data_5377 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5377 _Entry.Title ; Assignments of 1H, 13C and 15N resonances of human Ca2+-S100B in complex with the TRTK-12 peptide ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2002-05-15 _Entry.Accession_date 2002-05-15 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _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 Kimberly McClintock . A. . 5377 2 Gary Shaw . S. . 5377 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 5377 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 688 5377 '13C chemical shifts' 400 5377 '15N chemical shifts' 95 5377 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 . . . 2008-07-17 . update BMRB 'Updating non-standard residue' 5377 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5206 'human S100B in the calcium-bound form' 5377 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5377 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Letter to the Editor: Assignments of 1H, 13C and 15N resonances of human Ca2+-S100B in complex with the TRTK-12 peptide ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 23 _Citation.Journal_issue 3 _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 255 _Citation.Page_last 256 _Citation.Year 2002 _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 Kimberly McClintock . A. . 5377 1 2 Gary Shaw . S. . 5377 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID S100B 5377 1 TRTK-12 5377 1 'calcium-binding protein' 5377 1 stop_ save_ save_reference_1 _Citation.Sf_category citations _Citation.Sf_framecode reference_1 _Citation.Entry_ID 5377 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9519411 _Citation.Full_citation ; Smith SP, Shaw GS. A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form. Structure. 1998 Feb 15;6(2):211-22. ; _Citation.Title 'A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Structure _Citation.Journal_name_full 'Structure (London, England : 1993)' _Citation.Journal_volume 6 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0969-2126 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 211 _Citation.Page_last 222 _Citation.Year 1998 _Citation.Details ; BACKGROUND: S100B is a homodimeric member of the EF-hand calcium-binding protein superfamily. The protein has been implicated in cellular processes such as cell differentiation and growth, plays a role in cytoskeletal structure and function, and may have a role in neuropathological diseases, such as Alzheimers. The effects of S100B are mediated via its interaction with target proteins. While several studies have suggested that this interaction is propagated through a calcium-induced conformational change, leading to the exposure of a hydrophobic region of S100B, the molecular details behind this structural alteration remain unclear. RESULTS: The solution structure of calcium-saturated human S100B (Ca(2+)-S100B) has been determined by heteronuclear NMR spectroscopy. Ca(2+)-S100B forms a well defined globular structure comprising four EF-hand calcium-binding sites and an extensive hydrophobic dimer interface. A comparison of Ca(2+)-S100B with apo S100B and Ca(2+)-calbindin D9k indicates that while calcium-binding to S100B results in little change in the site I EF-hand, it induces a backbone reorientation of the N terminus of the site II EF-hand. This reorientation leads to a dramatic change in the position of helix III relative to the other helices. CONCLUSIONS: The calcium-induced reorientation of calcium-binding site II results in the increased exposure of several hydrophobic residues in helix IV and the linker region. While following the general mechanism of calcium modulatory proteins, whereby a hydrophobic target site is exposed, the 'calcium switch' observed in S100B appears to be unique from that of other EF-hand proteins and may provide insights into target specificity among calcium modulatory proteins. ; 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. P.' Smith S. P. . 5377 2 2 'G. S.' Shaw G. S. . 5377 2 stop_ save_ save_reference_2 _Citation.Sf_category citations _Citation.Sf_framecode reference_2 _Citation.Entry_ID 5377 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8520220 _Citation.Full_citation ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _Citation.Title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 277 _Citation.Page_last 293 _Citation.Year 1995 _Citation.Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; 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. Delaglio F. . . 5377 3 2 S. Grzesiek S. . . 5377 3 3 'G. W.' Vuister G. W. . 5377 3 4 G. Zhu G. . . 5377 3 5 J. Pfeifer J. . . 5377 3 6 A. Bax A. . . 5377 3 stop_ save_ save_reference_3 _Citation.Sf_category citations _Citation.Sf_framecode reference_3 _Citation.Entry_ID 5377 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Garrett, D.S., Powers, R., Gronenborn, A.M., Clore, G.M. (1991) J. Mag. Res. 95:214-220" ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_S100B-TRTK-12_complex _Assembly.Sf_category assembly _Assembly.Sf_framecode system_S100B-TRTK-12_complex _Assembly.Entry_ID 5377 _Assembly.ID 1 _Assembly.Name 'Ca(2+)S100B-TRTK-12 peptide complex' _Assembly.BMRB_code . _Assembly.Number_of_components 8 _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 'Entry 1UWO is the solution structure of human calcium-bound S100B.' _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID dimer 5377 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 'S100B subunit 1' 1 $S100B . . . native . . 1 . . 5377 1 2 'S100B subunit 2' 1 $S100B . . . native . . 1 . . 5377 1 3 'TRTK-12 molecule 1' 2 $TRTK-12 . . . native . . 2 . . 5377 1 4 'TRTK-12 molecule 2' 2 $TRTK-12 . . . native . . 2 . . 5377 1 5 'CALCIUM (II) ION 1' 3 $CA . . . native . . . . . 5377 1 6 'CALCIUM (II) ION 2' 3 $CA . . . native . . . . . 5377 1 7 'CALCIUM (II) ION 3' 3 $CA . . . native . . . . . 5377 1 8 'CALCIUM (II) ION 4' 3 $CA . . . native . . . . . 5377 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 coordination single . 1 . 1 SER 18 18 OG . 5 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 2 coordination single . 1 . 1 GLU 21 21 OE2 . 5 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 3 coordination single . 1 . 1 ASP 23 23 OD2 . 5 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 4 coordination single . 1 . 1 LYS 26 26 NZ . 5 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 5 coordination single . 1 . 1 LYS 28 28 NZ . 5 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 6 coordination single . 1 . 1 GLU 31 31 OE2 . 5 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 7 coordination single . 1 . 1 ASP 61 61 OD2 . 6 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 8 coordination single . 1 . 1 ASP 63 63 OD2 . 6 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 9 coordination single . 1 . 1 ASP 65 65 OD2 . 6 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 10 coordination single . 1 . 1 GLU 67 67 OE2 . 6 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 11 coordination single . 1 . 1 ASP 69 69 OD2 . 6 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 12 coordination single . 1 . 1 GLU 72 72 OE2 . 6 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 13 coordination single . 2 . 1 SER 18 18 OG . 7 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 14 coordination single . 2 . 1 GLU 21 21 OE2 . 7 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 15 coordination single . 2 . 1 ASP 23 23 OD2 . 7 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 16 coordination single . 2 . 1 LYS 26 26 NZ . 7 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 17 coordination single . 2 . 1 LYS 28 28 NZ . 7 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 18 coordination single . 2 . 1 GLU 31 31 OE2 . 7 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 19 coordination single . 2 . 1 ASP 61 61 OD2 . 8 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 20 coordination single . 2 . 1 ASP 63 63 OD2 . 8 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 21 coordination single . 2 . 1 ASP 65 65 OD2 . 8 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 22 coordination single . 2 . 1 GLU 67 67 OE2 . 8 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 23 coordination single . 2 . 1 ASP 69 69 OD2 . 8 . 3 CA 1 1 CA . . . . . . . . . . 5377 1 24 coordination single . 2 . 1 GLU 72 72 OE2 . 8 . 3 CA 1 1 CA . . . . . . . . . . 5377 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 . PDB 1UWO . . . . . . 5377 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Ca(2+)S100B-TRTK-12 peptide complex' system 5377 1 'S100B-TRTK-12 complex' abbreviation 5377 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_S100B _Entity.Sf_category entity _Entity.Sf_framecode S100B _Entity.Entry_ID 5377 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name S100B _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 ; SELEKAMVALIDVFHQYSGR EGDKHKLKKSELKELINNEL SHFLEEIKEQEVVDKVMETL DNDGDGECDFQEFMAFVAMV TTACHEFFEHE ; _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 91 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-03-24 _Entity.DB_query_revised_last_date 2008-01-23 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 . . SWISS-PROT P04631 . 'S100B_RAT Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . SWISS-PROT P50114 . 'S100B_MOUSE Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' . . . . . 98.91 92 99 99 9e-46 . . . . 5377 1 . . SWISS-PROT Q6YNR6 . 'S100B_RABIT Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . SWISS-PROT P04271 . 'S100B_HUMAN Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . REF XP_001487942.1 . 'PREDICTED: similar to ProteinS100-B (S100 calcium-binding protein B) (S-100 proteinbeta subunit) (S-100 protein beta cha' . . . . . 97.85 93 100 100 2e-46 . . . . 5377 1 . . REF XP_531586.1 . 'PREDICTED: S100 calcium-bindingprotein, beta isoform 3 [Pan troglodytes]' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . REF XP_001160520.1 . 'PREDICTED: S100 calcium-bindingprotein, beta isoform 1 [Pan troglodytes]' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . REF NP_006263.1 . 'S100 calcium-binding protein, beta[Homo sapiens]' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . REF NP_001076199.1 . 'S100 calcium-binding protein,beta [Oryctolagus cuniculus]' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . PRF 2003367B . 'S-100 protein:SUBUNIT=beta' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . GenBank AAX43954.1 . 'S100 calcium binding protein beta[synthetic construct]' . . . . . 97.85 93 100 100 2e-46 . . . . 5377 1 . . GenBank AAX43953.1 . 'S100 calcium binding protein beta[synthetic construct]' . . . . . 97.85 93 100 100 2e-46 . . . . 5377 1 . . GenBank AAP36596.1 . 'Homo sapiens S100 calcium bindingprotein, beta (neural) [synthetic construct]' . . . . . 97.85 93 100 100 2e-46 . . . . 5377 1 . . GenBank AAH01766.1 . 'S100 calcium binding protein B [Homosapiens]' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . GenBank AAA60367.1 . 'S100 protein beta subunit' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . EMBL CAA25567.1 . 'unnamed protein product [Rattusnorvegicus]' . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . EMBL CAG46920.1 . 'S100B [Homo sapiens]' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . DBJ BAE88979.1 . 'unnamed protein product [Macacafascicularis]' . . . . . 98.91 92 99 100 7e-46 . . . . 5377 1 . . DBJ BAE36647.1 . 'unnamed protein product [Musmusculus]' . . . . . 98.91 92 99 99 9e-46 . . . . 5377 1 . . DBJ BAE22413.1 . 'unnamed protein product [Musmusculus]' . . . . . 98.91 92 99 99 9e-46 . . . . 5377 1 . . DBJ BAE22214.1 . 'unnamed protein product [Musmusculus]' . . . . . 98.91 92 99 99 9e-46 . . . . 5377 1 . . PDB 1XYD . 'A Chain A, Nmr Solution Structure Of RatZinc-Calcium-S100b, 20 Structures' . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . PDB 1SYM . 'A Chain A, 3-D Solution Structure Of ReducedApo-S100b From Rat, Nmr, 20 Structures' . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . PDB 1QLK . 'A Chain A, Solution Structure OfCa(2+)-Loaded Rat S100b (Betabeta) Nmr, 20 Structures' . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . PDB 1MWN . 'A Chain A, Solution Nmr Structure Of S100bBound To The High-Affinity Target Peptide Trtk-12' . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . PDB 1DT7 . 'A Chain A, Solution Structure Of TheC-Terminal Negative Regulatory Domain Of P53 In AComplex With Ca2+-Bound S100b(Bb)' . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . PDB 1B4C . 'A Chain A, Solution Structure Of RatApo-S100b Using Dipolar Couplings' . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . PDB 2H61 . 'A Chain A, X-Ray Structure Of HumanCa2+-Loaded S100b' . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . PDB 1UWO . 'A Chain A, Calcium Form Of Human S100b,Nmr, 20 Structures' . . . . . 100.00 91 100 100 2e-46 . . . . 5377 1 . . PDB 1MQ1 . 'A Chain A, Ca2+-S100b-Trtk-12 Complex' . . . . . 100.00 91 100 100 2e-46 . . . . 5377 1 . . BMRB 5895 . S100B . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . BMRB 5544 . S100B . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . BMRB 4105 . S100B . . . . . 98.91 92 98 99 2e-45 . . . . 5377 1 . . BMRB 5206 . S100B . . . . . 98.91 92 100 100 2e-46 . . . . 5377 1 . . BMRB 4702 . 'S100B beta' . . . . . 100.00 91 98 99 2e-45 . . . . 5377 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID S100B common 5377 1 S100B abbreviation 5377 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . SER . 5377 1 2 . GLU . 5377 1 3 . LEU . 5377 1 4 . GLU . 5377 1 5 . LYS . 5377 1 6 . ALA . 5377 1 7 . MET . 5377 1 8 . VAL . 5377 1 9 . ALA . 5377 1 10 . LEU . 5377 1 11 . ILE . 5377 1 12 . ASP . 5377 1 13 . VAL . 5377 1 14 . PHE . 5377 1 15 . HIS . 5377 1 16 . GLN . 5377 1 17 . TYR . 5377 1 18 . SER . 5377 1 19 . GLY . 5377 1 20 . ARG . 5377 1 21 . GLU . 5377 1 22 . GLY . 5377 1 23 . ASP . 5377 1 24 . LYS . 5377 1 25 . HIS . 5377 1 26 . LYS . 5377 1 27 . LEU . 5377 1 28 . LYS . 5377 1 29 . LYS . 5377 1 30 . SER . 5377 1 31 . GLU . 5377 1 32 . LEU . 5377 1 33 . LYS . 5377 1 34 . GLU . 5377 1 35 . LEU . 5377 1 36 . ILE . 5377 1 37 . ASN . 5377 1 38 . ASN . 5377 1 39 . GLU . 5377 1 40 . LEU . 5377 1 41 . SER . 5377 1 42 . HIS . 5377 1 43 . PHE . 5377 1 44 . LEU . 5377 1 45 . GLU . 5377 1 46 . GLU . 5377 1 47 . ILE . 5377 1 48 . LYS . 5377 1 49 . GLU . 5377 1 50 . GLN . 5377 1 51 . GLU . 5377 1 52 . VAL . 5377 1 53 . VAL . 5377 1 54 . ASP . 5377 1 55 . LYS . 5377 1 56 . VAL . 5377 1 57 . MET . 5377 1 58 . GLU . 5377 1 59 . THR . 5377 1 60 . LEU . 5377 1 61 . ASP . 5377 1 62 . ASN . 5377 1 63 . ASP . 5377 1 64 . GLY . 5377 1 65 . ASP . 5377 1 66 . GLY . 5377 1 67 . GLU . 5377 1 68 . CYS . 5377 1 69 . ASP . 5377 1 70 . PHE . 5377 1 71 . GLN . 5377 1 72 . GLU . 5377 1 73 . PHE . 5377 1 74 . MET . 5377 1 75 . ALA . 5377 1 76 . PHE . 5377 1 77 . VAL . 5377 1 78 . ALA . 5377 1 79 . MET . 5377 1 80 . VAL . 5377 1 81 . THR . 5377 1 82 . THR . 5377 1 83 . ALA . 5377 1 84 . CYS . 5377 1 85 . HIS . 5377 1 86 . GLU . 5377 1 87 . PHE . 5377 1 88 . PHE . 5377 1 89 . GLU . 5377 1 90 . HIS . 5377 1 91 . GLU . 5377 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . SER 1 1 5377 1 . GLU 2 2 5377 1 . LEU 3 3 5377 1 . GLU 4 4 5377 1 . LYS 5 5 5377 1 . ALA 6 6 5377 1 . MET 7 7 5377 1 . VAL 8 8 5377 1 . ALA 9 9 5377 1 . LEU 10 10 5377 1 . ILE 11 11 5377 1 . ASP 12 12 5377 1 . VAL 13 13 5377 1 . PHE 14 14 5377 1 . HIS 15 15 5377 1 . GLN 16 16 5377 1 . TYR 17 17 5377 1 . SER 18 18 5377 1 . GLY 19 19 5377 1 . ARG 20 20 5377 1 . GLU 21 21 5377 1 . GLY 22 22 5377 1 . ASP 23 23 5377 1 . LYS 24 24 5377 1 . HIS 25 25 5377 1 . LYS 26 26 5377 1 . LEU 27 27 5377 1 . LYS 28 28 5377 1 . LYS 29 29 5377 1 . SER 30 30 5377 1 . GLU 31 31 5377 1 . LEU 32 32 5377 1 . LYS 33 33 5377 1 . GLU 34 34 5377 1 . LEU 35 35 5377 1 . ILE 36 36 5377 1 . ASN 37 37 5377 1 . ASN 38 38 5377 1 . GLU 39 39 5377 1 . LEU 40 40 5377 1 . SER 41 41 5377 1 . HIS 42 42 5377 1 . PHE 43 43 5377 1 . LEU 44 44 5377 1 . GLU 45 45 5377 1 . GLU 46 46 5377 1 . ILE 47 47 5377 1 . LYS 48 48 5377 1 . GLU 49 49 5377 1 . GLN 50 50 5377 1 . GLU 51 51 5377 1 . VAL 52 52 5377 1 . VAL 53 53 5377 1 . ASP 54 54 5377 1 . LYS 55 55 5377 1 . VAL 56 56 5377 1 . MET 57 57 5377 1 . GLU 58 58 5377 1 . THR 59 59 5377 1 . LEU 60 60 5377 1 . ASP 61 61 5377 1 . ASN 62 62 5377 1 . ASP 63 63 5377 1 . GLY 64 64 5377 1 . ASP 65 65 5377 1 . GLY 66 66 5377 1 . GLU 67 67 5377 1 . CYS 68 68 5377 1 . ASP 69 69 5377 1 . PHE 70 70 5377 1 . GLN 71 71 5377 1 . GLU 72 72 5377 1 . PHE 73 73 5377 1 . MET 74 74 5377 1 . ALA 75 75 5377 1 . PHE 76 76 5377 1 . VAL 77 77 5377 1 . ALA 78 78 5377 1 . MET 79 79 5377 1 . VAL 80 80 5377 1 . THR 81 81 5377 1 . THR 82 82 5377 1 . ALA 83 83 5377 1 . CYS 84 84 5377 1 . HIS 85 85 5377 1 . GLU 86 86 5377 1 . PHE 87 87 5377 1 . PHE 88 88 5377 1 . GLU 89 89 5377 1 . HIS 90 90 5377 1 . GLU 91 91 5377 1 stop_ save_ save_TRTK-12 _Entity.Sf_category entity _Entity.Sf_framecode TRTK-12 _Entity.Entry_ID 5377 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name TRTK-12 _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 XTRTKIDWNKILSX _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 14 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2005-11-24 _Entity.DB_query_revised_last_date 2002-08-25 loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID TRTK-12 common 5377 2 TRTK-12 abbreviation 5377 2 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 . ACE . 5377 2 2 . THR . 5377 2 3 . ARG . 5377 2 4 . THR . 5377 2 5 . LYS . 5377 2 6 . ILE . 5377 2 7 . ASP . 5377 2 8 . TRP . 5377 2 9 . ASN . 5377 2 10 . LYS . 5377 2 11 . ILE . 5377 2 12 . LEU . 5377 2 13 . SER . 5377 2 14 . NH2 . 5377 2 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 . ACE 1 1 5377 2 . THR 2 2 5377 2 . ARG 3 3 5377 2 . THR 4 4 5377 2 . LYS 5 5 5377 2 . ILE 6 6 5377 2 . ASP 7 7 5377 2 . TRP 8 8 5377 2 . ASN 9 9 5377 2 . LYS 10 10 5377 2 . ILE 11 11 5377 2 . LEU 12 12 5377 2 . SER 13 13 5377 2 . NH2 14 14 5377 2 stop_ save_ save_CA _Entity.Sf_category entity _Entity.Sf_framecode CA _Entity.Entry_ID 5377 _Entity.ID 3 _Entity.BMRB_code . _Entity.Name CA _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID CA _Entity.Nonpolymer_comp_label $chem_comp_CA _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 3 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . CA . 5377 3 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 5377 _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 $S100B . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . 'The TRTK-12 peptide has no natural source.' . . 5377 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 5377 _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 $S100B . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli N99 . . . . . . . . . . . . . . . . . . . . . . 5377 1 2 2 $TRTK-12 . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5377 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_ACE _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_ACE _Chem_comp.Entry_ID 5377 _Chem_comp.ID ACE _Chem_comp.Provenance . _Chem_comp.Name 'ACETYL GROUP' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code ACE _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces ACU _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code ACE _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C2 H4 O' _Chem_comp.Formula_weight 44.053 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site PDBE _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 16:15:33 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID O=CC SMILES ACDLabs 10.04 5377 ACE CC=O SMILES_CANONICAL CACTVS 3.341 5377 ACE CC=O SMILES CACTVS 3.341 5377 ACE CC=O SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5377 ACE CC=O SMILES 'OpenEye OEToolkits' 1.5.0 5377 ACE InChI=1S/C2H4O/c1-2-3/h2H,1H3 InChI InChI 1.03 5377 ACE IKHGUXGNUITLKF-UHFFFAOYSA-N InChIKey InChI 1.03 5377 ACE stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID acetaldehyde 'SYSTEMATIC NAME' ACDLabs 10.04 5377 ACE ethanal 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5377 ACE stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID C . C . . C . . N 0 . . . . no no . . . . 0.772 . -10.072 . 6.578 . -0.133 0.453 0.000 1 . 5377 ACE O . O . . O . . N 0 . . . . no no . . . . 1.973 . -10.223 . 6.862 . -1.113 -0.252 0.000 2 . 5377 ACE CH3 . CH3 . . C . . N 0 . . . . no no . . . . -0.322 . -10.677 . 7.405 . 1.241 -0.167 0.000 3 . 5377 ACE H . H . . H . . N 0 . . . . no no . . . . 0.685 . -9.453 . 5.669 . -0.240 1.528 0.000 4 . 5377 ACE H1 . H1 . . H . . N 0 . . . . no no . . . . -1.191 . -10.444 . 7.018 . 1.360 -0.785 0.890 5 . 5377 ACE H2 . H2 . . H . . N 0 . . . . no no . . . . -0.269 . -10.331 . 8.320 . 1.360 -0.785 -0.890 6 . 5377 ACE H3 . H3 . . H . . N 0 . . . . no no . . . . -0.221 . -11.652 . 7.418 . 1.995 0.620 0.000 7 . 5377 ACE stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . DOUB C O no N 1 . 5377 ACE 2 . SING C CH3 no N 2 . 5377 ACE 3 . SING C H no N 3 . 5377 ACE 4 . SING CH3 H1 no N 4 . 5377 ACE 5 . SING CH3 H2 no N 5 . 5377 ACE 6 . SING CH3 H3 no N 6 . 5377 ACE stop_ save_ save_chem_comp_NH2 _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_NH2 _Chem_comp.Entry_ID 5377 _Chem_comp.ID NH2 _Chem_comp.Provenance . _Chem_comp.Name 'AMINO GROUP' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code NH2 _Chem_comp.Ambiguous_flag yes _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2008-10-14 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code NH2 _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'H2 N' _Chem_comp.Formula_weight 16.023 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 2FLY _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 16:09:34 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID N SMILES ACDLabs 10.04 5377 NH2 InChI=1/H3N/h1H3 InChI InChI 1.02b 5377 NH2 QGZKDVFQNNGYKY-UHFFFAOYAF InChIKey InChI 1.02b 5377 NH2 [NH2] SMILES_CANONICAL CACTVS 3.341 5377 NH2 [NH2] SMILES CACTVS 3.341 5377 NH2 [NH2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5377 NH2 [NH2] SMILES 'OpenEye OEToolkits' 1.5.0 5377 NH2 stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID ammonia 'SYSTEMATIC NAME' ACDLabs 10.04 5377 NH2 l^{2}-azane 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5377 NH2 stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N . N . . N . . N 0 . . . . no no . . . . 10.091 . 8.978 . -7.810 . 0.000 0.000 0.000 1 . 5377 NH2 HN1 . HN1 . . H . . N 0 . . . . no no . . . . 9.517 . 8.769 . -7.044 . -0.385 -0.545 -0.771 2 . 5377 NH2 HN2 . HN2 . . H . . N 0 . . . . no no . . . . 10.323 . 9.890 . -8.082 . 1.020 0.000 0.000 3 . 5377 NH2 stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N HN1 no N 1 . 5377 NH2 2 . SING N HN2 no N 2 . 5377 NH2 stop_ save_ save_chem_comp_CA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CA _Chem_comp.Entry_ID 5377 _Chem_comp.ID CA _Chem_comp.Provenance . _Chem_comp.Name 'CALCIUM ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code CA _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CA _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Ca _Chem_comp.Formula_weight 40.078 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 13 17:18:35 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Ca+2] SMILES ACDLabs 10.04 5377 CA [Ca++] SMILES_CANONICAL CACTVS 3.341 5377 CA [Ca++] SMILES CACTVS 3.341 5377 CA [Ca+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5377 CA [Ca+2] SMILES 'OpenEye OEToolkits' 1.5.0 5377 CA InChI=1S/Ca/q+2 InChI InChI 1.03 5377 CA BHPQYMZQTOCNFJ-UHFFFAOYSA-N InChIKey InChI 1.03 5377 CA stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID calcium 'SYSTEMATIC NAME' ACDLabs 10.04 5377 CA 'calcium(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5377 CA stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID CA . CA . . CA . . N 2 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 5377 CA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5377 _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 S100B '[U-13C; U-15N]' . . 1 $S100B . . 1.0 . . mM . . . . 5377 1 2 TRTK-12 . . . 2 $TRTK-12 . . 1.2 . . mM . . . . 5377 1 3 'CALCIUM (II) ION' . . . 3 $CA . . 3 . . mM . . . . 5377 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5377 _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 S100B '[U-2H; U-15N]' . . 1 $S100B . . 0.350 . . mM . . . . 5377 2 2 TRTK-12 . . . 2 $TRTK-12 . . 0.8 . . mM . . . . 5377 2 3 'CALCIUM (II) ION' . . . 3 $CA . . 1.0 . . mM . . . . 5377 2 stop_ save_ save_sample_3 _Sample.Sf_category sample _Sample.Sf_framecode sample_3 _Sample.Entry_ID 5377 _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 S100B '[U-15N; U-13C]' . . 1 $S100B . . 1.0 . . mM . . . . 5377 3 2 TRTK-12 '[U-13C]-acetyl; [U-13C]-Ile' . . 2 $TRTK-12 . . 1.2 . . mM . . . . 5377 3 3 'CALCIUM (II) ION' . . . 3 $CA . . 3 . . mM . . . . 5377 3 stop_ save_ ####################### # Sample conditions # ####################### save_experimental_conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode experimental_conditions _Sample_condition_list.Entry_ID 5377 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.05 0.05 n/a 5377 1 temperature 308 0.10 K 5377 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 5377 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 5377 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $reference_2 5377 1 stop_ save_ save_Pipp _Software.Sf_category software _Software.Sf_framecode Pipp _Software.Entry_ID 5377 _Software.ID 2 _Software.Name Pipp _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak assignment' 5377 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $reference_3 5377 2 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 5377 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UNITY _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 5377 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 5377 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5377 _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 Varian UNITY . 500 . . . 5377 1 2 spectrometer_2 Varian INOVA . 600 . . . 5377 1 3 spectrometer_3 Varian INOVA . 800 . . . 5377 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 5377 _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 CBCA(CO)NH . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 2 HNCACB . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 3 C(CO)NH . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 4 HC(CO)NH . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 5 '1H-15N HSQC' . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 6 '1H-13N HSQC' . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 7 '1H-15N NOESY' . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 8 '1H-15N TOCSY' . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 9 '1H-13C NOESY' . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 10 HCCH-TOCSY . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 11 HNHA . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 12 HNCO . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 13 '1H-1H NOESY' . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 1 14 '1H-1H TOCSY' . . . . . . . . . . . . . . . . 1 $experimental_conditions . . . . . . . . . . . . . . . . . . . . . 5377 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 5377 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.00 external direct 1.000000000 external cylindrical . . . . . . . 5377 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 external indirect 0.101329118 external cylindrical . . . . . . . 5377 1 C 13 DSS 'methyl protons' . . . . ppm 0.00 external indirect 0.251449530 external cylindrical . . . . . . . 5377 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_chemical_shifts_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shifts_set_1 _Assigned_chem_shift_list.Entry_ID 5377 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $experimental_conditions _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 . 5377 1 . . 2 $sample_2 . 5377 1 . . 3 $sample_3 . 5377 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 SER H H 1 9.99 0.01 . 1 . . . . . . . . 5377 1 2 . 1 1 1 1 SER HA H 1 4.74 0.01 . 1 . . . . . . . . 5377 1 3 . 1 1 1 1 SER HB2 H 1 4.22 0.01 . 1 . . . . . . . . 5377 1 4 . 1 1 1 1 SER HB3 H 1 4.22 0.01 . 1 . . . . . . . . 5377 1 5 . 1 1 1 1 SER C C 13 174.68 0.20 . 1 . . . . . . . . 5377 1 6 . 1 1 1 1 SER CA C 13 57.11 0.20 . 1 . . . . . . . . 5377 1 7 . 1 1 1 1 SER CB C 13 65.68 0.20 . 1 . . . . . . . . 5377 1 8 . 1 1 1 1 SER N N 15 121.76 0.20 . 1 . . . . . . . . 5377 1 9 . 1 1 2 2 GLU H H 1 9.27 0.01 . 1 . . . . . . . . 5377 1 10 . 1 1 2 2 GLU HA H 1 4.12 0.01 . 1 . . . . . . . . 5377 1 11 . 1 1 2 2 GLU HB2 H 1 2.22 0.01 . 2 . . . . . . . . 5377 1 12 . 1 1 2 2 GLU HB3 H 1 2.26 0.01 . 2 . . . . . . . . 5377 1 13 . 1 1 2 2 GLU HG2 H 1 2.51 0.01 . 1 . . . . . . . . 5377 1 14 . 1 1 2 2 GLU HG3 H 1 2.51 0.01 . 1 . . . . . . . . 5377 1 15 . 1 1 2 2 GLU C C 13 179.66 0.20 . 1 . . . . . . . . 5377 1 16 . 1 1 2 2 GLU CA C 13 59.88 0.20 . 1 . . . . . . . . 5377 1 17 . 1 1 2 2 GLU CB C 13 29.31 0.20 . 1 . . . . . . . . 5377 1 18 . 1 1 2 2 GLU CG C 13 36.30 0.20 . 1 . . . . . . . . 5377 1 19 . 1 1 2 2 GLU N N 15 120.18 0.20 . 1 . . . . . . . . 5377 1 20 . 1 1 3 3 LEU H H 1 8.75 0.01 . 1 . . . . . . . . 5377 1 21 . 1 1 3 3 LEU HA H 1 4.22 0.01 . 1 . . . . . . . . 5377 1 22 . 1 1 3 3 LEU HB2 H 1 1.80 0.01 . 2 . . . . . . . . 5377 1 23 . 1 1 3 3 LEU HB3 H 1 1.93 0.01 . 2 . . . . . . . . 5377 1 24 . 1 1 3 3 LEU HG H 1 1.44 0.01 . 1 . . . . . . . . 5377 1 25 . 1 1 3 3 LEU HD11 H 1 0.69 0.01 . 2 . . . . . . . . 5377 1 26 . 1 1 3 3 LEU HD12 H 1 0.69 0.01 . 2 . . . . . . . . 5377 1 27 . 1 1 3 3 LEU HD13 H 1 0.69 0.01 . 2 . . . . . . . . 5377 1 28 . 1 1 3 3 LEU HD21 H 1 1.11 0.01 . 2 . . . . . . . . 5377 1 29 . 1 1 3 3 LEU HD22 H 1 1.11 0.01 . 2 . . . . . . . . 5377 1 30 . 1 1 3 3 LEU HD23 H 1 1.11 0.01 . 2 . . . . . . . . 5377 1 31 . 1 1 3 3 LEU C C 13 177.75 0.20 . 1 . . . . . . . . 5377 1 32 . 1 1 3 3 LEU CA C 13 58.10 0.20 . 1 . . . . . . . . 5377 1 33 . 1 1 3 3 LEU CB C 13 42.61 0.20 . 1 . . . . . . . . 5377 1 34 . 1 1 3 3 LEU CG C 13 27.75 0.20 . 1 . . . . . . . . 5377 1 35 . 1 1 3 3 LEU CD1 C 13 26.77 0.20 . 2 . . . . . . . . 5377 1 36 . 1 1 3 3 LEU CD2 C 13 24.92 0.20 . 2 . . . . . . . . 5377 1 37 . 1 1 3 3 LEU N N 15 121.84 0.20 . 1 . . . . . . . . 5377 1 38 . 1 1 4 4 GLU H H 1 8.24 0.01 . 1 . . . . . . . . 5377 1 39 . 1 1 4 4 GLU HA H 1 3.91 0.01 . 1 . . . . . . . . 5377 1 40 . 1 1 4 4 GLU HB2 H 1 2.37 0.01 . 1 . . . . . . . . 5377 1 41 . 1 1 4 4 GLU HB3 H 1 2.37 0.01 . 1 . . . . . . . . 5377 1 42 . 1 1 4 4 GLU HG2 H 1 2.53 0.01 . 1 . . . . . . . . 5377 1 43 . 1 1 4 4 GLU HG3 H 1 2.53 0.01 . 1 . . . . . . . . 5377 1 44 . 1 1 4 4 GLU C C 13 178.90 0.20 . 1 . . . . . . . . 5377 1 45 . 1 1 4 4 GLU CA C 13 59.34 0.20 . 1 . . . . . . . . 5377 1 46 . 1 1 4 4 GLU CB C 13 29.56 0.20 . 1 . . . . . . . . 5377 1 47 . 1 1 4 4 GLU CG C 13 38.18 0.20 . 1 . . . . . . . . 5377 1 48 . 1 1 4 4 GLU N N 15 120.03 0.20 . 1 . . . . . . . . 5377 1 49 . 1 1 5 5 LYS H H 1 8.73 0.01 . 1 . . . . . . . . 5377 1 50 . 1 1 5 5 LYS HA H 1 3.97 0.01 . 1 . . . . . . . . 5377 1 51 . 1 1 5 5 LYS HB2 H 1 1.93 0.01 . 1 . . . . . . . . 5377 1 52 . 1 1 5 5 LYS HB3 H 1 1.93 0.01 . 1 . . . . . . . . 5377 1 53 . 1 1 5 5 LYS HG2 H 1 1.42 0.01 . 1 . . . . . . . . 5377 1 54 . 1 1 5 5 LYS HG3 H 1 1.42 0.01 . 1 . . . . . . . . 5377 1 55 . 1 1 5 5 LYS HD2 H 1 1.72 0.01 . 2 . . . . . . . . 5377 1 56 . 1 1 5 5 LYS HD3 H 1 1.79 0.01 . 2 . . . . . . . . 5377 1 57 . 1 1 5 5 LYS HE2 H 1 2.91 0.01 . 1 . . . . . . . . 5377 1 58 . 1 1 5 5 LYS HE3 H 1 2.91 0.01 . 1 . . . . . . . . 5377 1 59 . 1 1 5 5 LYS C C 13 179.78 0.20 . 1 . . . . . . . . 5377 1 60 . 1 1 5 5 LYS CA C 13 60.01 0.20 . 1 . . . . . . . . 5377 1 61 . 1 1 5 5 LYS CB C 13 32.90 0.20 . 1 . . . . . . . . 5377 1 62 . 1 1 5 5 LYS CG C 13 26.69 0.20 . 1 . . . . . . . . 5377 1 63 . 1 1 5 5 LYS CD C 13 29.82 0.20 . 1 . . . . . . . . 5377 1 64 . 1 1 5 5 LYS CE C 13 42.01 0.20 . 1 . . . . . . . . 5377 1 65 . 1 1 5 5 LYS N N 15 117.67 0.20 . 1 . . . . . . . . 5377 1 66 . 1 1 6 6 ALA H H 1 8.08 0.01 . 1 . . . . . . . . 5377 1 67 . 1 1 6 6 ALA HA H 1 4.29 0.01 . 1 . . . . . . . . 5377 1 68 . 1 1 6 6 ALA HB1 H 1 1.79 0.01 . 1 . . . . . . . . 5377 1 69 . 1 1 6 6 ALA HB2 H 1 1.79 0.01 . 1 . . . . . . . . 5377 1 70 . 1 1 6 6 ALA HB3 H 1 1.79 0.01 . 1 . . . . . . . . 5377 1 71 . 1 1 6 6 ALA CA C 13 55.21 0.20 . 1 . . . . . . . . 5377 1 72 . 1 1 6 6 ALA CB C 13 18.20 0.20 . 1 . . . . . . . . 5377 1 73 . 1 1 6 6 ALA N N 15 124.14 0.20 . 1 . . . . . . . . 5377 1 74 . 1 1 7 7 MET H H 1 7.95 0.01 . 1 . . . . . . . . 5377 1 75 . 1 1 7 7 MET HA H 1 3.81 0.01 . 1 . . . . . . . . 5377 1 76 . 1 1 7 7 MET HB2 H 1 1.69 0.01 . 2 . . . . . . . . 5377 1 77 . 1 1 7 7 MET HB3 H 1 1.71 0.01 . 2 . . . . . . . . 5377 1 78 . 1 1 7 7 MET CA C 13 62.96 0.20 . 1 . . . . . . . . 5377 1 79 . 1 1 7 7 MET CB C 13 39.20 0.20 . 1 . . . . . . . . 5377 1 80 . 1 1 7 7 MET N N 15 116.75 0.20 . 1 . . . . . . . . 5377 1 81 . 1 1 8 8 VAL H H 1 8.08 0.01 . 1 . . . . . . . . 5377 1 82 . 1 1 8 8 VAL HA H 1 3.64 0.01 . 1 . . . . . . . . 5377 1 83 . 1 1 8 8 VAL HB H 1 2.27 0.01 . 1 . . . . . . . . 5377 1 84 . 1 1 8 8 VAL HG11 H 1 1.21 0.01 . 2 . . . . . . . . 5377 1 85 . 1 1 8 8 VAL HG12 H 1 1.21 0.01 . 2 . . . . . . . . 5377 1 86 . 1 1 8 8 VAL HG13 H 1 1.21 0.01 . 2 . . . . . . . . 5377 1 87 . 1 1 8 8 VAL HG21 H 1 1.05 0.01 . 2 . . . . . . . . 5377 1 88 . 1 1 8 8 VAL HG22 H 1 1.05 0.01 . 2 . . . . . . . . 5377 1 89 . 1 1 8 8 VAL HG23 H 1 1.05 0.01 . 2 . . . . . . . . 5377 1 90 . 1 1 8 8 VAL C C 13 177.77 0.20 . 1 . . . . . . . . 5377 1 91 . 1 1 8 8 VAL CA C 13 66.86 0.20 . 1 . . . . . . . . 5377 1 92 . 1 1 8 8 VAL CB C 13 31.83 0.20 . 1 . . . . . . . . 5377 1 93 . 1 1 8 8 VAL CG1 C 13 23.33 0.20 . 2 . . . . . . . . 5377 1 94 . 1 1 8 8 VAL CG2 C 13 21.73 0.20 . 2 . . . . . . . . 5377 1 95 . 1 1 8 8 VAL N N 15 117.22 0.20 . 1 . . . . . . . . 5377 1 96 . 1 1 9 9 ALA H H 1 8.22 0.01 . 1 . . . . . . . . 5377 1 97 . 1 1 9 9 ALA HA H 1 4.37 0.01 . 1 . . . . . . . . 5377 1 98 . 1 1 9 9 ALA HB1 H 1 1.67 0.01 . 1 . . . . . . . . 5377 1 99 . 1 1 9 9 ALA HB2 H 1 1.67 0.01 . 1 . . . . . . . . 5377 1 100 . 1 1 9 9 ALA HB3 H 1 1.67 0.01 . 1 . . . . . . . . 5377 1 101 . 1 1 9 9 ALA CA C 13 55.58 0.20 . 1 . . . . . . . . 5377 1 102 . 1 1 9 9 ALA CB C 13 18.38 0.20 . 1 . . . . . . . . 5377 1 103 . 1 1 9 9 ALA N N 15 123.37 0.20 . 1 . . . . . . . . 5377 1 104 . 1 1 10 10 LEU H H 1 8.07 0.01 . 1 . . . . . . . . 5377 1 105 . 1 1 10 10 LEU HA H 1 4.18 0.01 . 1 . . . . . . . . 5377 1 106 . 1 1 10 10 LEU HB2 H 1 1.63 0.01 . 2 . . . . . . . . 5377 1 107 . 1 1 10 10 LEU HB3 H 1 2.64 0.01 . 2 . . . . . . . . 5377 1 108 . 1 1 10 10 LEU HG H 1 2.44 0.01 . 1 . . . . . . . . 5377 1 109 . 1 1 10 10 LEU HD11 H 1 0.92 0.01 . 1 . . . . . . . . 5377 1 110 . 1 1 10 10 LEU HD12 H 1 0.92 0.01 . 1 . . . . . . . . 5377 1 111 . 1 1 10 10 LEU HD13 H 1 0.92 0.01 . 1 . . . . . . . . 5377 1 112 . 1 1 10 10 LEU HD21 H 1 0.92 0.01 . 1 . . . . . . . . 5377 1 113 . 1 1 10 10 LEU HD22 H 1 0.92 0.01 . 1 . . . . . . . . 5377 1 114 . 1 1 10 10 LEU HD23 H 1 0.92 0.01 . 1 . . . . . . . . 5377 1 115 . 1 1 10 10 LEU C C 13 178.62 0.20 . 1 . . . . . . . . 5377 1 116 . 1 1 10 10 LEU CA C 13 58.96 0.20 . 1 . . . . . . . . 5377 1 117 . 1 1 10 10 LEU CB C 13 42.06 0.20 . 1 . . . . . . . . 5377 1 118 . 1 1 10 10 LEU CG C 13 26.18 0.20 . 1 . . . . . . . . 5377 1 119 . 1 1 10 10 LEU CD1 C 13 23.99 0.20 . 2 . . . . . . . . 5377 1 120 . 1 1 10 10 LEU CD2 C 13 26.03 0.20 . 2 . . . . . . . . 5377 1 121 . 1 1 10 10 LEU N N 15 117.54 0.20 . 1 . . . . . . . . 5377 1 122 . 1 1 11 11 ILE H H 1 7.47 0.01 . 1 . . . . . . . . 5377 1 123 . 1 1 11 11 ILE HA H 1 3.70 0.01 . 1 . . . . . . . . 5377 1 124 . 1 1 11 11 ILE HB H 1 2.00 0.01 . 1 . . . . . . . . 5377 1 125 . 1 1 11 11 ILE HG21 H 1 0.83 0.01 . 1 . . . . . . . . 5377 1 126 . 1 1 11 11 ILE HG22 H 1 0.83 0.01 . 1 . . . . . . . . 5377 1 127 . 1 1 11 11 ILE HG23 H 1 0.83 0.01 . 1 . . . . . . . . 5377 1 128 . 1 1 11 11 ILE HD11 H 1 0.72 0.01 . 1 . . . . . . . . 5377 1 129 . 1 1 11 11 ILE HD12 H 1 0.72 0.01 . 1 . . . . . . . . 5377 1 130 . 1 1 11 11 ILE HD13 H 1 0.72 0.01 . 1 . . . . . . . . 5377 1 131 . 1 1 11 11 ILE C C 13 178.13 0.20 . 1 . . . . . . . . 5377 1 132 . 1 1 11 11 ILE CA C 13 65.72 0.20 . 1 . . . . . . . . 5377 1 133 . 1 1 11 11 ILE CB C 13 38.61 0.20 . 1 . . . . . . . . 5377 1 134 . 1 1 11 11 ILE CG2 C 13 18.02 0.20 . 1 . . . . . . . . 5377 1 135 . 1 1 11 11 ILE CD1 C 13 13.12 0.20 . 1 . . . . . . . . 5377 1 136 . 1 1 11 11 ILE N N 15 118.71 0.20 . 1 . . . . . . . . 5377 1 137 . 1 1 12 12 ASP H H 1 8.85 0.01 . 1 . . . . . . . . 5377 1 138 . 1 1 12 12 ASP HA H 1 4.59 0.01 . 1 . . . . . . . . 5377 1 139 . 1 1 12 12 ASP HB2 H 1 2.82 0.01 . 2 . . . . . . . . 5377 1 140 . 1 1 12 12 ASP HB3 H 1 2.95 0.01 . 2 . . . . . . . . 5377 1 141 . 1 1 12 12 ASP C C 13 179.97 0.20 . 1 . . . . . . . . 5377 1 142 . 1 1 12 12 ASP CA C 13 57.84 0.20 . 1 . . . . . . . . 5377 1 143 . 1 1 12 12 ASP CB C 13 40.90 0.20 . 1 . . . . . . . . 5377 1 144 . 1 1 12 12 ASP N N 15 120.39 0.20 . 1 . . . . . . . . 5377 1 145 . 1 1 13 13 VAL H H 1 9.01 0.01 . 1 . . . . . . . . 5377 1 146 . 1 1 13 13 VAL HA H 1 4.06 0.01 . 1 . . . . . . . . 5377 1 147 . 1 1 13 13 VAL HB H 1 2.42 0.01 . 1 . . . . . . . . 5377 1 148 . 1 1 13 13 VAL HG11 H 1 1.36 0.01 . 2 . . . . . . . . 5377 1 149 . 1 1 13 13 VAL HG12 H 1 1.36 0.01 . 2 . . . . . . . . 5377 1 150 . 1 1 13 13 VAL HG13 H 1 1.36 0.01 . 2 . . . . . . . . 5377 1 151 . 1 1 13 13 VAL HG21 H 1 1.37 0.01 . 2 . . . . . . . . 5377 1 152 . 1 1 13 13 VAL HG22 H 1 1.37 0.01 . 2 . . . . . . . . 5377 1 153 . 1 1 13 13 VAL HG23 H 1 1.37 0.01 . 2 . . . . . . . . 5377 1 154 . 1 1 13 13 VAL C C 13 178.19 0.20 . 1 . . . . . . . . 5377 1 155 . 1 1 13 13 VAL CA C 13 66.15 0.20 . 1 . . . . . . . . 5377 1 156 . 1 1 13 13 VAL CB C 13 31.14 0.20 . 1 . . . . . . . . 5377 1 157 . 1 1 13 13 VAL CG1 C 13 23.28 0.20 . 2 . . . . . . . . 5377 1 158 . 1 1 13 13 VAL CG2 C 13 22.11 0.20 . 2 . . . . . . . . 5377 1 159 . 1 1 13 13 VAL N N 15 120.64 0.20 . 1 . . . . . . . . 5377 1 160 . 1 1 14 14 PHE H H 1 7.75 0.01 . 1 . . . . . . . . 5377 1 161 . 1 1 14 14 PHE HA H 1 3.56 0.01 . 1 . . . . . . . . 5377 1 162 . 1 1 14 14 PHE HB2 H 1 2.83 0.01 . 2 . . . . . . . . 5377 1 163 . 1 1 14 14 PHE HB3 H 1 3.22 0.01 . 2 . . . . . . . . 5377 1 164 . 1 1 14 14 PHE HD1 H 1 6.08 0.01 . 1 . . . . . . . . 5377 1 165 . 1 1 14 14 PHE HD2 H 1 6.08 0.01 . 1 . . . . . . . . 5377 1 166 . 1 1 14 14 PHE HE1 H 1 6.98 0.01 . 1 . . . . . . . . 5377 1 167 . 1 1 14 14 PHE HE2 H 1 6.98 0.01 . 1 . . . . . . . . 5377 1 168 . 1 1 14 14 PHE HZ H 1 7.39 0.01 . 1 . . . . . . . . 5377 1 169 . 1 1 14 14 PHE C C 13 177.27 0.20 . 1 . . . . . . . . 5377 1 170 . 1 1 14 14 PHE CA C 13 62.88 0.20 . 1 . . . . . . . . 5377 1 171 . 1 1 14 14 PHE CB C 13 38.72 0.20 . 1 . . . . . . . . 5377 1 172 . 1 1 14 14 PHE CD1 C 13 131.47 0.20 . 1 . . . . . . . . 5377 1 173 . 1 1 14 14 PHE CD2 C 13 131.47 0.20 . 1 . . . . . . . . 5377 1 174 . 1 1 14 14 PHE CE1 C 13 129.78 0.20 . 1 . . . . . . . . 5377 1 175 . 1 1 14 14 PHE CE2 C 13 129.78 0.20 . 1 . . . . . . . . 5377 1 176 . 1 1 14 14 PHE CZ C 13 131.25 0.20 . 1 . . . . . . . . 5377 1 177 . 1 1 14 14 PHE N N 15 120.01 0.20 . 1 . . . . . . . . 5377 1 178 . 1 1 15 15 HIS H H 1 8.24 0.01 . 1 . . . . . . . . 