 . "peptide methionine sulfoxide reductase [Neisseria meningitidis Z2491]" . . . . . 100.00 522 100.00 100.00 2.21e-99 . . . . 6051 1 4 no EMBL CAM09346 . "peptide methionine sulfoxide reductase [Neisseria meningitidis FAM18]" . . . . . 100.00 522 100.00 100.00 2.21e-99 . . . . 6051 1 5 no EMBL CAX49031 . "peptide methionine sulfoxide reductase MsrA/MsrB [includes: thioredoxin, peptide methionine sulfoxide reductase MsrA (protein-m" . . . . . 100.00 522 100.00 100.00 2.21e-99 . . . . 6051 1 6 no EMBL CBA03711 . "Peptide methionine sulfoxide reductase [Neisseria meningitidis alpha153]" . . . . . 100.00 422 98.63 99.32 2.27e-99 . . . . 6051 1 7 no EMBL CBA06064 . "Peptide-methionine (S)-S-oxide reductase [Neisseria meningitidis alpha275]" . . . . . 100.00 371 100.00 100.00 1.87e-101 . . . . 6051 1 8 no GB AAF40515 . "peptide methionine sulfoxide reductase [Neisseria meningitidis MC58]" . . . . . 100.00 522 99.32 99.32 9.17e-99 . . . . 6051 1 9 no GB AAL89752 . "methionine sulfoxide reductase PilB [Neisseria gonorrhoeae]" . . . . . 100.00 522 97.26 98.63 1.19e-96 . . . . 6051 1 10 no GB AAW90666 . "putative peptide methionine sulfoxide reductase [Neisseria gonorrhoeae FA 1090]" . . . . . 100.00 522 97.26 97.95 4.35e-96 . . . . 6051 1 11 no GB ABX72275 . "peptide methionine sulfoxide reductase [Neisseria meningitidis 053442]" . . . . . 100.00 522 100.00 100.00 2.21e-99 . . . . 6051 1 12 no GB ACF30776 . "methionine sulfoxide reductase PilB [Neisseria gonorrhoeae NCCP11945]" . . . . . 100.00 532 97.95 98.63 4.10e-97 . . . . 6051 1 13 no REF NP_273110 . "trifunctional thioredoxin/methionine sulfoxide reductase A/B protein [Neisseria meningitidis MC58]" . . . . . 100.00 522 99.32 99.32 9.17e-99 . . . . 6051 1 14 no REF WP_002216163 . "methionine sulfoxide reductase [Neisseria meningitidis]" . . . . . 100.00 522 100.00 100.00 2.21e-99 . . . . 6051 1 15 no REF WP_002218473 . "peptide methionine sulfoxide reductase msrA/msrB, partial [Neisseria meningitidis]" . . . . . 100.00 488 100.00 100.00 5.27e-100 . . . . 6051 1 16 no REF WP_002221795 . "methionine sulfoxide reductase [Neisseria meningitidis]" . . . . . 100.00 522 99.32 99.32 1.02e-98 . . . . 6051 1 17 no REF WP_002223263 . "methionine sulfoxide reductase [Neisseria meningitidis]" . . . . . 100.00 522 99.32 100.00 6.15e-99 . . . . 6051 1 18 no SP P14930 . "RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB; Includes: RecName: Full=Thioredoxin; Includes: RecName: Full=Pe" . . . . . 100.00 522 97.26 98.63 1.19e-96 . . . . 6051 1 19 no SP Q9JWM8 . "RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB; Includes: RecName: Full=Thioredoxin; Includes: RecName: Full=Pe" . . . . . 100.00 522 100.00 100.00 2.21e-99 . . . . 6051 1 20 no SP Q9K1N8 . "RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB; Includes: RecName: Full=Thioredoxin; Includes: RecName: Full=Pe" . . . . . 100.00 522 99.32 99.32 9.17e-99 . . . . 6051 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'methionine sulfoxide reductase B' common 6051 1 MsrB abbreviation 6051 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 0 THR . 6051 1 2 1 TYR . 6051 1 3 2 LYS . 6051 1 4 3 LYS . 6051 1 5 4 PRO . 6051 1 6 5 SER . 6051 1 7 6 ASP . 6051 1 8 7 ALA . 6051 1 9 8 GLU . 6051 1 10 9 LEU . 6051 1 11 10 LYS . 6051 1 12 11 ARG . 6051 1 13 12 THR . 6051 1 14 13 LEU . 6051 1 15 14 THR . 6051 1 16 15 GLU . 6051 1 17 16 GLU . 6051 1 18 17 GLN . 6051 1 19 18 TYR . 6051 1 20 19 GLN . 6051 1 21 20 VAL . 6051 1 22 21 THR . 6051 1 23 22 GLN . 6051 1 24 23 ASN . 6051 1 25 24 SER . 6051 1 26 25 ALA . 6051 1 27 26 THR . 6051 1 28 27 GLU . 6051 1 29 28 TYR . 6051 1 30 29 ALA . 6051 1 31 30 PHE . 6051 1 32 31 SER . 6051 1 33 32 HIS . 6051 1 34 33 GLU . 6051 1 35 34 TYR . 6051 1 36 35 ASP . 6051 1 37 36 HIS . 6051 1 38 37 LEU . 6051 1 39 38 PHE . 6051 1 40 39 LYS . 6051 1 41 40 PRO . 6051 1 42 41 GLY . 6051 1 43 42 ILE . 6051 1 44 43 TYR . 6051 1 45 44 VAL . 6051 1 46 45 ASP . 6051 1 47 46 VAL . 6051 1 48 47 VAL . 6051 1 49 48 SER . 6051 1 50 49 GLY . 6051 1 51 50 GLU . 6051 1 52 51 PRO . 6051 1 53 52 LEU . 6051 1 54 53 PHE . 6051 1 55 54 SER . 6051 1 56 55 SER . 6051 1 57 56 ALA . 6051 1 58 57 ASP . 6051 1 59 58 LYS . 6051 1 60 59 TYR . 6051 1 61 60 ASP . 6051 1 62 61 SER . 6051 1 63 62 GLY . 6051 1 64 63 CYS . 6051 1 65 64 GLY . 6051 1 66 65 TRP . 6051 1 67 66 PRO . 6051 1 68 67 SER . 6051 1 69 68 PHE . 6051 1 70 69 THR . 6051 1 71 70 ARG . 6051 1 72 71 PRO . 6051 1 73 72 ILE . 6051 1 74 73 ASP . 6051 1 75 74 ALA . 6051 1 76 75 LYS . 6051 1 77 76 SER . 6051 1 78 77 VAL . 6051 1 79 78 THR . 6051 1 80 79 GLU . 6051 1 81 80 HIS . 6051 1 82 81 ASP . 6051 1 83 82 ASP . 6051 1 84 83 PHE . 6051 1 85 84 SER . 6051 1 86 85 TYR . 6051 1 87 86 ASN . 6051 1 88 87 MET . 6051 1 89 88 ARG . 6051 1 90 89 ARG . 6051 1 91 90 THR . 6051 1 92 91 GLU . 6051 1 93 92 VAL . 6051 1 94 93 ARG . 6051 1 95 94 SER . 6051 1 96 95 HIS . 6051 1 97 96 ALA . 6051 1 98 97 ALA . 6051 1 99 98 ASP . 6051 1 100 99 SER . 6051 1 101 100 HIS . 6051 1 102 101 LEU . 6051 1 103 102 GLY . 6051 1 104 103 HIS . 6051 1 105 104 VAL . 6051 1 106 105 PHE . 6051 1 107 106 PRO . 6051 1 108 107 ASP . 6051 1 109 108 GLY . 6051 1 110 109 PRO . 6051 1 111 110 ARG . 6051 1 112 111 ASP . 6051 1 113 112 LYS . 6051 1 114 113 GLY . 6051 1 115 113a GLY . 6051 1 116 114 LEU . 6051 1 117 115 ARG . 6051 1 118 116 TYR . 6051 1 119 117 CYS . 6051 1 120 118 ILE . 6051 1 121 129 ASN . 6051 1 122 120 GLY . 6051 1 123 121 ALA . 6051 1 124 122 SER . 6051 1 125 123 LEU . 6051 1 126 124 LYS . 6051 1 127 125 PHE . 6051 1 128 126 ILE . 6051 1 129 127 PRO . 6051 1 130 128 LEU . 6051 1 131 139 GLU . 6051 1 132 130 GLN . 6051 1 133 131 MET . 6051 1 134 132 ASP . 6051 1 135 133 ALA . 6051 1 136 134 ALA . 6051 1 137 135 GLY . 6051 1 138 136 TYR . 6051 1 139 137 GLY . 6051 1 140 138 ALA . 6051 1 141 149 LEU . 6051 1 142 140 LYS . 6051 1 143 141 SER . 6051 1 144 142 LYS . 6051 1 145 143 VAL . 6051 1 146 144 LYS . 6051 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 . THR 1 1 6051 1 . TYR 2 2 6051 1 . LYS 3 3 6051 1 . LYS 4 4 6051 1 . PRO 5 5 6051 1 . SER 6 6 6051 1 . ASP 7 7 6051 1 . ALA 8 8 6051 1 . GLU 9 9 6051 1 . LEU 10 10 6051 1 . LYS 11 11 6051 1 . ARG 12 12 6051 1 . THR 13 13 6051 1 . LEU 14 14 6051 1 . THR 15 15 6051 1 . GLU 16 16 6051 1 . GLU 17 17 6051 1 . GLN 18 18 6051 1 . TYR 19 19 6051 1 . GLN 20 20 6051 1 . VAL 21 21 6051 1 . THR 22 22 6051 1 . GLN 23 23 6051 1 . ASN 24 24 6051 1 . SER 25 25 6051 1 . ALA 26 26 6051 1 . THR 27 27 6051 1 . GLU 28 28 6051 1 . TYR 29 29 6051 1 . ALA 30 30 6051 1 . PHE 31 31 6051 1 . SER 32 32 6051 1 . HIS 33 33 6051 1 . GLU 34 34 6051 1 . TYR 35 35 6051 1 . ASP 36 36 6051 1 . HIS 37 37 6051 1 . LEU 38 38 6051 1 . PHE 39 39 6051 1 . LYS 40 40 6051 1 . PRO 41 41 6051 1 . GLY 42 42 6051 1 . ILE 43 43 6051 1 . TYR 44 44 6051 1 . VAL 45 45 6051 1 . ASP 46 46 6051 1 . VAL 47 47 6051 1 . VAL 48 48 6051 1 . SER 49 49 6051 1 . GLY 50 50 6051 1 . GLU 51 51 6051 1 . PRO 52 52 6051 1 . LEU 53 53 6051 1 . PHE 54 54 6051 1 . SER 55 55 6051 1 . SER 56 56 6051 1 . ALA 57 57 6051 1 . ASP 58 58 6051 1 . LYS 59 59 6051 1 . TYR 60 60 6051 1 . ASP 61 61 6051 1 . SER 62 62 6051 1 . GLY 63 63 6051 1 . CYS 64 64 6051 1 . GLY 65 65 6051 1 . TRP 66 66 6051 1 . PRO 67 67 6051 1 . SER 68 68 6051 1 . PHE 69 69 6051 1 . THR 70 70 6051 1 . ARG 71 71 6051 1 . PRO 72 72 6051 1 . ILE 73 73 6051 1 . ASP 74 74 6051 1 . ALA 75 75 6051 1 . LYS 76 76 6051 1 . SER 77 77 6051 1 . VAL 78 78 6051 1 . THR 79 79 6051 1 . GLU 80 80 6051 1 . HIS 81 81 6051 1 . ASP 82 82 6051 1 . ASP 83 83 6051 1 . PHE 84 84 6051 1 . SER 85 85 6051 1 . TYR 86 86 6051 1 . ASN 87 87 6051 1 . MET 88 88 6051 1 . ARG 89 89 6051 1 . ARG 90 90 6051 1 . THR 91 91 6051 1 . GLU 92 92 6051 1 . VAL 93 93 6051 1 . ARG 94 94 6051 1 . SER 95 95 6051 1 . HIS 96 96 6051 1 . ALA 97 97 6051 1 . ALA 98 98 6051 1 . ASP 99 99 6051 1 . SER 100 100 6051 1 . HIS 101 101 6051 1 . LEU 102 102 6051 1 . GLY 103 103 6051 1 . HIS 104 104 6051 1 . VAL 105 105 6051 1 . PHE 106 106 6051 1 . PRO 107 107 6051 1 . ASP 108 108 6051 1 . GLY 109 109 6051 1 . PRO 110 110 6051 1 . ARG 111 111 6051 1 . ASP 112 112 6051 1 . LYS 113 113 6051 1 . GLY 114 114 6051 1 . GLY 115 115 6051 1 . LEU 116 116 6051 1 . ARG 117 117 6051 1 . TYR 118 118 6051 1 . CYS 119 119 6051 1 . ILE 120 120 6051 1 . ASN 121 121 6051 1 . GLY 122 122 6051 1 . ALA 123 123 6051 1 . SER 124 124 6051 1 . LEU 125 125 6051 1 . LYS 126 126 6051 1 . PHE 127 127 6051 1 . ILE 128 128 6051 1 . PRO 129 129 6051 1 . LEU 130 130 6051 1 . GLU 131 131 6051 1 . GLN 132 132 6051 1 . MET 133 133 6051 1 . ASP 134 134 6051 1 . ALA 135 135 6051 1 . ALA 136 136 6051 1 . GLY 137 137 6051 1 . TYR 138 138 6051 1 . GLY 139 139 6051 1 . ALA 140 140 6051 1 . LEU 141 141 6051 1 . LYS 142 142 6051 1 . SER 143 143 6051 1 . LYS 144 144 6051 1 . VAL 145 145 6051 1 . LYS 146 146 6051 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 6051 _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 $MsrB . 487 organism . 'Neisseria meningitidis' 'Neisseria meningitidis' . . Eubacteria . Neisseria meningitidis . . . . . . . . . . . . . . . . . . . . . 6051 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 6051 _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 $MsrB . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 6051 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 6051 _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 'methionine sulfoxide reductase B' '[U-13C; U-15N]' . . 1 $MsrB . . 2 . . mM . . . . 6051 1 stop_ save_ ####################### # Sample conditions # ####################### save_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_1 _Sample_condition_list.Entry_ID 6051 _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 7.1 0.2 n/a 6051 1 temperature 298 0 K 6051 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 6051 _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_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 6051 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Inova _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 6051 _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 spectrometer_1 Bruker DRX . 600 . . . 6051 1 2 spectrometer_2 Varian Inova . 800 . . . 6051 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 6051 _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 '1H-15N HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 6051 1 2 HNCA . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 6051 1 3 HN(CO)CA . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 6051 1 4 HNCO . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 6051 1 5 HN(CA)CO . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 6051 1 6 CBCANH . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 6051 1 7 CBCA(CO)NH . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 6051 1 8 HNHA . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 6051 1 9 HCCH-TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 6051 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 6051 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 6051 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 6051 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 6051 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 6051 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _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 $sample_1 . 6051 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 2 2 TYR C C 13 173.628 0.20 . 1 . . . . . . . . 6051 1 2 . 1 1 2 2 TYR CA C 13 59.125 0.20 . 1 . . . . . . . . 6051 1 3 . 1 1 2 2 TYR HA H 1 3.912 0.01 . 1 . . . . . . . . 6051 1 4 . 1 1 2 2 TYR CB C 13 39.619 0.20 . 1 . . . . . . . . 6051 1 5 . 1 1 3 3 LYS H H 1 7.884 0.01 . 1 . . . . . . . . 6051 1 6 . 1 1 3 3 LYS N N 15 126.495 0.10 . 1 . . . . . . . . 6051 1 7 . 1 1 3 3 LYS C C 13 173.168 0.20 . 1 . . . . . . . . 6051 1 8 . 1 1 3 3 LYS CA C 13 55.008 0.20 . 1 . . . . . . . . 6051 1 9 . 1 1 3 3 LYS HA H 1 4.223 0.01 . 1 . . . . . . . . 6051 1 10 . 1 1 3 3 LYS CB C 13 34.759 0.20 . 1 . . . . . . . . 6051 1 11 . 1 1 3 3 LYS HB2 H 1 1.481 0.01 . 1 . . . . . . . . 6051 1 12 . 1 1 3 3 LYS HB3 H 1 1.481 0.01 . 1 . . . . . . . . 6051 1 13 . 1 1 3 3 LYS CG C 13 18.681 0.20 . 1 . . . . . . . . 6051 1 14 . 1 1 3 3 LYS HG2 H 1 1.333 0.01 . 