data_4566 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4566 _Entry.Title ; Assignment of 1H,13C and 15N signals of Bovine Adrenodoxin ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 1999-12-14 _Entry.Accession_date 1999-12-15 _Entry.Last_release_date 2000-09-25 _Entry.Original_release_date 2000-09-25 _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 Roland Weiss . . . 4566 2 Laurent Brachais . . . 4566 3 Frank Loehr . . . 4566 4 Judith Hartleib . . . 4566 5 Rita Bernhardt . . . 4566 6 Heinz Rueterjans . . . 4566 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4566 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 576 4566 '13C chemical shifts' 415 4566 '15N chemical shifts' 106 4566 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 . . 2000-09-25 1999-12-20 original author . 4566 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4566 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Letter to the Editor: Assignment of 1H, 13C and 15N signals of bovine adrenodoxin ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 17 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 355 _Citation.Page_last 356 _Citation.Year 2000 _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 Roland Weiss . . . 4566 1 2 Laurent Brachais . . . 4566 1 3 Frank Lohr . . . 4566 1 4 Judith Hartleib . . . 4566 1 5 Rita Bernhardt . . . 4566 1 6 Heinz Rueterjans . . . 4566 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4566 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 14317399 _Citation.Full_citation 'Kimura, T. and Suzuki (1965), Biochem. Biophys. Res. Comm. 19, S. 340-345' _Citation.Title 'AN IRON PROTEIN AS A COMPONENT OF STEROID 11-BETA-HYDROXYLASE COMPLEX.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochem. Biophys. Res. Commun.' _Citation.Journal_name_full 'Biochemical and biophysical research communications' _Citation.Journal_volume 19 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-291X _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 340 _Citation.Page_last 345 _Citation.Year 1965 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 K. SUZUKI K. . . 4566 2 2 T. KIMURA T. . . 4566 2 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4566 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 438190 _Citation.Full_citation 'Stormer, F.C., Pedersen, J.I. and Oftebro, H. (1979), JBC 254, S. 4331-4334' _Citation.Title 'The presence of an adrenodoxin-like ferredoxin and cytochrome P-450 in brain mitochondria.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 254 _Citation.Journal_issue 11 _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 4331 _Citation.Page_last 4334 _Citation.Year 1979 _Citation.Details ; An iron-sulfur protein has been isolated from bovine brain mitochondria and purified 200-fold. The optical spectrum (peaks at 412 and 455 nm which disappear upon reduction) and the EPR spectrum (g values at 1.94 and 2.02) were typical for a ferredoxin. In reconstitution experiments, the protein could replace adrenodoxin in the cholesterol side chain cleavage reaction. The additional detection of cytochrome P-450 in brain mitochondria indicates that the isolated ferredoxin is part of a cytochrome P-450-dependent hydroxylation system. ; 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 H. Oftebro H. . . 4566 3 2 F.C. Stormer F. C. . 4566 3 3 J.L. Pedersen J. L. . 4566 3 stop_ save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 4566 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 6274987 _Citation.Full_citation ; Saarem, K., Bjorkhem, I., Pedersen, J.I. and Oftebro, H. (1981), J.Lipid. Res. 22, S. 1254-1264 ; _Citation.Title 'Side chain hydroxylation of C27-steroids and vitamin D3 by a cytochrome P-450 enzyme system isolated from human liver mitochondria.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Lipid Res.' _Citation.Journal_name_full 'Journal of lipid research' _Citation.Journal_volume 22 _Citation.Journal_issue 8 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2275 _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 1254 _Citation.Page_last 1264 _Citation.Year 1981 _Citation.Details ; The present study was undertaken to obtain information on the involvement of cytochrome P-450 in the 26-hydroxylation on bile acid intermediates and in the 25-hydroxylation of vitamin D3 in human liver mitochondria. Cytochrome P-450 was solubilized from human liver mitochondria and purified two times to a specific content of 0.125 nmol per mg protein. Furthermore, a ferredoxin was isolated from the mitochondria and partly purified. This iron-sulfur protein had properties similar to bovine adrenal ferredoxin. A mitochondrial NADPH-ferredoxin reductase was also isolated and purified to homogeneity. This enzyme was a flavoprotein with properties very similar to the bovine adrenal NADPH-ferredoxin reductase. The cytochrome P-450 preparation catalyzed 26-hydroxylation of C27-steroids and 25-hydroxylation of vitamin D3 when reconstructed with NADPH, the ferredoxin and the ferredoxin reductase. With different substrates the following turnover numbers (nmol product X nmol P-450(-1) X min-1) were found: cholesterol, 8; 5-cholestene-3 beta, 7 alpha-diol, 10; 7 alpha-hydroxy-4-cholesten-3-one, 23; 7 alpha, 12 alpha-dihydroxy-4-cholesten-3-one, 27; 5 beta-cholestane-3 alpha, 7 alpha-diol, 28; 5 beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol, 41; and vitamin D3, 0.16. The hydroxylation reactions were inhibited by CO and metyrapone. The human liver mitochondrial ferredoxin and ferredoxin reductase could be replaced by adrenal ferredoxin and adrenal ferredoxin reductase without reduction of activity, but they could not be replaced by microsomal NADPH-cytochrome P-450 reductase. It is concluded that human liver mitochondria contain cytochrome P-450 involved in the oxidation of the side chain of C27-steroids and vitamin D3. ; 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 H. Oftebro H. . . 4566 4 2 K. Saarem K. . . 4566 4 3 I. Borkhem I. . . 4566 4 4 J.I. Pedersen J. I. . 4566 4 stop_ save_ save_ref_6 _Citation.Sf_category citations _Citation.Sf_framecode ref_6 _Citation.Entry_ID 4566 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 207706 _Citation.Full_citation 'Okuda, K. and Atsuta, Y. (1978), JBC 253, S. 4653-4658' _Citation.Title 'Isolation of rat liver mitochondrial ferredoxin and its reductase active in the 5beta-cholestane-3alpha, 7alpha, 12alpha-triol 26-hydroxylase.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 253 _Citation.Journal_issue 13 _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 4653 _Citation.Page_last 4658 _Citation.Year 1978 _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 Y. Atsuta Y. . . 4566 5 2 K. Okuda K. . . 4566 5 stop_ save_ save_ref_7 _Citation.Sf_category citations _Citation.Sf_framecode ref_7 _Citation.Entry_ID 4566 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 3080335 _Citation.Full_citation 'Hiwatashi, A., Ichikawa, Y. and Waki, N. (1986), FEBS Lett. 195, S. 87-91' _Citation.Title 'Purification and biochemical characterization of hepatic ferredoxin (hepatoredoxin) from bovine liver mitochondria.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'FEBS Lett.' _Citation.Journal_name_full 'FEBS letters' _Citation.Journal_volume 195 _Citation.Journal_issue 1-2 _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 87 _Citation.Page_last 91 _Citation.Year 1986 _Citation.Details ; Hepatic ferredoxin (hepatoredoxin) was purified from bovine liver mitochondria. The monomeric molecular mass of the hepatoredoxin was larger than that of adrenocortical ferredoxin (adrenodoxin) from bovine adrenocortical mitochondria at 14 kDa. We studied the amino acid residues and NH2-terminal sequence of this protein. The hepatoredoxin was organ-specific protein. The optical absorption spectrum of oxidized hepatoredoxin had two peaks, at 414 and 455 nm in the visible region. Hepatoredoxin formed an immunoprecipitin line against anti-adrenodoxin immunoglobulin in Ouchterlony double diffusion, and an immunochemical staining band in Western blotting. ; 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 N. Waki N. . . 4566 6 2 A. Hiwatashi A. . . 4566 6 3 Y. Ichikawa Y. . . 4566 6 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4566 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation 'Kimura, T. (1968), Struct. Bonding 5, S. 1-40' _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_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4566 _Citation.ID 8 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 3401007 _Citation.Full_citation ; Cupp, J.R., Vickery, L.E. and Coghlan, V.M. (1988), Arch.Biochem.Biophys. 264, S. 376-382 ; _Citation.Title 'Purification and characterization of human placental ferredoxin.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Arch. Biochem. Biophys.' _Citation.Journal_name_full 'Archives of biochemistry and biophysics' _Citation.Journal_volume 264 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0003-9861 _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 376 _Citation.Page_last 382 _Citation.Year 1988 _Citation.Details ; A ferredoxin-type iron-sulfur protein was isolated from human placenta mitochondria. The properties of the purified protein were very similar to those of adrenal ferredoxin (adrenodoxin), and immunological cross-reactivity with polyclonal antibodies to bovine adrenodoxin was observed. The N-terminal amino acid sequence and the visible absorption spectrum were identical to bovine adrenodoxin. The molecular mass as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Mr approximately 13,500), however, is slightly smaller than that of adrenodoxin, and the C-terminal sequence is different. Human placental ferredoxin can substitute for bovine adrenodoxin in reactions reconstituted with bovine adrenal enzymes which catalyze the side chain cleavage of cholesterol to pregnenolone and the 11 beta-hydroxylation of deoxycorticosterone to corticosterone. ; 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.M. Coghlan V. M. . 4566 8 2 J.R. Cupp J. R. . 4566 8 3 L.E. Vickery L. E. . 4566 8 stop_ save_ save_ref_8 _Citation.Sf_category citations _Citation.Sf_framecode ref_8 _Citation.Entry_ID 4566 _Citation.ID 9 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1332711 _Citation.Full_citation ; Uhlmann, H., Beckert, V., Schwarz, D. and Bernhardt, R. (1992), Biochem. Biophys. Res. Commun. 188, S. 1131-1138 ; _Citation.Title 'Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of /2 Fe-2S/ cluster ligands.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochem. Biophys. Res. Commun.' _Citation.Journal_name_full 'Biochemical and biophysical research communications' _Citation.Journal_volume 188 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-291X _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 1131 _Citation.Page_last 1138 _Citation.Year 1992 _Citation.Details ; Expression systems for adrenodoxin into the periplasm and the cytoplasm of E. coli have been developed as a prerequisite for site-directed mutagenesis studies. In both systems the /2Fe-2S/ cluster of the protein was correctly assembled, the cytoplasmic one gives, however, a tenfold higher expression level. To determine which of the five cysteines at positions 46, 52, 55, 92, and 95 coordinate the /2Fe-2S/ center, they have been individually mutated into serines. From these mutants, only C95S forms a functionally active holoprotein. Thus, residues 46, 52, 55, and 92 are the cysteines that coordinate the /2Fe-2S/ cluster in adrenodoxin. ; 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 H. Uhlmann H. . . 4566 9 2 V. Beckert V. . . 4566 9 3 D. Schwarz D. . . 4566 9 4 R. Bernhardt R. . . 4566 9 stop_ save_ save_ref_9 _Citation.Sf_category citations _Citation.Sf_framecode ref_9 _Citation.Entry_ID 4566 _Citation.ID 10 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9551550 _Citation.Full_citation ; Muller, A., Muller, J.J., Muller, Y.A., Uhlmann, H., Bernhardt, R. and Heinemann, U. (1998), Structure 6, S. 269-280 ; _Citation.Title 'New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108).' