data_4664 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4664 _Entry.Title ; Sequence-Specific Resonance Assignments of Q83, a Lipocalin Highly Expressed in v-myc-Transformed Avian Fibroblasts ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2000-02-07 _Entry.Accession_date 2000-02-10 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Georg Kontaxis . . . 4664 2 Theresia Matt . . . 4664 3 Wolfgang Schuler . . . 4664 4 Bernhard Krautler . . . 4664 5 Klaus Bister . . . 4664 6 Robert Konrat . . . 4664 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4664 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 493 4664 '13C chemical shifts' 419 4664 '15N chemical shifts' 138 4664 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2001-07-05 . update author 'residue 115 reassigned as a tyrosine' 4664 2 . . 2000-07-08 . original author 'original release date' 4664 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4664 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 20377250 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Sequence-specific Resonance Assignments of Q83, a Lipocalin Highly Expressed in v-myc-transformed Avian Fibroblasts ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of Biomolecular NMR' _Citation.Journal_volume 17 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 177 _Citation.Page_last 178 _Citation.Year 2000 _Citation.Details 'G. Kontaxis and T. Matt contributed equally' 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 Georg Kontaxis . . . 4664 1 2 Theresia Matt . . . 4664 1 3 Wolfgang Schuler . . . 4664 1 4 Bernhard Krautler . . . 4664 1 5 Klaus Bister . . . 4664 1 6 Robert Konrat . . . 4664 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'NMR assignments' 4664 1 'protein structure' 4664 1 'cell proliferation' 4664 1 oncogenes 4664 1 stop_ save_ save_ref-1 _Citation.Sf_category citations _Citation.Sf_framecode ref-1 _Citation.Entry_ID 4664 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8361751 _Citation.Full_citation ; Oncogene 1993 Sep;8(9):2317-24 Suppression in transformed avian fibroblasts of a gene (crp) encoding a cysteine-rich protein containing LIM domains. Weiskirchen R, Bister K ; _Citation.Title 'Suppression in transformed avian fibroblasts of a gene (crp) encoding a cysteine-rich protein containing LIM domains.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Oncogene _Citation.Journal_name_full Oncogene _Citation.Journal_volume 8 _Citation.Journal_issue 9 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0950-9232 _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 2317 _Citation.Page_last 2324 _Citation.Year 1993 _Citation.Details ; Using cDNA subtraction and differential hybridization techniques, a cDNA library derived from normal quail embryo fibroblasts was screened for clones corresponding to genes whose expression was suppressed in v-myc-transformed, as compared with normal, quail embryo fibroblasts. One of the isolated cDNA clones corresponded to a 0.9-kb mRNA that was present in normal quail and chicken embryo fibroblasts, but was virtually absent from all transformed avian cells tested: quail embryo fibroblasts transformed by the v-myc, v-myc/v-mil or v-src oncogenes, cells derived from a methylcholanthrene-induced quail fibrosarcoma or v-myc-transformed chicken macrophages. Nucleotide sequence analysis of the original and supplementary cDNA clones indicated that the corresponding gene encodes a 194 amino acid cysteine-rich protein (M(r) 20,911). A database search revealed that the gene is the avian homolog of a human primary response gene (crp) of unknown function. Both the quail and human CRP proteins contain two copies of a cysteine-rich amino acid sequence motif (LIM) with putative zinc-binding activity that was previously identified in several proteins with presumed regulatory functions essential for cell growth or differentiation. