data_5743 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5743 _Entry.Title ; Backbone 1H, 13C and 15N Chemical Shift Assignments for the extracellular domain of b-dystroglycan (654-750) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2003-03-17 _Entry.Accession_date 2003-03-17 _Entry.Last_release_date 2003-12-18 _Entry.Original_release_date 2003-12-18 _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 Manuela Bozzi . . . 5743 2 Andrea Brancaccio . . . 5743 3 Maurizio Paci . . . 5743 4 Daniel Cicero . O. . 5743 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5743 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 142 5743 '15N chemical shifts' 76 5743 '1H chemical shifts' 124 5743 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 . . 2003-12-18 2003-03-17 original author . 5743 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5743 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 14622018 _Citation.Full_citation . _Citation.Title ; Structural Characterization by NMR of the Natively Unfolded Extracellular Domain of beta-Dystroglycan: Toward the Identification of the Binding Epitope for alpha-Dystroglycan ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 42 _Citation.Journal_issue 46 _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 13717 _Citation.Page_last 13724 _Citation.Year 2003 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Manuela Bozzi . . . 5743 1 2 Marzia Bianchi . . . 5743 1 3 Francesca Sciandra . . . 5743 1 4 Maurizio Paci . . . 5743 1 5 Bruno Giardina . . . 5743 1 6 Andrea Brancaccio . . . 5743 1 7 Daniel Cicero . O. . 5743 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5743 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11166570 _Citation.Full_citation ; Winder S.J. Trends Biochem Sci. 2001 Feb;26(2):118-24 ; _Citation.Title 'The complexities of dystroglycan.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Trends Biochem. Sci.' _Citation.Journal_name_full 'Trends in biochemical sciences' _Citation.Journal_volume 26 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0968-0004 _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 118 _Citation.Page_last 124 _Citation.Year 2001 _Citation.Details ; The notion of dystroglycan as a simple laminin-binding receptor is increasingly being challenged. New roles and new binding partners are continually emerging. Recent structural advances have provided exciting new insights into the precise molecular interactions between dystroglycan and other key components of the dystroglycan complex. Coupled with an increasing understanding of dystroglycan function at the molecular level, we are finally beginning to probe the complexities of dystroglycan, not only in disease, but in development, adhesion and signalling. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'S. J.' Winder S. J. . 5743 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5743 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11257514 _Citation.Full_citation ; Boffi A, Bozzi M, Sciandra F, Woellner C, Bigotti MG, Ilari A, Brancaccio A. Biochim Biophys Acta. 2001 Mar 9;1546(1):114-21 ; _Citation.Title 'Plasticity of secondary structure in the N-terminal region of beta-dystroglycan.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochim. Biophys. Acta' _Citation.Journal_name_full 'Biochimica et biophysica acta' _Citation.Journal_volume 1546 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-3002 _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 114 _Citation.Page_last 121 _Citation.Year 2001 _Citation.Details ; The secondary structure content of the N-terminal extracellular domain of beta-dystroglycan (a recombinant fragment extending from positions 654 to 750) has been quantitatively determined by means of CD and FTIR spectroscopies. The elements of secondary structure, namely an 8-10 residue long alpha-helix (10%) and two beta-strands (24%) have been assigned to specific amino acid sequences by means of a GOR constrained prediction method. The remaining 66% of the whole sequence is classified as turns or unordered. The temperature dependence of CD and FTIR spectra has been investigated in detail. A reversible, non-cooperative thermal transition is observed with both CD and FTIR spectroscopies up to 95 degrees C. The profile of the transition is typical of the unfolding of isolated peptides and corresponds to the progressive loss of the secondary structure elements of the protein with no evidence for collapsing phenomena, typical of globular proteins, upon heating. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 A. Boffi A. . . 5743 3 2 M. Bozzi M. . . 5743 3 3 F. Sciandra F. . . 5743 3 4 C. Woellner C. . . 5743 3 5 'M. G.' Bigotti M. G. . 5743 3 6 A. Ilari A. . . 5743 3 7 A. Brancaccio A. . . 5743 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5743 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11502221 _Citation.Full_citation ; Sciandra F, Schneider M, Giardina B, Baumgartner S, Petrucci TC, Brancaccio A. Eur J Biochem 2001 Aug;268(16):4590-7 ; _Citation.Title 'Identification of the beta-dystroglycan binding epitope within the C-terminal region of alpha-dystroglycan.