data_5156 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5156 _Entry.Title ; Partial assignment of the calcium-bound calretinin I-II domain (residues 1-100): 1H, 13C and 15N backbone assignments (and partial sidechain assignment) for structured elements ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2001-09-23 _Entry.Accession_date 2001-09-24 _Entry.Last_release_date 2002-01-25 _Entry.Original_release_date 2002-01-25 _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 Malgorzata Palczewska . . . 5156 2 Patrick Groves . . . 5156 3 Attila Ambrus . . . 5156 4 Agata Kaleta . . . 5156 5 Katalin Kover . E . 5156 6 Gyula Batta . . . 5156 7 Jacek Kuznicki . . . 5156 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 5156 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 533 5156 '13C chemical shifts' 495 5156 '15N chemical shifts' 151 5156 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2002-01-25 2001-09-23 original author . 5156 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5156 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21590353 _Citation.DOI . _Citation.PubMed_ID 11733019 _Citation.Full_citation . _Citation.Title ; Structural and Biochemical Characterization of Neuronal Calretinin Domain I-II (residues 1-100). Comparison to Homologous Calbindin D28k Domain I-II (residues 1-93) ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full . _Citation.Journal_volume 268 _Citation.Journal_issue 23 _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 6229 _Citation.Page_last 6237 _Citation.Year 2001 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Malgorzata Palczewska . . . 5156 1 2 Patrick Groves . . . 5156 1 3 Attila Ambrus . . . 5156 1 4 Agata Kaleta . . . 5156 1 5 Katalin Kover . E. . 5156 1 6 Gyula Batta . . . 5156 1 7 Jacek Kuznicki . . . 5156 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID calretinin 5156 1 EF-hand 5156 1 calcium 5156 1 'calbindin D28k' 5156 1 'NMR secondary structure' 5156 1 stop_ save_ save_ref-1 _Citation.Sf_category citations _Citation.Sf_framecode ref-1 _Citation.Entry_ID 5156 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10600467 _Citation.Full_citation ; Palczewska M, Groves P, Kuznicki J. Use of Pichia pastoris for the expression, purification, and characterization of rat calretinin "EF-hand" domains. Protein Expr Purif. 1999 Dec;17(3):465-76. ; _Citation.Title 'Use of Pichia pastoris for the expression, purification, and characterization of rat calretinin "EF-hand" domains.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Expr. Purif.' _Citation.Journal_name_full 'Protein expression and purification' _Citation.Journal_volume 17 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1046-5928 _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 465 _Citation.Page_last 476 _Citation.Year 1999 _Citation.Details ; Calretinin (CR) is a calcium-binding, neuronal protein of undefined function. Related proteins either buffer intracellular calcium concentrations or are involved in calcium-signaling pathways. We transformed three CR gene fragment sequences, corresponding to its three complementary domains (I-II, III-IV, and V-VI), into Pichia pastoris. High yields of extracellular expression, of more than 200 mg/liter, were achieved. Simple purification protocols provide high yields of homogenous proteins: dialysis and DEAE-cellulose chromatography for domains I-II and III-IV or ammonium sulfate precipitation and octyl-Sepharose chromatography for domain V-VI. To our knowledge, this is the first report of the expression of an EF-hand protein using P. pastoris. Direct comparison of the purified yields of domain I-II indicates a approximately 20-fold improvement over Escherichia coli. N-terminal amino acid sequencing confirmed our gene products and two anti-calretinin antibodies recognized the appropriate domains. All three CR domains bind (45)Ca and the domain containing EF-hands V and VI seems to have a lower calcium capacity than the other domains. Circular dichroism indicates a high helix content for each of the domains. Calcium-induced structural changes in the first two domains, followed by tryptophan fluorescence, correspond with previous studies, while tyrosine emission fluorescence indicates calcium-induced structural changes also occur in domain V-VI. The methods and expression levels achieved are suitable for future NMR labeling of the proteins, with (15)N and (13)C, and structure-function studies that will help to further understand CR function. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M. Palczewska M. . . 5156 2 2 P. Groves P. . . 5156 2 3 J. Kuznicki J. . . 5156 2 stop_ save_ save_ref-2 _Citation.Sf_category citations _Citation.Sf_framecode ref-2 _Citation.Entry_ID 5156 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Kay, L. E., Keifer, P. & Saarinen, T. (1992) Pure Absorption Gradient Enhanced Heteronuclear Single Quantum Correlation Spectroscopy with Improved Sensitivity, J. Am. Chem. Soc. 114, 10663-10665. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref-3 _Citation.Sf_category citations _Citation.Sf_framecode ref-3 _Citation.Entry_ID 5156 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Palmer, A. G., Cavanagh, J., Wright, P. E. & Rance, M. (1991) Sensitivity Improvement in Proton-Detected 2-Dimensional Heteronuclear Correlation Nmr-Spectroscopy, J. Magn. Reson. 93, 151-170. ; _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-4 _Citation.Sf_category citations _Citation.Sf_framecode ref-4 _Citation.Entry_ID 5156 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8019138 _Citation.Full_citation ; Schleucher J, Schwendinger M, Sattler M, Schmidt P, Schedletzky O, Glaser SJ, Sorensen OW, Griesinger C. A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradients. J Biomol NMR. 1994 Mar;4(2):301-6. ; _Citation.Title 'A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradients.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 4 _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 301 _Citation.Page_last 306 _Citation.Year 1994 _Citation.Details ; General pulse sequence elements that achieve sensitivity-enhanced coherence transfer from a heteronucleus to protons of arbitrary multiplicity are introduced. The building blocks are derived from the sensitivity-enhancement scheme introduced by Cavanagh et al. ((1991) J. Magn. Reson., 91, 429-436), which was used in conjunction with gradient coherence selection by Kay et al. ((1992) J. Am. Chem. Soc., 114, 10663-10665), as well as from a multiple-pulse sequence effecting a heteronuclear planar coupling Hamiltonian. The building blocks are incorporated into heteronuclear correlation experiments, in conjunction with coherence selection by the formation of a heteronuclear gradient echo. This allows for efficient water suppression without the need for water presaturation. The methods are demonstrated in HSQC-type experiments on a sample of a decapeptide in H2O. The novel pulse sequence elements can be incorporated into multidimensional experiments. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 J. Schleucher J. . . 5156 5 2 M. Schwendinger M. . . 5156 5 3 M. Sattler M. . . 5156 5 4 P. Schmidt P. . . 5156 5 5 O. Schedletzky O. . . 5156 5 6 'S. J.' Glaser S. J. . 5156 5 7 'O. W.' Sorensen O. W. . 5156 5 8 C. Griesinger C. . . 5156 5 stop_ save_ save_ref-5 _Citation.Sf_category citations _Citation.Sf_framecode ref-5 _Citation.Entry_ID 5156 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Grzesiek, S. & Bax, A. (1992) Improved 3D Triple-Resonance NMR Techniques Applied to a 31 kDa Protein, J. Magn. Reson. 96, 432-440. ; _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-6 _Citation.Sf_category citations _Citation.Sf_framecode ref-6 _Citation.Entry_ID 5156 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Kay, L. E., Ikura, M., Tschudin, R. & Bax, A. (1990) 3-Dimensional Triple-Resonance NMR-Spectroscopy of Isotopically Enriched Proteins, J. Magn. Reson. 89, 496-514. ; _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-7 _Citation.Sf_category citations _Citation.Sf_framecode ref-7 _Citation.Entry_ID 5156 _Citation.ID 8 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Clubb, R. T., Thanabal, V. & Wagner, G. (1992) A Constant-Time Three-Dimensional Triple-Resonance Pulse Scheme to Correlate Intraresidue {+1}H{+N},{+15}N,and {+13}C' Chemical Shifts in {+15}N-{+13}C-Labeled Proteins, J. Magn. Reson. 97, 213-217. ; _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-8 _Citation.Sf_category citations _Citation.Sf_framecode ref-8 _Citation.Entry_ID 5156 _Citation.ID 9 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Kay, L. E., Xu, G. Y. & Yamazaki, T. (1994) Enhanced-Sensitivity Triple-Resonance Spectroscopy with Minimal H2O Saturation, J. Magn. Reson. Ser.A 109, 129-133. ; _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-9 _Citation.Sf_category citations _Citation.Sf_framecode ref-9 _Citation.Entry_ID 5156 _Citation.ID 10 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Sattler, M., Schleucher, J. & Griesinger, C. (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients, Prog. Nucl. Magn. Reson. Spect. 34, 93-158. ; _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-10 _Citation.Sf_category citations _Citation.Sf_framecode ref-10 _Citation.Entry_ID 5156 _Citation.ID 11 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Muhandiram, D. R. & Kay, L. E. (1994) Gradient-Enhanced Triple-Resonance 3-Dimensional Nmr Experiments With Improved Sensitivity, J. Magn. Reson. Ser.B 103, 203-216. ; _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-11 _Citation.Sf_category citations _Citation.Sf_framecode ref-11 _Citation.Entry_ID 5156 _Citation.ID 12 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Wittekind, M. & Mueller, L. (1993) HNCACB, a High-Sensitivity 3D NMR Experiment to Correlate Amide-Proton and Nitrogen Resonances with the Alpha-Carbon and Beta-Carbon Resonances in Proteins, J. Magn. Reson. Ser.B 101, 201-205. ; _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-12 _Citation.Sf_category citations _Citation.Sf_framecode ref-12 _Citation.Entry_ID 5156 _Citation.ID 13 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Grzesiek, S. & Bax, A. (1992) An Efficient Experiment For Sequential Backbone Assignment of Medium-Sized Isotopically Enriched Proteins, J. Magn. Reson. 99, 201-207. ; _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-13 _Citation.Sf_category citations _Citation.Sf_framecode ref-13 _Citation.Entry_ID 5156 _Citation.ID 14 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8477186 _Citation.Full_citation ; Grzesiek S, Bax A. Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. J Biomol NMR. 1993 Mar;3(2):185-204. ; _Citation.Title 'Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 3 _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 185 _Citation.Page_last 204 _Citation.Year 1993 _Citation.Details ; Experiments and procedures are described that greatly alleviate the sequential assignment process of uniformly 13C/15N-enriched proteins by determining the type of amino acid from experiments that correlate side chain with backbone amide resonances. A recently proposed 3D NMR experiment, CBCA(CO)NH, correlates C alpha and C beta resonances to the backbone amide 1H and 15N resonances of the next residue (Grzesiek, S. and Bax, A. (1992) J. Am. Chem. Soc., 114, 6291-6293). An extension of this experiment is described which correlates the proton H beta and H alpha resonances to the amide 1H and 15N resonances of the next amino acid, and a detailed product operator description is given. A simple 2D-edited constant-time HSQC experiment is described which rapidly identifies H beta and C beta resonances of aromatic or Asn/Asp residues. The extent to which combined knowledge of the C alpha and C beta chemical shift values determines the amino acid type is investigated, and it is demonstrated that the combined C alpha and C beta chemical shifts of three or four adjacent residues usually are sufficient for defining a unique position in the protein sequence. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 S. Grzesiek S. . . 5156 14 2 A. Bax A. . . 5156 14 stop_ save_ save_ref-14 _Citation.Sf_category citations _Citation.Sf_framecode ref-14 _Citation.Entry_ID 5156 _Citation.ID 15 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7812158 _Citation.Full_citation ; Kuboniwa H, Grzesiek S, Delaglio F, Bax A. Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J Biomol NMR. 1994 Nov;4(6):871-8. ; _Citation.Title 'Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 4 _Citation.Journal_issue 6 _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 871 _Citation.Page_last 878 _Citation.Year 1994 _Citation.Details ; Two new methods are described for the measurement of three-bond JHNH alpha couplings in proteins isotopically enriched with 15N. Both methods leave the water magnetization in an unsaturated state, parallel to the z-axis, and therefore offer significant enhancements in sensitivity for rapidly exchanging backbone amide protons. The J couplings can be measured either from a set of constant-time 2D 1H-15N HMQC spectra, which are modulated in intensity by JHNH alpha, or from a water-flip-back version of the 3D HNHA experiment. The method is demonstrated for a sample of calcium-free calmodulin. Residues Lys75-Asp80 have JHNH alpha values in the 6-7 Hz range, suggesting that a break in the 'central helix' occurs at the same position as previously observed in solution NMR studies of Ca(2+)-ligated calmodulin. ; 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. Kuboniwa H. . . 5156 15 2 S. Grzesiek S. . . 5156 15 3 F. Delaglio F. . . 5156 15 4 A. Bax A. . . 5156 15 stop_ save_ save_ref-15 _Citation.Sf_category citations _Citation.Sf_framecode ref-15 _Citation.Entry_ID 5156 _Citation.ID 16 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Sattler, M., Maurer, M., Schleucher, J. & Griesinger, C. (1995) A Simultaneous N-15,H-1-HSQC and C-13,H-1-HSQC With Sensitivity Enhancement and a Heteronuclear Gradient-Echo, J. Biomol. NMR 5, 97-102. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_calretinin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_calretinin _Assembly.Entry_ID 5156 _Assembly.ID 1 _Assembly.Name calretinin _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details ; D29-E40 and D76-E87 constitute two 12-residue calcium-binding loops. Both loops of calretinin I-II bind calcium. ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5156 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 'calretinin I-II domain' 1 $calretinin . . . native . . . . . 5156 1 2 'calcium ion, I' 2 $CA . . . native . . . . . 5156 1 3 'calcium ion, II' 2 $CA . . . native . . . . . 5156 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID calretinin system 5156 1 calretinin abbreviation 5156 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'Calcium-binding protein of the EF-hand family' 5156 1 'A member of the calbindin D28k subgroup' 5156 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_calretinin _Entity.Sf_category entity _Entity.Sf_framecode calretinin _Entity.Entry_ID 5156 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name calretinin _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 ; YVEFMAGPQQQPPYLHLAEL TASQFLEIWKHFDADGNGYI EGKELENFFQELEKARKGSG MMSKSDNFGEKMKEFMQKYD KNSDGKIEMAELAQILPTEE NFLL ; _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 104 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 12500 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; YVEF N-terminal tag is the reuslt of extracellular expression from Pichia pastoris, see ref 1. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no EMBL CAA39992 . "calretinin [Homo sapiens]" . . . . . 83.65 87 100.00 100.00 1.62e-55 . . . . 5156 1 2 no GB EDL92533 . "calbindin 2, isoform CRA_c [Rattus norvegicus]" . . . . . 84.62 113 98.86 100.00 3.94e-56 . . . . 5156 1 3 no REF XP_002802612 . "PREDICTED: calretinin-like [Macaca mulatta]" . . . . . 85.58 181 97.75 100.00 2.06e-55 . . . . 5156 1 4 no REF XP_004782213 . "PREDICTED: calretinin [Mustela putorius furo]" . . . . . 83.65 244 98.85 98.85 2.43e-53 . . . . 5156 1 5 no REF XP_006742579 . "PREDICTED: calretinin-like [Leptonychotes weddellii]" . . . . . 96.15 146 98.00 99.00 2.25e-64 . . . . 5156 1 6 no REF XP_008519580 . "PREDICTED: calretinin isoform X2 [Equus przewalskii]" . . . . . 83.65 244 100.00 100.00 3.44e-54 . . . . 5156 1 7 no REF XP_009429507 . "PREDICTED: calretinin [Pan troglodytes]" . . . . . 96.15 198 100.00 100.00 1.64e-64 . . . . 5156 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID calretinin common 5156 1 calretinin abbreviation 5156 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 -4 TYR . 5156 1 2 -3 VAL . 5156 1 3 -2 GLU . 5156 1 4 -1 PHE . 5156 1 5 1 MET . 5156 1 6 2 ALA . 5156 1 7 3 GLY . 5156 1 8 4 PRO . 5156 1 9 5 GLN . 5156 1 10 6 GLN . 5156 1 11 7 GLN . 5156 1 12 8 PRO . 5156 1 13 9 PRO . 5156 1 14 10 TYR . 5156 1 15 11 LEU . 5156 1 16 12 HIS . 5156 1 17 13 LEU . 5156 1 18 14 ALA . 5156 1 19 15 GLU . 5156 1 20 16 LEU . 5156 1 21 17 THR . 5156 1 22 18 ALA . 5156 1 23 19 SER . 5156 1 24 20 GLN . 5156 1 25 21 PHE . 5156 1 26 22 LEU . 5156 1 27 23 GLU . 5156 1 28 24 ILE . 5156 1 29 25 TRP . 5156 1 30 26 LYS . 5156 1 31 27 HIS . 5156 1 32 28 PHE . 5156 1 33 29 ASP . 5156 1 34 30 ALA . 5156 1 35 31 ASP . 5156 1 36 32 GLY . 5156 1 37 33 ASN . 5156 1 38 34 GLY . 5156 1 39 35 TYR . 5156 1 40 36 ILE . 5156 1 41 37 GLU . 5156 1 42 38 GLY . 5156 1 43 39 LYS . 5156 1 44 40 GLU . 5156 1 45 41 LEU . 5156 1 46 42 GLU . 5156 1 47 43 ASN . 5156 1 48 44 PHE . 5156 1 49 45 PHE . 5156 1 50 46 GLN . 5156 1 51 47 GLU . 5156 1 52 48 LEU . 5156 1 53 49 GLU . 5156 1 54 50 LYS . 5156 1 55 51 ALA . 5156 1 56 52 ARG . 5156 1 57 53 LYS . 5156 1 58 54 GLY . 5156 1 59 55 SER . 5156 1 60 56 GLY . 5156 1 61 57 MET . 5156 1 62 58 MET . 5156 1 63 59 SER . 5156 1 64 60 LYS . 5156 1 65 61 SER . 5156 1 66 62 ASP . 5156 1 67 63 ASN . 5156 1 68 64 PHE . 5156 1 69 65 GLY . 5156 1 70 66 GLU . 5156 1 71 67 LYS . 5156 1 72 68 MET . 5156 1 73 69 LYS . 5156 1 74 70 GLU . 5156 1 75 71 PHE . 5156 1 76 72 MET . 5156 1 77 73 GLN . 5156 1 78 74 LYS . 5156 1 79 75 TYR . 5156 1 80 76 ASP . 5156 1 81 77 LYS . 5156 1 82 78 ASN . 5156 1 83 79 SER . 5156 1 84 80 ASP . 5156 1 85 81 GLY . 5156 1 86 82 LYS . 5156 1 87 83 ILE . 5156 1 88 84 GLU . 5156 1 89 85 MET . 5156 1 90 86 ALA . 5156 1 91 87 GLU . 5156 1 92 88 LEU . 5156 1 93 89 ALA . 5156 1 94 90 GLN . 5156 1 95 91 ILE . 5156 1 96 92 LEU . 5156 1 97 93 PRO . 5156 1 98 94 THR . 5156 1 99 95 GLU . 5156 1 100 96 GLU . 5156 1 101 97 ASN . 5156 1 102 98 PHE . 5156 1 103 99 LEU . 5156 1 104 100 LEU . 5156 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 . TYR 1 1 5156 1 . VAL 2 2 5156 1 . GLU 3 3 5156 1 . PHE 4 4 5156 1 . MET 5 5 5156 1 . ALA 6 6 5156 1 . GLY 7 7 5156 1 . PRO 8 8 5156 1 . GLN 9 9 5156 1 . GLN 10 10 5156 1 . GLN 11 11 5156 1 . PRO 12 12 5156 1 . PRO 13 13 5156 1 . TYR 14 14 5156 1 . LEU 15 15 5156 1 . HIS 16 16 5156 1 . LEU 17 17 5156 1 . ALA 18 18 5156 1 . GLU 19 19 5156 1 . LEU 20 20 5156 1 . THR 21 21 5156 1 . ALA 22 22 5156 1 . SER 23 23 5156 1 . GLN 24 24 5156 1 . PHE 25 25 5156 1 . LEU 26 26 5156 1 . GLU 27 27 5156 1 . ILE 28 28 5156 1 . TRP 29 29 5156 1 . LYS 30 30 5156 1 . HIS 31 31 5156 1 . PHE 32 32 5156 1 . ASP 33 33 5156 1 . ALA 34 34 5156 1 . ASP 35 35 5156 1 . GLY 36 36 5156 1 . ASN 37 37 5156 1 . GLY 38 38 5156 1 . TYR 39 39 5156 1 . ILE 40 40 5156 1 . GLU 41 41 5156 1 . GLY 42 42 5156 1 . LYS 43 43 5156 1 . GLU 44 44 5156 1 . LEU 45 45 5156 1 . GLU 46 46 5156 1 . ASN 47 47 5156 1 . PHE 48 48 5156 1 . PHE 49 49 5156 1 . GLN 50 50 5156 1 . GLU 51 51 5156 1 . LEU 52 52 5156 1 . GLU 53 53 5156 1 . LYS 54 54 5156 1 . ALA 55 55 5156 1 . ARG 56 56 5156 1 . LYS 57 57 5156 1 . GLY 58 58 5156 1 . SER 59 59 5156 1 . GLY 60 60 5156 1 . MET 61 61 5156 1 . MET 62 62 5156 1 . SER 63 63 5156 1 . LYS 64 64 5156 1 . SER 65 65 5156 1 . ASP 66 66 5156 1 . ASN 67 67 5156 1 . PHE 68 68 5156 1 . GLY 69 69 5156 1 . GLU 70 70 5156 1 . LYS 71 71 5156 1 . MET 72 72 5156 1 . LYS 73 73 5156 1 . GLU 74 74 5156 1 . PHE 75 75 5156 1 . MET 76 76 5156 1 . GLN 77 77 5156 1 . LYS 78 78 5156 1 . TYR 79 79 5156 1 . ASP 80 80 5156 1 . LYS 81 81 5156 1 . ASN 82 82 5156 1 . SER 83 83 5156 1 . ASP 84 84 5156 1 . GLY 85 85 5156 1 . LYS 86 86 5156 1 . ILE 87 87 5156 1 . GLU 88 88 5156 1 . MET 89 89 5156 1 . ALA 90 90 5156 1 . GLU 91 91 5156 1 . LEU 92 92 5156 1 . ALA 93 93 5156 1 . GLN 94 94 5156 1 . ILE 95 95 5156 1 . LEU 96 96 5156 1 . PRO 97 97 5156 1 . THR 98 98 5156 1 . GLU 99 99 5156 1 . GLU 100 100 5156 1 . ASN 101 101 5156 1 . PHE 102 102 5156 1 . LEU 103 103 5156 1 . LEU 104 104 5156 1 stop_ save_ save_CA _Entity.Sf_category entity _Entity.Sf_framecode CA _Entity.Entry_ID 5156 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name CA _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 CA _Entity.Nonpolymer_comp_label $chem_comp_CA _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 . CA . 5156 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 5156 _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 $calretinin . 10116 organism . 'Rattus norvegicus' Rat . . Eukaryota Metazoa Rattus norvegicus Sprague-Dawley . . . brain . . . . . . . . . . . . . . . . 5156 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 5156 _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 $calretinin . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . ; YVEF N-terminal tag is the reuslt of extracellular expression from Pichia pastoris, see ref 1. ; . . 5156 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CA _Chem_comp.Entry_ID 5156 _Chem_comp.ID CA _Chem_comp.Provenance . _Chem_comp.Name 'CALCIUM ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code CA _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 CA _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 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Ca _Chem_comp.Formula_weight 40.078 _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 . _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 Thu Jul 21 12:25:57 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 [Ca+2] SMILES ACDLabs 10.04 5156 CA [Ca++] SMILES_CANONICAL CACTVS 3.341 5156 CA [Ca++] SMILES CACTVS 3.341 5156 CA [Ca+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5156 CA [Ca+2] SMILES 'OpenEye OEToolkits' 1.5.0 5156 CA InChI=1S/Ca/q+2 InChI InChI 1.03 5156 CA BHPQYMZQTOCNFJ-UHFFFAOYSA-N InChIKey InChI 1.03 5156 CA 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 calcium 'SYSTEMATIC NAME' ACDLabs 10.04 5156 CA 'calcium(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5156 CA 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 CA . CA . . CA . . N 2 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 5156 CA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5156 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 calretinin [U-15N] . . 1 $calretinin . . 1 . . mM . . . . 5156 1 2 TRIS [U-2H] . . . . . . 50 . . mM . . . . 5156 1 3 NaCl . . . . . . . 25 . . mM . . . . 5156 1 4 CaCl2 . . . . . . . 10 . . mM . . . . 5156 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5156 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 calretinin '[U-13C; U-15N]' . . 1 $calretinin . . 1 . . mM . . . . 5156 2 2 TRIS [U-2H] . . . . . . 50 . . mM . . . . 5156 2 3 NaCl . . . . . . . 25 . . mM . . . . 5156 2 4 CaCl2 . . . . . . . 10 . . mM . . . . 5156 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_1 _Sample_condition_list.Entry_ID 5156 _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 7.7 0.2 n/a 5156 1 temperature 303 1 K 5156 1 stop_ save_ save_sample_cond_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_2 _Sample_condition_list.Entry_ID 5156 _Sample_condition_list.ID 2 _Sample_condition_list.Details 'The pH was adjusted to pH 6.7 and a limited dataset was collected.' loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.7 0.2 n/a 5156 2 temperature 303 1 K 5156 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5156 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5156 _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 Bruker DRX . 500 . . . 5156 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 5156 _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 '(Acq. points / acq. time nucleus Size of processed data (LP/ linear prediction))' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 2 'experiment Dimension 1 Dimension 2 Dimension 3 Bruker pulse program' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 3 '1H -15N HSQC (128 / 90.2 ms 15N 192 LP /512) (512/ 102 ms 1H/1024)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 4 'invieagssi[ref-2; ref-3; ref-4];' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 5 'HNCO (48 / 21.2 ms 13C 72 LP / 128) (34 / 24 ms 15N 52 LP / 128)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 6 '(1024 / 79 ms 1H 1024) hncogs3d.2[ref-5; ref-6];' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 7 'HN(CA)CO (48 / 21.2 ms 13C 72 LP / 128) (34 / 24 ms 15N 52 LP / 128)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 8 '(1024 / 79 ms 1H 1024) hncacogs3d[ref-7; ref-8];' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 9 'HNCA (128 / 25.4 ms 13C 128) (34 / 24 ms 15N 52 LP / 128)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 10 '(1024 / 79 ms 1H 1024) hncags3d.2[ref-5];' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 11 'HN(CO)CA (84 / 59.3 ms 15N 128) (64 / 12.7 ms 13C 96 LP / 128)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 12 '(1024 / 79 ms 1H 1024) [ref-9];' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 13 'HNCACB (64 / 7.27 ms 13C 96 LP / 128) (34 / 24 ms 15N 52 LP / 128)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 14 '(1024 / 79 ms 1H 1024) hncacbgs3d[ref-10; ref-11];' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 15 'CBCANH (52 / 5.91 ms 13C 96 LP / 128) (34 / 24 ms 15N 52 LP / 128)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 16 '(1024 / 79 ms 1H 1024) cbcanhgs3d[ref-10; ref-12; ref-13];' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 17 'CBCA(CO)NH (84 / 59.2 ms 15N 100 LP / 128) (70 / 7.95 ms 13C 100 LP / 128)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 18 'HBHA(CO)NH (76 / 53.5 ms 15N 100 LP / 128) (100 / 30.6 ms 1H 150 LP/ 256)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 19 'HNHA (64 / 45.1 ms 15N 100 LP / 128) (128 / 19.7 ms 1H 192 LP / 256)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 20 '(1024 / 79 ms 1H 1024) [ref-14];' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 21 '(H)CC(CO)NH (84 / 59.2 ms 15N 100 LP / 128) (62 / 7.04 ms 13C 90 LP / 128)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 22 'H(CC)(CO)NH (76 / 53.5 ms 15N 100 LP / 128) (66 / 18.8 ms 1H 96 LP / 128)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 23 'NOESY-HSQC 15N and 13C (104 / 16 ms 1H 128 LP / 256)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 24 '(64 / 7.04 ms 13C 90 LP / 128) (1024 / 79 ms 1H 1024)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 25 noesiisism3d[ref-15]; . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 26 'NOESY-HSQC 15N (104 / 16 ms 1H 128 LP / 256) (64 / 45.1 ms 15N 100 LP / 128)' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 27 '(512 / 102 ms 1H 1024) noesiietf3gsrdf[ref-5].' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5156 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5156 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5156 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5156 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5156 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5156 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_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 . . 2 $sample_2 . 5156 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 16 16 HIS HA H 1 4.37 0.02 . 1 . . . . . . . . 5156 1 2 . 1 1 16 16 HIS HB2 H 1 2.89 0.02 . 2 . . . . . . . . 5156 1 3 . 1 1 16 16 HIS HB3 H 1 3.11 0.02 . 2 . . . . . . . . 5156 1 4 . 1 1 16 16 HIS C C 13 176.0 0.2 . 1 . . . . . . . . 5156 1 5 . 1 1 16 16 HIS CA C 13 56.5 0.2 . 1 . . . . . . . . 5156 1 6 . 1 1 16 16 HIS CB C 13 30.9 0.2 . 1 . . . . . . . . 5156 1 7 . 1 1 17 17 LEU H H 1 7.21 0.02 . 1 . . . . . . . . 5156 1 8 . 1 1 17 17 LEU HA H 1 3.99 0.02 . 1 . . . . . . . . 5156 1 9 . 1 1 17 17 LEU HB2 H 1 0.97 0.02 . 4 . . . . . . . . 5156 1 10 . 1 1 17 17 LEU C C 13 177.2 0.2 . 1 . . . . . . . . 5156 1 11 . 1 1 17 17 LEU CA C 13 55.3 0.2 . 1 . . . . . . . . 5156 1 12 . 1 1 17 17 LEU CB C 13 42.3 0.2 . 1 . . . . . . . . 5156 1 13 . 1 1 17 17 LEU CG C 13 26.5 0.2 . 4 . . . . . . . . 5156 1 14 . 1 1 17 17 LEU CD1 C 13 23.0 0.2 . 4 . . . . . . . . 5156 1 15 . 1 1 17 17 LEU N N 15 122.2 0.2 . 1 . . . . . . . . 5156 1 16 . 1 1 18 18 ALA H H 1 8.35 0.02 . 1 . . . . . . . . 5156 1 17 . 1 1 18 18 ALA HA H 1 4.12 0.02 . 1 . . . . . . . . 5156 1 18 . 1 1 18 18 ALA HB1 H 1 1.38 0.02 . 1 . . . . . . . . 5156 1 19 . 1 1 18 18 ALA HB2 H 1 1.38 0.02 . 1 . . . . . . . . 5156 1 20 . 1 1 18 18 ALA HB3 H 1 1.38 0.02 . 1 . . . . . . . . 5156 1 21 . 1 1 18 18 ALA C C 13 177.8 0.2 . 1 . . . . . . . . 5156 1 22 . 1 1 18 18 ALA CA C 13 53.8 0.2 . 1 . . . . . . . . 5156 1 23 . 1 1 18 18 ALA CB C 13 19.6 0.2 . 1 . . . . . . . . 5156 1 24 . 1 1 18 18 ALA N N 15 121.9 0.2 . 1 . . . . . . . . 5156 1 25 . 1 1 19 19 GLU H H 1 7.47 0.02 . 1 . . . . . . . . 5156 1 26 . 1 1 19 19 GLU HA H 1 4.38 0.02 . 1 . . . . . . . . 5156 1 27 . 1 1 19 19 GLU HB2 H 1 2.23 0.02 . 2 . . . . . . . . 5156 1 28 . 1 1 19 19 GLU HB3 H 1 2.69 0.02 . 2 . . . . . . . . 5156 1 29 . 1 1 19 19 GLU C C 13 174.9 0.2 . 1 . . . . . . . . 5156 1 30 . 1 1 19 19 GLU CA C 13 55.9 0.2 . 1 . . . . . . . . 5156 1 31 . 1 1 19 19 GLU CB C 13 33.0 0.2 . 1 . . . . . . . . 5156 1 32 . 1 1 19 19 GLU CG C 13 36.3 0.2 . 1 . . . . . . . . 5156 1 33 . 1 1 19 19 GLU N N 15 114.0 0.2 . 1 . . . . . . . . 5156 1 34 . 1 1 20 20 LEU H H 1 8.48 0.02 . 1 . . . . . . . . 5156 1 35 . 1 1 20 20 LEU HA H 1 4.80 0.02 . 1 . . . . . . . . 5156 1 36 . 1 1 20 20 LEU C C 13 178.5 0.2 . 1 . . . . . . . . 5156 1 37 . 1 1 20 20 LEU CA C 13 54.6 0.2 . 1 . . . . . . . . 5156 1 38 . 1 1 20 20 LEU CB C 13 45.1 0.2 . 1 . . . . . . . . 5156 1 39 . 1 1 20 20 LEU CG C 13 28.1 0.2 . 4 . . . . . . . . 5156 1 40 . 1 1 20 20 LEU N N 15 123.3 0.2 . 1 . . . . . . . . 5156 1 41 . 1 1 21 21 THR H H 1 8.53 0.02 . 1 . . . . . . . . 5156 1 42 . 1 1 21 21 THR HA H 1 4.40 0.02 . 1 . . . . . . . . 5156 1 43 . 1 1 21 21 THR HB H 1 4.62 0.02 . 1 . . . . . . . . 5156 1 44 . 1 1 21 21 THR HG21 H 1 1.16 0.02 . 1 . . . . . . . . 5156 1 45 . 1 1 21 21 THR HG22 H 1 1.16 0.02 . 1 . . . . . . . . 5156 1 46 . 1 1 21 21 THR HG23 H 1 1.16 0.02 . 1 . . . . . . . . 5156 1 47 . 1 1 21 21 THR C C 13 176.0 0.2 . 1 . . . . . . . . 5156 1 48 . 1 1 21 21 THR CA C 13 60.9 0.2 . 1 . . . . . . . . 5156 1 49 . 1 1 21 21 THR CB C 13 71.1 0.2 . 1 . . . . . . . . 5156 1 50 . 1 1 21 21 THR CG2 C 13 21.7 0.2 . 1 . . . . . . . . 5156 1 51 . 1 1 21 21 THR N N 15 112.4 0.2 . 1 . . . . . . . . 5156 1 52 . 1 1 22 22 ALA H H 1 9.21 0.02 . 1 . . . . . . . . 5156 1 53 . 1 1 22 22 ALA HA H 1 4.02 0.02 . 1 . . . . . . . . 5156 1 54 . 1 1 22 22 ALA HB1 H 1 1.39 0.02 . 1 . . . . . . . . 5156 1 55 . 1 1 22 22 ALA HB2 H 1 1.39 0.02 . 1 . . . . . . . . 5156 1 56 . 1 1 22 22 ALA HB3 H 1 1.39 0.02 . 1 . . . . . . . . 5156 1 57 . 1 1 22 22 ALA C C 13 180.4 0.2 . 1 . . . . . . . . 5156 1 58 . 1 1 22 22 ALA CA C 13 56.3 0.2 . 1 . . . . . . . . 5156 1 59 . 1 1 22 22 ALA CB C 13 18.3 0.2 . 1 . . . . . . . . 5156 1 60 . 1 1 22 22 ALA N N 15 123.7 0.2 . 1 . . . . . . . . 5156 1 61 . 1 1 23 23 SER H H 1 8.36 0.02 . 1 . . . . . . . . 5156 1 62 . 1 1 23 23 SER HA H 1 4.19 0.02 . 1 . . . . . . . . 5156 1 63 . 1 1 23 23 SER HB2 H 1 3.80 0.02 . 2 . . . . . . . . 5156 1 64 . 1 1 23 23 SER C C 13 177.9 0.2 . 1 . . . . . . . . 5156 1 65 . 1 1 23 23 SER CA C 13 61.9 0.2 . 1 . . . . . . . . 5156 1 66 . 1 1 23 23 SER N N 15 111.3 0.2 . 1 . . . . . . . . 5156 1 67 . 1 1 24 24 GLN H H 1 7.55 0.02 . 1 . . . . . . . . 5156 1 68 . 1 1 24 24 GLN HA H 1 3.77 0.02 . 1 . . . . . . . . 5156 1 69 . 1 1 24 24 GLN HB2 H 1 2.12 0.02 . 2 . . . . . . . . 5156 1 70 . 1 1 24 24 GLN HB3 H 1 1.29 0.02 . 2 . . . . . . . . 5156 1 71 . 1 1 24 24 GLN C C 13 178.7 0.2 . 1 . . . . . . . . 5156 1 72 . 1 1 24 24 GLN CA C 13 59.0 0.2 . 1 . . . . . . . . 5156 1 73 . 1 1 24 24 GLN CB C 13 29.1 0.2 . 1 . . . . . . . . 5156 1 74 . 1 1 24 24 GLN CG C 13 33.3 0.2 . 1 . . . . . . . . 5156 1 75 . 1 1 24 24 GLN N N 15 122.3 0.2 . 1 . . . . . . . . 5156 1 76 . 1 1 25 25 PHE H H 1 8.65 0.02 . 1 . . . . . . . . 5156 1 77 . 1 1 25 25 PHE HA H 1 3.89 0.02 . 1 . . . . . . . . 5156 1 78 . 1 1 25 25 PHE HB2 H 1 2.94 0.02 . 2 . . . . . . . . 5156 1 79 . 1 1 25 25 PHE HB3 H 1 3.23 0.02 . 2 . . . . . . . . 5156 1 80 . 1 1 25 25 PHE C C 13 177.0 0.2 . 1 . . . . . . . . 5156 1 81 . 1 1 25 25 PHE CA C 13 62.5 0.2 . 1 . . . . . . . . 5156 1 82 . 1 1 25 25 PHE CB C 13 39.6 0.2 . 1 . . . . . . . . 5156 1 83 . 1 1 25 25 PHE N N 15 119.2 0.2 . 1 . . . . . . . . 5156 1 84 . 1 1 26 26 LEU H H 1 8.25 0.02 . 1 . . . . . . . . 5156 1 85 . 1 1 26 26 LEU HA H 1 3.99 0.02 . 1 . . . . . . . . 5156 1 86 . 1 1 26 26 LEU HB2 H 1 1.69 0.02 . 2 . . . . . . . . 5156 1 87 . 1 1 26 26 LEU HB3 H 1 1.86 0.02 . 2 . . . . . . . . 5156 1 88 . 1 1 26 26 LEU HG H 1 0.95 0.02 . 4 . . . . . . . . 5156 1 89 . 1 1 26 26 LEU C C 13 179.4 0.2 . 1 . . . . . . . . 5156 1 90 . 1 1 26 26 LEU CA C 13 58.2 0.2 . 1 . . . . . . . . 5156 1 91 . 1 1 26 26 LEU CB C 13 41.8 0.2 . 1 . . . . . . . . 5156 1 92 . 1 1 26 26 LEU CG C 13 24.2 0.2 . 4 . . . . . . . . 5156 1 93 . 1 1 26 26 LEU N N 15 118.7 0.2 . 1 . . . . . . . . 5156 1 94 . 1 1 27 27 GLU H H 1 7.91 0.02 . 1 . . . . . . . . 5156 1 95 . 1 1 27 27 GLU HA H 1 3.99 0.02 . 1 . . . . . . . . 5156 1 96 . 1 1 27 27 GLU HB2 H 1 2.15 0.02 . 2 . . . . . . . . 5156 1 97 . 1 1 27 27 GLU HB3 H 1 2.34 0.02 . 2 . . . . . . . . 5156 1 98 . 1 1 27 27 GLU HG2 H 1 2.51 0.02 . 2 . . . . . . . . 5156 1 99 . 1 1 27 27 GLU C C 13 180.5 0.2 . 1 . . . . . . . . 5156 1 100 . 1 1 27 27 GLU CA C 13 60.3 0.2 . 1 . . . . . . . . 5156 1 101 . 1 1 27 27 GLU CB C 13 29.9 0.2 . 1 . . . . . . . . 5156 1 102 . 1 1 27 27 GLU CG C 13 36.9 0.2 . 1 . . . . . . . . 5156 1 103 . 1 1 27 27 GLU N N 15 118.1 0.2 . 1 . . . . . . . . 5156 1 104 . 1 1 28 28 ILE H H 1 8.00 0.02 . 1 . . . . . . . . 5156 1 105 . 1 1 28 28 ILE HA H 1 3.66 0.02 . 1 . . . . . . . . 5156 1 106 . 1 1 28 28 ILE HB H 1 1.01 0.02 . 4 . . . . . . . . 5156 1 107 . 1 1 28 28 ILE C C 13 177.7 0.2 . 1 . . . . . . . . 5156 1 108 . 1 1 28 28 ILE CA C 13 65.3 0.2 . 1 . . . . . . . . 5156 1 109 . 1 1 28 28 ILE CB C 13 37.3 0.2 . 9 . . . . . . . . 5156 1 110 . 1 1 28 28 ILE CG2 C 13 18.1 0.2 . 4 . . . . . . . . 5156 1 111 . 1 1 28 28 ILE N N 15 120.7 0.2 . 1 . . . . . . . . 5156 1 112 . 1 1 29 29 TRP H H 1 8.48 0.02 . 1 . . . . . . . . 5156 1 113 . 1 1 29 29 TRP HA H 1 3.72 0.02 . 1 . . . . . . . . 5156 1 114 . 1 1 29 29 TRP HB2 H 1 2.66 0.02 . 2 . . . . . . . . 5156 1 115 . 1 1 29 29 TRP HB3 H 1 3.14 0.02 . 2 . . . . . . . . 5156 1 116 . 1 1 29 29 TRP HE1 H 1 10.29 0.02 . 1 . . . . . . . . 5156 1 117 . 1 1 29 29 TRP C C 13 176.7 0.2 . 1 . . . . . . . . 5156 1 118 . 1 1 29 29 TRP CA C 13 61.3 0.2 . 1 . . . . . . . . 5156 1 119 . 1 1 29 29 TRP CB C 13 29.0 0.2 . 1 . . . . . . . . 5156 1 120 . 1 1 29 29 TRP N N 15 120.7 0.2 . 1 . . . . . . . . 5156 1 121 . 1 1 29 29 TRP NE1 N 15 129.7 0.2 . 1 . . . . . . . . 5156 1 122 . 1 1 30 30 LYS H H 1 8.35 0.02 . 1 . . . . . . . . 5156 1 123 . 1 1 30 30 LYS HA H 1 3.66 0.02 . 1 . . . . . . . . 5156 1 124 . 1 1 30 30 LYS HB2 H 1 1.81 0.02 . 2 . . . . . . . . 5156 1 125 . 1 1 30 30 LYS C C 13 178.4 0.2 . 1 . . . . . . . . 5156 1 126 . 1 1 30 30 LYS CA C 13 58.9 0.2 . 1 . . . . . . . . 5156 1 127 . 1 1 30 30 LYS CB C 13 32.8 0.2 . 1 . . . . . . . . 5156 1 128 . 1 1 30 30 LYS CG C 13 26.0 0.2 . 4 . . . . . . . . 5156 1 129 . 1 1 30 30 LYS N N 15 113.6 0.2 . 1 . . . . . . . . 5156 1 130 . 1 1 31 31 HIS H H 1 7.59 0.02 . 1 . . . . . . . . 5156 1 131 . 1 1 31 31 HIS HA H 1 3.88 0.02 . 1 . . . . . . . . 5156 1 132 . 1 1 31 31 HIS HB2 H 1 2.85 0.02 . 2 . . . . . . . . 5156 1 133 . 1 1 31 31 HIS C C 13 176.9 0.2 . 1 . . . . . . . . 5156 1 134 . 1 1 31 31 HIS CA C 13 59.7 0.2 . 1 . . . . . . . . 5156 1 135 . 1 1 31 31 HIS CB C 13 30.7 0.2 . 1 . . . . . . . . 5156 1 136 . 1 1 31 31 HIS N N 15 115.6 0.2 . 1 . . . . . . . . 5156 1 137 . 1 1 32 32 PHE H H 1 7.56 0.02 . 1 . . . . . . . . 5156 1 138 . 1 1 32 32 PHE HA H 1 4.19 0.02 . 1 . . . . . . . . 5156 1 139 . 1 1 32 32 PHE HB2 H 1 2.34 0.02 . 2 . . . . . . . . 5156 1 140 . 1 1 32 32 PHE HB3 H 1 2.81 0.02 . 2 . . . . . . . . 5156 1 141 . 1 1 32 32 PHE C C 13 178.1 0.2 . 1 . . . . . . . . 5156 1 142 . 1 1 32 32 PHE CA C 13 61.9 0.2 . 1 . . . . . . . . 5156 1 143 . 1 1 32 32 PHE CB C 13 40.1 0.2 . 1 . . . . . . . . 5156 1 144 . 1 1 32 32 PHE N N 15 112.1 0.2 . 1 . . . . . . . . 5156 1 145 . 1 1 33 33 ASP H H 1 8.13 0.02 . 1 . . . . . . . . 5156 1 146 . 1 1 33 33 ASP HA H 1 4.49 0.02 . 1 . . . . . . . . 5156 1 147 . 1 1 33 33 ASP HB2 H 1 1.79 0.02 . 2 . . . . . . . . 5156 1 148 . 1 1 33 33 ASP HB3 H 1 0.77 0.02 . 2 . . . . . . . . 5156 1 149 . 1 1 33 33 ASP C C 13 178.1 0.2 . 1 . . . . . . . . 5156 1 150 . 1 1 33 33 ASP CA C 13 52.7 0.2 . 1 . . . . . . . . 5156 1 151 . 1 1 33 33 ASP CB C 13 36.3 0.2 . 1 . . . . . . . . 5156 1 152 . 1 1 33 33 ASP N N 15 120.2 0.2 . 1 . . . . . . . . 5156 1 153 . 1 1 34 34 ALA H H 1 7.27 0.02 . 1 . . . . . . . . 5156 1 154 . 1 1 34 34 ALA HA H 1 3.73 0.02 . 1 . . . . . . . . 5156 1 155 . 1 1 34 34 ALA HB1 H 1 1.36 0.02 . 1 . . . . . . . . 5156 1 156 . 1 1 34 34 ALA HB2 H 1 1.36 0.02 . 1 . . . . . . . . 5156 1 157 . 1 1 34 34 ALA HB3 H 1 1.36 0.02 . 1 . . . . . . . . 5156 1 158 . 1 1 34 34 ALA C C 13 179.2 0.2 . 1 . . . . . . . . 5156 1 159 . 1 1 34 34 ALA CA C 13 55.3 0.2 . 1 . . . . . . . . 5156 1 160 . 1 1 34 34 ALA CB C 13 19.3 0.2 . 1 . . . . . . . . 5156 1 161 . 1 1 34 34 ALA N N 15 126.3 0.2 . 1 . . . . . . . . 5156 1 162 . 1 1 35 35 ASP H H 1 8.07 0.02 . 1 . . . . . . . . 5156 1 163 . 1 1 35 35 ASP HA H 1 4.51 0.02 . 1 . . . . . . . . 5156 1 164 . 1 1 35 35 ASP HB2 H 1 2.59 0.02 . 2 . . . . . . . . 5156 1 165 . 1 1 35 35 ASP HB3 H 1 3.04 0.02 . 2 . . . . . . . . 5156 1 166 . 1 1 35 35 ASP C C 13 178.2 0.2 . 1 . . . . . . . . 5156 1 167 . 1 1 35 35 ASP CA C 13 52.8 0.2 . 1 . . . . . . . . 5156 1 168 . 1 1 35 35 ASP CB C 13 39.9 0.2 . 1 . . . . . . . . 5156 1 169 . 1 1 35 35 ASP N N 15 113.0 0.2 . 1 . . . . . . . . 5156 1 170 . 1 1 36 36 GLY H H 1 7.81 0.02 . 1 . . . . . . . . 5156 1 171 . 1 1 36 36 GLY HA2 H 1 3.78 0.02 . 2 . . . . . . . . 5156 1 172 . 1 1 36 36 GLY C C 13 175.7 0.2 . 1 . . . . . . . . 5156 1 173 . 1 1 36 36 GLY CA C 13 47.5 0.2 . 1 . . . . . . . . 5156 1 174 . 1 1 36 36 GLY N N 15 109.1 0.2 . 1 . . . . . . . . 5156 1 175 . 1 1 37 37 ASN H H 1 8.29 0.02 . 1 . . . . . . . . 5156 1 176 . 1 1 37 37 ASN HA H 1 4.61 0.02 . 1 . . . . . . . . 5156 1 177 . 1 1 37 37 ASN HB2 H 1 2.54 0.02 . 