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 R Weiskirchen R. . . 4664 2 2 K Bister K. . . 4664 2 stop_ save_ save_ref-2 _Citation.Sf_category citations _Citation.Sf_framecode ref-2 _Citation.Entry_ID 4664 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8520220 _Citation.Full_citation ; J Biomol NMR 1995 Nov;6(3):277-93 NMRPipe: a multidimensional spectral processing system based on UNIX pipes. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A ; _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. . . 4664 3 2 S Grzesiek S. . . 4664 3 3 'G W' Vuister G. W. . 4664 3 4 G Zhu G. . . 4664 3 5 J Pfeifer J. . . 4664 3 6 A Bax A. . . 4664 3 stop_ save_ save_ref-3 _Citation.Sf_category citations _Citation.Sf_framecode ref-3 _Citation.Entry_ID 4664 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation 'Kraulis, P.J., J. Magn. Reson. (1989) 24, 627-633' _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_Q83 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_Q83 _Assembly.Entry_ID 4664 _Assembly.ID 1 _Assembly.Name 'lipocalin Q83' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4664 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 Q83 1 $Q83 . . . native . . . . . 4664 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 disulfide single . 1 . . CYS 59 59 SG . 1 . 1 CYS 152 152 SG . . . . . . . . . . 4664 1 stop_ loop_ _Entity_deleted_atom.ID _Entity_deleted_atom.Entity_atom_list_ID _Entity_deleted_atom.Entity_assembly_ID _Entity_deleted_atom.Entity_ID _Entity_deleted_atom.Comp_ID _Entity_deleted_atom.Comp_index_ID _Entity_deleted_atom.Seq_ID _Entity_deleted_atom.Atom_ID _Entity_deleted_atom.Auth_entity_assembly_ID _Entity_deleted_atom.Auth_seq_ID _Entity_deleted_atom.Auth_comp_ID _Entity_deleted_atom.Auth_atom_ID _Entity_deleted_atom.Entry_ID _Entity_deleted_atom.Assembly_ID . 1 1 1 CYS 59 59 HG . . . . 4664 1 . 2 1 1 CYS 152 152 HG . . . . 4664 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'lipocalin Q83' system 4664 1 Q83 abbreviation 4664 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Q83 _Entity.Sf_category entity _Entity.Sf_framecode Q83 _Entity.Entry_ID 4664 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Q83 _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 ; MTVPDRSEIAGKWYVVALAS NTEFFLREKDKMKMAMARIS FLGEDELKVSYAVPKPNGCR KWETTFKKTSDDGEVYYSEE AKKKVEVLDTDYKSYAVIYA TRVKDGRTLHMMRLYSRSPE VSPAATAIFRKLAGERNYTD EMVAMLPRQEECTVDEV ; _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 157 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 16682 . Q83 . . . . . 100.00 157 100.00 100.00 2.31e-110 . . . . 4664 1 2 no BMRB 17577 . Q83 . . . . . 100.00 157 100.00 100.00 2.31e-110 . . . . 4664 1 3 no PDB 1JZU . "Cell Transformation By The Myc Oncogene Activates Expression Of A Lipocalin: Analysis Of The Gene (Q83) And Solution Structure " . . . . . 100.00 157 100.00 100.00 2.31e-110 . . . . 4664 1 4 no PDB 2KT4 . "Lipocalin Q83 Is A Siderocalin" . . . . . 100.00 157 100.00 100.00 2.31e-110 . . . . 4664 1 5 no PDB 2LBV . "Siderocalin Q83 Reveals A Dual Ligand Binding Mode" . . . . . 100.00 157 100.00 100.00 2.31e-110 . . . . 4664 1 6 no GB AAF35894 . "lipocalin Q83 [Coturnix coturnix]" . . . . . 99.36 178 100.00 100.00 7.26e-110 . . . . 4664 1 7 no GB AAK31634 . "lipocalin Q83 [Coturnix coturnix]" . . . . . 99.36 178 99.36 100.00 3.14e-109 . . . . 4664 1 8 no SP Q9I9P7 . "RecName: Full=Extracellular fatty acid-binding protein; Short=Ex-FABP; AltName: Full=Lipocalin Q83; Flags: Precursor" . . . . . 