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European journal of biochemistry / FEBS' _Citation.Journal_volume 268 _Citation.Journal_issue 16 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-2956 _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 4590 _Citation.Page_last 4597 _Citation.Year 2001 _Citation.Details ; Dystroglycan is a receptor for extracellular matrix proteins that plays a crucial role during embryogenesis in addition to adult tissue stabilization. A precursor product of a single gene is post-translationally cleaved to form two different subunits, alpha and beta. The extracellular alpha-dystroglycan is a membrane-associated, highly glycosylated protein that binds to various extracellular matrix molecules, whereas the transmembrane beta-dystroglycan binds, via its cytosolic domain, to dystrophin and many other proteins. alpha- and beta-Dystroglycan interact tightly but noncovalently. We have previously shown that the N-terminal region of beta-dystroglycan, beta-DG(654-750), binds to the C-terminal region of murine alpha-dystroglycan independently from glycosylation. Preparing a series of deleted recombinant fragments and using solid-phase binding assays, the C-terminal sequence of alpha-dystroglycan containing the binding epitope for beta-dystroglycan has been defined more precisely. We found that a region of 36 amino acids, from position 550-585, is required for binding the extracellular region, amino acids 654-750 of beta-dystroglycan. Recently, a dystroglycan-like gene was identified in Drosophila that showed a moderate degree of conservation with vertebrate dystroglycan (31% identity, 48% similarity). Surprisingly, the Drosophila sequence contains a region showing a higher degree of identity and conservation (45% and 66%) that coincides with the 550-585 sequence of vertebrate alpha-dystroglycan. We have expressed this Drosophila dystroglycan fragment and measured its binding to the extracellular region of vertebrate (murine) beta-dystroglycan (Kd = 6 +/- 1 microM). These data confirm the proper identification of the beta-dystroglycan binding epitope and stress the importance of this region during evolution. This finding might help the rational design of dystroglycan-specific binding drugs, that could have important biomedical applications. ; 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 F. Sciandra F. . . 5743 4 2 M. Schneider M. . . 5743 4 3 B. Giardina B. . . 5743 4 4 S. Baumgartner S. . . 5743 4 5 'T. C.' Petrucci T. C. . 5743 4 6 A. Brancaccio A. . . 5743 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 5743 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11423118 _Citation.Full_citation ; Bozzi M, Veglia G, Paci M, Sciandra F, Giardina B, Brancaccio A. FEBS Lett 2001 Jun 22;499(3):210-4 ; _Citation.Title 'A synthetic peptide corresponding to the 550-585 region of alpha-dystroglycan binds beta-dystroglycan as revealed by NMR spectroscopy.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'FEBS Lett.' _Citation.Journal_name_full 'FEBS letters' _Citation.Journal_volume 499 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-5793 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 210 _Citation.Page_last 214 _Citation.Year 2001 _Citation.Details ; We have probed the binding of a synthetic peptide corresponding to the region 550-585 of the alpha subunit of dystroglycan with a recombinant protein fragment corresponding to the N-terminal extracellular region of beta-dystroglycan (654-750), using NMR in solution. In a 30:1 molar ratio, the peptide binds to the recombinant protein fragment in the fast/intermediate exchange regime. By monitoring the peptide intra-residue HN-Halpha peak volumes of the 2D TOCSY NMR spectra, both in the absence and in the presence of the recombinant fragment, we determined the differential binding affinities of each amino acid. We found that the residues in the region 550-565 (SWVQFNSNSQLMYGLP) are more influenced by the presence of the protein, whereas the C-terminal portion is marginally involved. These NMR results have been confirmed by solid-phase binding assays. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M. Bozzi M. . . 5743 5 2 G. Veglia G. . . 5743 5 3 M. Paci M. . . 5743 5 4 F. Sciandra F. . . 5743 5 5 B. Giardina B. . . 5743 5 6 A. Brancaccio A. . . 5743 5 stop_ save_ save_ref_5 _Citation.Sf_category citations _Citation.Sf_framecode ref_5 _Citation.Entry_ID 5743 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11495245 _Citation.Full_citation ; Panchal SC, Bhavesh NS, Hosur RV J Biomol NMR 2001 Jun;20(2):135-47 ; _Citation.Title 'Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: application to unfolded proteins.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 20 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 135 _Citation.Page_last 147 _Citation.Year 2001 _Citation.Details ; Two triple resonance experiments, HNN and HN(C)N, are presented which correlate HN and 15N resonances sequentially along the polypeptide chain of a doubly (13C, 15N) labeled protein. These incorporate several improvements over the previously published sequences for a similar purpose and have several novel features. The spectral characteristics enable direct identification of certain triplets of residues, which provide many starting points for the sequential assignment procedure. The experiments are sensitive and their utility has been demonstrated with a 22 kDa protein under unfolding conditions where most of the standard triple resonance experiments such as HNCA, CBCANH etc. have limited success because of poor amide, Calpha and Cbeta chemical shift dispersions. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'S. C.' Panchal S. C. . 5743 6 2 'N. S.' Bhavesh N. S. . 5743 6 3 'R. V.' Hosur R. V. . 5743 6 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_b-DG(654-750) _Assembly.Sf_category assembly _Assembly.Sf_framecode system_b-DG(654-750) _Assembly.Entry_ID 5743 _Assembly.ID 1 _Assembly.Name 'extracellular domain of beta subunit of dystroglycan' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all free' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5743 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 'extracellular domain of beta subunit of dystroglycan, b-DG(654-750)' 1 $b-DG(654-750) . . . native . . . . . 5743 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID b-DG(654-750) abbreviation 5743 1 'extracellular domain of beta subunit of dystroglycan' system 5743 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_b-DG(654-750) _Entity.Sf_category entity _Entity.Sf_framecode b-DG(654-750) _Entity.Entry_ID 5743 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'extracellular domain of beta subunit of dystroglycan' _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 ; GSSIVVEWTNNTLPLEPCPK EQIIGLSRRIADENGKPRPA FSNALEPDFKALSIAVTGSG SCRHLQFIPVAPPSPGSSAA PATEVPDRDPEKSSEDDVY ; _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 99 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 10528.72 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no DBJ BAC29332 . "unnamed protein product [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.97e-57 . . . . 5743 1 2 no DBJ BAC30105 . "unnamed protein product [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 3 no DBJ BAC35576 . "unnamed protein product [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 4 no GB AAA99779 . "dystroglycan 1 [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 5 no GB AAC52853 . "dystroglycan, partial [Mus musculus]" . . . . . 97.98 274 100.00 100.00 1.28e-60 . . . . 5743 1 6 no GB AAH07150 . "Dag1 protein [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 7 no GB EDL21272 . "dystroglycan 1 [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 8 no GB EGW08936 . "Dystroglycan [Cricetulus griseus]" . . . . . 97.98 893 96.91 100.00 7.02e-56 . . . . 5743 1 9 no REF NP_001263410 . "dystroglycan precursor [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 10 no REF NP_001263411 . "dystroglycan precursor [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 11 no REF NP_001263414 . "dystroglycan precursor [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 12 no REF NP_001263415 . "dystroglycan precursor [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 13 no REF NP_001263421 . "dystroglycan precursor [Mus musculus]" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 14 no SP Q62165 . "RecName: Full=Dystroglycan; AltName: Full=Dystrophin-associated glycoprotein 1; Contains: RecName: Full=Alpha-dystroglycan; Sho" . . . . . 97.98 893 100.00 100.00 3.78e-57 . . . . 5743 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID b-DG(654-750) abbreviation 5743 1 'extracellular domain of beta subunit of dystroglycan' common 5743 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 -2 GLY . 5743 1 2 -1 SER . 5743 1 3 654 SER . 5743 1 4 655 ILE . 5743 1 5 656 VAL . 5743 1 6 657 VAL . 5743 1 7 658 GLU . 5743 1 8 659 TRP . 5743 1 9 660 THR . 5743 1 10 661 ASN . 5743 1 11 662 ASN . 5743 1 12 663 THR . 5743 1 13 664 LEU . 5743 1 14 665 PRO . 5743 1 15 666 LEU . 5743 1 16 667 GLU . 5743 1 17 668 PRO . 5743 1 18 669 CYS . 5743 1 19 670 PRO . 5743 1 20 671 LYS . 5743 1 21 672 GLU . 5743 1 22 673 GLN . 5743 1 23 674 ILE . 5743 1 24 675 ILE . 5743 1 25 676 GLY . 5743 1 26 677 LEU . 5743 1 27 678 SER . 5743 1 28 679 ARG . 5743 1 29 680 ARG . 5743 1 30 681 ILE . 5743 1 31 682 ALA . 5743 1 32 683 ASP . 5743 1 33 684 GLU . 5743 1 34 685 ASN . 5743 1 35 686 GLY . 5743 1 36 687 LYS . 5743 1 37 688 PRO . 5743 1 38 689 ARG . 5743 1 39 690 PRO . 5743 1 40 691 ALA . 5743 1 41 692 PHE . 5743 1 42 693 SER . 5743 1 43 694 ASN . 5743 1 44 695 ALA . 5743 1 45 696 LEU . 5743 1 46 697 GLU . 5743 1 47 698 PRO . 5743 1 48 699 ASP . 5743 1 49 700 PHE . 5743 1 50 701 LYS . 5743 1 51 702 ALA . 5743 1 52 703 LEU . 5743 1 53 704 SER . 5743 1 54 705 ILE . 5743 1 55 706 ALA . 5743 1 56 707 VAL . 5743 1 57 708 THR . 5743 1 58 709 GLY . 5743 1 59 710 SER . 5743 1 60 711 GLY . 5743 1 61 712 SER . 5743 1 62 713 CYS . 5743 1 63 714 ARG . 5743 1 64 715 HIS . 5743 1 65 716 LEU . 5743 1 66 717 GLN . 5743 1 67 718 PHE . 5743 1 68 719 ILE . 5743 1 69 720 PRO . 5743 1 70 721 VAL . 5743 1 71 722 ALA . 5743 1 72 723 PRO . 5743 1 73 724 PRO . 5743 1 74 725 SER . 5743 1 75 726 PRO . 5743 1 76 727 GLY . 5743 1 77 728 SER . 5743 1 78 729 SER . 5743 1 79 730 ALA . 5743 1 80 731 ALA . 5743 1 81 732 PRO . 5743 1 82 733 ALA . 5743 1 83 734 THR . 5743 1 84 735 GLU . 5743 1 85 736 VAL . 5743 1 86 737 PRO . 5743 1 87 738 ASP . 5743 1 88 739 ARG . 5743 1 89 740 ASP . 5743 1 90 741 PRO . 5743 1 91 742 GLU . 5743 1 92 743 LYS . 5743 1 93 744 SER . 5743 1 94 745 SER . 5743 1 95 746 GLU . 5743 1 96 747 ASP . 5743 1 97 748 ASP . 5743 1 98 749 VAL . 5743 1 99 750 TYR . 