data_4467 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4467 _Entry.Title ; Sequence-specific 1H, 13C, and 15N Assignments of the MAR-binding Domain of Chicken MeCP2/ARBP ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 1999-12-01 _Entry.Accession_date 1999-12-01 _Entry.Last_release_date . _Entry.Original_release_date . _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 Eike Brunner . . . 4467 2 Joachim Weitzel . . . 4467 3 Bjoern Heitmann . . . 4467 4 Till Maurer . . . 4467 5 Wolf Straetling . H. . 4467 6 'Hans Robert' Kalbitzer . . . 4467 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4467 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 231 4467 '13C chemical shifts' 319 4467 '15N chemical shifts' 109 4467 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 . . 2002-07-12 . update BMRB 'Modify the saveframe name.' 4467 2 . . 2000-12-15 . original author 'Original release.' 4467 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4280 . 4467 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4467 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 20377249 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Sequence-specific 1H, 13C, and 15N Assignments of the MAR-binding Domain of Chicken MeCP2/ARBP ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of Biomolecular NMR' _Citation.Journal_volume 17 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 175 _Citation.Page_last 176 _Citation.Year 2000 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Eike Brunner . . . 4467 1 2 Joachim Weitzel . . . 4467 1 3 Bjoern Heitmann . . . 4467 1 4 Till Maurer . . . 4467 1 5 Wolf Straetling . H. . 4467 1 6 'Hans Robert' Kalbitzer . . . 4467 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Chicken methyl-CpG-binding protein 2 (cMeCP2/ARBP)' 4467 1 'NMR assignments' 4467 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4467 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10508514 _Citation.Full_citation ; Amir, R.E., Van den Veyver, I.B., Wan, M., Tran, C.Q., Francke, U. and Zoghbi, H.Y. (1999) Nature Genet. 23, 185-188. ; _Citation.Title 'Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Genet.' _Citation.Journal_name_full 'Nature genetics' _Citation.Journal_volume 23 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1061-4036 _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 188 _Citation.Year 1999 _Citation.Details ; Rett syndrome (RTT, MIM 312750) is a progressive neurodevelopmental disorder and one of the most common causes of mental retardation in females, with an incidence of 1 in 10,000-15,000 (ref. 2). Patients with classic RTT appear to develop normally until 6-18 months of age, then gradually lose speech and purposeful hand use, and develop microcephaly, seizures, autism, ataxia, intermittent hyperventilation and stereotypic hand movements. After initial regression, the condition stabilizes and patients usually survive into adulthood. As RTT occurs almost exclusively in females, it has been proposed that RTT is caused by an X-linked dominant mutation with lethality in hemizygous males. Previous exclusion mapping studies using RTT families mapped the locus to Xq28 (refs 6,9,10,11). Using a systematic gene screening approach, we have identified mutations in the gene (MECP2 ) encoding X-linked methyl-CpG-binding protein 2 (MeCP2) as the cause of some cases of RTT. MeCP2 selectively binds CpG dinucleotides in the mammalian genome and mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A (refs 12,13). In 5 of 21 sporadic patients, we found 3 de novo missense mutations in the region encoding the highly conserved methyl-binding domain (MBD) as well as a de novo frameshift and a de novo nonsense mutation, both of which disrupt the transcription repression domain (TRD). In two affected half-sisters of a RTT family, we found segregation of an additional missense mutation not detected in their obligate carrier mother. This suggests that the mother is a germline mosaic for this mutation. Our study reports the first disease-causing mutations in RTT and points to abnormal epigenetic regulation as the mechanism underlying the pathogenesis of RTT. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'R. E.' Amir R. E. . 4467 2 2 'I. B.' 'Van den Veyver' I. B. . 4467 2 3 M. Wan M. . . 4467 2 4 'C. Q.' Tran C. Q. . 4467 2 5 U. Francke U. . . 4467 2 6 'H. Y.' Zoghbi H. Y. . 4467 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4467 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9620779 _Citation.Full_citation ; Jones, P.L., Veenstra, G.J.C., Wade, P.A., Vermaak, D., Kass, S.U., Landsberger, N., Strouboulis, J. and Wolffe, A.P. (1998) Nature Genet. 19, 187-191. ; _Citation.Title 'Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nat. Genet.' _Citation.Journal_name_full 'Nature genetics' _Citation.Journal_volume 19 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1061-4036 _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 187 _Citation.Page_last 191 _Citation.Year 1998 _Citation.Details ; CpG methylation in vertebrates correlates with alterations in chromatin structure and gene silencing. Differences in DNA-methylation status are associated with imprinting phenomena and carcinogenesis. In Xenopus laevis oocytes, DNA methylation dominantly silences transcription through the assembly of a repressive nucleosomal array. Methylated DNA assembled into chromatin binds the transcriptional repressor MeCP2 which cofractionates with Sin3 and histone deacetylase. Silencing conferred by MeCP2 and methylated DNA can be relieved by inhibition of histone deacetylase, facilitating the remodelling of chromatin and transcriptional activation. These results establish a direct causal relationship between DNA methylation-dependent transcriptional silencing and the modification of chromatin. ; 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 'P. L.' Jones P. L. . 4467 3 2 'G. J.' Veenstra G. J. . 4467 3 3 'P. A.' Wade P. A. . 4467 3 4 D. Vermaak D. . . 4467 3 5 'S. U.' Kass S. U. . 4467 3 6 N. Landsberger N. . . 4467 3 7 J. Strouboulis J. . . 4467 3 8 'A. P.' Wolffe A. P. . 4467 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4467 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1606614 _Citation.Full_citation ; Lewis, J.D., Meehan, R.R., Henzel, W.J., Maurer-Fogy, I., Jeppesen, P., Klein, F. and Bird, A. (1992) Cell 69, 905-914. ; _Citation.Title 'Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Cell _Citation.Journal_name_full Cell _Citation.Journal_volume 69 _Citation.Journal_issue 6 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0092-8674 _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 905 _Citation.Page_last 914 _Citation.Year 1992 _Citation.Details ; Methylation of mammalian DNA can lead to repression of transcription and alteration of chromatin structure. Recent evidence suggests that both effects are the result of an interaction between the methylated sites and methyl-CpG-binding proteins (MeCPs). MeCP1 has previously been detected in crude nuclear extracts. Here we report the identification, purification, and cDNA cloning of a novel MeCP called MeCP2. Unlike MeCP1, the new protein is able to bind to DNA that contains a single methyl-CpG pair. By staining with an antibody, we show that the distribution of MeCP2 along the chromosomes parallels that of methyl-CpG. In mouse, for example, MeCP2 is concentrated in pericentromeric heterochromatin, which contains a large fraction (about 40%) of all genomic 5-methylcytosine. ; 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. D.' Lewis J. D. . 4467 4 2 'R. R.' Meehan R. R. . 4467 4 3 'W. J.' Henzel W. J. . 4467 4 4 I. Maurer-Fogy I. . . 4467 4 5 P. Jeppesen P. . . 4467 4 6 F. Klein F. . . 4467 4 7 A. Bird A. . . 4467 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4467 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Markley, J.L., Bax, A., Arata, Y., Hilbers, C.W., Kaptein, R., Sykes, B.D., Wright, P.E. and W?thrich, K. (1998) Pure & Appl. Chem. 70, 117-142. ; _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_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 4467 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8177735 _Citation.Full_citation 'Nan, X., Meehan, R.R. and Bird, A. (1993) Nucleic Acids Res. 21, 4886-4892.' _Citation.Title 'Dissection of the methyl-CpG binding domain from the chromosomal protein MeCP2.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nucleic Acids Res.' _Citation.Journal_name_full 'Nucleic acids research' _Citation.Journal_volume 21 _Citation.Journal_issue 21 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0305-1048 _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 4886 _Citation.Page_last 4892 _Citation.Year 1993 _Citation.Details ; MeCP2 is a chromosomal protein which binds to DNA that is methylated at CpG. In situ immunofluorescence in mouse cells has shown that the protein is most concentrated in pericentromeric heterochromatin, suggesting that MeCP2 may play a role in the formation of inert chromatin. Here we have isolated a minimal methyl-CpG binding domain (MBD) from MeCP2. MBD is 85 amino acids in length, and binds exclusively to DNA that contains one or more symmetrically methylated CpGs. MBD has negligable non-specific affinity for DNA, confirming that non-specific and methyl-CpG specific binding domains of MeCP2 are distinct. In vitro footprinting indicates that MBD binding can protect a 12 nucleotide region surrounding a methyl-CpG pair, with an approximate dissociation constant of 10(-9) M. ; 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 X. Nan X. . . 