99.36 178 100.00 100.00 7.26e-110 . . . . 4664 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Q83 common 4664 1 Q83 abbreviation 4664 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 . MET . 4664 1 2 . THR . 4664 1 3 . VAL . 4664 1 4 . PRO . 4664 1 5 . ASP . 4664 1 6 . ARG . 4664 1 7 . SER . 4664 1 8 . GLU . 4664 1 9 . ILE . 4664 1 10 . ALA . 4664 1 11 . GLY . 4664 1 12 . LYS . 4664 1 13 . TRP . 4664 1 14 . TYR . 4664 1 15 . VAL . 4664 1 16 . VAL . 4664 1 17 . ALA . 4664 1 18 . LEU . 4664 1 19 . ALA . 4664 1 20 . SER . 4664 1 21 . ASN . 4664 1 22 . THR . 4664 1 23 . GLU . 4664 1 24 . PHE . 4664 1 25 . PHE . 4664 1 26 . LEU . 4664 1 27 . ARG . 4664 1 28 . GLU . 4664 1 29 . LYS . 4664 1 30 . ASP . 4664 1 31 . LYS . 4664 1 32 . MET . 4664 1 33 . LYS . 4664 1 34 . MET . 4664 1 35 . ALA . 4664 1 36 . MET . 4664 1 37 . ALA . 4664 1 38 . ARG . 4664 1 39 . ILE . 4664 1 40 . SER . 4664 1 41 . PHE . 4664 1 42 . LEU . 4664 1 43 . GLY . 4664 1 44 . GLU . 4664 1 45 . ASP . 4664 1 46 . GLU . 4664 1 47 . LEU . 4664 1 48 . LYS . 4664 1 49 . VAL . 4664 1 50 . SER . 4664 1 51 . TYR . 4664 1 52 . ALA . 4664 1 53 . VAL . 4664 1 54 . PRO . 4664 1 55 . LYS . 4664 1 56 . PRO . 4664 1 57 . ASN . 4664 1 58 . GLY . 4664 1 59 . CYS . 4664 1 60 . ARG . 4664 1 61 . LYS . 4664 1 62 . TRP . 4664 1 63 . GLU . 4664 1 64 . THR . 4664 1 65 . THR . 4664 1 66 . PHE . 4664 1 67 . LYS . 4664 1 68 . LYS . 4664 1 69 . THR . 4664 1 70 . SER . 4664 1 71 . ASP . 4664 1 72 . ASP . 4664 1 73 . GLY . 4664 1 74 . GLU . 4664 1 75 . VAL . 4664 1 76 . TYR . 4664 1 77 . TYR . 4664 1 78 . SER . 4664 1 79 . GLU . 4664 1 80 . GLU . 4664 1 81 . ALA . 4664 1 82 . LYS . 4664 1 83 . LYS . 4664 1 84 . LYS . 4664 1 85 . VAL . 4664 1 86 . GLU . 4664 1 87 . VAL . 4664 1 88 . LEU . 4664 1 89 . ASP . 4664 1 90 . THR . 4664 1 91 . ASP . 4664 1 92 . TYR . 4664 1 93 . LYS . 4664 1 94 . SER . 4664 1 95 . TYR . 4664 1 96 . ALA . 4664 1 97 . VAL . 4664 1 98 . ILE . 4664 1 99 . TYR . 4664 1 100 . ALA . 4664 1 101 . THR . 4664 1 102 . ARG . 4664 1 103 . VAL . 4664 1 104 . LYS . 4664 1 105 . ASP . 4664 1 106 . GLY . 4664 1 107 . ARG . 4664 1 108 . THR . 4664 1 109 . LEU . 4664 1 110 . HIS . 4664 1 111 . MET . 4664 1 112 . MET . 4664 1 113 . ARG . 4664 1 114 . LEU . 4664 1 115 . TYR . 4664 1 116 . SER . 4664 1 117 . ARG . 4664 1 118 . SER . 4664 1 119 . PRO . 4664 1 120 . GLU . 4664 1 121 . VAL . 4664 1 122 . SER . 4664 1 123 . PRO . 4664 1 124 . ALA . 4664 1 125 . ALA . 4664 1 126 . THR . 4664 1 127 . ALA . 4664 1 128 . ILE . 4664 1 129 . PHE . 4664 1 130 . ARG . 4664 1 131 . LYS . 4664 1 132 . LEU . 4664 1 133 . ALA . 4664 1 134 . GLY . 4664 1 135 . GLU . 4664 1 136 . ARG . 4664 1 137 . ASN . 4664 1 138 . TYR . 4664 1 139 . THR . 4664 1 140 . ASP . 4664 1 141 . GLU . 4664 1 142 . MET . 4664 1 143 . VAL . 4664 1 144 . ALA . 4664 1 145 . MET . 4664 1 146 . LEU . 4664 1 147 . PRO . 4664 1 148 . ARG . 4664 1 149 . GLN . 4664 1 150 . GLU . 4664 1 151 . GLU . 4664 1 152 . CYS . 4664 1 153 . THR . 4664 1 154 . VAL . 4664 1 155 . ASP . 4664 1 156 . GLU . 4664 1 157 . VAL . 4664 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 . MET 1 1 4664 1 . THR 2 2 4664 1 . VAL 3 3 4664 1 . PRO 4 4 4664 1 . ASP 5 5 4664 1 . ARG 6 6 4664 1 . SER 7 7 4664 1 . GLU 8 8 4664 1 . ILE 9 9 4664 1 . ALA 10 10 4664 1 . GLY 11 11 4664 1 . LYS 12 12 4664 1 . TRP 13 13 4664 1 . TYR 14 14 4664 1 . VAL 15 15 4664 1 . VAL 16 16 4664 1 . ALA 17 17 4664 1 . LEU 18 18 4664 1 . ALA 19 19 4664 1 . SER 20 20 4664 1 . ASN 21 21 4664 1 . THR 22 22 4664 1 . GLU 23 23 4664 1 . PHE 24 24 4664 1 . PHE 25 25 4664 1 . LEU 26 26 4664 1 . ARG 27 27 4664 1 . GLU 28 28 4664 1 . LYS 29 29 4664 1 . ASP 30 30 4664 1 . LYS 31 31 4664 1 . MET 32 32 4664 1 . LYS 33 33 4664 1 . MET 34 34 4664 1 . ALA 35 35 4664 1 . MET 36 36 4664 1 . ALA 37 37 4664 1 . ARG 38 38 4664 1 . ILE 39 39 4664 1 . SER 40 40 4664 1 . PHE 41 41 4664 1 . LEU 42 42 4664 1 . GLY 43 43 4664 1 . GLU 44 44 4664 1 . ASP 45 45 4664 1 . GLU 46 46 4664 1 . LEU 47 47 4664 1 . LYS 48 48 4664 1 . VAL 49 49 4664 1 . SER 50 50 4664 1 . TYR 51 51 4664 1 . ALA 52 52 4664 1 . VAL 53 53 4664 1 . PRO 54 54 4664 1 . LYS 55 55 4664 1 . PRO 56 56 4664 1 . ASN 57 57 4664 1 . GLY 58 58 4664 1 . CYS 59 59 4664 1 . ARG 60 60 4664 1 . LYS 61 61 4664 1 . TRP 62 62 4664 1 . GLU 63 63 4664 1 . THR 64 64 4664 1 . THR 65 65 4664 1 . PHE 66 66 4664 1 . LYS 67 67 4664 1 . LYS 68 68 4664 1 . THR 69 69 4664 1 . SER 70 70 4664 1 . ASP 71 71 4664 1 . ASP 72 72 4664 1 . GLY 73 73 4664 1 . GLU 74 74 4664 1 . VAL 75 75 4664 1 . TYR 76 76 4664 1 . TYR 77 77 4664 1 . SER 78 78 4664 1 . GLU 79 79 4664 1 . GLU 80 80 4664 1 . ALA 81 81 4664 1 . LYS 82 82 4664 1 . LYS 83 83 4664 1 . LYS 84 84 4664 1 . VAL 85 85 4664 1 . GLU 86 86 4664 1 . VAL 87 87 4664 1 . LEU 88 88 4664 1 . ASP 89 89 4664 1 . THR 90 90 4664 1 . ASP 91 91 4664 1 . TYR 92 92 4664 1 . LYS 93 93 4664 1 . SER 94 94 4664 1 . TYR 95 95 4664 1 . ALA 96 96 4664 1 . VAL 97 97 4664 1 . ILE 98 98 4664 1 . TYR 99 99 4664 1 . ALA 100 100 4664 1 . THR 101 101 4664 1 . ARG 102 102 4664 1 . VAL 103 103 4664 1 . LYS 104 104 4664 1 . ASP 105 105 4664 1 . GLY 106 106 4664 1 . ARG 107 107 4664 1 . THR 108 108 4664 1 . LEU 109 109 4664 1 . HIS 110 110 4664 1 . MET 111 111 4664 1 . MET 112 112 4664 1 . ARG 113 113 4664 1 . LEU 114 114 4664 1 . TYR 115 115 4664 1 . SER 116 116 4664 1 . ARG 117 117 4664 1 . SER 118 118 4664 1 . PRO 119 119 4664 1 . GLU 120 120 4664 1 . VAL 121 121 4664 1 . SER 122 122 4664 1 . PRO 123 123 4664 1 . ALA 124 124 4664 1 . ALA 125 125 4664 1 . THR 126 126 4664 1 . ALA 127 127 4664 1 . ILE 128 128 4664 1 . PHE 129 129 4664 1 . ARG 130 130 4664 1 . LYS 131 131 4664 1 . LEU 132 132 4664 1 . ALA 133 133 4664 1 . GLY 134 134 4664 1 . GLU 135 135 4664 1 . ARG 136 136 4664 1 . ASN 137 137 4664 1 . TYR 138 138 4664 1 . THR 139 139 4664 1 . ASP 140 140 4664 1 . GLU 141 141 4664 1 . MET 142 142 4664 1 . VAL 143 143 4664 1 . ALA 144 144 4664 1 . MET 145 145 4664 1 . LEU 146 146 4664 1 . PRO 147 147 4664 1 . ARG 148 148 4664 1 . GLN 149 149 4664 1 . GLU 150 150 4664 1 . GLU 151 151 4664 1 . CYS 152 152 4664 1 . THR 153 153 4664 1 . VAL 154 154 4664 1 . ASP 155 155 4664 1 . GLU 156 156 4664 1 . VAL 157 157 4664 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4664 _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 $Q83 . 9091 organism . 'Coturnix coturnix' quail . . Eukaryota Metazoa Coturnix coturnix . . . . . . . . . . . . . . . . . . . . . 4664 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 4664 _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 $Q83 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21(DE3)pLysS . . . . . . . . . . . . plasmid . . pET3d-Q83 . . . . . . 4664 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4664 _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 Q83 '[U-13C; U-15N]' . . 1 $Q83 . . 3.0 . . mM . . . . 4664 1 2 'potassium phosphate' . . . . . . . 20 . . mM . . . . 4664 1 3 'potassium chloride' . . . . . . . 50 . . mM . . . . 4664 1 4 dithiothreitol . . . . . . . 0.5 . . mM . . . . 