5377 1 179 . 1 1 15 15 HIS HA H 1 4.87 0.01 . 1 . . . . . . . . 5377 1 180 . 1 1 15 15 HIS HB2 H 1 3.20 0.01 . 2 . . . . . . . . 5377 1 181 . 1 1 15 15 HIS HB3 H 1 3.76 0.01 . 2 . . . . . . . . 5377 1 182 . 1 1 15 15 HIS HD2 H 1 7.39 0.01 . 1 . . . . . . . . 5377 1 183 . 1 1 15 15 HIS C C 13 177.98 0.20 . 1 . . . . . . . . 5377 1 184 . 1 1 15 15 HIS CA C 13 58.94 0.20 . 1 . . . . . . . . 5377 1 185 . 1 1 15 15 HIS CB C 13 29.06 0.20 . 1 . . . . . . . . 5377 1 186 . 1 1 15 15 HIS CD2 C 13 123.34 0.20 . 1 . . . . . . . . 5377 1 187 . 1 1 15 15 HIS N N 15 117.45 0.20 . 1 . . . . . . . . 5377 1 188 . 1 1 16 16 GLN H H 1 8.39 0.01 . 1 . . . . . . . . 5377 1 189 . 1 1 16 16 GLN HA H 1 4.02 0.01 . 1 . . . . . . . . 5377 1 190 . 1 1 16 16 GLN HB2 H 1 2.17 0.01 . 2 . . . . . . . . 5377 1 191 . 1 1 16 16 GLN HB3 H 1 2.40 0.01 . 2 . . . . . . . . 5377 1 192 . 1 1 16 16 GLN HG2 H 1 2.20 0.01 . 2 . . . . . . . . 5377 1 193 . 1 1 16 16 GLN HG3 H 1 2.76 0.01 . 2 . . . . . . . . 5377 1 194 . 1 1 16 16 GLN HE21 H 1 6.86 0.01 . 2 . . . . . . . . 5377 1 195 . 1 1 16 16 GLN HE22 H 1 7.21 0.01 . 2 . . . . . . . . 5377 1 196 . 1 1 16 16 GLN C C 13 177.65 0.20 . 1 . . . . . . . . 5377 1 197 . 1 1 16 16 GLN CA C 13 58.38 0.20 . 1 . . . . . . . . 5377 1 198 . 1 1 16 16 GLN CB C 13 28.36 0.20 . 1 . . . . . . . . 5377 1 199 . 1 1 16 16 GLN CG C 13 33.76 0.20 . 1 . . . . . . . . 5377 1 200 . 1 1 16 16 GLN CD C 13 179.72 0.20 . 1 . . . . . . . . 5377 1 201 . 1 1 16 16 GLN N N 15 122.23 0.20 . 1 . . . . . . . . 5377 1 202 . 1 1 16 16 GLN NE2 N 15 111.20 0.20 . 1 . . . . . . . . 5377 1 203 . 1 1 17 17 TYR H H 1 7.29 0.01 . 1 . . . . . . . . 5377 1 204 . 1 1 17 17 TYR HA H 1 4.14 0.01 . 1 . . . . . . . . 5377 1 205 . 1 1 17 17 TYR HB2 H 1 2.51 0.01 . 2 . . . . . . . . 5377 1 206 . 1 1 17 17 TYR HB3 H 1 2.70 0.01 . 2 . . . . . . . . 5377 1 207 . 1 1 17 17 TYR HD1 H 1 7.37 0.01 . 1 . . . . . . . . 5377 1 208 . 1 1 17 17 TYR HD2 H 1 7.37 0.01 . 1 . . . . . . . . 5377 1 209 . 1 1 17 17 TYR HE1 H 1 6.71 0.01 . 1 . . . . . . . . 5377 1 210 . 1 1 17 17 TYR HE2 H 1 6.71 0.01 . 1 . . . . . . . . 5377 1 211 . 1 1 17 17 TYR C C 13 176.30 0.20 . 1 . . . . . . . . 5377 1 212 . 1 1 17 17 TYR CA C 13 60.77 0.20 . 1 . . . . . . . . 5377 1 213 . 1 1 17 17 TYR CB C 13 40.66 0.20 . 1 . . . . . . . . 5377 1 214 . 1 1 17 17 TYR CD1 C 13 133.12 0.20 . 1 . . . . . . . . 5377 1 215 . 1 1 17 17 TYR CD2 C 13 133.12 0.20 . 1 . . . . . . . . 5377 1 216 . 1 1 17 17 TYR CE1 C 13 117.13 0.20 . 1 . . . . . . . . 5377 1 217 . 1 1 17 17 TYR CE2 C 13 117.13 0.20 . 1 . . . . . . . . 5377 1 218 . 1 1 17 17 TYR N N 15 115.89 0.20 . 1 . . . . . . . . 5377 1 219 . 1 1 18 18 SER H H 1 9.03 0.01 . 1 . . . . . . . . 5377 1 220 . 1 1 18 18 SER HA H 1 3.64 0.01 . 1 . . . . . . . . 5377 1 221 . 1 1 18 18 SER HB2 H 1 2.21 0.01 . 2 . . . . . . . . 5377 1 222 . 1 1 18 18 SER HB3 H 1 3.14 0.01 . 2 . . . . . . . . 5377 1 223 . 1 1 18 18 SER C C 13 177.42 0.20 . 1 . . . . . . . . 5377 1 224 . 1 1 18 18 SER CA C 13 61.65 0.20 . 1 . . . . . . . . 5377 1 225 . 1 1 18 18 SER CB C 13 61.08 0.20 . 1 . . . . . . . . 5377 1 226 . 1 1 18 18 SER N N 15 115.90 0.20 . 1 . . . . . . . . 5377 1 227 . 1 1 19 19 GLY H H 1 7.71 0.01 . 1 . . . . . . . . 5377 1 228 . 1 1 19 19 GLY HA2 H 1 3.96 0.01 . 2 . . . . . . . . 5377 1 229 . 1 1 19 19 GLY HA3 H 1 4.14 0.01 . 2 . . . . . . . . 5377 1 230 . 1 1 19 19 GLY C C 13 173.78 0.20 . 1 . . . . . . . . 5377 1 231 . 1 1 19 19 GLY CA C 13 45.24 0.20 . 1 . . . . . . . . 5377 1 232 . 1 1 19 19 GLY N N 15 110.42 0.20 . 1 . . . . . . . . 5377 1 233 . 1 1 20 20 ARG H H 1 7.20 0.01 . 1 . . . . . . . . 5377 1 234 . 1 1 20 20 ARG HA H 1 3.99 0.01 . 1 . . . . . . . . 5377 1 235 . 1 1 20 20 ARG HB2 H 1 2.06 0.01 . 2 . . . . . . . . 5377 1 236 . 1 1 20 20 ARG HB3 H 1 2.23 0.01 . 2 . . . . . . . . 5377 1 237 . 1 1 20 20 ARG HG2 H 1 1.68 0.01 . 2 . . . . . . . . 5377 1 238 . 1 1 20 20 ARG HG3 H 1 1.90 0.01 . 2 . . . . . . . . 5377 1 239 . 1 1 20 20 ARG HD2 H 1 3.22 0.01 . 1 . . . . . . . . 5377 1 240 . 1 1 20 20 ARG HD3 H 1 3.22 0.01 . 1 . . . . . . . . 5377 1 241 . 1 1 20 20 ARG C C 13 177.38 0.20 . 1 . . . . . . . . 5377 1 242 . 1 1 20 20 ARG CA C 13 59.74 0.20 . 1 . . . . . . . . 5377 1 243 . 1 1 20 20 ARG CB C 13 30.75 0.20 . 1 . . . . . . . . 5377 1 244 . 1 1 20 20 ARG CG C 13 30.10 0.20 . 1 . . . . . . . . 5377 1 245 . 1 1 20 20 ARG CD C 13 43.68 0.20 . 1 . . . . . . . . 5377 1 246 . 1 1 20 20 ARG N N 15 121.73 0.20 . 1 . . . . . . . . 5377 1 247 . 1 1 21 21 GLU H H 1 9.48 0.01 . 1 . . . . . . . . 5377 1 248 . 1 1 21 21 GLU HA H 1 4.67 0.01 . 1 . . . . . . . . 5377 1 249 . 1 1 21 21 GLU HB2 H 1 1.75 0.01 . 2 . . . . . . . . 5377 1 250 . 1 1 21 21 GLU HB3 H 1 1.99 0.01 . 2 . . . . . . . . 5377 1 251 . 1 1 21 21 GLU HG2 H 1 2.11 0.01 . 2 . . . . . . . . 5377 1 252 . 1 1 21 21 GLU HG3 H 1 2.22 0.01 . 2 . . . . . . . . 5377 1 253 . 1 1 21 21 GLU CA C 13 54.69 0.20 . 1 . . . . . . . . 5377 1 254 . 1 1 21 21 GLU CB C 13 35.09 0.20 . 1 . . . . . . . . 5377 1 255 . 1 1 21 21 GLU N N 15 116.26 0.20 . 1 . . . . . . . . 5377 1 256 . 1 1 22 22 GLY HA2 H 1 3.83 0.01 . 2 . . . . . . . . 5377 1 257 . 1 1 22 22 GLY HA3 H 1 3.92 0.01 . 2 . . . . . . . . 5377 1 258 . 1 1 22 22 GLY CA C 13 45.96 0.20 . 1 . . . . . . . . 5377 1 259 . 1 1 23 23 ASP HA H 1 4.17 0.01 . 1 . . . . . . . . 5377 1 260 . 1 1 23 23 ASP HB2 H 1 2.85 0.01 . 2 . . . . . . . . 5377 1 261 . 1 1 23 23 ASP HB3 H 1 2.93 0.01 . 2 . . . . . . . . 5377 1 262 . 1 1 23 23 ASP C C 13 176.39 0.20 . 1 . . . . . . . . 5377 1 263 . 1 1 23 23 ASP CA C 13 58.74 0.20 . 1 . . . . . . . . 5377 1 264 . 1 1 23 23 ASP CB C 13 39.65 0.20 . 1 . . . . . . . . 5377 1 265 . 1 1 24 24 LYS H H 1 7.82 0.01 . 1 . . . . . . . . 5377 1 266 . 1 1 24 24 LYS HA H 1 4.43 0.01 . 1 . . . . . . . . 5377 1 267 . 1 1 24 24 LYS HB2 H 1 1.68 0.01 . 2 . . . . . . . . 5377 1 268 . 1 1 24 24 LYS HB3 H 1 1.81 0.01 . 2 . . . . . . . . 5377 1 269 . 1 1 24 24 LYS HG2 H 1 1.38 0.01 . 1 . . . . . . . . 5377 1 270 . 1 1 24 24 LYS HG3 H 1 1.38 0.01 . 1 . . . . . . . . 5377 1 271 . 1 1 24 24 LYS HE2 H 1 3.01 0.01 . 1 . . . . . . . . 5377 1 272 . 1 1 24 24 LYS HE3 H 1 3.01 0.01 . 1 . . . . . . . . 5377 1 273 . 1 1 24 24 LYS C C 13 176.67 0.20 . 1 . . . . . . . . 5377 1 274 . 1 1 24 24 LYS CA C 13 58.24 0.20 . 1 . . . . . . . . 5377 1 275 . 1 1 24 24 LYS CB C 13 31.24 0.20 . 1 . . . . . . . . 5377 1 276 . 1 1 24 24 LYS CG C 13 24.95 0.20 . 1 . . . . . . . . 5377 1 277 . 1 1 24 24 LYS CE C 13 42.41 0.20 . 1 . . . . . . . . 5377 1 278 . 1 1 24 24 LYS N N 15 118.47 0.20 . 1 . . . . . . . . 5377 1 279 . 1 1 25 25 HIS H H 1 9.55 0.01 . 1 . . . . . . . . 5377 1 280 . 1 1 25 25 HIS HA H 1 4.98 0.01 . 1 . . . . . . . . 5377 1 281 . 1 1 25 25 HIS HB2 H 1 3.27 0.01 . 2 . . . . . . . . 5377 1 282 . 1 1 25 25 HIS HB3 H 1 3.62 0.01 . 2 . . . . . . . . 5377 1 283 . 1 1 25 25 HIS HD2 H 1 7.26 0.01 . 1 . . . . . . . . 5377 1 284 . 1 1 25 25 HIS C C 13 173.30 0.20 . 1 . . . . . . . . 5377 1 285 . 1 1 25 25 HIS CA C 13 55.30 0.20 . 1 . . . . . . . . 5377 1 286 . 1 1 25 25 HIS CB C 13 31.13 0.20 . 1 . . . . . . . . 5377 1 287 . 1 1 25 25 HIS CD2 C 13 119.19 0.20 . 1 . . . . . . . . 5377 1 288 . 1 1 25 25 HIS N N 15 118.90 0.20 . 1 . . . . . . . . 5377 1 289 . 1 1 26 26 LYS H H 1 7.16 0.01 . 1 . . . . . . . . 5377 1 290 . 1 1 26 26 LYS HA H 1 5.15 0.01 . 1 . . . . . . . . 5377 1 291 . 1 1 26 26 LYS HB2 H 1 1.62 0.01 . 1 . . . . . . . . 5377 1 292 . 1 1 26 26 LYS HB3 H 1 1.62 0.01 . 1 . . . . . . . . 5377 1 293 . 1 1 26 26 LYS HG2 H 1 1.47 0.01 . 1 . . . . . . . . 5377 1 294 . 1 1 26 26 LYS HG3 H 1 1.47 0.01 . 1 . . . . . . . . 5377 1 295 . 1 1 26 26 LYS HE2 H 1 2.96 0.01 . 1 . . . . . . . . 5377 1 296 . 1 1 26 26 LYS HE3 H 1 2.96 0.01 . 1 . . . . . . . . 5377 1 297 . 1 1 26 26 LYS CA C 13 55.26 0.20 . 1 . . . . . . . . 5377 1 298 . 1 1 26 26 LYS CB C 13 38.91 0.20 . 1 . . . . . . . . 5377 1 299 . 1 1 26 26 LYS CD C 13 31.24 0.20 . 1 . . . . . . . . 5377 1 300 . 1 1 26 26 LYS CE C 13 40.26 0.20 . 1 . . . . . . . . 5377 1 301 . 1 1 26 26 LYS N N 15 115.41 0.20 . 1 . . . . . . . . 5377 1 302 . 1 1 27 27 LEU H H 1 9.64 0.01 . 1 . . . . . . . . 5377 1 303 . 1 1 27 27 LEU HA H 1 5.27 0.01 . 1 . . . . . . . . 5377 1 304 . 1 1 27 27 LEU HB2 H 1 1.18 0.01 . 2 . . . . . . . . 5377 1 305 . 1 1 27 27 LEU HB3 H 1 2.16 0.01 . 2 . . . . . . . . 5377 1 306 . 1 1 27 27 LEU HG H 1 1.26 0.01 . 1 . . . . . . . . 5377 1 307 . 1 1 27 27 LEU HD11 H 1 0.78 0.01 . 2 . . . . . . . . 5377 1 308 . 1 1 27 27 LEU HD12 H 1 0.78 0.01 . 2 . . . . . . . . 5377 1 309 . 1 1 27 27 LEU HD13 H 1 0.78 0.01 . 2 . . . . . . . . 5377 1 310 . 1 1 27 27 LEU HD21 H 1 0.32 0.01 . 2 . . . . . . . . 5377 1 311 . 1 1 27 27 LEU HD22 H 1 0.32 0.01 . 2 . . . . . . . . 5377 1 312 . 1 1 27 27 LEU HD23 H 1 0.32 0.01 . 2 . . . . . . . . 5377 1 313 . 1 1 27 27 LEU C C 13 175.96 0.20 . 1 . . . . . . . . 5377 1 314 . 1 1 27 27 LEU CA C 13 52.45 0.20 . 1 . . . . . . . . 5377 1 315 . 1 1 27 27 LEU CB C 13 43.73 0.20 . 1 . . . . . . . . 5377 1 316 . 1 1 27 27 LEU CG C 13 25.14 0.20 . 1 . . . . . . . . 5377 1 317 . 1 1 27 27 LEU CD1 C 13 29.03 0.20 . 2 . . . . . . . . 5377 1 318 . 1 1 27 27 LEU CD2 C 13 24.79 0.20 . 2 . . . . . . . . 5377 1 319 . 1 1 27 27 LEU N N 15 126.39 0.20 . 1 . . . . . . . . 5377 1 320 . 1 1 28 28 LYS H H 1 9.76 0.01 . 1 . . . . . . . . 5377 1 321 . 1 1 28 28 LYS HA H 1 4.61 0.01 . 1 . . . . . . . . 5377 1 322 . 1 1 28 28 LYS HB2 H 1 2.17 0.01 . 1 . . . . . . . . 5377 1 323 . 1 1 28 28 LYS HB3 H 1 2.17 0.01 . 1 . . . . . . . . 5377 1 324 . 1 1 28 28 LYS HD2 H 1 1.68 0.01 . 1 . . . . . . . . 5377 1 325 . 1 1 28 28 LYS HD3 H 1 1.68 0.01 . 1 . . . . . . . . 5377 1 326 . 1 1 28 28 LYS HE2 H 1 2.96 0.01 . 1 . . . . . . . . 5377 1 327 . 1 1 28 28 LYS HE3 H 1 2.96 0.01 . 1 . . . . . . . . 5377 1 328 . 1 1 28 28 LYS C C 13 177.73 0.20 . 1 . . . . . . . . 5377 1 329 . 1 1 28 28 LYS CA C 13 55.09 0.20 . 1 . . . . . . . . 5377 1 330 . 1 1 28 28 LYS CB C 13 33.14 0.20 . 1 . . . . . . . . 5377 1 331 . 1 1 28 28 LYS CG C 13 24.13 0.20 . 1 . . . . . . . . 5377 1 332 . 1 1 28 28 LYS CE C 13 39.95 0.20 . 1 . . . . . . . . 5377 1 333 . 1 1 28 28 LYS N N 15 124.63 0.20 . 1 . . . . . . . . 5377 1 334 . 1 1 29 29 LYS H H 1 9.09 0.01 . 1 . . . . . . . . 5377 1 335 . 1 1 29 29 LYS HA H 1 4.72 0.01 . 1 . . . . . . . . 5377 1 336 . 1 1 29 29 LYS HB2 H 1 1.82 0.01 . 2 . . . . . . . . 5377 1 337 . 1 1 29 29 LYS HB3 H 1 1.98 0.01 . 2 . . . . . . . . 5377 1 338 . 1 1 29 29 LYS HD2 H 1 1.87 0.01 . 1 . . . . . . . . 5377 1 339 . 1 1 29 29 LYS HD3 H 1 1.87 0.01 . 1 . . . . . . . . 5377 1 340 . 1 1 29 29 LYS HE2 H 1 3.60 0.01 . 1 . . . . . . . . 5377 1 341 . 1 1 29 29 LYS HE3 H 1 3.60 0.01 . 1 . . . . . . . . 5377 1 342 . 1 1 29 29 LYS C C 13 177.70 0.20 . 1 . . . . . . . . 5377 1 343 . 1 1 29 29 LYS CA C 13 62.23 0.20 . 1 . . . . . . . . 5377 1 344 . 1 1 29 29 LYS CB C 13 32.81 0.20 . 1 . . . . . . . . 5377 1 345 . 1 1 29 29 LYS CG C 13 29.23 0.20 . 1 . . . . . . . . 5377 1 346 . 1 1 29 29 LYS CD C 13 31.00 0.20 . 1 . . . . . . . . 5377 1 347 . 1 1 29 29 LYS N N 15 121.44 0.20 . 1 . . . . . . . . 5377 1 348 . 1 1 30 30 SER H H 1 8.14 0.01 . 1 . . . . . . . . 5377 1 349 . 1 1 30 30 SER HA H 1 4.72 0.01 . 1 . . . . . . . . 5377 1 350 . 1 1 30 30 SER HB2 H 1 3.98 0.01 . 1 . . . . . . . . 5377 1 351 . 1 1 30 30 SER HB3 H 1 3.98 0.01 . 1 . . . . . . . . 5377 1 352 . 1 1 30 30 SER C C 13 177.23 0.20 . 1 . . . . . . . . 5377 1 353 . 1 1 30 30 SER CA C 13 61.35 0.20 . 1 . . . . . . . . 5377 1 354 . 1 1 30 30 SER CB C 13 61.35 0.20 . 1 . . . . . . . . 5377 1 355 . 1 1 30 30 SER N N 15 110.41 0.20 . 1 . . . . . . . . 5377 1 356 . 1 1 31 31 GLU H H 1 6.61 0.01 . 1 . . . . . . . . 5377 1 357 . 1 1 31 31 GLU HA H 1 4.25 0.01 . 1 . . . . . . . . 5377 1 358 . 1 1 31 31 GLU HB2 H 1 2.37 0.01 . 1 . . . . . . . . 5377 1 359 . 1 1 31 31 GLU HB3 H 1 2.37 0.01 . 1 . . . . . . . . 5377 1 360 . 1 1 31 31 GLU C C 13 177.72 0.20 . 1 . . . . . . . . 5377 1 361 . 1 1 31 31 GLU CA C 13 58.68 0.20 . 1 . . . . . . . . 5377 1 362 . 1 1 31 31 GLU CB C 13 31.42 0.20 . 1 . . . . . . . . 5377 1 363 . 1 1 31 31 GLU CG C 13 37.14 0.20 . 1 . . . . . . . . 5377 1 364 . 1 1 31 31 GLU N N 15 123.71 0.20 . 1 . . . . . . . . 5377 1 365 . 1 1 32 32 LEU H H 1 8.51 0.01 . 1 . . . . . . . . 5377 1 366 . 1 1 32 32 LEU HA H 1 3.97 0.01 . 1 . . . . . . . . 5377 1 367 . 1 1 32 32 LEU HB2 H 1 1.17 0.01 . 2 . . . . . . . . 5377 1 368 . 1 1 32 32 LEU HB3 H 1 1.94 0.01 . 2 . . . . . . . . 5377 1 369 . 1 1 32 32 LEU HG H 1 1.33 0.01 . 1 . . . . . . . . 5377 1 370 . 1 1 32 32 LEU HD11 H 1 0.86 0.01 . 2 . . . . . . . . 5377 1 371 . 1 1 32 32 LEU HD12 H 1 0.86 0.01 . 2 . . . . . . . . 5377 1 372 . 1 1 32 32 LEU HD13 H 1 0.86 0.01 . 2 . . . . . . . . 5377 1 373 . 1 1 32 32 LEU HD21 H 1 0.66 0.01 . 2 . . . . . . . . 5377 1 374 . 1 1 32 32 LEU HD22 H 1 0.66 0.01 . 2 . . . . . . . . 5377 1 375 . 1 1 32 32 LEU HD23 H 1 0.66 0.01 . 2 . . . . . . . . 5377 1 376 . 1 1 32 32 LEU C C 13 177.39 0.20 . 1 . . . . . . . . 5377 1 377 . 1 1 32 32 LEU CA C 13 57.87 0.20 . 1 . . . . . . . . 5377 1 378 . 1 1 32 32 LEU CB C 13 42.06 0.20 . 1 . . . . . . . . 5377 1 379 . 1 1 32 32 LEU CG C 13 26.56 0.20 . 1 . . . . . . . . 5377 1 380 . 1 1 32 32 LEU CD1 C 13 22.35 0.20 . 