1 . . . . . . . . 6051 1 15 . 1 1 3 3 LYS HG3 H 1 1.333 0.01 . 1 . . . . . . . . 6051 1 16 . 1 1 3 3 LYS CD C 13 24.715 0.20 . 1 . . . . . . . . 6051 1 17 . 1 1 3 3 LYS HD2 H 1 1.156 0.01 . 1 . . . . . . . . 6051 1 18 . 1 1 3 3 LYS HD3 H 1 1.156 0.01 . 1 . . . . . . . . 6051 1 19 . 1 1 3 3 LYS CE C 13 42.580 0.20 . 1 . . . . . . . . 6051 1 20 . 1 1 3 3 LYS HE2 H 1 2.840 0.01 . 1 . . . . . . . . 6051 1 21 . 1 1 3 3 LYS HE3 H 1 2.840 0.01 . 1 . . . . . . . . 6051 1 22 . 1 1 4 4 LYS H H 1 8.344 0.01 . 1 . . . . . . . . 6051 1 23 . 1 1 4 4 LYS N N 15 126.104 0.10 . 1 . . . . . . . . 6051 1 24 . 1 1 4 4 LYS C C 13 174.062 0.20 . 1 . . . . . . . . 6051 1 25 . 1 1 4 4 LYS CA C 13 54.962 0.20 . 1 . . . . . . . . 6051 1 26 . 1 1 4 4 LYS HA H 1 4.263 0.01 . 1 . . . . . . . . 6051 1 27 . 1 1 4 4 LYS CB C 13 33.412 0.20 . 1 . . . . . . . . 6051 1 28 . 1 1 4 4 LYS HB2 H 1 1.697 0.01 . 1 . . . . . . . . 6051 1 29 . 1 1 4 4 LYS HB3 H 1 1.697 0.01 . 1 . . . . . . . . 6051 1 30 . 1 1 4 4 LYS HG2 H 1 1.502 0.01 . 1 . . . . . . . . 6051 1 31 . 1 1 4 4 LYS HG3 H 1 1.502 0.01 . 1 . . . . . . . . 6051 1 32 . 1 1 4 4 LYS HE2 H 1 2.909 0.01 . 1 . . . . . . . . 6051 1 33 . 1 1 4 4 LYS HE3 H 1 2.909 0.01 . 1 . . . . . . . . 6051 1 34 . 1 1 5 5 PRO C C 13 173.765 0.20 . 1 . . . . . . . . 6051 1 35 . 1 1 5 5 PRO CA C 13 63.055 0.20 . 1 . . . . . . . . 6051 1 36 . 1 1 5 5 PRO HA H 1 4.813 0.01 . 1 . . . . . . . . 6051 1 37 . 1 1 5 5 PRO CB C 13 32.729 0.20 . 1 . . . . . . . . 6051 1 38 . 1 1 5 5 PRO HB2 H 1 2.183 0.01 . 2 . . . . . . . . 6051 1 39 . 1 1 5 5 PRO HB3 H 1 2.084 0.01 . 2 . . . . . . . . 6051 1 40 . 1 1 5 5 PRO HG2 H 1 1.839 0.01 . 1 . . . . . . . . 6051 1 41 . 1 1 5 5 PRO HG3 H 1 1.839 0.01 . 1 . . . . . . . . 6051 1 42 . 1 1 5 5 PRO HD2 H 1 3.907 0.01 . 1 . . . . . . . . 6051 1 43 . 1 1 5 5 PRO HD3 H 1 3.907 0.01 . 1 . . . . . . . . 6051 1 44 . 1 1 6 6 SER H H 1 8.245 0.01 . 1 . . . . . . . . 6051 1 45 . 1 1 6 6 SER N N 15 114.520 0.10 . 1 . . . . . . . . 6051 1 46 . 1 1 6 6 SER C C 13 173.765 0.20 . 1 . . . . . . . . 6051 1 47 . 1 1 6 6 SER CA C 13 58.441 0.20 . 1 . . . . . . . . 6051 1 48 . 1 1 6 6 SER HA H 1 4.348 0.01 . 1 . . . . . . . . 6051 1 49 . 1 1 6 6 SER CB C 13 65.498 0.20 . 1 . . . . . . . . 6051 1 50 . 1 1 6 6 SER HB2 H 1 3.800 0.01 . 1 . . . . . . . . 6051 1 51 . 1 1 6 6 SER HB3 H 1 3.800 0.01 . 1 . . . . . . . . 6051 1 52 . 1 1 7 7 ASP H H 1 8.781 0.01 . 1 . . . . . . . . 6051 1 53 . 1 1 7 7 ASP N N 15 121.872 0.10 . 1 . . . . . . . . 6051 1 54 . 1 1 7 7 ASP C C 13 177.056 0.20 . 1 . . . . . . . . 6051 1 55 . 1 1 7 7 ASP CA C 13 58.915 0.20 . 1 . . . . . . . . 6051 1 56 . 1 1 7 7 ASP HA H 1 4.374 0.01 . 1 . . . . . . . . 6051 1 57 . 1 1 7 7 ASP CB C 13 42.305 0.20 . 1 . . . . . . . . 6051 1 58 . 1 1 7 7 ASP HB2 H 1 2.660 0.01 . 2 . . . . . . . . 6051 1 59 . 1 1 7 7 ASP HB3 H 1 2.490 0.01 . 2 . . . . . . . . 6051 1 60 . 1 1 8 8 ALA H H 1 8.319 0.01 . 1 . . . . . . . . 6051 1 61 . 1 1 8 8 ALA N N 15 118.162 0.10 . 1 . . . . . . . . 6051 1 62 . 1 1 8 8 ALA C C 13 180.180 0.20 . 1 . . . . . . . . 6051 1 63 . 1 1 8 8 ALA CA C 13 55.484 0.20 . 1 . . . . . . . . 6051 1 64 . 1 1 8 8 ALA HA H 1 3.889 0.01 . 1 . . . . . . . . 6051 1 65 . 1 1 8 8 ALA CB C 13 18.927 0.20 . 1 . . . . . . . . 6051 1 66 . 1 1 8 8 ALA HB1 H 1 1.328 0.01 . 1 . . . . . . . . 6051 1 67 . 1 1 8 8 ALA HB2 H 1 1.328 0.01 . 1 . . . . . . . . 6051 1 68 . 1 1 8 8 ALA HB3 H 1 1.328 0.01 . 1 . . . . . . . . 6051 1 69 . 1 1 9 9 GLU H H 1 7.570 0.01 . 1 . . . . . . . . 6051 1 70 . 1 1 9 9 GLU N N 15 118.471 0.10 . 1 . . . . . . . . 6051 1 71 . 1 1 9 9 GLU C C 13 179.403 0.20 . 1 . . . . . . . . 6051 1 72 . 1 1 9 9 GLU CA C 13 59.549 0.20 . 1 . . . . . . . . 6051 1 73 . 1 1 9 9 GLU HA H 1 3.998 0.01 . 1 . . . . . . . . 6051 1 74 . 1 1 9 9 GLU CB C 13 30.212 0.20 . 1 . . . . . . . . 6051 1 75 . 1 1 9 9 GLU HB2 H 1 2.303 0.01 . 2 . . . . . . . . 6051 1 76 . 1 1 9 9 GLU HB3 H 1 2.021 0.01 . 2 . . . . . . . . 6051 1 77 . 1 1 9 9 GLU HG2 H 1 2.159 0.01 . 1 . . . . . . . . 6051 1 78 . 1 1 9 9 GLU HG3 H 1 2.159 0.01 . 1 . . . . . . . . 6051 1 79 . 1 1 10 10 LEU H H 1 8.569 0.01 . 1 . . . . . . . . 6051 1 80 . 1 1 10 10 LEU N N 15 121.972 0.10 . 1 . . . . . . . . 6051 1 81 . 1 1 10 10 LEU C C 13 178.213 0.20 . 1 . . . . . . . . 6051 1 82 . 1 1 10 10 LEU CA C 13 58.603 0.20 . 1 . . . . . . . . 6051 1 83 . 1 1 10 10 LEU HA H 1 4.039 0.01 . 1 . . . . . . . . 6051 1 84 . 1 1 10 10 LEU CB C 13 42.002 0.20 . 1 . . . . . . . . 6051 1 85 . 1 1 10 10 LEU HB2 H 1 2.660 0.01 . 2 . . . . . . . . 6051 1 86 . 1 1 10 10 LEU HB3 H 1 2.540 0.01 . 2 . . . . . . . . 6051 1 87 . 1 1 10 10 LEU HD11 H 1 0.767 0.01 . 1 . . . . . . . . 6051 1 88 . 1 1 10 10 LEU HD12 H 1 0.767 0.01 . 1 . . . . . . . . 6051 1 89 . 1 1 10 10 LEU HD13 H 1 0.767 0.01 . 1 . . . . . . . . 6051 1 90 . 1 1 10 10 LEU HD21 H 1 0.767 0.01 . 1 . . . . . . . . 6051 1 91 . 1 1 10 10 LEU HD22 H 1 0.767 0.01 . 1 . . . . . . . . 6051 1 92 . 1 1 10 10 LEU HD23 H 1 0.767 0.01 . 1 . . . . . . . . 6051 1 93 . 1 1 11 11 LYS H H 1 8.397 0.01 . 1 . . . . . . . . 6051 1 94 . 1 1 11 11 LYS N N 15 117.795 0.10 . 1 . . . . . . . . 6051 1 95 . 1 1 11 11 LYS C C 13 177.535 0.20 . 1 . . . . . . . . 6051 1 96 . 1 1 11 11 LYS CA C 13 59.219 0.20 . 1 . . . . . . . . 6051 1 97 . 1 1 11 11 LYS HA H 1 3.753 0.01 . 1 . . . . . . . . 6051 1 98 . 1 1 11 11 LYS CB C 13 33.075 0.20 . 1 . . . . . . . . 6051 1 99 . 1 1 11 11 LYS HB2 H 1 1.600 0.01 . 1 . . . . . . . . 6051 1 100 . 1 1 11 11 LYS HB3 H 1 1.600 0.01 . 1 . . . . . . . . 6051 1 101 . 1 1 11 11 LYS HG2 H 1 1.549 0.01 . 1 . . . . . . . . 6051 1 102 . 1 1 11 11 LYS HG3 H 1 1.549 0.01 . 1 . . . . . . . . 6051 1 103 . 1 1 11 11 LYS HE2 H 1 2.652 0.01 . 1 . . . . . . . . 6051 1 104 . 1 1 11 11 LYS HE3 H 1 2.652 0.01 . 1 . . . . . . . . 6051 1 105 . 1 1 12 12 ARG H H 1 7.228 0.01 . 1 . . . . . . . . 6051 1 106 . 1 1 12 12 ARG N N 15 114.575 0.10 . 1 . . . . . . . . 6051 1 107 . 1 1 12 12 ARG C C 13 176.890 0.20 . 1 . . . . . . . . 6051 1 108 . 1 1 12 12 ARG CA C 13 57.822 0.20 . 1 . . . . . . . . 6051 1 109 . 1 1 12 12 ARG HA H 1 4.280 0.01 . 1 . . . . . . . . 6051 1 110 . 1 1 12 12 ARG CB C 13 31.896 0.20 . 1 . . . . . . . . 6051 1 111 . 1 1 12 12 ARG HB2 H 1 1.866 0.01 . 1 . . . . . . . . 6051 1 112 . 1 1 12 12 ARG HB3 H 1 1.866 0.01 . 1 . . . . . . . . 6051 1 113 . 1 1 12 12 ARG CG C 13 28.217 0.20 . 1 . . . . . . . . 6051 1 114 . 1 1 12 12 ARG HG2 H 1 1.639 0.01 . 1 . . . . . . . . 6051 1 115 . 1 1 12 12 ARG HG3 H 1 1.639 0.01 . 1 . . . . . . . . 6051 1 116 . 1 1 12 12 ARG CD C 13 44.028 0.20 . 1 . . . . . . . . 6051 1 117 . 1 1 12 12 ARG HD2 H 1 3.115 0.01 . 1 . . . . . . . . 6051 1 118 . 1 1 12 12 ARG HD3 H 1 3.115 0.01 . 1 . . . . . . . . 6051 1 119 . 1 1 13 13 THR H H 1 7.792 0.01 . 1 . . . . . . . . 6051 1 120 . 1 1 13 13 THR N N 15 111.011 0.10 . 1 . . . . . . . . 6051 1 121 . 1 1 13 13 THR C C 13 174.129 0.20 . 1 . . . . . . . . 6051 1 122 . 1 1 13 13 THR CA C 13 64.233 0.20 . 1 . . . . . . . . 6051 1 123 . 1 1 13 13 THR HA H 1 4.262 0.01 . 1 . . . . . . . . 6051 1 124 . 1 1 13 13 THR CB C 13 71.056 0.20 . 1 . . . . . . . . 6051 1 125 . 1 1 13 13 THR HB H 1 4.151 0.01 . 1 . . . . . . . . 6051 1 126 . 1 1 13 13 THR CG2 C 13 22.318 0.20 . 1 . . . . . . . . 6051 1 127 . 1 1 13 13 THR HG21 H 1 1.236 0.01 . 1 . . . . . . . . 6051 1 128 . 1 1 13 13 THR HG22 H 1 1.236 0.01 . 1 . . . . . . . . 6051 1 129 . 1 1 13 13 THR HG23 H 1 1.236 0.01 . 1 . . . . . . . . 6051 1 130 . 1 1 14 14 LEU H H 1 8.069 0.01 . 1 . . . . . . . . 6051 1 131 . 1 1 14 14 LEU N N 15 122.120 0.10 . 1 . . . . . . . . 6051 1 132 . 1 1 14 14 LEU C C 13 177.866 0.20 . 1 . . . . . . . . 6051 1 133 . 1 1 14 14 LEU CA C 13 54.542 0.20 . 1 . . . . . . . . 6051 1 134 . 1 1 14 14 LEU HA H 1 4.694 0.01 . 1 . . . . . . . . 6051 1 135 . 1 1 14 14 LEU CB C 13 43.184 0.20 . 1 . . . . . . . . 6051 1 136 . 1 1 14 14 LEU HB2 H 1 1.577 0.01 . 1 . . . . . . . . 6051 1 137 . 1 1 14 14 LEU HB3 H 1 1.577 0.01 . 1 . . . . . . . . 6051 1 138 . 1 1 14 14 LEU CG C 13 27.928 0.20 . 1 . . . . . . . . 6051 1 139 . 1 1 14 14 LEU HG H 1 1.573 0.01 . 1 . . . . . . . . 6051 1 140 . 1 1 14 14 LEU CD1 C 13 24.064 0.20 . 1 . . . . . . . . 6051 1 141 . 1 1 14 14 LEU HD11 H 1 0.768 0.01 . 1 . . . . . . . . 6051 1 142 . 1 1 14 14 LEU HD12 H 1 0.768 0.01 . 1 . . . . . . . . 6051 1 143 . 1 1 14 14 LEU HD13 H 1 0.768 0.01 . 1 . . . . . . . . 6051 1 144 . 1 1 14 14 LEU CD2 C 13 22.668 0.20 . 1 . . . . . . . . 6051 1 145 . 1 1 14 14 LEU HD21 H 1 0.768 0.01 . 1 . . . . . . . . 6051 1 146 . 1 1 14 14 LEU HD22 H 1 0.768 0.01 . 1 . . . . . . . . 6051 1 147 . 1 1 14 14 LEU HD23 H 1 0.768 0.01 . 1 . . . . . . . . 6051 1 148 . 1 1 15 15 THR H H 1 8.661 0.01 . 1 . . . . . . . . 6051 1 149 . 1 1 15 15 THR N N 15 112.228 0.10 . 1 . . . . . . . . 6051 1 150 . 1 1 15 15 THR C C 13 174.684 0.20 . 1 . . . . . . . . 6051 1 151 . 1 1 15 15 THR CA C 13 61.891 0.20 . 1 . . . . . . . . 6051 1 152 . 1 1 15 15 THR HA H 1 4.386 0.01 . 1 . . . . . . . . 6051 1 153 . 1 1 15 15 THR CB C 13 71.163 0.20 . 1 . . . . . . . . 6051 1 154 . 1 1 15 15 THR HB H 1 4.708 0.01 . 1 . . . . . . . . 6051 1 155 . 1 1 15 15 THR CG2 C 13 22.353 0.20 . 1 . . . . . . . . 6051 1 156 . 1 1 15 15 THR HG21 H 1 1.275 0.01 . 1 . . . . . . . . 6051 1 157 . 1 1 15 15 THR HG22 H 1 1.275 0.01 . 1 . . . . . . . . 6051 1 158 . 1 1 15 15 THR HG23 H 1 1.275 0.01 . 1 . . . . . . . . 6051 1 159 . 1 1 16 16 GLU H H 1 8.892 0.01 . 1 . . . . . . . . 6051 1 160 . 1 1 16 16 GLU N N 15 122.384 0.10 . 1 . . . . . . . . 6051 1 161 . 1 1 16 16 GLU C C 13 177.833 0.20 . 1 . . . . . . . . 6051 1 162 . 1 1 16 16 GLU CA C 13 60.892 0.20 . 1 . . . . . . . . 6051 1 163 . 1 1 16 16 GLU HA H 1 4.049 0.01 . 1 . . . . . . . . 6051 1 164 . 1 1 16 16 GLU CB C 13 29.454 0.20 . 1 . . . . . . . . 6051 1 165 . 1 1 16 16 GLU HB2 H 1 2.060 0.01 . 2 . . . . . . . . 6051 1 166 . 1 1 16 16 GLU HB3 H 1 1.895 0.01 . 2 . . . . . . . . 6051 1 167 . 1 1 16 16 GLU CG C 13 37.282 0.20 . 1 . . . . . . . . 6051 1 168 . 1 1 16 16 GLU HG2 H 1 2.237 0.01 . 2 . . . . . . . . 6051 1 169 . 1 1 16 16 GLU HG3 H 1 2.024 0.01 . 2 . . . . . . . . 6051 1 170 . 1 1 17 17 GLU H H 1 8.642 0.01 . 1 . . . . . . . . 6051 1 171 . 1 1 17 17 GLU N N 15 117.603 0.10 . 1 . . . . . . . . 6051 1 172 . 1 1 17 17 GLU C C 13 177.998 0.20 . 1 . . . . . . . . 6051 1 173 . 1 1 17 17 GLU CA C 13 60.951 0.20 . 1 . . . . . . . . 6051 1 174 . 1 1 17 17 GLU HA H 1 4.037 0.01 . 1 . . . . . . . . 6051 1 175 . 1 1 17 17 GLU CB C 13 30.128 0.20 . 1 . . . . . . . . 6051 1 176 . 1 1 17 17 GLU HB2 H 1 2.060 0.01 . 2 . . . . . . . . 6051 1 177 . 1 1 17 17 GLU HB3 H 1 1.895 0.01 . 2 . . . . . . . . 6051 1 178 . 1 1 17 17 GLU CG C 13 37.282 0.20 . 1 . . . . . . . . 6051 1 179 . 1 1 17 17 GLU HG2 H 1 2.237 0.01 . 2 . . . . . . . . 6051 1 180 . 1 1 17 17 GLU HG3 H 1 2.303 0.01 . 2 . . . . . . . . 6051 1 181 . 1 1 18 18 GLN H H 1 7.681 0.01 . 1 . . . . . . . . 6051 1 182 . 1 1 18 18 GLN N N 15 116.527 0.10 . 1 . . . . . . . . 6051 1 183 . 1 1 18 18 GLN C C 13 179.651 0.20 . 1 . . . . . . . . 6051 1 184 . 1 1 18 18 GLN CA C 13 59.388 0.20 . 1 . . . . . . . . 6051 1 185 . 1 1 18 18 GLN HA H 1 4.004 0.01 . 1 . . . . . . . . 6051 1 186 . 1 1 19 19 TYR H H 1 9.040 0.01 . 1 . . . . . . . . 6051 1 187 . 1 1 19 19 TYR N N 15 122.711 0.10 . 1 . . . . . . . . 6051 1 188 . 1 1 19 19 TYR CA C 13 63.155 0.20 . 1 . . . . . . . . 6051 1 189 . 1 1 19 19 TYR HA H 1 4.761 0.01 . 1 . . . . . . . . 6051 1 190 . 1 1 19 19 TYR HB2 H 1 2.016 0.01 . 1 . . . . . . . . 6051 1 191 . 1 1 21 21 VAL C C 13 176.890 0.20 . 1 . . . . . . . . 6051 1 192 . 1 1 21 21 VAL CA C 13 66.344 0.20 . 1 . . . . . . . . 6051 1 193 . 1 1 22 22 THR H H 1 7.663 0.01 . 1 . . . . . . . . 6051 1 194 . 1 1 22 22 THR N N 15 105.126 0.10 . 1 . . . . . . . . 6051 1 195 . 1 1 22 22 THR C C 13 177.419 0.20 . 1 . . . . . . . . 6051 1 196 . 1 1 22 22 THR CA C 13 66.106 0.20 . 1 . . . . . . . . 6051 1 197 . 1 1 22 22 THR HA H 1 4.590 0.01 . 1 . . . . . . . . 6051 1 198 . 1 1 22 22 THR CB C 13 77.401 0.20 . 1 . . . . . . . . 6051 1 199 . 1 1 22 22 THR HB H 1 4.074 0.01 . 1 . . . . . . . . 6051 1 200 . 1 1 22 22 THR CG2 C 13 22.658 0.20 . 1 . . . . . . . . 6051 1 201 . 1 1 22 22 THR HG21 H 1 1.410 0.01 . 1 . . . . . . . . 6051 1 202 . 1 1 22 22 THR HG22 H 1 1.410 0.01 . 1 . . . . . . . . 6051 1 203 . 1 1 22 22 THR HG23 H 1 1.410 0.01 . 