4664 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 4664 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.4 0.2 pH 4664 1 temperature 299 1 K 4664 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 4664 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectra processing' 4664 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref-2 4664 1 stop_ save_ save_ANSIG _Software.Sf_category software _Software.Sf_framecode ANSIG _Software.Entry_ID 4664 _Software.ID 2 _Software.Name ANSIG _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectra assignment and evaluation' 4664 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $ref-3 4664 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 4664 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model 'Unity Plus' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4664 _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 Plus' . 500 . . . 4664 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 4664 _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 '1H-15N HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 2 HNCO . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 3 HNCA . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 4 CBCA(CO)NNH . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 5 HNCACB . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 6 HCCH-TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 7 '1H-15N TOCSY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 8 '1H-15N NOESY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 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 4664 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 4664 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4664 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4664 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 4664 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 4664 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 4 4 PRO HA H 1 4.12 0.03 . 1 . . . . . . . . 4664 1 2 . 1 1 4 4 PRO HB2 H 1 1.93 0.03 . 2 . . . . . . . . 4664 1 3 . 1 1 4 4 PRO HB3 H 1 1.54 0.03 . 2 . . . . . . . . 4664 1 4 . 1 1 4 4 PRO CA C 13 64.12 0.50 . 1 . . . . . . . . 4664 1 5 . 1 1 4 4 PRO C C 13 176.70 0.50 . 1 . . . . . . . . 4664 1 6 . 1 1 4 4 PRO CB C 13 33.08 0.50 . 1 . . . . . . . . 4664 1 7 . 1 1 5 5 ASP H H 1 8.02 0.03 . 1 . . . . . . . . 4664 1 8 . 1 1 5 5 ASP HA H 1 4.42 0.03 . 1 . . . . . . . . 4664 1 9 . 1 1 5 5 ASP HB2 H 1 2.67 0.03 . 2 . . . . . . . . 4664 1 10 . 1 1 5 5 ASP HB3 H 1 2.50 0.03 . 2 . . . . . . . . 4664 1 11 . 1 1 5 5 ASP CA C 13 54.85 0.50 . 1 . . . . . . . . 4664 1 12 . 1 1 5 5 ASP C C 13 178.28 0.50 . 1 . . . . . . . . 4664 1 13 . 1 1 5 5 ASP CB C 13 42.58 0.50 . 1 . . . . . . . . 4664 1 14 . 1 1 5 5 ASP N N 15 119.93 0.25 . 1 . . . . . . . . 4664 1 15 . 1 1 6 6 ARG H H 1 8.53 0.03 . 1 . . . . . . . . 4664 1 16 . 1 1 6 6 ARG HA H 1 4.04 0.03 . 1 . . . . . . . . 4664 1 17 . 1 1 6 6 ARG HB2 H 1 1.76 0.03 . 2 . . . . . . . . 4664 1 18 . 1 1 6 6 ARG HB3 H 1 1.72 0.03 . 2 . . . . . . . . 4664 1 19 . 1 1 6 6 ARG CA C 13 59.37 0.50 . 1 . . . . . . . . 4664 1 20 . 1 1 6 6 ARG C C 13 178.50 0.50 . 1 . . . . . . . . 4664 1 21 . 1 1 6 6 ARG CB C 13 32.44 0.50 . 1 . . . . . . . . 4664 1 22 . 1 1 6 6 ARG N N 15 125.15 0.25 . 1 . . . . . . . . 4664 1 23 . 1 1 7 7 SER H H 1 8.32 0.03 . 1 . . . . . . . . 4664 1 24 . 1 1 7 7 SER HA H 1 4.09 0.03 . 1 . . . . . . . . 4664 1 25 . 1 1 7 7 SER HB2 H 1 3.85 0.03 . 1 . . . . . . . . 4664 1 26 . 1 1 7 7 SER HB3 H 1 3.85 0.03 . 1 . . . . . . . . 4664 1 27 . 1 1 7 7 SER CA C 13 62.36 0.50 . 1 . . . . . . . . 4664 1 28 . 1 1 7 7 SER C C 13 177.20 0.50 . 1 . . . . . . . . 4664 1 29 . 1 1 7 7 SER CB C 13 63.83 0.50 . 1 . . . . . . . . 4664 1 30 . 1 1 7 7 SER N N 15 115.20 0.25 . 1 . . . . . . . . 4664 1 31 . 1 1 8 8 GLU H H 1 7.90 0.03 . 1 . . . . . . . . 4664 1 32 . 1 1 8 8 GLU HA H 1 4.26 0.03 . 1 . . . . . . . . 4664 1 33 . 1 1 8 8 GLU HB2 H 1 2.22 0.03 . 2 . . . . . . . . 4664 1 34 . 1 1 8 8 GLU HB3 H 1 2.05 0.03 . 2 . . . . . . . . 4664 1 35 . 1 1 8 8 GLU CA C 13 58.54 0.50 . 