2 . . . . . . . . 5377 1 381 . 1 1 32 32 LEU N N 15 120.14 0.20 . 1 . . . . . . . . 5377 1 382 . 1 1 33 33 LYS H H 1 8.36 0.01 . 1 . . . . . . . . 5377 1 383 . 1 1 33 33 LYS HA H 1 3.63 0.01 . 1 . . . . . . . . 5377 1 384 . 1 1 33 33 LYS HB2 H 1 2.35 0.01 . 1 . . . . . . . . 5377 1 385 . 1 1 33 33 LYS HB3 H 1 2.35 0.01 . 1 . . . . . . . . 5377 1 386 . 1 1 33 33 LYS HG2 H 1 1.31 0.01 . 1 . . . . . . . . 5377 1 387 . 1 1 33 33 LYS HG3 H 1 1.31 0.01 . 1 . . . . . . . . 5377 1 388 . 1 1 33 33 LYS HD2 H 1 1.66 0.01 . 1 . . . . . . . . 5377 1 389 . 1 1 33 33 LYS HD3 H 1 1.66 0.01 . 1 . . . . . . . . 5377 1 390 . 1 1 33 33 LYS HE2 H 1 2.78 0.01 . 1 . . . . . . . . 5377 1 391 . 1 1 33 33 LYS HE3 H 1 2.78 0.01 . 1 . . . . . . . . 5377 1 392 . 1 1 33 33 LYS C C 13 177.08 0.20 . 1 . . . . . . . . 5377 1 393 . 1 1 33 33 LYS CA C 13 60.33 0.20 . 1 . . . . . . . . 5377 1 394 . 1 1 33 33 LYS CB C 13 32.38 0.20 . 1 . . . . . . . . 5377 1 395 . 1 1 33 33 LYS CG C 13 25.19 0.20 . 1 . . . . . . . . 5377 1 396 . 1 1 33 33 LYS CD C 13 30.30 0.20 . 1 . . . . . . . . 5377 1 397 . 1 1 33 33 LYS CE C 13 41.70 0.20 . 1 . . . . . . . . 5377 1 398 . 1 1 33 33 LYS N N 15 118.58 0.20 . 1 . . . . . . . . 5377 1 399 . 1 1 34 34 GLU H H 1 7.40 0.01 . 1 . . . . . . . . 5377 1 400 . 1 1 34 34 GLU HA H 1 4.06 0.01 . 1 . . . . . . . . 5377 1 401 . 1 1 34 34 GLU HB3 H 1 2.34 0.01 . 2 . . . . . . . . 5377 1 402 . 1 1 34 34 GLU HG2 H 1 2.47 0.01 . 2 . . . . . . . . 5377 1 403 . 1 1 34 34 GLU HG3 H 1 2.61 0.01 . 2 . . . . . . . . 5377 1 404 . 1 1 34 34 GLU C C 13 177.97 0.20 . 1 . . . . . . . . 5377 1 405 . 1 1 34 34 GLU CA C 13 59.50 0.20 . 1 . . . . . . . . 5377 1 406 . 1 1 34 34 GLU CB C 13 29.37 0.20 . 1 . . . . . . . . 5377 1 407 . 1 1 34 34 GLU CG C 13 36.58 0.20 . 1 . . . . . . . . 5377 1 408 . 1 1 34 34 GLU N N 15 116.70 0.20 . 1 . . . . . . . . 5377 1 409 . 1 1 35 35 LEU H H 1 7.96 0.01 . 1 . . . . . . . . 5377 1 410 . 1 1 35 35 LEU HA H 1 2.65 0.01 . 1 . . . . . . . . 5377 1 411 . 1 1 35 35 LEU HB2 H 1 1.00 0.01 . 2 . . . . . . . . 5377 1 412 . 1 1 35 35 LEU HB3 H 1 1.54 0.01 . 2 . . . . . . . . 5377 1 413 . 1 1 35 35 LEU HG H 1 1.12 0.01 . 1 . . . . . . . . 5377 1 414 . 1 1 35 35 LEU HD11 H 1 0.77 0.01 . 2 . . . . . . . . 5377 1 415 . 1 1 35 35 LEU HD12 H 1 0.77 0.01 . 2 . . . . . . . . 5377 1 416 . 1 1 35 35 LEU HD13 H 1 0.77 0.01 . 2 . . . . . . . . 5377 1 417 . 1 1 35 35 LEU HD21 H 1 0.64 0.01 . 2 . . . . . . . . 5377 1 418 . 1 1 35 35 LEU HD22 H 1 0.64 0.01 . 2 . . . . . . . . 5377 1 419 . 1 1 35 35 LEU HD23 H 1 0.64 0.01 . 2 . . . . . . . . 5377 1 420 . 1 1 35 35 LEU C C 13 179.17 0.20 . 1 . . . . . . . . 5377 1 421 . 1 1 35 35 LEU CA C 13 59.39 0.20 . 1 . . . . . . . . 5377 1 422 . 1 1 35 35 LEU CB C 13 41.97 0.20 . 1 . . . . . . . . 5377 1 423 . 1 1 35 35 LEU CG C 13 27.95 0.20 . 1 . . . . . . . . 5377 1 424 . 1 1 35 35 LEU CD1 C 13 24.23 0.20 . 2 . . . . . . . . 5377 1 425 . 1 1 35 35 LEU CD2 C 13 28.15 0.20 . 2 . . . . . . . . 5377 1 426 . 1 1 35 35 LEU N N 15 123.68 0.20 . 1 . . . . . . . . 5377 1 427 . 1 1 36 36 ILE H H 1 8.39 0.01 . 1 . . . . . . . . 5377 1 428 . 1 1 36 36 ILE HA H 1 3.45 0.01 . 1 . . . . . . . . 5377 1 429 . 1 1 36 36 ILE HB H 1 1.87 0.01 . 1 . . . . . . . . 5377 1 430 . 1 1 36 36 ILE HG12 H 1 1.92 0.01 . 1 . . . . . . . . 5377 1 431 . 1 1 36 36 ILE HG13 H 1 1.92 0.01 . 1 . . . . . . . . 5377 1 432 . 1 1 36 36 ILE HG21 H 1 1.23 0.01 . 1 . . . . . . . . 5377 1 433 . 1 1 36 36 ILE HG22 H 1 1.23 0.01 . 1 . . . . . . . . 5377 1 434 . 1 1 36 36 ILE HG23 H 1 1.23 0.01 . 1 . . . . . . . . 5377 1 435 . 1 1 36 36 ILE HD11 H 1 0.74 0.01 . 1 . . . . . . . . 5377 1 436 . 1 1 36 36 ILE HD12 H 1 0.74 0.01 . 1 . . . . . . . . 5377 1 437 . 1 1 36 36 ILE HD13 H 1 0.74 0.01 . 1 . . . . . . . . 5377 1 438 . 1 1 36 36 ILE C C 13 178.35 0.20 . 1 . . . . . . . . 5377 1 439 . 1 1 36 36 ILE CA C 13 66.10 0.20 . 1 . . . . . . . . 5377 1 440 . 1 1 36 36 ILE CB C 13 38.48 0.20 . 1 . . . . . . . . 5377 1 441 . 1 1 36 36 ILE CG1 C 13 30.30 0.20 . 1 . . . . . . . . 5377 1 442 . 1 1 36 36 ILE CG2 C 13 17.76 0.20 . 1 . . . . . . . . 5377 1 443 . 1 1 36 36 ILE CD1 C 13 11.85 0.20 . 1 . . . . . . . . 5377 1 444 . 1 1 36 36 ILE N N 15 120.90 0.20 . 1 . . . . . . . . 5377 1 445 . 1 1 37 37 ASN H H 1 8.46 0.01 . 1 . . . . . . . . 5377 1 446 . 1 1 37 37 ASN HA H 1 4.72 0.01 . 1 . . . . . . . . 5377 1 447 . 1 1 37 37 ASN HB2 H 1 2.87 0.01 . 1 . . . . . . . . 5377 1 448 . 1 1 37 37 ASN HB3 H 1 2.87 0.01 . 1 . . . . . . . . 5377 1 449 . 1 1 37 37 ASN HD21 H 1 7.15 0.01 . 2 . . . . . . . . 5377 1 450 . 1 1 37 37 ASN HD22 H 1 7.53 0.01 . 2 . . . . . . . . 5377 1 451 . 1 1 37 37 ASN C C 13 177.51 0.20 . 1 . . . . . . . . 5377 1 452 . 1 1 37 37 ASN CA C 13 54.68 0.20 . 1 . . . . . . . . 5377 1 453 . 1 1 37 37 ASN CB C 13 37.31 0.20 . 1 . . . . . . . . 5377 1 454 . 1 1 37 37 ASN CG C 13 175.34 0.20 . 1 . . . . . . . . 5377 1 455 . 1 1 37 37 ASN N N 15 117.60 0.20 . 1 . . . . . . . . 5377 1 456 . 1 1 37 37 ASN ND2 N 15 107.05 0.20 . 1 . . . . . . . . 5377 1 457 . 1 1 38 38 ASN H H 1 8.28 0.01 . 1 . . . . . . . . 5377 1 458 . 1 1 38 38 ASN HA H 1 4.92 0.01 . 1 . . . . . . . . 5377 1 459 . 1 1 38 38 ASN HB2 H 1 2.84 0.01 . 2 . . . . . . . . 5377 1 460 . 1 1 38 38 ASN HB3 H 1 3.34 0.01 . 2 . . . . . . . . 5377 1 461 . 1 1 38 38 ASN HD21 H 1 7.18 0.01 . 2 . . . . . . . . 5377 1 462 . 1 1 38 38 ASN HD22 H 1 8.09 0.01 . 2 . . . . . . . . 5377 1 463 . 1 1 38 38 ASN C C 13 177.12 0.20 . 1 . . . . . . . . 5377 1 464 . 1 1 38 38 ASN CA C 13 54.97 0.20 . 1 . . . . . . . . 5377 1 465 . 1 1 38 38 ASN CB C 13 40.37 0.20 . 1 . . . . . . . . 5377 1 466 . 1 1 38 38 ASN CG C 13 177.51 0.20 . 1 . . . . . . . . 5377 1 467 . 1 1 38 38 ASN N N 15 115.05 0.20 . 1 . . . . . . . . 5377 1 468 . 1 1 38 38 ASN ND2 N 15 113.97 0.20 . 1 . . . . . . . . 5377 1 469 . 1 1 39 39 GLU H H 1 8.56 0.01 . 1 . . . . . . . . 5377 1 470 . 1 1 39 39 GLU HA H 1 5.12 0.01 . 1 . . . . . . . . 5377 1 471 . 1 1 39 39 GLU HB2 H 1 1.96 0.01 . 1 . . . . . . . . 5377 1 472 . 1 1 39 39 GLU HB3 H 1 1.96 0.01 . 1 . . . . . . . . 5377 1 473 . 1 1 39 39 GLU HG2 H 1 2.54 0.01 . 2 . . . . . . . . 5377 1 474 . 1 1 39 39 GLU HG3 H 1 2.63 0.01 . 2 . . . . . . . . 5377 1 475 . 1 1 39 39 GLU C C 13 177.263 0.20 . 1 . . . . . . . . 5377 1 476 . 1 1 39 39 GLU CA C 13 55.20 0.20 . 1 . . . . . . . . 5377 1 477 . 1 1 39 39 GLU CB C 13 30.74 0.20 . 1 . . . . . . . . 5377 1 478 . 1 1 39 39 GLU CG C 13 35.14 0.20 . 1 . . . . . . . . 5377 1 479 . 1 1 39 39 GLU N N 15 114.02 0.20 . 1 . . . . . . . . 5377 1 480 . 1 1 40 40 LEU H H 1 7.74 0.01 . 1 . . . . . . . . 5377 1 481 . 1 1 40 40 LEU HA H 1 5.40 0.01 . 1 . . . . . . . . 5377 1 482 . 1 1 40 40 LEU HB2 H 1 2.14 0.01 . 1 . . . . . . . . 5377 1 483 . 1 1 40 40 LEU HB3 H 1 2.14 0.01 . 1 . . . . . . . . 5377 1 484 . 1 1 40 40 LEU HG H 1 1.65 0.01 . 1 . . . . . . . . 5377 1 485 . 1 1 40 40 LEU HD11 H 1 1.04 0.01 . 2 . . . . . . . . 5377 1 486 . 1 1 40 40 LEU HD12 H 1 1.04 0.01 . 2 . . . . . . . . 5377 1 487 . 1 1 40 40 LEU HD13 H 1 1.04 0.01 . 2 . . . . . . . . 5377 1 488 . 1 1 40 40 LEU HD21 H 1 0.94 0.01 . 2 . . . . . . . . 5377 1 489 . 1 1 40 40 LEU HD22 H 1 0.94 0.01 . 2 . . . . . . . . 5377 1 490 . 1 1 40 40 LEU HD23 H 1 0.94 0.01 . 2 . . . . . . . . 5377 1 491 . 1 1 40 40 LEU C C 13 177.41 0.20 . 1 . . . . . . . . 5377 1 492 . 1 1 40 40 LEU CA C 13 54.22 0.20 . 1 . . . . . . . . 5377 1 493 . 1 1 40 40 LEU CB C 13 42.09 0.20 . 1 . . . . . . . . 5377 1 494 . 1 1 40 40 LEU CG C 13 26.72 0.20 . 1 . . . . . . . . 5377 1 495 . 1 1 40 40 LEU CD1 C 13 25.22 0.20 . 2 . . . . . . . . 5377 1 496 . 1 1 40 40 LEU N N 15 120.49 0.20 . 1 . . . . . . . . 5377 1 497 . 1 1 41 41 SER H H 1 7.33 0.01 . 1 . . . . . . . . 5377 1 498 . 1 1 41 41 SER HA H 1 4.59 0.01 . 1 . . . . . . . . 5377 1 499 . 1 1 41 41 SER HB2 H 1 3.90 0.01 . 1 . . . . . . . . 5377 1 500 . 1 1 41 41 SER HB3 H 1 3.90 0.01 . 1 . . . . . . . . 5377 1 501 . 1 1 41 41 SER C C 13 175.75 0.20 . 1 . . . . . . . . 5377 1 502 . 1 1 41 41 SER CA C 13 60.10 0.20 . 1 . . . . . . . . 5377 1 503 . 1 1 41 41 SER CB C 13 63.96 0.20 . 1 . . . . . . . . 5377 1 504 . 1 1 41 41 SER N N 15 113.44 0.20 . 1 . . . . . . . . 5377 1 505 . 1 1 42 42 HIS H H 1 9.94 0.01 . 1 . . . . . . . . 5377 1 506 . 1 1 42 42 HIS HA H 1 4.45 0.01 . 1 . . . . . . . . 5377 1 507 . 1 1 42 42 HIS HB2 H 1 2.88 0.01 . 2 . . . . . . . . 5377 1 508 . 1 1 42 42 HIS HB3 H 1 3.22 0.01 . 2 . . . . . . . . 5377 1 509 . 1 1 42 42 HIS HD2 H 1 7.14 0.01 . 1 . . . . . . . . 5377 1 510 . 1 1 42 42 HIS C C 13 175.78 0.20 . 1 . . . . . . . . 5377 1 511 . 1 1 42 42 HIS CA C 13 58.58 0.20 . 1 . . . . . . . . 5377 1 512 . 1 1 42 42 HIS CB C 13 27.42 0.20 . 1 . . . . . . . . 5377 1 513 . 1 1 42 42 HIS CD2 C 13 119.58 0.20 . 1 . . . . . . . . 5377 1 514 . 1 1 42 42 HIS N N 15 119.45 0.20 . 1 . . . . . . . . 5377 1 515 . 1 1 43 43 PHE H H 1 7.87 0.01 . 1 . . . . . . . . 5377 1 516 . 1 1 43 43 PHE HB2 H 1 2.88 0.01 . 2 . . . . . . . . 5377 1 517 . 1 1 43 43 PHE HB3 H 1 3.27 0.01 . 2 . . . . . . . . 5377 1 518 . 1 1 43 43 PHE C C 13 174.70 0.20 . 1 . . . . . . . . 5377 1 519 . 1 1 43 43 PHE CA C 13 57.62 0.20 . 1 . . . . . . . . 5377 1 520 . 1 1 43 43 PHE CB C 13 39.34 0.20 . 1 . . . . . . . . 5377 1 521 . 1 1 43 43 PHE N N 15 118.38 0.20 . 1 . . . . . . . . 5377 1 522 . 1 1 44 44 LEU H H 1 8.34 0.01 . 1 . . . . . . . . 5377 1 523 . 1 1 44 44 LEU HA H 1 5.08 0.01 . 1 . . . . . . . . 5377 1 524 . 1 1 44 44 LEU HB2 H 1 1.57 0.01 . 1 . . . . . . . . 5377 1 525 . 1 1 44 44 LEU HB3 H 1 1.57 0.01 . 1 . . . . . . . . 5377 1 526 . 1 1 44 44 LEU HG H 1 1.72 0.01 . 1 . . . . . . . . 5377 1 527 . 1 1 44 44 LEU HD11 H 1 0.93 0.01 . 2 . . . . . . . . 5377 1 528 . 1 1 44 44 LEU HD12 H 1 0.93 0.01 . 2 . . . . . . . . 5377 1 529 . 1 1 44 44 LEU HD13 H 1 0.93 0.01 . 2 . . . . . . . . 5377 1 530 . 1 1 44 44 LEU HD21 H 1 0.99 0.01 . 2 . . . . . . . . 5377 1 531 . 1 1 44 44 LEU HD22 H 1 0.99 0.01 . 2 . . . . . . . . 5377 1 532 . 1 1 44 44 LEU HD23 H 1 0.99 0.01 . 2 . . . . . . . . 5377 1 533 . 1 1 44 44 LEU C C 13 176.31 0.20 . 1 . . . . . . . . 5377 1 534 . 1 1 44 44 LEU CA C 13 52.97 0.20 . 1 . . . . . . . . 5377 1 535 . 1 1 44 44 LEU CB C 13 44.54 0.20 . 1 . . . . . . . . 5377 1 536 . 1 1 44 44 LEU CG C 13 27.51 0.20 . 1 . . . . . . . . 5377 1 537 . 1 1 44 44 LEU CD1 C 13 23.73 0.20 . 2 . . . . . . . . 5377 1 538 . 1 1 44 44 LEU CD2 C 13 17.98 0.20 . 2 . . . . . . . . 5377 1 539 . 1 1 44 44 LEU N N 15 119.00 0.20 . 1 . . . . . . . . 5377 1 540 . 1 1 45 45 GLU H H 1 8.27 0.01 . 1 . . . . . . . . 5377 1 541 . 1 1 45 45 GLU HA H 1 4.07 0.01 . 1 . . . . . . . . 5377 1 542 . 1 1 45 45 GLU HB2 H 1 1.84 0.01 . 2 . . . . . . . . 5377 1 543 . 1 1 45 45 GLU HB3 H 1 2.00 0.01 . 2 . . . . . . . . 5377 1 544 . 1 1 45 45 GLU HG2 H 1 2.01 0.01 . 2 . . . . . . . . 5377 1 545 . 1 1 45 45 GLU HG3 H 1 2.38 0.01 . 2 . . . . . . . . 5377 1 546 . 1 1 45 45 GLU C C 13 175.56 0.20 . 1 . . . . . . . . 5377 1 547 . 1 1 45 45 GLU CA C 13 56.45 0.20 . 1 . . . . . . . . 5377 1 548 . 1 1 45 45 GLU CB C 13 30.57 0.20 . 1 . . . . . . . . 5377 1 549 . 1 1 45 45 GLU CG C 13 36.62 0.20 . 1 . . . . . . . . 5377 1 550 . 1 1 45 45 GLU N N 15 121.03 0.20 . 1 . . . . . . . . 5377 1 551 . 1 1 46 46 GLU H H 1 8.26 0.01 . 1 . . . . . . . . 5377 1 552 . 1 1 46 46 GLU HA H 1 4.27 0.01 . 1 . . . . . . . . 5377 1 553 . 1 1 46 46 GLU HB2 H 1 2.12 0.01 . 1 . . . . . . . . 5377 1 554 . 1 1 46 46 GLU HB3 H 1 2.12 0.01 . 1 . . . . . . . . 5377 1 555 . 1 1 46 46 GLU C C 13 177.26 0.20 . 1 . . . . . . . . 5377 1 556 . 1 1 46 46 GLU CA C 13 56.61 0.20 . 1 . . . . . . . . 5377 1 557 . 1 1 46 46 GLU CB C 13 30.85 0.20 . 1 . . . . . . . . 5377 1 558 . 1 1 46 46 GLU N N 15 123.21 0.20 . 1 . . . . . . . . 5377 1 559 . 1 1 47 47 ILE H H 1 9.84 0.01 . 1 . . . . . . . . 5377 1 560 . 1 1 47 47 ILE HA H 1 4.08 0.01 . 1 . . . . . . . . 5377 1 561 . 1 1 47 47 ILE HB H 1 1.74 0.01 . 1 . . . . . . . . 5377 1 562 . 1 1 47 47 ILE HG21 H 1 0.74 0.01 . 1 . . . . . . . . 5377 1 563 . 1 1 47 47 ILE HG22 H 1 0.74 0.01 . 1 . . . . . . . . 5377 1 564 . 1 1 47 47 ILE HG23 H 1 0.74 0.01 . 1 . . . . . . . . 5377 1 565 . 1 1 47 47 ILE C C 13 176.36 0.20 . 1 . . . . . . . . 5377 1 566 . 1 1 47 47 ILE CA C 13 62.24 0.20 . 1 . . . . . . . . 5377 1 567 . 1 1 47 47 ILE CB C 13 38.22 0.20 . 1 . . . . . . . . 5377 1 568 . 1 1 47 47 ILE CG1 C 13 27.78 0.20 . 1 . . . . . . . . 5377 1 569 . 1 1 47 47 ILE CG2 C 13 18.77 0.20 . 1 . . . . . . . . 5377 1 570 . 1 1 47 47 ILE N N 15 126.11 0.20 . 1 . . . . . . . . 5377 1 571 . 1 1 48 48 LYS H H 1 8.95 0.01 . 1 . . . . . . . . 5377 1 572 . 1 1 48 48 LYS HA H 1 4.55 0.01 . 1 . . . . . . . . 5377 1 573 . 1 1 48 48 LYS HB2 H 1 1.83 0.01 . 1 . . . . . . . . 5377 1 574 . 1 1 48 48 LYS HB3 H 1 1.83 0.01 . 1 . . . . . . . . 5377 1 575 . 1 1 48 48 LYS HG2 H 1 1.45 0.01 . 1 . . . . . . . . 5377 1 576 . 1 1 48 48 LYS HG3 H 1 1.45 0.01 . 1 . . . . . . . . 5377 1 577 . 1 1 48 48 LYS HE2 H 1 3.00 0.01 . 2 . . . . . . . . 5377 1 578 . 1 1 48 48 LYS HE3 H 1 3.71 0.01 . 2 . . . . . . . . 5377 1 579 . 1 1 48 48 LYS C C 13 176.12 0.20 . 1 . . . . . . . . 5377 1 580 . 1 1 48 48 LYS CA C 13 56.37 0.20 . 1 . . . . . . . . 5377 1 581 . 1 1 48 48 LYS CB C 13 34.36 0.20 . 1 . . . . . . . . 