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Structure _Citation.Journal_name_full 'Structure (London, England : 1993)' _Citation.Journal_volume 6 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0969-2126 _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 269 _Citation.Page_last 280 _Citation.Year 1998 _Citation.Details ; BACKGROUND: Adrenodoxin (Adx) is a [2Fe-2S] ferredoxin involved in steroid hormone biosynthesis in the adrenal gland mitochondrial matrix of mammals. Adx is a small soluble protein that transfers electrons from adrenodoxin reductase (AR) to different cytochrome P450 isoforms where they are consumed in hydroxylation reactions. A crystallographic study of Adx is expected to reveal the structural basis for an important electron transfer reaction mediated by a vertebrate [2Fe-2S] ferredoxin. RESULTS: The crystal structure of a truncated bovine adrenodoxin, Adx(4-108), was determined at 1.85 A resolution and refined to a crystallographic R value of 0.195. The structure was determined using multiple wavelength anomalous dispersion phasing techniques, making use of the iron atoms in the [2Fe-2S] cluster of the protein. The protein displays the compact (alpha + beta) fold typical for [2Fe-2S] ferredoxins. The polypeptide chain is organized into a large core domain and a smaller interaction domain which comprises 35 residues, including all those previously determined to be involved in binding to AR and cytochrome P450. A small interdomain motion is observed as a structural difference between the two independent molecules in the asymmetric unit of the crystal. Charged residues of Adx(4-108) are clustered to yield a strikingly asymmetric electric potential of the protein molecule. CONCLUSIONS: The crystal structure of Adx(4-108) provides the first detailed description of a vertebrate [2Fe-2S] ferredoxin and serves to explain a large body of biochemical studies in terms of a three-dimensional structure. The structure suggests how a change in the redox state of the [2Fe-2S] cluster may be coupled to a domain motion of the protein. It seems likely that the clearly asymmetric charge distribution on the surface of Adx(4-108) and the resulting strong molecular dipole are involved in electrostatic steering of the interactions with AR and cytochrome P450. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 A. Muller A. . . 4566 10 2 J.J. Muller J. J. . 4566 10 3 Y.A. Muller Y. A. . 4566 10 4 H. Uhlmann H. . . 4566 10 5 R. Bernhardt R. . . 4566 10 6 U. Heinemann U. . . 4566 10 stop_ save_ save_ref_10 _Citation.Sf_category citations _Citation.Sf_framecode ref_10 _Citation.Entry_ID 4566 _Citation.ID 11 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8589602 _Citation.Full_citation ; Wishart,David S., Bigam,Colin G., Yo,Jian, Abildgaard,Frits ,H. Dyson, H. Jane , Eric Oldfield, Markley,John L., and Sykes,Brian D. (1995), J. of. Biomolecular NMR 6, 135-140 ; _Citation.Title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 135 _Citation.Page_last 140 _Citation.Year 1995 _Citation.Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 D.S. Wishart D. S. . 4566 11 2 C.G. Bigam C. G. . 4566 11 3 J. Yao J. . . 4566 11 4 F. Abildgaard F. . . 4566 11 5 H.J. Dyson H. J. . 4566 11 6 E. Oldfield E. . . 4566 11 7 J.L. Markley J. L. . 4566 11 8 B.D. Sykes B. D. . 4566 11 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_bAdx _Assembly.Sf_category assembly _Assembly.Sf_framecode system_bAdx _Assembly.Entry_ID 4566 _Assembly.ID 1 _Assembly.Name 'bovine adrenodoxin' _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 yes _Assembly.Thiol_state 'free and other bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4566 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 'bovine adrenodoxin' 1 $bAdx . . . native . . . . . 4566 1 2 2[FeS] 2 $FES . . . native . . . . . 4566 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'bovine adrenodoxin' system 4566 1 bAdx abbreviation 4566 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_bAdx _Entity.Sf_category entity _Entity.Sf_framecode bAdx _Entity.Entry_ID 4566 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'bovine adrenodoxin' _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 ; SSSEDKITVHFINRDGETLT TKGKIGDSLLDVVVQNNLDI DGFGACEGTLACSTCHLIFE QHIFEKLEAITDEENDMLDL AYGLTDRSRLGCQICLTKAM DNMTVRVPDAVSDARESIDM GMNSSKIE ; _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 128 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'free and other bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 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 1AYF . "Bovine Adrenodoxin (oxidized)" . . . . . 82.03 105 100.00 100.00 1.04e-69 . . . . 4566 1 2 no PDB 1CJE . "Adrenodoxin From Bovine" . . . . . 99.22 127 100.00 100.00 6.18e-86 . . . . 4566 1 3 no PDB 1E6E . "Adrenodoxin Reductase/adrenodoxin Complex Of Mitochondrial P450 Systems" . . . . . 99.22 128 100.00 100.00 7.12e-86 . . . . 4566 1 4 no PDB 1L6U . "Nmr Structure Of Oxidized Adrenodoxin" . . . . . 99.22 128 100.00 100.00 6.39e-86 . . . . 4566 1 5 no PDB 1L6V . "Structure Of Reduced Bovine Adrenodoxin" . . . . . 100.00 128 100.00 100.00 1.04e-86 . . . . 4566 1 6 no PDB 2BT6 . "Ru(Bpy)2(Mbpy)-Modified Bovine Adrenodoxin" . . . . . 83.59 108 99.07 99.07 6.71e-70 . . . . 4566 1 7 no PDB 2JQR . "Solution Model Of Crosslinked Complex Of Cytochrome C And Adrenodoxin" . . . . . 82.03 105 98.10 98.10 2.02e-67 . . . . 4566 1 8 no DBJ BAA00362 . "adrenodoxin [Bos taurus]" . . . . . 100.00 186 100.00 100.00 3.51e-87 . . . . 4566 1 9 no DBJ BAA00363 . "adrenodoxin [Bos taurus]" . . . . . 100.00 186 100.00 100.00 3.51e-87 . . . . 4566 1 10 no GB AAA30357 . "adrenodoxin precursor, partial [Bos taurus]" . . . . . 100.00 186 100.00 100.00 4.37e-87 . . . . 4566 1 11 no GB AAA30358 . "adrenodoxin precursor [Bos taurus]" . . . . . 98.44 186 100.00 100.00 1.80e-85 . . . . 4566 1 12 no GB AAB21264 . "hepato-ferredoxin [Bos taurus]" . . . . . 100.00 186 100.00 100.00 3.51e-87 . . . . 4566 1 13 no GB AAI09850 . "FDX1 protein [Bos taurus]" . . . . . 100.00 186 100.00 100.00 3.44e-87 . . . . 4566 1 14 no GB ABQ13041 . "ferredoxin 1 precursor [Bos taurus]" . . . . . 100.00 186 100.00 100.00 3.51e-87 . . . . 4566 1 15 no REF NP_851354 . "adrenodoxin, mitochondrial precursor [Bos taurus]" . . . . . 98.44 186 100.00 100.00 1.80e-85 . . . . 4566 1 16 no REF XP_004329468 . "PREDICTED: adrenodoxin, mitochondrial-like [Tursiops truncatus]" . . . . . 66.41 91 97.65 98.82 1.20e-52 . . . . 4566 1 17 no REF XP_005889885 . "PREDICTED: adrenodoxin, mitochondrial [Bos mutus]" . . . . . 100.00 204 100.00 100.00 1.05e-86 . . . . 4566 1 18 no REF XP_006072637 . "PREDICTED: adrenodoxin, mitochondrial [Bubalus bubalis]" . . . . . 100.00 186 98.44 100.00 3.32e-86 . . . . 4566 1 19 no REF XP_010861227 . "PREDICTED: adrenodoxin, mitochondrial [Bison bison bison]" . . . . . 100.00 158 100.00 100.00 6.55e-87 . . . . 4566 1 20 no SP P00257 . "RecName: Full=Adrenodoxin, mitochondrial; AltName: Full=Adrenal ferredoxin; AltName: Full=Ferredoxin-1; AltName: Full=Hepato-fe" . . . . . 100.00 186 100.00 100.00 3.51e-87 . . . . 4566 1 21 no TPG DAA22428 . "TPA: adrenodoxin, mitochondrial precursor [Bos taurus]" . . . . . 72.66 153 100.00 100.00 2.76e-60 . . . . 4566 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'bovine adrenodoxin' common 4566 1 bAdx abbreviation 4566 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 . SER . 4566 1 2 . SER . 4566 1 3 . SER . 4566 1 4 . GLU . 4566 1 5 . ASP . 4566 1 6 . LYS . 4566 1 7 . ILE . 4566 1 8 . THR . 4566 1 9 . VAL . 4566 1 10 . HIS . 4566 1 11 . PHE . 4566 1 12 . ILE . 4566 1 13 . ASN . 4566 1 14 . ARG . 4566 1 15 . ASP . 4566 1 16 . GLY . 4566 1 17 . GLU . 4566 1 18 . THR . 4566 1 19 . LEU . 4566 1 20 . THR . 4566 1 21 . THR . 4566 1 22 . LYS . 4566 1 23 . GLY . 4566 1 24 . LYS . 4566 1 25 . ILE . 4566 1 26 . GLY . 4566 1 27 . ASP . 4566 1 28 . SER . 4566 1 29 . LEU . 4566 1 30 . LEU . 4566 1 31 . ASP . 4566 1 32 . VAL . 4566 1 33 . VAL . 4566 1 34 . VAL . 4566 1 35 . GLN . 4566 1 36 . ASN . 4566 1 37 . ASN . 4566 1 38 . LEU . 4566 1 39 . ASP . 4566 1 40 . ILE . 4566 1 41 . ASP . 4566 1 42 . GLY . 4566 1 43 . PHE . 4566 1 44 . GLY . 4566 1 45 . ALA . 4566 1 46 . CYS . 4566 1 47 . GLU . 4566 1 48 . GLY . 4566 1 49 . THR . 4566 1 50 . LEU . 4566 1 51 . ALA . 4566 1 52 . CYS . 4566 1 53 . SER . 4566 1 54 . THR . 4566 1 55 . CYS . 4566 1 56 . HIS . 4566 1 57 . LEU . 4566 1 58 . ILE . 4566 1 59 . PHE . 4566 1 60 . GLU . 4566 1 61 . GLN . 4566 1 62 . HIS . 4566 1 63 . ILE . 4566 1 64 . PHE . 4566 1 65 . GLU . 4566 1 66 . LYS . 4566 1 67 . LEU . 4566 1 68 . GLU . 4566 1 69 . ALA . 4566 1 70 . ILE . 4566 1 71 . THR . 4566 1 72 . ASP . 4566 1 73 . GLU . 4566 1 74 . GLU . 4566 1 75 . ASN . 4566 1 76 . ASP . 4566 1 77 . MET . 4566 1 78 . LEU . 4566 1 79 . ASP . 4566 1 80 . LEU . 4566 1 81 . ALA . 4566 1 82 . TYR . 4566 1 83 . GLY . 4566 1 84 . LEU . 4566 1 85 . THR . 4566 1 86 . ASP . 4566 1 87 . ARG . 4566 1 88 . SER . 4566 1 89 . ARG . 4566 1 90 . LEU . 4566 1 91 . GLY . 4566 1 92 . CYS . 4566 1 93 . GLN . 4566 1 94 . ILE . 4566 1 95 . CYS . 4566 1 96 . LEU . 4566 1 97 . THR . 4566 1 98 . LYS . 4566 1 99 . ALA . 4566 1 100 . MET . 4566 1 101 . ASP . 4566 1 102 . ASN . 4566 1 103 . MET . 4566 1 104 . THR . 4566 1 105 . VAL . 4566 1 106 . ARG . 4566 1 107 . VAL . 4566 1 108 . PRO . 4566 1 109 . ASP . 4566 1 110 . ALA . 4566 1 111 . VAL . 4566 1 112 . SER . 4566 1 113 . ASP . 4566 1 114 . ALA . 4566 1 115 . ARG . 4566 1 116 . GLU . 4566 1 117 . SER . 4566 1 118 . ILE . 4566 1 119 . ASP . 4566 1 120 . MET . 4566 1 121 . GLY . 4566 1 122 . MET . 4566 1 123 . ASN . 4566 1 124 . SER . 4566 1 125 . SER . 4566 1 126 . LYS . 4566 1 127 . ILE . 4566 1 128 . GLU . 4566 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 . SER 1 1 4566 1 . SER 2 2 4566 1 . SER 3 3 4566 1 . GLU 4 4 4566 1 . ASP 5 5 4566 1 . LYS 6 6 4566 1 . ILE 7 7 4566 1 . THR 8 8 4566 1 . VAL 9 9 4566 1 . HIS 10 10 4566 1 . PHE 11 11 4566 1 . ILE 12 12 4566 1 . ASN 13 13 4566 1 . ARG 14 14 4566 1 . ASP 15 15 4566 1 . GLY 16 16 4566 1 . GLU 17 17 4566 1 . THR 18 18 4566 1 . LEU 19 19 4566 1 . THR 20 20 4566 1 . THR 21 21 4566 1 . LYS 22 22 4566 1 . GLY 23 23 4566 1 . LYS 24 24 4566 1 . ILE 25 25 4566 1 . GLY 26 26 4566 1 . ASP 27 27 4566 1 . SER 28 28 4566 1 . LEU 29 29 4566 1 . LEU 30 30 4566 1 . ASP 31 31 4566 1 . VAL 32 32 4566 1 . VAL 33 33 4566 1 . VAL 34 34 4566 1 . GLN 35 35 4566 1 . ASN 36 36 4566 1 . ASN 37 37 4566 1 . LEU 38 38 4566 1 . ASP 39 39 4566 1 . ILE 40 40 4566 1 . ASP 41 41 4566 1 . GLY 42 42 4566 1 . PHE 43 43 4566 1 . GLY 44 44 4566 1 . ALA 45 45 4566 1 . CYS 46 46 4566 1 . GLU 47 47 4566 1 . GLY 48 48 4566 1 . THR 49 49 4566 1 . LEU 50 50 4566 1 . ALA 51 51 4566 1 . CYS 52 52 4566 1 . SER 53 53 4566 1 . THR 54 54 4566 1 . CYS 55 55 4566 1 . HIS 56 56 4566 1 . LEU 57 57 4566 1 . ILE 58 58 4566 1 . PHE 59 59 4566 1 . GLU 60 60 4566 1 . GLN 61 61 4566 1 . HIS 62 62 4566 1 . ILE 63 63 4566 1 . PHE 64 64 4566 1 . GLU 65 65 4566 1 . LYS 66 66 4566 1 . LEU 67 67 4566 1 . GLU 68 68 4566 1 . ALA 69 69 4566 1 . ILE 70 70 4566 1 . THR 71 71 4566 1 . ASP 72 72 4566 1 . GLU 73 73 4566 1 . GLU 74 74 4566 1 . ASN 75 75 4566 1 . ASP 76 76 4566 1 . MET 77 77 4566 1 . LEU 78 78 4566 1 . ASP 79 79 4566 1 . LEU 80 80 4566 1 . ALA 81 81 4566 1 . TYR 82 82 4566 1 . GLY 83 83 4566 1 . LEU 84 84 4566 1 . THR 85 85 4566 1 . ASP 86 86 4566 1 . ARG 87 87 4566 1 . SER 88 88 4566 1 . ARG 89 89 4566 1 . LEU 90 90 4566 1 . GLY 91 91 4566 1 . CYS 92 92 4566 1 . GLN 93 93 4566 1 . ILE 94 94 4566 1 . CYS 95 95 4566 1 . LEU 96 96 4566 1 . THR 97 97 4566 1 . LYS 98 98 4566 1 . ALA 99 99 4566 1 . MET 100 100 4566 1 . ASP 101 101 4566 1 . ASN 102 102 4566 1 . MET 103 103 4566 1 . THR 104 104 4566 1 . VAL 105 105 4566 1 . ARG 106 106 4566 1 . VAL 107 107 4566 1 . PRO 108 108 4566 1 . ASP 109 109 4566 1 . ALA 110 110 4566 1 . VAL 111 111 4566 1 . SER 112 112 4566 1 . ASP 113 113 4566 1 . ALA 114 114 4566 1 . ARG 115 115 4566 1 . GLU 116 116 4566 1 . SER 117 117 4566 1 . ILE 118 118 4566 1 . ASP 119 119 4566 1 . MET 120 120 4566 1 . GLY 121 121 4566 1 . MET 122 122 4566 1 . ASN 123 123 4566 1 . SER 124 124 4566 1 . SER 125 125 4566 1 . LYS 126 126 4566 1 . ILE 127 127 4566 1 . GLU 128 128 4566 1 stop_ save_ save_FES _Entity.Sf_category entity _Entity.Sf_framecode FES _Entity.Entry_ID 4566 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name FES _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID FES _Entity.Nonpolymer_comp_label $chem_comp_FES _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _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 . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . 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 . FES . 4566 2 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 4566 _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 $bAdx . 562 organism . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli . . . . . . . . . . . . . . pkkAdx . . . . . . 4566 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 4566 _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 $bAdx . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4566 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_FES _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_FES _Chem_comp.Entry_ID 4566 _Chem_comp.ID FES _Chem_comp.Provenance . _Chem_comp.Name 'FE2/S2 (INORGANIC) CLUSTER' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code FES _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code FES _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'Fe2 S2' _Chem_comp.Formula_weight 175.820 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1CZP _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 18 10:07:38 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Fe]1S[Fe]S1 SMILES ACDLabs 10.04 4566 FES S1[Fe]S[Fe]1 SMILES_CANONICAL CACTVS 3.341 4566 FES S1[Fe]S[Fe]1 SMILES CACTVS 3.341 4566 FES S1[Fe]S[Fe]1 SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 4566 FES S1[Fe]S[Fe]1 SMILES 'OpenEye OEToolkits' 1.5.0 4566 FES InChI=1S/2Fe.2S InChI InChI 1.03 4566 FES NIXDOXVAJZFRNF-UHFFFAOYSA-N InChIKey InChI 1.03 4566 FES stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID di-mu-sulfidediiron 'SYSTEMATIC NAME' ACDLabs 10.04 4566 FES 1,3-dithia-2$l^{2},4$l^{2}-diferracyclobutane 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 4566 FES stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID FE1 . FE1 . . FE . . N 0 . . . . no no . . . . 