4467 6 2 'R. R.' Meehan R. R. . 4467 6 3 A. Bird A. . . 4467 6 stop_ save_ save_ref_6 _Citation.Sf_category citations _Citation.Sf_framecode ref_6 _Citation.Entry_ID 4467 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9038338 _Citation.Full_citation 'Nan, X., Campoy, F.J. and Bird, A. (1997) Cell 88, 471-481.' _Citation.Title 'MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Cell _Citation.Journal_name_full Cell _Citation.Journal_volume 88 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0092-8674 _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 471 _Citation.Page_last 481 _Citation.Year 1997 _Citation.Details ; MeCP2 is an abundant mammalian protein that binds to methylated CpG. We have found that native and recombinant MeCP2 repress transcription in vitro from methylated promoters but do not repress nonmethylated promoters. Repression is nonlinearly dependent on the local density of methylation, becoming significant at the density found in bulk vertebrate genomic DNA. Transient transfection using fusions with the GAL4 DNA binding domain identified a region of MeCP2 that is capable of long-range repression in vivo. Moreover, MeCP2 is able to displace histone H1 from preassembled chromatin that contains methyl-CpG. These properties, together with the abundance of MeCP2 and the high frequency of its 2 bp binding site, suggest a role as a global transcriptional repressor in vertebrate genomes. ; 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 X. Nan X. . . 4467 7 2 'F. J.' Campoy F. J. . 4467 7 3 A. Bird A. . . 4467 7 stop_ save_ save_ref_7 _Citation.Sf_category citations _Citation.Sf_framecode ref_7 _Citation.Entry_ID 4467 _Citation.ID 8 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9620804 _Citation.Full_citation ; Nan, X., Ng, H.-H., Johnson, C.A., Laherty, C.D., Turner, B.M., Eisenmann, R.N. and Bird, A. (1998) Nature 393, 386-389. ; _Citation.Title 'Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Nature _Citation.Journal_name_full Nature _Citation.Journal_volume 393 _Citation.Journal_issue 6683 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0028-0836 _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 386 _Citation.Page_last 389 _Citation.Year 1998 _Citation.Details ; Cytosine residues in the sequence 5'CpG (cytosine-guanine) are often postsynthetically methylated in animal genomes. CpG methylation is involved in long-term silencing of certain genes during mammalian development and in repression of viral genomes. The methyl-CpG-binding proteins MeCP1 and MeCP2 interact specifically with methylated DNA and mediate transcriptional repression. Here we study the mechanism of repression by MeCP2, an abundant nuclear protein that is essential for mouse embryogenesis. MeCP2 binds tightly to chromosomes in a methylation-dependent manner. It contains a transcriptional-repression domain (TRD) that can function at a distance in vitro and in vivo. We show that a region of MeCP2 that localizes with the TRD associates with a corepressor complex containing the transcriptional repressor mSin3A and histone deacetylases. Transcriptional repression in vivo is relieved by the deacetylase inhibitor trichostatin A, indicating that deacetylation of histones (and/or of other proteins) is an essential component of this repression mechanism. The data suggest that two global mechanisms of gene regulation, DNA methylation and histone deacetylation, can be linked by MeCP2. ; 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 X. Nan X. . . 4467 8 2 'H. H.' Ng H. H. . 4467 8 3 'C. A.' Johnson C. A. . 4467 8 4 'C. D.' Laherty C. D. . 4467 8 5 'B. M.' Turner B. M. . 4467 8 6 'R. N.' Eisenman R. N. . 4467 8 7 A. Bird A. . . 4467 8 stop_ save_ save_ref_8 _Citation.Sf_category citations _Citation.Sf_framecode ref_8 _Citation.Entry_ID 4467 _Citation.ID 9 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1846084 _Citation.Full_citation 'von Kries, J.P., Buhrmester, H. and Str?tling, W.H. (1991) Cell 64, 123-135.' _Citation.Title 'A matrix/scaffold attachment region binding protein: identification, purification, and mode of binding.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Cell _Citation.Journal_name_full Cell _Citation.Journal_volume 64 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0092-8674 _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 123 _Citation.Page_last 135 _Citation.Year 1991 _Citation.Details ; Matrix/scaffold attachment regions (MARs/SARs) partition chromatin into functional loop domains. Here we have identified a chicken protein that selectively binds to MARs from the chicken lysozyme locus and to MARs from Drosophila, mouse, and human genes. This protein, named ARBP (for attachment region binding protein), was purified to homogeneity and shown to bind to MARs in a cooperative fashion. ARBP is an abundant nuclear protein and a component of the internal nuclear network. Deletion mutants indicate that multiple AT-rich sequences, if contained in a minimal approximately 350 bp MAR fragment, can lead to efficient binding of ARBP. Furthermore, dimerization mutants show that, to bind ARBP efficiently, MAR sequences can act synergistically over large distances, apparently with the intervening DNA looping out. The binding characteristics of ARBP to MARs reproduce those of unfractionated matrix preparations, suggesting that ARBP is an important nuclear element for the generation of functional chromatin loops. ; 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. P.' 'von Kries' J. P. . 4467 9 2 H. Buhrmester H. . . 4467 9 3 'W. H.' Stratling W. H. . 4467 9 stop_ save_ save_ref_9 _Citation.Sf_category citations _Citation.Sf_framecode ref_9 _Citation.Entry_ID 4467 _Citation.ID 10 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10518942 _Citation.Full_citation ; Wakefield, R.I.D., Smith, B.O., Nan, X., Free, A., Soteriou, A., Uhrin, D., Bird, A.P. and Barlow, P.N. (1999) J. Mol. Biol. 291, 1055-1065. ; _Citation.Title 'The solution structure of the domain from MeCP2 that binds to methylated DNA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 291 _Citation.Journal_issue 5 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _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 1055 _Citation.Page_last 1065 _Citation.Year 1999 _Citation.Details ; MeCP2 is an abundant mammalian protein that binds methylated CpG (mCpG) sequences within double-stranded DNA, represses transcription by recruiting histone deacetylases, and is essential for embryonic development. It is one of a family of proteins which mediate the biological consequences of DNA methylation. These proteins each possess a sequence motif of about 70 residues which, in MeCP2, form a domain necessary and sufficient for binding to mCpG. The solution structure of the mCpG-binding domain (MBD) from MeCP2 has been solved and the DNA-binding surface of the domain mapped using NMR spectroscopy. Residues 95-162 of MeCP2 adopt a novel fold forming a wedge-shaped structure. An N-terminal four-stranded antiparallel beta-sheet forms one face of the wedge, while the other face is formed mainly by a C-terminal helical region. The thin end of the wedge is extended by a long loop between beta-strands B and C containing many basic residues. The B-C loop together with residues in strands B, C and D, and at the N terminus of the alpha-helix, appears to form an interface with methylated DNA. Unstructured residues at the NH2 terminus of the domain are also involved in formation of the complex. The presence of numerous arginine and lysine side-chains on the DNA-binding surface of MBD is consistent with the requirement for the mCpG site to be flanked by non-specific sequences of base-pairs. The absence of symmetry in the domain implies that recognition does not exploit the symmetry of the binding site. A conserved hydrophobic pocket containing the side-chains of Tyr123 and Ile125 on the positively charged beta-sheet face is a candidate for the region of contact with the methyl-groups of the modified cytosine residues. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'R. I.' Wakefield R. I. . 4467 10 2 'B. O.' Smith B. O. . 4467 10 3 X. Nan X. . . 4467 10 4 A. Free A. . . 4467 10 5 A. Soteriou A. . . 4467 10 6 D. Uhrin D. . . 4467 10 7 'A. P.' Bird A. P. . 4467 10 8 'P. N.' Barlow P. N. . 4467 10 stop_ save_ save_ref_10 _Citation.Sf_category citations _Citation.Sf_framecode ref_10 _Citation.Entry_ID 4467 _Citation.ID 11 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9271441 _Citation.Full_citation ; Weitzel, J.M., Buhrmester, H. and Str?tling, W.H. (1997) Mol. Cell. Biol. 17, 5656-5666. ; _Citation.Title 'Chicken MAR-binding protein ARBP is homologous to rat methyl-CpG-binding protein MeCP2.