5743 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 . GLY 1 1 5743 1 . SER 2 2 5743 1 . SER 3 3 5743 1 . ILE 4 4 5743 1 . VAL 5 5 5743 1 . VAL 6 6 5743 1 . GLU 7 7 5743 1 . TRP 8 8 5743 1 . THR 9 9 5743 1 . ASN 10 10 5743 1 . ASN 11 11 5743 1 . THR 12 12 5743 1 . LEU 13 13 5743 1 . PRO 14 14 5743 1 . LEU 15 15 5743 1 . GLU 16 16 5743 1 . PRO 17 17 5743 1 . CYS 18 18 5743 1 . PRO 19 19 5743 1 . LYS 20 20 5743 1 . GLU 21 21 5743 1 . GLN 22 22 5743 1 . ILE 23 23 5743 1 . ILE 24 24 5743 1 . GLY 25 25 5743 1 . LEU 26 26 5743 1 . SER 27 27 5743 1 . ARG 28 28 5743 1 . ARG 29 29 5743 1 . ILE 30 30 5743 1 . ALA 31 31 5743 1 . ASP 32 32 5743 1 . GLU 33 33 5743 1 . ASN 34 34 5743 1 . GLY 35 35 5743 1 . LYS 36 36 5743 1 . PRO 37 37 5743 1 . ARG 38 38 5743 1 . PRO 39 39 5743 1 . ALA 40 40 5743 1 . PHE 41 41 5743 1 . SER 42 42 5743 1 . ASN 43 43 5743 1 . ALA 44 44 5743 1 . LEU 45 45 5743 1 . GLU 46 46 5743 1 . PRO 47 47 5743 1 . ASP 48 48 5743 1 . PHE 49 49 5743 1 . LYS 50 50 5743 1 . ALA 51 51 5743 1 . LEU 52 52 5743 1 . SER 53 53 5743 1 . ILE 54 54 5743 1 . ALA 55 55 5743 1 . VAL 56 56 5743 1 . THR 57 57 5743 1 . GLY 58 58 5743 1 . SER 59 59 5743 1 . GLY 60 60 5743 1 . SER 61 61 5743 1 . CYS 62 62 5743 1 . ARG 63 63 5743 1 . HIS 64 64 5743 1 . LEU 65 65 5743 1 . GLN 66 66 5743 1 . PHE 67 67 5743 1 . ILE 68 68 5743 1 . PRO 69 69 5743 1 . VAL 70 70 5743 1 . ALA 71 71 5743 1 . PRO 72 72 5743 1 . PRO 73 73 5743 1 . SER 74 74 5743 1 . PRO 75 75 5743 1 . GLY 76 76 5743 1 . SER 77 77 5743 1 . SER 78 78 5743 1 . ALA 79 79 5743 1 . ALA 80 80 5743 1 . PRO 81 81 5743 1 . ALA 82 82 5743 1 . THR 83 83 5743 1 . GLU 84 84 5743 1 . VAL 85 85 5743 1 . PRO 86 86 5743 1 . ASP 87 87 5743 1 . ARG 88 88 5743 1 . ASP 89 89 5743 1 . PRO 90 90 5743 1 . GLU 91 91 5743 1 . LYS 92 92 5743 1 . SER 93 93 5743 1 . SER 94 94 5743 1 . GLU 95 95 5743 1 . ASP 96 96 5743 1 . ASP 97 97 5743 1 . VAL 98 98 5743 1 . TYR 99 99 5743 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 5743 _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 $b-DG(654-750) . 10090 organism . 'Mus musculus' mouse . . Eukaryota Metazoa Mus musculus . . . . 'skeletal muscle' . . . . . . . . . . . . . . . . 5743 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 5743 _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 $b-DG(654-750) . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21(DE3) . . . . . . . . . . . . . . . . . . . . . . 5743 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5743 _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 'extracellular domain of beta subunit of dystroglycan' '[U-13C; U-15N]' . . 1 $b-DG(654-750) . . . 0.3 0.5 mM . . . . 5743 1 2 'sodium phosphate' . . . . . . . 20 . . mM . . . . 5743 1 3 'sodium chloride' . . . . . . . 0.15 . . M . . . . 5743 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex_conditions_1 _Sample_condition_list.Entry_ID 5743 _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 6.5 0.2 n/a 5743 1 temperature 298 0.01 K 5743 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 5743 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 400 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 5743 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5743 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 400 . . . 5743 1 2 spectrometer_2 Bruker Avance . 700 . . . 5743 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 5743 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '3D 15N-TOCSY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex_conditions_1 . . . . . . . . . . . . . . . . . . . . . 5743 1 2 '3D HNN' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex_conditions_1 . . . . . . . . . . . . . . . . . . . . . 5743 1 3 '3D HNCO' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex_conditions_1 . . . . . . . . . . . . . . . . . . . . . 5743 1 4 '3D HNCA' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex_conditions_1 . . . . . . . . . . . . . . . . . . . . . 5743 1 5 '3D HN(CO)CA' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex_conditions_1 . . . . . . . . . . . . . . . . . . . . . 5743 1 6 '3D CBCANH' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex_conditions_1 . . . . . . . . . . . . . . . . . . . . . 5743 1 7 '3D CBCA(CO)NH' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex_conditions_1 . . . . . . . . . . . . . . . . . . . . . 5743 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5743 _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 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5743 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 5743 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5743 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5743 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex_conditions_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 . 5743 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 4 4 ILE C C 13 176.20 0.05 . 1 . . . . . . . . 5743 1 2 . 1 1 4 4 ILE N N 15 122.10 0.05 . 1 . . . . . . . . 5743 1 3 . 1 1 5 5 VAL H H 1 8.22 0.03 . 1 . . . . . . . . 5743 1 4 . 1 1 5 5 VAL HA H 1 4.07 0.03 . 1 . . . . . . . . 5743 1 5 . 1 1 5 5 VAL C C 13 176.14 0.05 . 1 . . . . . . . . 5743 1 6 . 1 1 5 5 VAL CA C 13 62.27 0.05 . 1 . . . . . . . . 5743 1 7 . 1 1 5 5 VAL N N 15 125.12 0.05 . 1 . . . . . . . . 5743 1 8 . 1 1 6 6 VAL H H 1 8.24 0.03 . 1 . . . . . . . . 5743 1 9 . 1 1 6 6 VAL C C 13 176.01 0.05 . 1 . . . . . . . . 5743 1 10 . 1 1 6 6 VAL CA C 13 62.17 0.05 . 1 . . . . . . . . 