1 . . . . . . . . 4664 1 36 . 1 1 8 8 GLU C C 13 178.00 0.50 . 1 . . . . . . . . 4664 1 37 . 1 1 8 8 GLU CB C 13 31.09 0.50 . 1 . . . . . . . . 4664 1 38 . 1 1 8 8 GLU N N 15 120.87 0.25 . 1 . . . . . . . . 4664 1 39 . 1 1 9 9 ILE H H 1 7.39 0.03 . 1 . . . . . . . . 4664 1 40 . 1 1 9 9 ILE HA H 1 4.25 0.03 . 1 . . . . . . . . 4664 1 41 . 1 1 9 9 ILE HB H 1 2.04 0.03 . 1 . . . . . . . . 4664 1 42 . 1 1 9 9 ILE CA C 13 63.47 0.50 . 1 . . . . . . . . 4664 1 43 . 1 1 9 9 ILE C C 13 176.10 0.50 . 1 . . . . . . . . 4664 1 44 . 1 1 9 9 ILE CB C 13 40.54 0.50 . 1 . . . . . . . . 4664 1 45 . 1 1 9 9 ILE N N 15 115.00 0.25 . 1 . . . . . . . . 4664 1 46 . 1 1 10 10 ALA H H 1 7.37 0.03 . 1 . . . . . . . . 4664 1 47 . 1 1 10 10 ALA HA H 1 4.08 0.03 . 1 . . . . . . . . 4664 1 48 . 1 1 10 10 ALA HB1 H 1 1.57 0.03 . 1 . . . . . . . . 4664 1 49 . 1 1 10 10 ALA HB2 H 1 1.57 0.03 . 1 . . . . . . . . 4664 1 50 . 1 1 10 10 ALA HB3 H 1 1.57 0.03 . 1 . . . . . . . . 4664 1 51 . 1 1 10 10 ALA CA C 13 53.85 0.50 . 1 . . . . . . . . 4664 1 52 . 1 1 10 10 ALA C C 13 178.40 0.50 . 1 . . . . . . . . 4664 1 53 . 1 1 10 10 ALA CB C 13 20.53 0.50 . 1 . . . . . . . . 4664 1 54 . 1 1 10 10 ALA N N 15 120.68 0.25 . 1 . . . . . . . . 4664 1 55 . 1 1 11 11 GLY H H 1 8.62 0.03 . 1 . . . . . . . . 4664 1 56 . 1 1 11 11 GLY HA2 H 1 4.60 0.03 . 2 . . . . . . . . 4664 1 57 . 1 1 11 11 GLY HA3 H 1 3.62 0.03 . 2 . . . . . . . . 4664 1 58 . 1 1 11 11 GLY CA C 13 45.31 0.50 . 1 . . . . . . . . 4664 1 59 . 1 1 11 11 GLY C C 13 174.70 0.50 . 1 . . . . . . . . 4664 1 60 . 1 1 11 11 GLY N N 15 108.75 0.25 . 1 . . . . . . . . 4664 1 61 . 1 1 12 12 LYS H H 1 8.64 0.03 . 1 . . . . . . . . 4664 1 62 . 1 1 12 12 LYS HA H 1 4.76 0.03 . 1 . . . . . . . . 4664 1 63 . 1 1 12 12 LYS HB2 H 1 1.48 0.03 . 1 . . . . . . . . 4664 1 64 . 1 1 12 12 LYS HB3 H 1 1.48 0.03 . 1 . . . . . . . . 4664 1 65 . 1 1 12 12 LYS CA C 13 58.23 0.50 . 1 . . . . . . . . 4664 1 66 . 1 1 12 12 LYS C C 13 176.90 0.50 . 1 . . . . . . . . 4664 1 67 . 1 1 12 12 LYS CB C 13 34.78 0.50 . 1 . . . . . . . . 4664 1 68 . 1 1 12 12 LYS N N 15 123.32 0.25 . 1 . . . . . . . . 4664 1 69 . 1 1 13 13 TRP H H 1 9.36 0.03 . 1 . . . . . . . . 4664 1 70 . 1 1 13 13 TRP HA H 1 4.55 0.03 . 1 . . . . . . . . 4664 1 71 . 1 1 13 13 TRP HB2 H 1 3.25 0.03 . 2 . . . . . . . . 4664 1 72 . 1 1 13 13 TRP HB3 H 1 2.68 0.03 . 2 . . . . . . . . 4664 1 73 . 1 1 13 13 TRP CA C 13 57.69 0.50 . 1 . . . . . . . . 4664 1 74 . 1 1 13 13 TRP C C 13 174.30 0.50 . 1 . . . . . . . . 4664 1 75 . 1 1 13 13 TRP CB C 13 35.17 0.50 . 1 . . . . . . . . 4664 1 76 . 1 1 13 13 TRP N N 15 126.94 0.25 . 1 . . . . . . . . 4664 1 77 . 1 1 14 14 TYR H H 1 9.29 0.03 . 1 . . . . . . . . 4664 1 78 . 1 1 14 14 TYR HA H 1 4.94 0.03 . 1 . . . . . . . . 4664 1 79 . 1 1 14 14 TYR HB2 H 1 2.85 0.03 . 2 . . . . . . . . 4664 1 80 . 1 1 14 14 TYR HB3 H 1 2.72 0.03 . 2 . . . . . . . . 4664 1 81 . 1 1 14 14 TYR CA C 13 58.93 0.50 . 1 . . . . . . . . 4664 1 82 . 1 1 14 14 TYR C C 13 176.40 0.50 . 1 . . . . . . . . 4664 1 83 . 1 1 14 14 TYR CB C 13 41.49 0.50 . 1 . . . . . . . . 4664 1 84 . 1 1 14 14 TYR N N 15 119.21 0.25 . 1 . . . . . . . . 4664 1 85 . 1 1 15 15 VAL H H 1 8.89 0.03 . 1 . . . . . . . . 4664 1 86 . 1 1 15 15 VAL HA H 1 3.95 0.03 . 1 . . . . . . . . 4664 1 87 . 1 1 15 15 VAL HB H 1 1.88 0.03 . 1 . . . . . . . . 4664 1 88 . 1 1 15 15 VAL CA C 13 62.88 0.50 . 1 . . . . . . . . 4664 1 89 . 1 1 15 15 VAL C C 13 176.50 0.50 . 1 . . . . . . . . 4664 1 90 . 1 1 15 15 VAL CB C 13 32.48 0.50 . 1 . . . . . . . . 4664 1 91 . 1 1 15 15 VAL N N 15 125.01 0.25 . 1 . . . . . . . . 4664 1 92 . 1 1 16 16 VAL H H 1 8.37 0.03 . 1 . . . . . . . . 4664 1 93 . 1 1 16 16 VAL HA H 1 4.55 0.03 . 