1 . . . . . . . . 6051 1 204 . 1 1 23 23 GLN H H 1 8.559 0.01 . 1 . . . . . . . . 6051 1 205 . 1 1 23 23 GLN N N 15 116.402 0.10 . 1 . . . . . . . . 6051 1 206 . 1 1 23 23 GLN C C 13 176.560 0.20 . 1 . . . . . . . . 6051 1 207 . 1 1 23 23 GLN CA C 13 55.945 0.20 . 1 . . . . . . . . 6051 1 208 . 1 1 23 23 GLN HA H 1 4.220 0.01 . 1 . . . . . . . . 6051 1 209 . 1 1 23 23 GLN CB C 13 28.359 0.20 . 1 . . . . . . . . 6051 1 210 . 1 1 23 23 GLN HB2 H 1 1.297 0.01 . 2 . . . . . . . . 6051 1 211 . 1 1 23 23 GLN HB3 H 1 0.695 0.01 . 2 . . . . . . . . 6051 1 212 . 1 1 23 23 GLN HG2 H 1 1.799 0.01 . 1 . . . . . . . . 6051 1 213 . 1 1 23 23 GLN HG3 H 1 1.799 0.01 . 1 . . . . . . . . 6051 1 214 . 1 1 23 23 GLN NE2 N 15 110.090 0.10 . 1 . . . . . . . . 6051 1 215 . 1 1 23 23 GLN HE21 H 1 7.706 0.01 . 1 . . . . . . . . 6051 1 216 . 1 1 23 23 GLN HE22 H 1 7.006 0.01 . 1 . . . . . . . . 6051 1 217 . 1 1 24 24 ASN H H 1 6.867 0.01 . 1 . . . . . . . . 6051 1 218 . 1 1 24 24 ASN N N 15 114.989 0.10 . 1 . . . . . . . . 6051 1 219 . 1 1 24 24 ASN C C 13 174.460 0.20 . 1 . . . . . . . . 6051 1 220 . 1 1 24 24 ASN CA C 13 52.663 0.20 . 1 . . . . . . . . 6051 1 221 . 1 1 24 24 ASN HA H 1 5.128 0.01 . 1 . . . . . . . . 6051 1 222 . 1 1 24 24 ASN CB C 13 39.560 0.20 . 1 . . . . . . . . 6051 1 223 . 1 1 24 24 ASN HB2 H 1 3.093 0.01 . 2 . . . . . . . . 6051 1 224 . 1 1 24 24 ASN HB3 H 1 2.925 0.01 . 2 . . . . . . . . 6051 1 225 . 1 1 24 24 ASN ND2 N 15 110.639 0.10 . 1 . . . . . . . . 6051 1 226 . 1 1 24 24 ASN HD21 H 1 7.705 0.01 . 1 . . . . . . . . 6051 1 227 . 1 1 24 24 ASN HD22 H 1 6.999 0.01 . 1 . . . . . . . . 6051 1 228 . 1 1 25 25 SER H H 1 6.978 0.01 . 1 . . . . . . . . 6051 1 229 . 1 1 25 25 SER N N 15 109.473 0.10 . 1 . . . . . . . . 6051 1 230 . 1 1 25 25 SER C C 13 172.492 0.20 . 1 . . . . . . . . 6051 1 231 . 1 1 25 25 SER CA C 13 59.702 0.20 . 1 . . . . . . . . 6051 1 232 . 1 1 25 25 SER HA H 1 4.442 0.01 . 1 . . . . . . . . 6051 1 233 . 1 1 25 25 SER CB C 13 60.697 0.20 . 1 . . . . . . . . 6051 1 234 . 1 1 25 25 SER HB2 H 1 3.444 0.01 . 1 . . . . . . . . 6051 1 235 . 1 1 25 25 SER HB3 H 1 3.444 0.01 . 1 . . . . . . . . 6051 1 236 . 1 1 26 26 ALA H H 1 7.764 0.01 . 1 . . . . . . . . 6051 1 237 . 1 1 26 26 ALA N N 15 122.213 0.10 . 1 . . . . . . . . 6051 1 238 . 1 1 26 26 ALA C C 13 172.558 0.20 . 1 . . . . . . . . 6051 1 239 . 1 1 26 26 ALA CA C 13 52.536 0.20 . 1 . . . . . . . . 6051 1 240 . 1 1 26 26 ALA HA H 1 4.122 0.01 . 1 . . . . . . . . 6051 1 241 . 1 1 26 26 ALA CB C 13 19.487 0.20 . 1 . . . . . . . . 6051 1 242 . 1 1 26 26 ALA HB1 H 1 1.104 0.01 . 1 . . . . . . . . 6051 1 243 . 1 1 26 26 ALA HB2 H 1 1.104 0.01 . 1 . . . . . . . . 6051 1 244 . 1 1 26 26 ALA HB3 H 1 1.104 0.01 . 1 . . . . . . . . 6051 1 245 . 1 1 27 27 THR H H 1 7.588 0.01 . 1 . . . . . . . . 6051 1 246 . 1 1 27 27 THR N N 15 111.607 0.10 . 1 . . . . . . . . 6051 1 247 . 1 1 27 27 THR C C 13 174.782 0.20 . 1 . . . . . . . . 6051 1 248 . 1 1 27 27 THR CA C 13 61.421 0.20 . 1 . . . . . . . . 6051 1 249 . 1 1 27 27 THR HA H 1 4.760 0.01 . 1 . . . . . . . . 6051 1 250 . 1 1 27 27 THR CB C 13 72.000 0.20 . 1 . . . . . . . . 6051 1 251 . 1 1 27 27 THR HB H 1 3.709 0.01 . 1 . . . . . . . . 6051 1 252 . 1 1 27 27 THR HG21 H 1 1.282 0.01 . 1 . . . . . . . . 6051 1 253 . 1 1 27 27 THR HG22 H 1 1.282 0.01 . 1 . . . . . . . . 6051 1 254 . 1 1 27 27 THR HG23 H 1 1.282 0.01 . 1 . . . . . . . . 6051 1 255 . 1 1 31 31 PHE C C 13 175.187 0.20 . 1 . . . . . . . . 6051 1 256 . 1 1 31 31 PHE CA C 13 60.199 0.20 . 1 . . . . . . . . 6051 1 257 . 1 1 31 31 PHE CB C 13 36.219 0.20 . 1 . . . . . . . . 6051 1 258 . 1 1 32 32 SER H H 1 7.957 0.01 . 1 . . . . . . . . 6051 1 259 . 1 1 32 32 SER N N 15 114.006 0.10 . 1 . . . . . . . . 6051 1 260 . 1 1 32 32 SER C C 13 173.865 0.20 . 1 . . . . . . . . 6051 1 261 . 1 1 32 32 SER CA C 13 61.112 0.20 . 1 . . . . . . . . 6051 1 262 . 1 1 32 32 SER HA H 1 4.280 0.01 . 1 . . . . . . . . 6051 1 263 . 1 1 32 32 SER CB C 13 65.329 0.20 . 1 . . . . . . . . 6051 1 264 . 1 1 32 32 SER HB2 H 1 3.972 0.01 . 1 . . . . . . . . 6051 1 265 . 1 1 32 32 SER HB3 H 1 3.972 0.01 . 1 . . . . . . . . 6051 1 266 . 1 1 33 33 HIS H H 1 8.669 0.01 . 1 . . . . . . . . 6051 1 267 . 1 1 33 33 HIS N N 15 126.977 0.10 . 1 . . . . . . . . 6051 1 268 . 1 1 33 33 HIS C C 13 176.675 0.20 . 1 . . . . . . . . 6051 1 269 . 1 1 33 33 HIS CA C 13 59.075 0.20 . 1 . . . . . . . . 6051 1 270 . 1 1 33 33 HIS HA H 1 4.321 0.01 . 1 . . . . . . . . 6051 1 271 . 1 1 33 33 HIS CB C 13 34.591 0.20 . 1 . . . . . . . . 6051 1 272 . 1 1 33 33 HIS HB2 H 1 2.988 0.01 . 2 . . . . . . . . 6051 1 273 . 1 1 33 33 HIS HB3 H 1 2.802 0.01 . 2 . . . . . . . . 6051 1 274 . 1 1 34 34 GLU H H 1 8.394 0.01 . 1 . . . . . . . . 6051 1 275 . 1 1 34 34 GLU N N 15 130.418 0.10 . 1 . . . . . . . . 6051 1 276 . 1 1 34 34 GLU C C 13 178.191 0.20 . 1 . . . . . . . . 6051 1 277 . 1 1 34 34 GLU CA C 13 59.553 0.20 . 1 . . . . . . . . 6051 1 278 . 1 1 34 34 GLU HA H 1 4.228 0.01 . 1 . . . . . . . . 6051 1 279 . 1 1 34 34 GLU CB C 13 29.875 0.20 . 1 . . . . . . . . 6051 1 280 . 1 1 35 35 TYR C C 13 178.362 0.20 . 1 . . . . . . . . 6051 1 281 . 1 1 35 35 TYR CA C 13 56.402 0.20 . 1 . . . . . . . . 6051 1 282 . 1 1 35 35 TYR CB C 13 36.023 0.20 . 1 . . . . . . . . 6051 1 283 . 1 1 36 36 ASP H H 1 8.476 0.01 . 1 . . . . . . . . 6051 1 284 . 1 1 36 36 ASP N N 15 122.314 0.10 . 1 . . . . . . . . 6051 1 285 . 1 1 36 36 ASP C C 13 175.518 0.20 . 1 . . . . . . . . 6051 1 286 . 1 1 36 36 ASP CA C 13 59.234 0.20 . 1 . . . . . . . . 6051 1 287 . 1 1 36 36 ASP HA H 1 3.790 0.01 . 1 . . . . . . . . 6051 1 288 . 1 1 36 36 ASP CB C 13 42.254 0.20 . 1 . . . . . . . . 6051 1 289 . 1 1 36 36 ASP HB2 H 1 2.614 0.01 . 2 . . . . . . . . 6051 1 290 . 1 1 36 36 ASP HB3 H 1 2.521 0.01 . 2 . . . . . . . . 6051 1 291 . 1 1 37 37 HIS H H 1 7.015 0.01 . 1 . . . . . . . . 6051 1 292 . 1 1 37 37 HIS N N 15 110.691 0.10 . 1 . . . . . . . . 6051 1 293 . 1 1 37 37 HIS C C 13 172.129 0.20 . 1 . . . . . . . . 6051 1 294 . 1 1 37 37 HIS CA C 13 54.247 0.20 . 1 . . . . . . . . 6051 1 295 . 1 1 37 37 HIS HA H 1 4.859 0.01 . 1 . . . . . . . . 6051 1 296 . 1 1 37 37 HIS CB C 13 29.538 0.20 . 1 . . . . . . . . 6051 1 297 . 1 1 37 37 HIS HB2 H 1 3.334 0.01 . 2 . . . . . . . . 6051 1 298 . 1 1 37 37 HIS HB3 H 1 3.117 0.01 . 2 . . . . . . . . 6051 1 299 . 1 1 38 38 LEU H H 1 6.257 0.01 . 1 . . . . . . . . 6051 1 300 . 1 1 38 38 LEU N N 15 122.263 0.10 . 1 . . . . . . . . 6051 1 301 . 1 1 38 38 LEU C C 13 174.774 0.20 . 1 . . . . . . . . 6051 1 302 . 1 1 38 38 LEU CA C 13 55.392 0.20 . 1 . . . . . . . . 6051 1 303 . 1 1 38 38 LEU HA H 1 4.192 0.01 . 1 . . . . . . . . 6051 1 304 . 1 1 38 38 LEU CB C 13 44.612 0.20 . 1 . . . . . . . . 6051 1 305 . 1 1 38 38 LEU HB2 H 1 1.591 0.01 . 2 . . . . . . . . 6051 1 306 . 1 1 38 38 LEU HB3 H 1 1.276 0.01 . 2 . . . . . . . . 6051 1 307 . 1 1 38 38 LEU CG C 13 25.997 0.20 . 1 . . . . . . . . 6051 1 308 . 1 1 38 38 LEU HG H 1 1.276 0.01 . 1 . . . . . . . . 6051 1 309 . 1 1 38 38 LEU CD1 C 13 23.513 0.20 . 1 . . . . . . . . 6051 1 310 . 1 1 38 38 LEU HD11 H 1 0.665 0.01 . 1 . . . . . . . . 6051 1 311 . 1 1 38 38 LEU HD12 H 1 0.665 0.01 . 1 . . . . . . . . 6051 1 312 . 1 1 38 38 LEU HD13 H 1 0.665 0.01 . 1 . . . . . . . . 6051 1 313 . 1 1 38 38 LEU CD2 C 13 26.188 0.20 . 1 . . . . . . . . 6051 1 314 . 1 1 38 38 LEU HD21 H 1 -0.163 0.01 . 1 . . . . . . . . 6051 1 315 . 1 1 38 38 LEU HD22 H 1 -0.163 0.01 . 1 . . . . . . . . 6051 1 316 . 1 1 38 38 LEU HD23 H 1 -0.163 0.01 . 1 . . . . . . . . 6051 1 317 . 1 1 39 39 PHE H H 1 8.966 0.01 . 1 . . . . . . . . 6051 1 318 . 1 1 39 39 PHE N N 15 125.512 0.10 . 1 . . . . . . . . 6051 1 319 . 1 1 39 39 PHE C C 13 174.146 0.20 . 1 . . . . . . . . 6051 1 320 . 1 1 39 39 PHE CA C 13 58.131 0.20 . 1 . . . . . . . . 6051 1 321 . 1 1 39 39 PHE HA H 1 4.488 0.01 . 1 . . . . . . . . 6051 1 322 . 1 1 39 39 PHE CB C 13 39.812 0.20 . 1 . . . . . . . . 6051 1 323 . 1 1 39 39 PHE HB2 H 1 3.022 0.01 . 2 . . . . . . . . 6051 1 324 . 1 1 39 39 PHE HB3 H 1 2.911 0.01 . 2 . . . . . . . . 6051 1 325 . 1 1 40 40 LYS H H 1 6.359 0.01 . 1 . . . . . . . . 6051 1 326 . 1 1 40 40 LYS N N 15 120.477 0.10 . 1 . . . . . . . . 6051 1 327 . 1 1 40 40 LYS C C 13 173.585 0.20 . 1 . . . . . . . . 6051 1 328 . 1 1 40 40 LYS CA C 13 54.536 0.20 . 1 . . . . . . . . 6051 1 329 . 1 1 40 40 LYS HA H 1 4.746 0.01 . 1 . . . . . . . . 6051 1 330 . 1 1 40 40 LYS CB C 13 35.091 0.20 . 1 . . . . . . . . 6051 1 331 . 1 1 40 40 LYS HB2 H 1 1.895 0.01 . 2 . . . . . . . . 6051 1 332 . 1 1 40 40 LYS HB3 H 1 1.686 0.01 . 2 . . . . . . . . 6051 1 333 . 1 1 40 40 LYS HG2 H 1 1.419 0.01 . 1 . . . . . . . . 6051 1 334 . 1 1 40 40 LYS HG3 H 1 1.419 0.01 . 1 . . . . . . . . 6051 1 335 . 1 1 40 40 LYS HD2 H 1 1.570 0.01 . 1 . . . . . . . . 6051 1 336 . 1 1 40 40 LYS HD3 H 1 1.570 0.01 . 1 . . . . . . . . 6051 1 337 . 1 1 40 40 LYS CE C 13 42.813 0.20 . 1 . . . . . . . . 6051 1 338 . 1 1 40 40 LYS HE2 H 1 2.911 0.01 . 1 . . . . . . . . 6051 1 339 . 1 1 40 40 LYS HE3 H 1 2.911 0.01 . 1 . . . . . . . . 6051 1 340 . 1 1 41 41 PRO C C 13 177.502 0.20 . 1 . . . . . . . . 6051 1 341 . 1 1 41 41 PRO CA C 13 62.883 0.20 . 1 . . . . . . . . 6051 1 342 . 1 1 41 41 PRO HA H 1 4.776 0.01 . 1 . . . . . . . . 6051 1 343 . 1 1 41 41 PRO CB C 13 32.640 0.20 . 1 . . . . . . . . 6051 1 344 . 1 1 41 41 PRO HB2 H 1 2.197 0.01 . 2 . . . . . . . . 6051 1 345 . 1 1 41 41 PRO HB3 H 1 1.807 0.01 . 2 . . . . . . . . 6051 1 346 . 1 1 41 41 PRO CG C 13 27.661 0.20 . 1 . . . . . . . . 6051 1 347 . 1 1 41 41 PRO HG2 H 1 1.870 0.01 . 1 . . . . . . . . 6051 1 348 . 1 1 41 41 PRO HG3 H 1 1.870 0.01 . 1 . . . . . . . . 6051 1 349 . 1 1 41 41 PRO CD C 13 51.019 0.20 . 1 . . . . . . . . 6051 1 350 . 1 1 41 41 PRO HD2 H 1 3.905 0.01 . 2 . . . . . . . . 6051 1 351 . 1 1 41 41 PRO HD3 H 1 3.573 0.01 . 2 . . . . . . . . 6051 1 352 . 1 1 42 42 GLY H H 1 9.169 0.01 . 1 . . . . . . . . 6051 1 353 . 1 1 42 42 GLY N N 15 112.863 0.10 . 1 . . . . . . . . 6051 1 354 . 1 1 42 42 GLY C C 13 169.665 0.20 . 1 . . . . . . . . 6051 1 355 . 1 1 42 42 GLY CA C 13 46.258 0.20 . 1 . . . . . . . . 6051 1 356 . 1 1 42 42 GLY HA2 H 1 3.129 0.01 . 2 . . . . . . . . 6051 1 357 . 1 1 42 42 GLY HA3 H 1 3.894 0.01 . 2 . . . . . . . . 6051 1 358 . 1 1 43 43 ILE H H 1 7.755 0.01 . 1 . . . . . . . . 6051 1 359 . 1 1 43 43 ILE N N 15 109.644 0.10 . 1 . . . . . . . . 6051 1 360 . 1 1 43 43 ILE C C 13 171.302 0.20 . 1 . . . . . . . . 6051 1 361 . 1 1 43 43 ILE CA C 13 59.215 0.20 . 1 . . . . . . . . 6051 1 362 . 1 1 43 43 ILE HA H 1 5.182 0.01 . 1 . . . . . . . . 6051 1 363 . 1 1 43 43 ILE CB C 13 43.602 0.20 . 1 . . . . . . . . 6051 1 364 . 1 1 43 43 ILE HB H 1 1.484 0.01 . 1 . . . . . . . . 6051 1 365 . 1 1 43 43 ILE CG1 C 13 17.821 0.20 . 1 . . . . . . . . 6051 1 366 . 1 1 43 43 ILE HG12 H 1 0.674 0.01 . 1 . . . . . . . . 6051 1 367 . 1 1 43 43 ILE HG13 H 1 0.674 0.01 . 1 . . . . . . . . 6051 1 368 . 1 1 43 43 ILE CD1 C 13 15.610 0.20 . 1 . . . . . . . . 6051 1 369 . 1 1 43 43 ILE HD11 H 1 0.078 0.01 . 1 . . . . . . . . 6051 1 370 . 1 1 43 43 ILE HD12 H 1 0.078 0.01 . 1 . . . . . . . . 6051 1 371 . 1 1 43 43 ILE HD13 H 1 0.078 0.01 . 1 . . . . . . . . 6051 1 372 . 1 1 44 44 TYR H H 1 9.234 0.01 . 1 . . . . . . . . 6051 1 373 . 1 1 44 44 TYR N N 15 118.626 0.10 . 1 . . . . . . . . 6051 1 374 . 1 1 44 44 TYR C C 13 175.187 0.20 . 1 . . . . . . . . 6051 1 375 . 1 1 44 44 TYR CA C 13 57.045 0.20 . 1 . . . . . . . . 6051 1 376 . 1 1 44 44 TYR HA H 1 4.598 0.01 . 1 . . . . . . . . 6051 1 377 . 1 1 44 44 TYR CB C 13 40.514 0.20 . 1 . . . . . . . . 6051 1 378 . 1 1 45 45 VAL H H 1 9.188 0.01 . 1 . . . . . . . . 6051 1 379 . 1 1 45 45 VAL N N 15 118.185 0.10 . 1 . . . . . . . . 6051 1 380 . 1 1 45 45 VAL C C 13 173.501 0.20 . 1 . . . . . . . . 6051 1 381 . 1 1 45 45 VAL CA C 13 57.832 0.20 . 1 . . . . . . . . 6051 1 382 . 1 1 45 45 VAL HA H 1 4.806 0.01 . 1 . . . . . . . . 6051 1 383 . 1 1 45 45 VAL CB C 13 33.726 0.20 . 1 . . . . . . . . 6051 1 384 . 1 1 45 45 VAL HB H 1 1.585 0.01 . 1 . . . . . . . . 6051 1 385 . 1 1 45 45 VAL CG1 C 13 19.297 0.20 . 1 . . . . . . . . 6051 1 386 . 1 1 45 45 VAL HG11 H 1 0.721 0.01 . 1 . . . . . . . . 6051 1 387 . 1 1 45 45 VAL HG12 H 1 0.721 0.01 . 1 . . . . . . . . 6051 1 388 . 1 1 45 45 VAL HG13 H 1 0.721 0.01 . 