5377 1 582 . 1 1 48 48 LYS CG C 13 25.06 0.20 . 1 . . . . . . . . 5377 1 583 . 1 1 48 48 LYS CD C 13 29.32 0.20 . 1 . . . . . . . . 5377 1 584 . 1 1 48 48 LYS CE C 13 42.11 0.20 . 1 . . . . . . . . 5377 1 585 . 1 1 48 48 LYS N N 15 127.40 0.20 . 1 . . . . . . . . 5377 1 586 . 1 1 49 49 GLU H H 1 7.62 0.01 . 1 . . . . . . . . 5377 1 587 . 1 1 49 49 GLU HA H 1 4.65 0.01 . 1 . . . . . . . . 5377 1 588 . 1 1 49 49 GLU HB2 H 1 1.99 0.01 . 2 . . . . . . . . 5377 1 589 . 1 1 49 49 GLU HB3 H 1 2.33 0.01 . 2 . . . . . . . . 5377 1 590 . 1 1 49 49 GLU HG2 H 1 2.32 0.01 . 1 . . . . . . . . 5377 1 591 . 1 1 49 49 GLU HG3 H 1 2.32 0.01 . 1 . . . . . . . . 5377 1 592 . 1 1 49 49 GLU C C 13 176.73 0.20 . 1 . . . . . . . . 5377 1 593 . 1 1 49 49 GLU CA C 13 55.45 0.20 . 1 . . . . . . . . 5377 1 594 . 1 1 49 49 GLU CB C 13 31.25 0.20 . 1 . . . . . . . . 5377 1 595 . 1 1 49 49 GLU CG C 13 34.63 0.20 . 1 . . . . . . . . 5377 1 596 . 1 1 49 49 GLU N N 15 119.19 0.20 . 1 . . . . . . . . 5377 1 597 . 1 1 50 50 GLN H H 1 8.91 0.01 . 1 . . . . . . . . 5377 1 598 . 1 1 50 50 GLN HA H 1 3.77 0.01 . 1 . . . . . . . . 5377 1 599 . 1 1 50 50 GLN HB2 H 1 2.31 0.01 . 2 . . . . . . . . 5377 1 600 . 1 1 50 50 GLN HB3 H 1 2.49 0.01 . 2 . . . . . . . . 5377 1 601 . 1 1 50 50 GLN HG2 H 1 1.99 0.01 . 2 . . . . . . . . 5377 1 602 . 1 1 50 50 GLN HG3 H 1 2.24 0.01 . 2 . . . . . . . . 5377 1 603 . 1 1 50 50 GLN HE21 H 1 6.52 0.01 . 2 . . . . . . . . 5377 1 604 . 1 1 50 50 GLN HE22 H 1 8.04 0.01 . 2 . . . . . . . . 5377 1 605 . 1 1 50 50 GLN C C 13 177.05 0.20 . 1 . . . . . . . . 5377 1 606 . 1 1 50 50 GLN CA C 13 58.24 0.20 . 1 . . . . . . . . 5377 1 607 . 1 1 50 50 GLN CB C 13 28.23 0.20 . 1 . . . . . . . . 5377 1 608 . 1 1 50 50 GLN CG C 13 28.50 0.20 . 1 . . . . . . . . 5377 1 609 . 1 1 50 50 GLN CD C 13 180.44 0.20 . 1 . . . . . . . . 5377 1 610 . 1 1 50 50 GLN N N 15 125.45 0.20 . 1 . . . . . . . . 5377 1 611 . 1 1 50 50 GLN NE2 N 15 113.90 0.20 . 1 . . . . . . . . 5377 1 612 . 1 1 51 51 GLU H H 1 9.31 0.01 . 1 . . . . . . . . 5377 1 613 . 1 1 51 51 GLU HA H 1 4.17 0.01 . 1 . . . . . . . . 5377 1 614 . 1 1 51 51 GLU HB2 H 1 2.02 0.01 . 2 . . . . . . . . 5377 1 615 . 1 1 51 51 GLU HB3 H 1 2.11 0.01 . 2 . . . . . . . . 5377 1 616 . 1 1 51 51 GLU HG2 H 1 2.37 0.01 . 1 . . . . . . . . 5377 1 617 . 1 1 51 51 GLU HG3 H 1 2.37 0.01 . 1 . . . . . . . . 5377 1 618 . 1 1 51 51 GLU C C 13 178.68 0.20 . 1 . . . . . . . . 5377 1 619 . 1 1 51 51 GLU CA C 13 59.51 0.20 . 1 . . . . . . . . 5377 1 620 . 1 1 51 51 GLU CB C 13 28.94 0.20 . 1 . . . . . . . . 5377 1 621 . 1 1 51 51 GLU CG C 13 36.57 0.20 . 1 . . . . . . . . 5377 1 622 . 1 1 51 51 GLU N N 15 116.77 0.20 . 1 . . . . . . . . 5377 1 623 . 1 1 52 52 VAL H H 1 7.18 0.01 . 1 . . . . . . . . 5377 1 624 . 1 1 52 52 VAL HA H 1 3.59 0.01 . 1 . . . . . . . . 5377 1 625 . 1 1 52 52 VAL HB H 1 1.98 0.01 . 1 . . . . . . . . 5377 1 626 . 1 1 52 52 VAL HG11 H 1 0.97 0.01 . 2 . . . . . . . . 5377 1 627 . 1 1 52 52 VAL HG12 H 1 0.97 0.01 . 2 . . . . . . . . 5377 1 628 . 1 1 52 52 VAL HG13 H 1 0.97 0.01 . 2 . . . . . . . . 5377 1 629 . 1 1 52 52 VAL HG21 H 1 0.35 0.01 . 2 . . . . . . . . 5377 1 630 . 1 1 52 52 VAL HG22 H 1 0.35 0.01 . 2 . . . . . . . . 5377 1 631 . 1 1 52 52 VAL HG23 H 1 0.35 0.01 . 2 . . . . . . . . 5377 1 632 . 1 1 52 52 VAL C C 13 177.28 0.20 . 1 . . . . . . . . 5377 1 633 . 1 1 52 52 VAL CA C 13 66.14 0.20 . 1 . . . . . . . . 5377 1 634 . 1 1 52 52 VAL CB C 13 31.35 0.20 . 1 . . . . . . . . 5377 1 635 . 1 1 52 52 VAL CG1 C 13 22.46 0.20 . 2 . . . . . . . . 5377 1 636 . 1 1 52 52 VAL CG2 C 13 20.27 0.20 . 2 . . . . . . . . 5377 1 637 . 1 1 52 52 VAL N N 15 118.62 0.20 . 1 . . . . . . . . 5377 1 638 . 1 1 53 53 VAL H H 1 7.00 0.01 . 1 . . . . . . . . 5377 1 639 . 1 1 53 53 VAL HA H 1 3.37 0.01 . 1 . . . . . . . . 5377 1 640 . 1 1 53 53 VAL HB H 1 2.11 0.01 . 1 . . . . . . . . 5377 1 641 . 1 1 53 53 VAL HG11 H 1 0.91 0.01 . 2 . . . . . . . . 5377 1 642 . 1 1 53 53 VAL HG12 H 1 0.91 0.01 . 2 . . . . . . . . 5377 1 643 . 1 1 53 53 VAL HG13 H 1 0.91 0.01 . 2 . . . . . . . . 5377 1 644 . 1 1 53 53 VAL HG21 H 1 0.95 0.01 . 2 . . . . . . . . 5377 1 645 . 1 1 53 53 VAL HG22 H 1 0.95 0.01 . 2 . . . . . . . . 5377 1 646 . 1 1 53 53 VAL HG23 H 1 0.95 0.01 . 2 . . . . . . . . 5377 1 647 . 1 1 53 53 VAL C C 13 177.28 0.20 . 1 . . . . . . . . 5377 1 648 . 1 1 53 53 VAL CA C 13 66.20 0.20 . 1 . . . . . . . . 5377 1 649 . 1 1 53 53 VAL CB C 13 31.30 0.20 . 1 . . . . . . . . 5377 1 650 . 1 1 53 53 VAL CG1 C 13 18.48 0.20 . 2 . . . . . . . . 5377 1 651 . 1 1 53 53 VAL CG2 C 13 18.51 0.20 . 2 . . . . . . . . 5377 1 652 . 1 1 53 53 VAL N N 15 119.35 0.20 . 1 . . . . . . . . 5377 1 653 . 1 1 54 54 ASP H H 1 8.38 0.01 . 1 . . . . . . . . 5377 1 654 . 1 1 54 54 ASP HA H 1 4.17 0.01 . 1 . . . . . . . . 5377 1 655 . 1 1 54 54 ASP HB2 H 1 2.79 0.01 . 2 . . . . . . . . 5377 1 656 . 1 1 54 54 ASP HB3 H 1 2.87 0.01 . 2 . . . . . . . . 5377 1 657 . 1 1 54 54 ASP C C 13 178.55 0.20 . 1 . . . . . . . . 5377 1 658 . 1 1 54 54 ASP CA C 13 57.90 0.20 . 1 . . . . . . . . 5377 1 659 . 1 1 54 54 ASP CB C 13 39.56 0.20 . 1 . . . . . . . . 5377 1 660 . 1 1 54 54 ASP N N 15 120.93 0.20 . 1 . . . . . . . . 5377 1 661 . 1 1 55 55 LYS H H 1 7.62 0.01 . 1 . . . . . . . . 5377 1 662 . 1 1 55 55 LYS HA H 1 4.17 0.01 . 1 . . . . . . . . 5377 1 663 . 1 1 55 55 LYS HB2 H 1 1.98 0.01 . 1 . . . . . . . . 5377 1 664 . 1 1 55 55 LYS HB3 H 1 1.98 0.01 . 1 . . . . . . . . 5377 1 665 . 1 1 55 55 LYS HG2 H 1 1.54 0.01 . 1 . . . . . . . . 5377 1 666 . 1 1 55 55 LYS HG3 H 1 1.54 0.01 . 1 . . . . . . . . 5377 1 667 . 1 1 55 55 LYS HD2 H 1 1.63 0.01 . 1 . . . . . . . . 5377 1 668 . 1 1 55 55 LYS HD3 H 1 1.63 0.01 . 1 . . . . . . . . 5377 1 669 . 1 1 55 55 LYS HE2 H 1 3.06 0.01 . 2 . . . . . . . . 5377 1 670 . 1 1 55 55 LYS HE3 H 1 3.15 0.01 . 2 . . . . . . . . 5377 1 671 . 1 1 55 55 LYS C C 13 179.65 0.20 . 1 . . . . . . . . 5377 1 672 . 1 1 55 55 LYS CA C 13 58.63 0.20 . 1 . . . . . . . . 5377 1 673 . 1 1 55 55 LYS CB C 13 32.32 0.20 . 1 . . . . . . . . 5377 1 674 . 1 1 55 55 LYS CG C 13 25.41 0.20 . 1 . . . . . . . . 5377 1 675 . 1 1 55 55 LYS CD C 13 28.90 0.20 . 1 . . . . . . . . 5377 1 676 . 1 1 55 55 LYS CE C 13 42.40 0.20 . 1 . . . . . . . . 5377 1 677 . 1 1 55 55 LYS N N 15 121.37 0.20 . 1 . . . . . . . . 5377 1 678 . 1 1 56 56 VAL H H 1 8.50 0.01 . 1 . . . . . . . . 5377 1 679 . 1 1 56 56 VAL HA H 1 3.52 0.01 . 1 . . . . . . . . 5377 1 680 . 1 1 56 56 VAL HB H 1 1.95 0.01 . 1 . . . . . . . . 5377 1 681 . 1 1 56 56 VAL HG11 H 1 0.97 0.01 . 2 . . . . . . . . 5377 1 682 . 1 1 56 56 VAL HG12 H 1 0.97 0.01 . 2 . . . . . . . . 5377 1 683 . 1 1 56 56 VAL HG13 H 1 0.97 0.01 . 2 . . . . . . . . 5377 1 684 . 1 1 56 56 VAL HG21 H 1 0.74 0.01 . 2 . . . . . . . . 5377 1 685 . 1 1 56 56 VAL HG22 H 1 0.74 0.01 . 2 . . . . . . . . 5377 1 686 . 1 1 56 56 VAL HG23 H 1 0.74 0.01 . 2 . . . . . . . . 5377 1 687 . 1 1 56 56 VAL C C 13 177.77 0.20 . 1 . . . . . . . . 5377 1 688 . 1 1 56 56 VAL CA C 13 67.11 0.20 . 1 . . . . . . . . 5377 1 689 . 1 1 56 56 VAL CB C 13 31.57 0.20 . 1 . . . . . . . . 5377 1 690 . 1 1 56 56 VAL CG1 C 13 22.48 0.20 . 2 . . . . . . . . 5377 1 691 . 1 1 56 56 VAL CG2 C 13 21.92 0.20 . 2 . . . . . . . . 5377 1 692 . 1 1 56 56 VAL N N 15 122.31 0.20 . 1 . . . . . . . . 5377 1 693 . 1 1 57 57 MET H H 1 8.35 0.01 . 1 . . . . . . . . 5377 1 694 . 1 1 57 57 MET HA H 1 4.28 0.01 . 1 . . . . . . . . 5377 1 695 . 1 1 57 57 MET HB2 H 1 2.05 0.01 . 1 . . . . . . . . 5377 1 696 . 1 1 57 57 MET HB3 H 1 2.05 0.01 . 1 . . . . . . . . 5377 1 697 . 1 1 57 57 MET HG2 H 1 2.43 0.01 . 1 . . . . . . . . 5377 1 698 . 1 1 57 57 MET HG3 H 1 2.43 0.01 . 1 . . . . . . . . 5377 1 699 . 1 1 57 57 MET HE1 H 1 1.93 0.01 . 1 . . . . . . . . 5377 1 700 . 1 1 57 57 MET HE2 H 1 1.93 0.01 . 1 . . . . . . . . 5377 1 701 . 1 1 57 57 MET HE3 H 1 1.93 0.01 . 1 . . . . . . . . 5377 1 702 . 1 1 57 57 MET CA C 13 57.62 0.20 . 1 . . . . . . . . 5377 1 703 . 1 1 57 57 MET CB C 13 30.73 0.20 . 1 . . . . . . . . 5377 1 704 . 1 1 57 57 MET CG C 13 32.02 0.20 . 1 . . . . . . . . 5377 1 705 . 1 1 57 57 MET CE C 13 18.00 0.20 . 1 . . . . . . . . 5377 1 706 . 1 1 57 57 MET N N 15 118.05 0.20 . 1 . . . . . . . . 5377 1 707 . 1 1 58 58 GLU H H 1 8.18 0.01 . 1 . . . . . . . . 5377 1 708 . 1 1 58 58 GLU HA H 1 4.08 0.01 . 1 . . . . . . . . 5377 1 709 . 1 1 58 58 GLU HB2 H 1 2.19 0.01 . 1 . . . . . . . . 5377 1 710 . 1 1 58 58 GLU HB3 H 1 2.19 0.01 . 1 . . . . . . . . 5377 1 711 . 1 1 58 58 GLU HG2 H 1 2.35 0.01 . 2 . . . . . . . . 5377 1 712 . 1 1 58 58 GLU HG3 H 1 2.47 0.01 . 2 . . . . . . . . 5377 1 713 . 1 1 58 58 GLU C C 13 178.70 0.20 . 1 . . . . . . . . 5377 1 714 . 1 1 58 58 GLU CA C 13 58.88 0.20 . 1 . . . . . . . . 5377 1 715 . 1 1 58 58 GLU CB C 13 29.90 0.20 . 1 . . . . . . . . 5377 1 716 . 1 1 58 58 GLU CG C 13 36.35 0.20 . 1 . . . . . . . . 5377 1 717 . 1 1 58 58 GLU N N 15 117.29 0.20 . 1 . . . . . . . . 5377 1 718 . 1 1 59 59 THR H H 1 7.70 0.01 . 1 . . . . . . . . 5377 1 719 . 1 1 59 59 THR HA H 1 4.07 0.01 . 1 . . . . . . . . 5377 1 720 . 1 1 59 59 THR HB H 1 4.46 0.01 . 1 . . . . . . . . 5377 1 721 . 1 1 59 59 THR HG21 H 1 1.39 0.01 . 1 . . . . . . . . 5377 1 722 . 1 1 59 59 THR HG22 H 1 1.39 0.01 . 1 . . . . . . . . 5377 1 723 . 1 1 59 59 THR HG23 H 1 1.39 0.01 . 1 . . . . . . . . 5377 1 724 . 1 1 59 59 THR C C 13 175.16 0.20 . 1 . . . . . . . . 5377 1 725 . 1 1 59 59 THR CA C 13 65.94 0.20 . 1 . . . . . . . . 5377 1 726 . 1 1 59 59 THR CB C 13 68.96 0.20 . 1 . . . . . . . . 5377 1 727 . 1 1 59 59 THR CG2 C 13 20.70 0.20 . 1 . . . . . . . . 5377 1 728 . 1 1 59 59 THR N N 15 114.43 0.20 . 1 . . . . . . . . 5377 1 729 . 1 1 60 60 LEU H H 1 7.68 0.01 . 1 . . . . . . . . 5377 1 730 . 1 1 60 60 LEU HA H 1 4.35 0.01 . 1 . . . . . . . . 5377 1 731 . 1 1 60 60 LEU HB2 H 1 1.58 0.01 . 2 . . . . . . . . 5377 1 732 . 1 1 60 60 LEU HB3 H 1 1.73 0.01 . 2 . . . . . . . . 5377 1 733 . 1 1 60 60 LEU HG H 1 2.05 0.01 . 1 . . . . . . . . 5377 1 734 . 1 1 60 60 LEU HD11 H 1 0.88 0.01 . 2 . . . . . . . . 5377 1 735 . 1 1 60 60 LEU HD12 H 1 0.88 0.01 . 2 . . . . . . . . 5377 1 736 . 1 1 60 60 LEU HD13 H 1 0.88 0.01 . 2 . . . . . . . . 5377 1 737 . 1 1 60 60 LEU HD21 H 1 0.63 0.01 . 2 . . . . . . . . 5377 1 738 . 1 1 60 60 LEU HD22 H 1 0.63 0.01 . 2 . . . . . . . . 5377 1 739 . 1 1 60 60 LEU HD23 H 1 0.63 0.01 . 2 . . . . . . . . 5377 1 740 . 1 1 60 60 LEU C C 13 177.89 0.20 . 1 . . . . . . . . 5377 1 741 . 1 1 60 60 LEU CA C 13 55.67 0.20 . 1 . . . . . . . . 5377 1 742 . 1 1 60 60 LEU CB C 13 43.29 0.20 . 1 . . . . . . . . 5377 1 743 . 1 1 60 60 LEU CG C 13 25.71 0.20 . 1 . . . . . . . . 5377 1 744 . 1 1 60 60 LEU CD1 C 13 21.64 0.20 . 2 . . . . . . . . 5377 1 745 . 1 1 60 60 LEU CD2 C 13 20.55 0.20 . 2 . . . . . . . . 5377 1 746 . 1 1 60 60 LEU N N 15 119.72 0.20 . 1 . . . . . . . . 5377 1 747 . 1 1 61 61 ASP H H 1 8.14 0.01 . 1 . . . . . . . . 5377 1 748 . 1 1 61 61 ASP HA H 1 4.56 0.01 . 1 . . . . . . . . 5377 1 749 . 1 1 61 61 ASP HB2 H 1 2.50 0.01 . 2 . . . . . . . . 5377 1 750 . 1 1 61 61 ASP HB3 H 1 2.88 0.01 . 2 . . . . . . . . 5377 1 751 . 1 1 61 61 ASP C C 13 176.32 0.20 . 1 . . . . . . . . 5377 1 752 . 1 1 61 61 ASP CA C 13 54.60 0.20 . 1 . . . . . . . . 5377 1 753 . 1 1 61 61 ASP CB C 13 40.03 0.20 . 1 . . . . . . . . 5377 1 754 . 1 1 61 61 ASP N N 15 116.88 0.20 . 1 . . . . . . . . 5377 1 755 . 1 1 62 62 ASN H H 1 9.19 0.01 . 1 . . . . . . . . 5377 1 756 . 1 1 62 62 ASN HA H 1 4.84 0.01 . 1 . . . . . . . . 5377 1 757 . 1 1 62 62 ASN HB2 H 1 2.93 0.01 . 1 . . . . . . . . 5377 1 758 . 1 1 62 62 ASN HB3 H 1 2.93 0.01 . 1 . . . . . . . . 5377 1 759 . 1 1 62 62 ASN HD21 H 1 6.94 0.01 . 2 . . . . . . . . 5377 1 760 . 1 1 62 62 ASN HD22 H 1 7.75 0.01 . 2 . . . . . . . . 5377 1 761 . 1 1 62 62 ASN C C 13 176.31 0.20 . 1 . . . . . . . . 5377 1 762 . 1 1 62 62 ASN CA C 13 54.55 0.20 . 1 . . . . . . . . 5377 1 763 . 1 1 62 62 ASN CB C 13 40.21 0.20 . 1 . . . . . . . . 5377 1 764 . 1 1 62 62 ASN CG C 13 176.11 0.20 . 1 . . . . . . . . 5377 1 765 . 1 1 62 62 ASN N N 15 127.87 0.20 . 1 . . . . . . . . 5377 1 766 . 1 1 62 62 ASN ND2 N 15 113.50 0.20 . 1 . . . . . . . . 5377 1 767 . 1 1 63 63 ASP H H 1 8.31 0.01 . 1 . . . . . . . . 5377 1 768 . 1 1 63 63 ASP HA H 1 4.76 0.01 . 1 . . . . . . . . 5377 1 769 . 1 1 63 63 ASP HB2 H 1 2.71 0.01 . 2 . . . . . . . . 5377 1 770 . 1 1 63 63 ASP HB3 H 1 3.07 0.01 . 2 . . . . . . . . 5377 1 771 . 1 1 63 63 ASP C C 13 177.95 0.20 . 1 . . . . . . . . 5377 1 772 . 1 1 63 63 ASP CA C 13 53.29 0.20 . 1 . . . . . . . . 5377 1 773 . 1 1 63 63 ASP CB C 13 40.10 0.20 . 1 . . . . . . . . 5377 1 774 . 1 1 63 63 ASP N N 15 116.28 0.20 . 1 . . . . . . . . 5377 1 775 . 1 1 64 64 GLY H H 1 7.70 0.01 . 1 . . . . . . . . 5377 1 776 . 1 1 64 64 GLY HA2 H 1 3.92 0.01 . 2 . . . . . . . . 5377 1 777 . 1 1 64 64 GLY HA3 H 1 4.05 0.01 . 2 . . . . . . . . 5377 1 778 . 1 1 64 64 GLY C C 13 175.19 0.20 . 1 . . . . . . . . 5377 1 779 . 1 1 64 64 GLY CA C 13 47.50 0.20 . 1 . . . . . . . . 5377 1 780 . 1 1 64 64 GLY N N 15 109.35 0.20 . 1 . . . . . . . . 5377 1 781 . 1 1 65 65 ASP H H 1 8.40 0.01 . 1 . . . . . . . . 5377 1 782 . 1 1 65 65 ASP HA H 1 4.60 0.01 . 1 . . . . . . . . 5377 1 783 . 1 1 65 65 ASP HB2 H 1 2.62 0.01 . 