1 . . . . . . . . 4664 1 94 . 1 1 16 16 VAL HB H 1 2.37 0.03 . 1 . . . . . . . . 4664 1 95 . 1 1 16 16 VAL CA C 13 62.31 0.50 . 1 . . . . . . . . 4664 1 96 . 1 1 16 16 VAL C C 13 176.90 0.50 . 1 . . . . . . . . 4664 1 97 . 1 1 16 16 VAL CB C 13 33.48 0.50 . 1 . . . . . . . . 4664 1 98 . 1 1 16 16 VAL N N 15 115.31 0.25 . 1 . . . . . . . . 4664 1 99 . 1 1 17 17 ALA H H 1 7.52 0.03 . 1 . . . . . . . . 4664 1 100 . 1 1 17 17 ALA HA H 1 5.19 0.03 . 1 . . . . . . . . 4664 1 101 . 1 1 17 17 ALA HB1 H 1 0.90 0.03 . 1 . . . . . . . . 4664 1 102 . 1 1 17 17 ALA HB2 H 1 0.90 0.03 . 1 . . . . . . . . 4664 1 103 . 1 1 17 17 ALA HB3 H 1 0.90 0.03 . 1 . . . . . . . . 4664 1 104 . 1 1 17 17 ALA CA C 13 53.12 0.50 . 1 . . . . . . . . 4664 1 105 . 1 1 17 17 ALA C C 13 179.90 0.50 . 1 . . . . . . . . 4664 1 106 . 1 1 17 17 ALA CB C 13 24.17 0.50 . 1 . . . . . . . . 4664 1 107 . 1 1 17 17 ALA N N 15 123.65 0.25 . 1 . . . . . . . . 4664 1 108 . 1 1 18 18 LEU H H 1 8.50 0.03 . 1 . . . . . . . . 4664 1 109 . 1 1 18 18 LEU HA H 1 5.40 0.03 . 1 . . . . . . . . 4664 1 110 . 1 1 18 18 LEU CA C 13 54.07 0.50 . 1 . . . . . . . . 4664 1 111 . 1 1 18 18 LEU C C 13 177.20 0.50 . 1 . . . . . . . . 4664 1 112 . 1 1 18 18 LEU CB C 13 50.03 0.50 . 1 . . . . . . . . 4664 1 113 . 1 1 18 18 LEU N N 15 118.93 0.25 . 1 . . . . . . . . 4664 1 114 . 1 1 19 19 ALA H H 1 8.26 0.03 . 1 . . . . . . . . 4664 1 115 . 1 1 19 19 ALA HA H 1 5.35 0.03 . 1 . . . . . . . . 4664 1 116 . 1 1 19 19 ALA HB1 H 1 0.71 0.03 . 1 . . . . . . . . 4664 1 117 . 1 1 19 19 ALA HB2 H 1 0.71 0.03 . 1 . . . . . . . . 4664 1 118 . 1 1 19 19 ALA HB3 H 1 0.71 0.03 . 1 . . . . . . . . 4664 1 119 . 1 1 19 19 ALA CA C 13 52.77 0.50 . 1 . . . . . . . . 4664 1 120 . 1 1 19 19 ALA C C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 121 . 1 1 19 19 ALA CB C 13 23.21 0.50 . 1 . . . . . . . . 4664 1 122 . 1 1 19 19 ALA N N 15 120.95 0.25 . 1 . . . . . . . . 4664 1 123 . 1 1 20 20 SER H H 1 7.34 0.03 . 1 . . . . . . . . 4664 1 124 . 1 1 20 20 SER HA H 1 3.77 0.03 . 1 . . . . . . . . 4664 1 125 . 1 1 20 20 SER HB2 H 1 3.53 0.03 . 1 . . . . . . . . 4664 1 126 . 1 1 20 20 SER HB3 H 1 3.53 0.03 . 1 . . . . . . . . 4664 1 127 . 1 1 20 20 SER CA C 13 57.29 0.50 . 1 . . . . . . . . 4664 1 128 . 1 1 20 20 SER C C 13 171.80 0.50 . 1 . . . . . . . . 4664 1 129 . 1 1 20 20 SER CB C 13 64.27 0.50 . 1 . . . . . . . . 4664 1 130 . 1 1 20 20 SER N N 15 114.76 0.25 . 1 . . . . . . . . 4664 1 131 . 1 1 21 21 ASN H H 1 7.85 0.03 . 1 . . . . . . . . 4664 1 132 . 1 1 21 21 ASN HA H 1 5.14 0.03 . 1 . . . . . . . . 4664 1 133 . 1 1 21 21 ASN HB2 H 1 3.40 0.03 . 2 . . . . . . . . 4664 1 134 . 1 1 21 21 ASN HB3 H 1 3.13 0.03 . 2 . . . . . . . . 4664 1 135 . 1 1 21 21 ASN CA C 13 52.37 0.50 . 1 . . . . . . . . 4664 1 136 . 1 1 21 21 ASN C C 13 177.60 0.50 . 1 . . . . . . . . 4664 1 137 . 1 1 21 21 ASN CB C 13 40.33 0.50 . 1 . . . . . . . . 4664 1 138 . 1 1 21 21 ASN N N 15 117.99 0.25 . 1 . . . . . . . . 4664 1 139 . 1 1 22 22 THR H H 1 8.00 0.03 . 1 . . . . . . . . 4664 1 140 . 1 1 22 22 THR HA H 1 4.33 0.03 . 1 . . . . . . . . 4664 1 141 . 1 1 22 22 THR CA C 13 63.13 0.50 . 1 . . . . . . . . 4664 1 142 . 1 1 22 22 THR C C 13 175.90 0.50 . 1 . . . . . . . . 4664 1 143 . 1 1 22 22 THR CB C 13 71.56 0.50 . 1 . . . . . . . . 4664 1 144 . 1 1 22 22 THR N N 15 112.87 0.25 . 1 . . . . . . . . 4664 1 145 . 1 1 23 23 GLU H H 1 8.89 0.03 . 1 . . . . . . . . 4664 1 146 . 1 1 23 23 GLU HA H 1 4.68 0.03 . 1 . . . . . . . . 4664 1 147 . 1 1 23 23 GLU CA C 13 61.30 0.50 . 1 . . . . . . . . 4664 1 148 . 1 1 23 23 GLU CB C 13 30.31 0.50 . 1 . . . . . . . . 4664 1 149 . 1 1 23 23 GLU N N 15 123.46 0.25 . 1 . . . . . . . . 4664 1 150 . 1 1 26 26 LEU CA C 13 58.68 0.50 . 