1 . . . . . . . . 6051 1 389 . 1 1 45 45 VAL CG2 C 13 21.424 0.20 . 1 . . . . . . . . 6051 1 390 . 1 1 45 45 VAL HG21 H 1 0.144 0.01 . 1 . . . . . . . . 6051 1 391 . 1 1 45 45 VAL HG22 H 1 0.144 0.01 . 1 . . . . . . . . 6051 1 392 . 1 1 45 45 VAL HG23 H 1 0.144 0.01 . 1 . . . . . . . . 6051 1 393 . 1 1 46 46 ASP H H 1 8.448 0.01 . 1 . . . . . . . . 6051 1 394 . 1 1 46 46 ASP N N 15 121.584 0.10 . 1 . . . . . . . . 6051 1 395 . 1 1 46 46 ASP C C 13 177.717 0.20 . 1 . . . . . . . . 6051 1 396 . 1 1 46 46 ASP CA C 13 55.481 0.20 . 1 . . . . . . . . 6051 1 397 . 1 1 46 46 ASP HA H 1 4.417 0.01 . 1 . . . . . . . . 6051 1 398 . 1 1 46 46 ASP CB C 13 44.444 0.20 . 1 . . . . . . . . 6051 1 399 . 1 1 46 46 ASP HB2 H 1 2.552 0.01 . 2 . . . . . . . . 6051 1 400 . 1 1 46 46 ASP HB3 H 1 2.396 0.01 . 2 . . . . . . . . 6051 1 401 . 1 1 47 47 VAL H H 1 8.559 0.01 . 1 . . . . . . . . 6051 1 402 . 1 1 47 47 VAL N N 15 129.468 0.10 . 1 . . . . . . . . 6051 1 403 . 1 1 47 47 VAL C C 13 173.947 0.20 . 1 . . . . . . . . 6051 1 404 . 1 1 47 47 VAL CA C 13 65.165 0.20 . 1 . . . . . . . . 6051 1 405 . 1 1 47 47 VAL HA H 1 3.681 0.01 . 1 . . . . . . . . 6051 1 406 . 1 1 47 47 VAL CB C 13 32.563 0.20 . 1 . . . . . . . . 6051 1 407 . 1 1 47 47 VAL HB H 1 1.802 0.01 . 1 . . . . . . . . 6051 1 408 . 1 1 47 47 VAL CG1 C 13 22.363 0.20 . 1 . . . . . . . . 6051 1 409 . 1 1 47 47 VAL HG11 H 1 0.925 0.01 . 1 . . . . . . . . 6051 1 410 . 1 1 47 47 VAL HG12 H 1 0.925 0.01 . 1 . . . . . . . . 6051 1 411 . 1 1 47 47 VAL HG13 H 1 0.925 0.01 . 1 . . . . . . . . 6051 1 412 . 1 1 47 47 VAL HG21 H 1 0.925 0.01 . 1 . . . . . . . . 6051 1 413 . 1 1 47 47 VAL HG22 H 1 0.925 0.01 . 1 . . . . . . . . 6051 1 414 . 1 1 47 47 VAL HG23 H 1 0.925 0.01 . 1 . . . . . . . . 6051 1 415 . 1 1 48 48 VAL H H 1 8.707 0.01 . 1 . . . . . . . . 6051 1 416 . 1 1 48 48 VAL N N 15 120.069 0.10 . 1 . . . . . . . . 6051 1 417 . 1 1 48 48 VAL C C 13 176.212 0.20 . 1 . . . . . . . . 6051 1 418 . 1 1 48 48 VAL CA C 13 66.123 0.20 . 1 . . . . . . . . 6051 1 419 . 1 1 48 48 VAL HA H 1 3.680 0.01 . 1 . . . . . . . . 6051 1 420 . 1 1 48 48 VAL CB C 13 31.922 0.20 . 1 . . . . . . . . 6051 1 421 . 1 1 48 48 VAL HB H 1 1.985 0.01 . 1 . . . . . . . . 6051 1 422 . 1 1 48 48 VAL CG1 C 13 23.756 0.20 . 1 . . . . . . . . 6051 1 423 . 1 1 48 48 VAL HG11 H 1 0.864 0.01 . 1 . . . . . . . . 6051 1 424 . 1 1 48 48 VAL HG12 H 1 0.864 0.01 . 1 . . . . . . . . 6051 1 425 . 1 1 48 48 VAL HG13 H 1 0.864 0.01 . 1 . . . . . . . . 6051 1 426 . 1 1 48 48 VAL HG21 H 1 0.864 0.01 . 1 . . . . . . . . 6051 1 427 . 1 1 48 48 VAL HG22 H 1 0.864 0.01 . 1 . . . . . . . . 6051 1 428 . 1 1 48 48 VAL HG23 H 1 0.864 0.01 . 1 . . . . . . . . 6051 1 429 . 1 1 49 49 SER H H 1 7.320 0.01 . 1 . . . . . . . . 6051 1 430 . 1 1 49 49 SER N N 15 109.004 0.10 . 1 . . . . . . . . 6051 1 431 . 1 1 49 49 SER C C 13 175.402 0.20 . 1 . . . . . . . . 6051 1 432 . 1 1 49 49 SER CA C 13 58.748 0.20 . 1 . . . . . . . . 6051 1 433 . 1 1 49 49 SER CB C 13 67.603 0.20 . 1 . . . . . . . . 6051 1 434 . 1 1 50 50 GLY H H 1 8.642 0.01 . 1 . . . . . . . . 6051 1 435 . 1 1 50 50 GLY N N 15 111.370 0.10 . 1 . . . . . . . . 6051 1 436 . 1 1 50 50 GLY C C 13 174.030 0.20 . 1 . . . . . . . . 6051 1 437 . 1 1 50 50 GLY CA C 13 45.474 0.20 . 1 . . . . . . . . 6051 1 438 . 1 1 50 50 GLY HA2 H 1 4.329 0.01 . 2 . . . . . . . . 6051 1 439 . 1 1 50 50 GLY HA3 H 1 3.531 0.01 . 2 . . . . . . . . 6051 1 440 . 1 1 51 51 GLU H H 1 8.180 0.01 . 1 . . . . . . . . 6051 1 441 . 1 1 51 51 GLU N N 15 124.802 0.10 . 1 . . . . . . . . 6051 1 442 . 1 1 51 51 GLU C C 13 173.412 0.20 . 1 . . . . . . . . 6051 1 443 . 1 1 51 51 GLU CA C 13 55.180 0.20 . 1 . . . . . . . . 6051 1 444 . 1 1 51 51 GLU CB C 13 31.307 0.20 . 1 . . . . . . . . 6051 1 445 . 1 1 52 52 PRO C C 13 174.228 0.20 . 1 . . . . . . . . 6051 1 446 . 1 1 52 52 PRO CA C 13 64.715 0.20 . 1 . . . . . . . . 6051 1 447 . 1 1 52 52 PRO CB C 13 32.819 0.20 . 1 . . . . . . . . 6051 1 448 . 1 1 53 53 LEU H H 1 8.245 0.01 . 1 . . . . . . . . 6051 1 449 . 1 1 53 53 LEU N N 15 121.557 0.10 . 1 . . . . . . . . 6051 1 450 . 1 1 53 53 LEU C C 13 174.344 0.20 . 1 . . . . . . . . 6051 1 451 . 1 1 53 53 LEU CA C 13 56.576 0.20 . 1 . . . . . . . . 6051 1 452 . 1 1 53 53 LEU HA H 1 3.891 0.01 . 1 . . . . . . . . 6051 1 453 . 1 1 53 53 LEU CB C 13 47.583 0.20 . 1 . . . . . . . . 6051 1 454 . 1 1 53 53 LEU HB2 H 1 1.655 0.01 . 1 . . . . . . . . 6051 1 455 . 1 1 53 53 LEU HB3 H 1 1.655 0.01 . 1 . . . . . . . . 6051 1 456 . 1 1 53 53 LEU HD11 H 1 0.624 0.01 . 1 . . . . . . . . 6051 1 457 . 1 1 53 53 LEU HD12 H 1 0.624 0.01 . 1 . . . . . . . . 6051 1 458 . 1 1 53 53 LEU HD13 H 1 0.624 0.01 . 1 . . . . . . . . 6051 1 459 . 1 1 53 53 LEU HD21 H 1 0.165 0.01 . 1 . . . . . . . . 6051 1 460 . 1 1 53 53 LEU HD22 H 1 0.165 0.01 . 1 . . . . . . . . 6051 1 461 . 1 1 53 53 LEU HD23 H 1 0.165 0.01 . 1 . . . . . . . . 6051 1 462 . 1 1 54 54 PHE H H 1 7.857 0.01 . 1 . . . . . . . . 6051 1 463 . 1 1 54 54 PHE N N 15 111.671 0.10 . 1 . . . . . . . . 6051 1 464 . 1 1 54 54 PHE C C 13 173.418 0.20 . 1 . . . . . . . . 6051 1 465 . 1 1 54 54 PHE CA C 13 57.378 0.20 . 1 . . . . . . . . 6051 1 466 . 1 1 54 54 PHE HA H 1 4.306 0.01 . 1 . . . . . . . . 6051 1 467 . 1 1 54 54 PHE CB C 13 45.795 0.20 . 1 . . . . . . . . 6051 1 468 . 1 1 54 54 PHE HB2 H 1 1.498 0.01 . 1 . . . . . . . . 6051 1 469 . 1 1 54 54 PHE HB3 H 1 1.498 0.01 . 1 . . . . . . . . 6051 1 470 . 1 1 55 55 SER H H 1 10.353 0.01 . 1 . . . . . . . . 6051 1 471 . 1 1 55 55 SER N N 15 116.741 0.10 . 1 . . . . . . . . 6051 1 472 . 1 1 55 55 SER C C 13 175.387 0.20 . 1 . . . . . . . . 6051 1 473 . 1 1 55 55 SER CA C 13 55.975 0.20 . 1 . . . . . . . . 6051 1 474 . 1 1 55 55 SER HA H 1 5.029 0.01 . 1 . . . . . . . . 6051 1 475 . 1 1 55 55 SER CB C 13 64.494 0.20 . 1 . . . . . . . . 6051 1 476 . 1 1 55 55 SER HB2 H 1 3.719 0.01 . 1 . . . . . . . . 6051 1 477 . 1 1 55 55 SER HB3 H 1 3.719 0.01 . 1 . . . . . . . . 6051 1 478 . 1 1 56 56 SER H H 1 9.179 0.01 . 1 . . . . . . . . 6051 1 479 . 1 1 56 56 SER N N 15 123.558 0.10 . 1 . . . . . . . . 6051 1 480 . 1 1 56 56 SER C C 13 176.725 0.20 . 1 . . . . . . . . 6051 1 481 . 1 1 56 56 SER CA C 13 62.648 0.20 . 1 . . . . . . . . 6051 1 482 . 1 1 56 56 SER HA H 1 4.179 0.01 . 1 . . . . . . . . 6051 1 483 . 1 1 56 56 SER CB C 13 64.985 0.20 . 1 . . . . . . . . 6051 1 484 . 1 1 56 56 SER HB2 H 1 3.664 0.01 . 1 . . . . . . . . 6051 1 485 . 1 1 56 56 SER HB3 H 1 3.664 0.01 . 1 . . . . . . . . 6051 1 486 . 1 1 57 57 ALA H H 1 8.763 0.01 . 1 . . . . . . . . 6051 1 487 . 1 1 57 57 ALA N N 15 125.489 0.10 . 1 . . . . . . . . 6051 1 488 . 1 1 57 57 ALA C C 13 177.221 0.20 . 1 . . . . . . . . 6051 1 489 . 1 1 57 57 ALA CA C 13 55.167 0.20 . 1 . . . . . . . . 6051 1 490 . 1 1 57 57 ALA HA H 1 4.301 0.01 . 1 . . . . . . . . 6051 1 491 . 1 1 57 57 ALA CB C 13 20.190 0.20 . 1 . . . . . . . . 6051 1 492 . 1 1 57 57 ALA HB1 H 1 1.518 0.01 . 1 . . . . . . . . 6051 1 493 . 1 1 57 57 ALA HB2 H 1 1.518 0.01 . 1 . . . . . . . . 6051 1 494 . 1 1 57 57 ALA HB3 H 1 1.518 0.01 . 1 . . . . . . . . 6051 1 495 . 1 1 58 58 ASP H H 1 7.653 0.01 . 1 . . . . . . . . 6051 1 496 . 1 1 58 58 ASP N N 15 114.134 0.10 . 1 . . . . . . . . 6051 1 497 . 1 1 58 58 ASP C C 13 173.617 0.20 . 1 . . . . . . . . 6051 1 498 . 1 1 58 58 ASP CA C 13 54.852 0.20 . 1 . . . . . . . . 6051 1 499 . 1 1 58 58 ASP HA H 1 4.408 0.01 . 1 . . . . . . . . 6051 1 500 . 1 1 58 58 ASP CB C 13 42.928 0.20 . 1 . . . . . . . . 6051 1 501 . 1 1 58 58 ASP HB2 H 1 2.917 0.01 . 2 . . . . . . . . 6051 1 502 . 1 1 58 58 ASP HB3 H 1 1.615 0.01 . 2 . . . . . . . . 6051 1 503 . 1 1 59 59 LYS H H 1 7.644 0.01 . 1 . . . . . . . . 6051 1 504 . 1 1 59 59 LYS N N 15 124.534 0.10 . 1 . . . . . . . . 6051 1 505 . 1 1 59 59 LYS C C 13 175.419 0.20 . 1 . . . . . . . . 6051 1 506 . 1 1 59 59 LYS CA C 13 56.263 0.20 . 1 . . . . . . . . 6051 1 507 . 1 1 59 59 LYS CB C 13 36.528 0.20 . 1 . . . . . . . . 6051 1 508 . 1 1 60 60 TYR H H 1 8.818 0.01 . 1 . . . . . . . . 6051 1 509 . 1 1 60 60 TYR N N 15 124.536 0.10 . 1 . . . . . . . . 6051 1 510 . 1 1 60 60 TYR C C 13 172.261 0.20 . 1 . . . . . . . . 6051 1 511 . 1 1 60 60 TYR CA C 13 56.421 0.20 . 1 . . . . . . . . 6051 1 512 . 1 1 60 60 TYR HA H 1 4.652 0.01 . 1 . . . . . . . . 6051 1 513 . 1 1 60 60 TYR CB C 13 41.833 0.20 . 1 . . . . . . . . 6051 1 514 . 1 1 60 60 TYR HB2 H 1 3.024 0.01 . 1 . . . . . . . . 6051 1 515 . 1 1 60 60 TYR HB3 H 1 3.024 0.01 . 1 . . . . . . . . 6051 1 516 . 1 1 61 61 ASP H H 1 8.938 0.01 . 1 . . . . . . . . 6051 1 517 . 1 1 61 61 ASP N N 15 122.263 0.10 . 1 . . . . . . . . 6051 1 518 . 1 1 61 61 ASP C C 13 174.791 0.20 . 1 . . . . . . . . 6051 1 519 . 1 1 61 61 ASP CA C 13 52.985 0.20 . 1 . . . . . . . . 6051 1 520 . 1 1 61 61 ASP CB C 13 41.665 0.20 . 1 . . . . . . . . 6051 1 521 . 1 1 62 62 SER H H 1 7.995 0.01 . 1 . . . . . . . . 6051 1 522 . 1 1 62 62 SER N N 15 121.457 0.10 . 1 . . . . . . . . 6051 1 523 . 1 1 62 62 SER C C 13 175.617 0.20 . 1 . . . . . . . . 6051 1 524 . 1 1 62 62 SER CA C 13 59.079 0.20 . 1 . . . . . . . . 6051 1 525 . 1 1 62 62 SER HA H 1 4.245 0.01 . 1 . . . . . . . . 6051 1 526 . 1 1 62 62 SER CB C 13 65.666 0.20 . 1 . . . . . . . . 6051 1 527 . 1 1 62 62 SER HB2 H 1 3.991 0.01 . 2 . . . . . . . . 6051 1 528 . 1 1 62 62 SER HB3 H 1 3.773 0.01 . 2 . . . . . . . . 6051 1 529 . 1 1 63 63 GLY H H 1 8.707 0.01 . 1 . . . . . . . . 6051 1 530 . 1 1 63 63 GLY N N 15 111.644 0.10 . 1 . . . . . . . . 6051 1 531 . 1 1 63 63 GLY C C 13 173.980 0.20 . 1 . . . . . . . . 6051 1 532 . 1 1 63 63 GLY CA C 13 46.424 0.20 . 1 . . . . . . . . 6051 1 533 . 1 1 63 63 GLY HA2 H 1 4.046 0.01 . 1 . . . . . . . . 6051 1 534 . 1 1 63 63 GLY HA3 H 1 4.046 0.01 . 1 . . . . . . . . 6051 1 535 . 1 1 64 64 CYS H H 1 7.394 0.01 . 1 . . . . . . . . 6051 1 536 . 1 1 64 64 CYS N N 15 113.425 0.10 . 1 . . . . . . . . 6051 1 537 . 1 1 64 64 CYS C C 13 172.906 0.20 . 1 . . . . . . . . 6051 1 538 . 1 1 64 64 CYS CA C 13 59.856 0.20 . 1 . . . . . . . . 6051 1 539 . 1 1 64 64 CYS HA H 1 4.369 0.01 . 1 . . . . . . . . 6051 1 540 . 1 1 64 64 CYS CB C 13 30.043 0.20 . 1 . . . . . . . . 6051 1 541 . 1 1 64 64 CYS HB2 H 1 2.982 0.01 . 1 . . . . . . . . 6051 1 542 . 1 1 64 64 CYS HB3 H 1 2.982 0.01 . 1 . . . . . . . . 6051 1 543 . 1 1 65 65 GLY H H 1 8.587 0.01 . 1 . . . . . . . . 6051 1 544 . 1 1 65 65 GLY N N 15 108.230 0.10 . 1 . . . . . . . . 6051 1 545 . 1 1 65 65 GLY C C 13 172.906 0.20 . 1 . . . . . . . . 6051 1 546 . 1 1 65 65 GLY CA C 13 43.131 0.20 . 1 . . . . . . . . 6051 1 547 . 1 1 66 66 TRP H H 1 7.056 0.01 . 1 . . . . . . . . 6051 1 548 . 1 1 66 66 TRP N N 15 119.325 0.10 . 1 . . . . . . . . 6051 1 549 . 1 1 66 66 TRP C C 13 172.903 0.20 . 1 . . . . . . . . 6051 1 550 . 1 1 66 66 TRP CA C 13 57.989 0.20 . 1 . . . . . . . . 6051 1 551 . 1 1 66 66 TRP HA H 1 4.779 0.01 . 1 . . . . . . . . 6051 1 552 . 1 1 66 66 TRP CB C 13 30.801 0.20 . 1 . . . . . . . . 6051 1 553 . 1 1 66 66 TRP HB2 H 1 3.240 0.01 . 1 . . . . . . . . 6051 1 554 . 1 1 66 66 TRP HB3 H 1 3.240 0.01 . 1 . . . . . . . . 6051 1 555 . 1 1 67 67 PRO C C 13 178.114 0.20 . 1 . . . . . . . . 6051 1 556 . 1 1 67 67 PRO CA C 13 59.326 0.20 . 1 . . . . . . . . 6051 1 557 . 1 1 67 67 PRO CB C 13 29.759 0.20 . 1 . . . . . . . . 6051 1 558 . 1 1 68 68 SER H H 1 12.330 0.01 . 1 . . . . . . . . 6051 1 559 . 1 1 68 68 SER N N 15 121.377 0.10 . 1 . . . . . . . . 6051 1 560 . 1 1 68 68 SER C C 13 170.856 0.20 . 1 . . . . . . . . 6051 1 561 . 1 1 68 68 SER CA C 13 56.614 0.20 . 1 . . . . . . . . 6051 1 562 . 1 1 68 68 SER CB C 13 67.357 0.20 . 1 . . . . . . . . 6051 1 563 . 1 1 69 69 PHE H H 1 8.790 0.01 . 1 . . . . . . . . 6051 1 564 . 1 1 69 69 PHE N N 15 119.287 0.10 . 1 . . . . . . . . 6051 1 565 . 1 1 69 69 PHE C C 13 175.997 0.20 . 1 . . . . . . . . 6051 1 566 . 1 1 69 69 PHE CA C 13 55.018 0.20 . 1 . . . . . . . . 6051 1 567 . 1 1 69 69 PHE HA H 1 5.994 0.01 . 1 . . . . . . . . 6051 1 568 . 1 1 69 69 PHE CB C 13 45.455 0.20 . 1 . . . . . . . . 6051 1 569 . 1 1 69 69 PHE HB2 H 1 2.992 0.01 . 2 . . . . . . . . 6051 1 570 . 1 1 69 69 PHE HB3 H 1 2.238 0.01 . 2 . . . . . . . . 6051 1 571 . 1 1 70 70 THR H H 1 9.558 0.01 . 1 . . . . . . . . 6051 1 572 . 1 1 70 70 THR N N 15 111.790 0.10 . 1 . . . . . . . . 6051 1 573 . 1 1 70 70 THR C C 13 173.964 0.20 . 1 . . . . . . . . 6051 1 574 . 