2 . . . . . . . . 5156 1 178 . 1 1 37 37 ASN HB3 H 1 3.33 0.02 . 2 . . . . . . . . 5156 1 179 . 1 1 37 37 ASN C C 13 176.7 0.2 . 1 . . . . . . . . 5156 1 180 . 1 1 37 37 ASN CA C 13 53.2 0.2 . 1 . . . . . . . . 5156 1 181 . 1 1 37 37 ASN CB C 13 38.8 0.2 . 1 . . . . . . . . 5156 1 182 . 1 1 37 37 ASN N N 15 119.2 0.2 . 1 . . . . . . . . 5156 1 183 . 1 1 38 38 GLY H H 1 10.38 0.02 . 1 . . . . . . . . 5156 1 184 . 1 1 38 38 GLY HA2 H 1 4.16 0.02 . 2 . . . . . . . . 5156 1 185 . 1 1 38 38 GLY HA3 H 1 3.62 0.02 . 2 . . . . . . . . 5156 1 186 . 1 1 38 38 GLY C C 13 173.1 0.2 . 1 . . . . . . . . 5156 1 187 . 1 1 38 38 GLY CA C 13 45.6 0.2 . 1 . . . . . . . . 5156 1 188 . 1 1 38 38 GLY N N 15 111.9 0.2 . 1 . . . . . . . . 5156 1 189 . 1 1 39 39 TYR H H 1 7.70 0.02 . 1 . . . . . . . . 5156 1 190 . 1 1 39 39 TYR HA H 1 5.08 0.02 . 1 . . . . . . . . 5156 1 191 . 1 1 39 39 TYR HB2 H 1 2.56 0.02 . 2 . . . . . . . . 5156 1 192 . 1 1 39 39 TYR C C 13 175.2 0.2 . 1 . . . . . . . . 5156 1 193 . 1 1 39 39 TYR CA C 13 57.4 0.2 . 1 . . . . . . . . 5156 1 194 . 1 1 39 39 TYR CB C 13 43.7 0.2 . 1 . . . . . . . . 5156 1 195 . 1 1 39 39 TYR N N 15 115.2 0.2 . 1 . . . . . . . . 5156 1 196 . 1 1 40 40 ILE H H 1 9.81 0.02 . 1 . . . . . . . . 5156 1 197 . 1 1 40 40 ILE HA H 1 4.50 0.02 . 1 . . . . . . . . 5156 1 198 . 1 1 40 40 ILE HB H 1 1.76 0.02 . 1 . . . . . . . . 5156 1 199 . 1 1 40 40 ILE HG21 H 1 0.51 0.02 . 4 . . . . . . . . 5156 1 200 . 1 1 40 40 ILE HG22 H 1 0.51 0.02 . 4 . . . . . . . . 5156 1 201 . 1 1 40 40 ILE HG23 H 1 0.51 0.02 . 4 . . . . . . . . 5156 1 202 . 1 1 40 40 ILE C C 13 174.9 0.2 . 1 . . . . . . . . 5156 1 203 . 1 1 40 40 ILE CA C 13 62.2 0.2 . 1 . . . . . . . . 5156 1 204 . 1 1 40 40 ILE CB C 13 37.9 0.2 . 1 . . . . . . . . 5156 1 205 . 1 1 40 40 ILE CG1 C 13 17.6 0.2 . 4 . . . . . . . . 5156 1 206 . 1 1 40 40 ILE N N 15 128.0 0.2 . 1 . . . . . . . . 5156 1 207 . 1 1 41 41 GLU H H 1 9.00 0.02 . 1 . . . . . . . . 5156 1 208 . 1 1 41 41 GLU HA H 1 5.01 0.02 . 1 . . . . . . . . 5156 1 209 . 1 1 41 41 GLU C C 13 176.6 0.2 . 1 . . . . . . . . 5156 1 210 . 1 1 41 41 GLU CA C 13 54.6 0.2 . 1 . . . . . . . . 5156 1 211 . 1 1 41 41 GLU CB C 13 33.6 0.2 . 1 . . . . . . . . 5156 1 212 . 1 1 41 41 GLU N N 15 125.1 0.2 . 1 . . . . . . . . 5156 1 213 . 1 1 42 42 GLY H H 1 9.47 0.02 . 1 . . . . . . . . 5156 1 214 . 1 1 42 42 GLY CA C 13 47.2 0.2 . 1 . . . . . . . . 5156 1 215 . 1 1 42 42 GLY N N 15 112.3 0.2 . 1 . . . . . . . . 5156 1 216 . 1 1 44 44 GLU HA H 1 4.35 0.02 . 1 . . . . . . . . 5156 1 217 . 1 1 44 44 GLU HB2 H 1 2.41 0.02 . 2 . . . . . . . . 5156 1 218 . 1 1 44 44 GLU HB3 H 1 2.69 0.02 . 2 . . . . . . . . 5156 1 219 . 1 1 44 44 GLU HG2 H 1 2.75 0.02 . 2 . . . . . . . . 5156 1 220 . 1 1 44 44 GLU C C 13 180.1 0.2 . 1 . . . . . . . . 5156 1 221 . 1 1 44 44 GLU CA C 13 58.4 0.2 . 1 . . . . . . . . 5156 1 222 . 1 1 44 44 GLU CB C 13 30.7 0.2 . 1 . . . . . . . . 5156 1 223 . 1 1 44 44 GLU CG C 13 35.2 0.2 . 1 . . . . . . . . 5156 1 224 . 1 1 45 45 LEU H H 1 6.84 0.02 . 1 . . . . . . . . 5156 1 225 . 1 1 45 45 LEU HA H 1 3.92 0.02 . 1 . . . . . . . . 5156 1 226 . 1 1 45 45 LEU HB2 H 1 2.07 0.02 . 2 . . . . . . . . 5156 1 227 . 1 1 45 45 LEU HB3 H 1 1.22 0.02 . 2 . . . . . . . . 5156 1 228 . 1 1 45 45 LEU HD11 H 1 1.12 0.02 . 4 . . . . . . . . 5156 1 229 . 1 1 45 45 LEU HD12 H 1 1.12 0.02 . 4 . . . . . . . . 5156 1 230 . 1 1 45 45 LEU HD13 H 1 1.12 0.02 . 4 . . . . . . . . 5156 1 231 . 1 1 45 45 LEU C C 13 178.4 0.2 . 1 . . . . . . . . 5156 1 232 . 1 1 45 45 LEU CA C 13 57.2 0.2 . 1 . . . . . . . . 5156 1 233 . 1 1 45 45 LEU CB C 13 42.3 0.2 . 1 . . . . . . . . 5156 1 234 . 1 1 45 45 LEU CG C 13 26.1 0.2 . 4 . . . . . . . . 5156 1 235 . 1 1 45 45 LEU CD1 C 13 23.4 0.2 . 4 . . . . . . . . 5156 1 236 . 1 1 45 45 LEU N N 15 119.3 0.2 . 1 . . . . . . . . 5156 1 237 . 1 1 46 46 GLU H H 1 7.58 0.02 . 1 . . . . . . . . 5156 1 238 . 1 1 46 46 GLU HA H 1 3.99 0.02 . 1 . . . . . . . . 5156 1 239 . 1 1 46 46 GLU HB2 H 1 2.12 0.02 . 2 . . . . . . . . 5156 1 240 . 1 1 46 46 GLU C C 13 178.8 0.2 . 1 . . . . . . . . 5156 1 241 . 1 1 46 46 GLU CA C 13 60.6 0.2 . 1 . . . . . . . . 5156 1 242 . 1 1 46 46 GLU CB C 13 29.8 0.2 . 1 . . . . . . . . 5156 1 243 . 1 1 46 46 GLU CG C 13 36.8 0.2 . 1 . . . . . . . . 5156 1 244 . 1 1 46 46 GLU N N 15 118.9 0.2 . 1 . . . . . . . . 5156 1 245 . 1 1 47 47 ASN H H 1 8.11 0.02 . 1 . . . . . . . . 5156 1 246 . 1 1 47 47 ASN HA H 1 4.50 0.02 . 1 . . . . . . . . 5156 1 247 . 1 1 47 47 ASN HB2 H 1 3.12 0.02 . 2 . . . . . . . . 5156 1 248 . 1 1 47 47 ASN C C 13 177.1 0.2 . 1 . . . . . . . . 5156 1 249 . 1 1 47 47 ASN CA C 13 56.8 0.2 . 1 . . . . . . . . 5156 1 250 . 1 1 47 47 ASN CB C 13 39.0 0.2 . 1 . . . . . . . . 5156 1 251 . 1 1 47 47 ASN N N 15 116.4 0.2 . 1 . . . . . . . . 5156 1 252 . 1 1 48 48 PHE H H 1 8.49 0.02 . 1 . . . . . . . . 5156 1 253 . 1 1 48 48 PHE HA H 1 3.46 0.02 . 1 . . . . . . . . 5156 1 254 . 1 1 48 48 PHE HB2 H 1 2.61 0.02 . 2 . . . . . . . . 5156 1 255 . 1 1 48 48 PHE HB3 H 1 2.77 0.02 . 2 . . . . . . . . 5156 1 256 . 1 1 48 48 PHE C C 13 175.9 0.2 . 1 . . . . . . . . 5156 1 257 . 1 1 48 48 PHE CA C 13 61.3 0.2 . 1 . . . . . . . . 5156 1 258 . 1 1 48 48 PHE CB C 13 39.0 0.2 . 1 . . . . . . . . 5156 1 259 . 1 1 48 48 PHE N N 15 118.4 0.2 . 1 . . . . . . . . 5156 1 260 . 1 1 49 49 PHE H H 1 8.71 0.02 . 1 . . . . . . . . 5156 1 261 . 1 1 49 49 PHE HA H 1 3.27 0.02 . 1 . . . . . . . . 5156 1 262 . 1 1 49 49 PHE HB2 H 1 2.62 0.02 . 2 . . . . . . . . 5156 1 263 . 1 1 49 49 PHE HB3 H 1 2.86 0.02 . 2 . . . . . . . . 5156 1 264 . 1 1 49 49 PHE C C 13 177.4 0.2 . 1 . . . . . . . . 5156 1 265 . 1 1 49 49 PHE CA C 13 62.2 0.2 . 1 . . . . . . . . 5156 1 266 . 1 1 49 49 PHE CB C 13 39.5 0.2 . 1 . . . . . . . . 5156 1 267 . 1 1 49 49 PHE N N 15 118.1 0.2 . 1 . . . . . . . . 5156 1 268 . 1 1 50 50 GLN H H 1 8.18 0.02 . 1 . . . . . . . . 5156 1 269 . 1 1 50 50 GLN HA H 1 3.80 0.02 . 1 . . . . . . . . 5156 1 270 . 1 1 50 50 GLN HB2 H 1 2.08 0.02 . 2 . . . . . . . . 5156 1 271 . 1 1 50 50 GLN HB3 H 1 2.27 0.02 . 2 . . . . . . . . 5156 1 272 . 1 1 50 50 GLN HG2 H 1 2.40 0.02 . 2 . . . . . . . . 5156 1 273 . 1 1 50 50 GLN C C 13 179.8 0.2 . 1 . . . . . . . . 5156 1 274 . 1 1 50 50 GLN CA C 13 59.7 0.2 . 1 . . . . . . . . 5156 1 275 . 1 1 50 50 GLN CB C 13 28.9 0.2 . 1 . . . . . . . . 5156 1 276 . 1 1 50 50 GLN CG C 13 34.6 0.2 . 1 . . . . . . . . 5156 1 277 . 1 1 50 50 GLN N N 15 116.2 0.2 . 1 . . . . . . . . 5156 1 278 . 1 1 51 51 GLU H H 1 8.10 0.02 . 1 . . . . . . . . 5156 1 279 . 1 1 51 51 GLU HA H 1 3.98 0.02 . 1 . . . . . . . . 5156 1 280 . 1 1 51 51 GLU HB2 H 1 1.86 0.02 . 2 . . . . . . . . 5156 1 281 . 1 1 51 51 GLU HB3 H 1 2.04 0.02 . 2 . . . . . . . . 5156 1 282 . 1 1 51 51 GLU C C 13 179.8 0.2 . 1 . . . . . . . . 5156 1 283 . 1 1 51 51 GLU CA C 13 58.9 0.2 . 1 . . . . . . . . 5156 1 284 . 1 1 51 51 GLU CB C 13 28.8 0.2 . 1 . . . . . . . . 5156 1 285 . 1 1 51 51 GLU CG C 13 36.0 0.2 . 1 . . . . . . . . 5156 1 286 . 1 1 51 51 GLU N N 15 118.2 0.2 . 1 . . . . . . . . 5156 1 287 . 1 1 52 52 LEU H H 1 8.52 0.02 . 1 . . . . . . . . 5156 1 288 . 1 1 52 52 LEU HA H 1 3.58 0.02 . 1 . . . . . . . . 5156 1 289 . 1 1 52 52 LEU HB2 H 1 1.23 0.02 . 2 . . . . . . . . 5156 1 290 . 1 1 52 52 LEU HG H 1 0.61 0.02 . 4 . . . . . . . . 5156 1 291 . 1 1 52 52 LEU C C 13 178.7 0.2 . 1 . . . . . . . . 5156 1 292 . 1 1 52 52 LEU CA C 13 58.5 0.2 . 1 . . . . . . . . 5156 1 293 . 1 1 52 52 LEU CB C 13 41.7 0.2 . 1 . . . . . . . . 5156 1 294 . 1 1 52 52 LEU CG C 13 26.4 0.2 . 4 . . . . . . . . 5156 1 295 . 1 1 52 52 LEU CD1 C 13 23.9 0.2 . 9 . . . . . . . . 5156 1 296 . 1 1 52 52 LEU N N 15 123.9 0.2 . 1 . . . . . . . . 5156 1 297 . 1 1 53 53 GLU H H 1 7.93 0.02 . 1 . . . . . . . . 5156 1 298 . 1 1 53 53 GLU HA H 1 3.68 0.02 . 1 . . . . . . . . 5156 1 299 . 1 1 53 53 GLU HB2 H 1 1.65 0.02 . 2 . . . . . . . . 5156 1 300 . 1 1 53 53 GLU C C 13 179.7 0.2 . 1 . . . . . . . . 5156 1 301 . 1 1 53 53 GLU CA C 13 59.7 0.2 . 1 . . . . . . . . 5156 1 302 . 1 1 53 53 GLU CB C 13 29.6 0.2 . 1 . . . . . . . . 5156 1 303 . 1 1 53 53 GLU CG C 13 36.8 0.2 . 9 . . . . . . . . 5156 1 304 . 1 1 53 53 GLU N N 15 117.5 0.2 . 1 . . . . . . . . 5156 1 305 . 1 1 54 54 LYS H H 1 7.54 0.02 . 1 . . . . . . . . 5156 1 306 . 1 1 54 54 LYS HA H 1 3.85 0.02 . 1 . . . . . . . . 5156 1 307 . 1 1 54 54 LYS HB2 H 1 1.69 0.02 . 9 . . . . . . . . 5156 1 308 . 1 1 54 54 LYS HG2 H 1 1.39 0.02 . 9 . . . . . . . . 5156 1 309 . 1 1 54 54 LYS C C 13 179.2 0.2 . 1 . . . . . . . . 5156 1 310 . 1 1 54 54 LYS CA C 13 59.6 0.2 . 1 . . . . . . . . 5156 1 311 . 1 1 54 54 LYS CB C 13 33.0 0.2 . 1 . . . . . . . . 5156 1 312 . 1 1 54 54 LYS N N 15 117.8 0.2 . 1 . . . . . . . . 5156 1 313 . 1 1 55 55 ALA H H 1 7.88 0.02 . 1 . . . . . . . . 5156 1 314 . 1 1 55 55 ALA HA H 1 4.09 0.02 . 1 . . . . . . . . 5156 1 315 . 1 1 55 55 ALA HB1 H 1 1.33 0.02 . 1 . . . . . . . . 5156 1 316 . 1 1 55 55 ALA HB2 H 1 1.33 0.02 . 1 . . . . . . . . 5156 1 317 . 1 1 55 55 ALA HB3 H 1 1.33 0.02 . 1 . . . . . . . . 5156 1 318 . 1 1 55 55 ALA C C 13 179.8 0.2 . 1 . . . . . . . . 5156 1 319 . 1 1 55 55 ALA CA C 13 54.4 0.2 . 1 . . . . . . . . 5156 1 320 . 1 1 55 55 ALA CB C 13 20.1 0.2 . 1 . . . . . . . . 5156 1 321 . 1 1 55 55 ALA N N 15 120.1 0.2 . 1 . . . . . . . . 5156 1 322 . 1 1 56 56 ARG H H 1 7.99 0.02 . 1 . . . . . . . . 5156 1 323 . 1 1 56 56 ARG HA H 1 4.34 0.02 . 1 . . . . . . . . 5156 1 324 . 1 1 56 56 ARG C C 13 180.2 0.2 . 9 . . . . . . . . 5156 1 325 . 1 1 56 56 ARG CA C 13 57.2 0.2 . 1 . . . . . . . . 5156 1 326 . 1 1 56 56 ARG CB C 13 30.9 0.2 . 9 . . . . . . . . 5156 1 327 . 1 1 56 56 ARG N N 15 115.8 0.2 . 1 . . . . . . . . 5156 1 328 . 1 1 68 68 PHE HB2 H 1 3.16 0.02 . 4 . . . . . . . . 5156 1 329 . 1 1 68 68 PHE C C 13 177.1 0.2 . 1 . . . . . . . . 5156 1 330 . 1 1 68 68 PHE CA C 13 62.2 0.2 . 1 . . . . . . . . 5156 1 331 . 1 1 68 68 PHE CB C 13 39.6 0.2 . 1 . . . . . . . . 5156 1 332 . 1 1 69 69 GLY H H 1 8.62 0.02 . 1 . . . . . . . . 5156 1 333 . 1 1 69 69 GLY HA2 H 1 3.87 0.02 . 2 . . . . . . . . 5156 1 334 . 1 1 69 69 GLY C C 13 177.4 0.2 . 1 . . . . . . . . 5156 1 335 . 1 1 69 69 GLY CA C 13 47.5 0.2 . 1 . . . . . . . . 5156 1 336 . 1 1 69 69 GLY N N 15 106.0 0.2 . 1 . . . . . . . . 5156 1 337 . 1 1 70 70 GLU H H 1 7.90 0.02 . 1 . . . . . . . . 5156 1 338 . 1 1 70 70 GLU HA H 1 4.19 0.02 . 1 . . . . . . . . 5156 1 339 . 1 1 70 70 GLU C C 13 179.0 0.2 . 1 . . . . . . . . 5156 1 340 . 1 1 70 70 GLU CA C 13 59.3 0.2 . 1 . . . . . . . . 5156 1 341 . 1 1 70 70 GLU CB C 13 30.0 0.2 . 1 . . . . . . . . 5156 1 342 . 1 1 70 70 GLU N N 15 121.7 0.2 . 1 . . . . . . . . 5156 1 343 . 1 1 72 72 MET HA H 1 4.27 0.02 . 9 . . . . . . . . 5156 1 344 . 1 1 72 72 MET C C 13 178.1 0.2 . 1 . . . . . . . . 5156 1 345 . 1 1 72 72 MET CA C 13 58.4 0.2 . 1 . . . . . . . . 5156 1 346 . 1 1 72 72 MET CB C 13 31.9 0.2 . 1 . . . . . . . . 5156 1 347 . 1 1 73 73 LYS H H 1 7.67 0.02 . 1 . . . . . . . . 5156 1 348 . 1 1 73 73 LYS HA H 1 3.89 0.02 . 1 . . . . . . . . 5156 1 349 . 1 1 73 73 LYS HB2 H 1 1.81 0.02 . 2 . . . . . . . . 5156 1 350 . 1 1 73 73 LYS HG2 H 1 1.48 0.02 . 4 . . . . . . . . 5156 1 351 . 1 1 73 73 LYS C C 13 179.8 0.2 . 1 . . . . . . . . 5156 1 352 . 1 1 73 73 LYS CA C 13 60.0 0.2 . 1 . . . . . . . . 5156 1 353 . 1 1 73 73 LYS CB C 13 32.2 0.2 . 1 . . . . . . . . 5156 1 354 . 1 1 73 73 LYS CG C 13 25.3 0.2 . 4 . . . . . . . . 5156 1 355 . 1 1 73 73 LYS CD C 13 29.5 0.2 . 4 . . . . . . . . 5156 1 356 . 1 1 73 73 LYS CE C 13 42.3 0.2 . 9 . . . . . . . . 5156 1 357 . 1 1 73 73 LYS N N 15 119.4 0.2 . 1 . . . . . . . . 5156 1 358 . 1 1 74 74 GLU H H 1 7.81 0.02 . 1 . . . . . . . . 5156 1 359 . 1 1 74 74 GLU HA H 1 3.92 0.02 . 1 . . . . . . . . 5156 1 360 . 1 1 74 74 GLU C C 13 179.0 0.2 . 1 . . . . . . . . 5156 1 361 . 1 1 74 74 GLU CA C 13 60.0 0.2 . 1 . . . . . . . . 5156 1 362 . 1 1 74 74 GLU CB C 13 30.0 0.2 . 1 . . . . . . . . 5156 1 363 . 1 1 74 74 GLU CG C 13 36.9 0.2 . 1 . . . . . . . . 5156 1 364 . 1 1 74 74 GLU N N 15 119.8 0.2 . 1 . . . . . . . . 5156 1 365 . 1 1 75 75 PHE H H 1 8.03 0.02 . 1 . . . . . . . . 5156 1 366 . 1 1 75 75 PHE HA H 1 4.26 0.02 . 1 . . . . . . . . 5156 1 367 . 1 1 75 75 PHE HB2 H 1 3.11 0.02 . 2 . . . . . . . . 5156 1 368 . 1 1 75 75 PHE C C 13 177.9 0.2 . 1 . . . . . . . . 5156 1 369 . 1 1 75 75 PHE CA C 13 61.6 0.2 . 1 . . . . . . . . 5156 1 370 . 1 1 75 75 PHE CB C 13 39.8 0.2 . 1 . . . . . . . . 5156 1 371 . 1 1 75 75 PHE N N 15 121.1 0.2 . 1 . . . . . . . . 5156 1 372 . 1 1 76 76 MET H H 1 8.49 0.02 . 1 . . . . . . . . 5156 1 373 . 1 1 76 76 MET HA H 1 4.39 0.02 . 1 . . . . . . . . 5156 1 374 . 1 1 76 76 MET HB2 H 1 2.13 0.02 . 2 . . . . . . . . 5156 1 375 . 1 1 76 76 MET HG2 H 1 2.68 0.02 . 4 . . . . . . . . 5156 1 376 . 1 1 76 76 MET HG3 H 1 2.88 0.02 . 4 . . . . . . . . 5156 1 377 . 1 1 76 76 MET C C 13 180.1 0.2 . 1 . . . . . . . . 5156 1 378 . 1 1 76 76 MET CA C 13 56.7 0.2 . 1 . . . . . . . . 5156 1 379 . 1 1 76 76 MET CB C 13 31.0 0.2 . 1 . . . . . . . . 5156 1 380 . 1 1 76 76 MET N N 15 117.1 0.2 . 1 . . . . . . . . 5156 1 381 . 1 1 77 77 GLN H H 1 8.26 0.02 . 