2 . . . . . . . . 5377 1 784 . 1 1 65 65 ASP HB3 H 1 3.09 0.01 . 2 . . . . . . . . 5377 1 785 . 1 1 65 65 ASP C C 13 177.39 0.20 . 1 . . . . . . . . 5377 1 786 . 1 1 65 65 ASP CA C 13 53.60 0.20 . 1 . . . . . . . . 5377 1 787 . 1 1 65 65 ASP CB C 13 40.02 0.20 . 1 . . . . . . . . 5377 1 788 . 1 1 65 65 ASP N N 15 120.93 0.20 . 1 . . . . . . . . 5377 1 789 . 1 1 66 66 GLY H H 1 10.18 0.01 . 1 . . . . . . . . 5377 1 790 . 1 1 66 66 GLY HA2 H 1 3.49 0.01 . 2 . . . . . . . . 5377 1 791 . 1 1 66 66 GLY HA3 H 1 4.09 0.01 . 2 . . . . . . . . 5377 1 792 . 1 1 66 66 GLY C C 13 172.69 0.20 . 1 . . . . . . . . 5377 1 793 . 1 1 66 66 GLY CA C 13 45.82 0.20 . 1 . . . . . . . . 5377 1 794 . 1 1 66 66 GLY N N 15 113.95 0.20 . 1 . . . . . . . . 5377 1 795 . 1 1 67 67 GLU H H 1 7.94 0.01 . 1 . . . . . . . . 5377 1 796 . 1 1 67 67 GLU HA H 1 4.82 0.01 . 1 . . . . . . . . 5377 1 797 . 1 1 67 67 GLU HB2 H 1 1.51 0.01 . 2 . . . . . . . . 5377 1 798 . 1 1 67 67 GLU HB3 H 1 2.12 0.01 . 2 . . . . . . . . 5377 1 799 . 1 1 67 67 GLU HG2 H 1 2.07 0.01 . 2 . . . . . . . . 5377 1 800 . 1 1 67 67 GLU HG3 H 1 2.17 0.01 . 2 . . . . . . . . 5377 1 801 . 1 1 67 67 GLU C C 13 175.05 0.20 . 1 . . . . . . . . 5377 1 802 . 1 1 67 67 GLU CA C 13 54.98 0.20 . 1 . . . . . . . . 5377 1 803 . 1 1 67 67 GLU CB C 13 34.33 0.20 . 1 . . . . . . . . 5377 1 804 . 1 1 67 67 GLU CG C 13 36.11 0.20 . 1 . . . . . . . . 5377 1 805 . 1 1 67 67 GLU N N 15 118.20 0.20 . 1 . . . . . . . . 5377 1 806 . 1 1 68 68 CYS H H 1 9.49 0.01 . 1 . . . . . . . . 5377 1 807 . 1 1 68 68 CYS HA H 1 5.77 0.01 . 1 . . . . . . . . 5377 1 808 . 1 1 68 68 CYS HB2 H 1 2.47 0.01 . 2 . . . . . . . . 5377 1 809 . 1 1 68 68 CYS HB3 H 1 3.30 0.01 . 2 . . . . . . . . 5377 1 810 . 1 1 68 68 CYS C C 13 174.74 0.20 . 1 . . . . . . . . 5377 1 811 . 1 1 68 68 CYS CA C 13 56.74 0.20 . 1 . . . . . . . . 5377 1 812 . 1 1 68 68 CYS CB C 13 27.95 0.20 . 1 . . . . . . . . 5377 1 813 . 1 1 68 68 CYS N N 15 124.85 0.20 . 1 . . . . . . . . 5377 1 814 . 1 1 69 69 ASP H H 1 9.94 0.01 . 1 . . . . . . . . 5377 1 815 . 1 1 69 69 ASP HA H 1 5.22 0.01 . 1 . . . . . . . . 5377 1 816 . 1 1 69 69 ASP HB2 H 1 2.98 0.01 . 2 . . . . . . . . 5377 1 817 . 1 1 69 69 ASP HB3 H 1 3.60 0.01 . 2 . . . . . . . . 5377 1 818 . 1 1 69 69 ASP C C 13 175.54 0.20 . 1 . . . . . . . . 5377 1 819 . 1 1 69 69 ASP CA C 13 52.95 0.20 . 1 . . . . . . . . 5377 1 820 . 1 1 69 69 ASP CB C 13 40.21 0.20 . 1 . . . . . . . . 5377 1 821 . 1 1 69 69 ASP N N 15 132.25 0.20 . 1 . . . . . . . . 5377 1 822 . 1 1 70 70 PHE H H 1 8.97 0.01 . 1 . . . . . . . . 5377 1 823 . 1 1 70 70 PHE HA H 1 3.14 0.01 . 1 . . . . . . . . 5377 1 824 . 1 1 70 70 PHE HB2 H 1 2.22 0.01 . 2 . . . . . . . . 5377 1 825 . 1 1 70 70 PHE HB3 H 1 2.46 0.01 . 2 . . . . . . . . 5377 1 826 . 1 1 70 70 PHE HD1 H 1 6.95 0.01 . 1 . . . . . . . . 5377 1 827 . 1 1 70 70 PHE HD2 H 1 6.95 0.01 . 1 . . . . . . . . 5377 1 828 . 1 1 70 70 PHE HE1 H 1 7.01 0.01 . 1 . . . . . . . . 5377 1 829 . 1 1 70 70 PHE HE2 H 1 7.01 0.01 . 1 . . . . . . . . 5377 1 830 . 1 1 70 70 PHE C C 13 176.63 0.20 . 1 . . . . . . . . 5377 1 831 . 1 1 70 70 PHE CA C 13 63.23 0.20 . 1 . . . . . . . . 5377 1 832 . 1 1 70 70 PHE CB C 13 38.90 0.20 . 1 . . . . . . . . 5377 1 833 . 1 1 70 70 PHE CD1 C 13 131.46 0.20 . 1 . . . . . . . . 5377 1 834 . 1 1 70 70 PHE CD2 C 13 131.46 0.20 . 1 . . . . . . . . 5377 1 835 . 1 1 70 70 PHE CE1 C 13 129.63 0.20 . 1 . . . . . . . . 5377 1 836 . 1 1 70 70 PHE CE2 C 13 129.63 0.20 . 1 . . . . . . . . 5377 1 837 . 1 1 70 70 PHE N N 15 118.52 0.20 . 1 . . . . . . . . 5377 1 838 . 1 1 71 71 GLN H H 1 8.03 0.01 . 1 . . . . . . . . 5377 1 839 . 1 1 71 71 GLN HA H 1 3.78 0.01 . 1 . . . . . . . . 5377 1 840 . 1 1 71 71 GLN HB2 H 1 2.27 0.01 . 1 . . . . . . . . 5377 1 841 . 1 1 71 71 GLN HB3 H 1 2.27 0.01 . 1 . . . . . . . . 5377 1 842 . 1 1 71 71 GLN HG2 H 1 2.45 0.01 . 1 . . . . . . . . 5377 1 843 . 1 1 71 71 GLN HG3 H 1 2.45 0.01 . 1 . . . . . . . . 5377 1 844 . 1 1 71 71 GLN HE21 H 1 6.91 0.01 . 2 . . . . . . . . 5377 1 845 . 1 1 71 71 GLN HE22 H 1 7.64 0.01 . 2 . . . . . . . . 5377 1 846 . 1 1 71 71 GLN C C 13 179.80 0.20 . 1 . . . . . . . . 5377 1 847 . 1 1 71 71 GLN CA C 13 59.67 0.20 . 1 . . . . . . . . 5377 1 848 . 1 1 71 71 GLN CB C 13 30.02 0.20 . 1 . . . . . . . . 5377 1 849 . 1 1 71 71 GLN CG C 13 34.24 0.20 . 1 . . . . . . . . 5377 1 850 . 1 1 71 71 GLN CD C 13 180.32 0.20 . 1 . . . . . . . . 5377 1 851 . 1 1 71 71 GLN N N 15 119.23 0.20 . 1 . . . . . . . . 5377 1 852 . 1 1 71 71 GLN NE2 N 15 112.54 0.20 . 1 . . . . . . . . 5377 1 853 . 1 1 72 72 GLU H H 1 8.97 0.01 . 1 . . . . . . . . 5377 1 854 . 1 1 72 72 GLU HA H 1 4.20 0.01 . 1 . . . . . . . . 5377 1 855 . 1 1 72 72 GLU HB2 H 1 2.11 0.01 . 2 . . . . . . . . 5377 1 856 . 1 1 72 72 GLU HB3 H 1 2.21 0.01 . 2 . . . . . . . . 5377 1 857 . 1 1 72 72 GLU HG2 H 1 2.57 0.01 . 2 . . . . . . . . 5377 1 858 . 1 1 72 72 GLU HG3 H 1 2.83 0.01 . 2 . . . . . . . . 5377 1 859 . 1 1 72 72 GLU C C 13 179.47 0.20 . 1 . . . . . . . . 5377 1 860 . 1 1 72 72 GLU CA C 13 58.82 0.20 . 1 . . . . . . . . 5377 1 861 . 1 1 72 72 GLU CB C 13 29.83 0.20 . 1 . . . . . . . . 5377 1 862 . 1 1 72 72 GLU CG C 13 37.35 0.20 . 1 . . . . . . . . 5377 1 863 . 1 1 72 72 GLU N N 15 123.33 0.20 . 1 . . . . . . . . 5377 1 864 . 1 1 73 73 PHE H H 1 8.80 0.01 . 1 . . . . . . . . 5377 1 865 . 1 1 73 73 PHE HA H 1 4.21 0.01 . 1 . . . . . . . . 5377 1 866 . 1 1 73 73 PHE HB2 H 1 3.04 0.01 . 2 . . . . . . . . 5377 1 867 . 1 1 73 73 PHE HB3 H 1 3.23 0.01 . 2 . . . . . . . . 5377 1 868 . 1 1 73 73 PHE HE1 H 1 6.88 0.01 . 1 . . . . . . . . 5377 1 869 . 1 1 73 73 PHE HE2 H 1 6.88 0.01 . 1 . . . . . . . . 5377 1 870 . 1 1 73 73 PHE CA C 13 60.28 0.20 . 1 . . . . . . . . 5377 1 871 . 1 1 73 73 PHE CB C 13 39.23 0.20 . 1 . . . . . . . . 5377 1 872 . 1 1 73 73 PHE N N 15 122.31 0.20 . 1 . . . . . . . . 5377 1 873 . 1 1 74 74 MET H H 1 8.33 0.01 . 1 . . . . . . . . 5377 1 874 . 1 1 74 74 MET HA H 1 4.10 0.01 . 1 . . . . . . . . 5377 1 875 . 1 1 74 74 MET HB3 H 1 2.05 0.01 . 2 . . . . . . . . 5377 1 876 . 1 1 74 74 MET HG2 H 1 1.69 0.01 . 2 . . . . . . . . 5377 1 877 . 1 1 74 74 MET HG3 H 1 2.26 0.01 . 2 . . . . . . . . 5377 1 878 . 1 1 74 74 MET C C 13 179.17 0.20 . 1 . . . . . . . . 5377 1 879 . 1 1 74 74 MET CA C 13 55.21 0.20 . 1 . . . . . . . . 5377 1 880 . 1 1 74 74 MET CB C 13 29.29 0.20 . 1 . . . . . . . . 5377 1 881 . 1 1 74 74 MET N N 15 119.19 0.20 . 1 . . . . . . . . 5377 1 882 . 1 1 75 75 ALA H H 1 7.60 0.01 . 1 . . . . . . . . 5377 1 883 . 1 1 75 75 ALA HA H 1 4.18 0.01 . 1 . . . . . . . . 5377 1 884 . 1 1 75 75 ALA HB1 H 1 1.64 0.01 . 1 . . . . . . . . 5377 1 885 . 1 1 75 75 ALA HB2 H 1 1.64 0.01 . 1 . . . . . . . . 5377 1 886 . 1 1 75 75 ALA HB3 H 1 1.64 0.01 . 1 . . . . . . . . 5377 1 887 . 1 1 75 75 ALA C C 13 180.60 0.20 . 1 . . . . . . . . 5377 1 888 . 1 1 75 75 ALA CA C 13 55.17 0.20 . 1 . . . . . . . . 5377 1 889 . 1 1 75 75 ALA CB C 13 17.63 0.20 . 1 . . . . . . . . 5377 1 890 . 1 1 75 75 ALA N N 15 123.80 0.20 . 1 . . . . . . . . 5377 1 891 . 1 1 76 76 PHE H H 1 7.61 0.01 . 1 . . . . . . . . 5377 1 892 . 1 1 76 76 PHE HA H 1 4.51 0.01 . 1 . . . . . . . . 5377 1 893 . 1 1 76 76 PHE HB2 H 1 3.45 0.01 . 2 . . . . . . . . 5377 1 894 . 1 1 76 76 PHE HB3 H 1 3.55 0.01 . 2 . . . . . . . . 5377 1 895 . 1 1 76 76 PHE HD1 H 1 7.09 0.01 . 1 . . . . . . . . 5377 1 896 . 1 1 76 76 PHE HD2 H 1 7.09 0.01 . 1 . . . . . . . . 5377 1 897 . 1 1 76 76 PHE C C 13 176.72 0.20 . 1 . . . . . . . . 5377 1 898 . 1 1 76 76 PHE CA C 13 59.91 0.20 . 1 . . . . . . . . 5377 1 899 . 1 1 76 76 PHE CB C 13 37.98 0.20 . 1 . . . . . . . . 5377 1 900 . 1 1 76 76 PHE CD1 C 13 131.88 0.20 . 1 . . . . . . . . 5377 1 901 . 1 1 76 76 PHE CD2 C 13 131.88 0.20 . 1 . . . . . . . . 5377 1 902 . 1 1 76 76 PHE N N 15 121.74 0.20 . 1 . . . . . . . . 5377 1 903 . 1 1 77 77 VAL H H 1 8.49 0.01 . 1 . . . . . . . . 5377 1 904 . 1 1 77 77 VAL HA H 1 2.91 0.01 . 1 . . . . . . . . 5377 1 905 . 1 1 77 77 VAL HB H 1 1.97 0.01 . 1 . . . . . . . . 5377 1 906 . 1 1 77 77 VAL HG11 H 1 0.69 0.01 . 2 . . . . . . . . 5377 1 907 . 1 1 77 77 VAL HG12 H 1 0.69 0.01 . 2 . . . . . . . . 5377 1 908 . 1 1 77 77 VAL HG13 H 1 0.69 0.01 . 2 . . . . . . . . 5377 1 909 . 1 1 77 77 VAL HG21 H 1 0.35 0.01 . 2 . . . . . . . . 5377 1 910 . 1 1 77 77 VAL HG22 H 1 0.35 0.01 . 2 . . . . . . . . 5377 1 911 . 1 1 77 77 VAL HG23 H 1 0.35 0.01 . 2 . . . . . . . . 5377 1 912 . 1 1 77 77 VAL C C 13 179.69 0.20 . 1 . . . . . . . . 5377 1 913 . 1 1 77 77 VAL CA C 13 66.70 0.20 . 1 . . . . . . . . 5377 1 914 . 1 1 77 77 VAL CB C 13 31.36 0.20 . 1 . . . . . . . . 5377 1 915 . 1 1 77 77 VAL CG1 C 13 20.57 0.20 . 2 . . . . . . . . 5377 1 916 . 1 1 77 77 VAL CG2 C 13 23.29 0.20 . 2 . . . . . . . . 5377 1 917 . 1 1 77 77 VAL N N 15 120.52 0.20 . 1 . . . . . . . . 5377 1 918 . 1 1 78 78 ALA H H 1 8.51 0.01 . 1 . . . . . . . . 5377 1 919 . 1 1 78 78 ALA HA H 1 3.96 0.01 . 1 . . . . . . . . 5377 1 920 . 1 1 78 78 ALA HB1 H 1 1.46 0.01 . 1 . . . . . . . . 5377 1 921 . 1 1 78 78 ALA HB2 H 1 1.46 0.01 . 1 . . . . . . . . 5377 1 922 . 1 1 78 78 ALA HB3 H 1 1.46 0.01 . 1 . . . . . . . . 5377 1 923 . 1 1 78 78 ALA C C 13 179.26 0.20 . 1 . . . . . . . . 5377 1 924 . 1 1 78 78 ALA CA C 13 56.17 0.20 . 1 . . . . . . . . 5377 1 925 . 1 1 78 78 ALA CB C 13 17.74 0.20 . 1 . . . . . . . . 5377 1 926 . 1 1 78 78 ALA N N 15 125.09 0.20 . 1 . . . . . . . . 5377 1 927 . 1 1 79 79 MET H H 1 8.05 0.01 . 1 . . . . . . . . 5377 1 928 . 1 1 79 79 MET HA H 1 4.15 0.01 . 1 . . . . . . . . 5377 1 929 . 1 1 79 79 MET HB2 H 1 2.08 0.01 . 2 . . . . . . . . 5377 1 930 . 1 1 79 79 MET HB3 H 1 2.46 0.01 . 2 . . . . . . . . 5377 1 931 . 1 1 79 79 MET HG2 H 1 2.65 0.01 . 2 . . . . . . . . 5377 1 932 . 1 1 79 79 MET HG3 H 1 2.72 0.01 . 2 . . . . . . . . 5377 1 933 . 1 1 79 79 MET C C 13 178.99 0.20 . 1 . . . . . . . . 5377 1 934 . 1 1 79 79 MET CA C 13 59.47 0.20 . 1 . . . . . . . . 5377 1 935 . 1 1 79 79 MET CB C 13 33.61 0.20 . 1 . . . . . . . . 5377 1 936 . 1 1 79 79 MET CG C 13 31.60 0.20 . 1 . . . . . . . . 5377 1 937 . 1 1 79 79 MET CE C 13 16.81 0.20 . 1 . . . . . . . . 5377 1 938 . 1 1 79 79 MET N N 15 120.90 0.20 . 1 . . . . . . . . 5377 1 939 . 1 1 80 80 VAL H H 1 8.40 0.01 . 1 . . . . . . . . 5377 1 940 . 1 1 80 80 VAL HA H 1 3.46 0.01 . 1 . . . . . . . . 5377 1 941 . 1 1 80 80 VAL HB H 1 1.67 0.01 . 1 . . . . . . . . 5377 1 942 . 1 1 80 80 VAL HG11 H 1 0.77 0.01 . 2 . . . . . . . . 5377 1 943 . 1 1 80 80 VAL HG12 H 1 0.77 0.01 . 2 . . . . . . . . 5377 1 944 . 1 1 80 80 VAL HG13 H 1 0.77 0.01 . 2 . . . . . . . . 5377 1 945 . 1 1 80 80 VAL HG21 H 1 0.37 0.01 . 2 . . . . . . . . 5377 1 946 . 1 1 80 80 VAL HG22 H 1 0.37 0.01 . 2 . . . . . . . . 5377 1 947 . 1 1 80 80 VAL HG23 H 1 0.37 0.01 . 2 . . . . . . . . 5377 1 948 . 1 1 80 80 VAL C C 13 178.90 0.20 . 1 . . . . . . . . 5377 1 949 . 1 1 80 80 VAL CA C 13 66.63 0.20 . 1 . . . . . . . . 5377 1 950 . 1 1 80 80 VAL CB C 13 31.81 0.20 . 1 . . . . . . . . 5377 1 951 . 1 1 80 80 VAL CG1 C 13 22.46 0.20 . 2 . . . . . . . . 5377 1 952 . 1 1 80 80 VAL CG2 C 13 22.49 0.20 . 2 . . . . . . . . 5377 1 953 . 1 1 80 80 VAL N N 15 120.00 0.20 . 1 . . . . . . . . 5377 1 954 . 1 1 81 81 THR H H 1 8.70 0.01 . 1 . . . . . . . . 5377 1 955 . 1 1 81 81 THR HA H 1 3.98 0.01 . 1 . . . . . . . . 5377 1 956 . 1 1 81 81 THR HB H 1 3.77 0.01 . 1 . . . . . . . . 5377 1 957 . 1 1 81 81 THR HG21 H 1 1.55 0.01 . 1 . . . . . . . . 5377 1 958 . 1 1 81 81 THR HG22 H 1 1.55 0.01 . 1 . . . . . . . . 5377 1 959 . 1 1 81 81 THR HG23 H 1 1.55 0.01 . 1 . . . . . . . . 5377 1 960 . 1 1 81 81 THR CA C 13 68.45 0.20 . 1 . . . . . . . . 5377 1 961 . 1 1 81 81 THR CB C 13 68.18 0.20 . 1 . . . . . . . . 5377 1 962 . 1 1 81 81 THR CG2 C 13 23.14 0.20 . 1 . . . . . . . . 5377 1 963 . 1 1 81 81 THR N N 15 117.53 0.20 . 1 . . . . . . . . 5377 1 964 . 1 1 82 82 THR H H 1 8.19 0.01 . 1 . . . . . . . . 5377 1 965 . 1 1 82 82 THR HA H 1 4.08 0.01 . 1 . . . . . . . . 5377 1 966 . 1 1 82 82 THR HB H 1 4.26 0.01 . 1 . . . . . . . . 5377 1 967 . 1 1 82 82 THR HG21 H 1 1.31 0.01 . 1 . . . . . . . . 5377 1 968 . 1 1 82 82 THR HG22 H 1 1.31 0.01 . 1 . . . . . . . . 5377 1 969 . 1 1 82 82 THR HG23 H 1 1.31 0.01 . 1 . . . . . . . . 5377 1 970 . 1 1 82 82 THR C C 13 176.42 0.20 . 1 . . . . . . . . 5377 1 971 . 1 1 82 82 THR CA C 13 67.81 0.20 . 1 . . . . . . . . 5377 1 972 . 1 1 82 82 THR CB C 13 68.12 0.20 . 1 . . . . . . . . 5377 1 973 . 1 1 82 82 THR CG2 C 13 21.96 0.20 . 1 . . . . . . . . 5377 1 974 . 1 1 82 82 THR N N 15 116.89 0.20 . 1 . . . . . . . . 5377 1 975 . 1 1 83 83 ALA H H 1 7.57 0.01 . 1 . . . . . . . . 5377 1 976 . 1 1 83 83 ALA HA H 1 4.27 0.01 . 1 . . . . . . . . 5377 1 977 . 1 1 83 83 ALA HB1 H 1 1.50 0.01 . 1 . . . . . . . . 5377 1 978 . 1 1 83 83 ALA HB2 H 1 1.50 0.01 . 1 . . . . . . . . 5377 1 979 . 1 1 83 83 ALA HB3 H 1 1.50 0.01 . 1 . . . . . . . . 5377 1 980 . 1 1 83 83 ALA C C 13 179.86 0.20 . 1 . . . . . . . . 5377 1 981 . 1 1 83 83 ALA CA C 13 55.15 0.20 . 1 . . . . . . . . 5377 1 982 . 1 1 83 83 ALA CB C 13 18.10 0.20 . 1 . . . . . . . . 5377 1 983 . 1 1 83 83 ALA N N 15 124.59 0.20 . 1 . . . . . . . . 5377 1 984 . 1 1 84 84 CYS H H 1 8.34 0.01 . 1 . . . . . . . . 5377 1 985 . 