16.237 . 5.409 . 27.398 . 0.000 -0.213 -1.531 1 . 4566 FES FE2 . FE2 . . FE . . N 0 . . . . no no . . . . 16.361 . 2.666 . 27.488 . 0.000 -0.213 1.531 2 . 4566 FES S1 . S1 . . S . . N 0 . . . . no no . . . . 17.422 . 4.079 . 28.829 . 1.461 0.372 0.000 3 . 4566 FES S2 . S2 . . S . . N 0 . . . . no no . . . . 15.380 . 3.919 . 25.972 . -1.461 0.372 0.000 4 . 4566 FES stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING FE1 S1 no N 1 . 4566 FES 2 . SING FE1 S2 no N 2 . 4566 FES 3 . SING FE2 S1 no N 3 . 4566 FES 4 . SING FE2 S2 no N 4 . 4566 FES stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4566 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer. ; _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 'bovine adrenodoxin' '[U-100% 13C; U-100% 15N]' . . 1 $bAdx . . . 1.0 4.0 mM . . . . 4566 1 2 D2O . . . . . . . 5 . . % . . . . 4566 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4566 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; Every sample was fully 15N,13C labeled, only for definite experiments we used a only 15N-labeled sample (TOCSY-15N-HSQC;NOESY-15N-HSQC;HNHB). For each NMR experiment a new sample was neccessary. So we did approximatly 17 samples for the oxidized state. 1 to 5 mM oxydized Adx samples were obtained from E. coli and purified as described elsewhere [8]. For 15N-labelled samples, 15NH4CL was used and for 13C-labelled samples, both 13C6-glucose and 13C3-glycerol were introduced into the growth medium. Purity of the protein was checked by measuring A414/A290>0.9 in Tris/HCl (50mM, pH=7.4) buffer. ; _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 'bovine adrenodoxin' '[U-100% 15N]' . . 1 $bAdx . . . 1.0 4.0 mM . . . . 4566 2 2 D2O . . . . . . . 5 . . % . . . . 4566 2 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 4566 _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 7.4 0.2 n/a 4566 1 temperature 300 1 K 4566 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 4566 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4566 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model 'DMX Avance' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4566 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_1 Bruker DMX . 500 . . . 4566 1 2 NMR_spectrometer_2 Bruker 'DMX Avance' . 600 . . . 4566 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 4566 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 3D-TOCSY-(15N,1H)HSQC . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 2 3D-NOESY-(15N,1H)HSQC . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 3 3D-HNHB . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 4 HNCA . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 5 HN(CO)CA . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 6 H(N)CA,CO . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 7 HNCACB . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 8 HCACO . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 9 HNCO . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 10 (HCA)CO(CA)NH . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 11 HBHA(CO)NH . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 12 HCCH-TOCSY . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 13 HCCC(O)NH . . . . . . . . . . . . . . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 4566 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name 3D-TOCSY-(15N,1H)HSQC _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name 3D-NOESY-(15N,1H)HSQC _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name 3D-HNHB _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name HNCA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name HN(CO)CA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name H(N)CA,CO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name HNCACB _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name HCACO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_10 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_10 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 10 _NMR_spec_expt.Name (HCA)CO(CA)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_11 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_11 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 11 _NMR_spec_expt.Name HBHA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_12 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_12 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 12 _NMR_spec_expt.Name HCCH-TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_13 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_13 _NMR_spec_expt.Entry_ID 4566 _NMR_spec_expt.ID 13 _NMR_spec_expt.Name HCCC(O)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # 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 4566 _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 0.00 internal direct 1.0 internal spherical parallel . . . . . . 4566 1 C 13 DSS 'methyl protons' . . . . ppm 0.00 internal indirect 0.251449530 internal spherical parallel . . . . . . 4566 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 internal indirect 0.101329118 internal spherical parallel . . . . . . 4566 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_bAdx1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode bAdx1 _Assigned_chem_shift_list.Entry_ID 4566 _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 3D-TOCSY-(15N,1H)HSQC . . . 4566 1 2 3D-NOESY-(15N,1H)HSQC . . . 4566 1 3 3D-HNHB . . . 4566 1 4 HNCA . . . 4566 1 5 HN(CO)CA . . . 4566 1 6 H(N)CA,CO . . . 4566 1 7 HNCACB . . . 4566 1 8 HCACO . . . 4566 1 9 HNCO . . . 4566 1 10 (HCA)CO(CA)NH . . . 4566 1 11 HBHA(CO)NH . . . 4566 1 12 HCCH-TOCSY . . . 4566 1 13 HCCC(O)NH . . . 4566 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 3 3 SER CA C 13 58.05 0.03 . 4 . . . . . . . . 4566 1 2 . 1 1 3 3 SER CB C 13 62.81 0.03 . 4 . . . . . . . . 4566 1 3 . 1 1 4 4 GLU H H 1 8.39 0.022 . 1 . . . . . . . . 4566 1 4 . 1 1 4 4 GLU HA H 1 4.24 0.022 . 1 . . . . . . . . 4566 1 5 . 1 1 4 4 GLU HB2 H 1 2.01 0.022 . 2 . . . . . . . . 4566 1 6 . 1 1 4 4 GLU HB3 H 1 1.86 0.022 . 2 . . . . . . . . 4566 1 7 . 1 1 4 4 GLU HG2 H 1 2.37 0.022 . 2 . . . . . . . . 4566 1 8 . 1 1 4 4 GLU HG3 H 1 2.22 0.022 . 2 . . . . . . . . 4566 1 9 . 1 1 4 4 GLU C C 13 175.95 0.03 . 1 . . . . . . . . 4566 1 10 . 1 1 4 4 GLU CA C 13 56.25 0.03 . 1 . . . . . . . . 4566 1 11 . 1 1 4 4 GLU CB C 13 29.35 0.03 . 1 . . . . . . . . 4566 1 12 . 1 1 4 4 GLU CG C 13 35.91 0.03 . 1 . . . . . . . . 4566 1 13 . 1 1 4 4 GLU N N 15 121.2 0.04 . 1 . . . . . . . . 4566 1 14 . 1 1 5 5 ASP H H 1 8.25 0.022 . 1 . . . . . . . . 4566 1 15 . 1 1 5 5 ASP HA H 1 4.54 0.022 . 1 . . . . . . . . 4566 1 16 . 1 1 5 5 ASP HB2 H 1 3.03 0.022 . 2 . . . . . . . . 4566 1 17 . 1 1 5 5 ASP HB3 H 1 2.59 0.022 . 2 . . . . . . . . 4566 1 18 . 1 1 5 5 ASP C C 13 175.15 0.03 . 1 . . . . . . . . 4566 1 19 . 1 1 5 5 ASP CA C 13 53.76 0.03 . 1 . . . . . . . . 4566 1 20 . 1 1 5 5 ASP CB C 13 40.11 0.03 . 1 . . . . . . . . 4566 1 21 . 1 1 5 5 ASP N N 15 120.73 0.04 . 1 . . . . . . . . 4566 1 22 . 1 1 6 6 LYS H H 1 7.88 0.022 . 1 . . . . . . . . 4566 1 23 . 1 1 6 6 LYS HA H 1 4.89 0.022 . 1 . . . . . . . . 4566 1 24 . 1 1 6 6 LYS HB2 H 1 1.59 0.022 . 2 . . . . . . . . 4566 1 25 . 1 1 6 6 LYS HG2 H 1 1.45 0.022 . 2 . . . . . . . . 4566 1 26 . 1 1 6 6 LYS HG3 H 1 1.17 0.022 . 2 . . . . . . . . 4566 1 27 . 1 1 6 6 LYS HD2 H 1 1.66 0.022 . 4 . . . . . . . . 4566 1 28 . 1 1 6 6 LYS HE2 H 1 2.8 0.022 . 4 . . . . . . . . 4566 1 29 . 1 1 6 6 LYS C C 13 175.95 0.03 . 1 . . . . . . . . 4566 1 30 . 1 1 6 6 LYS CA C 13 54.72 0.03 . 1 . . . . . . . . 4566 1 31 . 1 1 6 6 LYS CB C 13 34.71 0.03 . 1 . . . . . . . . 4566 1 32 . 1 1 6 6 LYS CG C 13 24.81 0.03 . 1 . . . . . . . . 4566 1 33 . 1 1 6 6 LYS CD C 13 28.78 0.03 . 1 . . . . . . . . 4566 1 34 . 1 1 6 6 LYS CE C 13 41.72 0.03 . 1 . . . . . . . . 4566 1 35 . 1 1 6 6 LYS N N 15 118.92 0.04 . 1 . . . . . . . . 4566 1 36 . 1 1 7 7 ILE H H 1 8.92 0.022 . 1 . . . . . . . . 4566 1 37 . 1 1 7 7 ILE HA H 1 4.43 0.022 . 1 . . . . . . . . 4566 1 38 . 1 1 7 7 ILE HB H 1 1.85 0.022 . 1 . . . . . . . . 4566 1 39 . 1 1 7 7 ILE HG12 H 1 0.73 0.022 . 2 . . . . . . . . 4566 1 40 . 1 1 7 7 ILE HG13 H 1 0.61 0.022 . 2 . . . . . . . . 4566 1 41 . 1 1 7 7 ILE HG21 H 1 1.04 0.022 . 1 . . . . . . . . 4566 1 42 . 1 1 7 7 ILE HG22 H 1 1.04 0.022 . 1 . . . . . . . . 4566 1 43 . 1 1 7 7 ILE HG23 H 1 1.04 0.022 . 1 . . . . . . . . 4566 1 44 . 1 1 7 7 ILE HD11 H 1 0.64 0.022 . 1 . . . . . . . . 4566 1 45 . 1 1 7 7 ILE HD12 H 1 0.64 0.022 . 1 . . . . . . . . 4566 1 46 . 1 1 7 7 ILE HD13 H 1 0.64 0.022 . 1 . . . . . . . . 4566 1 47 . 1 1 7 7 ILE C C 13 174.58 0.03 . 1 . . . . . . . . 4566 1 48 . 1 1 7 7 ILE CA C 13 58.36 0.03 . 1 . . . . . . . . 4566 1 49 . 1 1 7 7 ILE CB C 13 40.11 0.03 . 1 . . . . . . . . 4566 1 50 . 1 1 7 7 ILE CG1 C 13 25.08 0.03 . 1 . . . . . . . . 4566 1 51 . 1 1 7 7 ILE CG2 C 13 17.68 0.03 . 1 . . . . . . . . 4566 1 52 . 1 1 7 7 ILE CD1 C 13 13.46 0.03 . 1 . . . . . . . . 4566 1 53 . 1 1 7 7 ILE N N 15 117.69 0.04 . 1 . . . . . . . . 4566 1 54 . 1 1 8 8 THR H H 1 8.76 0.022 . 1 . . . . . . . . 4566 1 55 . 1 1 8 8 THR HA H 1 4.73 0.022 . 1 . . . . . . . . 4566 1 56 . 1 1 8 8 THR HB H 1 3.83 0.022 . 1 . . . . . . . . 4566 1 57 . 1 1 8 8 THR HG21 H 1 0.78 0.022 . 1 . . . . . . . . 4566 1 58 . 1 1 8 8 THR HG22 H 1 0.78 0.022 . 1 . . . . . . . . 4566 1 59 . 1 1 8 8 THR HG23 H 1 0.78 0.022 . 1 . . . . . . . . 4566 1 60 . 1 1 8 8 THR C C 13 173.78 0.03 . 1 . . . . . . . . 4566 1 61 . 1 1 8 8 THR CA C 13 62.58 0.03 . 1 . . . . . . . . 4566 1 62 . 1 1 8 8 THR CB C 13 68.42 0.03 . 1 . . . . . . . . 4566 1 63 . 1 1 8 8 THR CG2 C 13 21.12 0.03 . 1 . . . . . . . . 4566 1 64 . 1 1 8 8 THR N N 15 121.32 0.04 . 1 . . . . . . . . 4566 1 65 . 1 1 9 9 VAL H H 1 8.53 0.022 . 1 . . . . . . . . 4566 1 66 . 1 1 9 9 VAL HA H 1 4.16 0.022 . 1 . . . . . . . . 4566 1 67 . 1 1 9 9 VAL HB H 1 1.52 0.022 . 1 . . . . . . . . 4566 1 68 . 1 1 9 9 VAL HG11 H 1 0.67 0.022 . 2 . . . . . . . . 4566 1 69 . 1 1 9 9 VAL HG12 H 1 0.67 0.022 . 2 . . . . . . . . 4566 1 70 . 1 1 9 9 VAL HG13 H 1 0.67 0.022 . 2 . . . . . . . . 4566 1 71 . 1 1 9 9 VAL HG21 H 1 0.35 0.022 . 2 . . . . . . . . 4566 1 72 . 1 1 9 9 VAL HG22 H 1 0.35 0.022 . 2 . . . . . . . . 4566 1 73 . 1 1 9 9 VAL HG23 H 1 0.35 0.022 . 2 . . . . . . . . 4566 1 74 . 1 1 9 9 VAL C C 13 173.21 0.03 . 1 . . . . . . . . 4566 1 75 . 1 1 9 9 VAL CA C 13 60.47 0.03 . 1 . . . . . . . . 4566 1 76 . 1 1 9 9 VAL CB C 13 34.71 0.03 . 1 . . . . . . . . 4566 1 77 . 1 1 9 9 VAL CG1 C 13 22.6 0.03 . 2 . . . . . . . . 4566 1 78 . 1 1 9 9 VAL CG2 C 13 21.65 0.03 . 2 . . . . . . . . 4566 1 79 . 1 1 9 9 VAL N N 15 124.54 0.04 . 1 . . . . . . . . 4566 1 80 . 1 1 10 10 HIS H H 1 8.57 0.022 . 1 . . . . . . . . 4566 1 81 . 1 1 10 10 HIS HA H 1 5.4 0.022 . 1 . . . . . . . . 4566 1 82 . 1 1 10 10 HIS HB2 H 1 3.24 0.022 . 2 . . . . . . . . 4566 1 83 . 1 1 10 10 HIS HB3 H 1 2.59 0.022 . 2 . . . . . . . . 4566 1 84 . 1 1 10 10 HIS C C 13 174.34 0.03 . 1 . . . . . . . . 4566 1 85 . 1 1 10 10 HIS CA C 13 53.76 0.03 . 1 . . . . . . . . 4566 1 86 . 1 1 10 10 HIS CB C 13 30.82 0.03 . 1 . . . . . . . . 4566 1 87 . 1 1 10 10 HIS N N 15 125.48 0.04 . 1 . . . . . . . . 4566 1 88 . 1 1 11 11 PHE H H 1 9.56 0.022 . 1 . . . . . . . . 4566 1 89 . 1 1 11 11 PHE HA H 1 5.08 0.022 . 1 . . . . . . . . 4566 1 90 . 1 1 11 11 PHE HB2 H 1 3.01 0.022 . 2 . . . . . . . . 4566 1 91 . 1 1 11 11 PHE HB3 H 1 2.21 0.022 . 2 . . . . . . . . 4566 1 92 . 1 1 11 11 PHE C C 13 175.27 0.03 . 1 . . . . . . . . 4566 1 93 . 1 1 11 11 PHE CA C 13 55.1 0.03 . 1 . . . . . . . . 4566 1 94 . 1 1 11 11 PHE CB C 13 40.95 0.03 . 1 . . . . . . . . 4566 1 95 . 1 1 11 11 PHE N N 15 122.32 0.04 . 1 . . . . . . . . 4566 1 96 . 1 1 12 12 ILE H H 1 9.02 0.022 . 1 . . . . . . . . 4566 1 97 . 1 1 12 12 ILE HA H 1 4.66 0.022 . 1 . . . . . . . . 4566 1 98 . 1 1 12 12 ILE HB H 1 1.67 0.022 . 1 . . . . . . . . 4566 1 99 . 1 1 12 12 ILE HG12 H 1 1.28 0.022 . 2 . . . . . . . . 4566 1 100 . 1 1 12 12 ILE HG13 H 1 1.06 0.022 . 2 . . . . . . . . 4566 1 101 . 1 1 12 12 ILE HG21 H 1 0.89 0.022 . 1 . . . . . . . . 4566 1 102 . 1 1 12 12 ILE HG22 H 1 0.89 0.022 . 1 . . . . . . . . 4566 1 103 . 1 1 12 12 ILE HG23 H 1 0.89 0.022 . 1 . . . . . . . . 4566 1 104 . 1 1 12 12 ILE HD11 H 1 0.66 0.022 . 1 . . . . . . . . 4566 1 105 . 1 1 12 12 ILE HD12 H 1 0.66 0.022 . 1 . . . . . . . . 4566 1 106 . 1 1 12 12 ILE HD13 H 1 0.66 0.022 . 1 . . . . . . . . 4566 1 107 . 1 1 12 12 ILE C C 13 175.84 0.03 . 1 . . . . . . . . 4566 1 108 . 1 1 12 12 ILE CA C 13 59.9 0.03 . 1 . . . . . . . . 4566 1 109 . 1 1 12 12 ILE CB C 13 36.63 0.03 . 