5743 1 11 . 1 1 6 6 VAL N N 15 124.75 0.05 . 1 . . . . . . . . 5743 1 12 . 1 1 7 7 GLU H H 1 8.38 0.03 . 1 . . . . . . . . 5743 1 13 . 1 1 7 7 GLU HA H 1 4.30 0.03 . 1 . . . . . . . . 5743 1 14 . 1 1 7 7 GLU C C 13 176.29 0.05 . 1 . . . . . . . . 5743 1 15 . 1 1 7 7 GLU CA C 13 56.47 0.05 . 1 . . . . . . . . 5743 1 16 . 1 1 7 7 GLU N N 15 124.50 0.05 . 1 . . . . . . . . 5743 1 17 . 1 1 8 8 TRP H H 1 8.26 0.03 . 1 . . . . . . . . 5743 1 18 . 1 1 8 8 TRP HA H 1 4.72 0.03 . 1 . . . . . . . . 5743 1 19 . 1 1 8 8 TRP C C 13 176.54 0.05 . 1 . . . . . . . . 5743 1 20 . 1 1 8 8 TRP CA C 13 57.37 0.05 . 1 . . . . . . . . 5743 1 21 . 1 1 8 8 TRP N N 15 122.44 0.05 . 1 . . . . . . . . 5743 1 22 . 1 1 9 9 THR H H 1 7.91 0.03 . 1 . . . . . . . . 5743 1 23 . 1 1 9 9 THR HA H 1 4.23 0.03 . 1 . . . . . . . . 5743 1 24 . 1 1 9 9 THR C C 13 176.50 0.05 . 1 . . . . . . . . 5743 1 25 . 1 1 9 9 THR CA C 13 61.67 0.05 . 1 . . . . . . . . 5743 1 26 . 1 1 9 9 THR N N 15 115.16 0.05 . 1 . . . . . . . . 5743 1 27 . 1 1 10 10 ASN H H 1 8.24 0.03 . 1 . . . . . . . . 5743 1 28 . 1 1 10 10 ASN C C 13 175.17 0.05 . 1 . . . . . . . . 5743 1 29 . 1 1 10 10 ASN CA C 13 53.57 0.05 . 1 . . . . . . . . 5743 1 30 . 1 1 10 10 ASN N N 15 120.05 0.05 . 1 . . . . . . . . 5743 1 31 . 1 1 11 11 ASN H H 1 8.35 0.03 . 1 . . . . . . . . 5743 1 32 . 1 1 11 11 ASN C C 13 175.49 0.05 . 1 . . . . . . . . 5743 1 33 . 1 1 11 11 ASN CA C 13 53.57 0.05 . 1 . . . . . . . . 5743 1 34 . 1 1 11 11 ASN N N 15 118.86 0.05 . 1 . . . . . . . . 5743 1 35 . 1 1 12 12 THR H H 1 8.06 0.03 . 1 . . . . . . . . 5743 1 36 . 1 1 12 12 THR C C 13 174.51 0.05 . 1 . . . . . . . . 5743 1 37 . 1 1 12 12 THR CA C 13 62.17 0.05 . 1 . . . . . . . . 5743 1 38 . 1 1 12 12 THR N N 15 113.67 0.05 . 1 . . . . . . . . 5743 1 39 . 1 1 13 13 LEU H H 1 8.13 0.03 . 1 . . . . . . . . 5743 1 40 . 1 1 13 13 LEU HA H 1 4.58 0.03 . 1 . . . . . . . . 5743 1 41 . 1 1 13 13 LEU CA C 13 53.37 0.05 . 1 . . . . . . . . 5743 1 42 . 1 1 13 13 LEU N N 15 125.39 0.05 . 1 . . . . . . . . 5743 1 43 . 1 1 14 14 PRO C C 13 176.79 0.05 . 1 . . . . . . . . 5743 1 44 . 1 1 14 14 PRO CA C 13 62.97 0.05 . 1 . . . . . . . . 5743 1 45 . 1 1 15 15 LEU H H 1 8.21 0.03 . 1 . . . . . . . . 5743 1 46 . 1 1 15 15 LEU HA H 1 4.27 0.03 . 1 . . . . . . . . 5743 1 47 . 1 1 15 15 LEU C C 13 177.41 0.05 . 1 . . . . . . . . 5743 1 48 . 1 1 15 15 LEU CA C 13 54.67 0.05 . 1 . . . . . . . . 5743 1 49 . 1 1 15 15 LEU N N 15 121.75 0.05 . 1 . . . . . . . . 5743 1 50 . 1 1 16 16 GLU H H 1 8.32 0.03 . 1 . . . . . . . . 5743 1 51 . 1 1 16 16 GLU CA C 13 54.27 0.05 . 1 . . . . . . . . 5743 1 52 . 1 1 16 16 GLU N N 15 122.39 0.05 . 1 . . . . . . . . 5743 1 53 . 1 1 19 19 PRO C C 13 177.13 0.05 . 1 . . . . . . . . 5743 1 54 . 1 1 20 20 LYS H H 1 8.47 0.03 . 1 . . . . . . . . 5743 1 55 . 1 1 20 20 LYS C C 13 177.09 0.05 . 1 . . . . . . . . 5743 1 56 . 1 1 20 20 LYS CA C 13 56.87 0.05 . 1 . . . . . . . . 5743 1 57 . 1 1 20 20 LYS N N 15 121.37 0.05 . 1 . . . . . . . . 5743 1 58 . 1 1 21 21 GLU H H 1 8.47 0.03 . 1 . . . . . . . . 5743 1 59 . 1 1 21 21 GLU CA C 13 56.87 0.05 . 1 . . . . . . . . 5743 1 60 . 1 1 21 21 GLU N N 15 120.68 0.05 . 1 . . . . . . . . 5743 1 61 . 1 1 22 22 GLN C C 13 174.47 0.05 . 1 . . . . . . . . 5743 1 62 . 1 1 22 22 GLN N N 15 117.89 0.05 . 1 . . . . . . . . 5743 1 63 . 1 1 23 23 ILE H H 1 8.21 0.03 . 1 . . . . . . . . 5743 1 64 . 1 1 23 23 ILE C C 13 176.53 0.05 . 1 . . . . . . . . 5743 1 65 . 1 1 23 23 ILE CA C 13 61.27 0.05 . 1 . . . . . . . . 5743 1 66 . 1 1 23 23 ILE N N 15 122.18 0.05 . 1 . . . . . . . . 5743 1 67 . 1 1 24 24 ILE H H 1 8.27 0.03 . 1 . . . . . . . . 5743 1 68 . 1 1 24 24 ILE HA H 1 4.11 0.03 . 1 . . . . . . . . 5743 1 69 . 1 1 24 24 ILE C C 13 176.95 0.05 . 1 . . . . . . . . 5743 1 70 . 1 1 24 24 ILE CA C 13 61.47 0.05 . 1 . . . . . . . . 5743 1 71 . 1 1 24 24 ILE N N 15 125.10 0.05 . 1 . . . . . . . . 5743 1 72 . 1 1 25 25 GLY H H 1 8.40 0.03 . 1 . . . . . . . . 5743 1 73 . 1 1 25 25 GLY HA2 H 1 3.92 0.03 . 1 . . . . . . . . 5743 1 74 . 1 1 25 25 GLY HA3 H 1 3.92 0.03 . 1 . . . . . . . . 5743 1 75 . 1 1 25 25 GLY C C 13 174.51 0.05 . 1 . . . . . . . . 5743 1 76 . 1 1 25 25 GLY CA C 13 45.57 0.05 . 1 . . . . . . . . 5743 1 77 . 1 1 25 25 GLY N N 15 111.81 0.05 . 1 . . . . . . . . 5743 1 78 . 1 1 26 26 LEU H H 1 8.05 0.03 . 1 . . . . . . . . 5743 1 79 . 1 1 26 26 LEU C C 13 177.66 0.05 . 1 . . . . . . . . 5743 1 80 . 1 1 26 26 LEU CA C 13 55.27 0.05 . 1 . . . . . . . . 5743 1 81 . 1 1 26 26 LEU N N 15 121.33 0.05 . 1 . . . . . . . . 5743 1 82 . 1 1 27 27 SER H H 1 8.34 0.03 . 1 . . . . . . . . 5743 1 83 . 1 1 27 27 SER HA H 1 4.44 0.03 . 1 . . . . . . . . 5743 1 84 . 1 1 27 27 SER C C 13 173.76 0.05 . 1 . . . . . . . . 5743 1 85 . 1 1 27 27 SER CA C 13 58.37 0.05 . 1 . . . . . . . . 5743 1 86 . 1 1 27 27 SER N N 15 116.92 0.05 . 1 . . . . . . . . 5743 1 87 . 1 1 28 28 ARG H H 1 7.99 0.03 . 1 . . . . . . . . 5743 1 88 . 1 1 28 28 ARG HA H 1 4.16 0.03 . 1 . . . . . . . . 5743 1 89 . 1 1 28 28 ARG CA C 13 57.67 0.05 . 1 . . . . . . . . 5743 1 90 . 1 1 28 28 ARG N N 15 127.67 0.05 . 1 . . . . . . . . 5743 1 91 . 1 1 30 30 ILE H H 1 7.75 0.03 . 1 . . . . . . . . 5743 1 92 . 1 1 30 30 ILE C C 13 176.01 0.05 . 1 . . . . . . . . 5743 1 93 . 1 1 30 30 ILE CA C 13 61.60 0.05 . 1 . . . . . . . . 5743 1 94 . 1 1 30 30 ILE N N 15 127.03 0.05 . 1 . . . . . . . . 5743 1 95 . 