1 1 84 84 CYS HA H 1 3.58 0.01 . 1 . . . . . . . . 5377 1 986 . 1 1 84 84 CYS HB2 H 1 2.03 0.01 . 2 . . . . . . . . 5377 1 987 . 1 1 84 84 CYS HB3 H 1 2.82 0.01 . 2 . . . . . . . . 5377 1 988 . 1 1 84 84 CYS C C 13 175.88 0.20 . 1 . . . . . . . . 5377 1 989 . 1 1 84 84 CYS CA C 13 62.44 0.20 . 1 . . . . . . . . 5377 1 990 . 1 1 84 84 CYS CB C 13 26.46 0.20 . 1 . . . . . . . . 5377 1 991 . 1 1 84 84 CYS N N 15 116.71 0.20 . 1 . . . . . . . . 5377 1 992 . 1 1 85 85 HIS H H 1 8.17 0.01 . 1 . . . . . . . . 5377 1 993 . 1 1 85 85 HIS HA H 1 4.01 0.01 . 1 . . . . . . . . 5377 1 994 . 1 1 85 85 HIS HB2 H 1 2.64 0.01 . 2 . . . . . . . . 5377 1 995 . 1 1 85 85 HIS HB3 H 1 3.15 0.01 . 2 . . . . . . . . 5377 1 996 . 1 1 85 85 HIS HD2 H 1 6.46 0.01 . 1 . . . . . . . . 5377 1 997 . 1 1 85 85 HIS HE1 H 1 8.13 0.01 . 1 . . . . . . . . 5377 1 998 . 1 1 85 85 HIS C C 13 177.48 0.20 . 1 . . . . . . . . 5377 1 999 . 1 1 85 85 HIS CA C 13 59.41 0.20 . 1 . . . . . . . . 5377 1 1000 . 1 1 85 85 HIS CB C 13 29.14 0.20 . 1 . . . . . . . . 5377 1 1001 . 1 1 85 85 HIS CD2 C 13 121.87 0.20 . 1 . . . . . . . . 5377 1 1002 . 1 1 85 85 HIS CE1 C 13 136.68 0.20 . 1 . . . . . . . . 5377 1 1003 . 1 1 85 85 HIS N N 15 119.13 0.20 . 1 . . . . . . . . 5377 1 1004 . 1 1 86 86 GLU H H 1 7.65 0.01 . 1 . . . . . . . . 5377 1 1005 . 1 1 86 86 GLU HA H 1 3.94 0.01 . 1 . . . . . . . . 5377 1 1006 . 1 1 86 86 GLU HB2 H 1 1.93 0.01 . 1 . . . . . . . . 5377 1 1007 . 1 1 86 86 GLU HB3 H 1 1.93 0.01 . 1 . . . . . . . . 5377 1 1008 . 1 1 86 86 GLU HG2 H 1 2.27 0.01 . 1 . . . . . . . . 5377 1 1009 . 1 1 86 86 GLU HG3 H 1 2.27 0.01 . 1 . . . . . . . . 5377 1 1010 . 1 1 86 86 GLU C C 13 177.66 0.20 . 1 . . . . . . . . 5377 1 1011 . 1 1 86 86 GLU CA C 13 58.47 0.20 . 1 . . . . . . . . 5377 1 1012 . 1 1 86 86 GLU CB C 13 29.57 0.20 . 1 . . . . . . . . 5377 1 1013 . 1 1 86 86 GLU CG C 13 36.66 0.20 . 1 . . . . . . . . 5377 1 1014 . 1 1 86 86 GLU N N 15 116.75 0.20 . 1 . . . . . . . . 5377 1 1015 . 1 1 87 87 PHE H H 1 7.65 0.01 . 1 . . . . . . . . 5377 1 1016 . 1 1 87 87 PHE HA H 1 4.50 0.01 . 1 . . . . . . . . 5377 1 1017 . 1 1 87 87 PHE HB3 H 1 2.87 0.01 . 2 . . . . . . . . 5377 1 1018 . 1 1 87 87 PHE HD1 H 1 7.12 0.01 . 1 . . . . . . . . 5377 1 1019 . 1 1 87 87 PHE HD2 H 1 7.12 0.01 . 1 . . . . . . . . 5377 1 1020 . 1 1 87 87 PHE CA C 13 58.65 0.20 . 1 . . . . . . . . 5377 1 1021 . 1 1 87 87 PHE CB C 13 40.63 0.20 . 1 . . . . . . . . 5377 1 1022 . 1 1 87 87 PHE CD1 C 13 131.43 0.20 . 1 . . . . . . . . 5377 1 1023 . 1 1 87 87 PHE CD2 C 13 131.43 0.20 . 1 . . . . . . . . 5377 1 1024 . 1 1 87 87 PHE N N 15 117.13 0.20 . 1 . . . . . . . . 5377 1 1025 . 1 1 88 88 PHE H H 1 7.66 0.01 . 1 . . . . . . . . 5377 1 1026 . 1 1 88 88 PHE HA H 1 4.50 0.01 . 1 . . . . . . . . 5377 1 1027 . 1 1 88 88 PHE HB2 H 1 2.87 0.01 . 2 . . . . . . . . 5377 1 1028 . 1 1 88 88 PHE HB3 H 1 3.02 0.01 . 2 . . . . . . . . 5377 1 1029 . 1 1 88 88 PHE C C 13 175.75 0.20 . 1 . . . . . . . . 5377 1 1030 . 1 1 88 88 PHE CA C 13 58.65 0.20 . 1 . . . . . . . . 5377 1 1031 . 1 1 88 88 PHE CB C 13 39.34 0.20 . 1 . . . . . . . . 5377 1 1032 . 1 1 88 88 PHE N N 15 117.13 0.20 . 1 . . . . . . . . 5377 1 1033 . 1 1 89 89 GLU H H 1 7.89 0.01 . 1 . . . . . . . . 5377 1 1034 . 1 1 89 89 GLU HA H 1 4.18 0.01 . 1 . . . . . . . . 5377 1 1035 . 1 1 89 89 GLU HB2 H 1 2.03 0.01 . 1 . . . . . . . . 5377 1 1036 . 1 1 89 89 GLU HB3 H 1 2.03 0.01 . 1 . . . . . . . . 5377 1 1037 . 1 1 89 89 GLU HG2 H 1 2.17 0.01 . 1 . . . . . . . . 5377 1 1038 . 1 1 89 89 GLU HG3 H 1 2.17 0.01 . 1 . . . . . . . . 5377 1 1039 . 1 1 89 89 GLU C C 13 175.70 0.20 . 1 . . . . . . . . 5377 1 1040 . 1 1 89 89 GLU CA C 13 56.73 0.20 . 1 . . . . . . . . 5377 1 1041 . 1 1 89 89 GLU CB C 13 30.17 0.20 . 1 . . . . . . . . 5377 1 1042 . 1 1 89 89 GLU CG C 13 36.21 0.20 . 1 . . . . . . . . 5377 1 1043 . 1 1 89 89 GLU N N 15 121.69 0.20 . 1 . . . . . . . . 5377 1 1044 . 1 1 90 90 HIS H H 1 8.05 0.01 . 1 . . . . . . . . 5377 1 1045 . 1 1 90 90 HIS HA H 1 4.56 0.01 . 1 . . . . . . . . 5377 1 1046 . 1 1 90 90 HIS HB2 H 1 3.08 0.01 . 2 . . . . . . . . 5377 1 1047 . 1 1 90 90 HIS HB3 H 1 3.17 0.01 . 2 . . . . . . . . 5377 1 1048 . 1 1 90 90 HIS HD2 H 1 7.14 0.01 . 1 . . . . . . . . 5377 1 1049 . 1 1 90 90 HIS HE1 H 1 8.17 0.01 . 1 . . . . . . . . 5377 1 1050 . 1 1 90 90 HIS C C 13 173.81 0.20 . 1 . . . . . . . . 5377 1 1051 . 1 1 90 90 HIS CA C 13 55.59 0.20 . 1 . . . . . . . . 5377 1 1052 . 1 1 90 90 HIS CB C 13 30.02 0.20 . 1 . . . . . . . . 5377 1 1053 . 1 1 90 90 HIS CD2 C 13 120.69 0.20 . 1 . . . . . . . . 5377 1 1054 . 1 1 90 90 HIS CE1 C 13 137.22 0.20 . 1 . . . . . . . . 5377 1 1055 . 1 1 90 90 HIS N N 15 119.32 0.20 . 1 . . . . . . . . 5377 1 1056 . 1 1 91 91 GLU H H 1 8.17 0.01 . 1 . . . . . . . . 5377 1 1057 . 1 1 91 91 GLU HA H 1 4.14 0.01 . 1 . . . . . . . . 5377 1 1058 . 1 1 91 91 GLU HB2 H 1 1.93 0.01 . 2 . . . . . . . . 5377 1 1059 . 1 1 91 91 GLU HB3 H 1 2.08 0.01 . 2 . . . . . . . . 5377 1 1060 . 1 1 91 91 GLU HG2 H 1 2.21 0.01 . 1 . . . . . . . . 5377 1 1061 . 1 1 91 91 GLU HG3 H 1 2.21 0.01 . 1 . . . . . . . . 5377 1 1062 . 1 1 91 91 GLU CA C 13 58.25 0.20 . 1 . . . . . . . . 5377 1 1063 . 1 1 91 91 GLU CB C 13 30.64 0.20 . 1 . . . . . . . . 5377 1 1064 . 1 1 91 91 GLU CG C 13 36.70 0.20 . 1 . . . . . . . . 5377 1 1065 . 1 1 91 91 GLU N N 15 127.85 0.20 . 1 . . . . . . . . 5377 1 stop_ save_ save_chemical_shifts_set_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shifts_set_2 _Assigned_chem_shift_list.Entry_ID 5377 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $experimental_conditions _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 . 5377 2 . . 2 $sample_2 . 5377 2 . . 3 $sample_3 . 5377 2 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 3 2 2 2 THR H H 1 7.59 0.01 . 1 . . . . . . . . 5377 2 2 . 3 2 2 2 THR HA H 1 4.27 0.01 . 1 . . . . . . . . 5377 2 3 . 3 2 2 2 THR HB H 1 3.88 0.01 . 1 . . . . . . . . 5377 2 4 . 3 2 2 2 THR HG21 H 1 1.18 0.01 . 1 . . . . . . . . 5377 2 5 . 3 2 2 2 THR HG22 H 1 1.18 0.01 . 1 . . . . . . . . 5377 2 6 . 3 2 2 2 THR HG23 H 1 1.18 0.01 . 1 . . . . . . . . 5377 2 7 . 3 2 2 2 THR CA C 13 65.14 0.20 . 1 . . . . . . . . 5377 2 8 . 3 2 2 2 THR CG2 C 13 21.79 0.20 . 1 . . . . . . . . 5377 2 9 . 3 2 3 3 ARG H H 1 7.90 0.01 . 1 . . . . . . . . 5377 2 10 . 3 2 3 3 ARG HA H 1 4.42 0.01 . 1 . . . . . . . . 5377 2 11 . 3 2 3 3 ARG HB2 H 1 1.78 0.01 . 2 . . . . . . . . 5377 2 12 . 3 2 3 3 ARG HB3 H 1 1.87 0.01 . 2 . . . . . . . . 5377 2 13 . 3 2 3 3 ARG HG2 H 1 1.64 0.01 . 1 . . . . . . . . 5377 2 14 . 3 2 3 3 ARG HG3 H 1 1.64 0.01 . 1 . . . . . . . . 5377 2 15 . 3 2 3 3 ARG HD2 H 1 3.17 0.01 . 1 . . . . . . . . 5377 2 16 . 3 2 3 3 ARG HD3 H 1 3.17 0.01 . 1 . . . . . . . . 5377 2 17 . 3 2 3 3 ARG CG C 13 27.16 0.20 . 1 . . . . . . . . 5377 2 18 . 3 2 3 3 ARG CD C 13 42.46 0.20 . 1 . . . . . . . . 5377 2 19 . 3 2 4 4 THR H H 1 7.74 0.01 . 1 . . . . . . . . 5377 2 20 . 3 2 4 4 THR HA H 1 4.23 0.01 . 1 . . . . . . . . 5377 2 21 . 3 2 4 4 THR HB H 1 3.82 0.01 . 1 . . . . . . . . 5377 2 22 . 3 2 4 4 THR HG21 H 1 1.13 0.01 . 1 . . . . . . . . 5377 2 23 . 3 2 4 4 THR HG22 H 1 1.13 0.01 . 1 . . . . . . . . 5377 2 24 . 3 2 4 4 THR HG23 H 1 1.13 0.01 . 1 . . . . . . . . 5377 2 25 . 3 2 4 4 THR CA C 13 65.06 0.20 . 1 . . . . . . . . 5377 2 26 . 3 2 4 4 THR CG2 C 13 21.68 0.20 . 1 . . . . . . . . 5377 2 27 . 3 2 5 5 LYS H H 1 7.88 0.01 . 1 . . . . . . . . 5377 2 28 . 3 2 5 5 LYS HA H 1 4.35 0.01 . 1 . . . . . . . . 5377 2 29 . 3 2 5 5 LYS HB2 H 1 1.87 0.01 . 1 . . . . . . . . 5377 2 30 . 3 2 5 5 LYS HB3 H 1 1.87 0.01 . 1 . . . . . . . . 5377 2 31 . 3 2 5 5 LYS HG2 H 1 1.54 0.01 . 1 . . . . . . . . 5377 2 32 . 3 2 5 5 LYS HG3 H 1 1.54 0.01 . 1 . . . . . . . . 5377 2 33 . 3 2 5 5 LYS HD2 H 1 1.75 0.01 . 1 . . . . . . . . 5377 2 34 . 3 2 5 5 LYS HD3 H 1 1.75 0.01 . 1 . . . . . . . . 5377 2 35 . 3 2 5 5 LYS HE2 H 1 2.92 0.01 . 1 . . . . . . . . 5377 2 36 . 3 2 5 5 LYS HE3 H 1 2.92 0.01 . 1 . . . . . . . . 5377 2 37 . 3 2 6 6 ILE H H 1 8.33 0.01 . 1 . . . . . . . . 5377 2 38 . 3 2 6 6 ILE HA H 1 3.72 0.01 . 1 . . . . . . . . 5377 2 39 . 3 2 6 6 ILE HB H 1 1.52 0.01 . 1 . . . . . . . . 5377 2 40 . 3 2 6 6 ILE HG12 H 1 1.06 0.01 . 2 . . . . . . . . 5377 2 41 . 3 2 6 6 ILE HG13 H 1 1.26 0.01 . 2 . . . . . . . . 5377 2 42 . 3 2 6 6 ILE HG21 H 1 0.62 0.01 . 1 . . . . . . . . 5377 2 43 . 3 2 6 6 ILE HG22 H 1 0.62 0.01 . 1 . . . . . . . . 5377 2 44 . 3 2 6 6 ILE HG23 H 1 0.62 0.01 . 1 . . . . . . . . 5377 2 45 . 3 2 6 6 ILE HD11 H 1 0.58 0.01 . 1 . . . . . . . . 5377 2 46 . 3 2 6 6 ILE HD12 H 1 0.58 0.01 . 1 . . . . . . . . 5377 2 47 . 3 2 6 6 ILE HD13 H 1 0.58 0.01 . 1 . . . . . . . . 5377 2 48 . 3 2 6 6 ILE CA C 13 61.60 0.20 . 1 . . . . . . . . 5377 2 49 . 3 2 6 6 ILE CB C 13 38.58 0.20 . 1 . . . . . . . . 5377 2 50 . 3 2 6 6 ILE CG1 C 13 27.61 0.20 . 1 . . . . . . . . 5377 2 51 . 3 2 6 6 ILE CG2 C 13 17.98 0.20 . 1 . . . . . . . . 5377 2 52 . 3 2 6 6 ILE CD1 C 13 14.20 0.20 . 1 . . . . . . . . 5377 2 53 . 3 2 7 7 ASP H H 1 7.99 0.01 . 1 . . . . . . . . 5377 2 54 . 3 2 7 7 ASP HA H 1 3.73 0.01 . 1 . . . . . . . . 5377 2 55 . 3 2 7 7 ASP HB2 H 1 2.64 0.01 . 2 . . . . . . . . 5377 2 56 . 3 2 7 7 ASP HB3 H 1 2.74 0.01 . 2 . . . . . . . . 5377 2 57 . 3 2 8 8 TRP H H 1 7.48 0.01 . 1 . . . . . . . . 5377 2 58 . 3 2 8 8 TRP HA H 1 4.18 0.01 . 1 . . . . . . . . 5377 2 59 . 3 2 8 8 TRP HB2 H 1 3.09 0.01 . 2 . . . . . . . . 5377 2 60 . 3 2 8 8 TRP HB3 H 1 3.30 0.01 . 2 . . . . . . . . 5377 2 61 . 3 2 8 8 TRP HE1 H 1 10.28 0.01 . 1 . . . . . . . . 5377 2 62 . 3 2 8 8 TRP HD1 H 1 7.38 0.01 . 1 . . . . . . . . 5377 2 63 . 3 2 8 8 TRP HE3 H 1 7.48 0.01 . 1 . . . . . . . . 5377 2 64 . 3 2 8 8 TRP HZ3 H 1 6.96 0.01 . 1 . . . . . . . . 5377 2 65 . 3 2 8 8 TRP HH2 H 1 7.11 0.01 . 1 . . . . . . . . 5377 2 66 . 3 2 8 8 TRP HZ2 H 1 7.44 0.01 . 1 . . . . . . . . 5377 2 67 . 3 2 9 9 ASN H H 1 7.64 0.01 . 1 . . . . . . . . 5377 2 68 . 3 2 9 9 ASN HA H 1 3.65 0.01 . 1 . . . . . . . . 5377 2 69 . 3 2 9 9 ASN HB2 H 1 3.15 0.01 . 1 . . . . . . . . 5377 2 70 . 3 2 9 9 ASN HB3 H 1 2.94 0.01 . 2 . . . . . . . . 5377 2 71 . 3 2 9 9 ASN CB C 13 42.48 0.20 . 1 . . . . . . . . 5377 2 72 . 3 2 10 10 LYS H H 1 7.82 0.01 . 1 . . . . . . . . 5377 2 73 . 3 2 10 10 LYS HA H 1 4.20 0.01 . 1 . . . . . . . . 5377 2 74 . 3 2 10 10 LYS HB2 H 1 1.84 0.01 . 1 . . . . . . . . 5377 2 75 . 3 2 10 10 LYS HB3 H 1 1.84 0.01 . 1 . . . . . . . . 5377 2 76 . 3 2 10 10 LYS HG2 H 1 1.43 0.01 . 1 . . . . . . . . 5377 2 77 . 3 2 10 10 LYS HG3 H 1 1.43 0.01 . 1 . . . . . . . . 5377 2 78 . 3 2 10 10 LYS HD2 H 1 1.65 0.01 . 1 . . . . . . . . 5377 2 79 . 3 2 10 10 LYS HD3 H 1 1.65 0.01 . 1 . . . . . . . . 5377 2 80 . 3 2 10 10 LYS HE2 H 1 2.92 0.01 . 1 . . . . . . . . 5377 2 81 . 3 2 10 10 LYS HE3 H 1 2.92 0.01 . 1 . . . . . . . . 5377 2 82 . 3 2 10 10 LYS CG C 13 24.85 0.20 . 1 . . . . . . . . 5377 2 83 . 3 2 10 10 LYS CD C 13 27.25 0.20 . 1 . . . . . . . . 5377 2 84 . 3 2 11 11 ILE H H 1 7.48 0.01 . 1 . . . . . . . . 5377 2 85 . 3 2 11 11 ILE HA H 1 3.88 0.01 . 1 . . . . . . . . 5377 2 86 . 3 2 11 11 ILE HB H 1 2.05 0.01 . 1 . . . . . . . . 5377 2 87 . 3 2 11 11 ILE HG12 H 1 0.73 0.01 . 2 . . . . . . . . 5377 2 88 . 3 2 11 11 ILE HG13 H 1 1.36 0.01 . 2 . . . . . . . . 5377 2 89 . 3 2 11 11 ILE HG21 H 1 0.97 0.01 . 1 . . . . . . . . 5377 2 90 . 3 2 11 11 ILE HG22 H 1 0.97 0.01 . 1 . . . . . . . . 5377 2 91 . 3 2 11 11 ILE HG23 H 1 0.97 0.01 . 1 . . . . . . . . 5377 2 92 . 3 2 11 11 ILE HD11 H 1 0.38 0.01 . 1 . . . . . . . . 5377 2 93 . 3 2 11 11 ILE HD12 H 1 0.38 0.01 . 1 . . . . . . . . 5377 2 94 . 3 2 11 11 ILE HD13 H 1 0.38 0.01 . 1 . . . . . . . . 5377 2 95 . 3 2 11 11 ILE CA C 13 62.99 0.20 . 1 . . . . . . . . 5377 2 96 . 3 2 11 11 ILE CB C 13 38.08 0.20 . 1 . . . . . . . . 5377 2 97 . 3 2 11 11 ILE CG1 C 13 27.72 0.20 . 1 . . . . . . . . 5377 2 98 . 3 2 11 11 ILE CG2 C 13 17.71 0.20 . 1 . . . . . . . . 5377 2 99 . 3 2 11 11 ILE CD1 C 13 12.19 0.20 . 1 . . . . . . . . 5377 2 100 . 3 2 12 12 LEU H H 1 7.73 0.01 . 1 . . . . . . . . 5377 2 101 . 3 2 12 12 LEU HA H 1 4.21 0.01 . 1 . . . . . . . . 5377 2 102 . 3 2 12 12 LEU HB2 H 1 1.85 0.01 . 2 . . . . . . . . 5377 2 103 . 3 2 12 12 LEU HB3 H 1 1.60 0.01 . 2 . . . . . . . . 5377 2 104 . 3 2 12 12 LEU HG H 1 1.39 0.01 . 1 . . . . . . . . 5377 2 105 . 3 2 12 12 LEU HD11 H 1 0.91 0.01 . 2 . . . . . . . . 5377 2 106 . 3 2 12 12 LEU HD12 H 1 0.91 0.01 . 2 . . . . . . . . 5377 2 107 . 3 2 12 12 LEU HD13 H 1 0.91 0.01 . 2 . . . . . . . . 5377 2 108 . 3 2 12 12 LEU HD21 H 1 0.85 0.01 . 2 . . . . . . . . 5377 2 109 . 3 2 12 12 LEU HD22 H 1 0.85 0.01 . 2 . . . . . . . . 5377 2 110 . 3 2 12 12 LEU HD23 H 1 0.85 0.01 . 2 . . . . . . . . 5377 2 111 . 3 2 12 12 LEU CB C 13 42.48 0.20 . 1 . . . . . . . . 5377 2 112 . 3 2 12 12 LEU CG C 13 24.77 0.20 . 1 . . . . . . . . 5377 2 113 . 3 2 12 12 LEU CD1 C 13 25.28 0.20 . 2 . . . . . . . . 5377 2 114 . 3 2 12 12 LEU CD2 C 13 12.95 0.20 . 2 . . . . . . . . 5377 2 115 . 3 2 13 13 SER H H 1 8.09 0.01 . 1 . . . . . . . . 5377 2 116 . 3 2 13 13 SER HA H 1 4.03 0.01 . 1 . . . . . . . . 5377 2 117 . 3 2 13 13 SER HB2 H 1 3.62 0.01 . 2 . . . . . . . . 5377 2 118 . 3 2 13 13 SER HB3 H 1 3.54 0.01 . 2 . . . . . . . . 5377 2 stop_ save_