1 . . . . . . . . 4566 1 110 . 1 1 12 12 ILE CG1 C 13 26.14 0.03 . 1 . . . . . . . . 4566 1 111 . 1 1 12 12 ILE CG2 C 13 16.36 0.03 . 1 . . . . . . . . 4566 1 112 . 1 1 12 12 ILE CD1 C 13 12.14 0.03 . 1 . . . . . . . . 4566 1 113 . 1 1 12 12 ILE N N 15 122.9 0.04 . 1 . . . . . . . . 4566 1 114 . 1 1 13 13 ASN H H 1 8.85 0.022 . 1 . . . . . . . . 4566 1 115 . 1 1 13 13 ASN HA H 1 4.69 0.022 . 1 . . . . . . . . 4566 1 116 . 1 1 13 13 ASN HB2 H 1 3.35 0.022 . 2 . . . . . . . . 4566 1 117 . 1 1 13 13 ASN HB3 H 1 2.97 0.022 . 2 . . . . . . . . 4566 1 118 . 1 1 13 13 ASN HD21 H 1 7.83 0.022 . 2 . . . . . . . . 4566 1 119 . 1 1 13 13 ASN HD22 H 1 7.3 0.022 . 2 . . . . . . . . 4566 1 120 . 1 1 13 13 ASN C C 13 176.75 0.03 . 1 . . . . . . . . 4566 1 121 . 1 1 13 13 ASN CA C 13 50.69 0.03 . 1 . . . . . . . . 4566 1 122 . 1 1 13 13 ASN CB C 13 38.07 0.03 . 1 . . . . . . . . 4566 1 123 . 1 1 13 13 ASN N N 15 125.07 0.04 . 1 . . . . . . . . 4566 1 124 . 1 1 13 13 ASN ND2 N 15 112.04 0.04 . 1 . . . . . . . . 4566 1 125 . 1 1 14 14 ARG H H 1 8.55 0.022 . 1 . . . . . . . . 4566 1 126 . 1 1 14 14 ARG HA H 1 4.01 0.022 . 1 . . . . . . . . 4566 1 127 . 1 1 14 14 ARG HB2 H 1 1.78 0.022 . 2 . . . . . . . . 4566 1 128 . 1 1 14 14 ARG HG2 H 1 1.57 0.022 . 2 . . . . . . . . 4566 1 129 . 1 1 14 14 ARG HD2 H 1 3.28 0.022 . 2 . . . . . . . . 4566 1 130 . 1 1 14 14 ARG C C 13 176.07 0.03 . 1 . . . . . . . . 4566 1 131 . 1 1 14 14 ARG CA C 13 58.56 0.03 . 1 . . . . . . . . 4566 1 132 . 1 1 14 14 ARG CB C 13 29.03 0.03 . 1 . . . . . . . . 4566 1 133 . 1 1 14 14 ARG CG C 13 28.2 0.03 . 1 . . . . . . . . 4566 1 134 . 1 1 14 14 ARG CD C 13 43.57 0.03 . 1 . . . . . . . . 4566 1 135 . 1 1 14 14 ARG N N 15 118.92 0.04 . 1 . . . . . . . . 4566 1 136 . 1 1 15 15 ASP H H 1 7.67 0.022 . 1 . . . . . . . . 4566 1 137 . 1 1 15 15 ASP HA H 1 4.54 0.022 . 1 . . . . . . . . 4566 1 138 . 1 1 15 15 ASP HB2 H 1 2.82 0.022 . 2 . . . . . . . . 4566 1 139 . 1 1 15 15 ASP HB3 H 1 2.67 0.022 . 2 . . . . . . . . 4566 1 140 . 1 1 15 15 ASP C C 13 176.46 0.03 . 1 . . . . . . . . 4566 1 141 . 1 1 15 15 ASP CA C 13 52.99 0.03 . 1 . . . . . . . . 4566 1 142 . 1 1 15 15 ASP CB C 13 39.9 0.03 . 1 . . . . . . . . 4566 1 143 . 1 1 15 15 ASP N N 15 116.04 0.04 . 1 . . . . . . . . 4566 1 144 . 1 1 16 16 GLY H H 1 8.17 0.022 . 1 . . . . . . . . 4566 1 145 . 1 1 16 16 GLY HA2 H 1 4.16 0.022 . 2 . . . . . . . . 4566 1 146 . 1 1 16 16 GLY HA3 H 1 3.43 0.022 . 2 . . . . . . . . 4566 1 147 . 1 1 16 16 GLY C C 13 175.81 0.03 . 1 . . . . . . . . 4566 1 148 . 1 1 16 16 GLY CA C 13 44.74 0.03 . 1 . . . . . . . . 4566 1 149 . 1 1 16 16 GLY N N 15 108.31 0.04 . 1 . . . . . . . . 4566 1 150 . 1 1 17 17 GLU H H 1 7.97 0.022 . 1 . . . . . . . . 4566 1 151 . 1 1 17 17 GLU HA H 1 4.26 0.022 . 1 . . . . . . . . 4566 1 152 . 1 1 17 17 GLU HB2 H 1 1.94 0.022 . 2 . . . . . . . . 4566 1 153 . 1 1 17 17 GLU HG2 H 1 2.27 0.022 . 2 . . . . . . . . 4566 1 154 . 1 1 17 17 GLU C C 13 175.38 0.03 . 1 . . . . . . . . 4566 1 155 . 1 1 17 17 GLU CA C 13 55.49 0.03 . 1 . . . . . . . . 4566 1 156 . 1 1 17 17 GLU CB C 13 29.52 0.03 . 1 . . . . . . . . 4566 1 157 . 1 1 17 17 GLU CG C 13 35.64 0.03 . 1 . . . . . . . . 4566 1 158 . 1 1 17 17 GLU N N 15 122.32 0.04 . 1 . . . . . . . . 4566 1 159 . 1 1 18 18 THR H H 1 8.63 0.022 . 1 . . . . . . . . 4566 1 160 . 1 1 18 18 THR HA H 1 4.89 0.022 . 1 . . . . . . . . 4566 1 161 . 1 1 18 18 THR HB H 1 3.97 0.022 . 1 . . . . . . . . 4566 1 162 . 1 1 18 18 THR HG21 H 1 1.06 0.022 . 1 . . . . . . . . 4566 1 163 . 1 1 18 18 THR HG22 H 1 1.06 0.022 . 1 . . . . . . . . 4566 1 164 . 1 1 18 18 THR HG23 H 1 1.06 0.022 . 1 . . . . . . . . 4566 1 165 . 1 1 18 18 THR C C 13 174.13 0.03 . 1 . . . . . . . . 4566 1 166 . 1 1 18 18 THR CA C 13 62.39 0.03 . 1 . . . . . . . . 4566 1 167 . 1 1 18 18 THR CB C 13 68.21 0.03 . 1 . . . . . . . . 4566 1 168 . 1 1 18 18 THR CG2 C 13 21.12 0.03 . 1 . . . . . . . . 4566 1 169 . 1 1 18 18 THR N N 15 119.09 0.04 . 1 . . . . . . . . 4566 1 170 . 1 1 19 19 LEU H H 1 10.02 0.022 . 1 . . . . . . . . 4566 1 171 . 1 1 19 19 LEU HA H 1 4.76 0.022 . 1 . . . . . . . . 4566 1 172 . 1 1 19 19 LEU HB2 H 1 1.9 0.022 . 2 . . . . . . . . 4566 1 173 . 1 1 19 19 LEU HB3 H 1 1.43 0.022 . 2 . . . . . . . . 4566 1 174 . 1 1 19 19 LEU HG H 1 1.7 0.022 . 1 . . . . . . . . 4566 1 175 . 1 1 19 19 LEU HD11 H 1 0.83 0.022 . 2 . . . . . . . . 4566 1 176 . 1 1 19 19 LEU HD12 H 1 0.83 0.022 . 2 . . . . . . . . 4566 1 177 . 1 1 19 19 LEU HD13 H 1 0.83 0.022 . 2 . . . . . . . . 4566 1 178 . 1 1 19 19 LEU C C 13 175.38 0.03 . 1 . . . . . . . . 4566 1 179 . 1 1 19 19 LEU CA C 13 52.8 0.03 . 1 . . . . . . . . 4566 1 180 . 1 1 19 19 LEU CB C 13 42.05 0.03 . 1 . . . . . . . . 4566 1 181 . 1 1 19 19 LEU CG C 13 25.34 0.03 . 1 . . . . . . . . 4566 1 182 . 1 1 19 19 LEU CD1 C 13 22.7 0.03 . 2 . . . . . . . . 4566 1 183 . 1 1 19 19 LEU N N 15 131.28 0.04 . 1 . . . . . . . . 4566 1 184 . 1 1 20 20 THR H H 1 8.8 0.022 . 1 . . . . . . . . 4566 1 185 . 1 1 20 20 THR HA H 1 4.89 0.022 . 1 . . . . . . . . 4566 1 186 . 1 1 20 20 THR HB H 1 3.78 0.022 . 1 . . . . . . . . 4566 1 187 . 1 1 20 20 THR HG21 H 1 1.17 0.022 . 1 . . . . . . . . 4566 1 188 . 1 1 20 20 THR HG22 H 1 1.17 0.022 . 1 . . . . . . . . 4566 1 189 . 1 1 20 20 THR HG23 H 1 1.17 0.022 . 1 . . . . . . . . 4566 1 190 . 1 1 20 20 THR C C 13 173.9 0.03 . 1 . . . . . . . . 4566 1 191 . 1 1 20 20 THR CA C 13 63.35 0.03 . 1 . . . . . . . . 4566 1 192 . 1 1 20 20 THR CB C 13 69.51 0.03 . 1 . . . . . . . . 4566 1 193 . 1 1 20 20 THR CG2 C 13 22.17 0.03 . 1 . . . . . . . . 4566 1 194 . 1 1 20 20 THR N N 15 122.96 0.04 . 1 . . . . . . . . 4566 1 195 . 1 1 21 21 THR H H 1 8.82 0.022 . 1 . . . . . . . . 4566 1 196 . 1 1 21 21 THR HA H 1 4.71 0.022 . 1 . . . . . . . . 4566 1 197 . 1 1 21 21 THR HB H 1 3.74 0.022 . 1 . . . . . . . . 4566 1 198 . 1 1 21 21 THR HG21 H 1 0.9 0.022 . 1 . . . . . . . . 4566 1 199 . 1 1 21 21 THR HG22 H 1 0.9 0.022 . 1 . . . . . . . . 4566 1 200 . 1 1 21 21 THR HG23 H 1 0.9 0.022 . 1 . . . . . . . . 4566 1 201 . 1 1 21 21 THR C C 13 171.61 0.03 . 1 . . . . . . . . 4566 1 202 . 1 1 21 21 THR CA C 13 59.52 0.03 . 1 . . . . . . . . 4566 1 203 . 1 1 21 21 THR CB C 13 69.51 0.03 . 1 . . . . . . . . 4566 1 204 . 1 1 21 21 THR CG2 C 13 19.53 0.03 . 1 . . . . . . . . 4566 1 205 . 1 1 21 21 THR N N 15 122.49 0.04 . 1 . . . . . . . . 4566 1 206 . 1 1 22 22 LYS H H 1 7.97 0.022 . 1 . . . . . . . . 4566 1 207 . 1 1 22 22 LYS HA H 1 5.54 0.022 . 1 . . . . . . . . 4566 1 208 . 1 1 22 22 LYS HB2 H 1 1.67 0.022 . 2 . . . . . . . . 4566 1 209 . 1 1 22 22 LYS HB3 H 1 1.44 0.022 . 2 . . . . . . . . 4566 1 210 . 1 1 22 22 LYS HE2 H 1 2.76 0.022 . 2 . . . . . . . . 4566 1 211 . 1 1 22 22 LYS C C 13 176.18 0.03 . 1 . . . . . . . . 4566 1 212 . 1 1 22 22 LYS CA C 13 53.38 0.03 . 1 . . . . . . . . 4566 1 213 . 1 1 22 22 LYS CB C 13 35.12 0.03 . 1 . . . . . . . . 4566 1 214 . 1 1 22 22 LYS CG C 13 24.02 0.03 . 1 . . . . . . . . 4566 1 215 . 1 1 22 22 LYS CD C 13 28.78 0.03 . 1 . . . . . . . . 4566 1 216 . 1 1 22 22 LYS CE C 13 41.72 0.03 . 1 . . . . . . . . 4566 1 217 . 1 1 22 22 LYS N N 15 118.33 0.04 . 1 . . . . . . . . 4566 1 218 . 1 1 23 23 GLY H H 1 8.81 0.022 . 1 . . . . . . . . 4566 1 219 . 1 1 23 23 GLY HA2 H 1 4.58 0.022 . 2 . . . . . . . . 4566 1 220 . 1 1 23 23 GLY HA3 H 1 3.2 0.022 . 2 . . . . . . . . 4566 1 221 . 1 1 23 23 GLY C C 13 170.73 0.03 . 1 . . . . . . . . 4566 1 222 . 1 1 23 23 GLY CA C 13 43.4 0.03 . 1 . . . . . . . . 4566 1 223 . 1 1 23 23 GLY N N 15 107.14 0.04 . 1 . . . . . . . . 4566 1 224 . 1 1 24 24 LYS H H 1 8.85 0.022 . 1 . . . . . . . . 4566 1 225 . 1 1 24 24 LYS HA H 1 4.62 0.022 . 1 . . . . . . . . 4566 1 226 . 1 1 24 24 LYS HB2 H 1 1.59 0.022 . 2 . . . . . . . . 4566 1 227 . 1 1 24 24 LYS HG2 H 1 1.38 0.022 . 2 . . . . . . . . 4566 1 228 . 1 1 24 24 LYS HE2 H 1 2.95 0.022 . 2 . . . . . . . . 4566 1 229 . 1 1 24 24 LYS C C 13 175.95 0.03 . 1 . . . . . . . . 4566 1 230 . 1 1 24 24 LYS CA C 13 54.53 0.03 . 1 . . . . . . . . 4566 1 231 . 1 1 24 24 LYS CB C 13 32.98 0.03 . 1 . . . . . . . . 4566 1 232 . 1 1 24 24 LYS CG C 13 24.02 0.03 . 1 . . . . . . . . 4566 1 233 . 1 1 24 24 LYS CD C 13 28.51 0.03 . 1 . . . . . . . . 4566 1 234 . 1 1 24 24 LYS CE C 13 41.57 0.03 . 1 . . . . . . . . 4566 1 235 . 1 1 24 24 LYS N N 15 121.91 0.04 . 1 . . . . . . . . 4566 1 236 . 1 1 25 25 ILE H H 1 8.3 0.022 . 1 . . . . . . . . 4566 1 237 . 1 1 25 25 ILE HA H 1 3.28 0.022 . 1 . . . . . . . . 4566 1 238 . 1 1 25 25 ILE HB H 1 1.7 0.022 . 1 . . . . . . . . 4566 1 239 . 1 1 25 25 ILE HG12 H 1 1.52 0.022 . 2 . . . . . . . . 4566 1 240 . 1 1 25 25 ILE HG21 H 1 0.9 0.022 . 1 . . . . . . . . 4566 1 241 . 1 1 25 25 ILE HG22 H 1 0.9 0.022 . 1 . . . . . . . . 4566 1 242 . 1 1 25 25 ILE HG23 H 1 0.9 0.022 . 1 . . . . . . . . 4566 1 243 . 1 1 25 25 ILE HD11 H 1 0.71 0.022 . 1 . . . . . . . . 4566 1 244 . 1 1 25 25 ILE HD12 H 1 0.71 0.022 . 1 . . . . . . . . 4566 1 245 . 1 1 25 25 ILE HD13 H 1 0.71 0.022 . 1 . . . . . . . . 4566 1 246 . 1 1 25 25 ILE C C 13 177.35 0.03 . 1 . . . . . . . . 4566 1 247 . 1 1 25 25 ILE CA C 13 62.78 0.03 . 1 . . . . . . . . 4566 1 248 . 1 1 25 25 ILE CB C 13 36.14 0.03 . 1 . . . . . . . . 4566 1 249 . 1 1 25 25 ILE CG1 C 13 28.25 0.03 . 1 . . . . . . . . 4566 1 250 . 1 1 25 25 ILE CG2 C 13 16.63 0.03 . 1 . . . . . . . . 4566 1 251 . 1 1 25 25 ILE CD1 C 13 11.87 0.03 . 1 . . . . . . . . 4566 1 252 . 1 1 25 25 ILE N N 15 122.49 0.04 . 1 . . . . . . . . 4566 1 253 . 1 1 26 26 GLY H H 1 8.84 0.022 . 1 . . . . . . . . 4566 1 254 . 1 1 26 26 GLY HA2 H 1 4.49 0.022 . 2 . . . . . . . . 4566 1 255 . 1 1 26 26 GLY HA3 H 1 3.56 0.022 . 2 . . . . . . . . 4566 1 256 . 1 1 26 26 GLY C C 13 173.94 0.03 . 1 . . . . . . . . 4566 1 257 . 1 1 26 26 GLY CA C 13 44.55 0.03 . 1 . . . . . . . . 4566 1 258 . 1 1 26 26 GLY N N 15 117.04 0.04 . 1 . . . . . . . . 4566 1 259 . 1 1 27 27 ASP H H 1 8.09 0.022 . 1 . . . . . . . . 4566 1 260 . 1 1 27 27 ASP HA H 1 4.84 0.022 . 1 . . . . . . . . 4566 1 261 . 1 1 27 27 ASP HB2 H 1 2.9 0.022 . 2 . . . . . . . . 4566 1 262 . 1 1 27 27 ASP HB3 H 1 2.82 0.022 . 2 . . . . . . . . 4566 1 263 . 1 1 27 27 ASP C C 13 176.18 0.03 . 1 . . . . . . . . 4566 1 264 . 1 1 27 27 ASP CA C 13 53.95 0.03 . 1 . . . . . . . . 4566 1 265 . 1 1 27 27 ASP CB C 13 40.55 0.03 . 1 . . . . . . . . 4566 1 266 . 1 1 27 27 ASP N N 15 122.32 0.04 . 1 . . . . . . . . 4566 1 267 . 1 1 28 28 SER H H 1 9.68 0.022 . 1 . . . . . . . . 4566 1 268 . 1 1 28 28 SER HA H 1 5.77 0.022 . 1 . . . . . . . . 4566 1 269 . 1 1 28 28 SER HB2 H 1 4.21 0.022 . 2 . . . . . . . . 4566 1 270 . 1 1 28 28 SER HB3 H 1 3.99 0.022 . 2 . . . . . . . . 4566 1 271 . 1 1 28 28 SER C C 13 176.41 0.03 . 1 . . . . . . . . 4566 1 272 . 1 1 28 28 SER CA C 13 56.64 0.03 . 1 . . . . . . . . 4566 1 273 . 1 1 28 28 SER CB C 13 65.62 0.03 . 1 . . . . . . . . 4566 1 274 . 1 1 28 28 SER N N 15 118.04 0.04 . 1 . . . . . . . . 4566 1 275 . 1 1 29 29 LEU H H 1 8.16 0.022 . 1 . . . . . . . . 4566 1 276 . 1 1 29 29 LEU HA H 1 4.21 0.022 . 1 . . . . . . . . 4566 1 277 . 1 1 29 29 LEU HB2 H 1 2.33 0.022 . 2 . . . . . . . . 4566 1 278 . 1 1 29 29 LEU HB3 H 1 1.47 0.022 . 2 . . . . . . . . 4566 1 279 . 1 1 29 29 LEU HG H 1 1.8 0.022 . 1 . . . . . . . . 4566 1 280 . 1 1 29 29 LEU HD11 H 1 1.04 0.022 . 2 . . . . . . . . 4566 1 281 . 1 1 29 29 LEU HD12 H 1 1.04 0.022 . 2 . . . . . . . . 4566 1 282 . 1 1 29 29 LEU HD13 H 1 1.04 0.022 . 2 . . . . . . . . 4566 1 283 . 1 1 29 29 LEU HD21 H 1 0.85 0.022 . 2 . . . . . . . . 4566 1 284 . 1 1 29 29 LEU HD22 H 1 0.85 0.022 . 2 . . . . . . . . 4566 1 285 . 1 1 29 29 LEU HD23 H 1 0.85 0.022 . 2 . . . . . . . . 4566 1 286 . 1 1 29 29 LEU C C 13 179.04 0.03 . 1 . . . . . . . . 4566 1 287 . 1 1 29 29 LEU CA C 13 57.4 0.03 . 1 . . . . . . . . 4566 1 288 . 1 1 29 29 LEU CB C 13 40.36 0.03 . 1 . . . . . . . . 4566 1 289 . 1 1 29 29 LEU CG C 13 25.87 0.03 . 1 . . . . . . . . 4566 1 290 . 1 1 29 29 LEU CD1 C 13 23.76 0.03 . 2 . . . . . . . . 4566 1 291 . 1 1 29 29 LEU N N 15 118.68 0.04 . 1 . . . . . . . . 4566 1 292 . 1 1 30 30 LEU H H 1 7.26 0.022 . 1 . . . . . . . . 4566 1 293 . 1 1 30 30 LEU HA H 1 4.49 0.022 . 1 . . . . . . . . 4566 1 294 . 1 1 30 30 LEU HB2 H 1 2.23 0.022 . 2 . . . . . . . . 4566 1 295 . 1 1 30 30 LEU HB3 H 1 1.32 0.022 . 2 . . . . . . . . 4566 1 296 . 1 1 30 30 LEU HG H 1 1.85 0.022 . 1 . . . . . . . . 4566 1 297 . 1 1 30 30 LEU HD11 H 1 0.78 0.022 . 2 . . . . . . . . 4566 1 298 . 1 1 30 30 LEU HD12 H 1 0.78 0.022 . 2 . . . . . . . . 4566 1 299 . 1 1 30 30 LEU HD13 H 1 0.78 0.022 . 2 . . . . . . . . 4566 1 300 . 1 1 30 30 LEU HD21 H 1 0.66 0.022 . 2 . . . . . . . . 4566 1 301 . 1 1 30 30 LEU HD22 H 1 0.66 0.022 . 2 . . . . . . . . 4566 1 302 . 1 1 30 30 LEU HD23 H 1 0.66 0.022 . 2 . . . . . . . . 4566 1 303 . 1 1 30 30 LEU C C 13 176.42 0.03 . 1 . . . . . . . . 4566 1 304 . 1 1 30 30 LEU CA C 13 57.79 0.03 . 1 . . . . . . . . 4566 1 305 . 1 1 30 30 LEU CB C 13 42.09 0.03 . 1 . . . . . . . . 4566 1 306 . 1 1 30 30 LEU CG C 13 27.12 0.03 . 1 . . . . . . . . 4566 1 307 . 1 1 30 30 LEU CD1 C 13 22.44 0.03 . 4 . . . . . . . . 4566 1 308 . 1 1 30 30 LEU N N 15 116.75 0.04 . 1 . . . . . . . . 