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Mol. Cell. Biol.' _Citation.Journal_name_full 'Molecular and cellular biology' _Citation.Journal_volume 17 _Citation.Journal_issue 9 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0270-7306 _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 5656 _Citation.Page_last 5666 _Citation.Year 1997 _Citation.Details ; Here, we describe the cloning and further characterization of chicken ARBP, an abundant nuclear protein with a high affinity for MAR/SARs. Surprisingly, ARBP was found to be homologous to the rat protein MeCP2, previously identified as a methyl-CpG-binding protein. A region spanning 125 amino acids in the N-terminal halves is 96.8% identical between chicken ARBP and rat MeCP2. A deletion mutation analysis using Southwestern and band shift assays identified this highly conserved region as the MAR DNA binding domain. Alignment of chicken ARBP with rat and human MeCP2 proteins revealed six trinucleotide amplifications generating up to 34-fold repetitions of a single amino acid. Because MeCP2 was previously localized to pericentromeric heterochromatin in mouse chromosomes, we analyzed the in vitro binding of ARBP to various repetitive sequences. In band shift experiments, ARBP binds to two chicken repetitive sequences as well as to mouse satellite DNA with high affinity similar to that of its binding to chicken lysozyme MAR fragments. In mouse satellite DNA, use of several footprinting techniques characterized two high-affinity binding sites, whose sequences are related to the ARBP binding site consensus in the chicken lysozyme MAR (5'-GGTGT-3'). Band shift experiments indicated that methylation increased in vitro binding of ARBP to mouse satellite DNA two- to fivefold. Our results suggest that ARBP/MeCP2 is a multifunctional protein with roles in loop domain organization of chromatin, the structure of pericentromeric heterochromatin, and DNA methylation. ; 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. M.' Weitzel J. M. . 4467 11 2 H. Buhrmester H. . . 4467 11 3 'W. H.' Stratling W. H. . 4467 11 stop_ save_ save_ref_11 _Citation.Sf_category citations _Citation.Sf_framecode ref_11 _Citation.Entry_ID 4467 _Citation.ID 12 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8019132 _Citation.Full_citation 'Wishart, D.S. and Sykes B.D. (1994) J. Biomol. NMR 4, 171-180.' _Citation.Title 'The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.' _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 171 _Citation.Page_last 180 _Citation.Year 1994 _Citation.Details ; A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both 1H and 13C chemical-shift indices to produce a 'consensus' estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'D. S.' Wishart D. S. . 4467 12 2 'B. D.' Sykes B. D. . 4467 12 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_MeCP2_ARBP _Assembly.Sf_category assembly _Assembly.Sf_framecode system_MeCP2_ARBP _Assembly.Entry_ID 4467 _Assembly.ID 1 _Assembly.Name 'chicken MeCP2/ARBP monomer' _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 ; The sequence studied in our paper (125 residues) is significantly longer than the methyl binding domain studied in PDB entry 1qk9 (88 residues) and includes the complete biologically important domain binding nuclear matrix attached regions. A second difference is, that our system stems from chicken, the other one from rat. ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4467 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 MeCP2/ARBP 1 $MeCP2_ARBP . . . native . . . . . 4467 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1qk9 . . . . . . 4467 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'chicken MeCP2/ARBP monomer' system 4467 1 MeCP2/ARBP abbreviation 4467 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID ; methyl-CpG-binding protein, attachment region binding protein ; 4467 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_MeCP2_ARBP _Entity.Sf_category entity _Entity.Sf_framecode MeCP2_ARBP _Entity.Entry_ID 4467 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Methyl-CpG-binding protein, attachment region binding protein' _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 ; APAVPEASASPKQRRSIIRD RGPMYDDPTLPEGWTRKLKQ RKSGRSAGKYDVYLINPQGK AFRSKVELIAYFEKVGDTSL DPNDFDFTVTGRGSPSRREQ RPPKKAKSPKSPGSGRGRGR PKGSG ; _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 125 _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 16300 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 4280 . "Methyl binding domain of MeCP2" . . . . . 72.00 92 98.89 98.89 9.51e-56 . . . . 4467 1 2 no PDB 1QK9 . "The Solution Structure Of The Domain From Mecp2 That Binds To Methylated Dna" . . . . . 72.00 92 98.89 98.89 9.51e-56 . . . . 4467 1 3 no PDB 1UB1 . "Solution Structure Of The Matrix Attachment Region-Binding Domain Of Chicken Mecp2" . . . . . 100.00 133 100.00 100.00 6.98e-82 . . . . 4467 1 4 no EMBL CAA74577 . "attachment region binding protein, partial [Gallus gallus]" . . . . . 100.00 344 100.00 100.00 1.78e-80 . . . . 4467 1 5 no GB EPY78157 . "interleukin-1 receptor-associated kinase 1 [Camelus ferus]" . . . . . 70.40 786 100.00 100.00 6.90e-52 . . . . 4467 1 6 no REF XP_004645154 . "PREDICTED: methyl-CpG-binding protein 2 isoform X1 [Octodon degus]" . . . . . 100.00 498 97.60 99.20 5.64e-78 . . . . 4467 1 7 no REF XP_004645155 . "PREDICTED: methyl-CpG-binding protein 2 isoform X2 [Octodon degus]" . . . . . 100.00 486 97.60 99.20 5.44e-78 . . . . 4467 1 8 no REF XP_006113271 . "PREDICTED: methyl-CpG-binding protein 2 [Pelodiscus sinensis]" . . . . . 77.60 208 98.97 100.00 1.14e-61 . . . . 4467 1 9 no REF XP_007054114 . "PREDICTED: uncharacterized protein LOC102941306, partial [Chelonia mydas]" . . . . . 77.60 337 98.97 100.00 3.19e-60 . . . . 4467 1 10 no REF XP_008175578 . "PREDICTED: methyl-CpG-binding protein 2 [Chrysemys picta bellii]" . . . . . 60.00 141 98.67 98.67 6.85e-45 . . . . 4467 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Methyl-CpG-binding protein, attachment region binding protein' common 4467 1 MeCP2/ARBP abbreviation 4467 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 . ALA . 4467 1 2 . PRO . 4467 1 3 . ALA . 4467 1 4 . VAL . 4467 1 5 . PRO . 4467 1 6 . GLU . 4467 1 7 . ALA . 4467 1 8 . SER . 4467 1 9 . ALA . 4467 1 10 . SER . 4467 1 11 . PRO . 4467 1 12 . LYS . 4467 1 13 . GLN . 4467 1 14 . ARG . 4467 1 15 . ARG . 4467 1 16 . SER . 4467 1 17 . ILE . 4467 1 18 . ILE . 4467 1 19 . ARG . 4467 1 20 . ASP . 4467 1 21 . ARG . 4467 1 22 . GLY . 4467 1 23 . PRO . 4467 1 24 . MET . 4467 1 25 . TYR . 4467 1 26 . ASP . 4467 1 27 . ASP . 4467 1 28 . PRO . 4467 1 29 . THR . 4467 1 30 . LEU . 4467 1 31 . PRO . 4467 1 32 . GLU . 4467 1 33 . GLY . 4467 1 34 . TRP . 4467 1 35 . THR . 4467 1 36 . ARG . 4467 1 37 . LYS . 4467 1 38 . LEU . 4467 1 39 . LYS . 4467 1 40 . GLN . 4467 1 41 . ARG . 4467 1 42 . LYS . 4467 1 43 . SER . 4467 1 44 . GLY . 4467 1 45 . ARG . 4467 1 46 . SER . 4467 1 47 . ALA . 4467 1 48 . GLY . 4467 1 49 . LYS . 4467 1 50 . TYR . 4467 1 51 . ASP . 4467 1 52 . VAL . 4467 1 53 . TYR . 4467 1 54 . LEU . 4467 1 55 . ILE . 4467 1 56 . ASN . 4467 1 57 . PRO . 4467 1 58 . GLN . 4467 1 59 . GLY . 4467 1 60 . LYS . 4467 1 61 . ALA . 4467 1 62 . PHE . 4467 1 63 . ARG . 4467 1 64 . SER . 4467 1 65 . LYS . 4467 1 66 . VAL . 4467 1 67 . GLU . 4467 1 68 . LEU . 4467 1 69 . ILE . 4467 1 70 . ALA . 4467 1 71 . TYR . 4467 1 72 . PHE . 4467 1 73 . GLU . 4467 1 74 . LYS . 4467 1 75 . VAL . 4467 1 76 . GLY . 4467 1 77 . ASP . 4467 1 78 . THR . 4467 1 79 . SER . 4467 1 80 . LEU . 4467 1 81 . ASP . 4467 1 82 . PRO . 4467 1 83 . ASN . 4467 1 84 . ASP . 4467 1 85 . PHE . 4467 1 86 . ASP . 4467 1 87 . PHE . 4467 1 88 . THR . 4467 1 89 . VAL . 4467 1 90 . THR . 4467 1 91 . GLY . 4467 1 92 . ARG . 4467 1 93 . GLY . 4467 1 94 . SER . 4467 1 95 . PRO . 4467 1 96 . SER . 4467 1 97 . ARG . 4467 1 98 . ARG . 4467 1 99 . GLU . 4467 1 100 . GLN . 4467 1 101 . ARG . 4467 1 102 . PRO . 4467 1 103 . PRO . 4467 1 104 . LYS . 4467 1 105 . LYS . 4467 1 106 . ALA . 4467 1 107 . LYS . 4467 1 108 . SER . 4467 1 109 . PRO . 4467 1 110 . LYS . 4467 1 111 . SER . 4467 1 112 . PRO . 4467 1 113 . GLY . 4467 1 114 . SER . 4467 1 115 . GLY . 4467 1 116 . ARG . 4467 1 117 . GLY . 4467 1 118 . ARG . 4467 1 119 . GLY . 4467 1 120 . ARG . 4467 1 121 . PRO . 4467 1 122 . LYS . 4467 1 123 . GLY . 4467 1 124 . SER . 4467 1 125 . GLY . 4467 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 . ALA 1 1 4467 1 . PRO 2 2 4467 1 . ALA 3 3 4467 1 . VAL 4 4 4467 1 . PRO 5 5 4467 1 . GLU 6 6 4467 1 . ALA 7 7 4467 1 . SER 8 8 4467 1 . ALA 9 9 4467 1 . SER 10 10 4467 1 . PRO 11 11 4467 1 . LYS 12 12 4467 1 . GLN 13 13 4467 1 . ARG 14 14 4467 1 . ARG 15 15 4467 1 . SER 16 16 4467 1 . ILE 17 17 4467 1 . ILE 18 18 4467 1 . ARG 19 19 4467 1 . ASP 20 20 4467 1 . ARG 21 21 4467 1 . GLY 22 22 4467 1 . PRO 23 23 4467 1 . MET 24 24 4467 1 . TYR 25 25 4467 1 . ASP 26 26 4467 1 . ASP 27 27 4467 1 . PRO 28 28 4467 1 . THR 29 29 4467 1 . LEU 30 30 4467 1 . PRO 31 31 4467 1 . GLU 32 32 4467 1 . GLY 33 33 4467 1 . TRP 34 34 4467 1 . THR 35 35 4467 1 . ARG 36 36 4467 1 . LYS 37 37 4467 1 . LEU 38 38 4467 1 . LYS 39 39 4467 1 . GLN 40 40 4467 1 . ARG 41 41 4467 1 . LYS 42 42 4467 1 . SER 43 43 4467 1 . GLY 44 44 4467 1 . ARG 45 45 4467 1 . SER 46 46 4467 1 . ALA 47 47 4467 1 . GLY 48 48 4467 1 . LYS 49 49 4467 1 . TYR 50 50 4467 1 . ASP 51 51 4467 1 . VAL 52 52 4467 1 . TYR 53 53 4467 1 . LEU 54 54 4467 1 . ILE 55 55 4467 1 . ASN 56 56 4467 1 . PRO 57 57 4467 1 . GLN 58 58 4467 1 . GLY 59 59 4467 1 . LYS 60 60 4467 1 . ALA 61 61 4467 1 . PHE 62 62 4467 1 . ARG 63 63 4467 1 . SER 64 64 4467 1 . LYS 65 65 4467 1 . VAL 66 66 4467 1 . GLU 67 67 4467 1 . LEU 68 68 4467 1 . ILE 69 69 4467 1 . ALA 70 70 4467 1 . TYR 71 71 4467 1 . PHE 72 72 4467 1 . GLU 73 73 4467 1 . LYS 74 74 4467 1 . VAL 75 75 4467 1 . GLY 76 76 4467 1 . ASP 77 77 4467 1 . THR 78 78 4467 1 . SER 79 79 4467 1 . LEU 80 80 4467 1 . ASP 81 81 4467 1 . PRO 82 82 4467 1 . ASN 83 83 4467 1 . ASP 84 84 4467 1 . PHE 85 85 4467 1 . ASP 86 86 4467 1 . PHE 87 87 4467 1 . THR 88 88 4467 1 . VAL 89 89 4467 1 . THR 90 90 4467 1 . GLY 91 91 4467 1 . ARG 92 92 4467 1 . GLY 93 93 4467 1 . SER 94 94 4467 1 . PRO 95 95 4467 1 . SER 96 96 4467 1 . ARG 97 97 4467 1 . ARG 98 98 4467 1 . GLU 99 99 4467 1 . GLN 100 100 4467 1 . ARG 101 101 4467 1 . PRO 102 102 4467 1 . PRO 103 103 4467 1 . LYS 104 104 4467 1 . LYS 105 105 4467 1 . ALA 106 106 4467 1 . LYS 107 107 4467 1 . SER 108 108 4467 1 . PRO 109 109 4467 1 . LYS 110 110 4467 1 . SER 111 111 4467 1 . PRO 112 112 4467 1 . GLY 113 113 4467 1 . SER 114 114 4467 1 . GLY 115 115 4467 1 . ARG 116 116 4467 1 . GLY 117 117 4467 1 . ARG 118 118 4467 1 . GLY 119 119 4467 1 . ARG 120 120 4467 1 . PRO 121 121 4467 1 . LYS 122 122 4467 1 . GLY 123 123 4467 1 . SER 124 124 4467 1 . GLY 125 125 4467 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4467 _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 $MeCP2_ARBP . 