1 1 70 70 THR CA C 13 63.291 0.20 . 1 . . . . . . . . 6051 1 575 . 1 1 70 70 THR HA H 1 5.103 0.01 . 1 . . . . . . . . 6051 1 576 . 1 1 70 70 THR CB C 13 69.624 0.20 . 1 . . . . . . . . 6051 1 577 . 1 1 70 70 THR HB H 1 4.526 0.01 . 1 . . . . . . . . 6051 1 578 . 1 1 70 70 THR CG2 C 13 21.930 0.20 . 1 . . . . . . . . 6051 1 579 . 1 1 70 70 THR HG21 H 1 1.122 0.01 . 1 . . . . . . . . 6051 1 580 . 1 1 70 70 THR HG22 H 1 1.122 0.01 . 1 . . . . . . . . 6051 1 581 . 1 1 70 70 THR HG23 H 1 1.122 0.01 . 1 . . . . . . . . 6051 1 582 . 1 1 71 71 ARG H H 1 7.172 0.01 . 1 . . . . . . . . 6051 1 583 . 1 1 71 71 ARG N N 15 112.543 0.10 . 1 . . . . . . . . 6051 1 584 . 1 1 71 71 ARG C C 13 172.073 0.20 . 1 . . . . . . . . 6051 1 585 . 1 1 71 71 ARG CA C 13 54.709 0.20 . 1 . . . . . . . . 6051 1 586 . 1 1 71 71 ARG HA H 1 4.662 0.01 . 1 . . . . . . . . 6051 1 587 . 1 1 71 71 ARG CB C 13 29.875 0.20 . 1 . . . . . . . . 6051 1 588 . 1 1 71 71 ARG HB2 H 1 1.657 0.01 . 1 . . . . . . . . 6051 1 589 . 1 1 71 71 ARG HB3 H 1 1.657 0.01 . 1 . . . . . . . . 6051 1 590 . 1 1 71 71 ARG CG C 13 25.588 0.20 . 1 . . . . . . . . 6051 1 591 . 1 1 71 71 ARG HG2 H 1 1.430 0.01 . 1 . . . . . . . . 6051 1 592 . 1 1 71 71 ARG HG3 H 1 1.430 0.01 . 1 . . . . . . . . 6051 1 593 . 1 1 71 71 ARG CD C 13 42.715 0.20 . 1 . . . . . . . . 6051 1 594 . 1 1 71 71 ARG HD2 H 1 2.899 0.01 . 1 . . . . . . . . 6051 1 595 . 1 1 71 71 ARG HD3 H 1 2.899 0.01 . 1 . . . . . . . . 6051 1 596 . 1 1 72 72 PRO C C 13 175.749 0.20 . 1 . . . . . . . . 6051 1 597 . 1 1 72 72 PRO CA C 13 61.554 0.20 . 1 . . . . . . . . 6051 1 598 . 1 1 72 72 PRO HA H 1 4.371 0.01 . 1 . . . . . . . . 6051 1 599 . 1 1 72 72 PRO CB C 13 32.103 0.20 . 1 . . . . . . . . 6051 1 600 . 1 1 72 72 PRO HB2 H 1 1.543 0.01 . 2 . . . . . . . . 6051 1 601 . 1 1 72 72 PRO HB3 H 1 1.327 0.01 . 2 . . . . . . . . 6051 1 602 . 1 1 72 72 PRO HG2 H 1 1.278 0.01 . 1 . . . . . . . . 6051 1 603 . 1 1 72 72 PRO HG3 H 1 1.278 0.01 . 1 . . . . . . . . 6051 1 604 . 1 1 72 72 PRO HD2 H 1 3.643 0.01 . 1 . . . . . . . . 6051 1 605 . 1 1 72 72 PRO HD3 H 1 3.643 0.01 . 1 . . . . . . . . 6051 1 606 . 1 1 73 73 ILE H H 1 8.153 0.01 . 1 . . . . . . . . 6051 1 607 . 1 1 73 73 ILE N N 15 121.552 0.10 . 1 . . . . . . . . 6051 1 608 . 1 1 73 73 ILE C C 13 173.088 0.20 . 1 . . . . . . . . 6051 1 609 . 1 1 73 73 ILE CA C 13 64.571 0.20 . 1 . . . . . . . . 6051 1 610 . 1 1 73 73 ILE HA H 1 4.082 0.01 . 1 . . . . . . . . 6051 1 611 . 1 1 73 73 ILE CB C 13 39.560 0.20 . 1 . . . . . . . . 6051 1 612 . 1 1 74 74 ASP H H 1 6.879 0.01 . 1 . . . . . . . . 6051 1 613 . 1 1 74 74 ASP N N 15 118.080 0.10 . 1 . . . . . . . . 6051 1 614 . 1 1 74 74 ASP C C 13 170.980 0.20 . 1 . . . . . . . . 6051 1 615 . 1 1 74 74 ASP CA C 13 53.795 0.20 . 1 . . . . . . . . 6051 1 616 . 1 1 74 74 ASP HA H 1 4.419 0.01 . 1 . . . . . . . . 6051 1 617 . 1 1 74 74 ASP CB C 13 45.539 0.20 . 1 . . . . . . . . 6051 1 618 . 1 1 74 74 ASP HB2 H 1 2.552 0.01 . 2 . . . . . . . . 6051 1 619 . 1 1 74 74 ASP HB3 H 1 2.379 0.01 . 2 . . . . . . . . 6051 1 620 . 1 1 75 75 ALA C C 13 177.965 0.20 . 1 . . . . . . . . 6051 1 621 . 1 1 75 75 ALA CA C 13 55.367 0.20 . 1 . . . . . . . . 6051 1 622 . 1 1 75 75 ALA HA H 1 3.927 0.01 . 1 . . . . . . . . 6051 1 623 . 1 1 75 75 ALA CB C 13 19.308 0.20 . 1 . . . . . . . . 6051 1 624 . 1 1 75 75 ALA HB1 H 1 1.323 0.01 . 1 . . . . . . . . 6051 1 625 . 1 1 75 75 ALA HB2 H 1 1.323 0.01 . 1 . . . . . . . . 6051 1 626 . 1 1 75 75 ALA HB3 H 1 1.323 0.01 . 1 . . . . . . . . 6051 1 627 . 1 1 76 76 LYS H H 1 8.375 0.01 . 1 . . . . . . . . 6051 1 628 . 1 1 76 76 LYS N N 15 113.642 0.10 . 1 . . . . . . . . 6051 1 629 . 1 1 76 76 LYS CA C 13 56.580 0.20 . 1 . . . . . . . . 6051 1 630 . 1 1 76 76 LYS HA H 1 4.202 0.01 . 1 . . . . . . . . 6051 1 631 . 1 1 76 76 LYS CB C 13 32.193 0.20 . 1 . . . . . . . . 6051 1 632 . 1 1 76 76 LYS HB2 H 1 1.515 0.01 . 1 . . . . . . . . 6051 1 633 . 1 1 76 76 LYS HB3 H 1 1.515 0.01 . 1 . . . . . . . . 6051 1 634 . 1 1 76 76 LYS CG C 13 24.889 0.20 . 1 . . . . . . . . 6051 1 635 . 1 1 76 76 LYS HG2 H 1 1.169 0.01 . 1 . . . . . . . . 6051 1 636 . 1 1 76 76 LYS HG3 H 1 1.169 0.01 . 1 . . . . . . . . 6051 1 637 . 1 1 76 76 LYS CD C 13 25.407 0.20 . 1 . . . . . . . . 6051 1 638 . 1 1 76 76 LYS HD2 H 1 1.333 0.01 . 1 . . . . . . . . 6051 1 639 . 1 1 76 76 LYS HD3 H 1 1.333 0.01 . 1 . . . . . . . . 6051 1 640 . 1 1 76 76 LYS CE C 13 42.434 0.20 . 1 . . . . . . . . 6051 1 641 . 1 1 76 76 LYS HE2 H 1 2.834 0.01 . 1 . . . . . . . . 6051 1 642 . 1 1 76 76 LYS HE3 H 1 2.834 0.01 . 1 . . . . . . . . 6051 1 643 . 1 1 77 77 SER H H 1 7.607 0.01 . 1 . . . . . . . . 6051 1 644 . 1 1 77 77 SER N N 15 114.348 0.10 . 1 . . . . . . . . 6051 1 645 . 1 1 77 77 SER C C 13 172.228 0.20 . 1 . . . . . . . . 6051 1 646 . 1 1 77 77 SER CA C 13 62.670 0.20 . 1 . . . . . . . . 6051 1 647 . 1 1 77 77 SER HA H 1 4.155 0.01 . 1 . . . . . . . . 6051 1 648 . 1 1 77 77 SER CB C 13 64.941 0.20 . 1 . . . . . . . . 6051 1 649 . 1 1 77 77 SER HB2 H 1 4.276 0.01 . 1 . . . . . . . . 6051 1 650 . 1 1 77 77 SER HB3 H 1 4.276 0.01 . 1 . . . . . . . . 6051 1 651 . 1 1 78 78 VAL H H 1 7.098 0.01 . 1 . . . . . . . . 6051 1 652 . 1 1 78 78 VAL N N 15 109.472 0.10 . 1 . . . . . . . . 6051 1 653 . 1 1 78 78 VAL C C 13 174.129 0.20 . 1 . . . . . . . . 6051 1 654 . 1 1 78 78 VAL CA C 13 58.625 0.20 . 1 . . . . . . . . 6051 1 655 . 1 1 78 78 VAL HA H 1 5.113 0.01 . 1 . . . . . . . . 6051 1 656 . 1 1 78 78 VAL CB C 13 35.682 0.20 . 1 . . . . . . . . 6051 1 657 . 1 1 78 78 VAL HB H 1 1.998 0.01 . 1 . . . . . . . . 6051 1 658 . 1 1 78 78 VAL CG1 C 13 19.554 0.20 . 1 . . . . . . . . 6051 1 659 . 1 1 78 78 VAL HG11 H 1 0.518 0.01 . 1 . . . . . . . . 6051 1 660 . 1 1 78 78 VAL HG12 H 1 0.518 0.01 . 1 . . . . . . . . 6051 1 661 . 1 1 78 78 VAL HG13 H 1 0.518 0.01 . 1 . . . . . . . . 6051 1 662 . 1 1 78 78 VAL CG2 C 13 22.635 0.20 . 1 . . . . . . . . 6051 1 663 . 1 1 78 78 VAL HG21 H 1 0.420 0.01 . 2 . . . . . . . . 6051 1 664 . 1 1 78 78 VAL HG22 H 1 0.420 0.01 . 2 . . . . . . . . 6051 1 665 . 1 1 78 78 VAL HG23 H 1 0.420 0.01 . 2 . . . . . . . . 6051 1 666 . 1 1 79 79 THR H H 1 9.373 0.01 . 1 . . . . . . . . 6051 1 667 . 1 1 79 79 THR N N 15 113.769 0.10 . 1 . . . . . . . . 6051 1 668 . 1 1 79 79 THR C C 13 172.244 0.20 . 1 . . . . . . . . 6051 1 669 . 1 1 79 79 THR CA C 13 60.003 0.20 . 1 . . . . . . . . 6051 1 670 . 1 1 79 79 THR HA H 1 4.486 0.01 . 1 . . . . . . . . 6051 1 671 . 1 1 79 79 THR CB C 13 71.115 0.20 . 1 . . . . . . . . 6051 1 672 . 1 1 79 79 THR HB H 1 4.040 0.01 . 1 . . . . . . . . 6051 1 673 . 1 1 79 79 THR CG2 C 13 22.341 0.20 . 1 . . . . . . . . 6051 1 674 . 1 1 79 79 THR HG21 H 1 1.048 0.01 . 1 . . . . . . . . 6051 1 675 . 1 1 79 79 THR HG22 H 1 1.048 0.01 . 1 . . . . . . . . 6051 1 676 . 1 1 79 79 THR HG23 H 1 1.048 0.01 . 1 . . . . . . . . 6051 1 677 . 1 1 80 80 GLU H H 1 8.060 0.01 . 1 . . . . . . . . 6051 1 678 . 1 1 80 80 GLU N N 15 120.750 0.10 . 1 . . . . . . . . 6051 1 679 . 1 1 80 80 GLU C C 13 175.948 0.20 . 1 . . . . . . . . 6051 1 680 . 1 1 80 80 GLU CA C 13 55.320 0.20 . 1 . . . . . . . . 6051 1 681 . 1 1 80 80 GLU HA H 1 5.171 0.01 . 1 . . . . . . . . 6051 1 682 . 1 1 80 80 GLU CB C 13 33.244 0.20 . 1 . . . . . . . . 6051 1 683 . 1 1 80 80 GLU HB2 H 1 1.586 0.01 . 1 . . . . . . . . 6051 1 684 . 1 1 80 80 GLU HB3 H 1 1.586 0.01 . 1 . . . . . . . . 6051 1 685 . 1 1 80 80 GLU HG2 H 1 2.082 0.01 . 2 . . . . . . . . 6051 1 686 . 1 1 80 80 GLU HG3 H 1 1.872 0.01 . 2 . . . . . . . . 6051 1 687 . 1 1 81 81 HIS H H 1 8.772 0.01 . 1 . . . . . . . . 6051 1 688 . 1 1 81 81 HIS N N 15 119.556 0.10 . 1 . . . . . . . . 6051 1 689 . 1 1 81 81 HIS C C 13 173.501 0.20 . 1 . . . . . . . . 6051 1 690 . 1 1 81 81 HIS CA C 13 55.161 0.20 . 1 . . . . . . . . 6051 1 691 . 1 1 81 81 HIS HA H 1 4.572 0.01 . 1 . . . . . . . . 6051 1 692 . 1 1 81 81 HIS CB C 13 34.086 0.20 . 1 . . . . . . . . 6051 1 693 . 1 1 81 81 HIS HB3 H 1 2.324 0.01 . 2 . . . . . . . . 6051 1 694 . 1 1 82 82 ASP H H 1 8.883 0.01 . 1 . . . . . . . . 6051 1 695 . 1 1 82 82 ASP N N 15 124.614 0.10 . 1 . . . . . . . . 6051 1 696 . 1 1 82 82 ASP C C 13 174.890 0.20 . 1 . . . . . . . . 6051 1 697 . 1 1 82 82 ASP CA C 13 56.520 0.20 . 1 . . . . . . . . 6051 1 698 . 1 1 82 82 ASP HA H 1 4.553 0.01 . 1 . . . . . . . . 6051 1 699 . 1 1 82 82 ASP CB C 13 42.423 0.20 . 1 . . . . . . . . 6051 1 700 . 1 1 82 82 ASP HB2 H 1 2.447 0.01 . 2 . . . . . . . . 6051 1 701 . 1 1 82 82 ASP HB3 H 1 2.095 0.01 . 2 . . . . . . . . 6051 1 702 . 1 1 83 83 ASP H H 1 8.587 0.01 . 1 . . . . . . . . 6051 1 703 . 1 1 83 83 ASP N N 15 122.879 0.10 . 1 . . . . . . . . 6051 1 704 . 1 1 83 83 ASP C C 13 175.832 0.20 . 1 . . . . . . . . 6051 1 705 . 1 1 83 83 ASP CA C 13 53.455 0.20 . 1 . . . . . . . . 6051 1 706 . 1 1 83 83 ASP HA H 1 4.832 0.01 . 1 . . . . . . . . 6051 1 707 . 1 1 83 83 ASP CB C 13 43.914 0.20 . 1 . . . . . . . . 6051 1 708 . 1 1 83 83 ASP HB2 H 1 2.885 0.01 . 2 . . . . . . . . 6051 1 709 . 1 1 83 83 ASP HB3 H 1 2.140 0.01 . 2 . . . . . . . . 6051 1 710 . 1 1 84 84 PHE H H 1 9.132 0.01 . 1 . . . . . . . . 6051 1 711 . 1 1 84 84 PHE N N 15 128.318 0.10 . 1 . . . . . . . . 6051 1 712 . 1 1 84 84 PHE CA C 13 57.446 0.20 . 1 . . . . . . . . 6051 1 713 . 1 1 84 84 PHE HA H 1 5.568 0.01 . 1 . . . . . . . . 6051 1 714 . 1 1 84 84 PHE CB C 13 39.056 0.20 . 1 . . . . . . . . 6051 1 715 . 1 1 84 84 PHE HB2 H 1 3.568 0.01 . 2 . . . . . . . . 6051 1 716 . 1 1 84 84 PHE HB3 H 1 2.668 0.01 . 2 . . . . . . . . 6051 1 717 . 1 1 86 86 TYR C C 13 173.554 0.20 . 1 . . . . . . . . 6051 1 718 . 1 1 86 86 TYR CA C 13 55.171 0.20 . 1 . . . . . . . . 6051 1 719 . 1 1 86 86 TYR CB C 13 38.052 0.20 . 1 . . . . . . . . 6051 1 720 . 1 1 87 87 ASN H H 1 7.385 0.01 . 1 . . . . . . . . 6051 1 721 . 1 1 87 87 ASN N N 15 116.477 0.10 . 1 . . . . . . . . 6051 1 722 . 1 1 87 87 ASN C C 13 172.767 0.20 . 1 . . . . . . . . 6051 1 723 . 1 1 87 87 ASN CA C 13 55.019 0.20 . 1 . . . . . . . . 6051 1 724 . 1 1 87 87 ASN HA H 1 4.598 0.01 . 1 . . . . . . . . 6051 1 725 . 1 1 87 87 ASN CB C 13 36.666 0.20 . 1 . . . . . . . . 6051 1 726 . 1 1 87 87 ASN HB2 H 1 2.317 0.01 . 2 . . . . . . . . 6051 1 727 . 1 1 87 87 ASN HB3 H 1 1.952 0.01 . 2 . . . . . . . . 6051 1 728 . 1 1 88 88 MET H H 1 8.208 0.01 . 1 . . . . . . . . 6051 1 729 . 1 1 88 88 MET N N 15 120.066 0.10 . 1 . . . . . . . . 6051 1 730 . 1 1 88 88 MET CA C 13 56.422 0.20 . 1 . . . . . . . . 6051 1 731 . 1 1 88 88 MET HA H 1 4.194 0.01 . 1 . . . . . . . . 6051 1 732 . 1 1 88 88 MET CB C 13 31.391 0.20 . 1 . . . . . . . . 6051 1 733 . 1 1 89 89 ARG C C 13 174.840 0.20 . 1 . . . . . . . . 6051 1 734 . 1 1 89 89 ARG CA C 13 56.351 0.20 . 1 . . . . . . . . 6051 1 735 . 1 1 89 89 ARG CB C 13 31.208 0.20 . 1 . . . . . . . . 6051 1 736 . 1 1 90 90 ARG H H 1 8.615 0.01 . 1 . . . . . . . . 6051 1 737 . 1 1 90 90 ARG N N 15 124.582 0.10 . 1 . . . . . . . . 6051 1 738 . 1 1 90 90 ARG C C 13 174.129 0.20 . 1 . . . . . . . . 6051 1 739 . 1 1 90 90 ARG CA C 13 54.550 0.20 . 1 . . . . . . . . 6051 1 740 . 1 1 91 91 THR H H 1 9.151 0.01 . 1 . . . . . . . . 6051 1 741 . 1 1 91 91 THR N N 15 119.994 0.10 . 1 . . . . . . . . 6051 1 742 . 1 1 91 91 THR C C 13 173.170 0.20 . 1 . . . . . . . . 6051 1 743 . 1 1 91 91 THR CA C 13 62.518 0.20 . 1 . . . . . . . . 6051 1 744 . 1 1 91 91 THR HA H 1 4.719 0.01 . 1 . . . . . . . . 6051 1 745 . 1 1 91 91 THR CB C 13 69.684 0.20 . 1 . . . . . . . . 6051 1 746 . 1 1 91 91 THR HB H 1 3.930 0.01 . 1 . . . . . . . . 6051 1 747 . 1 1 91 91 THR CG2 C 13 22.325 0.20 . 1 . . . . . . . . 6051 1 748 . 1 1 91 91 THR HG21 H 1 0.949 0.01 . 1 . . . . . . . . 6051 1 749 . 1 1 91 91 THR HG22 H 1 0.949 0.01 . 1 . . . . . . . . 6051 1 750 . 1 1 91 91 THR HG23 H 1 0.949 0.01 . 1 . . . . . . . . 6051 1 751 . 1 1 92 92 GLU H H 1 9.401 0.01 . 1 . . . . . . . . 6051 1 752 . 1 1 92 92 GLU N N 15 129.976 0.10 . 1 . . . . . . . . 6051 1 753 . 1 1 92 92 GLU C C 13 174.344 0.20 . 1 . . . . . . . . 6051 1 754 . 1 1 92 92 GLU CA C 13 55.326 0.20 . 1 . . . . . . . . 6051 1 755 . 1 1 92 92 GLU CB C 13 31.029 0.20 . 1 . . . . . . . . 6051 1 756 . 1 1 93 93 VAL H H 1 8.291 0.01 . 1 . . . . . . . . 6051 1 757 . 1 1 93 93 VAL N N 15 123.316 0.10 . 1 . . . . . . . . 6051 1 758 . 1 1 93 93 VAL C C 13 174.228 0.20 . 1 . . . . . . . . 6051 1 759 . 1 1 93 93 VAL CA C 13 60.183 0.20 . 