1 . . . . . . . . 5156 1 382 . 1 1 77 77 GLN HA H 1 3.88 0.02 . 1 . . . . . . . . 5156 1 383 . 1 1 77 77 GLN HB2 H 1 1.99 0.02 . 2 . . . . . . . . 5156 1 384 . 1 1 77 77 GLN HB3 H 1 2.10 0.02 . 2 . . . . . . . . 5156 1 385 . 1 1 77 77 GLN HG2 H 1 2.33 0.02 . 2 . . . . . . . . 5156 1 386 . 1 1 77 77 GLN C C 13 178.4 0.2 . 1 . . . . . . . . 5156 1 387 . 1 1 77 77 GLN CA C 13 59.2 0.2 . 1 . . . . . . . . 5156 1 388 . 1 1 77 77 GLN CB C 13 28.4 0.2 . 1 . . . . . . . . 5156 1 389 . 1 1 77 77 GLN CG C 13 34.2 0.2 . 1 . . . . . . . . 5156 1 390 . 1 1 77 77 GLN N N 15 119.6 0.2 . 1 . . . . . . . . 5156 1 391 . 1 1 78 78 LYS H H 1 7.31 0.02 . 1 . . . . . . . . 5156 1 392 . 1 1 78 78 LYS HA H 1 3.79 0.02 . 1 . . . . . . . . 5156 1 393 . 1 1 78 78 LYS HB2 H 1 0.93 0.02 . 2 . . . . . . . . 5156 1 394 . 1 1 78 78 LYS HB3 H 1 1.28 0.02 . 2 . . . . . . . . 5156 1 395 . 1 1 78 78 LYS C C 13 178.8 0.2 . 1 . . . . . . . . 5156 1 396 . 1 1 78 78 LYS CA C 13 59.0 0.2 . 1 . . . . . . . . 5156 1 397 . 1 1 78 78 LYS CB C 13 33.2 0.2 . 1 . . . . . . . . 5156 1 398 . 1 1 78 78 LYS CG C 13 25.0 0.2 . 4 . . . . . . . . 5156 1 399 . 1 1 78 78 LYS CD C 13 29.7 0.2 . 4 . . . . . . . . 5156 1 400 . 1 1 78 78 LYS CE C 13 42.2 0.2 . 4 . . . . . . . . 5156 1 401 . 1 1 78 78 LYS N N 15 116.2 0.2 . 1 . . . . . . . . 5156 1 402 . 1 1 79 79 TYR H H 1 7.76 0.02 . 1 . . . . . . . . 5156 1 403 . 1 1 79 79 TYR HA H 1 4.68 0.02 . 1 . . . . . . . . 5156 1 404 . 1 1 79 79 TYR HB2 H 1 1.98 0.02 . 2 . . . . . . . . 5156 1 405 . 1 1 79 79 TYR HB3 H 1 2.86 0.02 . 2 . . . . . . . . 5156 1 406 . 1 1 79 79 TYR C C 13 177.0 0.2 . 1 . . . . . . . . 5156 1 407 . 1 1 79 79 TYR CA C 13 59.2 0.2 . 1 . . . . . . . . 5156 1 408 . 1 1 79 79 TYR CB C 13 40.5 0.2 . 1 . . . . . . . . 5156 1 409 . 1 1 79 79 TYR N N 15 112.7 0.2 . 1 . . . . . . . . 5156 1 410 . 1 1 80 80 ASP H H 1 8.84 0.02 . 1 . . . . . . . . 5156 1 411 . 1 1 80 80 ASP HA H 1 4.82 0.02 . 1 . . . . . . . . 5156 1 412 . 1 1 80 80 ASP HB2 H 1 2.45 0.02 . 2 . . . . . . . . 5156 1 413 . 1 1 80 80 ASP HB3 H 1 3.29 0.02 . 2 . . . . . . . . 5156 1 414 . 1 1 80 80 ASP C C 13 178.5 0.2 . 1 . . . . . . . . 5156 1 415 . 1 1 80 80 ASP CA C 13 53.1 0.2 . 1 . . . . . . . . 5156 1 416 . 1 1 80 80 ASP CB C 13 39.1 0.2 . 1 . . . . . . . . 5156 1 417 . 1 1 80 80 ASP N N 15 119.8 0.2 . 1 . . . . . . . . 5156 1 418 . 1 1 81 81 LYS H H 1 7.71 0.02 . 1 . . . . . . . . 5156 1 419 . 1 1 81 81 LYS HA H 1 3.97 0.02 . 1 . . . . . . . . 5156 1 420 . 1 1 81 81 LYS HB2 H 1 1.90 0.02 . 2 . . . . . . . . 5156 1 421 . 1 1 81 81 LYS HG2 H 1 1.58 0.02 . 4 . . . . . . . . 5156 1 422 . 1 1 81 81 LYS C C 13 177.9 0.2 . 1 . . . . . . . . 5156 1 423 . 1 1 81 81 LYS CA C 13 58.6 0.2 . 1 . . . . . . . . 5156 1 424 . 1 1 81 81 LYS CB C 13 32.8 0.2 . 1 . . . . . . . . 5156 1 425 . 1 1 81 81 LYS N N 15 125.4 0.2 . 1 . . . . . . . . 5156 1 426 . 1 1 82 82 ASN H H 1 7.98 0.02 . 1 . . . . . . . . 5156 1 427 . 1 1 82 82 ASN HA H 1 4.81 0.02 . 1 . . . . . . . . 5156 1 428 . 1 1 82 82 ASN HB2 H 1 2.74 0.02 . 2 . . . . . . . . 5156 1 429 . 1 1 82 82 ASN HB3 H 1 3.22 0.02 . 2 . . . . . . . . 5156 1 430 . 1 1 82 82 ASN C C 13 175.1 0.2 . 1 . . . . . . . . 5156 1 431 . 1 1 82 82 ASN CA C 13 51.7 0.2 . 1 . . . . . . . . 5156 1 432 . 1 1 82 82 ASN CB C 13 37.2 0.2 . 1 . . . . . . . . 5156 1 433 . 1 1 82 82 ASN N N 15 112.8 0.2 . 1 . . . . . . . . 5156 1 434 . 1 1 83 83 SER H H 1 7.74 0.02 . 1 . . . . . . . . 5156 1 435 . 1 1 83 83 SER HA H 1 3.92 0.02 . 1 . . . . . . . . 5156 1 436 . 1 1 83 83 SER HB2 H 1 3.76 0.02 . 2 . . . . . . . . 5156 1 437 . 1 1 83 83 SER C C 13 174.2 0.2 . 1 . . . . . . . . 5156 1 438 . 1 1 83 83 SER CA C 13 59.6 0.2 . 1 . . . . . . . . 5156 1 439 . 1 1 83 83 SER CB C 13 61.8 0.2 . 1 . . . . . . . . 5156 1 440 . 1 1 83 83 SER N N 15 111.5 0.2 . 1 . . . . . . . . 5156 1 441 . 1 1 84 84 ASP H H 1 8.22 0.02 . 1 . . . . . . . . 5156 1 442 . 1 1 84 84 ASP HA H 1 4.61 0.02 . 1 . . . . . . . . 5156 1 443 . 1 1 84 84 ASP HB2 H 1 2.35 0.02 . 2 . . . . . . . . 5156 1 444 . 1 1 84 84 ASP HB3 H 1 2.90 0.02 . 2 . . . . . . . . 5156 1 445 . 1 1 84 84 ASP C C 13 178.5 0.2 . 1 . . . . . . . . 5156 1 446 . 1 1 84 84 ASP CA C 13 52.8 0.2 . 1 . . . . . . . . 5156 1 447 . 1 1 84 84 ASP CB C 13 40.9 0.2 . 1 . . . . . . . . 5156 1 448 . 1 1 84 84 ASP N N 15 117.3 0.2 . 1 . . . . . . . . 5156 1 449 . 1 1 85 85 GLY H H 1 10.61 0.02 . 1 . . . . . . . . 5156 1 450 . 1 1 85 85 GLY HA2 H 1 3.99 0.02 . 2 . . . . . . . . 5156 1 451 . 1 1 85 85 GLY HA3 H 1 3.36 0.02 . 2 . . . . . . . . 5156 1 452 . 1 1 85 85 GLY C C 13 173.3 0.2 . 1 . . . . . . . . 5156 1 453 . 1 1 85 85 GLY CA C 13 46.2 0.2 . 1 . . . . . . . . 5156 1 454 . 1 1 85 85 GLY N N 15 113.0 0.2 . 1 . . . . . . . . 5156 1 455 . 1 1 86 86 LYS H H 1 8.08 0.02 . 1 . . . . . . . . 5156 1 456 . 1 1 86 86 LYS HA H 1 4.80 0.02 . 1 . . . . . . . . 5156 1 457 . 1 1 86 86 LYS HB2 H 1 1.57 0.02 . 2 . . . . . . . . 5156 1 458 . 1 1 86 86 LYS HB3 H 1 1.63 0.02 . 2 . . . . . . . . 5156 1 459 . 1 1 86 86 LYS C C 13 175.9 0.2 . 1 . . . . . . . . 5156 1 460 . 1 1 86 86 LYS CA C 13 54.0 0.2 . 1 . . . . . . . . 5156 1 461 . 1 1 86 86 LYS CB C 13 37.0 0.2 . 1 . . . . . . . . 5156 1 462 . 1 1 86 86 LYS CG C 13 24.3 0.2 . 4 . . . . . . . . 5156 1 463 . 1 1 86 86 LYS CE C 13 42.1 0.2 . 4 . . . . . . . . 5156 1 464 . 1 1 86 86 LYS N N 15 117.3 0.2 . 1 . . . . . . . . 5156 1 465 . 1 1 87 87 ILE H H 1 9.21 0.02 . 1 . . . . . . . . 5156 1 466 . 1 1 87 87 ILE HA H 1 5.45 0.02 . 1 . . . . . . . . 5156 1 467 . 1 1 87 87 ILE HB H 1 2.08 0.02 . 1 . . . . . . . . 5156 1 468 . 1 1 87 87 ILE HG21 H 1 0.85 0.02 . 4 . . . . . . . . 5156 1 469 . 1 1 87 87 ILE HG22 H 1 0.85 0.02 . 4 . . . . . . . . 5156 1 470 . 1 1 87 87 ILE HG23 H 1 0.85 0.02 . 4 . . . . . . . . 5156 1 471 . 1 1 87 87 ILE C C 13 175.9 0.2 . 1 . . . . . . . . 5156 1 472 . 1 1 87 87 ILE CA C 13 57.9 0.2 . 1 . . . . . . . . 5156 1 473 . 1 1 87 87 ILE CB C 13 38.1 0.2 . 1 . . . . . . . . 5156 1 474 . 1 1 87 87 ILE CG1 C 13 17.9 0.2 . 4 . . . . . . . . 5156 1 475 . 1 1 87 87 ILE CD1 C 13 9.50 0.2 . 4 . . . . . . . . 5156 1 476 . 1 1 87 87 ILE N N 15 124.6 0.2 . 1 . . . . . . . . 5156 1 477 . 1 1 88 88 GLU H H 1 9.05 0.02 . 1 . . . . . . . . 5156 1 478 . 1 1 88 88 GLU HA H 1 5.39 0.02 . 1 . . . . . . . . 5156 1 479 . 1 1 88 88 GLU HB2 H 1 2.37 0.02 . 2 . . . . . . . . 5156 1 480 . 1 1 88 88 GLU C C 13 177.4 0.2 . 1 . . . . . . . . 5156 1 481 . 1 1 88 88 GLU CA C 13 54.2 0.2 . 1 . . . . . . . . 5156 1 482 . 1 1 88 88 GLU CB C 13 33.3 0.2 . 1 . . . . . . . . 5156 1 483 . 1 1 88 88 GLU CG C 13 35.9 0.2 . 1 . . . . . . . . 5156 1 484 . 1 1 88 88 GLU N N 15 126.1 0.2 . 1 . . . . . . . . 5156 1 485 . 1 1 89 89 MET H H 1 8.87 0.02 . 1 . . . . . . . . 5156 1 486 . 1 1 89 89 MET HA H 1 3.12 0.02 . 1 . . . . . . . . 5156 1 487 . 1 1 89 89 MET HB2 H 1 1.40 0.02 . 2 . . . . . . . . 5156 1 488 . 1 1 89 89 MET HG2 H 1 1.80 0.02 . 4 . . . . . . . . 5156 1 489 . 1 1 89 89 MET C C 13 178.6 0.2 . 1 . . . . . . . . 5156 1 490 . 1 1 89 89 MET CA C 13 62.0 0.2 . 1 . . . . . . . . 5156 1 491 . 1 1 89 89 MET CB C 13 32.2 0.2 . 1 . . . . . . . . 5156 1 492 . 1 1 89 89 MET CG C 13 29.1 0.2 . 1 . . . . . . . . 5156 1 493 . 1 1 89 89 MET N N 15 126.1 0.2 . 1 . . . . . . . . 5156 1 494 . 1 1 90 90 ALA H H 1 9.07 0.02 . 1 . . . . . . . . 5156 1 495 . 1 1 90 90 ALA HA H 1 3.97 0.02 . 1 . . . . . . . . 5156 1 496 . 1 1 90 90 ALA HB1 H 1 1.36 0.02 . 1 . . . . . . . . 5156 1 497 . 1 1 90 90 ALA HB2 H 1 1.36 0.02 . 1 . . . . . . . . 5156 1 498 . 1 1 90 90 ALA HB3 H 1 1.36 0.02 . 1 . . . . . . . . 5156 1 499 . 1 1 90 90 ALA C C 13 181.5 0.2 . 1 . . . . . . . . 5156 1 500 . 1 1 90 90 ALA CA C 13 55.3 0.2 . 1 . . . . . . . . 5156 1 501 . 1 1 90 90 ALA CB C 13 19.6 0.2 . 1 . . . . . . . . 5156 1 502 . 1 1 90 90 ALA N N 15 117.8 0.2 . 1 . . . . . . . . 5156 1 503 . 1 1 91 91 GLU H H 1 7.11 0.02 . 1 . . . . . . . . 5156 1 504 . 1 1 91 91 GLU HA H 1 4.39 0.02 . 1 . . . . . . . . 5156 1 505 . 1 1 91 91 GLU C C 13 180.5 0.2 . 1 . . . . . . . . 5156 1 506 . 1 1 91 91 GLU CA C 13 57.9 0.2 . 1 . . . . . . . . 5156 1 507 . 1 1 91 91 GLU CB C 13 30.3 0.2 . 1 . . . . . . . . 5156 1 508 . 1 1 91 91 GLU CG C 13 37.0 0.2 . 1 . . . . . . . . 5156 1 509 . 1 1 91 91 GLU N N 15 114.3 0.2 . 1 . . . . . . . . 5156 1 510 . 1 1 92 92 LEU H H 1 8.45 0.02 . 1 . . . . . . . . 5156 1 511 . 1 1 92 92 LEU HA H 1 4.01 0.02 . 1 . . . . . . . . 5156 1 512 . 1 1 92 92 LEU HB2 H 1 2.25 0.02 . 4 . . . . . . . . 5156 1 513 . 1 1 92 92 LEU HD11 H 1 0.69 0.02 . 4 . . . . . . . . 5156 1 514 . 1 1 92 92 LEU HD12 H 1 0.69 0.02 . 4 . . . . . . . . 5156 1 515 . 1 1 92 92 LEU HD13 H 1 0.69 0.02 . 4 . . . . . . . . 5156 1 516 . 1 1 92 92 LEU C C 13 178.8 0.2 . 1 . . . . . . . . 5156 1 517 . 1 1 92 92 LEU CA C 13 58.1 0.2 . 1 . . . . . . . . 5156 1 518 . 1 1 92 92 LEU CB C 13 41.3 0.2 . 1 . . . . . . . . 5156 1 519 . 1 1 92 92 LEU CG C 13 26.9 0.2 . 4 . . . . . . . . 5156 1 520 . 1 1 92 92 LEU N N 15 123.2 0.2 . 1 . . . . . . . . 5156 1 521 . 1 1 93 93 ALA H H 1 8.16 0.02 . 1 . . . . . . . . 5156 1 522 . 1 1 93 93 ALA HA H 1 3.99 0.02 . 1 . . . . . . . . 5156 1 523 . 1 1 93 93 ALA HB1 H 1 1.16 0.02 . 1 . . . . . . . . 5156 1 524 . 1 1 93 93 ALA HB2 H 1 1.16 0.02 . 1 . . . . . . . . 5156 1 525 . 1 1 93 93 ALA HB3 H 1 1.16 0.02 . 1 . . . . . . . . 5156 1 526 . 1 1 93 93 ALA C C 13 177.4 0.2 . 1 . . . . . . . . 5156 1 527 . 1 1 93 93 ALA CA C 13 54.3 0.2 . 1 . . . . . . . . 5156 1 528 . 1 1 93 93 ALA CB C 13 18.2 0.2 . 1 . . . . . . . . 5156 1 529 . 1 1 93 93 ALA N N 15 118.9 0.2 . 1 . . . . . . . . 5156 1 530 . 1 1 94 94 GLN H H 1 7.20 0.02 . 1 . . . . . . . . 5156 1 531 . 1 1 94 94 GLN HA H 1 4.29 0.02 . 1 . . . . . . . . 5156 1 532 . 1 1 94 94 GLN HB2 H 1 2.41 0.02 . 2 . . . . . . . . 5156 1 533 . 1 1 94 94 GLN HB3 H 1 2.51 0.02 . 2 . . . . . . . . 5156 1 534 . 1 1 94 94 GLN C C 13 177.0 0.2 . 1 . . . . . . . . 5156 1 535 . 1 1 94 94 GLN CA C 13 56.6 0.2 . 1 . . . . . . . . 5156 1 536 . 1 1 94 94 GLN CB C 13 29.8 0.2 . 1 . . . . . . . . 5156 1 537 . 1 1 94 94 GLN CG C 13 34.4 0.2 . 1 . . . . . . . . 5156 1 538 . 1 1 94 94 GLN N N 15 112.5 0.2 . 1 . . . . . . . . 5156 1 539 . 1 1 95 95 ILE H H 1 7.39 0.02 . 1 . . . . . . . . 5156 1 540 . 1 1 95 95 ILE HA H 1 3.32 0.02 . 1 . . . . . . . . 5156 1 541 . 1 1 95 95 ILE HB H 1 1.77 0.02 . 1 . . . . . . . . 5156 1 542 . 1 1 95 95 ILE HG21 H 1 0.80 0.02 . 4 . . . . . . . . 5156 1 543 . 1 1 95 95 ILE HG22 H 1 0.80 0.02 . 4 . . . . . . . . 5156 1 544 . 1 1 95 95 ILE HG23 H 1 0.80 0.02 . 4 . . . . . . . . 5156 1 545 . 1 1 95 95 ILE C C 13 176.1 0.2 . 1 . . . . . . . . 5156 1 546 . 1 1 95 95 ILE CA C 13 64.1 0.2 . 1 . . . . . . . . 5156 1 547 . 1 1 95 95 ILE CB C 13 39.9 0.2 . 1 . . . . . . . . 5156 1 548 . 1 1 95 95 ILE CG1 C 13 17.8 0.2 . 4 . . . . . . . . 5156 1 549 . 1 1 95 95 ILE N N 15 119.7 0.2 . 1 . . . . . . . . 5156 1 550 . 1 1 96 96 LEU H H 1 7.75 0.02 . 1 . . . . . . . . 5156 1 551 . 1 1 96 96 LEU HA H 1 4.70 0.02 . 1 . . . . . . . . 5156 1 552 . 1 1 96 96 LEU C C 13 173.0 0.2 . 1 . . . . . . . . 5156 1 553 . 1 1 96 96 LEU CA C 13 51.6 0.2 . 1 . . . . . . . . 5156 1 554 . 1 1 96 96 LEU CB C 13 42.8 0.2 . 1 . . . . . . . . 5156 1 555 . 1 1 96 96 LEU N N 15 118.7 0.2 . 1 . . . . . . . . 5156 1 556 . 1 1 97 97 PRO HA H 1 4.53 0.02 . 1 . . . . . . . . 5156 1 557 . 1 1 97 97 PRO HB2 H 1 2.04 0.02 . 2 . . . . . . . . 5156 1 558 . 1 1 97 97 PRO C C 13 176.8 0.2 . 1 . . . . . . . . 5156 1 559 . 1 1 97 97 PRO CA C 13 63.4 0.2 . 1 . . . . . . . . 5156 1 560 . 1 1 97 97 PRO CB C 13 31.5 0.2 . 1 . . . . . . . . 5156 1 561 . 1 1 98 98 THR H H 1 8.09 0.02 . 1 . . . . . . . . 5156 1 562 . 1 1 98 98 THR HA H 1 4.82 0.02 . 1 . . . . . . . . 5156 1 563 . 1 1 98 98 THR HB H 1 3.90 0.02 . 1 . . . . . . . . 5156 1 564 . 1 1 98 98 THR HG21 H 1 0.76 0.02 . 1 . . . . . . . . 5156 1 565 . 1 1 98 98 THR HG22 H 1 0.76 0.02 . 1 . . . . . . . . 5156 1 566 . 1 1 98 98 THR HG23 H 1 0.76 0.02 . 1 . . . . . . . . 5156 1 567 . 1 1 98 98 THR C C 13 175.3 0.2 . 1 . . . . . . . . 5156 1 568 . 1 1 98 98 THR CA C 13 60.3 0.2 . 1 . . . . . . . . 5156 1 569 . 1 1 98 98 THR CB C 13 71.3 0.2 . 1 . . . . . . . . 5156 1 570 . 1 1 98 98 THR CG2 C 13 21.1 0.2 . 1 . . . . . . . . 5156 1 571 . 1 1 98 98 THR N N 15 114.6 0.2 . 1 . . . . . . . . 5156 1 572 . 1 1 99 99 GLU H H 1 8.32 0.02 . 1 . . . . . . . . 5156 1 573 . 1 1 99 99 GLU HA H 1 4.18 0.02 . 1 . . . . . . . . 5156 1 574 . 1 1 99 99 GLU HB2 H 1 1.92 0.02 . 2 . . . . . . . . 5156 1 575 . 1 1 99 99 GLU C C 13 176.7 0.2 . 1 . . . . . . . . 5156 1 576 . 1 1 99 99 GLU CA C 13 56.9 0.2 . 1 . . . . . . . . 5156 1 577 . 1 1 99 99 GLU CB C 13 31.0 0.2 . 1 . . . . . . . . 5156 1 578 . 1 1 99 99 GLU CG C 13 36.1 0.2 . 1 . . . . . . . . 5156 1 579 . 1 1 99 99 GLU N N 15 122.3 0.2 . 1 . . . . . . . . 5156 1 580 . 1 1 100 100 GLU H H 1 8.27 0.02 . 1 . . . . . . . . 5156 1 581 . 1 1 100 100 GLU HA H 1 4.09 0.02 . 1 . . . . . . . . 5156 1 582 . 1 1 100 100 GLU HB2 H 1 1.78 0.02 . 2 . . . . . . . . 5156 1 583 . 1 1 100 100 GLU C C 13 176.2 0.2 . 1 . . . . . . . . 5156 1 584 . 1 1 100 100 GLU CA C 13 56.8 0.2 . 1 . . . . . . . . 