4566 1 309 . 1 1 31 31 ASP H H 1 7.87 0.022 . 1 . . . . . . . . 4566 1 310 . 1 1 31 31 ASP HA H 1 4.31 0.022 . 1 . . . . . . . . 4566 1 311 . 1 1 31 31 ASP HB2 H 1 2.76 0.022 . 2 . . . . . . . . 4566 1 312 . 1 1 31 31 ASP HB3 H 1 2.49 0.022 . 2 . . . . . . . . 4566 1 313 . 1 1 31 31 ASP C C 13 178.01 0.03 . 1 . . . . . . . . 4566 1 314 . 1 1 31 31 ASP CA C 13 57.4 0.03 . 1 . . . . . . . . 4566 1 315 . 1 1 31 31 ASP CB C 13 39.45 0.03 . 1 . . . . . . . . 4566 1 316 . 1 1 31 31 ASP N N 15 120.73 0.04 . 1 . . . . . . . . 4566 1 317 . 1 1 32 32 VAL H H 1 7.75 0.022 . 1 . . . . . . . . 4566 1 318 . 1 1 32 32 VAL HA H 1 3.58 0.022 . 1 . . . . . . . . 4566 1 319 . 1 1 32 32 VAL HB H 1 2.28 0.022 . 1 . . . . . . . . 4566 1 320 . 1 1 32 32 VAL HG11 H 1 1.18 0.022 . 2 . . . . . . . . 4566 1 321 . 1 1 32 32 VAL HG12 H 1 1.18 0.022 . 2 . . . . . . . . 4566 1 322 . 1 1 32 32 VAL HG13 H 1 1.18 0.022 . 2 . . . . . . . . 4566 1 323 . 1 1 32 32 VAL HG21 H 1 0.85 0.022 . 2 . . . . . . . . 4566 1 324 . 1 1 32 32 VAL HG22 H 1 0.85 0.022 . 2 . . . . . . . . 4566 1 325 . 1 1 32 32 VAL HG23 H 1 0.85 0.022 . 2 . . . . . . . . 4566 1 326 . 1 1 32 32 VAL C C 13 178.13 0.03 . 1 . . . . . . . . 4566 1 327 . 1 1 32 32 VAL CA C 13 65.85 0.03 . 1 . . . . . . . . 4566 1 328 . 1 1 32 32 VAL CB C 13 31.39 0.03 . 1 . . . . . . . . 4566 1 329 . 1 1 32 32 VAL CG1 C 13 22.7 0.03 . 1 . . . . . . . . 4566 1 330 . 1 1 32 32 VAL CG2 C 13 23.49 0.03 . 1 . . . . . . . . 4566 1 331 . 1 1 32 32 VAL N N 15 117.16 0.04 . 1 . . . . . . . . 4566 1 332 . 1 1 33 33 VAL H H 1 7.42 0.022 . 1 . . . . . . . . 4566 1 333 . 1 1 33 33 VAL HA H 1 3.04 0.022 . 1 . . . . . . . . 4566 1 334 . 1 1 33 33 VAL HB H 1 2.11 0.022 . 1 . . . . . . . . 4566 1 335 . 1 1 33 33 VAL HG11 H 1 0.18 0.022 . 2 . . . . . . . . 4566 1 336 . 1 1 33 33 VAL HG12 H 1 0.18 0.022 . 2 . . . . . . . . 4566 1 337 . 1 1 33 33 VAL HG13 H 1 0.18 0.022 . 2 . . . . . . . . 4566 1 338 . 1 1 33 33 VAL HG21 H 1 0.56 0.022 . 2 . . . . . . . . 4566 1 339 . 1 1 33 33 VAL HG22 H 1 0.56 0.022 . 2 . . . . . . . . 4566 1 340 . 1 1 33 33 VAL HG23 H 1 0.56 0.022 . 2 . . . . . . . . 4566 1 341 . 1 1 33 33 VAL C C 13 177.78 0.03 . 1 . . . . . . . . 4566 1 342 . 1 1 33 33 VAL CA C 13 66.61 0.03 . 1 . . . . . . . . 4566 1 343 . 1 1 33 33 VAL CB C 13 31.25 0.03 . 1 . . . . . . . . 4566 1 344 . 1 1 33 33 VAL CG1 C 13 22.97 0.03 . 4 . . . . . . . . 4566 1 345 . 1 1 33 33 VAL CG2 C 13 20.32 0.03 . 4 . . . . . . . . 4566 1 346 . 1 1 33 33 VAL N N 15 120.97 0.04 . 1 . . . . . . . . 4566 1 347 . 1 1 34 34 VAL H H 1 8.46 0.022 . 1 . . . . . . . . 4566 1 348 . 1 1 34 34 VAL HA H 1 3.7 0.022 . 1 . . . . . . . . 4566 1 349 . 1 1 34 34 VAL HB H 1 2.13 0.022 . 1 . . . . . . . . 4566 1 350 . 1 1 34 34 VAL HG11 H 1 0.9 0.022 . 2 . . . . . . . . 4566 1 351 . 1 1 34 34 VAL HG12 H 1 0.9 0.022 . 2 . . . . . . . . 4566 1 352 . 1 1 34 34 VAL HG13 H 1 0.9 0.022 . 2 . . . . . . . . 4566 1 353 . 1 1 34 34 VAL HG21 H 1 1.09 0.022 . 2 . . . . . . . . 4566 1 354 . 1 1 34 34 VAL HG22 H 1 1.09 0.022 . 2 . . . . . . . . 4566 1 355 . 1 1 34 34 VAL HG23 H 1 1.09 0.022 . 2 . . . . . . . . 4566 1 356 . 1 1 34 34 VAL C C 13 180.87 0.03 . 1 . . . . . . . . 4566 1 357 . 1 1 34 34 VAL CA C 13 65.65 0.03 . 1 . . . . . . . . 4566 1 358 . 1 1 34 34 VAL CB C 13 31.9 0.03 . 1 . . . . . . . . 4566 1 359 . 1 1 34 34 VAL CG1 C 13 21.65 0.03 . 4 . . . . . . . . 4566 1 360 . 1 1 34 34 VAL CG2 C 13 20.59 0.03 . 4 . . . . . . . . 4566 1 361 . 1 1 34 34 VAL N N 15 118.33 0.04 . 1 . . . . . . . . 4566 1 362 . 1 1 35 35 GLN H H 1 9.14 0.022 . 1 . . . . . . . . 4566 1 363 . 1 1 35 35 GLN HA H 1 4.01 0.022 . 1 . . . . . . . . 4566 1 364 . 1 1 35 35 GLN HB2 H 1 2.01 0.022 . 2 . . . . . . . . 4566 1 365 . 1 1 35 35 GLN HG2 H 1 2.57 0.022 . 2 . . . . . . . . 4566 1 366 . 1 1 35 35 GLN HG3 H 1 2.46 0.022 . 2 . . . . . . . . 4566 1 367 . 1 1 35 35 GLN HE21 H 1 7.42 0.022 . 2 . . . . . . . . 4566 1 368 . 1 1 35 35 GLN HE22 H 1 6.97 0.022 . 2 . . . . . . . . 4566 1 369 . 1 1 35 35 GLN C C 13 177.33 0.03 . 1 . . . . . . . . 4566 1 370 . 1 1 35 35 GLN CA C 13 57.98 0.03 . 1 . . . . . . . . 4566 1 371 . 1 1 35 35 GLN CB C 13 27.36 0.03 . 1 . . . . . . . . 4566 1 372 . 1 1 35 35 GLN CG C 13 34.06 0.03 . 1 . . . . . . . . 4566 1 373 . 1 1 35 35 GLN N N 15 118.68 0.04 . 1 . . . . . . . . 4566 1 374 . 1 1 35 35 GLN NE2 N 15 110.82 0.04 . 1 . . . . . . . . 4566 1 375 . 1 1 36 36 ASN H H 1 7.17 0.022 . 1 . . . . . . . . 4566 1 376 . 1 1 36 36 ASN HA H 1 4.77 0.022 . 1 . . . . . . . . 4566 1 377 . 1 1 36 36 ASN HB2 H 1 2.7 0.022 . 2 . . . . . . . . 4566 1 378 . 1 1 36 36 ASN HB3 H 1 2.51 0.022 . 2 . . . . . . . . 4566 1 379 . 1 1 36 36 ASN HD21 H 1 7.63 0.022 . 2 . . . . . . . . 4566 1 380 . 1 1 36 36 ASN HD22 H 1 6.95 0.022 . 2 . . . . . . . . 4566 1 381 . 1 1 36 36 ASN C C 13 172.87 0.03 . 1 . . . . . . . . 4566 1 382 . 1 1 36 36 ASN CA C 13 52.8 0.03 . 1 . . . . . . . . 4566 1 383 . 1 1 36 36 ASN CB C 13 38.6 0.03 . 1 . . . . . . . . 4566 1 384 . 1 1 36 36 ASN N N 15 112.29 0.04 . 1 . . . . . . . . 4566 1 385 . 1 1 36 36 ASN ND2 N 15 113.05 0.04 . 1 . . . . . . . . 4566 1 386 . 1 1 37 37 ASN H H 1 7.83 0.022 . 1 . . . . . . . . 4566 1 387 . 1 1 37 37 ASN HA H 1 4.31 0.022 . 1 . . . . . . . . 4566 1 388 . 1 1 37 37 ASN HB2 H 1 2.93 0.022 . 2 . . . . . . . . 4566 1 389 . 1 1 37 37 ASN HB3 H 1 2.59 0.022 . 2 . . . . . . . . 4566 1 390 . 1 1 37 37 ASN HD21 H 1 7.51 0.022 . 2 . . . . . . . . 4566 1 391 . 1 1 37 37 ASN HD22 H 1 6.74 0.022 . 2 . . . . . . . . 4566 1 392 . 1 1 37 37 ASN C C 13 174.47 0.03 . 1 . . . . . . . . 4566 1 393 . 1 1 37 37 ASN CA C 13 53.57 0.03 . 1 . . . . . . . . 4566 1 394 . 1 1 37 37 ASN CB C 13 36.44 0.03 . 1 . . . . . . . . 4566 1 395 . 1 1 37 37 ASN N N 15 117.16 0.04 . 1 . . . . . . . . 4566 1 396 . 1 1 37 37 ASN ND2 N 15 112.24 0.04 . 1 . . . . . . . . 4566 1 397 . 1 1 38 38 LEU H H 1 7.78 0.022 . 1 . . . . . . . . 4566 1 398 . 1 1 38 38 LEU HA H 1 4.9 0.022 . 1 . . . . . . . . 4566 1 399 . 1 1 38 38 LEU HB2 H 1 1.29 0.022 . 2 . . . . . . . . 4566 1 400 . 1 1 38 38 LEU C C 13 177.67 0.03 . 1 . . . . . . . . 4566 1 401 . 1 1 38 38 LEU CA C 13 54.91 0.03 . 1 . . . . . . . . 4566 1 402 . 1 1 38 38 LEU CB C 13 41.19 0.03 . 1 . . . . . . . . 4566 1 403 . 1 1 38 38 LEU CG C 13 26.14 0.03 . 1 . . . . . . . . 4566 1 404 . 1 1 38 38 LEU CD1 C 13 25.08 0.03 . 2 . . . . . . . . 4566 1 405 . 1 1 38 38 LEU CD2 C 13 21.91 0.03 . 2 . . . . . . . . 4566 1 406 . 1 1 38 38 LEU N N 15 115.52 0.04 . 1 . . . . . . . . 4566 1 407 . 1 1 39 39 ASP H H 1 8.55 0.022 . 1 . . . . . . . . 4566 1 408 . 1 1 39 39 ASP HA H 1 4.46 0.022 . 1 . . . . . . . . 4566 1 409 . 1 1 39 39 ASP HB2 H 1 2.74 0.022 . 2 . . . . . . . . 4566 1 410 . 1 1 39 39 ASP HB3 H 1 2.43 0.022 . 2 . . . . . . . . 4566 1 411 . 1 1 39 39 ASP C C 13 174.47 0.03 . 1 . . . . . . . . 4566 1 412 . 1 1 39 39 ASP CA C 13 52.99 0.03 . 1 . . . . . . . . 4566 1 413 . 1 1 39 39 ASP CB C 13 38.6 0.03 . 1 . . . . . . . . 4566 1 414 . 1 1 39 39 ASP N N 15 122.84 0.04 . 1 . . . . . . . . 4566 1 415 . 1 1 40 40 ILE H H 1 7.59 0.022 . 1 . . . . . . . . 4566 1 416 . 1 1 40 40 ILE HA H 1 4.12 0.022 . 1 . . . . . . . . 4566 1 417 . 1 1 40 40 ILE HB H 1 1.29 0.022 . 1 . . . . . . . . 4566 1 418 . 1 1 40 40 ILE HG12 H 1 0.9 0.022 . 2 . . . . . . . . 4566 1 419 . 1 1 40 40 ILE HG21 H 1 0.63 0.022 . 1 . . . . . . . . 4566 1 420 . 1 1 40 40 ILE HG22 H 1 0.63 0.022 . 1 . . . . . . . . 4566 1 421 . 1 1 40 40 ILE HG23 H 1 0.63 0.022 . 1 . . . . . . . . 4566 1 422 . 1 1 40 40 ILE HD11 H 1 0.01 0.022 . 1 . . . . . . . . 4566 1 423 . 1 1 40 40 ILE HD12 H 1 0.01 0.022 . 1 . . . . . . . . 4566 1 424 . 1 1 40 40 ILE HD13 H 1 0.01 0.022 . 1 . . . . . . . . 4566 1 425 . 1 1 40 40 ILE C C 13 175.61 0.03 . 1 . . . . . . . . 4566 1 426 . 1 1 40 40 ILE CA C 13 59.52 0.03 . 1 . . . . . . . . 4566 1 427 . 1 1 40 40 ILE CB C 13 37.74 0.03 . 1 . . . . . . . . 4566 1 428 . 1 1 40 40 ILE CG1 C 13 25.34 0.03 . 1 . . . . . . . . 4566 1 429 . 1 1 40 40 ILE CG2 C 13 18.48 0.03 . 1 . . . . . . . . 4566 1 430 . 1 1 40 40 ILE CD1 C 13 12.66 0.03 . 1 . . . . . . . . 4566 1 431 . 1 1 40 40 ILE N N 15 123.78 0.04 . 1 . . . . . . . . 4566 1 432 . 1 1 41 41 ASP H H 1 8.53 0.022 . 1 . . . . . . . . 4566 1 433 . 1 1 41 41 ASP HA H 1 4.35 0.022 . 1 . . . . . . . . 4566 1 434 . 1 1 41 41 ASP HB2 H 1 2.64 0.022 . 2 . . . . . . . . 4566 1 435 . 1 1 41 41 ASP C C 13 177.9 0.03 . 1 . . . . . . . . 4566 1 436 . 1 1 41 41 ASP CA C 13 56.25 0.03 . 1 . . . . . . . . 4566 1 437 . 1 1 41 41 ASP CB C 13 40.76 0.03 . 1 . . . . . . . . 4566 1 438 . 1 1 41 41 ASP N N 15 127.77 0.04 . 1 . . . . . . . . 4566 1 439 . 1 1 42 42 GLY H H 1 8.99 0.022 . 1 . . . . . . . . 4566 1 440 . 1 1 42 42 GLY HA2 H 1 4.01 0.022 . 2 . . . . . . . . 4566 1 441 . 1 1 42 42 GLY HA3 H 1 3.73 0.022 . 2 . . . . . . . . 4566 1 442 . 1 1 42 42 GLY C C 13 173.78 0.03 . 1 . . . . . . . . 4566 1 443 . 1 1 42 42 GLY CA C 13 45.7 0.03 . 1 . . . . . . . . 4566 1 444 . 1 1 42 42 GLY N N 15 113.7 0.04 . 1 . . . . . . . . 4566 1 445 . 1 1 43 43 PHE H H 1 7.64 0.022 . 1 . . . . . . . . 4566 1 446 . 1 1 43 43 PHE HA H 1 4.06 0.022 . 1 . . . . . . . . 4566 1 447 . 1 1 43 43 PHE HB2 H 1 3.01 0.022 . 2 . . . . . . . . 4566 1 448 . 1 1 43 43 PHE HB3 H 1 2.01 0.022 . 2 . . . . . . . . 4566 1 449 . 1 1 43 43 PHE C C 13 178.01 0.03 . 1 . . . . . . . . 4566 1 450 . 1 1 43 43 PHE CA C 13 58.75 0.03 . 1 . . . . . . . . 4566 1 451 . 1 1 43 43 PHE CB C 13 40.33 0.03 . 1 . . . . . . . . 4566 1 452 . 1 1 57 57 LEU H H 1 9.39 0.022 . 1 . . . . . . . . 4566 1 453 . 1 1 57 57 LEU HA H 1 4.82 0.022 . 1 . . . . . . . . 4566 1 454 . 1 1 57 57 LEU HB2 H 1 1.66 0.022 . 2 . . . . . . . . 4566 1 455 . 1 1 57 57 LEU HG H 1 0.9 0.022 . 1 . . . . . . . . 4566 1 456 . 1 1 57 57 LEU C C 13 173.56 0.03 . 1 . . . . . . . . 4566 1 457 . 1 1 57 57 LEU CA C 13 53.18 0.03 . 1 . . . . . . . . 4566 1 458 . 1 1 57 57 LEU CB C 13 48.54 0.03 . 1 . . . . . . . . 4566 1 459 . 1 1 57 57 LEU CG C 13 27.98 0.03 . 1 . . . . . . . . 4566 1 460 . 1 1 57 57 LEU CD1 C 13 25.51 0.03 . 2 . . . . . . . . 4566 1 461 . 1 1 57 57 LEU CD2 C 13 23.49 0.03 . 2 . . . . . . . . 4566 1 462 . 1 1 57 57 LEU N N 15 128.35 0.04 . 1 . . . . . . . . 4566 1 463 . 1 1 58 58 ILE H H 1 8.46 0.022 . 1 . . . . . . . . 4566 1 464 . 1 1 58 58 ILE HA H 1 4.46 0.022 . 1 . . . . . . . . 4566 1 465 . 1 1 58 58 ILE HB H 1 1.4 0.022 . 1 . . . . . . . . 4566 1 466 . 1 1 58 58 ILE HG12 H 1 1.23 0.022 . 2 . . . . . . . . 4566 1 467 . 1 1 58 58 ILE HG13 H 1 0.99 0.022 . 2 . . . . . . . . 4566 1 468 . 1 1 58 58 ILE HG21 H 1 0.86 0.022 . 1 . . . . . . . . 4566 1 469 . 1 1 58 58 ILE HG22 H 1 0.86 0.022 . 1 . . . . . . . . 4566 1 470 . 1 1 58 58 ILE HG23 H 1 0.86 0.022 . 1 . . . . . . . . 4566 1 471 . 1 1 58 58 ILE HD11 H 1 0.61 0.022 . 1 . . . . . . . . 4566 1 472 . 1 1 58 58 ILE HD12 H 1 0.61 0.022 . 1 . . . . . . . . 4566 1 473 . 1 1 58 58 ILE HD13 H 1 0.61 0.022 . 1 . . . . . . . . 4566 1 474 . 1 1 58 58 ILE C C 13 176.75 0.03 . 1 . . . . . . . . 4566 1 475 . 1 1 58 58 ILE CA C 13 60.86 0.03 . 1 . . . . . . . . 4566 1 476 . 1 1 58 58 ILE CB C 13 39.46 0.03 . 1 . . . . . . . . 4566 1 477 . 1 1 58 58 ILE CG1 C 13 27.46 0.03 . 1 . . . . . . . . 4566 1 478 . 1 1 58 58 ILE CG2 C 13 17.15 0.03 . 1 . . . . . . . . 4566 1 479 . 1 1 58 58 ILE CD1 C 13 13.98 0.03 . 1 . . . . . . . . 4566 1 480 . 1 1 58 58 ILE N N 15 119.5 0.04 . 1 . . . . . . . . 4566 1 481 . 1 1 59 59 PHE H H 1 8.66 0.022 . 1 . . . . . . . . 4566 1 482 . 1 1 59 59 PHE HA H 1 4.51 0.022 . 1 . . . . . . . . 4566 1 483 . 1 1 59 59 PHE HB2 H 1 3.15 0.022 . 2 . . . . . . . . 4566 1 484 . 1 1 59 59 PHE HB3 H 1 3.12 0.022 . 2 . . . . . . . . 4566 1 485 . 1 1 59 59 PHE C C 13 175.5 0.03 . 1 . . . . . . . . 4566 1 486 . 1 1 59 59 PHE CA C 13 57.79 0.03 . 1 . . . . . . . . 4566 1 487 . 1 1 59 59 PHE CB C 13 42.06 0.03 . 1 . . . . . . . . 4566 1 488 . 1 1 59 59 PHE N N 15 127.88 0.04 . 1 . . . . . . . . 4566 1 489 . 1 1 60 60 GLU H H 1 9.18 0.022 . 1 . . . . . . . . 4566 1 490 . 1 1 60 60 GLU HA H 1 4.34 0.022 . 1 . . . . . . . . 4566 1 491 . 1 1 60 60 GLU HB2 H 1 2.05 0.022 . 2 . . . . . . . . 4566 1 492 . 1 1 60 60 GLU HB3 H 1 1.88 0.022 . 2 . . . . . . . . 4566 1 493 . 1 1 60 60 GLU HG2 H 1 2.23 0.022 . 2 . . . . . . . . 4566 1 494 . 1 1 60 60 GLU C C 13 178.78 0.03 . 1 . . . . . . . . 4566 1 495 . 1 1 60 60 GLU CA C 13 56.25 0.03 . 1 . . . . . . . . 4566 1 496 . 1 1 60 60 GLU CB C 13 31.04 0.03 . 1 . . . . . . . . 4566 1 497 . 1 1 60 60 GLU CG C 13 37.49 0.03 . 1 . . . . . . . . 4566 1 498 . 1 1 60 60 GLU N N 15 119.39 0.04 . 1 . . . . . . . . 4566 1 499 . 1 1 61 61 GLN H H 1 9.58 0.022 . 1 . . . . . . . . 4566 1 500 . 1 1 61 61 GLN HA H 1 3.74 0.022 . 1 . . . . . . . . 4566 1 501 . 1 1 61 61 GLN HB2 H 1 2.22 0.022 . 2 . . . . . . . . 4566 1 502 . 1 1 61 61 GLN HB3 H 1 2.12 0.022 . 2 . . . . . . . . 4566 1 503 . 1 1 61 61 GLN HG2 H 1 2.47 0.022 . 2 . . . . . . . . 4566 1 504 . 1 1 61 61 GLN HG3 H 1 2.33 0.022 . 2 . . . . . . . . 4566 1 505 . 1 1 61 61 GLN HE21 H 1 7.97 0.022 . 2 . . . . . . . . 4566 1 506 . 1 1 61 61 GLN HE22 H 1 6.95 0.022 . 2 . . . . . . . . 4566 1 507 . 1 1 61 61 GLN C C 13 176.39 0.03 . 1 . . . . . . . . 