9031 organism . 'Gallus gallus' chicken . . Eukaryota Metazoa Gallus gallus . . . . . . . . . . . . . . . . . . . . . 4467 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 4467 _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 $MeCP2_ARBP . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21(DE3)pLysS . . . . . . . . . . . . plasmid . . pET-cARBP-Ex4.2 . . . . . . 4467 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4467 _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 'Methyl-CpG-binding protein, attachment region binding protein' '[U-15N; U-13C]' . . 1 $MeCP2_ARBP . . 2.0 . . mM . . . . 4467 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4467 _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 'Methyl-CpG-binding protein, attachment region binding protein' [U-15N] . . 1 $MeCP2_ARBP . . 2.0 . . mM . . . . 4467 2 stop_ save_ save_sample_3 _Sample.Sf_category sample _Sample.Sf_framecode sample_3 _Sample.Entry_ID 4467 _Sample.ID 3 _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 'Methyl-CpG-binding protein, attachment region binding protein' . . . 1 $MeCP2_ARBP . . 2.0 . . mM . . . . 4467 3 stop_ save_ save_sample_4 _Sample.Sf_category sample _Sample.Sf_framecode sample_4 _Sample.Entry_ID 4467 _Sample.ID 4 _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 'Methyl-CpG-binding protein, attachment region binding protein' '[U-2H; U-13C; U-15N]' . . 1 $MeCP2_ARBP . . 2.0 . . mM . . . . 4467 4 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 4467 _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 6.8 0.1 n/a 4467 1 temperature 298 1 K 4467 1 stop_ save_ ############################ # Computer software used # ############################ save_AURELIA _Software.Sf_category software _Software.Sf_framecode AURELIA _Software.Entry_ID 4467 _Software.ID 1 _Software.Name AURELIA _Software.Version 2.5 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID visualisation 4467 1 stop_ save_ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 4467 _Software.ID 2 _Software.Name XWINNMR _Software.Version 2.5 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 4467 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 4467 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4467 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4467 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_1 Bruker DRX . 800 . . . 4467 1 2 NMR_spectrometer_2 Bruker DRX . 600 . . . 4467 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 4467 _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 HNCA . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4467 1 2 CBCA(CO)NH . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4467 1 3 1H-15N-HSQC . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4467 1 4 '1H-15N-NOESY HSQC' . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4467 1 5 '1H-15N-TOCSY HSQC' . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4467 1 6 HNCO . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4467 1 7 HCCH-TOCSY . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4467 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4467 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name HNCA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4467 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name CBCA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4467 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name 1H-15N-HSQC _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4467 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '1H-15N-NOESY HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4467 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '1H-15N-TOCSY HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 4467 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 4467 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name HCCH-TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # 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 4467 _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 . . . . . . . . . 4467 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4467 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4467 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_Assigned_chemical_shifts_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode Assigned_chemical_shifts_set_1 _Assigned_chem_shift_list.Entry_ID 4467 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 4467 1 . . 2 $sample_2 . 4467 1 . . 3 $sample_3 . 4467 1 . . 4 $sample_4 . 4467 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 1 1 ALA H H 1 8.453 0.02 . 1 . . . . . . . . 4467 1 2 . 1 1 1 1 ALA HA H 1 4.6 0.05 . 1 . . . . . . . . 4467 1 3 . 1 1 1 1 ALA CA C 13 50.33 0.2 . 1 . . . . . . . . 4467 1 4 . 1 1 1 1 ALA N N 15 126.5 0.34 . 1 . . . . . . . . 4467 1 5 . 1 1 2 2 PRO C C 13 176.4 0.2 . 1 . . . . . . . . 4467 1 6 . 1 1 2 2 PRO CA C 13 62.54 0.2 . 1 . . . . . . . . 4467 1 7 . 1 1 2 2 PRO CB C 13 31.5 0.2 . 1 . . . . . . . . 4467 1 8 . 1 1 3 3 ALA H H 1 8.426 0.02 . 1 . . . . . . . . 4467 1 9 . 1 1 3 3 ALA HA H 1 4.384 0.05 . 1 . . . . . . . . 4467 1 10 . 1 1 3 3 ALA C C 13 176.2 0.2 . 1 . . . . . . . . 4467 1 11 . 1 1 3 3 ALA CA C 13 52.08 0.2 . 1 . . . . . . . . 4467 1 12 . 1 1 3 3 ALA CB C 13 18.89 0.2 . 1 . . . . . . . . 4467 1 13 . 1 1 3 3 ALA N N 15 123.95 0.34 . 1 . . . . . . . . 4467 1 14 . 1 1 4 4 VAL H H 1 7.85 0.02 . 1 . . . . . . . . 4467 1 15 . 1 1 4 4 VAL HA H 1 4.289 0.05 . 1 . . . . . . . . 4467 1 16 . 1 1 4 4 VAL CA C 13 58.5 0.2 . 1 . . . . . . . . 4467 1 17 . 1 1 4 4 VAL N N 15 117.5 0.34 . 1 . . . . . . . . 4467 1 18 . 1 1 5 5 PRO C C 13 177.01 0.2 . 1 . . . . . . . . 4467 1 19 . 1 1 5 5 PRO CA C 13 62.82 0.2 . 1 . . . . . . . . 4467 1 20 . 1 1 5 5 PRO CB C 13 31.32 0.2 . 1 . . . . . . . . 4467 1 21 . 1 1 6 6 GLU H H 1 8.569 0.02 . 1 . . . . . . . . 4467 1 22 . 1 1 6 6 GLU HA H 1 4.372 0.05 . 1 . . . . . . . . 4467 1 23 . 1 1 6 6 GLU C C 13 176.6 0.2 . 1 . . . . . . . . 4467 1 24 . 1 1 6 6 GLU CA C 13 56.46 0.2 . 1 . . . . . . . . 4467 1 25 . 1 1 6 6 GLU CB C 13 29.5 0.2 . 1 . . . . . . . . 4467 1 26 . 1 1 6 6 GLU N N 15 120.7 0.34 . 1 . . . . . . . . 4467 1 27 . 1 1 7 7 ALA H H 1 8.43 0.02 . 1 . . . . . . . . 4467 1 28 . 1 1 7 7 ALA HA H 1 4.184 0.05 . 1 . . . . . . . . 4467 1 29 . 1 1 7 7 ALA C C 13 177.8 0.2 . 1 . . . . . . . . 4467 1 30 . 1 1 7 7 ALA CA C 13 52.47 0.2 . 1 . . . . . . . . 4467 1 31 . 1 1 7 7 ALA CB C 13 18.6 0.2 . 1 . . . . . . . . 4467 1 32 . 1 1 7 7 ALA N N 15 124.59 0.34 . 1 . . . . . . . . 4467 1 33 . 1 1 8 8 SER H H 1 8.263 0.02 . 1 . . . . . . . . 4467 1 34 . 1 1 8 8 SER HA H 1 4.327 0.05 . 1 . . . . . . . . 4467 1 35 . 1 1 8 8 SER C C 13 174.2 0.2 . 1 . . . . . . . . 4467 1 36 . 1 1 8 8 SER CA C 13 58.023 0.2 . 1 . . . . . . . . 4467 1 37 . 1 1 8 8 SER CB C 13 63.66 0.2 . 1 . . . . . . . . 4467 1 38 . 1 1 8 8 SER N N 15 114.3 0.34 . 1 . . . . . . . . 4467 1 39 . 1 1 9 9 ALA H H 1 8.262 0.02 . 1 . . . . . . . . 4467 1 40 . 1 1 9 9 ALA HA H 1 4.399 0.05 . 1 . . . . . . . . 4467 1 41 . 1 1 9 9 ALA C C 13 177.4 0.2 . 1 . . . . . . . . 4467 1 42 . 1 1 9 9 ALA CA C 13 52.03 0.2 . 1 . . . . . . . . 4467 1 43 . 1 1 9 9 ALA CB C 13 18.82 0.2 . 1 . . . . . . . . 4467 1 44 . 1 1 9 9 ALA N N 15 125.23 0.34 . 1 . . . . . . . . 4467 1 45 . 1 1 10 10 SER H H 1 8.278 0.02 . 1 . . . . . . . . 4467 1 46 . 1 1 10 10 SER HA H 1 4.661 0.05 . 1 . . . . . . . . 4467 1 47 . 1 1 10 10 SER CA C 13 56.14 0.2 . 1 . . . . . . . . 4467 1 48 . 1 1 10 10 SER N N 15 116.24 0.34 . 1 . . . . . . . . 4467 1 49 . 1 1 11 11 PRO C C 13 177.2 0.2 . 1 . . . . . . . . 4467 1 50 . 1 1 11 11 PRO CA C 13 63.15 0.2 . 1 . . . . . . . . 4467 1 51 . 1 1 11 11 PRO CB C 13 31.38 0.2 . 1 . . . . . . . . 4467 1 52 . 1 1 12 12 LYS H H 1 8.35 0.02 . 1 . . . . . . . . 4467 1 53 . 1 1 12 12 LYS HA H 1 4.463 0.05 . 1 . . . . . . . . 4467 1 54 . 1 1 12 12 LYS C C 13 176.78 0.2 . 1 . . . . . . . . 4467 1 55 . 1 1 12 12 LYS CA C 13 56.31 0.2 . 1 . . . . . . . . 4467 1 56 . 1 1 12 12 LYS CB C 13 32.46 0.2 . 1 . . . . . . . . 4467 1 57 . 1 1 12 12 LYS N N 15 120 0.34 . 1 . . . . . . . . 4467 1 58 . 1 1 13 13 GLN H H 1 8.27 0.02 . 1 . . . . . . . . 4467 1 59 . 1 1 13 13 GLN HA H 1 4.266 0.05 . 1 . . . . . . . . 4467 1 60 . 1 1 13 13 GLN C C 13 176.59 0.2 . 1 . . . . . . . . 4467 1 61 . 1 1 13 13 GLN CA C 13 55.65 0.2 . 1 . . . . . . . . 4467 1 62 . 1 1 13 13 GLN CB C 13 32.32 0.2 . 1 . . . . . . . . 4467 1 63 . 1 1 13 13 GLN N N 15 120 0.34 . 1 . . . . . . . . 4467 1 64 . 1 1 14 14 ARG H H 1 8.347 0.02 . 1 . . . . . . . . 4467 1 65 . 1 1 14 14 ARG HA H 1 4.231 0.05 . 1 . . . . . . . . 4467 1 66 . 1 1 14 14 ARG C C 13 176.11 0.2 . 1 . . . . . . . . 4467 1 67 . 1 1 14 14 ARG CA C 13 55.73 0.2 . 1 . . . . . . . . 4467 1 68 . 1 1 14 14 ARG CB C 13 29.2 0.2 . 1 . . . . . . . . 4467 1 69 . 1 1 14 14 ARG N N 15 122.66 0.34 . 