5156 1 585 . 1 1 100 100 GLU CB C 13 30.7 0.2 . 1 . . . . . . . . 5156 1 586 . 1 1 100 100 GLU CG C 13 36.3 0.2 . 1 . . . . . . . . 5156 1 587 . 1 1 100 100 GLU N N 15 120.6 0.2 . 1 . . . . . . . . 5156 1 588 . 1 1 101 101 ASN H H 1 8.20 0.02 . 1 . . . . . . . . 5156 1 589 . 1 1 101 101 ASN C C 13 178.1 0.2 . 1 . . . . . . . . 5156 1 590 . 1 1 101 101 ASN CA C 13 53.4 0.2 . 1 . . . . . . . . 5156 1 591 . 1 1 101 101 ASN CB C 13 39.2 0.2 . 1 . . . . . . . . 5156 1 592 . 1 1 101 101 ASN N N 15 119.3 0.2 . 1 . . . . . . . . 5156 1 593 . 1 1 102 102 PHE H H 1 7.62 0.02 . 1 . . . . . . . . 5156 1 594 . 1 1 102 102 PHE HA H 1 4.29 0.02 . 1 . . . . . . . . 5156 1 595 . 1 1 102 102 PHE C C 13 174.2 0.2 . 1 . . . . . . . . 5156 1 596 . 1 1 102 102 PHE CA C 13 59.5 0.2 . 1 . . . . . . . . 5156 1 597 . 1 1 102 102 PHE CB C 13 40.8 0.2 . 1 . . . . . . . . 5156 1 598 . 1 1 102 102 PHE N N 15 125.2 0.2 . 1 . . . . . . . . 5156 1 stop_ loop_ _Ambiguous_atom_chem_shift.Ambiguous_shift_set_ID _Ambiguous_atom_chem_shift.Atom_chem_shift_ID _Ambiguous_atom_chem_shift.Entry_ID _Ambiguous_atom_chem_shift.Assigned_chem_shift_list_ID . 9 5156 1 1 14 5156 1 1 13 5156 1 . 39 5156 1 . 88 5156 1 . 92 5156 1 . 106 5156 1 . 110 5156 1 . 128 5156 1 2 205 5156 1 2 201 5156 1 2 200 5156 1 2 199 5156 1 3 230 5156 1 3 229 5156 1 3 228 5156 1 4 235 5156 1 4 234 5156 1 . 290 5156 1 . 294 5156 1 . 328 5156 1 . 350 5156 1 5 355 5156 1 5 354 5156 1 6 376 5156 1 6 375 5156 1 7 400 5156 1 7 399 5156 1 7 398 5156 1 . 421 5156 1 8 463 5156 1 8 462 5156 1 9 470 5156 1 9 469 5156 1 9 468 5156 1 10 475 5156 1 10 474 5156 1 . 488 5156 1 11 515 5156 1 11 514 5156 1 11 513 5156 1 11 512 5156 1 . 519 5156 1 12 544 5156 1 12 543 5156 1 12 542 5156 1 . 548 5156 1 stop_ save_ save_shift_set_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_2 _Assigned_chem_shift_list.Entry_ID 5156 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 2 _Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_2 _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 . . 2 $sample_2 . 5156 2 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 6 6 ALA HA H 1 4.25 0.02 . 1 . . . . . . . . 5156 2 2 . 1 1 6 6 ALA HB1 H 1 1.44 0.02 . 1 . . . . . . . . 5156 2 3 . 1 1 6 6 ALA HB2 H 1 1.44 0.02 . 1 . . . . . . . . 5156 2 4 . 1 1 6 6 ALA HB3 H 1 1.44 0.02 . 1 . . . . . . . . 5156 2 5 . 1 1 6 6 ALA CA C 13 54.7 0.2 . 1 . . . . . . . . 5156 2 6 . 1 1 7 7 GLY H H 1 8.14 0.02 . 1 . . . . . . . . 5156 2 7 . 1 1 7 7 GLY CA C 13 46.0 0.2 . 1 . . . . . . . . 5156 2 8 . 1 1 7 7 GLY N N 15 108.3 0.2 . 1 . . . . . . . . 5156 2 9 . 1 1 16 16 HIS HA H 1 4.56 0.02 . 1 . . . . . . . . 5156 2 10 . 1 1 16 16 HIS HB2 H 1 3.12 0.02 . 2 . . . . . . . . 5156 2 11 . 1 1 16 16 HIS C C 13 175.5 0.2 . 1 . . . . . . . . 5156 2 12 . 1 1 16 16 HIS CA C 13 56.0 0.2 . 1 . . . . . . . . 5156 2 13 . 1 1 16 16 HIS CB C 13 30.2 0.2 . 1 . . . . . . . . 5156 2 14 . 1 1 17 17 LEU H H 1 7.58 0.02 . 1 . . . . . . . . 5156 2 15 . 1 1 17 17 LEU HA H 1 4.15 0.02 . 1 . . . . . . . . 5156 2 16 . 1 1 17 17 LEU C C 13 177.1 0.2 . 1 . . . . . . . . 5156 2 17 . 1 1 17 17 LEU CA C 13 55.6 0.2 . 1 . . . . . . . . 5156 2 18 . 1 1 17 17 LEU CB C 13 42.5 0.2 . 1 . . . . . . . . 5156 2 19 . 1 1 17 17 LEU N N 15 121.9 0.2 . 1 . . . . . . . . 5156 2 20 . 1 1 18 18 ALA H H 1 8.26 0.02 . 1 . . . . . . . . 5156 2 21 . 1 1 18 18 ALA HA H 1 4.20 0.02 . 1 . . . . . . . . 5156 2 22 . 1 1 18 18 ALA HB1 H 1 1.41 0.02 . 1 . . . . . . . . 5156 2 23 . 1 1 18 18 ALA HB2 H 1 1.41 0.02 . 1 . . . . . . . . 5156 2 24 . 1 1 18 18 ALA HB3 H 1 1.41 0.02 . 1 . . . . . . . . 5156 2 25 . 1 1 18 18 ALA C C 13 177.7 0.2 . 1 . . . . . . . . 5156 2 26 . 1 1 18 18 ALA CA C 13 53.5 0.2 . 1 . . . . . . . . 5156 2 27 . 1 1 18 18 ALA CB C 13 19.6 0.2 . 1 . . . . . . . . 5156 2 28 . 1 1 18 18 ALA N N 15 121.8 0.2 . 1 . . . . . . . . 5156 2 29 . 1 1 19 19 GLU H H 1 7.77 0.02 . 1 . . . . . . . . 5156 2 30 . 1 1 19 19 GLU HA H 1 4.34 0.02 . 1 . . . . . . . . 5156 2 31 . 1 1 19 19 GLU HB2 H 1 2.10 0.02 . 2 . . . . . . . . 5156 2 32 . 1 1 19 19 GLU C C 13 175.6 0.2 . 1 . . . . . . . . 5156 2 33 . 1 1 19 19 GLU CA C 13 56.2 0.2 . 1 . . . . . . . . 5156 2 34 . 1 1 19 19 GLU CB C 13 31.5 0.2 . 1 . . . . . . . . 5156 2 35 . 1 1 19 19 GLU N N 15 115.3 0.2 . 1 . . . . . . . . 5156 2 36 . 1 1 20 20 LEU H H 1 8.39 0.02 . 1 . . . . . . . . 5156 2 37 . 1 1 20 20 LEU HA H 1 4.82 0.02 . 1 . . . . . . . . 5156 2 38 . 1 1 20 20 LEU C C 13 178.4 0.2 . 1 . . . . . . . . 5156 2 39 . 1 1 20 20 LEU CA C 13 54.7 0.2 . 1 . . . . . . . . 5156 2 40 . 1 1 20 20 LEU CB C 13 44.7 0.2 . 1 . . . . . . . . 5156 2 41 . 1 1 20 20 LEU N N 15 123.3 0.2 . 1 . . . . . . . . 5156 2 42 . 1 1 21 21 THR H H 1 8.48 0.02 . 1 . . . . . . . . 5156 2 43 . 1 1 21 21 THR HA H 1 4.53 0.02 . 1 . . . . . . . . 5156 2 44 . 1 1 21 21 THR HB H 1 4.58 0.02 . 1 . . . . . . . . 5156 2 45 . 1 1 21 21 THR C C 13 176.1 0.2 . 1 . . . . . . . . 5156 2 46 . 1 1 21 21 THR CA C 13 60.8 0.2 . 1 . . . . . . . . 5156 2 47 . 1 1 21 21 THR CB C 13 71.2 0.2 . 1 . . . . . . . . 5156 2 48 . 1 1 21 21 THR N N 15 112.8 0.2 . 1 . . . . . . . . 5156 2 49 . 1 1 22 22 ALA H H 1 9.11 0.02 . 1 . . . . . . . . 5156 2 50 . 1 1 22 22 ALA HA H 1 4.11 0.02 . 1 . . . . . . . . 5156 2 51 . 1 1 22 22 ALA HB1 H 1 1.44 0.02 . 1 . . . . . . . . 5156 2 52 . 1 1 22 22 ALA HB2 H 1 1.44 0.02 . 1 . . . . . . . . 5156 2 53 . 1 1 22 22 ALA HB3 H 1 1.44 0.02 . 1 . . . . . . . . 5156 2 54 . 1 1 22 22 ALA C C 13 180.8 0.2 . 1 . . . . . . . . 5156 2 55 . 1 1 22 22 ALA CA C 13 56.2 0.2 . 1 . . . . . . . . 5156 2 56 . 1 1 22 22 ALA CB C 13 18.2 0.2 . 1 . . . . . . . . 5156 2 57 . 1 1 22 22 ALA N N 15 123.7 0.2 . 1 . . . . . . . . 5156 2 58 . 1 1 23 23 SER H H 1 8.42 0.02 . 1 . . . . . . . . 5156 2 59 . 1 1 23 23 SER HA H 1 4.23 0.02 . 1 . . . . . . . . 5156 2 60 . 1 1 23 23 SER HB2 H 1 3.90 0.02 . 2 . . . . . . . . 5156 2 61 . 1 1 23 23 SER C C 13 177.8 0.2 . 1 . . . . . . . . 5156 2 62 . 1 1 23 23 SER CA C 13 61.9 0.2 . 1 . . . . . . . . 5156 2 63 . 1 1 23 23 SER N N 15 111.6 0.2 . 1 . . . . . . . . 5156 2 64 . 1 1 24 24 GLN H H 1 7.65 0.02 . 1 . . . . . . . . 5156 2 65 . 1 1 24 24 GLN HA H 1 3.92 0.02 . 1 . . . . . . . . 5156 2 66 . 1 1 24 24 GLN HB2 H 1 2.24 0.02 . 2 . . . . . . . . 5156 2 67 . 1 1 24 24 GLN C C 13 178.9 0.2 . 1 . . . . . . . . 5156 2 68 . 1 1 24 24 GLN CA C 13 58.7 0.2 . 1 . . . . . . . . 5156 2 69 . 1 1 24 24 GLN CB C 13 29.2 0.2 . 1 . . . . . . . . 5156 2 70 . 1 1 24 24 GLN N N 15 122.4 0.2 . 1 . . . . . . . . 5156 2 71 . 1 1 25 25 PHE H H 1 8.68 0.02 . 1 . . . . . . . . 5156 2 72 . 1 1 25 25 PHE HA H 1 4.02 0.02 . 1 . . . . . . . . 5156 2 73 . 1 1 25 25 PHE HB2 H 1 3.05 0.02 . 2 . . . . . . . . 5156 2 74 . 1 1 25 25 PHE HB3 H 1 3.32 0.02 . 2 . . . . . . . . 5156 2 75 . 1 1 25 25 PHE C C 13 176.9 0.2 . 1 . . . . . . . . 5156 2 76 . 1 1 25 25 PHE CA C 13 62.4 0.2 . 1 . . . . . . . . 5156 2 77 . 1 1 25 25 PHE CB C 13 39.5 0.2 . 1 . . . . . . . . 5156 2 78 . 1 1 25 25 PHE N N 15 119.6 0.2 . 1 . . . . . . . . 5156 2 79 . 1 1 26 26 LEU H H 1 8.12 0.02 . 1 . . . . . . . . 5156 2 80 . 1 1 26 26 LEU HA H 1 4.07 0.02 . 1 . . . . . . . . 5156 2 81 . 1 1 26 26 LEU HB2 H 1 1.75 0.02 . 2 . . . . . . . . 5156 2 82 . 1 1 26 26 LEU HB3 H 1 1.87 0.02 . 2 . . . . . . . . 5156 2 83 . 1 1 26 26 LEU C C 13 179.5 0.2 . 1 . . . . . . . . 5156 2 84 . 1 1 26 26 LEU CA C 13 58.1 0.2 . 1 . . . . . . . . 5156 2 85 . 1 1 26 26 LEU CB C 13 41.7 0.2 . 1 . . . . . . . . 5156 2 86 . 1 1 26 26 LEU N N 15 118.6 0.2 . 1 . . . . . . . . 5156 2 87 . 1 1 27 27 GLU H H 1 7.83 0.02 . 1 . . . . . . . . 5156 2 88 . 1 1 27 27 GLU HA H 1 4.01 0.02 . 1 . . . . . . . . 5156 2 89 . 1 1 27 27 GLU HB2 H 1 2.12 0.02 . 2 . . . . . . . . 5156 2 90 . 1 1 27 27 GLU C C 13 180.4 0.2 . 1 . . . . . . . . 5156 2 91 . 1 1 27 27 GLU CA C 13 60.0 0.2 . 1 . . . . . . . . 5156 2 92 . 1 1 27 27 GLU CB C 13 29.7 0.2 . 1 . . . . . . . . 5156 2 93 . 1 1 27 27 GLU N N 15 118.1 0.2 . 1 . . . . . . . . 5156 2 94 . 1 1 28 28 ILE H H 1 7.98 0.02 . 1 . . . . . . . . 5156 2 95 . 1 1 28 28 ILE HA H 1 3.76 0.02 . 1 . . . . . . . . 5156 2 96 . 1 1 28 28 ILE C C 13 177.9 0.2 . 1 . . . . . . . . 5156 2 97 . 1 1 28 28 ILE CA C 13 65.3 0.2 . 1 . . . . . . . . 5156 2 98 . 1 1 28 28 ILE N N 15 121.1 0.2 . 1 . . . . . . . . 5156 2 99 . 1 1 29 29 TRP H H 1 8.45 0.02 . 1 . . . . . . . . 5156 2 100 . 1 1 29 29 TRP HA H 1 3.77 0.02 . 1 . . . . . . . . 5156 2 101 . 1 1 29 29 TRP C C 13 176.9 0.2 . 1 . . . . . . . . 5156 2 102 . 1 1 29 29 TRP CA C 13 61.2 0.2 . 1 . . . . . . . . 5156 2 103 . 1 1 29 29 TRP CB C 13 28.9 0.2 . 1 . . . . . . . . 5156 2 104 . 1 1 29 29 TRP N N 15 120.5 0.2 . 1 . . . . . . . . 5156 2 105 . 1 1 30 30 LYS H H 1 8.34 0.02 . 1 . . . . . . . . 5156 2 106 . 1 1 30 30 LYS HA H 1 3.70 0.02 . 1 . . . . . . . . 5156 2 107 . 1 1 30 30 LYS HB2 H 1 1.80 0.02 . 2 . . . . . . . . 5156 2 108 . 1 1 30 30 LYS C C 13 178.4 0.2 . 1 . . . . . . . . 5156 2 109 . 1 1 30 30 LYS CA C 13 58.8 0.2 . 1 . . . . . . . . 5156 2 110 . 1 1 30 30 LYS CB C 13 32.8 0.2 . 1 . . . . . . . . 5156 2 111 . 1 1 30 30 LYS N N 15 114.0 0.2 . 1 . . . . . . . . 5156 2 112 . 1 1 31 31 HIS H H 1 7.60 0.02 . 1 . . . . . . . . 5156 2 113 . 1 1 31 31 HIS HA H 1 3.97 0.02 . 1 . . . . . . . . 5156 2 114 . 1 1 31 31 HIS HB2 H 1 2.94 0.02 . 2 . . . . . . . . 5156 2 115 . 1 1 31 31 HIS C C 13 176.6 0.2 . 1 . . . . . . . . 5156 2 116 . 1 1 31 31 HIS CA C 13 59.0 0.2 . 1 . . . . . . . . 5156 2 117 . 1 1 31 31 HIS CB C 13 29.6 0.2 . 1 . . . . . . . . 5156 2 118 . 1 1 31 31 HIS N N 15 115.1 0.2 . 1 . . . . . . . . 5156 2 119 . 1 1 32 32 PHE H H 1 7.50 0.02 . 1 . . . . . . . . 5156 2 120 . 1 1 32 32 PHE HA H 1 4.28 0.02 . 1 . . . . . . . . 5156 2 121 . 1 1 32 32 PHE HB2 H 1 2.35 0.02 . 2 . . . . . . . . 5156 2 122 . 1 1 32 32 PHE HB3 H 1 2.85 0.02 . 2 . . . . . . . . 5156 2 123 . 1 1 32 32 PHE C C 13 178.0 0.2 . 1 . . . . . . . . 5156 2 124 . 1 1 32 32 PHE CA C 13 61.4 0.2 . 1 . . . . . . . . 5156 2 125 . 1 1 32 32 PHE CB C 13 40.3 0.2 . 1 . . . . . . . . 5156 2 126 . 1 1 32 32 PHE N N 15 112.4 0.2 . 1 . . . . . . . . 5156 2 127 . 1 1 33 33 ASP H H 1 8.16 0.02 . 1 . . . . . . . . 5156 2 128 . 1 1 33 33 ASP HA H 1 4.54 0.02 . 1 . . . . . . . . 5156 2 129 . 1 1 33 33 ASP HB2 H 1 0.85 0.02 . 2 . . . . . . . . 5156 2 130 . 1 1 33 33 ASP HB3 H 1 1.82 0.02 . 2 . . . . . . . . 5156 2 131 . 1 1 33 33 ASP C C 13 177.8 0.2 . 1 . . . . . . . . 5156 2 132 . 1 1 33 33 ASP CA C 13 52.6 0.2 . 1 . . . . . . . . 5156 2 133 . 1 1 33 33 ASP CB C 13 36.4 0.2 . 1 . . . . . . . . 5156 2 134 . 1 1 33 33 ASP N N 15 120.4 0.2 . 1 . . . . . . . . 5156 2 135 . 1 1 34 34 ALA H H 1 7.27 0.02 . 1 . . . . . . . . 5156 2 136 . 1 1 34 34 ALA HA H 1 3.82 0.02 . 1 . . . . . . . . 5156 2 137 . 1 1 34 34 ALA HB1 H 1 1.40 0.02 . 1 . . . . . . . . 5156 2 138 . 1 1 34 34 ALA HB2 H 1 1.40 0.02 . 1 . . . . . . . . 5156 2 139 . 1 1 34 34 ALA HB3 H 1 1.40 0.02 . 1 . . . . . . . . 5156 2 140 . 1 1 34 34 ALA C C 13 178.9 0.2 . 1 . . . . . . . . 5156 2 141 . 1 1 34 34 ALA CA C 13 55.2 0.2 . 1 . . . . . . . . 5156 2 142 . 1 1 34 34 ALA CB C 13 19.3 0.2 . 1 . . . . . . . . 5156 2 143 . 1 1 34 34 ALA N N 15 126.3 0.2 . 1 . . . . . . . . 5156 2 144 . 1 1 35 35 ASP H H 1 8.08 0.02 . 1 . . . . . . . . 5156 2 145 . 1 1 35 35 ASP HA H 1 4.61 0.02 . 1 . . . . . . . . 5156 2 146 . 1 1 35 35 ASP HB2 H 1 2.68 0.02 . 2 . . . . . . . . 5156 2 147 . 1 1 35 35 ASP HB3 H 1 3.11 0.02 . 2 . . . . . . . . 5156 2 148 . 1 1 35 35 ASP C C 13 178.2 0.2 . 1 . . . . . . . . 5156 2 149 . 1 1 35 35 ASP CA C 13 52.8 0.2 . 1 . . . . . . . . 5156 2 150 . 1 1 35 35 ASP CB C 13 39.9 0.2 . 1 . . . . . . . . 5156 2 151 . 1 1 35 35 ASP N N 15 113.0 0.2 . 1 . . . . . . . . 5156 2 152 . 1 1 36 36 GLY H H 1 7.81 0.02 . 1 . . . . . . . . 5156 2 153 . 1 1 36 36 GLY HA2 H 1 3.87 0.02 . 2 . . . . . . . . 5156 2 154 . 1 1 36 36 GLY C C 13 175.6 0.2 . 1 . . . . . . . . 5156 2 155 . 1 1 36 36 GLY CA C 13 47.4 0.2 . 1 . . . . . . . . 5156 2 156 . 1 1 36 36 GLY N N 15 109.0 0.2 . 1 . . . . . . . . 5156 2 157 . 1 1 37 37 ASN H H 1 8.30 0.02 . 1 . . . . . . . . 5156 2 158 . 1 1 37 37 ASN HA H 1 4.69 0.02 . 1 . . . . . . . . 5156 2 159 . 1 1 37 37 ASN HB2 H 1 2.60 0.02 . 2 . . . . . . . . 5156 2 160 . 1 1 37 37 ASN HB3 H 1 3.39 0.02 . 2 . . . . . . . . 5156 2 161 . 1 1 37 37 ASN C C 13 176.6 0.2 . 1 . . . . . . . . 5156 2 162 . 1 1 37 37 ASN CA C 13 53.2 0.2 . 1 . . . . . . . . 5156 2 163 . 1 1 37 37 ASN CB C 13 38.8 0.2 . 1 . . . . . . . . 5156 2 164 . 1 1 37 37 ASN N N 15 119.3 0.2 . 1 . . . . . . . . 5156 2 165 . 1 1 38 38 GLY H H 1 10.39 0.02 . 1 . . . . . . . . 5156 2 166 . 1 1 38 38 GLY HA2 H 1 3.64 0.02 . 2 . . . . . . . . 5156 2 167 . 1 1 38 38 GLY HA3 H 1 4.22 0.02 . 2 . . . . . . . . 5156 2 168 . 1 1 38 38 GLY C C 13 173.0 0.2 . 1 . . . . . . . . 5156 2 169 . 1 1 38 38 GLY CA C 13 45.5 0.2 . 1 . . . . . . . . 5156 2 170 . 1 1 38 38 GLY N N 15 111.8 0.2 . 1 . . . . . . . . 5156 2 171 . 1 1 39 39 TYR H H 1 7.71 0.02 . 1 . . . . . . . . 5156 2 172 . 1 1 39 39 TYR HA H 1 5.13 0.02 . 1 . . . . . . . . 5156 2 173 . 1 1 39 39 TYR HB2 H 1 2.60 0.02 . 2 . . . . . . . . 5156 2 174 . 