1 1 31 31 ALA H H 1 8.47 0.03 . 1 . . . . . . . . 5743 1 96 . 1 1 31 31 ALA HA H 1 4.77 0.03 . 1 . . . . . . . . 5743 1 97 . 1 1 31 31 ALA C C 13 177.55 0.05 . 1 . . . . . . . . 5743 1 98 . 1 1 31 31 ALA CA C 13 52.74 0.05 . 1 . . . . . . . . 5743 1 99 . 1 1 31 31 ALA N N 15 127.49 0.05 . 1 . . . . . . . . 5743 1 100 . 1 1 32 32 ASP H H 1 8.26 0.03 . 1 . . . . . . . . 5743 1 101 . 1 1 32 32 ASP C C 13 176.91 0.05 . 1 . . . . . . . . 5743 1 102 . 1 1 32 32 ASP CA C 13 54.45 0.05 . 1 . . . . . . . . 5743 1 103 . 1 1 32 32 ASP N N 15 119.28 0.05 . 1 . . . . . . . . 5743 1 104 . 1 1 33 33 GLU H H 1 8.54 0.03 . 1 . . . . . . . . 5743 1 105 . 1 1 33 33 GLU HA H 1 4.20 0.03 . 1 . . . . . . . . 5743 1 106 . 1 1 33 33 GLU C C 13 176.95 0.05 . 1 . . . . . . . . 5743 1 107 . 1 1 33 33 GLU CA C 13 57.13 0.05 . 1 . . . . . . . . 5743 1 108 . 1 1 33 33 GLU N N 15 121.02 0.05 . 1 . . . . . . . . 5743 1 109 . 1 1 34 34 ASN H H 1 8.47 0.03 . 1 . . . . . . . . 5743 1 110 . 1 1 34 34 ASN C C 13 176.08 0.05 . 1 . . . . . . . . 5743 1 111 . 1 1 34 34 ASN CA C 13 53.80 0.05 . 1 . . . . . . . . 5743 1 112 . 1 1 34 34 ASN N N 15 118.47 0.05 . 1 . . . . . . . . 5743 1 113 . 1 1 35 35 GLY H H 1 8.34 0.03 . 1 . . . . . . . . 5743 1 114 . 1 1 35 35 GLY HA2 H 1 3.90 0.03 . 1 . . . . . . . . 5743 1 115 . 1 1 35 35 GLY HA3 H 1 3.90 0.03 . 1 . . . . . . . . 5743 1 116 . 1 1 35 35 GLY C C 13 174.14 0.05 . 1 . . . . . . . . 5743 1 117 . 1 1 35 35 GLY CA C 13 45.72 0.05 . 1 . . . . . . . . 5743 1 118 . 1 1 35 35 GLY N N 15 108.39 0.05 . 1 . . . . . . . . 5743 1 119 . 1 1 36 36 LYS H H 1 7.98 0.03 . 1 . . . . . . . . 5743 1 120 . 1 1 36 36 LYS CA C 13 54.25 0.05 . 1 . . . . . . . . 5743 1 121 . 1 1 36 36 LYS N N 15 121.56 0.05 . 1 . . . . . . . . 5743 1 122 . 1 1 37 37 PRO C C 13 177.04 0.05 . 1 . . . . . . . . 5743 1 123 . 1 1 37 37 PRO CA C 13 63.07 0.05 . 1 . . . . . . . . 5743 1 124 . 1 1 38 38 ARG H H 1 8.48 0.03 . 1 . . . . . . . . 5743 1 125 . 1 1 38 38 ARG HA H 1 4.58 0.03 . 1 . . . . . . . . 5743 1 126 . 1 1 38 38 ARG CA C 13 54.07 0.05 . 1 . . . . . . . . 5743 1 127 . 1 1 38 38 ARG N N 15 122.62 0.05 . 1 . . . . . . . . 5743 1 128 . 1 1 39 39 PRO C C 13 176.76 0.05 . 1 . . . . . . . . 5743 1 129 . 1 1 39 39 PRO CA C 13 63.07 0.05 . 1 . . . . . . . . 5743 1 130 . 1 1 40 40 ALA H H 1 8.36 0.03 . 1 . . . . . . . . 5743 1 131 . 1 1 40 40 ALA HA H 1 4.20 0.03 . 1 . . . . . . . . 5743 1 132 . 1 1 40 40 ALA C C 13 177.78 0.05 . 1 . . . . . . . . 5743 1 133 . 1 1 40 40 ALA CA C 13 52.67 0.05 . 1 . . . . . . . . 5743 1 134 . 1 1 40 40 ALA N N 15 123.60 0.05 . 1 . . . . . . . . 5743 1 135 . 1 1 41 41 PHE H H 1 8.08 0.03 . 1 . . . . . . . . 5743 1 136 . 1 1 41 41 PHE HA H 1 4.63 0.03 . 1 . . . . . . . . 5743 1 137 . 1 1 41 41 PHE C C 13 175.96 0.05 . 1 . . . . . . . . 5743 1 138 . 1 1 41 41 PHE CA C 13 57.67 0.05 . 1 . . . . . . . . 5743 1 139 . 1 1 41 41 PHE N N 15 117.74 0.05 . 1 . . . . . . . . 5743 1 140 . 1 1 42 42 SER H H 1 8.18 0.03 . 1 . . . . . . . . 5743 1 141 . 1 1 42 42 SER HA H 1 4.36 0.03 . 1 . . . . . . . . 5743 1 142 . 1 1 42 42 SER C C 13 176.89 0.05 . 1 . . . . . . . . 5743 1 143 . 1 1 42 42 SER CA C 13 58.17 0.05 . 1 . . . . . . . . 5743 1 144 . 1 1 42 42 SER N N 15 116.32 0.05 . 1 . . . . . . . . 5743 1 145 . 1 1 43 43 ASN H H 1 8.39 0.03 . 1 . . . . . . . . 5743 1 146 . 1 1 43 43 ASN C C 13 175.09 0.05 . 1 . . . . . . . . 5743 1 147 . 1 1 43 43 ASN CA C 13 53.37 0.05 . 1 . . . . . . . . 5743 1 148 . 1 1 43 43 ASN N N 15 120.54 0.05 . 1 . . . . . . . . 5743 1 149 . 1 1 44 44 ALA H H 1 8.19 0.03 . 1 . . . . . . . . 5743 1 150 . 1 1 44 44 ALA HA H 1 4.74 0.03 . 1 . . . . . . . . 5743 1 151 . 1 1 44 44 ALA C C 13 176.19 0.05 . 1 . . . . . . . . 5743 1 152 . 1 1 44 44 ALA CA C 13 53.57 0.05 . 1 . . . . . . . . 5743 1 153 . 1 1 44 44 ALA N N 15 123.48 0.05 . 1 . . . . . . . . 5743 1 154 . 1 1 45 45 LEU H H 1 8.12 0.03 . 1 . . . . . . . . 5743 1 155 . 1 1 45 45 LEU C C 13 177.42 0.05 . 1 . . . . . . . . 5743 1 156 . 1 1 45 45 LEU N N 15 120.40 0.05 . 1 . . . . . . . . 5743 1 157 . 1 1 46 46 GLU H H 1 8.19 0.03 . 1 . . . . . . . . 5743 1 158 . 1 1 46 46 GLU HA H 1 4.53 0.03 . 1 . . . . . . . . 5743 1 159 . 1 1 46 46 GLU CA C 13 54.57 0.05 . 1 . . . . . . . . 5743 1 160 . 1 1 46 46 GLU N N 15 122.29 0.05 . 1 . . . . . . . . 5743 1 161 . 1 1 47 47 PRO C C 13 176.76 0.05 . 1 . . . . . . . . 5743 1 162 . 1 1 47 47 PRO CA C 13 63.37 0.05 . 1 . . . . . . . . 5743 1 163 . 1 1 48 48 ASP H H 1 8.30 0.03 . 1 . . . . . . . . 5743 1 164 . 1 1 48 48 ASP HA H 1 4.53 0.03 . 1 . . . . . . . . 5743 1 165 . 1 1 48 48 ASP C C 13 176.60 0.05 . 1 . . . . . . . . 5743 1 166 . 1 1 48 48 ASP CA C 13 54.37 0.05 . 1 . . . . . . . . 5743 1 167 . 1 1 48 48 ASP N N 15 119.01 0.05 . 1 . . . . . . . . 5743 1 168 . 1 1 49 49 PHE H H 1 8.08 0.03 . 1 . . . . . . . . 5743 1 169 . 1 1 49 49 PHE CA C 13 57.87 0.05 . 1 . . . . . . . . 5743 1 170 . 1 1 49 49 PHE N N 15 120.62 0.05 . 1 . . . . . . . . 5743 1 171 . 1 1 50 50 LYS N N 15 127.48 0.05 . 1 . . . . . . . . 5743 1 172 . 1 1 53 53 SER N N 15 117.35 0.05 . 1 . . . . . . . . 5743 1 173 . 1 1 54 54 ILE H H 1 8.18 0.03 . 1 . . . . . . . . 5743 1 174 . 1 1 54 54 ILE N N 15 122.12 0.05 . 1 . . . . . . . . 5743 1 175 . 1 1 55 55 ALA H H 1 8.34 0.03 . 1 . . . . . . . . 5743 1 176 . 1 1 55 55 ALA C C 13 177.95 0.05 . 1 . . . . . . . . 5743 1 177 . 1 1 55 55 ALA N N 15 127.41 0.05 . 1 . . . . . . . . 