1 . . . . . . . . 6051 1 760 . 1 1 93 93 VAL HA H 1 5.150 0.01 . 1 . . . . . . . . 6051 1 761 . 1 1 93 93 VAL CB C 13 34.340 0.20 . 1 . . . . . . . . 6051 1 762 . 1 1 93 93 VAL HB H 1 1.487 0.01 . 1 . . . . . . . . 6051 1 763 . 1 1 93 93 VAL CG1 C 13 23.083 0.20 . 1 . . . . . . . . 6051 1 764 . 1 1 93 93 VAL HG11 H 1 0.832 0.01 . 1 . . . . . . . . 6051 1 765 . 1 1 93 93 VAL HG12 H 1 0.832 0.01 . 1 . . . . . . . . 6051 1 766 . 1 1 93 93 VAL HG13 H 1 0.832 0.01 . 1 . . . . . . . . 6051 1 767 . 1 1 93 93 VAL CG2 C 13 21.614 0.20 . 1 . . . . . . . . 6051 1 768 . 1 1 93 93 VAL HG21 H 1 0.674 0.01 . 1 . . . . . . . . 6051 1 769 . 1 1 93 93 VAL HG22 H 1 0.674 0.01 . 1 . . . . . . . . 6051 1 770 . 1 1 93 93 VAL HG23 H 1 0.674 0.01 . 1 . . . . . . . . 6051 1 771 . 1 1 94 94 ARG H H 1 8.864 0.01 . 1 . . . . . . . . 6051 1 772 . 1 1 94 94 ARG N N 15 124.658 0.10 . 1 . . . . . . . . 6051 1 773 . 1 1 94 94 ARG C C 13 174.923 0.20 . 1 . . . . . . . . 6051 1 774 . 1 1 94 94 ARG CA C 13 54.396 0.20 . 1 . . . . . . . . 6051 1 775 . 1 1 94 94 ARG HA H 1 4.212 0.01 . 1 . . . . . . . . 6051 1 776 . 1 1 94 94 ARG CB C 13 34.928 0.20 . 1 . . . . . . . . 6051 1 777 . 1 1 94 94 ARG HB2 H 1 1.445 0.01 . 1 . . . . . . . . 6051 1 778 . 1 1 94 94 ARG HB3 H 1 1.445 0.01 . 1 . . . . . . . . 6051 1 779 . 1 1 94 94 ARG CG C 13 24.462 0.20 . 1 . . . . . . . . 6051 1 780 . 1 1 94 94 ARG HG2 H 1 1.169 0.01 . 1 . . . . . . . . 6051 1 781 . 1 1 94 94 ARG HG3 H 1 1.169 0.01 . 1 . . . . . . . . 6051 1 782 . 1 1 94 94 ARG CD C 13 42.549 0.20 . 1 . . . . . . . . 6051 1 783 . 1 1 94 94 ARG HD2 H 1 2.854 0.01 . 1 . . . . . . . . 6051 1 784 . 1 1 94 94 ARG HD3 H 1 2.854 0.01 . 1 . . . . . . . . 6051 1 785 . 1 1 95 95 SER H H 1 8.818 0.01 . 1 . . . . . . . . 6051 1 786 . 1 1 95 95 SER N N 15 114.864 0.10 . 1 . . . . . . . . 6051 1 787 . 1 1 95 95 SER C C 13 175.036 0.20 . 1 . . . . . . . . 6051 1 788 . 1 1 95 95 SER CA C 13 57.050 0.20 . 1 . . . . . . . . 6051 1 789 . 1 1 95 95 SER CB C 13 66.508 0.20 . 1 . . . . . . . . 6051 1 790 . 1 1 96 96 HIS H H 1 8.273 0.01 . 1 . . . . . . . . 6051 1 791 . 1 1 96 96 HIS N N 15 122.851 0.10 . 1 . . . . . . . . 6051 1 792 . 1 1 96 96 HIS C C 13 175.501 0.20 . 1 . . . . . . . . 6051 1 793 . 1 1 96 96 HIS CA C 13 60.604 0.20 . 1 . . . . . . . . 6051 1 794 . 1 1 96 96 HIS HA H 1 4.145 0.01 . 1 . . . . . . . . 6051 1 795 . 1 1 96 96 HIS CB C 13 30.549 0.20 . 1 . . . . . . . . 6051 1 796 . 1 1 96 96 HIS HB2 H 1 3.434 0.01 . 2 . . . . . . . . 6051 1 797 . 1 1 96 96 HIS HB3 H 1 2.932 0.01 . 2 . . . . . . . . 6051 1 798 . 1 1 97 97 ALA H H 1 10.547 0.01 . 1 . . . . . . . . 6051 1 799 . 1 1 97 97 ALA N N 15 124.048 0.10 . 1 . . . . . . . . 6051 1 800 . 1 1 97 97 ALA C C 13 178.907 0.20 . 1 . . . . . . . . 6051 1 801 . 1 1 97 97 ALA CA C 13 55.801 0.20 . 1 . . . . . . . . 6051 1 802 . 1 1 97 97 ALA HA H 1 3.807 0.01 . 1 . . . . . . . . 6051 1 803 . 1 1 97 97 ALA CB C 13 17.610 0.20 . 1 . . . . . . . . 6051 1 804 . 1 1 97 97 ALA HB1 H 1 1.119 0.01 . 1 . . . . . . . . 6051 1 805 . 1 1 97 97 ALA HB2 H 1 1.119 0.01 . 1 . . . . . . . . 6051 1 806 . 1 1 97 97 ALA HB3 H 1 1.119 0.01 . 1 . . . . . . . . 6051 1 807 . 1 1 98 98 ALA H H 1 8.495 0.01 . 1 . . . . . . . . 6051 1 808 . 1 1 98 98 ALA N N 15 116.087 0.10 . 1 . . . . . . . . 6051 1 809 . 1 1 98 98 ALA C C 13 176.130 0.20 . 1 . . . . . . . . 6051 1 810 . 1 1 98 98 ALA CA C 13 52.044 0.20 . 1 . . . . . . . . 6051 1 811 . 1 1 98 98 ALA HA H 1 4.117 0.01 . 1 . . . . . . . . 6051 1 812 . 1 1 98 98 ALA CB C 13 19.601 0.20 . 1 . . . . . . . . 6051 1 813 . 1 1 98 98 ALA HB1 H 1 1.096 0.01 . 1 . . . . . . . . 6051 1 814 . 1 1 98 98 ALA HB2 H 1 1.096 0.01 . 1 . . . . . . . . 6051 1 815 . 1 1 98 98 ALA HB3 H 1 1.096 0.01 . 1 . . . . . . . . 6051 1 816 . 1 1 99 99 ASP H H 1 7.191 0.01 . 1 . . . . . . . . 6051 1 817 . 1 1 99 99 ASP N N 15 119.384 0.10 . 1 . . . . . . . . 6051 1 818 . 1 1 99 99 ASP C C 13 175.766 0.20 . 1 . . . . . . . . 6051 1 819 . 1 1 99 99 ASP CA C 13 55.635 0.20 . 1 . . . . . . . . 6051 1 820 . 1 1 99 99 ASP HA H 1 4.268 0.01 . 1 . . . . . . . . 6051 1 821 . 1 1 99 99 ASP CB C 13 40.741 0.20 . 1 . . . . . . . . 6051 1 822 . 1 1 99 99 ASP HB2 H 1 2.642 0.01 . 2 . . . . . . . . 6051 1 823 . 1 1 99 99 ASP HB3 H 1 2.489 0.01 . 2 . . . . . . . . 6051 1 824 . 1 1 100 100 SER H H 1 8.097 0.01 . 1 . . . . . . . . 6051 1 825 . 1 1 100 100 SER N N 15 113.180 0.10 . 1 . . . . . . . . 6051 1 826 . 1 1 100 100 SER C C 13 175.387 0.20 . 1 . . . . . . . . 6051 1 827 . 1 1 100 100 SER CA C 13 57.995 0.20 . 1 . . . . . . . . 6051 1 828 . 1 1 100 100 SER HA H 1 3.762 0.01 . 1 . . . . . . . . 6051 1 829 . 1 1 100 100 SER CB C 13 63.565 0.20 . 1 . . . . . . . . 6051 1 830 . 1 1 100 100 SER HB2 H 1 3.894 0.01 . 1 . . . . . . . . 6051 1 831 . 1 1 100 100 SER HB3 H 1 3.894 0.01 . 1 . . . . . . . . 6051 1 832 . 1 1 101 101 HIS H H 1 9.197 0.01 . 1 . . . . . . . . 6051 1 833 . 1 1 101 101 HIS N N 15 123.484 0.10 . 1 . . . . . . . . 6051 1 834 . 1 1 101 101 HIS C C 13 172.393 0.20 . 1 . . . . . . . . 6051 1 835 . 1 1 101 101 HIS CA C 13 59.696 0.20 . 1 . . . . . . . . 6051 1 836 . 1 1 102 102 LEU H H 1 7.542 0.01 . 1 . . . . . . . . 6051 1 837 . 1 1 102 102 LEU N N 15 121.779 0.10 . 1 . . . . . . . . 6051 1 838 . 1 1 102 102 LEU C C 13 177.122 0.20 . 1 . . . . . . . . 6051 1 839 . 1 1 102 102 LEU CA C 13 54.657 0.20 . 1 . . . . . . . . 6051 1 840 . 1 1 102 102 LEU HA H 1 4.402 0.01 . 1 . . . . . . . . 6051 1 841 . 1 1 102 102 LEU CB C 13 43.686 0.20 . 1 . . . . . . . . 6051 1 842 . 1 1 102 102 LEU HB2 H 1 1.633 0.01 . 1 . . . . . . . . 6051 1 843 . 1 1 102 102 LEU HB3 H 1 1.633 0.01 . 1 . . . . . . . . 6051 1 844 . 1 1 102 102 LEU HG H 1 1.570 0.01 . 1 . . . . . . . . 6051 1 845 . 1 1 102 102 LEU HD11 H 1 0.880 0.01 . 1 . . . . . . . . 6051 1 846 . 1 1 102 102 LEU HD12 H 1 0.880 0.01 . 1 . . . . . . . . 6051 1 847 . 1 1 102 102 LEU HD13 H 1 0.880 0.01 . 1 . . . . . . . . 6051 1 848 . 1 1 102 102 LEU HD21 H 1 0.773 0.01 . 1 . . . . . . . . 6051 1 849 . 1 1 102 102 LEU HD22 H 1 0.773 0.01 . 1 . . . . . . . . 6051 1 850 . 1 1 102 102 LEU HD23 H 1 0.773 0.01 . 1 . . . . . . . . 6051 1 851 . 1 1 103 103 GLY H H 1 6.599 0.01 . 1 . . . . . . . . 6051 1 852 . 1 1 103 103 GLY N N 15 104.534 0.10 . 1 . . . . . . . . 6051 1 853 . 1 1 103 103 GLY C C 13 170.839 0.20 . 1 . . . . . . . . 6051 1 854 . 1 1 103 103 GLY CA C 13 46.734 0.20 . 1 . . . . . . . . 6051 1 855 . 1 1 103 103 GLY HA2 H 1 3.992 0.01 . 2 . . . . . . . . 6051 1 856 . 1 1 103 103 GLY HA3 H 1 4.112 0.01 . 2 . . . . . . . . 6051 1 857 . 1 1 104 104 HIS H H 1 8.670 0.01 . 1 . . . . . . . . 6051 1 858 . 1 1 104 104 HIS N N 15 122.777 0.10 . 1 . . . . . . . . 6051 1 859 . 1 1 104 104 HIS C C 13 171.418 0.20 . 1 . . . . . . . . 6051 1 860 . 1 1 104 104 HIS CA C 13 57.198 0.20 . 1 . . . . . . . . 6051 1 861 . 1 1 104 104 HIS CB C 13 37.370 0.20 . 1 . . . . . . . . 6051 1 862 . 1 1 105 105 VAL H H 1 8.143 0.01 . 1 . . . . . . . . 6051 1 863 . 1 1 105 105 VAL N N 15 118.163 0.10 . 1 . . . . . . . . 6051 1 864 . 1 1 105 105 VAL C C 13 172.740 0.20 . 1 . . . . . . . . 6051 1 865 . 1 1 105 105 VAL CA C 13 58.296 0.20 . 1 . . . . . . . . 6051 1 866 . 1 1 105 105 VAL HA H 1 5.192 0.01 . 1 . . . . . . . . 6051 1 867 . 1 1 105 105 VAL CB C 13 34.928 0.20 . 1 . . . . . . . . 6051 1 868 . 1 1 105 105 VAL HB H 1 1.996 0.01 . 1 . . . . . . . . 6051 1 869 . 1 1 105 105 VAL CG1 C 13 19.716 0.20 . 1 . . . . . . . . 6051 1 870 . 1 1 105 105 VAL HG11 H 1 0.549 0.01 . 1 . . . . . . . . 6051 1 871 . 1 1 105 105 VAL HG12 H 1 0.549 0.01 . 1 . . . . . . . . 6051 1 872 . 1 1 105 105 VAL HG13 H 1 0.549 0.01 . 1 . . . . . . . . 6051 1 873 . 1 1 105 105 VAL CG2 C 13 22.694 0.20 . 1 . . . . . . . . 6051 1 874 . 1 1 105 105 VAL HG21 H 1 0.422 0.01 . 1 . . . . . . . . 6051 1 875 . 1 1 105 105 VAL HG22 H 1 0.422 0.01 . 1 . . . . . . . . 6051 1 876 . 1 1 105 105 VAL HG23 H 1 0.422 0.01 . 1 . . . . . . . . 6051 1 877 . 1 1 106 106 PHE H H 1 9.058 0.01 . 1 . . . . . . . . 6051 1 878 . 1 1 106 106 PHE N N 15 127.197 0.10 . 1 . . . . . . . . 6051 1 879 . 1 1 106 106 PHE C C 13 174.409 0.20 . 1 . . . . . . . . 6051 1 880 . 1 1 106 106 PHE CA C 13 55.321 0.20 . 1 . . . . . . . . 6051 1 881 . 1 1 107 107 PRO C C 13 174.807 0.20 . 1 . . . . . . . . 6051 1 882 . 1 1 107 107 PRO CA C 13 63.957 0.20 . 1 . . . . . . . . 6051 1 883 . 1 1 107 107 PRO HA H 1 5.145 0.01 . 1 . . . . . . . . 6051 1 884 . 1 1 107 107 PRO CB C 13 29.240 0.20 . 1 . . . . . . . . 6051 1 885 . 1 1 107 107 PRO HB2 H 1 2.511 0.01 . 2 . . . . . . . . 6051 1 886 . 1 1 107 107 PRO HB3 H 1 1.832 0.01 . 2 . . . . . . . . 6051 1 887 . 1 1 107 107 PRO HG2 H 1 1.793 0.01 . 1 . . . . . . . . 6051 1 888 . 1 1 107 107 PRO HG3 H 1 1.793 0.01 . 1 . . . . . . . . 6051 1 889 . 1 1 107 107 PRO HD2 H 1 3.809 0.01 . 1 . . . . . . . . 6051 1 890 . 1 1 107 107 PRO HD3 H 1 3.809 0.01 . 1 . . . . . . . . 6051 1 891 . 1 1 108 108 ASP H H 1 7.810 0.01 . 1 . . . . . . . . 6051 1 892 . 1 1 108 108 ASP N N 15 121.753 0.10 . 1 . . . . . . . . 6051 1 893 . 1 1 108 108 ASP C C 13 176.940 0.20 . 1 . . . . . . . . 6051 1 894 . 1 1 108 108 ASP CA C 13 53.151 0.20 . 1 . . . . . . . . 6051 1 895 . 1 1 108 108 ASP HA H 1 4.768 0.01 . 1 . . . . . . . . 6051 1 896 . 1 1 108 108 ASP CB C 13 41.160 0.20 . 1 . . . . . . . . 6051 1 897 . 1 1 108 108 ASP HB2 H 1 2.984 0.01 . 2 . . . . . . . . 6051 1 898 . 1 1 108 108 ASP HB3 H 1 2.139 0.01 . 2 . . . . . . . . 6051 1 899 . 1 1 109 109 GLY H H 1 7.561 0.01 . 1 . . . . . . . . 6051 1 900 . 1 1 109 109 GLY N N 15 106.879 0.10 . 1 . . . . . . . . 6051 1 901 . 1 1 109 109 GLY C C 13 170.188 0.20 . 1 . . . . . . . . 6051 1 902 . 1 1 109 109 GLY CA C 13 44.978 0.20 . 1 . . . . . . . . 6051 1 903 . 1 1 109 109 GLY HA2 H 1 4.185 0.01 . 2 . . . . . . . . 6051 1 904 . 1 1 109 109 GLY HA3 H 1 3.271 0.01 . 2 . . . . . . . . 6051 1 905 . 1 1 110 110 PRO C C 13 178.213 0.20 . 1 . . . . . . . . 6051 1 906 . 1 1 110 110 PRO CA C 13 66.462 0.20 . 1 . . . . . . . . 6051 1 907 . 1 1 110 110 PRO HA H 1 4.623 0.01 . 1 . . . . . . . . 6051 1 908 . 1 1 110 110 PRO CB C 13 39.082 0.20 . 1 . . . . . . . . 6051 1 909 . 1 1 110 110 PRO HB2 H 1 1.857 0.01 . 2 . . . . . . . . 6051 1 910 . 1 1 110 110 PRO HB3 H 1 1.424 0.01 . 2 . . . . . . . . 6051 1 911 . 1 1 110 110 PRO HG2 H 1 1.424 0.01 . 1 . . . . . . . . 6051 1 912 . 1 1 110 110 PRO HG3 H 1 1.424 0.01 . 1 . . . . . . . . 6051 1 913 . 1 1 110 110 PRO HD2 H 1 3.896 0.01 . 1 . . . . . . . . 6051 1 914 . 1 1 110 110 PRO HD3 H 1 3.896 0.01 . 1 . . . . . . . . 6051 1 915 . 1 1 111 111 ARG H H 1 8.393 0.01 . 1 . . . . . . . . 6051 1 916 . 1 1 111 111 ARG N N 15 117.601 0.10 . 1 . . . . . . . . 6051 1 917 . 1 1 111 111 ARG C C 13 177.618 0.20 . 1 . . . . . . . . 6051 1 918 . 1 1 111 111 ARG CA C 13 59.082 0.20 . 1 . . . . . . . . 6051 1 919 . 1 1 111 111 ARG HA H 1 3.718 0.01 . 1 . . . . . . . . 6051 1 920 . 1 1 111 111 ARG CB C 13 30.313 0.20 . 1 . . . . . . . . 6051 1 921 . 1 1 111 111 ARG HB2 H 1 1.598 0.01 . 2 . . . . . . . . 6051 1 922 . 1 1 111 111 ARG HB3 H 1 1.165 0.01 . 2 . . . . . . . . 6051 1 923 . 1 1 111 111 ARG HG2 H 1 0.785 0.01 . 1 . . . . . . . . 6051 1 924 . 1 1 111 111 ARG HG3 H 1 0.785 0.01 . 1 . . . . . . . . 6051 1 925 . 1 1 111 111 ARG HD2 H 1 2.535 0.01 . 1 . . . . . . . . 6051 1 926 . 1 1 111 111 ARG HD3 H 1 2.535 0.01 . 1 . . . . . . . . 6051 1 927 . 1 1 112 112 ASP H H 1 8.920 0.01 . 1 . . . . . . . . 6051 1 928 . 1 1 112 112 ASP N N 15 115.991 0.10 . 1 . . . . . . . . 6051 1 929 . 1 1 112 112 ASP C C 13 175.650 0.20 . 1 . . . . . . . . 6051 1 930 . 1 1 112 112 ASP CA C 13 55.318 0.20 . 1 . . . . . . . . 6051 1 931 . 1 1 112 112 ASP HA H 1 3.822 0.01 . 1 . . . . . . . . 6051 1 932 . 1 1 112 112 ASP CB C 13 39.858 0.20 . 1 . . . . . . . . 6051 1 933 . 1 1 112 112 ASP HB2 H 1 2.728 0.01 . 2 . . . . . . . . 6051 1 934 . 1 1 112 112 ASP HB3 H 1 2.566 0.01 . 2 . . . . . . . . 6051 1 935 . 1 1 113 113 LYS H H 1 7.062 0.01 . 1 . . . . . . . . 6051 1 936 . 1 1 113 113 LYS N N 15 116.845 0.10 . 1 . . . . . . . . 6051 1 937 . 1 1 113 113 LYS C C 13 176.378 0.20 . 1 . . . . . . . . 6051 1 938 . 1 1 113 113 LYS CA C 13 54.700 0.20 . 1 . . . . . . . . 6051 1 939 . 1 1 113 113 LYS HA H 1 4.672 0.01 . 1 . . . . . . . . 6051 1 940 . 1 1 113 113 LYS CB C 13 34.170 0.20 . 1 . . . . . . . . 6051 1 941 . 1 1 113 113 LYS HB2 H 1 1.687 0.01 . 