1 1 39 39 TYR C C 13 175.2 0.2 . 1 . . . . . . . . 5156 2 175 . 1 1 39 39 TYR CA C 13 57.2 0.2 . 1 . . . . . . . . 5156 2 176 . 1 1 39 39 TYR CB C 13 43.6 0.2 . 1 . . . . . . . . 5156 2 177 . 1 1 39 39 TYR N N 15 115.2 0.2 . 1 . . . . . . . . 5156 2 178 . 1 1 40 40 ILE H H 1 9.80 0.02 . 1 . . . . . . . . 5156 2 179 . 1 1 40 40 ILE HA H 1 4.59 0.02 . 1 . . . . . . . . 5156 2 180 . 1 1 40 40 ILE C C 13 174.9 0.2 . 1 . . . . . . . . 5156 2 181 . 1 1 40 40 ILE CA C 13 62.2 0.2 . 1 . . . . . . . . 5156 2 182 . 1 1 40 40 ILE CB C 13 37.4 0.2 . 1 . . . . . . . . 5156 2 183 . 1 1 40 40 ILE N N 15 128.0 0.2 . 1 . . . . . . . . 5156 2 184 . 1 1 41 41 GLU H H 1 8.98 0.02 . 1 . . . . . . . . 5156 2 185 . 1 1 41 41 GLU HA H 1 5.08 0.02 . 1 . . . . . . . . 5156 2 186 . 1 1 41 41 GLU HB2 H 1 2.09 0.02 . 2 . . . . . . . . 5156 2 187 . 1 1 41 41 GLU C C 13 176.6 0.2 . 1 . . . . . . . . 5156 2 188 . 1 1 41 41 GLU CA C 13 54.4 0.2 . 1 . . . . . . . . 5156 2 189 . 1 1 41 41 GLU CB C 13 33.6 0.2 . 1 . . . . . . . . 5156 2 190 . 1 1 41 41 GLU N N 15 125.1 .02 . 1 . . . . . . . . 5156 2 191 . 1 1 42 42 GLY H H 1 9.44 0.02 . 1 . . . . . . . . 5156 2 192 . 1 1 42 42 GLY CA C 13 47.5 0.2 . 1 . . . . . . . . 5156 2 193 . 1 1 42 42 GLY N N 15 112.3 0.2 . 1 . . . . . . . . 5156 2 194 . 1 1 44 44 GLU HA H 1 4.39 0.02 . 1 . . . . . . . . 5156 2 195 . 1 1 44 44 GLU HB2 H 1 2.47 0.02 . 2 . . . . . . . . 5156 2 196 . 1 1 44 44 GLU HB3 H 1 2.74 0.02 . 2 . . . . . . . . 5156 2 197 . 1 1 44 44 GLU C C 13 180.2 0.2 . 1 . . . . . . . . 5156 2 198 . 1 1 44 44 GLU CA C 13 58.3 0.2 . 1 . . . . . . . . 5156 2 199 . 1 1 44 44 GLU CB C 13 30.7 0.2 . 1 . . . . . . . . 5156 2 200 . 1 1 45 45 LEU H H 1 6.88 0.02 . 1 . . . . . . . . 5156 2 201 . 1 1 45 45 LEU HA H 1 3.98 0.02 . 1 . . . . . . . . 5156 2 202 . 1 1 45 45 LEU HB2 H 1 2.15 0.02 . 2 . . . . . . . . 5156 2 203 . 1 1 45 45 LEU C C 13 178.4 0.2 . 1 . . . . . . . . 5156 2 204 . 1 1 45 45 LEU CA C 13 57.0 0.2 . 1 . . . . . . . . 5156 2 205 . 1 1 45 45 LEU CB C 13 42.4 0.2 . 1 . . . . . . . . 5156 2 206 . 1 1 45 45 LEU N N 15 119.3 0.2 . 1 . . . . . . . . 5156 2 207 . 1 1 46 46 GLU H H 1 7.55 0.02 . 1 . . . . . . . . 5156 2 208 . 1 1 46 46 GLU HA H 1 4.06 0.02 . 1 . . . . . . . . 5156 2 209 . 1 1 46 46 GLU HB2 H 1 2.16 0.02 . 2 . . . . . . . . 5156 2 210 . 1 1 46 46 GLU C C 13 178.9 0.2 . 1 . . . . . . . . 5156 2 211 . 1 1 46 46 GLU CA C 13 60.5 0.2 . 1 . . . . . . . . 5156 2 212 . 1 1 46 46 GLU CB C 13 29.8 0.2 . 1 . . . . . . . . 5156 2 213 . 1 1 46 46 GLU N N 15 118.9 0.2 . 1 . . . . . . . . 5156 2 214 . 1 1 47 47 ASN H H 1 8.08 0.02 . 1 . . . . . . . . 5156 2 215 . 1 1 47 47 ASN HA H 1 4.55 0.02 . 1 . . . . . . . . 5156 2 216 . 1 1 47 47 ASN HB2 H 1 3.16 0.02 . 2 . . . . . . . . 5156 2 217 . 1 1 47 47 ASN C C 13 177.3 0.2 . 1 . . . . . . . . 5156 2 218 . 1 1 47 47 ASN CA C 13 56.7 0.2 . 1 . . . . . . . . 5156 2 219 . 1 1 47 47 ASN CB C 13 38.9 0.2 . 1 . . . . . . . . 5156 2 220 . 1 1 47 47 ASN N N 15 116.6 0.2 . 1 . . . . . . . . 5156 2 221 . 1 1 48 48 PHE H H 1 8.42 0.02 . 1 . . . . . . . . 5156 2 222 . 1 1 48 48 PHE HA H 1 3.55 0.02 . 1 . . . . . . . . 5156 2 223 . 1 1 48 48 PHE HB2 H 1 2.64 0.02 . 2 . . . . . . . . 5156 2 224 . 1 1 48 48 PHE HB3 H 1 2.83 0.02 . 2 . . . . . . . . 5156 2 225 . 1 1 48 48 PHE C C 13 175.9 0.2 . 1 . . . . . . . . 5156 2 226 . 1 1 48 48 PHE CA C 13 61.0 0.2 . 1 . . . . . . . . 5156 2 227 . 1 1 48 48 PHE CB C 13 39.0 0.2 . 1 . . . . . . . . 5156 2 228 . 1 1 48 48 PHE N N 15 118.8 0.2 . 1 . . . . . . . . 5156 2 229 . 1 1 49 49 PHE H H 1 8.69 0.02 . 1 . . . . . . . . 5156 2 230 . 1 1 49 49 PHE HA H 1 3.35 0.02 . 1 . . . . . . . . 5156 2 231 . 1 1 49 49 PHE HB2 H 1 2.68 0.02 . 2 . . . . . . . . 5156 2 232 . 1 1 49 49 PHE HB3 H 1 2.90 0.02 . 2 . . . . . . . . 5156 2 233 . 1 1 49 49 PHE C C 13 177.5 0.2 . 1 . . . . . . . . 5156 2 234 . 1 1 49 49 PHE CA C 13 61.9 0.2 . 1 . . . . . . . . 5156 2 235 . 1 1 49 49 PHE CB C 13 39.5 0.2 . 1 . . . . . . . . 5156 2 236 . 1 1 49 49 PHE N N 15 118.3 0.2 . 1 . . . . . . . . 5156 2 237 . 1 1 50 50 GLN H H 1 8.15 0.02 . 1 . . . . . . . . 5156 2 238 . 1 1 50 50 GLN HA H 1 3.86 0.02 . 1 . . . . . . . . 5156 2 239 . 1 1 50 50 GLN HB2 H 1 2.12 0.02 . 2 . . . . . . . . 5156 2 240 . 1 1 50 50 GLN HB3 H 1 2.32 0.02 . 2 . . . . . . . . 5156 2 241 . 1 1 50 50 GLN C C 13 179.8 0.2 . 1 . . . . . . . . 5156 2 242 . 1 1 50 50 GLN CA C 13 59.5 0.2 . 1 . . . . . . . . 5156 2 243 . 1 1 50 50 GLN CB C 13 29.0 0.2 . 1 . . . . . . . . 5156 2 244 . 1 1 50 50 GLN N N 15 116.3 0.2 . 1 . . . . . . . . 5156 2 245 . 1 1 51 51 GLU H H 1 8.04 0.02 . 1 . . . . . . . . 5156 2 246 . 1 1 51 51 GLU HA H 1 4.04 0.02 . 1 . . . . . . . . 5156 2 247 . 1 1 51 51 GLU HB2 H 1 1.97 0.02 . 2 . . . . . . . . 5156 2 248 . 1 1 51 51 GLU HB3 H 1 2.13 0.02 . 2 . . . . . . . . 5156 2 249 . 1 1 51 51 GLU C C 13 179.7 0.2 . 1 . . . . . . . . 5156 2 250 . 1 1 51 51 GLU CA C 13 59.1 0.2 . 1 . . . . . . . . 5156 2 251 . 1 1 51 51 GLU CB C 13 29.0 0.2 . 1 . . . . . . . . 5156 2 252 . 1 1 51 51 GLU N N 15 118.6 0.2 . 1 . . . . . . . . 5156 2 253 . 1 1 52 52 LEU H H 1 8.42 0.02 . 1 . . . . . . . . 5156 2 254 . 1 1 52 52 LEU HA H 1 3.68 0.02 . 1 . . . . . . . . 5156 2 255 . 1 1 52 52 LEU HB2 H 1 1.22 0.02 . 2 . . . . . . . . 5156 2 256 . 1 1 52 52 LEU HB3 H 1 0.62 0.02 . 2 . . . . . . . . 5156 2 257 . 1 1 52 52 LEU C C 13 178.8 0.2 . 1 . . . . . . . . 5156 2 258 . 1 1 52 52 LEU CA C 13 58.3 0.2 . 1 . . . . . . . . 5156 2 259 . 1 1 52 52 LEU CB C 13 41.5 0.2 . 1 . . . . . . . . 5156 2 260 . 1 1 52 52 LEU N N 15 123.5 0.2 . 1 . . . . . . . . 5156 2 261 . 1 1 53 53 GLU H H 1 7.93 0.02 . 1 . . . . . . . . 5156 2 262 . 1 1 53 53 GLU HA H 1 3.80 0.02 . 1 . . . . . . . . 5156 2 263 . 1 1 53 53 GLU HB2 H 1 1.73 0.02 . 2 . . . . . . . . 5156 2 264 . 1 1 53 53 GLU C C 13 179.7 0.2 . 1 . . . . . . . . 5156 2 265 . 1 1 53 53 GLU CA C 13 59.4 0.2 . 1 . . . . . . . . 5156 2 266 . 1 1 53 53 GLU CB C 13 29.6 0.2 . 1 . . . . . . . . 5156 2 267 . 1 1 53 53 GLU N N 15 117.6 0.2 . 1 . . . . . . . . 5156 2 268 . 1 1 54 54 LYS H H 1 7.53 0.02 . 1 . . . . . . . . 5156 2 269 . 1 1 54 54 LYS HA H 1 3.92 0.02 . 1 . . . . . . . . 5156 2 270 . 1 1 54 54 LYS HB2 H 1 1.82 0.02 . 2 . . . . . . . . 5156 2 271 . 1 1 54 54 LYS C C 13 179.2 0.2 . 1 . . . . . . . . 5156 2 272 . 1 1 54 54 LYS CA C 13 59.5 0.2 . 1 . . . . . . . . 5156 2 273 . 1 1 54 54 LYS CB C 13 32.8 0.2 . 1 . . . . . . . . 5156 2 274 . 1 1 54 54 LYS N N 15 118.0 0.2 . 1 . . . . . . . . 5156 2 275 . 1 1 55 55 ALA H H 1 7.88 0.02 . 1 . . . . . . . . 5156 2 276 . 1 1 55 55 ALA HA H 1 4.10 0.02 . 1 . . . . . . . . 5156 2 277 . 1 1 55 55 ALA CA C 13 54.5 0.2 . 1 . . . . . . . . 5156 2 278 . 1 1 55 55 ALA CB C 13 19.4 0.2 . 1 . . . . . . . . 5156 2 279 . 1 1 55 55 ALA N N 15 120.8 0.2 . 1 . . . . . . . . 5156 2 280 . 1 1 56 56 ARG H H 1 8.07 0.02 . 1 . . . . . . . . 5156 2 281 . 1 1 56 56 ARG CA C 13 58.1 0.2 . 1 . . . . . . . . 5156 2 282 . 1 1 56 56 ARG N N 15 116.8 0.2 . 1 . . . . . . . . 5156 2 283 . 1 1 57 57 LYS HA H 1 4.22 0.02 . 1 . . . . . . . . 5156 2 284 . 1 1 57 57 LYS HB2 H 1 1.86 0.02 . 2 . . . . . . . . 5156 2 285 . 1 1 57 57 LYS C C 13 178.2 0.2 . 1 . . . . . . . . 5156 2 286 . 1 1 57 57 LYS CA C 13 57.7 0.2 . 1 . . . . . . . . 5156 2 287 . 1 1 57 57 LYS CB C 13 32.6 0.2 . 1 . . . . . . . . 5156 2 288 . 1 1 58 58 GLY H H 1 8.15 0.05 . 1 . . . . . . . . 5156 2 289 . 1 1 58 58 GLY HA2 H 1 4.01 0.02 . 2 . . . . . . . . 5156 2 290 . 1 1 58 58 GLY C C 13 175.0 0.2 . 1 . . . . . . . . 5156 2 291 . 1 1 58 58 GLY CA C 13 46.0 0.2 . 1 . . . . . . . . 5156 2 292 . 1 1 58 58 GLY N N 15 108.4 0.2 . 1 . . . . . . . . 5156 2 293 . 1 1 59 59 SER H H 1 8.14 0.02 . 1 . . . . . . . . 5156 2 294 . 1 1 59 59 SER HA H 1 4.48 0.02 . 1 . . . . . . . . 5156 2 295 . 1 1 59 59 SER HB2 H 1 3.92 0.02 . 2 . . . . . . . . 5156 2 296 . 1 1 59 59 SER C C 13 175.6 0.2 . 1 . . . . . . . . 5156 2 297 . 1 1 59 59 SER CA C 13 58.9 0.2 . 1 . . . . . . . . 5156 2 298 . 1 1 59 59 SER CB C 13 64.0 0.2 . 1 . . . . . . . . 5156 2 299 . 1 1 59 59 SER N N 15 115.2 0.2 . 1 . . . . . . . . 5156 2 300 . 1 1 60 60 GLY H H 1 8.43 0.02 . 1 . . . . . . . . 5156 2 301 . 1 1 60 60 GLY HA2 H 1 3.97 0.02 . 2 . . . . . . . . 5156 2 302 . 1 1 60 60 GLY C C 13 173.8 0.2 . 1 . . . . . . . . 5156 2 303 . 1 1 60 60 GLY CA C 13 45.9 0.2 . 1 . . . . . . . . 5156 2 304 . 1 1 60 60 GLY N N 15 110.8 0.2 . 1 . . . . . . . . 5156 2 305 . 1 1 61 61 MET H H 1 7.82 0.02 . 1 . . . . . . . . 5156 2 306 . 1 1 61 61 MET CA C 13 57.3 0.2 . 1 . . . . . . . . 5156 2 307 . 1 1 61 61 MET N N 15 124.5 0.2 . 1 . . . . . . . . 5156 2 308 . 1 1 62 62 MET HA H 1 4.14 0.02 . 1 . . . . . . . . 5156 2 309 . 1 1 62 62 MET HB2 H 1 1.98 0.02 . 2 . . . . . . . . 5156 2 310 . 1 1 62 62 MET C C 13 179.3 0.2 . 1 . . . . . . . . 5156 2 311 . 1 1 62 62 MET CA C 13 59.1 0.2 . 1 . . . . . . . . 5156 2 312 . 1 1 62 62 MET CB C 13 31.9 0.2 . 1 . . . . . . . . 5156 2 313 . 1 1 63 63 SER H H 1 7.99 0.02 . 1 . . . . . . . . 5156 2 314 . 1 1 63 63 SER HA H 1 4.42 0.02 . 1 . . . . . . . . 5156 2 315 . 1 1 63 63 SER C C 13 175.1 0.2 . 1 . . . . . . . . 5156 2 316 . 1 1 63 63 SER CA C 13 58.4 0.2 . 1 . . . . . . . . 5156 2 317 . 1 1 63 63 SER CB C 13 64.0 0.2 . 1 . . . . . . . . 5156 2 318 . 1 1 63 63 SER N N 15 115.7 0.2 . 1 . . . . . . . . 5156 2 319 . 1 1 64 64 LYS H H 1 8.27 0.02 . 1 . . . . . . . . 5156 2 320 . 1 1 64 64 LYS CA C 13 56.8 0.2 . 1 . . . . . . . . 5156 2 321 . 1 1 64 64 LYS N N 15 121.9 0.2 . 1 . . . . . . . . 5156 2 322 . 1 1 65 65 SER HA H 1 4.54 0.02 . 1 . . . . . . . . 5156 2 323 . 1 1 65 65 SER HB2 H 1 3.89 0.02 . 2 . . . . . . . . 5156 2 324 . 1 1 65 65 SER C C 13 174.5 0.2 . 1 . . . . . . . . 5156 2 325 . 1 1 65 65 SER CA C 13 58.4 0.2 . 1 . . . . . . . . 5156 2 326 . 1 1 65 65 SER CB C 13 64.0 0.2 . 1 . . . . . . . . 5156 2 327 . 1 1 66 66 ASP H H 1 8.53 0.02 . 1 . . . . . . . . 5156 2 328 . 1 1 66 66 ASP HA H 1 4.63 0.02 . 1 . . . . . . . . 5156 2 329 . 1 1 66 66 ASP HB2 H 1 2.63 0.02 . 2 . . . . . . . . 5156 2 330 . 1 1 66 66 ASP C C 13 176.5 0.2 . 1 . . . . . . . . 5156 2 331 . 1 1 66 66 ASP CA C 13 54.8 0.2 . 1 . . . . . . . . 5156 2 332 . 1 1 66 66 ASP CB C 13 41.5 0.2 . 1 . . . . . . . . 5156 2 333 . 1 1 66 66 ASP N N 15 122.3 0.2 . 1 . . . . . . . . 5156 2 334 . 1 1 67 67 ASN H H 1 8.37 0.02 . 1 . . . . . . . . 5156 2 335 . 1 1 67 67 ASN HA H 1 4.73 0.02 . 1 . . . . . . . . 5156 2 336 . 1 1 67 67 ASN HB2 H 1 2.82 0.02 . 2 . . . . . . . . 5156 2 337 . 1 1 67 67 ASN C C 13 176.0 0.2 . 1 . . . . . . . . 5156 2 338 . 1 1 67 67 ASN CA C 13 53.8 0.2 . 1 . . . . . . . . 5156 2 339 . 1 1 67 67 ASN CB C 13 39.0 0.2 . 1 . . . . . . . . 5156 2 340 . 1 1 67 67 ASN N N 15 118.5 0.2 . 1 . . . . . . . . 5156 2 341 . 1 1 68 68 PHE H H 1 8.48 0.04 . 1 . . . . . . . . 5156 2 342 . 1 1 68 68 PHE HA H 1 4.29 0.02 . 1 . . . . . . . . 5156 2 343 . 1 1 68 68 PHE HB2 H 1 3.06 0.02 . 2 . . . . . . . . 5156 2 344 . 1 1 68 68 PHE HB3 H 1 3.27 0.02 . 2 . . . . . . . . 5156 2 345 . 1 1 68 68 PHE C C 13 177.2 0.2 . 1 . . . . . . . . 5156 2 346 . 1 1 68 68 PHE CA C 13 61.0 0.2 . 1 . . . . . . . . 5156 2 347 . 1 1 68 68 PHE CB C 13 39.7 0.2 . 1 . . . . . . . . 5156 2 348 . 1 1 68 68 PHE N N 15 121.8 0.2 . 1 . . . . . . . . 5156 2 349 . 1 1 69 69 GLY H H 1 8.58 0.02 . 1 . . . . . . . . 5156 2 350 . 1 1 69 69 GLY HA2 H 1 3.75 0.02 . 2 . . . . . . . . 5156 2 351 . 1 1 69 69 GLY HA3 H 1 3.95 0.02 . 2 . . . . . . . . 5156 2 352 . 1 1 69 69 GLY C C 13 176.9 0.2 . 1 . . . . . . . . 5156 2 353 . 1 1 69 69 GLY CA C 13 47.1 0.2 . 1 . . . . . . . . 5156 2 354 . 1 1 69 69 GLY N N 15 106.8 0.2 . 1 . . . . . . . . 5156 2 355 . 1 1 70 70 GLU H H 1 8.09 0.02 . 1 . . . . . . . . 5156 2 356 . 1 1 70 70 GLU HA H 1 4.06 0.02 . 1 . . . . . . . . 5156 2 357 . 1 1 70 70 GLU HB2 H 1 2.08 0.02 . 2 . . . . . . . . 5156 2 358 . 1 1 70 70 GLU C C 13 179.4 0.2 . 1 . . . . . . . . 5156 2 359 . 1 1 70 70 GLU CA C 13 59.4 0.2 . 1 . . . . . . . . 5156 2 360 . 1 1 70 70 GLU CB C 13 29.6 0.2 . 1 . . . . . . . . 5156 2 361 . 1 1 70 70 GLU N N 15 121.4 0.2 . 1 . . . . . . . . 5156 2 362 . 1 1 71 71 LYS H H 1 8.10 0.02 . 1 . . . . . . . . 5156 2 363 . 1 1 71 71 LYS HA H 1 4.09 0.02 . 1 . . . . . . . . 5156 2 364 . 1 1 71 71 LYS HB2 H 1 1.84 0.02 . 2 . . . . . . . . 5156 2 365 . 1 1 71 71 LYS C C 13 179.3 0.2 . 1 . . . . . . . . 5156 2 366 . 1 1 71 71 LYS CA C 13 59.2 0.2 . 1 . . . . . . . . 5156 2 367 . 1 1 71 71 LYS CB C 13 31.8 0.2 . 1 . . . . . . . . 5156 2 368 . 1 1 71 71 LYS N N 15 119.7 0.2 . 1 . . . . . . . . 5156 2 369 . 1 1 72 72 MET H H 1 8.20 0.02 . 1 . . . . . . . . 5156 2 370 . 1 1 72 72 MET HA H 1 3.43 0.02 . 1 . . . . . . . . 5156 2 371 . 1 1 72 72 MET HB2 H 1 1.90 0.02 . 2 . . . . . . . . 5156 2 372 . 1 1 72 72 MET C C 13 178.0 0.2 . 1 . . . . . . . . 5156 2 373 . 1 1 72 72 MET CA C 13 58.3 0.2 . 1 . . . . . . . . 5156 2 374 . 1 1 72 72 MET CB C 13 32.3 0.2 . 1 . . . . . . . . 5156 2 375 . 1 1 72 72 MET N N 15 119.7 0.2 . 1 . . . . . . . . 5156 2 376 . 1 1 73 73 LYS H H 1 7.76 0.02 . 1 . . . . . . . . 5156 2 377 . 1 1 73 73 LYS HA H 1 3.93 0.02 . 1 . . . . . . . . 5156 2 378 . 1 1 73 73 LYS HB2 H 1 1.89 0.02 . 