4566 1 508 . 1 1 61 61 GLN CA C 13 59.71 0.03 . 1 . . . . . . . . 4566 1 509 . 1 1 61 61 GLN CB C 13 28.44 0.03 . 1 . . . . . . . . 4566 1 510 . 1 1 61 61 GLN CG C 13 31.95 0.03 . 1 . . . . . . . . 4566 1 511 . 1 1 61 61 GLN N N 15 125.3 0.04 . 1 . . . . . . . . 4566 1 512 . 1 1 61 61 GLN NE2 N 15 112.44 0.04 . 1 . . . . . . . . 4566 1 513 . 1 1 62 62 HIS H H 1 8.42 0.022 . 1 . . . . . . . . 4566 1 514 . 1 1 62 62 HIS HA H 1 4.43 0.022 . 1 . . . . . . . . 4566 1 515 . 1 1 62 62 HIS HB2 H 1 3.19 0.022 . 2 . . . . . . . . 4566 1 516 . 1 1 62 62 HIS HB3 H 1 3.09 0.022 . 2 . . . . . . . . 4566 1 517 . 1 1 62 62 HIS C C 13 176.64 0.03 . 1 . . . . . . . . 4566 1 518 . 1 1 62 62 HIS CA C 13 58.36 0.03 . 1 . . . . . . . . 4566 1 519 . 1 1 62 62 HIS CB C 13 28.86 0.03 . 1 . . . . . . . . 4566 1 520 . 1 1 62 62 HIS N N 15 112.82 0.04 . 1 . . . . . . . . 4566 1 521 . 1 1 63 63 ILE H H 1 6.3 0.022 . 1 . . . . . . . . 4566 1 522 . 1 1 63 63 ILE HA H 1 3.81 0.022 . 1 . . . . . . . . 4566 1 523 . 1 1 63 63 ILE HB H 1 2.16 0.022 . 1 . . . . . . . . 4566 1 524 . 1 1 63 63 ILE HG12 H 1 1.38 0.022 . 2 . . . . . . . . 4566 1 525 . 1 1 63 63 ILE HG13 H 1 1.06 0.022 . 2 . . . . . . . . 4566 1 526 . 1 1 63 63 ILE HG21 H 1 0.97 0.022 . 1 . . . . . . . . 4566 1 527 . 1 1 63 63 ILE HG22 H 1 0.97 0.022 . 1 . . . . . . . . 4566 1 528 . 1 1 63 63 ILE HG23 H 1 0.97 0.022 . 1 . . . . . . . . 4566 1 529 . 1 1 63 63 ILE C C 13 177.44 0.03 . 1 . . . . . . . . 4566 1 530 . 1 1 63 63 ILE CA C 13 59.32 0.03 . 1 . . . . . . . . 4566 1 531 . 1 1 63 63 ILE CB C 13 35.57 0.03 . 1 . . . . . . . . 4566 1 532 . 1 1 63 63 ILE CG1 C 13 25.34 0.03 . 1 . . . . . . . . 4566 1 533 . 1 1 63 63 ILE CG2 C 13 17.15 0.03 . 1 . . . . . . . . 4566 1 534 . 1 1 63 63 ILE CD1 C 13 8.44 0.03 . 1 . . . . . . . . 4566 1 535 . 1 1 63 63 ILE N N 15 119.56 0.04 . 1 . . . . . . . . 4566 1 536 . 1 1 64 64 PHE H H 1 8.7 0.022 . 1 . . . . . . . . 4566 1 537 . 1 1 64 64 PHE HA H 1 3.51 0.022 . 1 . . . . . . . . 4566 1 538 . 1 1 64 64 PHE HB2 H 1 3.09 0.022 . 2 . . . . . . . . 4566 1 539 . 1 1 64 64 PHE HB3 H 1 2.86 0.022 . 2 . . . . . . . . 4566 1 540 . 1 1 64 64 PHE C C 13 177.21 0.03 . 1 . . . . . . . . 4566 1 541 . 1 1 64 64 PHE CA C 13 61.05 0.03 . 1 . . . . . . . . 4566 1 542 . 1 1 64 64 PHE CB C 13 39.68 0.03 . 1 . . . . . . . . 4566 1 543 . 1 1 64 64 PHE N N 15 120.26 0.04 . 1 . . . . . . . . 4566 1 544 . 1 1 65 65 GLU H H 1 7.97 0.022 . 1 . . . . . . . . 4566 1 545 . 1 1 65 65 GLU HA H 1 4.01 0.022 . 1 . . . . . . . . 4566 1 546 . 1 1 65 65 GLU HB2 H 1 2.05 0.022 . 2 . . . . . . . . 4566 1 547 . 1 1 65 65 GLU HG2 H 1 2.5 0.022 . 2 . . . . . . . . 4566 1 548 . 1 1 65 65 GLU C C 13 176.3 0.03 . 1 . . . . . . . . 4566 1 549 . 1 1 65 65 GLU CA C 13 57.4 0.03 . 1 . . . . . . . . 4566 1 550 . 1 1 65 65 GLU CB C 13 29.09 0.03 . 1 . . . . . . . . 4566 1 551 . 1 1 65 65 GLU CG C 13 35.38 0.03 . 1 . . . . . . . . 4566 1 552 . 1 1 65 65 GLU N N 15 113.23 0.04 . 1 . . . . . . . . 4566 1 553 . 1 1 66 66 LYS H H 1 7.43 0.022 . 1 . . . . . . . . 4566 1 554 . 1 1 66 66 LYS HA H 1 4.35 0.022 . 1 . . . . . . . . 4566 1 555 . 1 1 66 66 LYS HB2 H 1 1.98 0.022 . 2 . . . . . . . . 4566 1 556 . 1 1 66 66 LYS HB3 H 1 1.67 0.022 . 2 . . . . . . . . 4566 1 557 . 1 1 66 66 LYS HG2 H 1 1.6 0.022 . 2 . . . . . . . . 4566 1 558 . 1 1 66 66 LYS HG3 H 1 1.37 0.022 . 2 . . . . . . . . 4566 1 559 . 1 1 66 66 LYS HD2 H 1 1.66 0.022 . 2 . . . . . . . . 4566 1 560 . 1 1 66 66 LYS HE2 H 1 3.03 0.022 . 2 . . . . . . . . 4566 1 561 . 1 1 66 66 LYS C C 13 176.3 0.03 . 1 . . . . . . . . 4566 1 562 . 1 1 66 66 LYS CA C 13 54.34 0.03 . 1 . . . . . . . . 4566 1 563 . 1 1 66 66 LYS CB C 13 32.52 0.03 . 1 . . . . . . . . 4566 1 564 . 1 1 66 66 LYS CG C 13 24.29 0.03 . 1 . . . . . . . . 4566 1 565 . 1 1 66 66 LYS CD C 13 28.25 0.03 . 1 . . . . . . . . 4566 1 566 . 1 1 66 66 LYS CE C 13 41.72 0.03 . 1 . . . . . . . . 4566 1 567 . 1 1 66 66 LYS N N 15 116.92 0.04 . 1 . . . . . . . . 4566 1 568 . 1 1 67 67 LEU H H 1 6.76 0.022 . 1 . . . . . . . . 4566 1 569 . 1 1 67 67 LEU HA H 1 4.01 0.022 . 1 . . . . . . . . 4566 1 570 . 1 1 67 67 LEU HB2 H 1 1.21 0.022 . 2 . . . . . . . . 4566 1 571 . 1 1 67 67 LEU HG H 1 1.71 0.022 . 1 . . . . . . . . 4566 1 572 . 1 1 67 67 LEU HD11 H 1 0.42 0.022 . 1 . . . . . . . . 4566 1 573 . 1 1 67 67 LEU HD12 H 1 0.42 0.022 . 1 . . . . . . . . 4566 1 574 . 1 1 67 67 LEU HD13 H 1 0.42 0.022 . 1 . . . . . . . . 4566 1 575 . 1 1 67 67 LEU HD21 H 1 0.01 0.022 . 1 . . . . . . . . 4566 1 576 . 1 1 67 67 LEU HD22 H 1 0.01 0.022 . 1 . . . . . . . . 4566 1 577 . 1 1 67 67 LEU HD23 H 1 0.01 0.022 . 1 . . . . . . . . 4566 1 578 . 1 1 67 67 LEU C C 13 177.1 0.03 . 1 . . . . . . . . 4566 1 579 . 1 1 67 67 LEU CA C 13 53.95 0.03 . 1 . . . . . . . . 4566 1 580 . 1 1 67 67 LEU CB C 13 40.55 0.03 . 1 . . . . . . . . 4566 1 581 . 1 1 67 67 LEU CG C 13 24.55 0.03 . 1 . . . . . . . . 4566 1 582 . 1 1 67 67 LEU CD1 C 13 24.99 0.03 . 2 . . . . . . . . 4566 1 583 . 1 1 67 67 LEU CD2 C 13 21.38 0.03 . 2 . . . . . . . . 4566 1 584 . 1 1 67 67 LEU N N 15 119.27 0.04 . 1 . . . . . . . . 4566 1 585 . 1 1 68 68 GLU H H 1 9.05 0.022 . 1 . . . . . . . . 4566 1 586 . 1 1 68 68 GLU HA H 1 3.89 0.022 . 1 . . . . . . . . 4566 1 587 . 1 1 68 68 GLU HB2 H 1 1.96 0.022 . 2 . . . . . . . . 4566 1 588 . 1 1 68 68 GLU HB3 H 1 1.84 0.022 . 2 . . . . . . . . 4566 1 589 . 1 1 68 68 GLU HG2 H 1 2.34 0.022 . 2 . . . . . . . . 4566 1 590 . 1 1 68 68 GLU HG3 H 1 2.26 0.022 . 2 . . . . . . . . 4566 1 591 . 1 1 68 68 GLU C C 13 175.73 0.03 . 1 . . . . . . . . 4566 1 592 . 1 1 68 68 GLU CA C 13 56.25 0.03 . 1 . . . . . . . . 4566 1 593 . 1 1 68 68 GLU CB C 13 29.09 0.03 . 1 . . . . . . . . 4566 1 594 . 1 1 68 68 GLU CG C 13 36.17 0.03 . 1 . . . . . . . . 4566 1 595 . 1 1 68 68 GLU N N 15 121.96 0.04 . 1 . . . . . . . . 4566 1 596 . 1 1 69 69 ALA H H 1 8.21 0.022 . 1 . . . . . . . . 4566 1 597 . 1 1 69 69 ALA HA H 1 3.89 0.022 . 1 . . . . . . . . 4566 1 598 . 1 1 69 69 ALA HB1 H 1 1.25 0.022 . 1 . . . . . . . . 4566 1 599 . 1 1 69 69 ALA HB2 H 1 1.25 0.022 . 1 . . . . . . . . 4566 1 600 . 1 1 69 69 ALA HB3 H 1 1.25 0.022 . 1 . . . . . . . . 4566 1 601 . 1 1 69 69 ALA C C 13 178.13 0.03 . 1 . . . . . . . . 4566 1 602 . 1 1 69 69 ALA CA C 13 52.23 0.03 . 1 . . . . . . . . 4566 1 603 . 1 1 69 69 ALA CB C 13 18.06 0.03 . 1 . . . . . . . . 4566 1 604 . 1 1 69 69 ALA N N 15 123.9 0.04 . 1 . . . . . . . . 4566 1 605 . 1 1 70 70 ILE H H 1 8.37 0.022 . 1 . . . . . . . . 4566 1 606 . 1 1 70 70 ILE HA H 1 3.91 0.022 . 1 . . . . . . . . 4566 1 607 . 1 1 70 70 ILE HB H 1 1.44 0.022 . 1 . . . . . . . . 4566 1 608 . 1 1 70 70 ILE HG12 H 1 1.29 0.022 . 2 . . . . . . . . 4566 1 609 . 1 1 70 70 ILE HG21 H 1 0.86 0.022 . 1 . . . . . . . . 4566 1 610 . 1 1 70 70 ILE HG22 H 1 0.86 0.022 . 1 . . . . . . . . 4566 1 611 . 1 1 70 70 ILE HG23 H 1 0.86 0.022 . 1 . . . . . . . . 4566 1 612 . 1 1 70 70 ILE C C 13 175.84 0.03 . 1 . . . . . . . . 4566 1 613 . 1 1 70 70 ILE CA C 13 62.39 0.03 . 1 . . . . . . . . 4566 1 614 . 1 1 70 70 ILE CB C 13 38.6 0.03 . 1 . . . . . . . . 4566 1 615 . 1 1 70 70 ILE CG1 C 13 28.51 0.03 . 1 . . . . . . . . 4566 1 616 . 1 1 70 70 ILE CG2 C 13 15.83 0.03 . 1 . . . . . . . . 4566 1 617 . 1 1 70 70 ILE CD1 C 13 14.25 0.03 . 1 . . . . . . . . 4566 1 618 . 1 1 70 70 ILE N N 15 124.43 0.04 . 1 . . . . . . . . 4566 1 619 . 1 1 71 71 THR H H 1 7.91 0.022 . 1 . . . . . . . . 4566 1 620 . 1 1 71 71 THR HA H 1 4.46 0.022 . 1 . . . . . . . . 4566 1 621 . 1 1 71 71 THR HB H 1 4.62 0.022 . 1 . . . . . . . . 4566 1 622 . 1 1 71 71 THR HG21 H 1 1.18 0.022 . 1 . . . . . . . . 4566 1 623 . 1 1 71 71 THR HG22 H 1 1.18 0.022 . 1 . . . . . . . . 4566 1 624 . 1 1 71 71 THR HG23 H 1 1.18 0.022 . 1 . . . . . . . . 4566 1 625 . 1 1 71 71 THR C C 13 175.5 0.03 . 1 . . . . . . . . 4566 1 626 . 1 1 71 71 THR CA C 13 60.28 0.03 . 1 . . . . . . . . 4566 1 627 . 1 1 71 71 THR CB C 13 71.45 0.03 . 1 . . . . . . . . 4566 1 628 . 1 1 71 71 THR CG2 C 13 21.12 0.03 . 1 . . . . . . . . 4566 1 629 . 1 1 71 71 THR N N 15 118.27 0.04 . 1 . . . . . . . . 4566 1 630 . 1 1 72 72 ASP H H 1 8.96 0.022 . 1 . . . . . . . . 4566 1 631 . 1 1 72 72 ASP HA H 1 4.24 0.022 . 1 . . . . . . . . 4566 1 632 . 1 1 72 72 ASP HB2 H 1 2.74 0.022 . 2 . . . . . . . . 4566 1 633 . 1 1 72 72 ASP HB3 H 1 2.7 0.022 . 2 . . . . . . . . 4566 1 634 . 1 1 72 72 ASP C C 13 177.55 0.03 . 1 . . . . . . . . 4566 1 635 . 1 1 72 72 ASP CA C 13 57.21 0.03 . 1 . . . . . . . . 4566 1 636 . 1 1 72 72 ASP CB C 13 39.25 0.03 . 1 . . . . . . . . 4566 1 637 . 1 1 72 72 ASP N N 15 122.49 0.04 . 1 . . . . . . . . 4566 1 638 . 1 1 73 73 GLU H H 1 8.95 0.022 . 1 . . . . . . . . 4566 1 639 . 1 1 73 73 GLU HA H 1 3.97 0.022 . 1 . . . . . . . . 4566 1 640 . 1 1 73 73 GLU HB2 H 1 1.94 0.022 . 2 . . . . . . . . 4566 1 641 . 1 1 73 73 GLU HG2 H 1 2.47 0.022 . 2 . . . . . . . . 4566 1 642 . 1 1 73 73 GLU HG3 H 1 2.28 0.022 . 2 . . . . . . . . 4566 1 643 . 1 1 73 73 GLU C C 13 179.04 0.03 . 1 . . . . . . . . 4566 1 644 . 1 1 73 73 GLU CA C 13 60.09 0.03 . 1 . . . . . . . . 4566 1 645 . 1 1 73 73 GLU CB C 13 28.44 0.03 . 1 . . . . . . . . 4566 1 646 . 1 1 73 73 GLU CG C 13 36.97 0.03 . 1 . . . . . . . . 4566 1 647 . 1 1 73 73 GLU N N 15 117.39 0.04 . 1 . . . . . . . . 4566 1 648 . 1 1 74 74 GLU H H 1 7.52 0.022 . 1 . . . . . . . . 4566 1 649 . 1 1 74 74 GLU HA H 1 3.89 0.022 . 1 . . . . . . . . 4566 1 650 . 1 1 74 74 GLU HB2 H 1 2.01 0.022 . 2 . . . . . . . . 4566 1 651 . 1 1 74 74 GLU HG2 H 1 2.96 0.022 . 2 . . . . . . . . 4566 1 652 . 1 1 74 74 GLU C C 13 177.76 0.03 . 1 . . . . . . . . 4566 1 653 . 1 1 74 74 GLU CA C 13 58.75 0.03 . 1 . . . . . . . . 4566 1 654 . 1 1 74 74 GLU CB C 13 28.23 0.03 . 1 . . . . . . . . 4566 1 655 . 1 1 74 74 GLU CG C 13 35.64 0.03 . 1 . . . . . . . . 4566 1 656 . 1 1 74 74 GLU N N 15 119.5 0.04 . 1 . . . . . . . . 4566 1 657 . 1 1 75 75 ASN H H 1 8.56 0.022 . 1 . . . . . . . . 4566 1 658 . 1 1 75 75 ASN HA H 1 4.3 0.022 . 1 . . . . . . . . 4566 1 659 . 1 1 75 75 ASN HB2 H 1 2.93 0.022 . 2 . . . . . . . . 4566 1 660 . 1 1 75 75 ASN HB3 H 1 2.63 0.022 . 2 . . . . . . . . 4566 1 661 . 1 1 75 75 ASN HD21 H 1 7.63 0.022 . 2 . . . . . . . . 4566 1 662 . 1 1 75 75 ASN HD22 H 1 6.72 0.022 . 2 . . . . . . . . 4566 1 663 . 1 1 75 75 ASN C C 13 176.87 0.03 . 1 . . . . . . . . 4566 1 664 . 1 1 75 75 ASN CA C 13 56.64 0.03 . 1 . . . . . . . . 4566 1 665 . 1 1 75 75 ASN CB C 13 38.38 0.03 . 1 . . . . . . . . 4566 1 666 . 1 1 75 75 ASN N N 15 119.56 0.04 . 1 . . . . . . . . 4566 1 667 . 1 1 75 75 ASN ND2 N 15 113.46 0.04 . 1 . . . . . . . . 4566 1 668 . 1 1 76 76 ASP H H 1 8.32 0.022 . 1 . . . . . . . . 4566 1 669 . 1 1 76 76 ASP HA H 1 4.23 0.022 . 1 . . . . . . . . 4566 1 670 . 1 1 76 76 ASP HB2 H 1 2.67 0.022 . 2 . . . . . . . . 4566 1 671 . 1 1 76 76 ASP HB3 H 1 2.51 0.022 . 2 . . . . . . . . 4566 1 672 . 1 1 76 76 ASP C C 13 178.35 0.03 . 1 . . . . . . . . 4566 1 673 . 1 1 76 76 ASP CA C 13 56.64 0.03 . 1 . . . . . . . . 4566 1 674 . 1 1 76 76 ASP CB C 13 39.8 0.03 . 1 . . . . . . . . 4566 1 675 . 1 1 76 76 ASP N N 15 117.33 0.04 . 1 . . . . . . . . 4566 1 676 . 1 1 77 77 MET H H 1 7.06 0.022 . 1 . . . . . . . . 4566 1 677 . 1 1 77 77 MET HA H 1 4.5 0.022 . 1 . . . . . . . . 4566 1 678 . 1 1 77 77 MET C C 13 179.61 0.03 . 1 . . . . . . . . 4566 1 679 . 1 1 77 77 MET CA C 13 55.1 0.03 . 1 . . . . . . . . 4566 1 680 . 1 1 77 77 MET CB C 13 33.2 0.03 . 1 . . . . . . . . 4566 1 681 . 1 1 77 77 MET CG C 13 32.49 0.03 . 1 . . . . . . . . 4566 1 682 . 1 1 77 77 MET CE C 13 19.63 0.03 . 1 . . . . . . . . 4566 1 683 . 1 1 77 77 MET N N 15 116.1 0.04 . 1 . . . . . . . . 4566 1 684 . 1 1 78 78 LEU H H 1 8.79 0.022 . 1 . . . . . . . . 4566 1 685 . 1 1 78 78 LEU HA H 1 3.78 0.022 . 1 . . . . . . . . 4566 1 686 . 1 1 78 78 LEU HB2 H 1 1.75 0.022 . 2 . . . . . . . . 4566 1 687 . 1 1 78 78 LEU HG H 1 1.61 0.022 . 1 . . . . . . . . 4566 1 688 . 1 1 78 78 LEU HD11 H 1 0.76 0.022 . 2 . . . . . . . . 4566 1 689 . 1 1 78 78 LEU HD12 H 1 0.76 0.022 . 2 . . . . . . . . 4566 1 690 . 1 1 78 78 LEU HD13 H 1 0.76 0.022 . 2 . . . . . . . . 4566 1 691 . 1 1 78 78 LEU HD21 H 1 0.52 0.022 . 2 . . . . . . . . 4566 1 692 . 1 1 78 78 LEU HD22 H 1 0.52 0.022 . 2 . . . . . . . . 4566 1 693 . 1 1 78 78 LEU HD23 H 1 0.52 0.022 . 2 . . . . . . . . 4566 1 694 . 1 1 78 78 LEU C C 13 178.13 0.03 . 1 . . . . . . . . 4566 1 695 . 1 1 78 78 LEU CA C 13 57.21 0.03 . 1 . . . . . . . . 4566 1 696 . 1 1 78 78 LEU CB C 13 40.92 0.03 . 1 . . . . . . . . 4566 1 697 . 1 1 78 78 LEU CG C 13 26.14 0.03 . 1 . . . . . . . . 4566 1 698 . 1 1 78 78 LEU CD1 C 13 24.55 0.03 . 2 . . . . . . . . 4566 1 699 . 1 1 78 78 LEU CD2 C 13 22.97 0.03 . 2 . . . . . . . . 4566 1 700 . 1 1 78 78 LEU N N 15 123.55 0.04 . 1 . . . . . . . . 4566 1 701 . 1 1 79 79 ASP H H 1 7.85 0.022 . 1 . . . . . . . . 4566 1 702 . 1 1 79 79 ASP HA H 1 4.38 0.022 . 1 . . . . . . . . 4566 1 703 . 1 1 79 79 ASP HB2 H 1 2.67 0.022 . 2 . . . . . . . . 4566 1 704 . 1 1 79 79 ASP HB3 H 1 2.44 0.022 . 2 . . . . . . . . 4566 1 705 . 1 1 79 79 ASP C C 13 177.21 0.03 . 1 . . . . . . . . 4566 1 706 . 1 1 79 79 ASP CA C 13 56.25 0.03 . 1 . . . . . . . . 4566 1 707 . 