1 . . . . . . . . 4467 1 70 . 1 1 15 15 ARG H H 1 8.407 0.02 . 1 . . . . . . . . 4467 1 71 . 1 1 15 15 ARG HA H 1 4.316 0.05 . 1 . . . . . . . . 4467 1 72 . 1 1 15 15 ARG C C 13 176.29 0.2 . 1 . . . . . . . . 4467 1 73 . 1 1 15 15 ARG CA C 13 56.1 0.2 . 1 . . . . . . . . 4467 1 74 . 1 1 15 15 ARG CB C 13 30.37 0.2 . 1 . . . . . . . . 4467 1 75 . 1 1 15 15 ARG N N 15 122 0.34 . 1 . . . . . . . . 4467 1 76 . 1 1 16 16 SER H H 1 8.39 0.02 . 1 . . . . . . . . 4467 1 77 . 1 1 16 16 SER HA H 1 4.358 0.05 . 1 . . . . . . . . 4467 1 78 . 1 1 16 16 SER C C 13 174.2 0.2 . 1 . . . . . . . . 4467 1 79 . 1 1 16 16 SER CA C 13 57.97 0.2 . 1 . . . . . . . . 4467 1 80 . 1 1 16 16 SER CB C 13 63.64 0.2 . 1 . . . . . . . . 4467 1 81 . 1 1 16 16 SER N N 15 116.88 0.34 . 1 . . . . . . . . 4467 1 82 . 1 1 17 17 ILE H H 1 8.209 0.02 . 1 . . . . . . . . 4467 1 83 . 1 1 17 17 ILE HA H 1 4.185 0.05 . 1 . . . . . . . . 4467 1 84 . 1 1 17 17 ILE C C 13 176 0.2 . 1 . . . . . . . . 4467 1 85 . 1 1 17 17 ILE CA C 13 60.8 0.2 . 1 . . . . . . . . 4467 1 86 . 1 1 17 17 ILE CB C 13 38 0.2 . 1 . . . . . . . . 4467 1 87 . 1 1 17 17 ILE N N 15 122 0.34 . 1 . . . . . . . . 4467 1 88 . 1 1 18 18 ILE H H 1 8.251 0.02 . 1 . . . . . . . . 4467 1 89 . 1 1 18 18 ILE HA H 1 4.194 0.05 . 1 . . . . . . . . 4467 1 90 . 1 1 18 18 ILE C C 13 175.2 0.2 . 1 . . . . . . . . 4467 1 91 . 1 1 18 18 ILE CA C 13 60.67 0.2 . 1 . . . . . . . . 4467 1 92 . 1 1 18 18 ILE CB C 13 37.7 0.2 . 1 . . . . . . . . 4467 1 93 . 1 1 18 18 ILE N N 15 124.59 0.34 . 1 . . . . . . . . 4467 1 94 . 1 1 19 19 ARG H H 1 8.422 0.02 . 1 . . . . . . . . 4467 1 95 . 1 1 19 19 ARG HA H 1 4.147 0.05 . 1 . . . . . . . . 4467 1 96 . 1 1 19 19 ARG C C 13 174.66 0.2 . 1 . . . . . . . . 4467 1 97 . 1 1 19 19 ARG CA C 13 55.7 0.2 . 1 . . . . . . . . 4467 1 98 . 1 1 19 19 ARG CB C 13 30.54 0.2 . 1 . . . . . . . . 4467 1 99 . 1 1 19 19 ARG N N 15 125.23 0.34 . 1 . . . . . . . . 4467 1 100 . 1 1 20 20 ASP H H 1 8.355 0.02 . 1 . . . . . . . . 4467 1 101 . 1 1 20 20 ASP HA H 1 4.34 0.05 . 1 . . . . . . . . 4467 1 102 . 1 1 20 20 ASP C C 13 175.83 0.2 . 1 . . . . . . . . 4467 1 103 . 1 1 20 20 ASP CA C 13 54.09 0.2 . 1 . . . . . . . . 4467 1 104 . 1 1 20 20 ASP CB C 13 40.6 0.2 . 1 . . . . . . . . 4467 1 105 . 1 1 20 20 ASP N N 15 121.38 0.34 . 1 . . . . . . . . 4467 1 106 . 1 1 21 21 ARG H H 1 8.355 0.02 . 1 . . . . . . . . 4467 1 107 . 1 1 21 21 ARG C C 13 176.27 0.2 . 1 . . . . . . . . 4467 1 108 . 1 1 21 21 ARG CA C 13 55.96 0.2 . 1 . . . . . . . . 4467 1 109 . 1 1 21 21 ARG CB C 13 30.79 0.2 . 1 . . . . . . . . 4467 1 110 . 1 1 21 21 ARG N N 15 120.74 0.34 . 1 . . . . . . . . 4467 1 111 . 1 1 22 22 GLY H H 1 8.357 0.02 . 1 . . . . . . . . 4467 1 112 . 1 1 22 22 GLY HA2 H 1 4.337 0.05 . 2 . . . . . . . . 4467 1 113 . 1 1 22 22 GLY HA3 H 1 4.042 0.05 . 2 . . . . . . . . 4467 1 114 . 1 1 22 22 GLY CA C 13 44.2 0.2 . 1 . . . . . . . . 4467 1 115 . 1 1 22 22 GLY N N 15 109.2 0.34 . 1 . . . . . . . . 4467 1 116 . 1 1 23 23 PRO C C 13 177.17 0.2 . 1 . . . . . . . . 4467 1 117 . 1 1 23 23 PRO CA C 13 62.58 0.2 . 1 . . . . . . . . 4467 1 118 . 1 1 23 23 PRO CB C 13 33.76 0.2 . 1 . . . . . . . . 4467 1 119 . 1 1 24 24 MET CA C 13 56.5 0.2 . 1 . . . . . . . . 4467 1 120 . 1 1 24 24 MET CB C 13 34.5 0.2 . 1 . . . . . . . . 4467 1 121 . 1 1 25 25 TYR H H 1 8.4 0.02 . 1 . . . . . . . . 4467 1 122 . 1 1 25 25 TYR HA H 1 4.368 0.05 . 1 . . . . . . . . 4467 1 123 . 1 1 25 25 TYR C C 13 174.84 0.2 . 1 . . . . . . . . 4467 1 124 . 1 1 25 25 TYR CA C 13 60.6 0.2 . 1 . . . . . . . . 4467 1 125 . 1 1 25 25 TYR CB C 13 38.55 0.2 . 1 . . . . . . . . 4467 1 126 . 1 1 25 25 TYR N N 15 124.05 0.34 . 1 . . . . . . . . 4467 1 127 . 1 1 26 26 ASP H H 1 7.679 0.02 . 1 . . . . . . . . 4467 1 128 . 1 1 26 26 ASP HA H 1 4.906 0.05 . 1 . . . . . . . . 4467 1 129 . 1 1 26 26 ASP C C 13 174.06 0.2 . 1 . . . . . . . . 4467 1 130 . 1 1 26 26 ASP CA C 13 52.647 0.2 . 1 . . . . . . . . 4467 1 131 . 1 1 26 26 ASP CB C 13 43.3 0.2 . 1 . . . . . . . . 4467 1 132 . 1 1 26 26 ASP N N 15 115.5 0.34 . 1 . . . . . . . . 4467 1 133 . 1 1 27 27 ASP H H 1 8.748 0.02 . 1 . . . . . . . . 4467 1 134 . 1 1 27 27 ASP HA H 1 5.3 0.05 . 1 . . . . . . . . 4467 1 135 . 1 1 27 27 ASP CA C 13 50.01 0.2 . 1 . . . . . . . . 4467 1 136 . 1 1 27 27 ASP CB C 13 43.09 0.2 . 1 . . . . . . . . 4467 1 137 . 1 1 27 27 ASP N N 15 118.81 0.34 . 1 . . . . . . . . 4467 1 138 . 1 1 28 28 PRO C C 13 176.8 0.2 . 1 . . . . . . . . 4467 1 139 . 1 1 28 28 PRO CA C 13 63.2 0.2 . 1 . . . . . . . . 4467 1 140 . 1 1 28 28 PRO CB C 13 31.9 0.2 . 1 . . . . . . . . 4467 1 141 . 1 1 29 29 THR H H 1 8.44 0.02 . 1 . . . . . . . . 4467 1 142 . 1 1 29 29 THR HA H 1 4.25 0.05 . 1 . . . . . . . . 4467 1 143 . 1 1 29 29 THR C C 13 175.4 0.2 . 1 . . . . . . . . 4467 1 144 . 1 1 29 29 THR CA C 13 61.9 0.2 . 1 . . . . . . . . 4467 1 145 . 1 1 29 29 THR CB C 13 68.96 0.2 . 1 . . . . . . . . 4467 1 146 . 1 1 29 29 THR N N 15 109.8 0.34 . 1 . . . . . . . . 4467 1 147 . 1 1 30 30 LEU H H 1 7.025 0.02 . 1 . . . . . . . . 4467 1 148 . 1 1 30 30 LEU HA H 1 4.136 0.05 . 1 . . . . . . . . 4467 1 149 . 1 1 30 30 LEU CA C 13 53.152 0.2 . 1 . . . . . . . . 4467 1 150 . 1 1 30 30 LEU N N 15 123.3 0.34 . 1 . . . . . . . . 4467 1 151 . 1 1 31 31 PRO HA H 1 4.707 0.05 . 1 . . . . . . . . 4467 1 152 . 1 1 31 31 PRO C C 13 175.75 0.2 . 1 . . . . . . . . 4467 1 153 . 1 1 31 31 PRO CA C 13 61.985 0.2 . 1 . . . . . . . . 4467 1 154 . 1 1 31 31 PRO CB C 13 30.45 0.2 . 1 . . . . . . . . 4467 1 155 . 1 1 32 32 GLU H H 1 8.438 0.02 . 1 . . . . . . . . 4467 1 156 . 1 1 32 32 GLU HA H 1 5.44 0.05 . 1 . . . . . . . . 4467 1 157 . 1 1 32 32 GLU C C 13 175.4 0.2 . 1 . . . . . . . . 4467 1 158 . 1 1 32 32 GLU CA C 13 58.22 0.2 . 1 . . . . . . . . 4467 1 159 . 1 1 32 32 GLU CB C 13 29.1 0.2 . 1 . . . . . . . . 4467 1 160 . 1 1 32 32 GLU N N 15 120 0.34 . 1 . . . . . . . . 4467 1 161 . 1 1 33 33 GLY H H 1 8.928 0.02 . 1 . . . . . . . . 4467 1 162 . 1 1 33 33 GLY HA2 H 1 4.35 0.05 . 2 . . . . . . . . 4467 1 163 . 1 1 33 33 GLY HA3 H 1 3.721 0.05 . 2 . . . . . . . . 4467 1 164 . 1 1 33 33 GLY C C 13 173.2 0.2 . 1 . . . . . . . . 4467 1 165 . 1 1 33 33 GLY CA C 13 45.32 0.2 . 1 . . . . . . . . 4467 1 166 . 1 1 33 33 GLY N N 15 113.67 0.34 . 1 . . . . . . . . 4467 1 167 . 1 1 34 34 TRP H H 1 8.498 0.02 . 1 . . . . . . . . 4467 1 168 . 1 1 34 34 TRP HA H 1 5.249 0.05 . 1 . . . . . . . . 4467 1 169 . 1 1 34 34 TRP C C 13 174.2 0.2 . 1 . . . . . . . . 4467 1 170 . 1 1 34 34 TRP CA C 13 57.2 0.2 . 1 . . . . . . . . 4467 1 171 . 1 1 34 34 TRP CB C 13 29.2 0.2 . 1 . . . . . . . . 4467 1 172 . 1 1 34 34 TRP N N 15 121.4 0.34 . 1 . . . . . . . . 4467 1 173 . 1 1 35 35 THR H H 1 9.209 0.02 . 1 . . . . . . . . 4467 1 174 . 1 1 35 35 THR HA H 1 4.705 0.05 . 1 . . . . . . . . 4467 1 175 . 1 1 35 35 THR C C 13 172 0.2 . 1 . . . . . . . . 4467 1 176 . 1 1 35 35 THR CA C 13 60.8 0.2 . 1 . . . . . . . . 4467 1 177 . 1 1 35 35 THR CB C 13 72.4 0.2 . 1 . . . . . . . . 4467 1 178 . 1 1 35 35 THR N N 15 112.39 0.34 . 1 . . . . . . . . 4467 1 179 . 1 1 36 36 ARG H H 1 8.446 0.02 . 1 . . . . . . . . 4467 1 180 . 1 1 36 36 ARG HA H 1 5.46 0.05 . 1 . . . . . . . . 4467 1 181 . 1 1 36 36 ARG C C 13 175 0.2 . 1 . . . . . . . . 4467 1 182 . 1 1 36 36 ARG CA C 13 53.8 0.2 . 1 . . . . . . . . 4467 1 183 . 1 1 36 36 ARG CB C 13 33.5 0.2 . 1 . . . . . . . . 4467 1 184 . 1 1 36 36 ARG N N 15 120 0.34 . 1 . . . . . . . . 4467 1 185 . 1 1 37 37 LYS H H 1 9.479 0.02 . 1 . . . . . . . . 4467 1 186 . 1 1 37 37 LYS HA H 1 4.878 0.05 . 1 . . . . . . . . 4467 1 187 . 1 1 37 37 LYS C C 13 174.1 0.2 . 1 . . . . . . . . 4467 1 188 . 1 1 37 37 LYS CA C 13 54.4 0.2 . 1 . . . . . . . . 4467 1 189 . 1 1 37 37 LYS CB C 13 35.2 0.2 . 1 . . . . . . . . 4467 1 190 . 1 1 37 37 LYS N N 15 123.95 0.34 . 1 . . . . . . . . 4467 1 191 . 1 1 38 38 LEU H H 1 9.04 0.02 . 1 . . . . . . . . 4467 1 192 . 1 1 38 38 LEU HA H 1 5.384 0.05 . 1 . . . . . . . . 4467 1 193 . 1 1 38 38 LEU C C 13 177.3 0.2 . 1 . . . . . . . . 4467 1 194 . 1 1 38 38 LEU CA C 13 53.6 0.2 . 1 . . . . . . . . 4467 1 195 . 1 1 38 38 LEU CB C 13 42.8 0.2 . 1 . . . . . . . . 4467 1 196 . 1 1 38 38 LEU N N 15 125.23 0.34 . 1 . . . . . . . . 4467 1 197 . 1 1 39 39 LYS H H 1 9.035 0.02 . 1 . . . . . . . . 4467 1 198 . 1 1 39 39 LYS HA H 1 4.895 0.05 . 1 . . . . . . . . 4467 1 199 . 1 1 39 39 LYS C C 13 175.4 0.2 . 1 . . . . . . . . 4467 1 200 . 1 1 39 39 LYS CA C 13 54.6 0.2 . 1 . . . . . . . . 4467 1 201 . 1 1 39 39 LYS CB C 13 35.04 0.2 . 1 . . . . . . . . 4467 1 202 . 1 1 39 39 LYS N N 15 122 0.34 . 1 . . . . . . . . 4467 1 203 . 1 1 40 40 GLN H H 1 9.192 0.02 . 1 . . . . . . . . 4467 1 204 . 1 1 40 40 GLN HA H 1 4.24 0.05 . 1 . . . . . . . . 4467 1 205 . 1 1 40 40 GLN C C 13 175.9 0.2 . 1 . . . . . . . . 4467 1 206 . 1 1 40 40 GLN CA C 13 55.72 0.2 . 1 . . . . . . . . 4467 1 207 . 1 1 40 40 GLN CB C 13 29.2 0.2 . 1 . . . . . . . . 4467 1 208 . 1 1 40 40 GLN N N 15 126.5 0.34 . 1 . . . . . . . . 4467 1 209 . 1 1 41 41 ARG H H 1 8.806 0.02 . 1 . . . . . . . . 4467 1 210 . 1 1 41 41 ARG HA H 1 5 0.05 . 1 . . . . . . . . 4467 1 211 . 1 1 41 41 ARG CA C 13 56.1 0.2 . 1 . . . . . . . . 4467 1 212 . 1 1 41 41 ARG CB C 13 30.05 0.2 . 1 . . . . . . . . 4467 1 213 . 1 1 41 41 ARG N N 15 125.7 0.34 . 1 . . . . . . . . 4467 1 214 . 1 1 42 42 LYS H H 1 8.771 0.02 . 1 . . . . . . . . 4467 1 215 . 1 1 42 42 LYS HA H 1 4.316 0.05 . 1 . . . . . . . . 4467 1 216 . 1 1 42 42 LYS C C 13 176.1 0.2 . 1 . . . . . . . . 4467 1 217 . 1 1 42 42 LYS CA C 13 56.36 0.2 . 1 . . . . . . . . 4467 1 218 . 1 1 42 42 LYS CB C 13 32.7 0.2 . 