5743 1 178 . 1 1 56 56 VAL H H 1 8.12 0.03 . 1 . . . . . . . . 5743 1 179 . 1 1 56 56 VAL HA H 1 4.17 0.03 . 1 . . . . . . . . 5743 1 180 . 1 1 56 56 VAL C C 13 176.80 0.05 . 1 . . . . . . . . 5743 1 181 . 1 1 56 56 VAL CA C 13 62.37 0.05 . 1 . . . . . . . . 5743 1 182 . 1 1 56 56 VAL N N 15 118.47 0.05 . 1 . . . . . . . . 5743 1 183 . 1 1 57 57 THR H H 1 8.19 0.03 . 1 . . . . . . . . 5743 1 184 . 1 1 57 57 THR HA H 1 4.35 0.03 . 1 . . . . . . . . 5743 1 185 . 1 1 57 57 THR C C 13 175.44 0.05 . 1 . . . . . . . . 5743 1 186 . 1 1 57 57 THR CA C 13 62.17 0.05 . 1 . . . . . . . . 5743 1 187 . 1 1 57 57 THR N N 15 116.63 0.05 . 1 . . . . . . . . 5743 1 188 . 1 1 58 58 GLY H H 1 8.42 0.03 . 1 . . . . . . . . 5743 1 189 . 1 1 58 58 GLY HA2 H 1 4.00 0.03 . 1 . . . . . . . . 5743 1 190 . 1 1 58 58 GLY HA3 H 1 4.00 0.03 . 1 . . . . . . . . 5743 1 191 . 1 1 58 58 GLY N N 15 110.62 0.05 . 1 . . . . . . . . 5743 1 192 . 1 1 59 59 SER H H 1 8.31 0.03 . 1 . . . . . . . . 5743 1 193 . 1 1 59 59 SER HA H 1 4.43 0.03 . 1 . . . . . . . . 5743 1 194 . 1 1 59 59 SER C C 13 175.45 0.05 . 1 . . . . . . . . 5743 1 195 . 1 1 59 59 SER CA C 13 58.70 0.05 . 1 . . . . . . . . 5743 1 196 . 1 1 59 59 SER N N 15 115.22 0.05 . 1 . . . . . . . . 5743 1 197 . 1 1 60 60 GLY H H 1 8.55 0.03 . 1 . . . . . . . . 5743 1 198 . 1 1 60 60 GLY HA2 H 1 3.97 0.03 . 1 . . . . . . . . 5743 1 199 . 1 1 60 60 GLY HA3 H 1 3.97 0.03 . 1 . . . . . . . . 5743 1 200 . 1 1 60 60 GLY N N 15 110.58 0.05 . 1 . . . . . . . . 5743 1 201 . 1 1 61 61 SER H H 1 8.26 0.03 . 1 . . . . . . . . 5743 1 202 . 1 1 61 61 SER HA H 1 4.43 0.03 . 1 . . . . . . . . 5743 1 203 . 1 1 61 61 SER CA C 13 58.58 0.05 . 1 . . . . . . . . 5743 1 204 . 1 1 61 61 SER N N 15 115.26 0.05 . 1 . . . . . . . . 5743 1 205 . 1 1 64 64 HIS C C 13 175.08 0.05 . 1 . . . . . . . . 5743 1 206 . 1 1 65 65 LEU H H 1 8.16 0.03 . 1 . . . . . . . . 5743 1 207 . 1 1 65 65 LEU C C 13 176.96 0.05 . 1 . . . . . . . . 5743 1 208 . 1 1 65 65 LEU CA C 13 55.59 0.05 . 1 . . . . . . . . 5743 1 209 . 1 1 65 65 LEU N N 15 122.85 0.05 . 1 . . . . . . . . 5743 1 210 . 1 1 66 66 GLN H H 1 8.31 0.03 . 1 . . . . . . . . 5743 1 211 . 1 1 66 66 GLN HA H 1 4.30 0.03 . 1 . . . . . . . . 5743 1 212 . 1 1 66 66 GLN C C 13 175.35 0.05 . 1 . . . . . . . . 5743 1 213 . 1 1 66 66 GLN CA C 13 55.78 0.05 . 1 . . . . . . . . 5743 1 214 . 1 1 66 66 GLN N N 15 120.27 0.05 . 1 . . . . . . . . 5743 1 215 . 1 1 67 67 PHE H H 1 8.23 0.03 . 1 . . . . . . . . 5743 1 216 . 1 1 67 67 PHE HA H 1 4.64 0.03 . 1 . . . . . . . . 5743 1 217 . 1 1 67 67 PHE C C 13 175.08 0.05 . 1 . . . . . . . . 5743 1 218 . 1 1 67 67 PHE CA C 13 57.57 0.05 . 1 . . . . . . . . 5743 1 219 . 1 1 67 67 PHE N N 15 121.27 0.05 . 1 . . . . . . . . 5743 1 220 . 1 1 68 68 ILE H H 1 8.08 0.03 . 1 . . . . . . . . 5743 1 221 . 1 1 68 68 ILE HA H 1 4.39 0.03 . 1 . . . . . . . . 5743 1 222 . 1 1 68 68 ILE CA C 13 58.07 0.05 . 1 . . . . . . . . 5743 1 223 . 1 1 68 68 ILE N N 15 125.00 0.05 . 1 . . . . . . . . 5743 1 224 . 1 1 69 69 PRO C C 13 176.18 0.05 . 1 . . . . . . . . 5743 1 225 . 1 1 70 70 VAL H H 1 8.16 0.03 . 1 . . . . . . . . 5743 1 226 . 1 1 70 70 VAL HA H 1 4.01 0.03 . 1 . . . . . . . . 5743 1 227 . 1 1 70 70 VAL C C 13 175.88 0.05 . 1 . . . . . . . . 5743 1 228 . 1 1 70 70 VAL CA C 13 62.17 0.05 . 1 . . . . . . . . 5743 1 229 . 1 1 70 70 VAL N N 15 120.09 0.05 . 1 . . . . . . . . 5743 1 230 . 1 1 71 71 ALA H H 1 8.34 0.03 . 1 . . . . . . . . 5743 1 231 . 1 1 71 71 ALA HA H 1 4.58 0.03 . 1 . . . . . . . . 5743 1 232 . 1 1 71 71 ALA CA C 13 50.47 0.05 . 1 . . . . . . . . 5743 1 233 . 1 1 71 71 ALA N N 15 129.03 0.05 . 1 . . . . . . . . 5743 1 234 . 1 1 73 73 PRO C C 13 177.06 0.05 . 1 . . . . . . . . 5743 1 235 . 1 1 74 74 SER H H 1 8.43 0.03 . 1 . . . . . . . . 5743 1 236 . 1 1 74 74 SER HA H 1 4.48 0.03 . 1 . . . . . . . . 5743 1 237 . 1 1 74 74 SER CA C 13 56.47 0.05 . 1 . . . . . . . . 5743 1 238 . 1 1 74 74 SER N N 15 117.01 0.05 . 1 . . . . . . . . 5743 1 239 . 1 1 75 75 PRO C C 13 177.93 0.05 . 1 . . . . . . . . 5743 1 240 . 1 1 75 75 PRO CA C 13 63.67 0.05 . 1 . . . . . . . . 5743 1 241 . 1 1 76 76 GLY H H 1 8.50 0.03 . 1 . . . . . . . . 5743 1 242 . 1 1 76 76 GLY HA2 H 1 3.96 0.03 . 1 . . . . . . . . 5743 1 243 . 1 1 76 76 GLY HA3 H 1 3.96 0.03 . 1 . . . . . . . . 5743 1 244 . 1 1 76 76 GLY C C 13 174.66 0.05 . 1 . . . . . . . . 5743 1 245 . 1 1 76 76 GLY CA C 13 45.57 0.05 . 1 . . . . . . . . 5743 1 246 . 1 1 76 76 GLY N N 15 109.17 0.05 . 1 . . . . . . . . 5743 1 247 . 1 1 77 77 SER H H 1 8.15 0.03 . 1 . . . . . . . . 5743 1 248 . 1 1 77 77 SER HA H 1 4.44 0.03 . 1 . . . . . . . . 5743 1 249 . 1 1 77 77 SER C C 13 174.98 0.05 . 1 . . . . . . . . 5743 1 250 . 1 1 77 77 SER CA C 13 58.47 0.05 . 1 . . . . . . . . 5743 1 251 . 1 1 77 77 SER N N 15 115.28 0.05 . 1 . . . . . . . . 5743 1 252 . 1 1 78 78 SER H H 1 8.39 0.03 . 1 . . . . . . . . 5743 1 253 . 1 1 78 78 SER C C 13 174.23 0.05 . 1 . . . . . . . . 5743 1 254 . 1 1 78 78 SER CA C 13 58.47 0.05 . 1 . . . . . . . . 5743 1 255 . 1 1 78 78 SER N N 15 117.40 0.05 . 1 . . . . . . . . 5743 1 256 . 1 1 79 79 ALA H H 1 8.25 0.03 . 1 . . . . . . . . 5743 1 257 . 1 1 79 79 ALA C C 13 177.23 0.05 . 1 . . . . . . . . 5743 1 258 . 1 1 79 79 ALA CA C 13 52.37 0.05 . 1 . . . . . . . . 5743 1 259 . 1 1 79 79 ALA N N 15 125.47 0.05 . 1 . . . . . . . . 5743 1 260 . 1 1 80 80 ALA H H 1 8.23 0.03 . 