1 1 79 79 ASP CB C 13 40.55 0.03 . 1 . . . . . . . . 4566 1 708 . 1 1 79 79 ASP N N 15 115.87 0.04 . 1 . . . . . . . . 4566 1 709 . 1 1 80 80 LEU H H 1 7.1 0.022 . 1 . . . . . . . . 4566 1 710 . 1 1 80 80 LEU HA H 1 4.33 0.022 . 1 . . . . . . . . 4566 1 711 . 1 1 80 80 LEU HB2 H 1 1.76 0.022 . 2 . . . . . . . . 4566 1 712 . 1 1 80 80 LEU HB3 H 1 1.63 0.022 . 2 . . . . . . . . 4566 1 713 . 1 1 80 80 LEU HG H 1 1.38 0.022 . 1 . . . . . . . . 4566 1 714 . 1 1 80 80 LEU HD11 H 1 0.85 0.022 . 2 . . . . . . . . 4566 1 715 . 1 1 80 80 LEU HD12 H 1 0.85 0.022 . 2 . . . . . . . . 4566 1 716 . 1 1 80 80 LEU HD13 H 1 0.85 0.022 . 2 . . . . . . . . 4566 1 717 . 1 1 80 80 LEU HD21 H 1 0.47 0.022 . 2 . . . . . . . . 4566 1 718 . 1 1 80 80 LEU HD22 H 1 0.47 0.022 . 2 . . . . . . . . 4566 1 719 . 1 1 80 80 LEU HD23 H 1 0.47 0.022 . 2 . . . . . . . . 4566 1 720 . 1 1 80 80 LEU C C 13 177.1 0.03 . 1 . . . . . . . . 4566 1 721 . 1 1 80 80 LEU CA C 13 53.38 0.03 . 1 . . . . . . . . 4566 1 722 . 1 1 80 80 LEU CB C 13 41.41 0.03 . 1 . . . . . . . . 4566 1 723 . 1 1 80 80 LEU CG C 13 26.14 0.03 . 1 . . . . . . . . 4566 1 724 . 1 1 80 80 LEU CD1 C 13 25.08 0.03 . 2 . . . . . . . . 4566 1 725 . 1 1 80 80 LEU CD2 C 13 21.91 0.03 . 2 . . . . . . . . 4566 1 726 . 1 1 80 80 LEU N N 15 116.63 0.04 . 1 . . . . . . . . 4566 1 727 . 1 1 81 81 ALA H H 1 7.85 0.022 . 1 . . . . . . . . 4566 1 728 . 1 1 81 81 ALA HA H 1 4.16 0.022 . 1 . . . . . . . . 4566 1 729 . 1 1 81 81 ALA HB1 H 1 1.21 0.022 . 1 . . . . . . . . 4566 1 730 . 1 1 81 81 ALA HB2 H 1 1.21 0.022 . 1 . . . . . . . . 4566 1 731 . 1 1 81 81 ALA HB3 H 1 1.21 0.022 . 1 . . . . . . . . 4566 1 732 . 1 1 81 81 ALA C C 13 176.66 0.03 . 1 . . . . . . . . 4566 1 733 . 1 1 81 81 ALA CA C 13 51.84 0.03 . 1 . . . . . . . . 4566 1 734 . 1 1 81 81 ALA CB C 13 18.75 0.03 . 1 . . . . . . . . 4566 1 735 . 1 1 81 81 ALA N N 15 124.02 0.04 . 1 . . . . . . . . 4566 1 736 . 1 1 82 82 TYR H H 1 8.25 0.022 . 1 . . . . . . . . 4566 1 737 . 1 1 82 82 TYR HA H 1 4.43 0.022 . 1 . . . . . . . . 4566 1 738 . 1 1 82 82 TYR HB2 H 1 2.97 0.022 . 2 . . . . . . . . 4566 1 739 . 1 1 82 82 TYR HB3 H 1 2.82 0.022 . 2 . . . . . . . . 4566 1 740 . 1 1 82 82 TYR C C 13 176.56 0.03 . 1 . . . . . . . . 4566 1 741 . 1 1 82 82 TYR CA C 13 57.4 0.03 . 1 . . . . . . . . 4566 1 742 . 1 1 82 82 TYR CB C 13 38.47 0.03 . 1 . . . . . . . . 4566 1 743 . 1 1 82 82 TYR N N 15 122.43 0.04 . 1 . . . . . . . . 4566 1 744 . 1 1 83 83 GLY H H 1 8.34 0.022 . 1 . . . . . . . . 4566 1 745 . 1 1 83 83 GLY HA2 H 1 4.05 0.022 . 2 . . . . . . . . 4566 1 746 . 1 1 83 83 GLY HA3 H 1 3.58 0.022 . 2 . . . . . . . . 4566 1 747 . 1 1 83 83 GLY C C 13 174.56 0.03 . 1 . . . . . . . . 4566 1 748 . 1 1 83 83 GLY CA C 13 45.89 0.03 . 1 . . . . . . . . 4566 1 749 . 1 1 83 83 GLY N N 15 112.65 0.04 . 1 . . . . . . . . 4566 1 750 . 1 1 84 84 LEU H H 1 7.32 0.022 . 1 . . . . . . . . 4566 1 751 . 1 1 84 84 LEU HA H 1 3.81 0.022 . 1 . . . . . . . . 4566 1 752 . 1 1 84 84 LEU HB2 H 1 1.52 0.022 . 2 . . . . . . . . 4566 1 753 . 1 1 84 84 LEU HG H 1 1.52 0.022 . 1 . . . . . . . . 4566 1 754 . 1 1 84 84 LEU HD11 H 1 0.8 0.022 . 2 . . . . . . . . 4566 1 755 . 1 1 84 84 LEU HD12 H 1 0.8 0.022 . 2 . . . . . . . . 4566 1 756 . 1 1 84 84 LEU HD13 H 1 0.8 0.022 . 2 . . . . . . . . 4566 1 757 . 1 1 84 84 LEU C C 13 176.41 0.03 . 1 . . . . . . . . 4566 1 758 . 1 1 84 84 LEU CA C 13 56.31 0.03 . 1 . . . . . . . . 4566 1 759 . 1 1 84 84 LEU CB C 13 42.06 0.03 . 1 . . . . . . . . 4566 1 760 . 1 1 84 84 LEU CG C 13 25.87 0.03 . 1 . . . . . . . . 4566 1 761 . 1 1 84 84 LEU CD1 C 13 24.02 0.03 . 2 . . . . . . . . 4566 1 762 . 1 1 84 84 LEU CD2 C 13 23.49 0.03 . 2 . . . . . . . . 4566 1 763 . 1 1 84 84 LEU N N 15 118.51 0.04 . 1 . . . . . . . . 4566 1 764 . 1 1 85 85 THR H H 1 8.77 0.022 . 1 . . . . . . . . 4566 1 765 . 1 1 85 85 THR HA H 1 4.3 0.022 . 1 . . . . . . . . 4566 1 766 . 1 1 85 85 THR HB H 1 4.85 0.022 . 1 . . . . . . . . 4566 1 767 . 1 1 85 85 THR HG21 H 1 1.18 0.022 . 1 . . . . . . . . 4566 1 768 . 1 1 85 85 THR HG22 H 1 1.18 0.022 . 1 . . . . . . . . 4566 1 769 . 1 1 85 85 THR HG23 H 1 1.18 0.022 . 1 . . . . . . . . 4566 1 770 . 1 1 85 85 THR C C 13 174.47 0.03 . 1 . . . . . . . . 4566 1 771 . 1 1 85 85 THR CA C 13 59.52 0.03 . 1 . . . . . . . . 4566 1 772 . 1 1 85 85 THR CB C 13 73.1 0.03 . 1 . . . . . . . . 4566 1 773 . 1 1 85 85 THR CG2 C 13 21.38 0.03 . 1 . . . . . . . . 4566 1 774 . 1 1 85 85 THR N N 15 116.69 0.04 . 1 . . . . . . . . 4566 1 775 . 1 1 86 86 ASP H H 1 8.56 0.022 . 1 . . . . . . . . 4566 1 776 . 1 1 86 86 ASP HA H 1 4.39 0.022 . 1 . . . . . . . . 4566 1 777 . 1 1 86 86 ASP HB2 H 1 2.67 0.022 . 2 . . . . . . . . 4566 1 778 . 1 1 86 86 ASP HB3 H 1 2.63 0.022 . 2 . . . . . . . . 4566 1 779 . 1 1 86 86 ASP C C 13 175.61 0.03 . 1 . . . . . . . . 4566 1 780 . 1 1 86 86 ASP CA C 13 54.14 0.03 . 1 . . . . . . . . 4566 1 781 . 1 1 86 86 ASP CB C 13 38.91 0.03 . 1 . . . . . . . . 4566 1 782 . 1 1 86 86 ASP N N 15 117.74 0.04 . 1 . . . . . . . . 4566 1 783 . 1 1 87 87 ARG H H 1 8.07 0.022 . 1 . . . . . . . . 4566 1 784 . 1 1 87 87 ARG HA H 1 2.87 0.022 . 1 . . . . . . . . 4566 1 785 . 1 1 87 87 ARG HB2 H 1 2.05 0.022 . 2 . . . . . . . . 4566 1 786 . 1 1 87 87 ARG HB3 H 1 1.95 0.022 . 2 . . . . . . . . 4566 1 787 . 1 1 87 87 ARG HG2 H 1 1.18 0.022 . 2 . . . . . . . . 4566 1 788 . 1 1 87 87 ARG HG3 H 1 0.8 0.022 . 2 . . . . . . . . 4566 1 789 . 1 1 87 87 ARG HD2 H 1 3.14 0.022 . 2 . . . . . . . . 4566 1 790 . 1 1 87 87 ARG HD3 H 1 3.04 0.022 . 2 . . . . . . . . 4566 1 791 . 1 1 87 87 ARG C C 13 175 0.03 . 1 . . . . . . . . 4566 1 792 . 1 1 87 87 ARG CA C 13 54.3 0.03 . 1 . . . . . . . . 4566 1 793 . 1 1 87 87 ARG CB C 13 29.64 0.03 . 1 . . . . . . . . 4566 1 794 . 1 1 87 87 ARG CG C 13 27.19 0.03 . 1 . . . . . . . . 4566 1 795 . 1 1 87 87 ARG CD C 13 42.78 0.03 . 1 . . . . . . . . 4566 1 796 . 1 1 87 87 ARG N N 15 119.57 0.04 . 1 . . . . . . . . 4566 1 797 . 1 1 88 88 SER H H 1 6.88 0.022 . 1 . . . . . . . . 4566 1 798 . 1 1 88 88 SER HA H 1 5.38 0.022 . 1 . . . . . . . . 4566 1 799 . 1 1 88 88 SER HB2 H 1 3.85 0.022 . 2 . . . . . . . . 4566 1 800 . 1 1 88 88 SER HB3 H 1 3.78 0.022 . 2 . . . . . . . . 4566 1 801 . 1 1 88 88 SER C C 13 174.01 0.03 . 1 . . . . . . . . 4566 1 802 . 1 1 88 88 SER CA C 13 60.28 0.03 . 1 . . . . . . . . 4566 1 803 . 1 1 88 88 SER CB C 13 64.32 0.03 . 1 . . . . . . . . 4566 1 804 . 1 1 88 88 SER N N 15 119.56 0.04 . 1 . . . . . . . . 4566 1 805 . 1 1 89 89 ARG H H 1 9.17 0.022 . 1 . . . . . . . . 4566 1 806 . 1 1 89 89 ARG HA H 1 4.84 0.022 . 1 . . . . . . . . 4566 1 807 . 1 1 89 89 ARG HB2 H 1 2.02 0.022 . 2 . . . . . . . . 4566 1 808 . 1 1 89 89 ARG HB3 H 1 1.68 0.022 . 2 . . . . . . . . 4566 1 809 . 1 1 89 89 ARG C C 13 175.5 0.03 . 1 . . . . . . . . 4566 1 810 . 1 1 89 89 ARG CA C 13 52.23 0.03 . 1 . . . . . . . . 4566 1 811 . 1 1 89 89 ARG CB C 13 33.63 0.03 . 1 . . . . . . . . 4566 1 812 . 1 1 89 89 ARG N N 15 117.28 0.04 . 1 . . . . . . . . 4566 1 813 . 1 1 94 94 ILE C C 13 176.41 0.03 . 1 . . . . . . . . 4566 1 814 . 1 1 94 94 ILE CA C 13 57.19 0.03 . 1 . . . . . . . . 4566 1 815 . 1 1 94 94 ILE CB C 13 36.01 0.03 . 1 . . . . . . . . 4566 1 816 . 1 1 94 94 ILE CG1 C 13 25.08 0.03 . 1 . . . . . . . . 4566 1 817 . 1 1 94 94 ILE CG2 C 13 17.42 0.03 . 1 . . . . . . . . 4566 1 818 . 1 1 94 94 ILE CD1 C 13 8.44 0.03 . 1 . . . . . . . . 4566 1 819 . 1 1 95 95 CYS H H 1 7.97 0.022 . 1 . . . . . . . . 4566 1 820 . 1 1 95 95 CYS HA H 1 4.61 0.022 . 1 . . . . . . . . 4566 1 821 . 1 1 95 95 CYS HB2 H 1 1.98 0.022 . 2 . . . . . . . . 4566 1 822 . 1 1 95 95 CYS HB3 H 1 1.06 0.022 . 2 . . . . . . . . 4566 1 823 . 1 1 95 95 CYS C C 13 174.65 0.03 . 1 . . . . . . . . 4566 1 824 . 1 1 95 95 CYS CA C 13 52.99 0.03 . 1 . . . . . . . . 4566 1 825 . 1 1 95 95 CYS CB C 13 40.14 0.03 . 1 . . . . . . . . 4566 1 826 . 1 1 95 95 CYS N N 15 124.54 0.04 . 1 . . . . . . . . 4566 1 827 . 1 1 96 96 LEU H H 1 9.03 0.022 . 1 . . . . . . . . 4566 1 828 . 1 1 96 96 LEU HA H 1 4.62 0.022 . 1 . . . . . . . . 4566 1 829 . 1 1 96 96 LEU HB2 H 1 1.98 0.022 . 2 . . . . . . . . 4566 1 830 . 1 1 96 96 LEU HB3 H 1 1.06 0.022 . 2 . . . . . . . . 4566 1 831 . 1 1 96 96 LEU HG H 1 1.77 0.022 . 1 . . . . . . . . 4566 1 832 . 1 1 96 96 LEU HD11 H 1 0.72 0.022 . 2 . . . . . . . . 4566 1 833 . 1 1 96 96 LEU HD12 H 1 0.72 0.022 . 2 . . . . . . . . 4566 1 834 . 1 1 96 96 LEU HD13 H 1 0.72 0.022 . 2 . . . . . . . . 4566 1 835 . 1 1 96 96 LEU HD21 H 1 0.66 0.022 . 2 . . . . . . . . 4566 1 836 . 1 1 96 96 LEU HD22 H 1 0.66 0.022 . 2 . . . . . . . . 4566 1 837 . 1 1 96 96 LEU HD23 H 1 0.66 0.022 . 2 . . . . . . . . 4566 1 838 . 1 1 96 96 LEU C C 13 178.3 0.03 . 1 . . . . . . . . 4566 1 839 . 1 1 96 96 LEU CA C 13 55.49 0.03 . 1 . . . . . . . . 4566 1 840 . 1 1 96 96 LEU CB C 13 41.57 0.03 . 1 . . . . . . . . 4566 1 841 . 1 1 96 96 LEU CG C 13 26.4 0.03 . 1 . . . . . . . . 4566 1 842 . 1 1 96 96 LEU CD1 C 13 24.29 0.03 . 2 . . . . . . . . 4566 1 843 . 1 1 96 96 LEU N N 15 121.55 0.04 . 1 . . . . . . . . 4566 1 844 . 1 1 97 97 THR H H 1 7.72 0.022 . 1 . . . . . . . . 4566 1 845 . 1 1 97 97 THR HA H 1 4.65 0.022 . 1 . . . . . . . . 4566 1 846 . 1 1 97 97 THR HB H 1 4.54 0.022 . 1 . . . . . . . . 4566 1 847 . 1 1 97 97 THR HG21 H 1 1.16 0.022 . 1 . . . . . . . . 4566 1 848 . 1 1 97 97 THR HG22 H 1 1.16 0.022 . 1 . . . . . . . . 4566 1 849 . 1 1 97 97 THR HG23 H 1 1.16 0.022 . 1 . . . . . . . . 4566 1 850 . 1 1 97 97 THR C C 13 174.81 0.03 . 1 . . . . . . . . 4566 1 851 . 1 1 97 97 THR CA C 13 58.56 0.03 . 1 . . . . . . . . 4566 1 852 . 1 1 97 97 THR CB C 13 71.02 0.03 . 1 . . . . . . . . 4566 1 853 . 1 1 97 97 THR CG2 C 13 21.12 0.03 . 1 . . . . . . . . 4566 1 854 . 1 1 97 97 THR N N 15 113.47 0.04 . 1 . . . . . . . . 4566 1 855 . 1 1 98 98 LYS H H 1 9.04 0.022 . 1 . . . . . . . . 4566 1 856 . 1 1 98 98 LYS HA H 1 3.81 0.022 . 1 . . . . . . . . 4566 1 857 . 1 1 98 98 LYS HB2 H 1 1.88 0.022 . 2 . . . . . . . . 4566 1 858 . 1 1 98 98 LYS HG2 H 1 1.47 0.022 . 2 . . . . . . . . 4566 1 859 . 1 1 98 98 LYS HG3 H 1 1.37 0.022 . 2 . . . . . . . . 4566 1 860 . 1 1 98 98 LYS HD2 H 1 1.64 0.022 . 2 . . . . . . . . 4566 1 861 . 1 1 98 98 LYS HE2 H 1 2.95 0.022 . 2 . . . . . . . . 4566 1 862 . 1 1 98 98 LYS C C 13 178.13 0.03 . 1 . . . . . . . . 4566 1 863 . 1 1 98 98 LYS CA C 13 58.88 0.03 . 1 . . . . . . . . 4566 1 864 . 1 1 98 98 LYS CB C 13 31.25 0.03 . 1 . . . . . . . . 4566 1 865 . 1 1 98 98 LYS CG C 13 24.55 0.03 . 1 . . . . . . . . 4566 1 866 . 1 1 98 98 LYS CD C 13 28.51 0.03 . 1 . . . . . . . . 4566 1 867 . 1 1 98 98 LYS CE C 13 41.46 0.03 . 1 . . . . . . . . 4566 1 868 . 1 1 98 98 LYS N N 15 120.56 0.04 . 1 . . . . . . . . 4566 1 869 . 1 1 99 99 ALA H H 1 7.86 0.022 . 1 . . . . . . . . 4566 1 870 . 1 1 99 99 ALA HA H 1 4.12 0.022 . 1 . . . . . . . . 4566 1 871 . 1 1 99 99 ALA HB1 H 1 1.33 0.022 . 1 . . . . . . . . 4566 1 872 . 1 1 99 99 ALA HB2 H 1 1.33 0.022 . 1 . . . . . . . . 4566 1 873 . 1 1 99 99 ALA HB3 H 1 1.33 0.022 . 1 . . . . . . . . 4566 1 874 . 1 1 99 99 ALA C C 13 177.67 0.03 . 1 . . . . . . . . 4566 1 875 . 1 1 99 99 ALA CA C 13 53.18 0.03 . 1 . . . . . . . . 4566 1 876 . 1 1 99 99 ALA CB C 13 17.89 0.03 . 1 . . . . . . . . 4566 1 877 . 1 1 99 99 ALA N N 15 119.91 0.04 . 1 . . . . . . . . 4566 1 878 . 1 1 100 100 MET H H 1 7.62 0.022 . 1 . . . . . . . . 4566 1 879 . 1 1 100 100 MET HA H 1 4.01 0.022 . 1 . . . . . . . . 4566 1 880 . 1 1 100 100 MET HB2 H 1 2.44 0.022 . 2 . . . . . . . . 4566 1 881 . 1 1 100 100 MET HB3 H 1 1.99 0.022 . 2 . . . . . . . . 4566 1 882 . 1 1 100 100 MET C C 13 173.9 0.03 . 1 . . . . . . . . 4566 1 883 . 1 1 100 100 MET CA C 13 56.06 0.03 . 1 . . . . . . . . 4566 1 884 . 1 1 100 100 MET CB C 13 31.47 0.03 . 1 . . . . . . . . 4566 1 885 . 1 1 100 100 MET CG C 13 33.53 0.03 . 1 . . . . . . . . 4566 1 886 . 1 1 100 100 MET N N 15 115.58 0.04 . 1 . . . . . . . . 4566 1 887 . 1 1 101 101 ASP H H 1 7.27 0.022 . 1 . . . . . . . . 4566 1 888 . 1 1 101 101 ASP HA H 1 4.39 0.022 . 1 . . . . . . . . 4566 1 889 . 1 1 101 101 ASP HB2 H 1 2.66 0.022 . 2 . . . . . . . . 4566 1 890 . 1 1 101 101 ASP HB3 H 1 2.47 0.022 . 2 . . . . . . . . 4566 1 891 . 1 1 101 101 ASP C C 13 177.55 0.03 . 1 . . . . . . . . 4566 1 892 . 1 1 101 101 ASP CA C 13 56.25 0.03 . 1 . . . . . . . . 4566 1 893 . 1 1 101 101 ASP CB C 13 40.34 0.03 . 1 . . . . . . . . 4566 1 894 . 1 1 101 101 ASP N N 15 118.27 0.04 . 1 . . . . . . . . 4566 1 895 . 1 1 102 102 ASN H H 1 10.04 0.022 . 1 . . . . . . . . 4566 1 896 . 1 1 102 102 ASN HA H 1 3.81 0.022 . 1 . . . . . . . . 4566 1 897 . 1 1 102 102 ASN HB2 H 1 3.16 0.022 . 2 . . . . . . . . 4566 1 898 . 1 1 102 102 ASN HB3 H 1 2.97 0.022 . 2 . . . . . . . . 4566 1 899 . 1 1 102 102 ASN HD21 H 1 7.61 0.022 . 2 . . . . . . . . 4566 1 900 . 1 1 102 102 ASN HD22 H 1 6.85 0.022 . 2 . . . . . . . . 4566 1 901 . 1 1 102 102 ASN C C 13 174.01 0.03 . 1 . . . . . . . . 4566 1 902 . 1 1 102 102 ASN CA C 13 55.29 0.03 . 1 . . . . . . . . 4566 1 903 . 1 1 102 102 ASN CB C 13 37.3 0.03 . 1 . . . . . . . . 4566 1 904 . 1 1 102 102 ASN N N 15 122.96 0.04 . 1 . . . . . . . . 4566 1 905 . 1 1 102 102 ASN ND2 N 15 114.48 0.04 . 