2 . . . . . . . . 6051 1 942 . 1 1 113 113 LYS HB3 H 1 1.657 0.01 . 2 . . . . . . . . 6051 1 943 . 1 1 113 113 LYS HG2 H 1 1.570 0.01 . 1 . . . . . . . . 6051 1 944 . 1 1 113 113 LYS HG3 H 1 1.570 0.01 . 1 . . . . . . . . 6051 1 945 . 1 1 113 113 LYS HD2 H 1 1.500 0.01 . 1 . . . . . . . . 6051 1 946 . 1 1 113 113 LYS HD3 H 1 1.500 0.01 . 1 . . . . . . . . 6051 1 947 . 1 1 113 113 LYS HE2 H 1 3.032 0.01 . 1 . . . . . . . . 6051 1 948 . 1 1 113 113 LYS HE3 H 1 3.032 0.01 . 1 . . . . . . . . 6051 1 949 . 1 1 114 114 GLY H H 1 7.635 0.01 . 1 . . . . . . . . 6051 1 950 . 1 1 114 114 GLY N N 15 108.202 0.10 . 1 . . . . . . . . 6051 1 951 . 1 1 114 114 GLY C C 13 174.576 0.20 . 1 . . . . . . . . 6051 1 952 . 1 1 114 114 GLY CA C 13 45.943 0.20 . 1 . . . . . . . . 6051 1 953 . 1 1 114 114 GLY HA2 H 1 4.459 0.01 . 2 . . . . . . . . 6051 1 954 . 1 1 114 114 GLY HA3 H 1 3.648 0.01 . 2 . . . . . . . . 6051 1 955 . 1 1 115 115 GLY H H 1 7.773 0.01 . 1 . . . . . . . . 6051 1 956 . 1 1 115 115 GLY N N 15 106.466 0.10 . 1 . . . . . . . . 6051 1 957 . 1 1 115 115 GLY C C 13 172.790 0.20 . 1 . . . . . . . . 6051 1 958 . 1 1 115 115 GLY CA C 13 45.955 0.20 . 1 . . . . . . . . 6051 1 959 . 1 1 115 115 GLY HA2 H 1 4.445 0.01 . 2 . . . . . . . . 6051 1 960 . 1 1 115 115 GLY HA3 H 1 3.461 0.01 . 2 . . . . . . . . 6051 1 961 . 1 1 116 116 LEU H H 1 8.698 0.01 . 1 . . . . . . . . 6051 1 962 . 1 1 116 116 LEU N N 15 122.264 0.10 . 1 . . . . . . . . 6051 1 963 . 1 1 116 116 LEU C C 13 173.716 0.20 . 1 . . . . . . . . 6051 1 964 . 1 1 116 116 LEU CA C 13 54.543 0.20 . 1 . . . . . . . . 6051 1 965 . 1 1 116 116 LEU HA H 1 4.980 0.01 . 1 . . . . . . . . 6051 1 966 . 1 1 116 116 LEU CB C 13 44.612 0.20 . 1 . . . . . . . . 6051 1 967 . 1 1 116 116 LEU HB2 H 1 1.998 0.01 . 2 . . . . . . . . 6051 1 968 . 1 1 116 116 LEU HB3 H 1 0.886 0.01 . 2 . . . . . . . . 6051 1 969 . 1 1 116 116 LEU CG C 13 26.732 0.20 . 1 . . . . . . . . 6051 1 970 . 1 1 116 116 LEU HG H 1 0.912 0.01 . 1 . . . . . . . . 6051 1 971 . 1 1 116 116 LEU CD1 C 13 22.882 0.20 . 1 . . . . . . . . 6051 1 972 . 1 1 116 116 LEU HD11 H 1 0.627 0.01 . 1 . . . . . . . . 6051 1 973 . 1 1 116 116 LEU HD12 H 1 0.627 0.01 . 1 . . . . . . . . 6051 1 974 . 1 1 116 116 LEU HD13 H 1 0.627 0.01 . 1 . . . . . . . . 6051 1 975 . 1 1 116 116 LEU HD21 H 1 0.627 0.01 . 1 . . . . . . . . 6051 1 976 . 1 1 116 116 LEU HD22 H 1 0.627 0.01 . 1 . . . . . . . . 6051 1 977 . 1 1 116 116 LEU HD23 H 1 0.627 0.01 . 1 . . . . . . . . 6051 1 978 . 1 1 117 117 ARG H H 1 8.337 0.01 . 1 . . . . . . . . 6051 1 979 . 1 1 117 117 ARG N N 15 120.947 0.10 . 1 . . . . . . . . 6051 1 980 . 1 1 117 117 ARG C C 13 174.708 0.20 . 1 . . . . . . . . 6051 1 981 . 1 1 117 117 ARG CA C 13 55.497 0.20 . 1 . . . . . . . . 6051 1 982 . 1 1 117 117 ARG HA H 1 4.226 0.01 . 1 . . . . . . . . 6051 1 983 . 1 1 117 117 ARG CB C 13 34.429 0.20 . 1 . . . . . . . . 6051 1 984 . 1 1 117 117 ARG HB2 H 1 2.203 0.01 . 2 . . . . . . . . 6051 1 985 . 1 1 117 117 ARG HB3 H 1 1.461 0.01 . 2 . . . . . . . . 6051 1 986 . 1 1 117 117 ARG CG C 13 24.729 0.20 . 1 . . . . . . . . 6051 1 987 . 1 1 117 117 ARG HG2 H 1 1.157 0.01 . 1 . . . . . . . . 6051 1 988 . 1 1 117 117 ARG HG3 H 1 1.157 0.01 . 1 . . . . . . . . 6051 1 989 . 1 1 117 117 ARG CD C 13 42.526 0.20 . 1 . . . . . . . . 6051 1 990 . 1 1 117 117 ARG HD2 H 1 2.842 0.01 . 1 . . . . . . . . 6051 1 991 . 1 1 117 117 ARG HD3 H 1 2.842 0.01 . 1 . . . . . . . . 6051 1 992 . 1 1 118 118 TYR H H 1 9.854 0.01 . 1 . . . . . . . . 6051 1 993 . 1 1 118 118 TYR N N 15 127.441 0.10 . 1 . . . . . . . . 6051 1 994 . 1 1 118 118 TYR C C 13 173.137 0.20 . 1 . . . . . . . . 6051 1 995 . 1 1 118 118 TYR CA C 13 59.544 0.20 . 1 . . . . . . . . 6051 1 996 . 1 1 118 118 TYR HA H 1 4.322 0.01 . 1 . . . . . . . . 6051 1 997 . 1 1 118 118 TYR CB C 13 37.960 0.20 . 1 . . . . . . . . 6051 1 998 . 1 1 118 118 TYR HB2 H 1 3.025 0.01 . 2 . . . . . . . . 6051 1 999 . 1 1 118 118 TYR HB3 H 1 2.754 0.01 . 2 . . . . . . . . 6051 1 1000 . 1 1 119 119 CYS H H 1 9.317 0.01 . 1 . . . . . . . . 6051 1 1001 . 1 1 119 119 CYS N N 15 128.979 0.10 . 1 . . . . . . . . 6051 1 1002 . 1 1 119 119 CYS C C 13 171.062 0.20 . 1 . . . . . . . . 6051 1 1003 . 1 1 119 119 CYS CA C 13 59.073 0.20 . 1 . . . . . . . . 6051 1 1004 . 1 1 119 119 CYS HA H 1 4.735 0.01 . 1 . . . . . . . . 6051 1 1005 . 1 1 119 119 CYS CB C 13 28.434 0.20 . 1 . . . . . . . . 6051 1 1006 . 1 1 119 119 CYS HB2 H 1 3.175 0.01 . 2 . . . . . . . . 6051 1 1007 . 1 1 119 119 CYS HB3 H 1 2.453 0.01 . 2 . . . . . . . . 6051 1 1008 . 1 1 120 120 ILE H H 1 8.791 0.01 . 1 . . . . . . . . 6051 1 1009 . 1 1 120 120 ILE N N 15 128.954 0.10 . 1 . . . . . . . . 6051 1 1010 . 1 1 120 120 ILE C C 13 173.278 0.20 . 1 . . . . . . . . 6051 1 1011 . 1 1 120 120 ILE CA C 13 57.243 0.20 . 1 . . . . . . . . 6051 1 1012 . 1 1 120 120 ILE CB C 13 41.677 0.20 . 1 . . . . . . . . 6051 1 1013 . 1 1 121 121 ASN H H 1 7.912 0.01 . 1 . . . . . . . . 6051 1 1014 . 1 1 121 121 ASN N N 15 120.433 0.10 . 1 . . . . . . . . 6051 1 1015 . 1 1 121 121 ASN CA C 13 54.872 0.20 . 1 . . . . . . . . 6051 1 1016 . 1 1 121 121 ASN HA H 1 4.463 0.01 . 1 . . . . . . . . 6051 1 1017 . 1 1 121 121 ASN CB C 13 39.981 0.20 . 1 . . . . . . . . 6051 1 1018 . 1 1 121 121 ASN HB2 H 1 2.728 0.01 . 2 . . . . . . . . 6051 1 1019 . 1 1 121 121 ASN HB3 H 1 2.569 0.01 . 2 . . . . . . . . 6051 1 1020 . 1 1 121 121 ASN ND2 N 15 113.495 0.10 . 1 . . . . . . . . 6051 1 1021 . 1 1 121 121 ASN HD21 H 1 7.892 0.01 . 1 . . . . . . . . 6051 1 1022 . 1 1 121 121 ASN HD22 H 1 7.098 0.01 . 1 . . . . . . . . 6051 1 1023 . 1 1 122 122 GLY C C 13 175.700 0.20 . 1 . . . . . . . . 6051 1 1024 . 1 1 122 122 GLY CA C 13 47.672 0.20 . 1 . . . . . . . . 6051 1 1025 . 1 1 122 122 GLY HA2 H 1 3.260 0.01 . 2 . . . . . . . . 6051 1 1026 . 1 1 122 122 GLY HA3 H 1 2.598 0.01 . 2 . . . . . . . . 6051 1 1027 . 1 1 123 123 ALA H H 1 9.327 0.01 . 1 . . . . . . . . 6051 1 1028 . 1 1 123 123 ALA N N 15 119.654 0.10 . 1 . . . . . . . . 6051 1 1029 . 1 1 123 123 ALA C C 13 176.659 0.20 . 1 . . . . . . . . 6051 1 1030 . 1 1 123 123 ALA CA C 13 53.912 0.20 . 1 . . . . . . . . 6051 1 1031 . 1 1 123 123 ALA HA H 1 4.141 0.01 . 1 . . . . . . . . 6051 1 1032 . 1 1 123 123 ALA CB C 13 19.938 0.20 . 1 . . . . . . . . 6051 1 1033 . 1 1 123 123 ALA HB1 H 1 1.392 0.01 . 1 . . . . . . . . 6051 1 1034 . 1 1 123 123 ALA HB2 H 1 1.392 0.01 . 1 . . . . . . . . 6051 1 1035 . 1 1 123 123 ALA HB3 H 1 1.392 0.01 . 1 . . . . . . . . 6051 1 1036 . 1 1 124 124 SER H H 1 7.283 0.01 . 1 . . . . . . . . 6051 1 1037 . 1 1 124 124 SER N N 15 108.882 0.10 . 1 . . . . . . . . 6051 1 1038 . 1 1 124 124 SER C C 13 172.724 0.20 . 1 . . . . . . . . 6051 1 1039 . 1 1 124 124 SER CA C 13 59.830 0.20 . 1 . . . . . . . . 6051 1 1040 . 1 1 124 124 SER HA H 1 4.273 0.01 . 1 . . . . . . . . 6051 1 1041 . 1 1 124 124 SER CB C 13 65.582 0.20 . 1 . . . . . . . . 6051 1 1042 . 1 1 124 124 SER HB2 H 1 3.730 0.01 . 1 . . . . . . . . 6051 1 1043 . 1 1 124 124 SER HB3 H 1 3.730 0.01 . 1 . . . . . . . . 6051 1 1044 . 1 1 125 125 LEU H H 1 7.838 0.01 . 1 . . . . . . . . 6051 1 1045 . 1 1 125 125 LEU N N 15 119.157 0.10 . 1 . . . . . . . . 6051 1 1046 . 1 1 125 125 LEU C C 13 175.518 0.20 . 1 . . . . . . . . 6051 1 1047 . 1 1 125 125 LEU CA C 13 53.757 0.20 . 1 . . . . . . . . 6051 1 1048 . 1 1 125 125 LEU HA H 1 5.435 0.01 . 1 . . . . . . . . 6051 1 1049 . 1 1 125 125 LEU CB C 13 48.318 0.20 . 1 . . . . . . . . 6051 1 1050 . 1 1 125 125 LEU HB2 H 1 2.269 0.01 . 1 . . . . . . . . 6051 1 1051 . 1 1 125 125 LEU HB3 H 1 2.269 0.01 . 1 . . . . . . . . 6051 1 1052 . 1 1 125 125 LEU CG C 13 26.679 0.20 . 1 . . . . . . . . 6051 1 1053 . 1 1 125 125 LEU HG H 1 1.961 0.01 . 1 . . . . . . . . 6051 1 1054 . 1 1 125 125 LEU CD1 C 13 23.662 0.20 . 1 . . . . . . . . 6051 1 1055 . 1 1 125 125 LEU HD11 H 1 0.678 0.01 . 1 . . . . . . . . 6051 1 1056 . 1 1 125 125 LEU HD12 H 1 0.678 0.01 . 1 . . . . . . . . 6051 1 1057 . 1 1 125 125 LEU HD13 H 1 0.678 0.01 . 1 . . . . . . . . 6051 1 1058 . 1 1 125 125 LEU CD2 C 13 25.144 0.20 . 1 . . . . . . . . 6051 1 1059 . 1 1 125 125 LEU HD21 H 1 0.582 0.01 . 1 . . . . . . . . 6051 1 1060 . 1 1 125 125 LEU HD22 H 1 0.582 0.01 . 1 . . . . . . . . 6051 1 1061 . 1 1 125 125 LEU HD23 H 1 0.582 0.01 . 1 . . . . . . . . 6051 1 1062 . 1 1 126 126 LYS H H 1 8.911 0.01 . 1 . . . . . . . . 6051 1 1063 . 1 1 126 126 LYS N N 15 119.538 0.10 . 1 . . . . . . . . 6051 1 1064 . 1 1 126 126 LYS C C 13 174.427 0.20 . 1 . . . . . . . . 6051 1 1065 . 1 1 126 126 LYS CA C 13 56.092 0.20 . 1 . . . . . . . . 6051 1 1066 . 1 1 126 126 LYS HA H 1 4.843 0.01 . 1 . . . . . . . . 6051 1 1067 . 1 1 126 126 LYS CB C 13 36.023 0.20 . 1 . . . . . . . . 6051 1 1068 . 1 1 126 126 LYS HB2 H 1 1.548 0.01 . 1 . . . . . . . . 6051 1 1069 . 1 1 126 126 LYS HB3 H 1 1.548 0.01 . 1 . . . . . . . . 6051 1 1070 . 1 1 126 126 LYS CG C 13 25.427 0.20 . 1 . . . . . . . . 6051 1 1071 . 1 1 126 126 LYS HG2 H 1 1.111 0.01 . 1 . . . . . . . . 6051 1 1072 . 1 1 126 126 LYS HG3 H 1 1.111 0.01 . 1 . . . . . . . . 6051 1 1073 . 1 1 126 126 LYS CD C 13 29.835 0.20 . 1 . . . . . . . . 6051 1 1074 . 1 1 126 126 LYS HD2 H 1 1.468 0.01 . 1 . . . . . . . . 6051 1 1075 . 1 1 126 126 LYS HD3 H 1 1.468 0.01 . 1 . . . . . . . . 6051 1 1076 . 1 1 126 126 LYS CE C 13 42.688 0.20 . 1 . . . . . . . . 6051 1 1077 . 1 1 126 126 LYS HE2 H 1 2.894 0.01 . 1 . . . . . . . . 6051 1 1078 . 1 1 126 126 LYS HE3 H 1 2.894 0.01 . 1 . . . . . . . . 6051 1 1079 . 1 1 127 127 PHE H H 1 8.217 0.01 . 1 . . . . . . . . 6051 1 1080 . 1 1 127 127 PHE N N 15 125.829 0.10 . 1 . . . . . . . . 6051 1 1081 . 1 1 127 127 PHE C C 13 173.286 0.20 . 1 . . . . . . . . 6051 1 1082 . 1 1 127 127 PHE CA C 13 56.733 0.20 . 1 . . . . . . . . 6051 1 1083 . 1 1 127 127 PHE HA H 1 4.378 0.01 . 1 . . . . . . . . 6051 1 1084 . 1 1 127 127 PHE CB C 13 40.402 0.20 . 1 . . . . . . . . 6051 1 1085 . 1 1 128 128 ILE H H 1 8.679 0.01 . 1 . . . . . . . . 6051 1 1086 . 1 1 128 128 ILE N N 15 130.180 0.10 . 1 . . . . . . . . 6051 1 1087 . 1 1 128 128 ILE C C 13 171.186 0.20 . 1 . . . . . . . . 6051 1 1088 . 1 1 128 128 ILE CA C 13 56.414 0.20 . 1 . . . . . . . . 6051 1 1089 . 1 1 128 128 ILE HA H 1 4.086 0.01 . 1 . . . . . . . . 6051 1 1090 . 1 1 128 128 ILE CB C 13 43.012 0.20 . 1 . . . . . . . . 6051 1 1091 . 1 1 128 128 ILE HB H 1 1.532 0.01 . 1 . . . . . . . . 6051 1 1092 . 1 1 128 128 ILE CG1 C 13 25.516 0.20 . 1 . . . . . . . . 6051 1 1093 . 1 1 128 128 ILE HG12 H 1 1.258 0.01 . 2 . . . . . . . . 6051 1 1094 . 1 1 128 128 ILE HG13 H 1 0.815 0.01 . 2 . . . . . . . . 6051 1 1095 . 1 1 128 128 ILE HG21 H 1 0.862 0.01 . 1 . . . . . . . . 6051 1 1096 . 1 1 128 128 ILE HG22 H 1 0.862 0.01 . 1 . . . . . . . . 6051 1 1097 . 1 1 128 128 ILE HG23 H 1 0.862 0.01 . 1 . . . . . . . . 6051 1 1098 . 1 1 128 128 ILE HD11 H 1 0.800 0.01 . 1 . . . . . . . . 6051 1 1099 . 1 1 128 128 ILE HD12 H 1 0.800 0.01 . 1 . . . . . . . . 6051 1 1100 . 1 1 128 128 ILE HD13 H 1 0.800 0.01 . 1 . . . . . . . . 6051 1 1101 . 1 1 129 129 PRO C C 13 177.171 0.20 . 1 . . . . . . . . 6051 1 1102 . 1 1 129 129 PRO CA C 13 62.615 0.20 . 1 . . . . . . . . 6051 1 1103 . 1 1 129 129 PRO HA H 1 4.439 0.01 . 1 . . . . . . . . 6051 1 1104 . 1 1 129 129 PRO CB C 13 34.856 0.20 . 1 . . . . . . . . 6051 1 1105 . 1 1 129 129 PRO HB2 H 1 2.338 0.01 . 2 . . . . . . . . 6051 1 1106 . 1 1 129 129 PRO HB3 H 1 1.925 0.01 . 2 . . . . . . . . 6051 1 1107 . 1 1 129 129 PRO HG2 H 1 1.696 0.01 . 1 . . . . . . . . 6051 1 1108 . 1 1 129 129 PRO HG3 H 1 1.696 0.01 . 1 . . . . . . . . 6051 1 1109 . 1 1 129 129 PRO HD2 H 1 3.184 0.01 . 1 . . . . . . . . 6051 1 1110 . 1 1 129 129 PRO HD3 H 1 3.184 0.01 . 1 . . . . . . . . 6051 1 1111 . 1 1 130 130 LEU H H 1 8.347 0.01 . 1 . . . . . . . . 6051 1 1112 . 1 1 130 130 LEU N N 15 126.041 0.10 . 1 . . . . . . . . 6051 1 1113 . 1 1 130 130 LEU C C 13 177.634 0.20 . 1 . . . . . . . . 6051 1 1114 . 1 1 130 130 LEU CA C 13 59.072 0.20 . 1 . . . . . . . . 6051 1 1115 . 1 1 130 130 LEU HA H 1 3.971 0.01 . 1 . . . . . . . . 6051 1 1116 . 1 1 130 130 LEU CB C 13 43.855 0.20 . 1 . . . . . . . . 6051 1 1117 . 1 1 130 130 LEU HB2 H 1 1.670 0.01 . 2 . . . . . . . . 6051 1 1118 . 1 1 130 130 LEU HB3 H 1 1.138 0.01 . 2 . . . . . . . . 6051 1 1119 . 1 1 130 130 LEU CG C 13 27.648 0.20 . 1 . . . . . . . . 