1 . . . . . . . . 5743 1 261 . 1 1 80 80 ALA HA H 1 4.55 0.03 . 1 . . . . . . . . 5743 1 262 . 1 1 80 80 ALA CA C 13 50.67 0.05 . 1 . . . . . . . . 5743 1 263 . 1 1 80 80 ALA N N 15 124.50 0.05 . 1 . . . . . . . . 5743 1 264 . 1 1 81 81 PRO C C 13 176.95 0.05 . 1 . . . . . . . . 5743 1 265 . 1 1 81 81 PRO CA C 13 62.97 0.05 . 1 . . . . . . . . 5743 1 266 . 1 1 82 82 ALA H H 1 8.46 0.03 . 1 . . . . . . . . 5743 1 267 . 1 1 82 82 ALA HA H 1 4.34 0.03 . 1 . . . . . . . . 5743 1 268 . 1 1 82 82 ALA C C 13 178.17 0.05 . 1 . . . . . . . . 5743 1 269 . 1 1 82 82 ALA CA C 13 52.67 0.05 . 1 . . . . . . . . 5743 1 270 . 1 1 82 82 ALA N N 15 124.23 0.05 . 1 . . . . . . . . 5743 1 271 . 1 1 83 83 THR H H 1 8.08 0.03 . 1 . . . . . . . . 5743 1 272 . 1 1 83 83 THR HA H 1 4.27 0.03 . 1 . . . . . . . . 5743 1 273 . 1 1 83 83 THR C C 13 174.66 0.05 . 1 . . . . . . . . 5743 1 274 . 1 1 83 83 THR CA C 13 61.87 0.05 . 1 . . . . . . . . 5743 1 275 . 1 1 83 83 THR N N 15 112.84 0.05 . 1 . . . . . . . . 5743 1 276 . 1 1 84 84 GLU H H 1 8.39 0.03 . 1 . . . . . . . . 5743 1 277 . 1 1 84 84 GLU HA H 1 4.30 0.03 . 1 . . . . . . . . 5743 1 278 . 1 1 84 84 GLU C C 13 176.33 0.05 . 1 . . . . . . . . 5743 1 279 . 1 1 84 84 GLU CA C 13 56.47 0.05 . 1 . . . . . . . . 5743 1 280 . 1 1 84 84 GLU N N 15 123.17 0.05 . 1 . . . . . . . . 5743 1 281 . 1 1 85 85 VAL H H 1 8.28 0.03 . 1 . . . . . . . . 5743 1 282 . 1 1 85 85 VAL HA H 1 4.39 0.03 . 1 . . . . . . . . 5743 1 283 . 1 1 85 85 VAL CA C 13 59.87 0.05 . 1 . . . . . . . . 5743 1 284 . 1 1 85 85 VAL N N 15 122.64 0.05 . 1 . . . . . . . . 5743 1 285 . 1 1 86 86 PRO C C 13 176.89 0.05 . 1 . . . . . . . . 5743 1 286 . 1 1 86 86 PRO CA C 13 63.17 0.05 . 1 . . . . . . . . 5743 1 287 . 1 1 87 87 ASP H H 1 8.38 0.03 . 1 . . . . . . . . 5743 1 288 . 1 1 87 87 ASP HA H 1 4.51 0.03 . 1 . . . . . . . . 5743 1 289 . 1 1 87 87 ASP C C 13 176.20 0.05 . 1 . . . . . . . . 5743 1 290 . 1 1 87 87 ASP CA C 13 54.57 0.05 . 1 . . . . . . . . 5743 1 291 . 1 1 87 87 ASP N N 15 120.12 0.05 . 1 . . . . . . . . 5743 1 292 . 1 1 88 88 ARG H H 1 8.12 0.03 . 1 . . . . . . . . 5743 1 293 . 1 1 88 88 ARG C C 13 175.86 0.05 . 1 . . . . . . . . 5743 1 294 . 1 1 88 88 ARG CA C 13 55.77 0.05 . 1 . . . . . . . . 5743 1 295 . 1 1 88 88 ARG N N 15 120.28 0.05 . 1 . . . . . . . . 5743 1 296 . 1 1 89 89 ASP H H 1 8.51 0.03 . 1 . . . . . . . . 5743 1 297 . 1 1 89 89 ASP HA H 1 4.81 0.03 . 1 . . . . . . . . 5743 1 298 . 1 1 89 89 ASP CA C 13 52.67 0.05 . 1 . . . . . . . . 5743 1 299 . 1 1 89 89 ASP N N 15 123.57 0.05 . 1 . . . . . . . . 5743 1 300 . 1 1 90 90 PRO C C 13 177.53 0.05 . 1 . . . . . . . . 5743 1 301 . 1 1 90 90 PRO CA C 13 63.57 0.05 . 1 . . . . . . . . 5743 1 302 . 1 1 91 91 GLU H H 1 8.49 0.03 . 1 . . . . . . . . 5743 1 303 . 1 1 91 91 GLU HA H 1 4.20 0.03 . 1 . . . . . . . . 5743 1 304 . 1 1 91 91 GLU C C 13 176.95 0.05 . 1 . . . . . . . . 5743 1 305 . 1 1 91 91 GLU CA C 13 56.87 0.05 . 1 . . . . . . . . 5743 1 306 . 1 1 91 91 GLU N N 15 119.41 0.05 . 1 . . . . . . . . 5743 1 307 . 1 1 92 92 LYS H H 1 8.09 0.03 . 1 . . . . . . . . 5743 1 308 . 1 1 92 92 LYS HA H 1 4.11 0.03 . 1 . . . . . . . . 5743 1 309 . 1 1 92 92 LYS C C 13 175.02 0.05 . 1 . . . . . . . . 5743 1 310 . 1 1 92 92 LYS CA C 13 56.17 0.05 . 1 . . . . . . . . 5743 1 311 . 1 1 92 92 LYS N N 15 121.47 0.05 . 1 . . . . . . . . 5743 1 312 . 1 1 93 93 SER H H 1 8.43 0.03 . 1 . . . . . . . . 5743 1 313 . 1 1 93 93 SER C C 13 176.77 0.05 . 1 . . . . . . . . 5743 1 314 . 1 1 93 93 SER CA C 13 58.47 0.05 . 1 . . . . . . . . 5743 1 315 . 1 1 93 93 SER N N 15 117.48 0.05 . 1 . . . . . . . . 5743 1 316 . 1 1 94 94 SER H H 1 8.46 0.03 . 1 . . . . . . . . 5743 1 317 . 1 1 94 94 SER HA H 1 4.48 0.03 . 1 . . . . . . . . 5743 1 318 . 1 1 94 94 SER C C 13 175.08 0.05 . 1 . . . . . . . . 5743 1 319 . 1 1 94 94 SER CA C 13 58.57 0.05 . 1 . . . . . . . . 5743 1 320 . 1 1 94 94 SER N N 15 117.72 0.05 . 1 . . . . . . . . 5743 1 321 . 1 1 95 95 GLU H H 1 8.50 0.03 . 1 . . . . . . . . 5743 1 322 . 1 1 95 95 GLU HA H 1 4.28 0.03 . 1 . . . . . . . . 5743 1 323 . 1 1 95 95 GLU C C 13 176.49 0.05 . 1 . . . . . . . . 5743 1 324 . 1 1 95 95 GLU CA C 13 56.97 0.05 . 1 . . . . . . . . 5743 1 325 . 1 1 95 95 GLU N N 15 122.07 0.05 . 1 . . . . . . . . 5743 1 326 . 1 1 96 96 ASP H H 1 8.19 0.03 . 1 . . . . . . . . 5743 1 327 . 1 1 96 96 ASP C C 13 176.49 0.05 . 1 . . . . . . . . 5743 1 328 . 1 1 96 96 ASP CA C 13 54.67 0.05 . 1 . . . . . . . . 5743 1 329 . 1 1 96 96 ASP N N 15 119.84 0.05 . 1 . . . . . . . . 5743 1 330 . 1 1 97 97 ASP H H 1 8.17 0.03 . 1 . . . . . . . . 5743 1 331 . 1 1 97 97 ASP C C 13 175.92 0.05 . 1 . . . . . . . . 5743 1 332 . 1 1 97 97 ASP CA C 13 54.57 0.05 . 1 . . . . . . . . 5743 1 333 . 1 1 97 97 ASP N N 15 120.14 0.05 . 1 . . . . . . . . 5743 1 334 . 1 1 98 98 VAL H H 1 7.87 0.03 . 1 . . . . . . . . 5743 1 335 . 1 1 98 98 VAL HA H 1 4.03 0.03 . 1 . . . . . . . . 5743 1 336 . 1 1 98 98 VAL C C 13 175.17 0.05 . 1 . . . . . . . . 5743 1 337 . 1 1 98 98 VAL CA C 13 62.27 0.05 . 1 . . . . . . . . 5743 1 338 . 1 1 98 98 VAL N N 15 119.10 0.05 . 1 . . . . . . . . 5743 1 339 . 1 1 99 99 TYR H H 1 7.73 0.03 . 1 . . . . . . . . 5743 1 340 . 1 1 99 99 TYR HA H 1 4.38 0.03 . 1 . . . . . . . . 5743 1 341 . 1 1 99 99 TYR CA C 13 59.27 0.05 . 1 . . . . . . . . 5743 1 342 . 1 1 99 99 TYR N N 15 128.36 0.05 . 1 . . . . . . . . 5743 1 stop_ save_