1 . . . . . . . . 4467 1 219 . 1 1 42 42 LYS N N 15 123.3 0.34 . 1 . . . . . . . . 4467 1 220 . 1 1 43 43 SER H H 1 7.94 0.02 . 1 . . . . . . . . 4467 1 221 . 1 1 43 43 SER HA H 1 4.752 0.05 . 1 . . . . . . . . 4467 1 222 . 1 1 43 43 SER C C 13 176.27 0.2 . 1 . . . . . . . . 4467 1 223 . 1 1 43 43 SER CA C 13 57.15 0.2 . 1 . . . . . . . . 4467 1 224 . 1 1 43 43 SER CB C 13 64.56 0.2 . 1 . . . . . . . . 4467 1 225 . 1 1 43 43 SER N N 15 113.67 0.34 . 1 . . . . . . . . 4467 1 226 . 1 1 44 44 GLY H H 1 8.586 0.02 . 1 . . . . . . . . 4467 1 227 . 1 1 44 44 GLY HA2 H 1 4.176 0.05 . 2 . . . . . . . . 4467 1 228 . 1 1 44 44 GLY HA3 H 1 3.896 0.05 . 2 . . . . . . . . 4467 1 229 . 1 1 44 44 GLY C C 13 177.03 0.2 . 1 . . . . . . . . 4467 1 230 . 1 1 44 44 GLY CA C 13 45.12 0.2 . 1 . . . . . . . . 4467 1 231 . 1 1 44 44 GLY N N 15 109.2 0.34 . 1 . . . . . . . . 4467 1 232 . 1 1 45 45 ARG H H 1 8.596 0.02 . 1 . . . . . . . . 4467 1 233 . 1 1 45 45 ARG HA H 1 4.386 0.05 . 1 . . . . . . . . 4467 1 234 . 1 1 45 45 ARG CA C 13 57.21 0.2 . 1 . . . . . . . . 4467 1 235 . 1 1 45 45 ARG CB C 13 29.66 0.2 . 1 . . . . . . . . 4467 1 236 . 1 1 45 45 ARG N N 15 120 0.34 . 1 . . . . . . . . 4467 1 237 . 1 1 46 46 SER H H 1 8.375 0.02 . 1 . . . . . . . . 4467 1 238 . 1 1 46 46 SER HA H 1 4.503 0.05 . 1 . . . . . . . . 4467 1 239 . 1 1 46 46 SER C C 13 173.9 0.2 . 1 . . . . . . . . 4467 1 240 . 1 1 46 46 SER CA C 13 57.45 0.2 . 1 . . . . . . . . 4467 1 241 . 1 1 46 46 SER CB C 13 63.05 0.2 . 1 . . . . . . . . 4467 1 242 . 1 1 46 46 SER N N 15 114.31 0.34 . 1 . . . . . . . . 4467 1 243 . 1 1 47 47 ALA H H 1 7.76 0.02 . 1 . . . . . . . . 4467 1 244 . 1 1 47 47 ALA HA H 1 3.961 0.05 . 1 . . . . . . . . 4467 1 245 . 1 1 47 47 ALA C C 13 178 0.2 . 1 . . . . . . . . 4467 1 246 . 1 1 47 47 ALA CA C 13 53.06 0.2 . 1 . . . . . . . . 4467 1 247 . 1 1 47 47 ALA CB C 13 18.1 0.2 . 1 . . . . . . . . 4467 1 248 . 1 1 47 47 ALA N N 15 123.3 0.34 . 1 . . . . . . . . 4467 1 249 . 1 1 48 48 GLY H H 1 8.513 0.02 . 1 . . . . . . . . 4467 1 250 . 1 1 48 48 GLY HA2 H 1 4.15 0.05 . 2 . . . . . . . . 4467 1 251 . 1 1 48 48 GLY HA3 H 1 3.88 0.05 . 2 . . . . . . . . 4467 1 252 . 1 1 48 48 GLY C C 13 174 0.2 . 1 . . . . . . . . 4467 1 253 . 1 1 48 48 GLY CA C 13 44.93 0.2 . 1 . . . . . . . . 4467 1 254 . 1 1 48 48 GLY N N 15 109.2 0.34 . 1 . . . . . . . . 4467 1 255 . 1 1 49 49 LYS H H 1 8.02 0.02 . 1 . . . . . . . . 4467 1 256 . 1 1 49 49 LYS HA H 1 4.42 0.05 . 1 . . . . . . . . 4467 1 257 . 1 1 49 49 LYS C C 13 175.5 0.2 . 1 . . . . . . . . 4467 1 258 . 1 1 49 49 LYS CA C 13 55.68 0.2 . 1 . . . . . . . . 4467 1 259 . 1 1 49 49 LYS CB C 13 33.05 0.2 . 1 . . . . . . . . 4467 1 260 . 1 1 49 49 LYS N N 15 120 0.34 . 1 . . . . . . . . 4467 1 261 . 1 1 50 50 TYR H H 1 8.576 0.02 . 1 . . . . . . . . 4467 1 262 . 1 1 50 50 TYR HA H 1 5.007 0.05 . 1 . . . . . . . . 4467 1 263 . 1 1 50 50 TYR C C 13 175.1 0.2 . 1 . . . . . . . . 4467 1 264 . 1 1 50 50 TYR CA C 13 57.7 0.2 . 1 . . . . . . . . 4467 1 265 . 1 1 50 50 TYR CB C 13 40.8 0.2 . 1 . . . . . . . . 4467 1 266 . 1 1 50 50 TYR N N 15 118.2 0.34 . 1 . . . . . . . . 4467 1 267 . 1 1 51 51 ASP H H 1 9.002 0.02 . 1 . . . . . . . . 4467 1 268 . 1 1 51 51 ASP HA H 1 5.052 0.05 . 1 . . . . . . . . 4467 1 269 . 1 1 51 51 ASP CA C 13 53.5 0.2 . 1 . . . . . . . . 4467 1 270 . 1 1 51 51 ASP N N 15 120 0.34 . 1 . . . . . . . . 4467 1 271 . 1 1 52 52 VAL H H 1 7.56 0.02 . 1 . . . . . . . . 4467 1 272 . 1 1 52 52 VAL HA H 1 4.385 0.05 . 1 . . . . . . . . 4467 1 273 . 1 1 52 52 VAL C C 13 174.5 0.2 . 1 . . . . . . . . 4467 1 274 . 1 1 52 52 VAL CA C 13 62.1 0.2 . 1 . . . . . . . . 4467 1 275 . 1 1 52 52 VAL CB C 13 32.43 0.2 . 1 . . . . . . . . 4467 1 276 . 1 1 53 53 TYR H H 1 9 0.02 . 1 . . . . . . . . 4467 1 277 . 1 1 53 53 TYR HA H 1 5.305 0.05 . 1 . . . . . . . . 4467 1 278 . 1 1 53 53 TYR C C 13 174.5 0.2 . 1 . . . . . . . . 4467 1 279 . 1 1 53 53 TYR CA C 13 55.7 0.2 . 1 . . . . . . . . 4467 1 280 . 1 1 53 53 TYR CB C 13 39.7 0.2 . 1 . . . . . . . . 4467 1 281 . 1 1 53 53 TYR N N 15 123.3 0.34 . 1 . . . . . . . . 4467 1 282 . 1 1 54 54 LEU H H 1 9.125 0.02 . 1 . . . . . . . . 4467 1 283 . 1 1 54 54 LEU HA H 1 5.45 0.05 . 1 . . . . . . . . 4467 1 284 . 1 1 54 54 LEU C C 13 175.9 0.2 . 1 . . . . . . . . 4467 1 285 . 1 1 54 54 LEU CA C 13 53.3 0.2 . 1 . . . . . . . . 4467 1 286 . 1 1 54 54 LEU CB C 13 42.7 0.2 . 1 . . . . . . . . 4467 1 287 . 1 1 54 54 LEU N N 15 121.4 0.34 . 1 . . . . . . . . 4467 1 288 . 1 1 55 55 ILE H H 1 9.586 0.02 . 1 . . . . . . . . 4467 1 289 . 1 1 55 55 ILE HA H 1 5.054 0.05 . 1 . . . . . . . . 4467 1 290 . 1 1 55 55 ILE C C 13 176.1 0.2 . 1 . . . . . . . . 4467 1 291 . 1 1 55 55 ILE CA C 13 59.15 0.2 . 1 . . . . . . . . 4467 1 292 . 1 1 55 55 ILE CB C 13 37.83 0.2 . 1 . . . . . . . . 4467 1 293 . 1 1 55 55 ILE N N 15 123.3 0.34 . 1 . . . . . . . . 4467 1 294 . 1 1 56 56 ASN H H 1 8.477 0.02 . 1 . . . . . . . . 4467 1 295 . 1 1 56 56 ASN HA H 1 5.052 0.05 . 1 . . . . . . . . 4467 1 296 . 1 1 56 56 ASN CA C 13 50.8 0.2 . 1 . . . . . . . . 4467 1 297 . 1 1 56 56 ASN N N 15 125.88 0.34 . 1 . . . . . . . . 4467 1 298 . 1 1 57 57 PRO HA H 1 5.07 0.05 . 1 . . . . . . . . 4467 1 299 . 1 1 57 57 PRO C C 13 177.1 0.2 . 1 . . . . . . . . 4467 1 300 . 1 1 57 57 PRO CA C 13 64.74 0.2 . 1 . . . . . . . . 4467 1 301 . 1 1 57 57 PRO CB C 13 30.8 0.2 . 1 . . . . . . . . 4467 1 302 . 1 1 58 58 GLN H H 1 6.95 0.02 . 1 . . . . . . . . 4467 1 303 . 1 1 58 58 GLN HA H 1 4.294 0.05 . 1 . . . . . . . . 4467 1 304 . 1 1 58 58 GLN C C 13 176.2 0.2 . 1 . . . . . . . . 4467 1 305 . 1 1 58 58 GLN CA C 13 55.81 0.2 . 1 . . . . . . . . 4467 1 306 . 1 1 58 58 GLN CB C 13 27.77 0.2 . 1 . . . . . . . . 4467 1 307 . 1 1 58 58 GLN N N 15 112.39 0.34 . 1 . . . . . . . . 4467 1 308 . 1 1 59 59 GLY H H 1 8.168 0.02 . 1 . . . . . . . . 4467 1 309 . 1 1 59 59 GLY HA2 H 1 4.093 0.05 . 2 . . . . . . . . 4467 1 310 . 1 1 59 59 GLY HA3 H 1 4.268 0.05 . 2 . . . . . . . . 4467 1 311 . 1 1 59 59 GLY C C 13 172.9 0.2 . 1 . . . . . . . . 4467 1 312 . 1 1 59 59 GLY CA C 13 45.2 0.2 . 1 . . . . . . . . 4467 1 313 . 1 1 59 59 GLY N N 15 107.89 0.34 . 1 . . . . . . . . 4467 1 314 . 1 1 60 60 LYS H H 1 7.76 0.02 . 1 . . . . . . . . 4467 1 315 . 1 1 60 60 LYS HA H 1 3.98 0.05 . 1 . . . . . . . . 4467 1 316 . 1 1 60 60 LYS C C 13 173.2 0.2 . 1 . . . . . . . . 4467 1 317 . 1 1 60 60 LYS CA C 13 55.3 0.2 . 1 . . . . . . . . 4467 1 318 . 1 1 60 60 LYS CB C 13 31.59 0.2 . 1 . . . . . . . . 4467 1 319 . 1 1 60 60 LYS N N 15 122.66 0.34 . 1 . . . . . . . . 4467 1 320 . 1 1 61 61 ALA H H 1 7.92 0.02 . 1 . . . . . . . . 4467 1 321 . 1 1 61 61 ALA HA H 1 5.103 0.05 . 1 . . . . . . . . 4467 1 322 . 1 1 61 61 ALA C C 13 177 0.2 . 1 . . . . . . . . 4467 1 323 . 1 1 61 61 ALA CA C 13 50.2 0.2 . 1 . . . . . . . . 4467 1 324 . 1 1 61 61 ALA CB C 13 21.7 0.2 . 1 . . . . . . . . 4467 1 325 . 1 1 61 61 ALA N N 15 124.59 0.34 . 1 . . . . . . . . 4467 1 326 . 1 1 62 62 PHE H H 1 9.66 0.02 . 1 . . . . . . . . 4467 1 327 . 1 1 62 62 PHE HA H 1 4.922 0.05 . 1 . . . . . . . . 4467 1 328 . 1 1 62 62 PHE C C 13 175.8 0.2 . 1 . . . . . . . . 4467 1 329 . 1 1 62 62 PHE CA C 13 57 0.2 . 1 . . . . . . . . 4467 1 330 . 1 1 62 62 PHE CB C 13 42.3 0.2 . 1 . . . . . . . . 4467 1 331 . 1 1 62 62 PHE N N 15 119.5 0.34 . 1 . . . . . . . . 4467 1 332 . 1 1 63 63 ARG H H 1 9.41 0.02 . 1 . . . . . . . . 4467 1 333 . 1 1 63 63 ARG HA H 1 4.892 0.05 . 1 . . . . . . . . 4467 1 334 . 1 1 63 63 ARG C C 13 175.3 0.2 . 1 . . . . . . . . 4467 1 335 . 1 1 63 63 ARG CA C 13 55.09 0.2 . 1 . . . . . . . . 4467 1 336 . 1 1 63 63 ARG CB C 13 31.4 0.2 . 1 . . . . . . . . 4467 1 337 . 1 1 63 63 ARG N N 15 119.5 0.34 . 1 . . . . . . . . 4467 1 338 . 1 1 64 64 SER H H 1 7.302 0.02 . 1 . . . . . . . . 4467 1 339 . 1 1 64 64 SER HA H 1 4.884 0.05 . 1 . . . . . . . . 4467 1 340 . 1 1 64 64 SER C C 13 174.6 0.2 . 1 . . . . . . . . 4467 1 341 . 1 1 64 64 SER CA C 13 55.716 0.2 . 1 . . . . . . . . 4467 1 342 . 1 1 64 64 SER N N 15 111.1 0.34 . 1 . . . . . . . . 4467 1 343 . 1 1 65 65 LYS H H 1 8.515 0.02 . 1 . . . . . . . . 4467 1 344 . 1 1 65 65 LYS HA H 1 3.59 0.05 . 1 . . . . . . . . 4467 1 345 . 1 1 65 65 LYS C C 13 177.7 0.2 . 1 . . . . . . . . 4467 1 346 . 1 1 65 65 LYS CA C 13 59.18 0.2 . 1 . . . . . . . . 4467 1 347 . 1 1 65 65 LYS CB C 13 31.13 0.2 . 1 . . . . . . . . 4467 1 348 . 1 1 65 65 LYS N N 15 122 0.34 . 1 . . . . . . . . 4467 1 349 . 1 1 66 66 VAL H H 1 7.666 0.02 . 1 . . . . . . . . 4467 1 350 . 1 1 66 66 VAL HA H 1 3.67 0.05 . 1 . . . . . . . . 4467 1 351 . 1 1 66 66 VAL C C 13 178.7 0.2 . 1 . . . . . . . . 4467 1 352 . 1 1 66 66 VAL CA C 13 66 0.2 . 1 . . . . . . . . 4467 1 353 . 1 1 66 66 VAL CB C 13 31.1 0.2 . 1 . . . . . . . . 4467 1 354 . 1 1 66 66 VAL N N 15 116.24 0.34 . 1 . . . . . . . . 4467 1 355 . 1 1 67 67 GLU H H 1 7.424 0.02 . 1 . . . . . . . . 4467 1 356 . 1 1 67 67 GLU HA H 1 4.178 0.05 . 1 . . . . . . . . 4467 1 357 . 1 1 67 67 GLU C C 13 179.7 0.2 . 1 . . . . . . . . 4467 1 358 . 1 1 67 67 GLU CA C 13 58.87 0.2 . 1 . . . . . . . . 4467 1 359 . 1 1 67 67 GLU CB C 13 30 0.2 . 1 . . . . . . . . 4467 1 360 . 1 1 67 67 GLU N N 15 119.5 0.34 . 1 . . . . . . . . 4467 1 361 . 1 1 68 68 LEU H H 1 7.55 0.02 . 1 . . . . . . . . 4467 1 362 . 1 1 68 68 LEU HA H 1 3.423 0.05 . 1 . . . . . . . . 4467 1 363 . 1 1 68 68 LEU C C 13 177.1 0.2 . 1 . . . . . . . . 4467 1 364 . 1 1 68 68 LEU CA C 13 57.56 0.2 . 1 . . . . . . . . 4467 1 365 . 1 1 68 68 LEU CB C 13 41.99 0.2 . 1 . . . . . . . . 4467 1 366 . 1 1 68 68 LEU N N 15 120.7 0.34 . 1 . . . . . . . . 4467 1 367 . 