6051 1 1120 . 1 1 130 130 LEU HG H 1 1.516 0.01 . 1 . . . . . . . . 6051 1 1121 . 1 1 130 130 LEU CD1 C 13 24.003 0.20 . 1 . . . . . . . . 6051 1 1122 . 1 1 130 130 LEU HD11 H 1 0.937 0.01 . 1 . . . . . . . . 6051 1 1123 . 1 1 130 130 LEU HD12 H 1 0.937 0.01 . 1 . . . . . . . . 6051 1 1124 . 1 1 130 130 LEU HD13 H 1 0.937 0.01 . 1 . . . . . . . . 6051 1 1125 . 1 1 130 130 LEU CD2 C 13 26.475 0.20 . 1 . . . . . . . . 6051 1 1126 . 1 1 130 130 LEU HD21 H 1 0.874 0.01 . 1 . . . . . . . . 6051 1 1127 . 1 1 130 130 LEU HD22 H 1 0.874 0.01 . 1 . . . . . . . . 6051 1 1128 . 1 1 130 130 LEU HD23 H 1 0.874 0.01 . 1 . . . . . . . . 6051 1 1129 . 1 1 131 131 GLU H H 1 9.872 0.01 . 1 . . . . . . . . 6051 1 1130 . 1 1 131 131 GLU N N 15 115.575 0.10 . 1 . . . . . . . . 6051 1 1131 . 1 1 131 131 GLU C C 13 175.964 0.20 . 1 . . . . . . . . 6051 1 1132 . 1 1 131 131 GLU CA C 13 59.542 0.20 . 1 . . . . . . . . 6051 1 1133 . 1 1 131 131 GLU HA H 1 4.111 0.01 . 1 . . . . . . . . 6051 1 1134 . 1 1 131 131 GLU CB C 13 29.035 0.20 . 1 . . . . . . . . 6051 1 1135 . 1 1 131 131 GLU HB2 H 1 2.305 0.01 . 2 . . . . . . . . 6051 1 1136 . 1 1 131 131 GLU HB3 H 1 2.020 0.01 . 2 . . . . . . . . 6051 1 1137 . 1 1 132 132 GLN H H 1 7.986 0.01 . 1 . . . . . . . . 6051 1 1138 . 1 1 132 132 GLN N N 15 117.306 0.10 . 1 . . . . . . . . 6051 1 1139 . 1 1 132 132 GLN C C 13 175.369 0.20 . 1 . . . . . . . . 6051 1 1140 . 1 1 132 132 GLN CA C 13 55.635 0.20 . 1 . . . . . . . . 6051 1 1141 . 1 1 132 132 GLN HA H 1 4.584 0.01 . 1 . . . . . . . . 6051 1 1142 . 1 1 132 132 GLN CB C 13 31.054 0.20 . 1 . . . . . . . . 6051 1 1143 . 1 1 132 132 GLN HB2 H 1 1.679 0.01 . 1 . . . . . . . . 6051 1 1144 . 1 1 132 132 GLN HB3 H 1 1.679 0.01 . 1 . . . . . . . . 6051 1 1145 . 1 1 132 132 GLN HG2 H 1 2.304 0.01 . 1 . . . . . . . . 6051 1 1146 . 1 1 132 132 GLN HG3 H 1 2.304 0.01 . 1 . . . . . . . . 6051 1 1147 . 1 1 132 132 GLN NE2 N 15 111.349 0.10 . 1 . . . . . . . . 6051 1 1148 . 1 1 132 132 GLN HE21 H 1 7.556 0.01 . 1 . . . . . . . . 6051 1 1149 . 1 1 132 132 GLN HE22 H 1 6.858 0.01 . 1 . . . . . . . . 6051 1 1150 . 1 1 133 133 MET H H 1 7.514 0.01 . 1 . . . . . . . . 6051 1 1151 . 1 1 133 133 MET N N 15 119.406 0.10 . 1 . . . . . . . . 6051 1 1152 . 1 1 133 133 MET C C 13 177.138 0.20 . 1 . . . . . . . . 6051 1 1153 . 1 1 133 133 MET CA C 13 62.205 0.20 . 1 . . . . . . . . 6051 1 1154 . 1 1 133 133 MET CB C 13 32.729 0.20 . 1 . . . . . . . . 6051 1 1155 . 1 1 134 134 ASP H H 1 9.021 0.01 . 1 . . . . . . . . 6051 1 1156 . 1 1 134 134 ASP N N 15 119.538 0.10 . 1 . . . . . . . . 6051 1 1157 . 1 1 134 134 ASP C C 13 179.370 0.20 . 1 . . . . . . . . 6051 1 1158 . 1 1 134 134 ASP CA C 13 56.092 0.20 . 1 . . . . . . . . 6051 1 1159 . 1 1 134 134 ASP HA H 1 4.243 0.01 . 1 . . . . . . . . 6051 1 1160 . 1 1 134 134 ASP CB C 13 40.486 0.20 . 1 . . . . . . . . 6051 1 1161 . 1 1 134 134 ASP HB2 H 1 2.696 0.01 . 2 . . . . . . . . 6051 1 1162 . 1 1 134 134 ASP HB3 H 1 2.548 0.01 . 2 . . . . . . . . 6051 1 1163 . 1 1 135 135 ALA H H 1 8.522 0.01 . 1 . . . . . . . . 6051 1 1164 . 1 1 135 135 ALA N N 15 124.412 0.10 . 1 . . . . . . . . 6051 1 1165 . 1 1 135 135 ALA C C 13 178.312 0.20 . 1 . . . . . . . . 6051 1 1166 . 1 1 135 135 ALA CA C 13 55.159 0.20 . 1 . . . . . . . . 6051 1 1167 . 1 1 135 135 ALA HA H 1 4.020 0.01 . 1 . . . . . . . . 6051 1 1168 . 1 1 135 135 ALA CB C 13 18.590 0.20 . 1 . . . . . . . . 6051 1 1169 . 1 1 135 135 ALA HB1 H 1 1.363 0.01 . 1 . . . . . . . . 6051 1 1170 . 1 1 135 135 ALA HB2 H 1 1.363 0.01 . 1 . . . . . . . . 6051 1 1171 . 1 1 135 135 ALA HB3 H 1 1.363 0.01 . 1 . . . . . . . . 6051 1 1172 . 1 1 136 136 ALA H H 1 7.764 0.01 . 1 . . . . . . . . 6051 1 1173 . 1 1 136 136 ALA N N 15 116.603 0.10 . 1 . . . . . . . . 6051 1 1174 . 1 1 136 136 ALA C C 13 175.832 0.20 . 1 . . . . . . . . 6051 1 1175 . 1 1 136 136 ALA CA C 13 52.664 0.20 . 1 . . . . . . . . 6051 1 1176 . 1 1 136 136 ALA HA H 1 4.305 0.01 . 1 . . . . . . . . 6051 1 1177 . 1 1 136 136 ALA CB C 13 20.213 0.20 . 1 . . . . . . . . 6051 1 1178 . 1 1 136 136 ALA HB1 H 1 1.511 0.01 . 1 . . . . . . . . 6051 1 1179 . 1 1 136 136 ALA HB2 H 1 1.511 0.01 . 1 . . . . . . . . 6051 1 1180 . 1 1 136 136 ALA HB3 H 1 1.511 0.01 . 1 . . . . . . . . 6051 1 1181 . 1 1 137 137 GLY H H 1 7.367 0.01 . 1 . . . . . . . . 6051 1 1182 . 1 1 137 137 GLY N N 15 103.537 0.10 . 1 . . . . . . . . 6051 1 1183 . 1 1 137 137 GLY C C 13 174.675 0.20 . 1 . . . . . . . . 6051 1 1184 . 1 1 137 137 GLY CA C 13 45.859 0.20 . 1 . . . . . . . . 6051 1 1185 . 1 1 137 137 GLY HA2 H 1 4.022 0.01 . 2 . . . . . . . . 6051 1 1186 . 1 1 137 137 GLY HA3 H 1 3.739 0.01 . 2 . . . . . . . . 6051 1 1187 . 1 1 138 138 TYR H H 1 8.354 0.01 . 1 . . . . . . . . 6051 1 1188 . 1 1 138 138 TYR N N 15 118.877 0.10 . 1 . . . . . . . . 6051 1 1189 . 1 1 138 138 TYR C C 13 175.981 0.20 . 1 . . . . . . . . 6051 1 1190 . 1 1 138 138 TYR CA C 13 57.076 0.20 . 1 . . . . . . . . 6051 1 1191 . 1 1 138 138 TYR HA H 1 4.809 0.01 . 1 . . . . . . . . 6051 1 1192 . 1 1 138 138 TYR CB C 13 40.823 0.20 . 1 . . . . . . . . 6051 1 1193 . 1 1 138 138 TYR HB2 H 1 3.304 0.01 . 2 . . . . . . . . 6051 1 1194 . 1 1 138 138 TYR HB3 H 1 2.102 0.01 . 2 . . . . . . . . 6051 1 1195 . 1 1 139 139 GLY H H 1 9.179 0.01 . 1 . . . . . . . . 6051 1 1196 . 1 1 139 139 GLY N N 15 111.692 0.10 . 1 . . . . . . . . 6051 1 1197 . 1 1 139 139 GLY C C 13 175.733 0.20 . 1 . . . . . . . . 6051 1 1198 . 1 1 139 139 GLY CA C 13 48.607 0.20 . 1 . . . . . . . . 6051 1 1199 . 1 1 139 139 GLY HA2 H 1 4.152 0.01 . 2 . . . . . . . . 6051 1 1200 . 1 1 139 139 GLY HA3 H 1 3.481 0.01 . 2 . . . . . . . . 6051 1 1201 . 1 1 140 140 ALA H H 1 8.580 0.01 . 1 . . . . . . . . 6051 1 1202 . 1 1 140 140 ALA N N 15 121.201 0.10 . 1 . . . . . . . . 6051 1 1203 . 1 1 140 140 ALA C C 13 178.163 0.20 . 1 . . . . . . . . 6051 1 1204 . 1 1 140 140 ALA CA C 13 54.532 0.20 . 1 . . . . . . . . 6051 1 1205 . 1 1 140 140 ALA HA H 1 3.962 0.01 . 1 . . . . . . . . 6051 1 1206 . 1 1 140 140 ALA CB C 13 18.843 0.20 . 1 . . . . . . . . 6051 1 1207 . 1 1 140 140 ALA HB1 H 1 1.360 0.01 . 1 . . . . . . . . 6051 1 1208 . 1 1 140 140 ALA HB2 H 1 1.360 0.01 . 1 . . . . . . . . 6051 1 1209 . 1 1 140 140 ALA HB3 H 1 1.360 0.01 . 1 . . . . . . . . 6051 1 1210 . 1 1 141 141 LEU H H 1 7.838 0.01 . 1 . . . . . . . . 6051 1 1211 . 1 1 141 141 LEU N N 15 116.087 0.10 . 1 . . . . . . . . 6051 1 1212 . 1 1 141 141 LEU C C 13 177.386 0.20 . 1 . . . . . . . . 6051 1 1213 . 1 1 141 141 LEU CA C 13 54.852 0.20 . 1 . . . . . . . . 6051 1 1214 . 1 1 141 141 LEU HA H 1 4.408 0.01 . 1 . . . . . . . . 6051 1 1215 . 1 1 141 141 LEU CB C 13 42.928 0.20 . 1 . . . . . . . . 6051 1 1216 . 1 1 141 141 LEU HB2 H 1 1.612 0.01 . 1 . . . . . . . . 6051 1 1217 . 1 1 141 141 LEU HB3 H 1 1.612 0.01 . 1 . . . . . . . . 6051 1 1218 . 1 1 141 141 LEU CG C 13 28.026 0.20 . 1 . . . . . . . . 6051 1 1219 . 1 1 141 141 LEU HG H 1 1.564 0.01 . 1 . . . . . . . . 6051 1 1220 . 1 1 141 141 LEU CD1 C 13 27.102 0.20 . 1 . . . . . . . . 6051 1 1221 . 1 1 141 141 LEU HD11 H 1 0.879 0.01 . 1 . . . . . . . . 6051 1 1222 . 1 1 141 141 LEU HD12 H 1 0.879 0.01 . 1 . . . . . . . . 6051 1 1223 . 1 1 141 141 LEU HD13 H 1 0.879 0.01 . 1 . . . . . . . . 6051 1 1224 . 1 1 141 141 LEU CD2 C 13 24.039 0.20 . 1 . . . . . . . . 6051 1 1225 . 1 1 141 141 LEU HD21 H 1 0.761 0.01 . 1 . . . . . . . . 6051 1 1226 . 1 1 141 141 LEU HD22 H 1 0.761 0.01 . 1 . . . . . . . . 6051 1 1227 . 1 1 141 141 LEU HD23 H 1 0.761 0.01 . 1 . . . . . . . . 6051 1 1228 . 1 1 142 142 LYS H H 1 7.524 0.01 . 1 . . . . . . . . 6051 1 1229 . 1 1 142 142 LYS N N 15 121.090 0.10 . 1 . . . . . . . . 6051 1 1230 . 1 1 142 142 LYS C C 13 178.099 0.20 . 1 . . . . . . . . 6051 1 1231 . 1 1 142 142 LYS CA C 13 62.212 0.20 . 1 . . . . . . . . 6051 1 1232 . 1 1 142 142 LYS HA H 1 3.564 0.01 . 1 . . . . . . . . 6051 1 1233 . 1 1 142 142 LYS CB C 13 31.541 0.20 . 1 . . . . . . . . 6051 1 1234 . 1 1 142 142 LYS HB2 H 1 1.736 0.01 . 1 . . . . . . . . 6051 1 1235 . 1 1 142 142 LYS HG2 H 1 0.868 0.01 . 1 . . . . . . . . 6051 1 1236 . 1 1 142 142 LYS HG3 H 1 0.868 0.01 . 1 . . . . . . . . 6051 1 1237 . 1 1 142 142 LYS HD2 H 1 1.510 0.01 . 1 . . . . . . . . 6051 1 1238 . 1 1 142 142 LYS HD3 H 1 1.510 0.01 . 1 . . . . . . . . 6051 1 1239 . 1 1 142 142 LYS CE C 13 40.936 0.20 . 1 . . . . . . . . 6051 1 1240 . 1 1 142 142 LYS HE2 H 1 2.988 0.01 . 1 . . . . . . . . 6051 1 1241 . 1 1 142 142 LYS HE3 H 1 2.988 0.01 . 1 . . . . . . . . 6051 1 1242 . 1 1 143 143 SER C C 13 174.807 0.20 . 1 . . . . . . . . 6051 1 1243 . 1 1 143 143 SER CA C 13 60.736 0.20 . 1 . . . . . . . . 6051 1 1244 . 1 1 143 143 SER HA H 1 4.273 0.01 . 1 . . . . . . . . 6051 1 1245 . 1 1 143 143 SER CB C 13 62.973 0.20 . 1 . . . . . . . . 6051 1 1246 . 1 1 143 143 SER HB2 H 1 3.946 0.01 . 1 . . . . . . . . 6051 1 1247 . 1 1 143 143 SER HB3 H 1 3.946 0.01 . 1 . . . . . . . . 6051 1 1248 . 1 1 144 144 LYS H H 1 7.644 0.01 . 1 . . . . . . . . 6051 1 1249 . 1 1 144 144 LYS N N 15 118.266 0.10 . 1 . . . . . . . . 6051 1 1250 . 1 1 144 144 LYS C C 13 176.874 0.20 . 1 . . . . . . . . 6051 1 1251 . 1 1 144 144 LYS CA C 13 55.957 0.20 . 1 . . . . . . . . 6051 1 1252 . 1 1 144 144 LYS HA H 1 4.344 0.01 . 1 . . . . . . . . 6051 1 1253 . 1 1 144 144 LYS CB C 13 32.738 0.20 . 1 . . . . . . . . 6051 1 1254 . 1 1 144 144 LYS HB2 H 1 1.922 0.01 . 2 . . . . . . . . 6051 1 1255 . 1 1 144 144 LYS HB3 H 1 1.772 0.01 . 2 . . . . . . . . 6051 1 1256 . 1 1 144 144 LYS CG C 13 25.472 0.20 . 1 . . . . . . . . 6051 1 1257 . 1 1 144 144 LYS HG2 H 1 1.378 0.01 . 1 . . . . . . . . 6051 1 1258 . 1 1 144 144 LYS HG3 H 1 1.378 0.01 . 1 . . . . . . . . 6051 1 1259 . 1 1 144 144 LYS CD C 13 28.091 0.20 . 1 . . . . . . . . 6051 1 1260 . 1 1 144 144 LYS HD2 H 1 1.626 0.01 . 1 . . . . . . . . 6051 1 1261 . 1 1 144 144 LYS HD3 H 1 1.626 0.01 . 1 . . . . . . . . 6051 1 1262 . 1 1 144 144 LYS CE C 13 42.860 0.20 . 1 . . . . . . . . 6051 1 1263 . 1 1 144 144 LYS HE2 H 1 2.926 0.01 . 1 . . . . . . . . 6051 1 1264 . 1 1 144 144 LYS HE3 H 1 2.926 0.01 . 1 . . . . . . . . 6051 1 1265 . 1 1 145 145 VAL H H 1 7.829 0.01 . 1 . . . . . . . . 6051 1 1266 . 1 1 145 145 VAL N N 15 123.144 0.10 . 1 . . . . . . . . 6051 1 1267 . 1 1 145 145 VAL C C 13 173.137 0.20 . 1 . . . . . . . . 6051 1 1268 . 1 1 145 145 VAL CA C 13 64.397 0.20 . 1 . . . . . . . . 6051 1 1269 . 1 1 145 145 VAL HA H 1 3.805 0.01 . 1 . . . . . . . . 6051 1 1270 . 1 1 145 145 VAL CB C 13 33.075 0.20 . 1 . . . . . . . . 6051 1 1271 . 1 1 145 145 VAL HB H 1 2.255 0.01 . 1 . . . . . . . . 6051 1 1272 . 1 1 145 145 VAL CG1 C 13 23.708 0.20 . 1 . . . . . . . . 6051 1 1273 . 1 1 145 145 VAL HG11 H 1 0.983 0.01 . 1 . . . . . . . . 6051 1 1274 . 1 1 145 145 VAL HG12 H 1 0.983 0.01 . 1 . . . . . . . . 6051 1 1275 . 1 1 145 145 VAL HG13 H 1 0.983 0.01 . 1 . . . . . . . . 6051 1 1276 . 1 1 145 145 VAL CG2 C 13 22.138 0.20 . 1 . . . . . . . . 6051 1 1277 . 1 1 145 145 VAL HG21 H 1 0.832 0.01 . 1 . . . . . . . . 6051 1 1278 . 1 1 145 145 VAL HG22 H 1 0.832 0.01 . 1 . . . . . . . . 6051 1 1279 . 1 1 145 145 VAL HG23 H 1 0.832 0.01 . 1 . . . . . . . . 6051 1 1280 . 1 1 146 146 LYS H H 1 7.002 0.01 . 1 . . . . . . . . 6051 1 1281 . 1 1 146 146 LYS N N 15 126.214 0.10 . 1 . . . . . . . . 6051 1 1282 . 1 1 146 146 LYS C C 13 179.387 0.20 . 1 . . . . . . . . 6051 1 1283 . 1 1 146 146 LYS CA C 13 58.143 0.20 . 1 . . . . . . . . 6051 1 1284 . 1 1 146 146 LYS HA H 1 4.119 0.01 . 1 . . . . . . . . 6051 1 1285 . 1 1 146 146 LYS CG C 13 25.137 0.20 . 1 . . . . . . . . 6051 1 1286 . 1 1 146 146 LYS HG2 H 1 1.315 0.01 . 1 . . . . . . . . 6051 1 1287 . 1 1 146 146 LYS HG3 H 1 1.315 0.01 . 1 . . . . . . . . 6051 1 1288 . 1 1 146 146 LYS CB C 13 35.265 0.20 . 1 . . . . . . . . 6051 1 1289 . 1 1 146 146 LYS HB2 H 1 1.801 0.01 . 2 . . . . . . . . 6051 1 1290 . 1 1 146 146 LYS HB3 H 1 1.645 0.01 . 2 . . . . . . . . 6051 1 1291 . 1 1 146 146 LYS CD C 13 29.819 0.20 . 1 . . . . . . . . 6051 1 1292 . 1 1 146 146 LYS HD2 H 1 1.630 0.01 . 1 . . . . . . . . 6051 1 1293 . 1 1 146 146 LYS HD3 H 1 1.630 0.01 . 1 . . . . . . . . 6051 1 1294 . 1 1 146 146 LYS CE C 13 42.718 0.20 . 1 . . . . . . . . 6051 1 1295 . 1 1 146 146 LYS HE2 H 1 2.931 0.01 . 1 . . . . . . . . 6051 1 1296 . 1 1 146 146 LYS HE3 H 1 2.931 0.01 . 1 . . . . . . . . 6051 1 stop_ save_