1 . . . . . . . . 4566 1 906 . 1 1 103 103 MET H H 1 8.43 0.022 . 1 . . . . . . . . 4566 1 907 . 1 1 103 103 MET HA H 1 4.62 0.022 . 1 . . . . . . . . 4566 1 908 . 1 1 103 103 MET HB2 H 1 2.17 0.022 . 2 . . . . . . . . 4566 1 909 . 1 1 103 103 MET HG2 H 1 2.95 0.022 . 2 . . . . . . . . 4566 1 910 . 1 1 103 103 MET HE1 H 1 2.01 0.022 . 1 . . . . . . . . 4566 1 911 . 1 1 103 103 MET HE2 H 1 2.01 0.022 . 1 . . . . . . . . 4566 1 912 . 1 1 103 103 MET HE3 H 1 2.01 0.022 . 1 . . . . . . . . 4566 1 913 . 1 1 103 103 MET C C 13 172.87 0.03 . 1 . . . . . . . . 4566 1 914 . 1 1 103 103 MET CA C 13 56.06 0.03 . 1 . . . . . . . . 4566 1 915 . 1 1 103 103 MET CB C 13 30.82 0.03 . 1 . . . . . . . . 4566 1 916 . 1 1 103 103 MET CG C 13 32.48 0.03 . 1 . . . . . . . . 4566 1 917 . 1 1 103 103 MET CE C 13 20.4 0.03 . 1 . . . . . . . . 4566 1 918 . 1 1 103 103 MET N N 15 118.1 0.04 . 1 . . . . . . . . 4566 1 919 . 1 1 104 104 THR H H 1 8.57 0.022 . 1 . . . . . . . . 4566 1 920 . 1 1 104 104 THR HA H 1 5.35 0.022 . 1 . . . . . . . . 4566 1 921 . 1 1 104 104 THR HB H 1 3.66 0.022 . 1 . . . . . . . . 4566 1 922 . 1 1 104 104 THR HG21 H 1 0.98 0.022 . 1 . . . . . . . . 4566 1 923 . 1 1 104 104 THR HG22 H 1 0.98 0.022 . 1 . . . . . . . . 4566 1 924 . 1 1 104 104 THR HG23 H 1 0.98 0.022 . 1 . . . . . . . . 4566 1 925 . 1 1 104 104 THR C C 13 175.5 0.03 . 1 . . . . . . . . 4566 1 926 . 1 1 104 104 THR CA C 13 61.24 0.03 . 1 . . . . . . . . 4566 1 927 . 1 1 104 104 THR CB C 13 69.72 0.03 . 1 . . . . . . . . 4566 1 928 . 1 1 104 104 THR CG2 C 13 21.12 0.03 . 1 . . . . . . . . 4566 1 929 . 1 1 104 104 THR N N 15 116.69 0.04 . 1 . . . . . . . . 4566 1 930 . 1 1 105 105 VAL H H 1 9.11 0.022 . 1 . . . . . . . . 4566 1 931 . 1 1 105 105 VAL HA H 1 4.5 0.022 . 1 . . . . . . . . 4566 1 932 . 1 1 105 105 VAL HB H 1 1.25 0.022 . 1 . . . . . . . . 4566 1 933 . 1 1 105 105 VAL HG11 H 1 0.04 0.022 . 2 . . . . . . . . 4566 1 934 . 1 1 105 105 VAL HG12 H 1 0.04 0.022 . 2 . . . . . . . . 4566 1 935 . 1 1 105 105 VAL HG13 H 1 0.04 0.022 . 2 . . . . . . . . 4566 1 936 . 1 1 105 105 VAL HG21 H 1 0 0.022 . 2 . . . . . . . . 4566 1 937 . 1 1 105 105 VAL HG22 H 1 0 0.022 . 2 . . . . . . . . 4566 1 938 . 1 1 105 105 VAL HG23 H 1 0 0.022 . 2 . . . . . . . . 4566 1 939 . 1 1 105 105 VAL C C 13 172.98 0.03 . 1 . . . . . . . . 4566 1 940 . 1 1 105 105 VAL CA C 13 57.79 0.03 . 1 . . . . . . . . 4566 1 941 . 1 1 105 105 VAL CB C 13 33.63 0.03 . 1 . . . . . . . . 4566 1 942 . 1 1 105 105 VAL CG1 C 13 22.7 0.03 . 2 . . . . . . . . 4566 1 943 . 1 1 105 105 VAL CG2 C 13 19 0.03 . 2 . . . . . . . . 4566 1 944 . 1 1 105 105 VAL N N 15 122.73 0.04 . 1 . . . . . . . . 4566 1 945 . 1 1 106 106 ARG H H 1 8.44 0.022 . 1 . . . . . . . . 4566 1 946 . 1 1 106 106 ARG HA H 1 4.81 0.022 . 1 . . . . . . . . 4566 1 947 . 1 1 106 106 ARG HB2 H 1 1.63 0.022 . 2 . . . . . . . . 4566 1 948 . 1 1 106 106 ARG HB3 H 1 1.45 0.022 . 2 . . . . . . . . 4566 1 949 . 1 1 106 106 ARG HG2 H 1 1.29 0.022 . 2 . . . . . . . . 4566 1 950 . 1 1 106 106 ARG HD2 H 1 2.99 0.022 . 2 . . . . . . . . 4566 1 951 . 1 1 106 106 ARG C C 13 174.47 0.03 . 1 . . . . . . . . 4566 1 952 . 1 1 106 106 ARG CA C 13 53.95 0.03 . 1 . . . . . . . . 4566 1 953 . 1 1 106 106 ARG CB C 13 32.98 0.03 . 1 . . . . . . . . 4566 1 954 . 1 1 106 106 ARG CG C 13 27.48 0.03 . 1 . . . . . . . . 4566 1 955 . 1 1 106 106 ARG CD C 13 43.04 0.03 . 1 . . . . . . . . 4566 1 956 . 1 1 106 106 ARG N N 15 121.14 0.04 . 1 . . . . . . . . 4566 1 957 . 1 1 107 107 VAL H H 1 8.35 0.022 . 1 . . . . . . . . 4566 1 958 . 1 1 107 107 VAL HA H 1 4.45 0.022 . 1 . . . . . . . . 4566 1 959 . 1 1 107 107 VAL HB H 1 2.23 0.022 . 1 . . . . . . . . 4566 1 960 . 1 1 107 107 VAL HG11 H 1 1.18 0.022 . 2 . . . . . . . . 4566 1 961 . 1 1 107 107 VAL HG12 H 1 1.18 0.022 . 2 . . . . . . . . 4566 1 962 . 1 1 107 107 VAL HG13 H 1 1.18 0.022 . 2 . . . . . . . . 4566 1 963 . 1 1 107 107 VAL HG21 H 1 0.9 0.022 . 2 . . . . . . . . 4566 1 964 . 1 1 107 107 VAL HG22 H 1 0.9 0.022 . 2 . . . . . . . . 4566 1 965 . 1 1 107 107 VAL HG23 H 1 0.9 0.022 . 2 . . . . . . . . 4566 1 966 . 1 1 107 107 VAL C C 13 177.56 0.03 . 1 . . . . . . . . 4566 1 967 . 1 1 107 107 VAL CA C 13 59.32 0.03 . 1 . . . . . . . . 4566 1 968 . 1 1 107 107 VAL CB C 13 31.59 0.03 . 1 . . . . . . . . 4566 1 969 . 1 1 107 107 VAL N N 15 124.6 0.04 . 1 . . . . . . . . 4566 1 970 . 1 1 108 108 PRO HA H 1 4.24 0.022 . 1 . . . . . . . . 4566 1 971 . 1 1 108 108 PRO HB2 H 1 1.98 0.022 . 2 . . . . . . . . 4566 1 972 . 1 1 108 108 PRO HB3 H 1 1.9 0.022 . 2 . . . . . . . . 4566 1 973 . 1 1 108 108 PRO HD2 H 1 3.65 0.022 . 2 . . . . . . . . 4566 1 974 . 1 1 108 108 PRO C C 13 175.69 0.03 . 1 . . . . . . . . 4566 1 975 . 1 1 108 108 PRO CA C 13 62.2 0.03 . 1 . . . . . . . . 4566 1 976 . 1 1 108 108 PRO CB C 13 31.68 0.03 . 1 . . . . . . . . 4566 1 977 . 1 1 108 108 PRO CG C 13 26.14 0.03 . 1 . . . . . . . . 4566 1 978 . 1 1 108 108 PRO CD C 13 50.7 0.03 . 1 . . . . . . . . 4566 1 979 . 1 1 109 109 ASP H H 1 8.47 0.022 . 1 . . . . . . . . 4566 1 980 . 1 1 109 109 ASP HA H 1 4.39 0.022 . 1 . . . . . . . . 4566 1 981 . 1 1 109 109 ASP HB2 H 1 2.74 0.022 . 2 . . . . . . . . 4566 1 982 . 1 1 109 109 ASP HB3 H 1 2.67 0.022 . 2 . . . . . . . . 4566 1 983 . 1 1 109 109 ASP C C 13 175.15 0.03 . 1 . . . . . . . . 4566 1 984 . 1 1 109 109 ASP CA C 13 54.34 0.03 . 1 . . . . . . . . 4566 1 985 . 1 1 109 109 ASP CB C 13 40.76 0.03 . 1 . . . . . . . . 4566 1 986 . 1 1 109 109 ASP N N 15 120.03 0.04 . 1 . . . . . . . . 4566 1 987 . 1 1 110 110 ALA H H 1 8.16 0.022 . 1 . . . . . . . . 4566 1 988 . 1 1 110 110 ALA HA H 1 4.3 0.022 . 1 . . . . . . . . 4566 1 989 . 1 1 110 110 ALA HB1 H 1 1.17 0.022 . 1 . . . . . . . . 4566 1 990 . 1 1 110 110 ALA HB2 H 1 1.17 0.022 . 1 . . . . . . . . 4566 1 991 . 1 1 110 110 ALA HB3 H 1 1.17 0.022 . 1 . . . . . . . . 4566 1 992 . 1 1 110 110 ALA C C 13 176.75 0.03 . 1 . . . . . . . . 4566 1 993 . 1 1 110 110 ALA CA C 13 51.07 0.03 . 1 . . . . . . . . 4566 1 994 . 1 1 110 110 ALA CB C 13 19.37 0.03 . 1 . . . . . . . . 4566 1 995 . 1 1 110 110 ALA N N 15 122.28 0.04 . 1 . . . . . . . . 4566 1 996 . 1 1 111 111 VAL H H 1 7.85 0.022 . 1 . . . . . . . . 4566 1 997 . 1 1 111 111 VAL HA H 1 3.85 0.022 . 1 . . . . . . . . 4566 1 998 . 1 1 111 111 VAL HB H 1 1.82 0.022 . 1 . . . . . . . . 4566 1 999 . 1 1 111 111 VAL HG11 H 1 0.78 0.022 . 2 . . . . . . . . 4566 1 1000 . 1 1 111 111 VAL HG12 H 1 0.78 0.022 . 2 . . . . . . . . 4566 1 1001 . 1 1 111 111 VAL HG13 H 1 0.78 0.022 . 2 . . . . . . . . 4566 1 1002 . 1 1 111 111 VAL C C 13 174.81 0.03 . 1 . . . . . . . . 4566 1 1003 . 1 1 111 111 VAL CA C 13 61.43 0.03 . 1 . . . . . . . . 4566 1 1004 . 1 1 111 111 VAL CB C 13 32.11 0.03 . 1 . . . . . . . . 4566 1 1005 . 1 1 111 111 VAL CG1 C 13 20.06 0.03 . 2 . . . . . . . . 4566 1 1006 . 1 1 111 111 VAL CG2 C 13 19.8 0.03 . 2 . . . . . . . . 4566 1 1007 . 1 1 111 111 VAL N N 15 118.11 0.04 . 1 . . . . . . . . 4566 1 1008 . 1 1 112 112 SER H H 1 8.12 0.022 . 1 . . . . . . . . 4566 1 1009 . 1 1 112 112 SER HA H 1 4.14 0.022 . 1 . . . . . . . . 4566 1 1010 . 1 1 112 112 SER HB2 H 1 3.83 0.022 . 2 . . . . . . . . 4566 1 1011 . 1 1 112 112 SER HB3 H 1 3.79 0.022 . 2 . . . . . . . . 4566 1 1012 . 1 1 112 112 SER C C 13 178.24 0.03 . 1 . . . . . . . . 4566 1 1013 . 1 1 112 112 SER CA C 13 57.4 0.03 . 1 . . . . . . . . 4566 1 1014 . 1 1 112 112 SER CB C 13 63.24 0.03 . 1 . . . . . . . . 4566 1 1015 . 1 1 112 112 SER N N 15 118.68 0.04 . 1 . . . . . . . . 4566 1 1016 . 1 1 113 113 ASP H H 1 8.2 0.022 . 1 . . . . . . . . 4566 1 1017 . 1 1 113 113 ASP HA H 1 4.18 0.022 . 1 . . . . . . . . 4566 1 1018 . 1 1 113 113 ASP HB2 H 1 2.97 0.022 . 2 . . . . . . . . 4566 1 1019 . 1 1 113 113 ASP HB3 H 1 2.81 0.022 . 2 . . . . . . . . 4566 1 1020 . 1 1 113 113 ASP C C 13 175.73 0.03 . 1 . . . . . . . . 4566 1 1021 . 1 1 113 113 ASP CA C 13 53.51 0.03 . 1 . . . . . . . . 4566 1 1022 . 1 1 113 113 ASP CB C 13 40.55 0.03 . 1 . . . . . . . . 4566 1 1023 . 1 1 113 113 ASP N N 15 123.19 0.04 . 1 . . . . . . . . 4566 1 1024 . 1 1 114 114 ALA H H 1 8.23 0.022 . 1 . . . . . . . . 4566 1 1025 . 1 1 114 114 ALA HA H 1 4.26 0.022 . 1 . . . . . . . . 4566 1 1026 . 1 1 114 114 ALA HB1 H 1 1.34 0.022 . 1 . . . . . . . . 4566 1 1027 . 1 1 114 114 ALA HB2 H 1 1.34 0.022 . 1 . . . . . . . . 4566 1 1028 . 1 1 114 114 ALA HB3 H 1 1.34 0.022 . 1 . . . . . . . . 4566 1 1029 . 1 1 114 114 ALA CA C 13 52 0.03 . 1 . . . . . . . . 4566 1 1030 . 1 1 114 114 ALA CB C 13 18.5 0.03 . 1 . . . . . . . . 4566 1 1031 . 1 1 114 114 ALA N N 15 124.84 0.04 . 1 . . . . . . . . 4566 1 1032 . 1 1 115 115 ARG H H 1 8.28 0.022 . 1 . . . . . . . . 4566 1 1033 . 1 1 115 115 ARG HA H 1 4.26 0.022 . 1 . . . . . . . . 4566 1 1034 . 1 1 115 115 ARG HB2 H 1 1.8 0.022 . 2 . . . . . . . . 4566 1 1035 . 1 1 115 115 ARG HB3 H 1 1.64 0.022 . 2 . . . . . . . . 4566 1 1036 . 1 1 115 115 ARG CA C 13 55.67 0.03 . 1 . . . . . . . . 4566 1 1037 . 1 1 115 115 ARG CB C 13 29.96 0.03 . 1 . . . . . . . . 4566 1 1038 . 1 1 115 115 ARG CG C 13 26.4 0.03 . 1 . . . . . . . . 4566 1 1039 . 1 1 115 115 ARG CD C 13 42.78 0.03 . 1 . . . . . . . . 4566 1 1040 . 1 1 115 115 ARG N N 15 119.97 0.04 . 1 . . . . . . . . 4566 1 1041 . 1 1 116 116 GLU H H 1 8.37 0.022 . 1 . . . . . . . . 4566 1 1042 . 1 1 116 116 GLU HA H 1 4.26 0.022 . 1 . . . . . . . . 4566 1 1043 . 1 1 116 116 GLU HB2 H 1 2.03 0.022 . 2 . . . . . . . . 4566 1 1044 . 1 1 116 116 GLU HB3 H 1 1.92 0.022 . 2 . . . . . . . . 4566 1 1045 . 1 1 116 116 GLU HG2 H 1 2.23 0.022 . 2 . . . . . . . . 4566 1 1046 . 1 1 116 116 GLU CA C 13 55.89 0.03 . 1 . . . . . . . . 4566 1 1047 . 1 1 116 116 GLU CB C 13 29.52 0.03 . 1 . . . . . . . . 4566 1 1048 . 1 1 116 116 GLU CG C 13 35.64 0.03 . 1 . . . . . . . . 4566 1 1049 . 1 1 116 116 GLU N N 15 121.85 0.04 . 1 . . . . . . . . 4566 1 1050 . 1 1 117 117 SER H H 1 8.28 0.022 . 1 . . . . . . . . 4566 1 1051 . 1 1 117 117 SER HA H 1 4.8 0.022 . 1 . . . . . . . . 4566 1 1052 . 1 1 117 117 SER HB2 H 1 3.79 0.022 . 2 . . . . . . . . 4566 1 1053 . 1 1 117 117 SER CA C 13 57.62 0.03 . 1 . . . . . . . . 4566 1 1054 . 1 1 117 117 SER CB C 13 63.02 0.03 . 1 . . . . . . . . 4566 1 1055 . 1 1 117 117 SER N N 15 116.69 0.04 . 1 . . . . . . . . 4566 1 1056 . 1 1 118 118 ILE H H 1 8.05 0.022 . 1 . . . . . . . . 4566 1 1057 . 1 1 118 118 ILE HA H 1 4.18 0.022 . 1 . . . . . . . . 4566 1 1058 . 1 1 118 118 ILE HB H 1 1.88 0.022 . 1 . . . . . . . . 4566 1 1059 . 1 1 118 118 ILE HG12 H 1 0.9 0.022 . 2 . . . . . . . . 4566 1 1060 . 1 1 118 118 ILE CA C 13 60.64 0.03 . 1 . . . . . . . . 4566 1 1061 . 1 1 118 118 ILE CB C 13 38.17 0.03 . 1 . . . . . . . . 4566 1 1062 . 1 1 118 118 ILE CG1 C 13 26.66 0.03 . 1 . . . . . . . . 4566 1 1063 . 1 1 118 118 ILE CG2 C 13 16.89 0.03 . 1 . . . . . . . . 4566 1 1064 . 1 1 118 118 ILE CD1 C 13 12.66 0.03 . 1 . . . . . . . . 4566 1 1065 . 1 1 118 118 ILE N N 15 122.28 0.04 . 1 . . . . . . . . 4566 1 1066 . 1 1 119 119 ASP H H 1 8.35 0.022 . 1 . . . . . . . . 4566 1 1067 . 1 1 119 119 ASP HA H 1 4.61 0.022 . 1 . . . . . . . . 4566 1 1068 . 1 1 119 119 ASP HB2 H 1 2.74 0.022 . 1 . . . . . . . . 4566 1 1069 . 1 1 119 119 ASP HB3 H 1 2.58 0.022 . 1 . . . . . . . . 4566 1 1070 . 1 1 119 119 ASP CA C 13 53.73 0.03 . 1 . . . . . . . . 4566 1 1071 . 1 1 119 119 ASP CB C 13 40.55 0.03 . 1 . . . . . . . . 4566 1 1072 . 1 1 119 119 ASP N N 15 123.84 0.04 . 1 . . . . . . . . 4566 1 1073 . 1 1 120 120 MET CA C 13 55.19 0.03 . 1 . . . . . . . . 4566 1 1074 . 1 1 120 120 MET CB C 13 31.68 0.03 . 1 . . . . . . . . 4566 1 1075 . 1 1 120 120 MET CG C 13 28.25 0.03 . 1 . . . . . . . . 4566 1 1076 . 1 1 120 120 MET CE C 13 19.53 0.03 . 1 . . . . . . . . 4566 1 1077 . 1 1 121 121 GLY H H 1 8.49 0.022 . 1 . . . . . . . . 4566 1 1078 . 1 1 121 121 GLY HA2 H 1 4.5 0.022 . 2 . . . . . . . . 4566 1 1079 . 1 1 121 121 GLY C C 13 173.95 0.03 . 1 . . . . . . . . 4566 1 1080 . 1 1 121 121 GLY CA C 13 45.13 0.03 . 1 . . . . . . . . 4566 1 1081 . 1 1 121 121 GLY N N 15 109.36 0.04 . 1 . . . . . . . . 4566 1 1082 . 1 1 122 122 MET H H 1 8.11 0.022 . 1 . . . . . . . . 4566 1 1083 . 1 1 122 122 MET HA H 1 4.24 0.022 . 1 . . . . . . . . 4566 1 1084 . 1 1 122 122 MET HB2 H 1 2.01 0.022 . 2 . . . . . . . . 4566 1 1085 . 1 1 122 122 MET HB3 H 1 1.86 0.022 . 2 . . . . . . . . 4566 1 1086 . 1 1 122 122 MET HG2 H 1 2.18 0.022 . 2 . . . . . . . . 4566 1 1087 . 1 1 122 122 MET C C 13 175.05 0.03 . 1 . . . . . . . . 4566 1 1088 . 1 1 122 122 MET CA C 13 54.85 0.03 . 1 . . . . . . . . 4566 1 1089 . 1 1 122 122 MET CB C 13 29.31 0.03 . 1 . . . . . . . . 4566 1 1090 . 1 1 122 122 MET CG C 13 31.42 0.03 . 1 . . . . . . . . 4566 1 1091 . 1 1 122 122 MET CE C 13 19.75 0.03 . 1 . . . . . . . . 4566 1 1092 . 1 1 122 122 MET N N 15 119.62 0.04 . 1 . . . . . . . . 4566 1 1093 . 1 1 123 123 ASN H H 1 8.03 0.022 . 1 . . . . . . . . 4566 1 1094 . 1 1 123 123 ASN C C 13 179.27 0.03 . 1 . . . . . . . . 4566 1 1095 . 1 1 123 123 ASN CA C 13 54.34 0.03 . 1 . . . . . . . . 4566 1 1096 . 1 1 123 123 ASN CB C 13 39.9 0.03 . 1 . . . . . . . . 4566 1 1097 . 1 1 123 123 ASN N N 15 125.07 0.04 . 1 . . . . . . . . 4566 1 stop_ save_