1 1 69 69 ILE H H 1 8.428 0.02 . 1 . . . . . . . . 4467 1 368 . 1 1 69 69 ILE HA H 1 4.291 0.05 . 1 . . . . . . . . 4467 1 369 . 1 1 69 69 ILE C C 13 178.3 0.2 . 1 . . . . . . . . 4467 1 370 . 1 1 69 69 ILE CA C 13 65.56 0.2 . 1 . . . . . . . . 4467 1 371 . 1 1 69 69 ILE CB C 13 37.79 0.2 . 1 . . . . . . . . 4467 1 372 . 1 1 69 69 ILE N N 15 117.5 0.34 . 1 . . . . . . . . 4467 1 373 . 1 1 70 70 ALA H H 1 7.59 0.02 . 1 . . . . . . . . 4467 1 374 . 1 1 70 70 ALA HA H 1 4.202 0.05 . 1 . . . . . . . . 4467 1 375 . 1 1 70 70 ALA C C 13 180.4 0.2 . 1 . . . . . . . . 4467 1 376 . 1 1 70 70 ALA CA C 13 54.68 0.2 . 1 . . . . . . . . 4467 1 377 . 1 1 70 70 ALA CB C 13 17 0.2 . 1 . . . . . . . . 4467 1 378 . 1 1 70 70 ALA N N 15 119.5 0.34 . 1 . . . . . . . . 4467 1 379 . 1 1 71 71 TYR H H 1 7.79 0.02 . 1 . . . . . . . . 4467 1 380 . 1 1 71 71 TYR HA H 1 4.43 0.05 . 1 . . . . . . . . 4467 1 381 . 1 1 71 71 TYR C C 13 176.9 0.2 . 1 . . . . . . . . 4467 1 382 . 1 1 71 71 TYR CA C 13 61.16 0.2 . 1 . . . . . . . . 4467 1 383 . 1 1 71 71 TYR CB C 13 38.54 0.2 . 1 . . . . . . . . 4467 1 384 . 1 1 71 71 TYR N N 15 119.5 0.34 . 1 . . . . . . . . 4467 1 385 . 1 1 72 72 PHE H H 1 8.786 0.02 . 1 . . . . . . . . 4467 1 386 . 1 1 72 72 PHE HA H 1 4.457 0.05 . 1 . . . . . . . . 4467 1 387 . 1 1 72 72 PHE C C 13 179.4 0.2 . 1 . . . . . . . . 4467 1 388 . 1 1 72 72 PHE CA C 13 58.069 0.2 . 1 . . . . . . . . 4467 1 389 . 1 1 72 72 PHE N N 15 118.2 0.34 . 1 . . . . . . . . 4467 1 390 . 1 1 73 73 GLU H H 1 8.374 0.02 . 1 . . . . . . . . 4467 1 391 . 1 1 73 73 GLU HA H 1 4.128 0.05 . 1 . . . . . . . . 4467 1 392 . 1 1 73 73 GLU C C 13 178.8 0.2 . 1 . . . . . . . . 4467 1 393 . 1 1 73 73 GLU CA C 13 58.7 0.2 . 1 . . . . . . . . 4467 1 394 . 1 1 73 73 GLU CB C 13 28.8 0.2 . 1 . . . . . . . . 4467 1 395 . 1 1 73 73 GLU N N 15 117.53 0.34 . 1 . . . . . . . . 4467 1 396 . 1 1 74 74 LYS H H 1 7.885 0.02 . 1 . . . . . . . . 4467 1 397 . 1 1 74 74 LYS HA H 1 4.116 0.05 . 1 . . . . . . . . 4467 1 398 . 1 1 74 74 LYS C C 13 179 0.2 . 1 . . . . . . . . 4467 1 399 . 1 1 74 74 LYS CA C 13 58.7 0.2 . 1 . . . . . . . . 4467 1 400 . 1 1 74 74 LYS CB C 13 31.7 0.2 . 1 . . . . . . . . 4467 1 401 . 1 1 74 74 LYS N N 15 120 0.34 . 1 . . . . . . . . 4467 1 402 . 1 1 75 75 VAL H H 1 8.02 0.02 . 1 . . . . . . . . 4467 1 403 . 1 1 75 75 VAL HA H 1 4.259 0.05 . 1 . . . . . . . . 4467 1 404 . 1 1 75 75 VAL C C 13 177 0.2 . 1 . . . . . . . . 4467 1 405 . 1 1 75 75 VAL CA C 13 61.67 0.2 . 1 . . . . . . . . 4467 1 406 . 1 1 75 75 VAL CB C 13 31 0.2 . 1 . . . . . . . . 4467 1 407 . 1 1 75 75 VAL N N 15 110.5 0.34 . 1 . . . . . . . . 4467 1 408 . 1 1 76 76 GLY H H 1 7.8 0.02 . 1 . . . . . . . . 4467 1 409 . 1 1 76 76 GLY HA2 H 1 4.2 0.05 . 2 . . . . . . . . 4467 1 410 . 1 1 76 76 GLY HA3 H 1 3.9 0.05 . 2 . . . . . . . . 4467 1 411 . 1 1 76 76 GLY C C 13 174.1 0.2 . 1 . . . . . . . . 4467 1 412 . 1 1 76 76 GLY CA C 13 46.46 0.2 . 1 . . . . . . . . 4467 1 413 . 1 1 76 76 GLY N N 15 111.1 0.34 . 1 . . . . . . . . 4467 1 414 . 1 1 77 77 ASP H H 1 8.08 0.02 . 1 . . . . . . . . 4467 1 415 . 1 1 77 77 ASP HA H 1 4.785 0.05 . 1 . . . . . . . . 4467 1 416 . 1 1 77 77 ASP C C 13 176.6 0.2 . 1 . . . . . . . . 4467 1 417 . 1 1 77 77 ASP CA C 13 53.495 0.2 . 1 . . . . . . . . 4467 1 418 . 1 1 77 77 ASP CB C 13 41 0.2 . 1 . . . . . . . . 4467 1 419 . 1 1 77 77 ASP N N 15 119.45 0.34 . 1 . . . . . . . . 4467 1 420 . 1 1 78 78 THR H H 1 8.425 0.02 . 1 . . . . . . . . 4467 1 421 . 1 1 78 78 THR HA H 1 4.5 0.05 . 1 . . . . . . . . 4467 1 422 . 1 1 78 78 THR C C 13 175.1 0.2 . 1 . . . . . . . . 4467 1 423 . 1 1 78 78 THR CA C 13 60.66 0.2 . 1 . . . . . . . . 4467 1 424 . 1 1 78 78 THR CB C 13 68.6 0.2 . 1 . . . . . . . . 4467 1 425 . 1 1 78 78 THR N N 15 115.5 0.34 . 1 . . . . . . . . 4467 1 426 . 1 1 79 79 SER H H 1 8.674 0.02 . 1 . . . . . . . . 4467 1 427 . 1 1 79 79 SER HA H 1 4.28 0.05 . 1 . . . . . . . . 4467 1 428 . 1 1 79 79 SER C C 13 174.2 0.2 . 1 . . . . . . . . 4467 1 429 . 1 1 79 79 SER CA C 13 60.05 0.2 . 1 . . . . . . . . 4467 1 430 . 1 1 79 79 SER CB C 13 63.94 0.2 . 1 . . . . . . . . 4467 1 431 . 1 1 79 79 SER N N 15 118.167 0.34 . 1 . . . . . . . . 4467 1 432 . 1 1 80 80 LEU H H 1 7.66 0.02 . 1 . . . . . . . . 4467 1 433 . 1 1 80 80 LEU HA H 1 4.399 0.05 . 1 . . . . . . . . 4467 1 434 . 1 1 80 80 LEU C C 13 174.6 0.2 . 1 . . . . . . . . 4467 1 435 . 1 1 80 80 LEU CA C 13 53.4 0.2 . 1 . . . . . . . . 4467 1 436 . 1 1 80 80 LEU CB C 13 43.4 0.2 . 1 . . . . . . . . 4467 1 437 . 1 1 80 80 LEU N N 15 122.66 0.34 . 1 . . . . . . . . 4467 1 438 . 1 1 81 81 ASP H H 1 8.84 0.02 . 1 . . . . . . . . 4467 1 439 . 1 1 81 81 ASP HA H 1 4.99 0.05 . 1 . . . . . . . . 4467 1 440 . 1 1 81 81 ASP CA C 13 50.2 0.2 . 1 . . . . . . . . 4467 1 441 . 1 1 81 81 ASP N N 15 122.66 0.34 . 1 . . . . . . . . 4467 1 442 . 1 1 82 82 PRO C C 13 177.5 0.2 . 1 . . . . . . . . 4467 1 443 . 1 1 82 82 PRO CA C 13 64.63 0.2 . 1 . . . . . . . . 4467 1 444 . 1 1 82 82 PRO CB C 13 31.9 0.2 . 1 . . . . . . . . 4467 1 445 . 1 1 83 83 ASN H H 1 8.879 0.02 . 1 . . . . . . . . 4467 1 446 . 1 1 83 83 ASN HA H 1 4.549 0.05 . 1 . . . . . . . . 4467 1 447 . 1 1 83 83 ASN C C 13 176.25 0.2 . 1 . . . . . . . . 4467 1 448 . 1 1 83 83 ASN CA C 13 54.99 0.2 . 1 . . . . . . . . 4467 1 449 . 1 1 83 83 ASN CB C 13 37.67 0.2 . 1 . . . . . . . . 4467 1 450 . 1 1 83 83 ASN N N 15 114.3 0.34 . 1 . . . . . . . . 4467 1 451 . 1 1 84 84 ASP H H 1 8.381 0.02 . 1 . . . . . . . . 4467 1 452 . 1 1 84 84 ASP HA H 1 4.55 0.05 . 1 . . . . . . . . 4467 1 453 . 1 1 84 84 ASP C C 13 174.9 0.2 . 1 . . . . . . . . 4467 1 454 . 1 1 84 84 ASP CA C 13 54.84 0.2 . 1 . . . . . . . . 4467 1 455 . 1 1 84 84 ASP CB C 13 39.7 0.2 . 1 . . . . . . . . 4467 1 456 . 1 1 84 84 ASP N N 15 118.8 0.34 . 1 . . . . . . . . 4467 1 457 . 1 1 85 85 PHE H H 1 7.15 0.02 . 1 . . . . . . . . 4467 1 458 . 1 1 85 85 PHE HA H 1 3.994 0.05 . 1 . . . . . . . . 4467 1 459 . 1 1 85 85 PHE C C 13 173.6 0.2 . 1 . . . . . . . . 4467 1 460 . 1 1 85 85 PHE CA C 13 57.375 0.2 . 1 . . . . . . . . 4467 1 461 . 1 1 85 85 PHE CB C 13 38.57 0.2 . 1 . . . . . . . . 4467 1 462 . 1 1 85 85 PHE N N 15 118.8 0.34 . 1 . . . . . . . . 4467 1 463 . 1 1 86 86 ASP H H 1 8.91 0.02 . 1 . . . . . . . . 4467 1 464 . 1 1 86 86 ASP HA H 1 4.565 0.05 . 1 . . . . . . . . 4467 1 465 . 1 1 86 86 ASP C C 13 176 0.2 . 1 . . . . . . . . 4467 1 466 . 1 1 86 86 ASP CA C 13 53.25 0.2 . 1 . . . . . . . . 4467 1 467 . 1 1 86 86 ASP CB C 13 40.65 0.2 . 1 . . . . . . . . 4467 1 468 . 1 1 86 86 ASP N N 15 124 0.34 . 1 . . . . . . . . 4467 1 469 . 1 1 87 87 PHE H H 1 9.14 0.02 . 1 . . . . . . . . 4467 1 470 . 1 1 87 87 PHE HA H 1 4.389 0.05 . 1 . . . . . . . . 4467 1 471 . 1 1 87 87 PHE C C 13 175.5 0.2 . 1 . . . . . . . . 4467 1 472 . 1 1 87 87 PHE CA C 13 58.66 0.2 . 1 . . . . . . . . 4467 1 473 . 1 1 87 87 PHE CB C 13 39.04 0.2 . 1 . . . . . . . . 4467 1 474 . 1 1 87 87 PHE N N 15 124.59 0.34 . 1 . . . . . . . . 4467 1 475 . 1 1 88 88 THR H H 1 9.09 0.02 . 1 . . . . . . . . 4467 1 476 . 1 1 88 88 THR HA H 1 4.498 0.05 . 1 . . . . . . . . 4467 1 477 . 1 1 88 88 THR C C 13 176.6 0.2 . 1 . . . . . . . . 4467 1 478 . 1 1 88 88 THR CA C 13 61.93 0.2 . 1 . . . . . . . . 4467 1 479 . 1 1 88 88 THR CB C 13 70.3 0.2 . 1 . . . . . . . . 4467 1 480 . 1 1 88 88 THR N N 15 113 0.34 . 1 . . . . . . . . 4467 1 481 . 1 1 89 89 VAL H H 1 8.98 0.02 . 1 . . . . . . . . 4467 1 482 . 1 1 89 89 VAL HA H 1 4.741 0.05 . 1 . . . . . . . . 4467 1 483 . 1 1 89 89 VAL C C 13 177.05 0.2 . 1 . . . . . . . . 4467 1 484 . 1 1 89 89 VAL CA C 13 66.69 0.2 . 1 . . . . . . . . 4467 1 485 . 1 1 89 89 VAL N N 15 123.3 0.34 . 1 . . . . . . . . 4467 1 486 . 1 1 90 90 THR H H 1 7.89 0.02 . 1 . . . . . . . . 4467 1 487 . 1 1 90 90 THR HA H 1 4.26 0.05 . 1 . . . . . . . . 4467 1 488 . 1 1 90 90 THR C C 13 175 0.2 . 1 . . . . . . . . 4467 1 489 . 1 1 90 90 THR CA C 13 61.75 0.2 . 1 . . . . . . . . 4467 1 490 . 1 1 90 90 THR CB C 13 69.56 0.2 . 1 . . . . . . . . 4467 1 491 . 1 1 90 90 THR N N 15 105.37 0.34 . 1 . . . . . . . . 4467 1 492 . 1 1 91 91 GLY H H 1 7.5 0.02 . 1 . . . . . . . . 4467 1 493 . 1 1 91 91 GLY HA2 H 1 4.323 0.05 . 2 . . . . . . . . 4467 1 494 . 1 1 91 91 GLY HA3 H 1 3.941 0.05 . 2 . . . . . . . . 4467 1 495 . 1 1 91 91 GLY C C 13 177.34 0.2 . 1 . . . . . . . . 4467 1 496 . 1 1 91 91 GLY CA C 13 44.64 0.2 . 1 . . . . . . . . 4467 1 497 . 1 1 91 91 GLY N N 15 110.45 0.34 . 1 . . . . . . . . 4467 1 498 . 1 1 92 92 ARG H H 1 9.1 0.02 . 1 . . . . . . . . 4467 1 499 . 1 1 92 92 ARG C C 13 178.05 0.2 . 1 . . . . . . . . 4467 1 500 . 1 1 92 92 ARG CA C 13 56.28 0.2 . 1 . . . . . . . . 4467 1 501 . 1 1 92 92 ARG N N 15 122 0.34 . 1 . . . . . . . . 4467 1 502 . 1 1 93 93 GLY H H 1 8.518 0.02 . 1 . . . . . . . . 4467 1 503 . 1 1 93 93 GLY HA2 H 1 4.195 0.05 . 2 . . . . . . . . 4467 1 504 . 1 1 93 93 GLY HA3 H 1 3.911 0.05 . 2 . . . . . . . . 4467 1 505 . 1 1 93 93 GLY C C 13 173.77 0.2 . 1 . . . . . . . . 4467 1 506 . 1 1 93 93 GLY CA C 13 44.7 0.2 . 1 . . . . . . . . 4467 1 507 . 1 1 93 93 GLY N N 15 108.8 0.34 . 1 . . . . . . . . 4467 1 508 . 1 1 94 94 SER H H 1 8.196 0.02 . 1 . . . . . . . . 4467 1 509 . 1 1 94 94 SER HA H 1 4.682 0.05 . 1 . . . . . . . . 4467 1 510 . 1 1 94 94 SER CA C 13 56.16 0.2 . 1 . . . . . . . . 4467 1 511 . 1 1 94 94 SER N N 15 116.24 0.34 . 1 . . . . . . . . 4467 1 512 . 1 1 95 95 PRO C C 13 177.28 0.2 . 1 . . . . . . . . 4467 1 513 . 1 1 95 95 PRO CA C 13 63.44 0.2 . 1 . . . . . . . . 4467 1 514 . 1 1 95 95 PRO CB C 13 31.3 0.2 . 1 . . . . . . . . 4467 1 515 . 1 1 96 96 SER H H 1 8.337 0.02 . 1 . . . . . . . . 