2 . . . . . . . . 5156 2 379 . 1 1 73 73 LYS C C 13 179.8 0.2 . 1 . . . . . . . . 5156 2 380 . 1 1 73 73 LYS CA C 13 60.2 0.2 . 1 . . . . . . . . 5156 2 381 . 1 1 73 73 LYS CB C 13 32.3 0.2 . 1 . . . . . . . . 5156 2 382 . 1 1 73 73 LYS N N 15 119.8 0.2 . 1 . . . . . . . . 5156 2 383 . 1 1 74 74 GLU H H 1 7.85 0.02 . 1 . . . . . . . . 5156 2 384 . 1 1 74 74 GLU C C 13 179.0 0.2 . 1 . . . . . . . . 5156 2 385 . 1 1 74 74 GLU CA C 13 59.7 0.2 . 1 . . . . . . . . 5156 2 386 . 1 1 74 74 GLU CB C 13 29.7 0.2 . 1 . . . . . . . . 5156 2 387 . 1 1 74 74 GLU N N 15 119.5 0.2 . 1 . . . . . . . . 5156 2 388 . 1 1 75 75 PHE H H 1 7.96 0.02 . 1 . . . . . . . . 5156 2 389 . 1 1 75 75 PHE HA H 1 4.32 0.02 . 1 . . . . . . . . 5156 2 390 . 1 1 75 75 PHE HB2 H 1 3.19 0.02 . 2 . . . . . . . . 5156 2 391 . 1 1 75 75 PHE C C 13 177.9 0.2 . 1 . . . . . . . . 5156 2 392 . 1 1 75 75 PHE CA C 13 61.4 0.2 . 1 . . . . . . . . 5156 2 393 . 1 1 75 75 PHE CB C 13 39.9 0.2 . 1 . . . . . . . . 5156 2 394 . 1 1 75 75 PHE N N 15 121.1 0.2 . 1 . . . . . . . . 5156 2 395 . 1 1 76 76 MET H H 1 8.51 0.02 . 1 . . . . . . . . 5156 2 396 . 1 1 76 76 MET HA H 1 4.44 0.02 . 1 . . . . . . . . 5156 2 397 . 1 1 76 76 MET HB2 H 1 2.19 0.02 . 2 . . . . . . . . 5156 2 398 . 1 1 76 76 MET C C 13 180.1 0.2 . 1 . . . . . . . . 5156 2 399 . 1 1 76 76 MET CA C 13 56.8 0.2 . 1 . . . . . . . . 5156 2 400 . 1 1 76 76 MET CB C 13 30.8 0.2 . 1 . . . . . . . . 5156 2 401 . 1 1 76 76 MET N N 15 117.3 0.2 . 1 . . . . . . . . 5156 2 402 . 1 1 77 77 GLN H H 1 8.26 0.02 . 1 . . . . . . . . 5156 2 403 . 1 1 77 77 GLN HA H 1 3.96 0.02 . 1 . . . . . . . . 5156 2 404 . 1 1 77 77 GLN HB2 H 1 2.05 0.02 . 2 . . . . . . . . 5156 2 405 . 1 1 77 77 GLN HB3 H 1 2.19 0.02 . 2 . . . . . . . . 5156 2 406 . 1 1 77 77 GLN C C 13 178.4 0.2 . 1 . . . . . . . . 5156 2 407 . 1 1 77 77 GLN CA C 13 59.0 0.2 . 1 . . . . . . . . 5156 2 408 . 1 1 77 77 GLN CB C 13 28.4 0.2 . 1 . . . . . . . . 5156 2 409 . 1 1 77 77 GLN N N 15 119.4 0.2 . 1 . . . . . . . . 5156 2 410 . 1 1 78 78 LYS H H 1 7.30 0.02 . 1 . . . . . . . . 5156 2 411 . 1 1 78 78 LYS HA H 1 3.87 0.02 . 1 . . . . . . . . 5156 2 412 . 1 1 78 78 LYS HB2 H 1 0.98 0.02 . 2 . . . . . . . . 5156 2 413 . 1 1 78 78 LYS HB3 H 1 1.35 0.02 . 2 . . . . . . . . 5156 2 414 . 1 1 78 78 LYS C C 13 178.7 0.2 . 1 . . . . . . . . 5156 2 415 . 1 1 78 78 LYS CA C 13 58.9 0.2 . 1 . . . . . . . . 5156 2 416 . 1 1 78 78 LYS CB C 13 33.3 0.2 . 1 . . . . . . . . 5156 2 417 . 1 1 78 78 LYS N N 15 116.2 0.2 . 1 . . . . . . . . 5156 2 418 . 1 1 79 79 TYR H H 1 7.77 0.02 . 1 . . . . . . . . 5156 2 419 . 1 1 79 79 TYR HA H 1 4.69 0.02 . 1 . . . . . . . . 5156 2 420 . 1 1 79 79 TYR HB2 H 1 2.00 0.02 . 2 . . . . . . . . 5156 2 421 . 1 1 79 79 TYR HB3 H 1 2.90 0.02 . 2 . . . . . . . . 5156 2 422 . 1 1 79 79 TYR C C 13 177.0 0.2 . 1 . . . . . . . . 5156 2 423 . 1 1 79 79 TYR CA C 13 59.2 0.2 . 1 . . . . . . . . 5156 2 424 . 1 1 79 79 TYR CB C 13 40.6 0.2 . 1 . . . . . . . . 5156 2 425 . 1 1 79 79 TYR N N 15 112.7 0.2 . 1 . . . . . . . . 5156 2 426 . 1 1 80 80 ASP H H 1 8.83 0.02 . 1 . . . . . . . . 5156 2 427 . 1 1 80 80 ASP HA H 1 4.90 0.02 . 1 . . . . . . . . 5156 2 428 . 1 1 80 80 ASP HB2 H 1 2.51 0.02 . 2 . . . . . . . . 5156 2 429 . 1 1 80 80 ASP HB3 H 1 3.36 0.02 . 2 . . . . . . . . 5156 2 430 . 1 1 80 80 ASP C C 13 178.5 0.2 . 1 . . . . . . . . 5156 2 431 . 1 1 80 80 ASP CA C 13 53.0 0.2 . 1 . . . . . . . . 5156 2 432 . 1 1 80 80 ASP CB C 13 39.0 0.2 . 1 . . . . . . . . 5156 2 433 . 1 1 80 80 ASP N N 15 119.7 0.2 . 1 . . . . . . . . 5156 2 434 . 1 1 81 81 LYS H H 1 7.70 0.02 . 1 . . . . . . . . 5156 2 435 . 1 1 81 81 LYS HA H 1 4.02 0.02 . 1 . . . . . . . . 5156 2 436 . 1 1 81 81 LYS HB2 H 1 1.94 0.02 . 2 . . . . . . . . 5156 2 437 . 1 1 81 81 LYS C C 13 177.9 0.2 . 1 . . . . . . . . 5156 2 438 . 1 1 81 81 LYS CA C 13 58.6 0.2 . 1 . . . . . . . . 5156 2 439 . 1 1 81 81 LYS CB C 13 32.6 0.2 . 1 . . . . . . . . 5156 2 440 . 1 1 81 81 LYS N N 15 125.3 0.2 . 1 . . . . . . . . 5156 2 441 . 1 1 82 82 ASN H H 1 7.99 0.02 . 1 . . . . . . . . 5156 2 442 . 1 1 82 82 ASN HA H 1 4.89 0.02 . 1 . . . . . . . . 5156 2 443 . 1 1 82 82 ASN HB2 H 1 2.79 0.02 . 2 . . . . . . . . 5156 2 444 . 1 1 82 82 ASN HB3 H 1 3.30 0.02 . 2 . . . . . . . . 5156 2 445 . 1 1 82 82 ASN C C 13 175.1 0.2 . 1 . . . . . . . . 5156 2 446 . 1 1 82 82 ASN CA C 13 51.7 0.2 . 1 . . . . . . . . 5156 2 447 . 1 1 82 82 ASN CB C 13 37.2 0.2 . 1 . . . . . . . . 5156 2 448 . 1 1 82 82 ASN N N 15 112.8 0.2 . 1 . . . . . . . . 5156 2 449 . 1 1 83 83 SER H H 1 7.76 0.02 . 1 . . . . . . . . 5156 2 450 . 1 1 83 83 SER HA H 1 4.01 0.02 . 1 . . . . . . . . 5156 2 451 . 1 1 83 83 SER HB2 H 1 3.82 0.02 . 2 . . . . . . . . 5156 2 452 . 1 1 83 83 SER C C 13 174.2 0.2 . 1 . . . . . . . . 5156 2 453 . 1 1 83 83 SER CA C 13 59.5 0.2 . 1 . . . . . . . . 5156 2 454 . 1 1 83 83 SER CB C 13 61.7 0.2 . 1 . . . . . . . . 5156 2 455 . 1 1 83 83 SER N N 15 111.6 0.2 . 1 . . . . . . . . 5156 2 456 . 1 1 84 84 ASP H H 1 8.24 0.02 . 1 . . . . . . . . 5156 2 457 . 1 1 84 84 ASP HA H 1 4.68 0.02 . 1 . . . . . . . . 5156 2 458 . 1 1 84 84 ASP HB2 H 1 2.95 0.02 . 2 . . . . . . . . 5156 2 459 . 1 1 84 84 ASP HB3 H 1 2.39 0.02 . 2 . . . . . . . . 5156 2 460 . 1 1 84 84 ASP C C 13 178.5 0.2 . 1 . . . . . . . . 5156 2 461 . 1 1 84 84 ASP CA C 13 52.8 0.2 . 1 . . . . . . . . 5156 2 462 . 1 1 84 84 ASP CB C 13 40.8 0.2 . 1 . . . . . . . . 5156 2 463 . 1 1 84 84 ASP N N 15 117.3 0.2 . 1 . . . . . . . . 5156 2 464 . 1 1 85 85 GLY H H 1 10.61 0.02 . 1 . . . . . . . . 5156 2 465 . 1 1 85 85 GLY HA2 H 1 4.08 0.02 . 2 . . . . . . . . 5156 2 466 . 1 1 85 85 GLY HA3 H 1 3.42 0.02 . 2 . . . . . . . . 5156 2 467 . 1 1 85 85 GLY C C 13 173.2 0.2 . 1 . . . . . . . . 5156 2 468 . 1 1 85 85 GLY CA C 13 46.2 0.2 . 1 . . . . . . . . 5156 2 469 . 1 1 85 85 GLY N N 15 113.0 0.2 . 1 . . . . . . . . 5156 2 470 . 1 1 86 86 LYS H H 1 8.08 0.02 . 1 . . . . . . . . 5156 2 471 . 1 1 86 86 LYS HA H 1 4.88 0.02 . 1 . . . . . . . . 5156 2 472 . 1 1 86 86 LYS HB2 H 1 1.60 0.02 . 2 . . . . . . . . 5156 2 473 . 1 1 86 86 LYS HB3 H 1 1.68 0.02 . 2 . . . . . . . . 5156 2 474 . 1 1 86 86 LYS C C 13 175.9 0.2 . 1 . . . . . . . . 5156 2 475 . 1 1 86 86 LYS CA C 13 53.9 0.2 . 1 . . . . . . . . 5156 2 476 . 1 1 86 86 LYS CB C 13 36.9 0.2 . 1 . . . . . . . . 5156 2 477 . 1 1 86 86 LYS N N 15 117.1 0.2 . 1 . . . . . . . . 5156 2 478 . 1 1 87 87 ILE H H 1 9.21 0.02 . 1 . . . . . . . . 5156 2 479 . 1 1 87 87 ILE HA H 1 5.51 0.02 . 1 . . . . . . . . 5156 2 480 . 1 1 87 87 ILE HB H 1 2.11 0.02 . 1 . . . . . . . . 5156 2 481 . 1 1 87 87 ILE C C 13 175.9 0.2 . 1 . . . . . . . . 5156 2 482 . 1 1 87 87 ILE CA C 13 57.8 0.2 . 1 . . . . . . . . 5156 2 483 . 1 1 87 87 ILE CB C 13 38.0 0.2 . 1 . . . . . . . . 5156 2 484 . 1 1 87 87 ILE N N 15 124.6 0.2 . 1 . . . . . . . . 5156 2 485 . 1 1 88 88 GLU H H 1 9.05 0.02 . 1 . . . . . . . . 5156 2 486 . 1 1 88 88 GLU HA H 1 5.44 0.02 . 1 . . . . . . . . 5156 2 487 . 1 1 88 88 GLU HB2 H 1 2.42 0.02 . 2 . . . . . . . . 5156 2 488 . 1 1 88 88 GLU C C 13 177.5 0.2 . 1 . . . . . . . . 5156 2 489 . 1 1 88 88 GLU CA C 13 54.2 0.2 . 1 . . . . . . . . 5156 2 490 . 1 1 88 88 GLU CB C 13 33.3 0.2 . 1 . . . . . . . . 5156 2 491 . 1 1 88 88 GLU N N 15 126.2 0.2 . 1 . . . . . . . . 5156 2 492 . 1 1 89 89 MET H H 1 8.85 0.02 . 1 . . . . . . . . 5156 2 493 . 1 1 89 89 MET HA H 1 3.18 0.02 . 1 . . . . . . . . 5156 2 494 . 1 1 89 89 MET HB2 H 1 1.43 0.02 . 2 . . . . . . . . 5156 2 495 . 1 1 89 89 MET C C 13 178.5 0.2 . 1 . . . . . . . . 5156 2 496 . 1 1 89 89 MET CA C 13 61.9 0.2 . 1 . . . . . . . . 5156 2 497 . 1 1 89 89 MET CB C 13 32.3 0.2 . 1 . . . . . . . . 5156 2 498 . 1 1 89 89 MET N N 15 126.0 0.2 . 1 . . . . . . . . 5156 2 499 . 1 1 90 90 ALA H H 1 9.07 0.02 . 1 . . . . . . . . 5156 2 500 . 1 1 90 90 ALA HA H 1 4.02 0.02 . 1 . . . . . . . . 5156 2 501 . 1 1 90 90 ALA HB1 H 1 1.42 0.02 . 1 . . . . . . . . 5156 2 502 . 1 1 90 90 ALA HB2 H 1 1.42 0.02 . 1 . . . . . . . . 5156 2 503 . 1 1 90 90 ALA HB3 H 1 1.42 0.02 . 1 . . . . . . . . 5156 2 504 . 1 1 90 90 ALA C C 13 181.5 0.2 . 1 . . . . . . . . 5156 2 505 . 1 1 90 90 ALA CA C 13 55.2 0.2 . 1 . . . . . . . . 5156 2 506 . 1 1 90 90 ALA CB C 13 19.0 0.2 . 1 . . . . . . . . 5156 2 507 . 1 1 90 90 ALA N N 15 117.8 0.2 . 1 . . . . . . . . 5156 2 508 . 1 1 91 91 GLU H H 1 7.13 0.02 . 1 . . . . . . . . 5156 2 509 . 1 1 91 91 GLU HA H 1 4.43 0.02 . 1 . . . . . . . . 5156 2 510 . 1 1 91 91 GLU HB2 H 1 2.35 0.02 . 2 . . . . . . . . 5156 2 511 . 1 1 91 91 GLU C C 13 180.4 0.2 . 1 . . . . . . . . 5156 2 512 . 1 1 91 91 GLU CA C 13 57.9 0.2 . 1 . . . . . . . . 5156 2 513 . 1 1 91 91 GLU CB C 13 30.1 0.2 . 1 . . . . . . . . 5156 2 514 . 1 1 91 91 GLU N N 15 114.3 0.2 . 1 . . . . . . . . 5156 2 515 . 1 1 92 92 LEU H H 1 8.42 0.02 . 1 . . . . . . . . 5156 2 516 . 1 1 92 92 LEU C C 13 178.8 0.2 . 1 . . . . . . . . 5156 2 517 . 1 1 92 92 LEU CA C 13 58.0 0.2 . 1 . . . . . . . . 5156 2 518 . 1 1 92 92 LEU CB C 13 41.6 0.2 . 1 . . . . . . . . 5156 2 519 . 1 1 92 92 LEU N N 15 122.9 0.2 . 1 . . . . . . . . 5156 2 520 . 1 1 93 93 ALA H H 1 8.20 0.02 . 1 . . . . . . . . 5156 2 521 . 1 1 93 93 ALA HA H 1 4.05 0.02 . 1 . . . . . . . . 5156 2 522 . 1 1 93 93 ALA HB1 H 1 1.22 0.02 . 1 . . . . . . . . 5156 2 523 . 1 1 93 93 ALA HB2 H 1 1.22 0.02 . 1 . . . . . . . . 5156 2 524 . 1 1 93 93 ALA HB3 H 1 1.22 0.02 . 1 . . . . . . . . 5156 2 525 . 1 1 93 93 ALA C C 13 177.6 0.2 . 1 . . . . . . . . 5156 2 526 . 1 1 93 93 ALA CA C 13 54.4 0.2 . 1 . . . . . . . . 5156 2 527 . 1 1 93 93 ALA CB C 13 18.2 0.2 . 1 . . . . . . . . 5156 2 528 . 1 1 93 93 ALA N N 15 118.7 0.2 . 1 . . . . . . . . 5156 2 529 . 1 1 94 94 GLN H H 1 7.20 0.02 . 1 . . . . . . . . 5156 2 530 . 1 1 94 94 GLN HA H 1 4.36 0.02 . 1 . . . . . . . . 5156 2 531 . 1 1 94 94 GLN HB2 H 1 2.25 0.02 . 2 . . . . . . . . 5156 2 532 . 1 1 94 94 GLN HB3 H 1 2.45 0.02 . 2 . . . . . . . . 5156 2 533 . 1 1 94 94 GLN C C 13 177.0 0.2 . 1 . . . . . . . . 5156 2 534 . 1 1 94 94 GLN CA C 13 56.6 0.2 . 1 . . . . . . . . 5156 2 535 . 1 1 94 94 GLN CB C 13 29.6 0.2 . 1 . . . . . . . . 5156 2 536 . 1 1 94 94 GLN N N 15 112.5 0.2 . 1 . . . . . . . . 5156 2 537 . 1 1 95 95 ILE H H 1 7.44 0.02 . 1 . . . . . . . . 5156 2 538 . 1 1 95 95 ILE HA H 1 3.46 0.02 . 1 . . . . . . . . 5156 2 539 . 1 1 95 95 ILE C C 13 176.0 0.2 . 1 . . . . . . . . 5156 2 540 . 1 1 95 95 ILE CA C 13 64.0 0.2 . 1 . . . . . . . . 5156 2 541 . 1 1 95 95 ILE CB C 13 40.0 0.2 . 1 . . . . . . . . 5156 2 542 . 1 1 95 95 ILE N N 15 119.5 0.2 . 1 . . . . . . . . 5156 2 543 . 1 1 96 96 LEU H H 1 7.68 0.02 . 1 . . . . . . . . 5156 2 544 . 1 1 96 96 LEU CA C 13 51.9 0.2 . 1 . . . . . . . . 5156 2 545 . 1 1 96 96 LEU N N 15 118.6 0.2 . 1 . . . . . . . . 5156 2 546 . 1 1 97 97 PRO HA H 1 4.54 0.02 . 1 . . . . . . . . 5156 2 547 . 1 1 97 97 PRO C C 13 177.2 0.2 . 1 . . . . . . . . 5156 2 548 . 1 1 97 97 PRO CA C 13 63.4 0.2 . 1 . . . . . . . . 5156 2 549 . 1 1 97 97 PRO CB C 13 32.0 0.2 . 1 . . . . . . . . 5156 2 550 . 1 1 98 98 THR H H 1 8.06 0.02 . 1 . . . . . . . . 5156 2 551 . 1 1 98 98 THR HA H 1 4.79 0.02 . 1 . . . . . . . . 5156 2 552 . 1 1 98 98 THR HB H 1 4.01 0.02 . 1 . . . . . . . . 5156 2 553 . 1 1 98 98 THR C C 13 175.2 0.2 . 1 . . . . . . . . 5156 2 554 . 1 1 98 98 THR CA C 13 60.7 0.2 . 1 . . . . . . . . 5156 2 555 . 1 1 98 98 THR CB C 13 71.1 0.2 . 1 . . . . . . . . 5156 2 556 . 1 1 98 98 THR N N 15 113.7 0.2 . 1 . . . . . . . . 5156 2 557 . 1 1 99 99 GLU H H 1 8.36 0.02 . 1 . . . . . . . . 5156 2 558 . 1 1 99 99 GLU HA H 1 4.24 0.02 . 1 . . . . . . . . 5156 2 559 . 1 1 99 99 GLU HB2 H 1 1.98 0.02 . 2 . . . . . . . . 5156 2 560 . 1 1 99 99 GLU C C 13 176.8 0.2 . 1 . . . . . . . . 5156 2 561 . 1 1 99 99 GLU CA C 13 56.8 0.2 . 1 . . . . . . . . 5156 2 562 . 1 1 99 99 GLU CB C 13 30.7 0.2 . 1 . . . . . . . . 5156 2 563 . 1 1 99 99 GLU N N 15 122.2 0.2 . 1 . . . . . . . . 5156 2 564 . 1 1 100 100 GLU H H 1 8.26 0.02 . 1 . . . . . . . . 5156 2 565 . 1 1 100 100 GLU HA H 1 4.19 0.02 . 1 . . . . . . . . 5156 2 566 . 1 1 100 100 GLU HB2 H 1 1.82 0.02 . 1 . . . . . . . . 5156 2 567 . 1 1 100 100 GLU C C 13 176.1 0.2 . 1 . . . . . . . . 5156 2 568 . 1 1 100 100 GLU CA C 13 56.9 0.2 . 1 . . . . . . . . 5156 2 569 . 1 1 100 100 GLU CB C 13 30.8 0.2 . 1 . . . . . . . . 5156 2 570 . 1 1 100 100 GLU N N 15 120.5 0.2 . 1 . . . . . . . . 5156 2 571 . 1 1 101 101 ASN H H 1 8.24 0.02 . 1 . . . . . . . . 5156 2 572 . 1 1 101 101 ASN HA H 1 4.65 0.02 . 1 . . . . . . . . 5156 2 573 . 1 1 101 101 ASN HB2 H 1 2.61 0.02 . 2 . . . . . . . . 5156 2 574 . 1 1 101 101 ASN HB3 H 1 2.69 0.02 . 2 . . . . . . . . 5156 2 575 . 1 1 101 101 ASN C C 13 174.1 0.2 . 1 . . . . . . . . 5156 2 576 . 1 1 101 101 ASN CA C 13 53.4 0.2 . 1 . . . . . . . . 5156 2 577 . 1 1 101 101 ASN CB C 13 39.5 0.2 . 1 . . . . . . . . 5156 2 578 . 1 1 101 101 ASN N N 15 119.3 0.2 . 1 . . . . . . . . 5156 2 579 . 1 1 102 102 PHE H H 1 7.65 0.02 . 1 . . . . . . . . 5156 2 580 . 1 1 102 102 PHE CA C 13 59.6 0.2 . 1 . . . . . . . . 5156 2 581 . 1 1 102 102 PHE N N 15 125.1 0.2 . 1 . . . . . . . . 5156 2 stop_ save_