4467 1 516 . 1 1 96 96 SER HA H 1 4.411 0.05 . 1 . . . . . . . . 4467 1 517 . 1 1 96 96 SER C C 13 174.69 0.2 . 1 . . . . . . . . 4467 1 518 . 1 1 96 96 SER CA C 13 58.3 0.2 . 1 . . . . . . . . 4467 1 519 . 1 1 96 96 SER CB C 13 63.3 0.2 . 1 . . . . . . . . 4467 1 520 . 1 1 96 96 SER N N 15 114.3 0.34 . 1 . . . . . . . . 4467 1 521 . 1 1 97 97 ARG H H 1 8.459 0.02 . 1 . . . . . . . . 4467 1 522 . 1 1 97 97 ARG HA H 1 4.31 0.05 . 1 . . . . . . . . 4467 1 523 . 1 1 97 97 ARG C C 13 176.24 0.2 . 1 . . . . . . . . 4467 1 524 . 1 1 97 97 ARG CA C 13 55.9 0.2 . 1 . . . . . . . . 4467 1 525 . 1 1 97 97 ARG CB C 13 30.3 0.2 . 1 . . . . . . . . 4467 1 526 . 1 1 97 97 ARG N N 15 122 0.34 . 1 . . . . . . . . 4467 1 527 . 1 1 98 98 ARG H H 1 8.4 0.02 . 1 . . . . . . . . 4467 1 528 . 1 1 98 98 ARG HA H 1 4.327 0.05 . 1 . . . . . . . . 4467 1 529 . 1 1 98 98 ARG C C 13 176.22 0.2 . 1 . . . . . . . . 4467 1 530 . 1 1 98 98 ARG CA C 13 56 0.2 . 1 . . . . . . . . 4467 1 531 . 1 1 98 98 ARG CB C 13 32.42 0.2 . 1 . . . . . . . . 4467 1 532 . 1 1 98 98 ARG N N 15 121 0.34 . 1 . . . . . . . . 4467 1 533 . 1 1 99 99 GLU H H 1 8.401 0.02 . 1 . . . . . . . . 4467 1 534 . 1 1 99 99 GLU HA H 1 4.549 0.05 . 1 . . . . . . . . 4467 1 535 . 1 1 99 99 GLU C C 13 175.86 0.2 . 1 . . . . . . . . 4467 1 536 . 1 1 99 99 GLU CA C 13 56.08 0.2 . 1 . . . . . . . . 4467 1 537 . 1 1 99 99 GLU CB C 13 32.38 0.2 . 1 . . . . . . . . 4467 1 538 . 1 1 99 99 GLU N N 15 118.2 0.34 . 1 . . . . . . . . 4467 1 539 . 1 1 100 100 GLN H H 1 8.115 0.02 . 1 . . . . . . . . 4467 1 540 . 1 1 100 100 GLN HA H 1 4.616 0.05 . 1 . . . . . . . . 4467 1 541 . 1 1 100 100 GLN C C 13 175.63 0.2 . 1 . . . . . . . . 4467 1 542 . 1 1 100 100 GLN CA C 13 55.44 0.2 . 1 . . . . . . . . 4467 1 543 . 1 1 100 100 GLN CB C 13 28.82 0.2 . 1 . . . . . . . . 4467 1 544 . 1 1 100 100 GLN N N 15 116.2 0.34 . 1 . . . . . . . . 4467 1 545 . 1 1 101 101 ARG H H 1 8.416 0.02 . 1 . . . . . . . . 4467 1 546 . 1 1 101 101 ARG HA H 1 4.744 0.05 . 1 . . . . . . . . 4467 1 547 . 1 1 101 101 ARG CA C 13 53.57 0.2 . 1 . . . . . . . . 4467 1 548 . 1 1 101 101 ARG N N 15 122.6 0.34 . 1 . . . . . . . . 4467 1 549 . 1 1 103 103 PRO C C 13 176.88 0.2 . 1 . . . . . . . . 4467 1 550 . 1 1 103 103 PRO CA C 13 62.27 0.2 . 1 . . . . . . . . 4467 1 551 . 1 1 103 103 PRO CB C 13 31.51 0.2 . 1 . . . . . . . . 4467 1 552 . 1 1 104 104 LYS H H 1 8.39 0.02 . 1 . . . . . . . . 4467 1 553 . 1 1 104 104 LYS HA H 1 4.994 0.05 . 1 . . . . . . . . 4467 1 554 . 1 1 104 104 LYS C C 13 176.63 0.2 . 1 . . . . . . . . 4467 1 555 . 1 1 104 104 LYS CA C 13 56.02 0.2 . 1 . . . . . . . . 4467 1 556 . 1 1 104 104 LYS CB C 13 28.84 0.2 . 1 . . . . . . . . 4467 1 557 . 1 1 104 104 LYS N N 15 121 0.34 . 1 . . . . . . . . 4467 1 558 . 1 1 105 105 LYS H H 1 8.348 0.02 . 1 . . . . . . . . 4467 1 559 . 1 1 105 105 LYS HA H 1 4.221 0.05 . 1 . . . . . . . . 4467 1 560 . 1 1 105 105 LYS C C 13 176.09 0.2 . 1 . . . . . . . . 4467 1 561 . 1 1 105 105 LYS CA C 13 55.9 0.2 . 1 . . . . . . . . 4467 1 562 . 1 1 105 105 LYS CB C 13 32.813 0.2 . 1 . . . . . . . . 4467 1 563 . 1 1 105 105 LYS N N 15 122.6 0.34 . 1 . . . . . . . . 4467 1 564 . 1 1 106 106 ALA H H 1 8.379 0.02 . 1 . . . . . . . . 4467 1 565 . 1 1 106 106 ALA HA H 1 4.287 0.05 . 1 . . . . . . . . 4467 1 566 . 1 1 106 106 ALA CA C 13 52.007 0.2 . 1 . . . . . . . . 4467 1 567 . 1 1 106 106 ALA N N 15 125.875 0.34 . 1 . . . . . . . . 4467 1 568 . 1 1 107 107 LYS H H 1 8.394 0.02 . 1 . . . . . . . . 4467 1 569 . 1 1 107 107 LYS HA H 1 4.33 0.05 . 1 . . . . . . . . 4467 1 570 . 1 1 107 107 LYS CA C 13 55.77 0.2 . 1 . . . . . . . . 4467 1 571 . 1 1 107 107 LYS CB C 13 32.44 0.2 . 1 . . . . . . . . 4467 1 572 . 1 1 107 107 LYS N N 15 120.7 0.34 . 1 . . . . . . . . 4467 1 573 . 1 1 108 108 SER H H 1 8.524 0.02 . 1 . . . . . . . . 4467 1 574 . 1 1 108 108 SER HA H 1 4.756 0.05 . 1 . . . . . . . . 4467 1 575 . 1 1 108 108 SER CA C 13 56.18 0.2 . 1 . . . . . . . . 4467 1 576 . 1 1 108 108 SER N N 15 118.8 0.34 . 1 . . . . . . . . 4467 1 577 . 1 1 109 109 PRO C C 13 176.18 0.2 . 1 . . . . . . . . 4467 1 578 . 1 1 109 109 PRO CA C 13 62.36 0.2 . 1 . . . . . . . . 4467 1 579 . 1 1 109 109 PRO CB C 13 33.74 0.2 . 1 . . . . . . . . 4467 1 580 . 1 1 110 110 LYS H H 1 8.619 0.02 . 1 . . . . . . . . 4467 1 581 . 1 1 110 110 LYS HA H 1 4.734 0.05 . 1 . . . . . . . . 4467 1 582 . 1 1 110 110 LYS C C 13 176.48 0.2 . 1 . . . . . . . . 4467 1 583 . 1 1 110 110 LYS CA C 13 56.72 0.2 . 1 . . . . . . . . 4467 1 584 . 1 1 110 110 LYS CB C 13 29.84 0.2 . 1 . . . . . . . . 4467 1 585 . 1 1 110 110 LYS N N 15 121.4 0.34 . 1 . . . . . . . . 4467 1 586 . 1 1 111 111 SER H H 1 8.077 0.02 . 1 . . . . . . . . 4467 1 587 . 1 1 111 111 SER HA H 1 4.78 0.05 . 1 . . . . . . . . 4467 1 588 . 1 1 111 111 SER CA C 13 56.57 0.2 . 1 . . . . . . . . 4467 1 589 . 1 1 111 111 SER N N 15 120.7 0.34 . 1 . . . . . . . . 4467 1 590 . 1 1 112 112 PRO C C 13 177.12 0.2 . 1 . . . . . . . . 4467 1 591 . 1 1 112 112 PRO CA C 13 63.3 0.2 . 1 . . . . . . . . 4467 1 592 . 1 1 112 112 PRO CB C 13 31.4 0.2 . 1 . . . . . . . . 4467 1 593 . 1 1 113 113 GLY H H 1 8.487 0.02 . 1 . . . . . . . . 4467 1 594 . 1 1 113 113 GLY HA2 H 1 4.429 0.05 . 2 . . . . . . . . 4467 1 595 . 1 1 113 113 GLY HA3 H 1 3.938 0.05 . 2 . . . . . . . . 4467 1 596 . 1 1 113 113 GLY C C 13 174.2 0.2 . 1 . . . . . . . . 4467 1 597 . 1 1 113 113 GLY CA C 13 45.04 0.2 . 1 . . . . . . . . 4467 1 598 . 1 1 113 113 GLY N N 15 108.53 0.34 . 1 . . . . . . . . 4467 1 599 . 1 1 114 114 SER H H 1 8.269 0.02 . 1 . . . . . . . . 4467 1 600 . 1 1 114 114 SER HA H 1 4.788 0.05 . 1 . . . . . . . . 4467 1 601 . 1 1 114 114 SER C C 13 177.21 0.2 . 1 . . . . . . . . 4467 1 602 . 1 1 114 114 SER CA C 13 58.21 0.2 . 1 . . . . . . . . 4467 1 603 . 1 1 114 114 SER CB C 13 63.6 0.2 . 1 . . . . . . . . 4467 1 604 . 1 1 114 114 SER N N 15 115 0.34 . 1 . . . . . . . . 4467 1 605 . 1 1 115 115 GLY H H 1 8.554 0.02 . 1 . . . . . . . . 4467 1 606 . 1 1 115 115 GLY HA2 H 1 4.775 0.05 . 2 . . . . . . . . 4467 1 607 . 1 1 115 115 GLY HA3 H 1 3.989 0.05 . 2 . . . . . . . . 4467 1 608 . 1 1 115 115 GLY C C 13 174.23 0.2 . 1 . . . . . . . . 4467 1 609 . 1 1 115 115 GLY CA C 13 45.3 0.2 . 1 . . . . . . . . 4467 1 610 . 1 1 115 115 GLY N N 15 110.5 0.34 . 1 . . . . . . . . 4467 1 611 . 1 1 116 116 ARG H H 1 8.285 0.02 . 1 . . . . . . . . 4467 1 612 . 1 1 116 116 ARG HA H 1 4.76 0.05 . 1 . . . . . . . . 4467 1 613 . 1 1 116 116 ARG C C 13 177 0.2 . 1 . . . . . . . . 4467 1 614 . 1 1 116 116 ARG CA C 13 55.87 0.2 . 1 . . . . . . . . 4467 1 615 . 1 1 116 116 ARG N N 15 120 0.34 . 1 . . . . . . . . 4467 1 616 . 1 1 117 117 GLY H H 1 8.492 0.02 . 1 . . . . . . . . 4467 1 617 . 1 1 117 117 GLY HA2 H 1 4.31 0.05 . 2 . . . . . . . . 4467 1 618 . 1 1 117 117 GLY HA3 H 1 3.89 0.05 . 2 . . . . . . . . 4467 1 619 . 1 1 117 117 GLY C C 13 173.17 0.2 . 1 . . . . . . . . 4467 1 620 . 1 1 117 117 GLY CA C 13 44.88 0.2 . 1 . . . . . . . . 4467 1 621 . 1 1 117 117 GLY N N 15 109.5 0.34 . 1 . . . . . . . . 4467 1 622 . 1 1 118 118 ARG H H 1 7.912 0.02 . 1 . . . . . . . . 4467 1 623 . 1 1 118 118 ARG HA H 1 4.6 0.05 . 1 . . . . . . . . 4467 1 624 . 1 1 118 118 ARG C C 13 176.28 0.2 . 1 . . . . . . . . 4467 1 625 . 1 1 118 118 ARG CA C 13 55.61 0.2 . 1 . . . . . . . . 4467 1 626 . 1 1 118 118 ARG N N 15 115 0.34 . 1 . . . . . . . . 4467 1 627 . 1 1 119 119 GLY H H 1 8.269 0.02 . 1 . . . . . . . . 4467 1 628 . 1 1 119 119 GLY C C 13 173.22 0.2 . 1 . . . . . . . . 4467 1 629 . 1 1 119 119 GLY CA C 13 45.18 0.2 . 1 . . . . . . . . 4467 1 630 . 1 1 119 119 GLY N N 15 108.5 0.34 . 1 . . . . . . . . 4467 1 631 . 1 1 120 120 ARG H H 1 7.942 0.02 . 1 . . . . . . . . 4467 1 632 . 1 1 120 120 ARG CA C 13 53.41 0.2 . 1 . . . . . . . . 4467 1 633 . 1 1 120 120 ARG N N 15 119.45 0.34 . 1 . . . . . . . . 4467 1 634 . 1 1 121 121 PRO C C 13 177.02 0.2 . 1 . . . . . . . . 4467 1 635 . 1 1 121 121 PRO CA C 13 62.85 0.2 . 1 . . . . . . . . 4467 1 636 . 1 1 121 121 PRO CB C 13 31.16 0.2 . 1 . . . . . . . . 4467 1 637 . 1 1 122 122 LYS H H 1 8.55 0.02 . 1 . . . . . . . . 4467 1 638 . 1 1 122 122 LYS HA H 1 4.384 0.05 . 1 . . . . . . . . 4467 1 639 . 1 1 122 122 LYS C C 13 177.09 0.2 . 1 . . . . . . . . 4467 1 640 . 1 1 122 122 LYS CA C 13 56.48 0.2 . 1 . . . . . . . . 4467 1 641 . 1 1 122 122 LYS CB C 13 32.48 0.2 . 1 . . . . . . . . 4467 1 642 . 1 1 122 122 LYS N N 15 121.4 0.34 . 1 . . . . . . . . 4467 1 643 . 1 1 123 123 GLY H H 1 8.529 0.02 . 1 . . . . . . . . 4467 1 644 . 1 1 123 123 GLY HA2 H 1 4.256 0.05 . 2 . . . . . . . . 4467 1 645 . 1 1 123 123 GLY HA3 H 1 4.001 0.05 . 2 . . . . . . . . 4467 1 646 . 1 1 123 123 GLY C C 13 174.18 0.2 . 1 . . . . . . . . 4467 1 647 . 1 1 123 123 GLY CA C 13 45.1 0.2 . 1 . . . . . . . . 4467 1 648 . 1 1 123 123 GLY N N 15 110.5 0.34 . 1 . . . . . . . . 4467 1 649 . 1 1 124 124 SER H H 1 8.25 0.02 . 1 . . . . . . . . 4467 1 650 . 1 1 124 124 SER HA H 1 4.78 0.05 . 1 . . . . . . . . 4467 1 651 . 1 1 124 124 SER C C 13 174.02 0.2 . 1 . . . . . . . . 4467 1 652 . 1 1 124 124 SER CA C 13 58.06 0.2 . 1 . . . . . . . . 4467 1 653 . 1 1 124 124 SER CB C 13 64.23 0.2 . 1 . . . . . . . . 4467 1 654 . 1 1 124 124 SER N N 15 114.96 0.34 . 1 . . . . . . . . 4467 1 655 . 1 1 125 125 GLY H H 1 8.158 0.02 . 1 . . . . . . . . 4467 1 656 . 1 1 125 125 GLY HA2 H 1 3.757 0.05 . 1 . . . . . . . . 4467 1 657 . 1 1 125 125 GLY HA3 H 1 3.757 0.05 . 1 . . . . . . . . 4467 1 658 . 1 1 125 125 GLY CA C 13 46.07 0.2 . 1 . . . . . . . . 4467 1 659 . 1 1 125 125 GLY N N 15 116.24 0.34 . 1 . . . . . . . . 4467 1 stop_ save_