1 . . . . . . . . 4664 1 151 . 1 1 26 26 LEU C C 13 180.30 0.50 . 1 . . . . . . . . 4664 1 152 . 1 1 26 26 LEU CB C 13 41.91 0.50 . 1 . . . . . . . . 4664 1 153 . 1 1 27 27 ARG H H 1 7.63 0.03 . 1 . . . . . . . . 4664 1 154 . 1 1 27 27 ARG HA H 1 4.06 0.03 . 1 . . . . . . . . 4664 1 155 . 1 1 27 27 ARG HB2 H 1 1.74 0.03 . 1 . . . . . . . . 4664 1 156 . 1 1 27 27 ARG HB3 H 1 1.74 0.03 . 1 . . . . . . . . 4664 1 157 . 1 1 27 27 ARG CA C 13 59.10 0.50 . 1 . . . . . . . . 4664 1 158 . 1 1 27 27 ARG C C 13 179.40 0.50 . 1 . . . . . . . . 4664 1 159 . 1 1 27 27 ARG CB C 13 32.03 0.50 . 1 . . . . . . . . 4664 1 160 . 1 1 27 27 ARG N N 15 117.67 0.25 . 1 . . . . . . . . 4664 1 161 . 1 1 28 28 GLU H H 1 7.55 0.03 . 1 . . . . . . . . 4664 1 162 . 1 1 28 28 GLU HA H 1 4.29 0.03 . 1 . . . . . . . . 4664 1 163 . 1 1 28 28 GLU CA C 13 56.75 0.50 . 1 . . . . . . . . 4664 1 164 . 1 1 28 28 GLU C C 13 179.40 0.50 . 1 . . . . . . . . 4664 1 165 . 1 1 28 28 GLU CB C 13 30.93 0.50 . 1 . . . . . . . . 4664 1 166 . 1 1 28 28 GLU N N 15 116.73 0.25 . 1 . . . . . . . . 4664 1 167 . 1 1 29 29 LYS H H 1 7.80 0.03 . 1 . . . . . . . . 4664 1 168 . 1 1 29 29 LYS CA C 13 59.93 0.50 . 1 . . . . . . . . 4664 1 169 . 1 1 29 29 LYS C C 13 178.80 0.50 . 1 . . . . . . . . 4664 1 170 . 1 1 29 29 LYS CB C 13 31.45 0.50 . 1 . . . . . . . . 4664 1 171 . 1 1 29 29 LYS N N 15 121.49 0.25 . 1 . . . . . . . . 4664 1 172 . 1 1 30 30 ASP H H 1 8.29 0.03 . 1 . . . . . . . . 4664 1 173 . 1 1 30 30 ASP HA H 1 4.30 0.03 . 1 . . . . . . . . 4664 1 174 . 1 1 30 30 ASP HB2 H 1 2.59 0.03 . 2 . . . . . . . . 4664 1 175 . 1 1 30 30 ASP HB3 H 1 2.53 0.03 . 2 . . . . . . . . 4664 1 176 . 1 1 30 30 ASP CA C 13 57.11 0.50 . 1 . . . . . . . . 4664 1 177 . 1 1 30 30 ASP C C 13 178.10 0.50 . 1 . . . . . . . . 4664 1 178 . 1 1 30 30 ASP CB C 13 40.59 0.50 . 1 . . . . . . . . 4664 1 179 . 1 1 30 30 ASP N N 15 119.60 0.25 . 1 . . . . . . . . 4664 1 180 . 1 1 31 31 LYS H H 1 8.01 0.03 . 1 . . . . . . . . 4664 1 181 . 1 1 31 31 LYS HA H 1 4.29 0.03 . 1 . . . . . . . . 4664 1 182 . 1 1 31 31 LYS HB2 H 1 1.88 0.03 . 1 . . . . . . . . 4664 1 183 . 1 1 31 31 LYS HB3 H 1 1.88 0.03 . 1 . . . . . . . . 4664 1 184 . 1 1 31 31 LYS CA C 13 56.94 0.50 . 1 . . . . . . . . 4664 1 185 . 1 1 31 31 LYS C C 13 178.20 0.50 . 1 . . . . . . . . 4664 1 186 . 1 1 31 31 LYS CB C 13 34.15 0.50 . 1 . . . . . . . . 4664 1 187 . 1 1 31 31 LYS N N 15 118.77 0.25 . 1 . . . . . . . . 4664 1 188 . 1 1 32 32 MET H H 1 7.13 0.03 . 1 . . . . . . . . 4664 1 189 . 1 1 32 32 MET HA H 1 4.43 0.03 . 1 . . . . . . . . 4664 1 190 . 1 1 32 32 MET HB2 H 1 2.07 0.03 . 1 . . . . . . . . 4664 1 191 . 1 1 32 32 MET HB3 H 1 2.07 0.03 . 1 . . . . . . . . 4664 1 192 . 1 1 32 32 MET CA C 13 57.92 0.50 . 1 . . . . . . . . 4664 1 193 . 1 1 32 32 MET C C 13 177.30 0.50 . 1 . . . . . . . . 4664 1 194 . 1 1 32 32 MET CB C 13 33.55 0.50 . 1 . . . . . . . . 4664 1 195 . 1 1 32 32 MET N N 15 121.09 0.25 . 1 . . . . . . . . 4664 1 196 . 1 1 33 33 LYS H H 1 8.45 0.03 . 1 . . . . . . . . 4664 1 197 . 1 1 33 33 LYS HA H 1 4.56 0.03 . 1 . . . . . . . . 4664 1 198 . 1 1 33 33 LYS HB2 H 1 1.59 0.03 . 1 . . . . . . . . 4664 1 199 . 1 1 33 33 LYS HB3 H 1 1.59 0.03 . 1 . . . . . . . . 4664 1 200 . 1 1 33 33 LYS CA C 13 55.91 0.50 . 1 . . . . . . . . 4664 1 201 . 1 1 33 33 LYS C C 13 174.00 0.50 . 1 . . . . . . . . 4664 1 202 . 1 1 33 33 LYS CB C 13 39.29 0.50 . 1 . . . . . . . . 4664 1 203 . 1 1 33 33 LYS N N 15 120.98 0.25 . 1 . . . . . . . . 4664 1 204 . 1 1 34 34 MET H H 1 8.24 0.03 . 1 . . . . . . . . 4664 1 205 . 1 1 34 34 MET HA H 1 4.31 0.03 . 1 . . . . . . . . 4664 1 206 . 1 1 34 34 MET CA C 13 59.52 0.50 . 1 . . . . . . . . 4664 1 207 . 1 1 34 34 MET C C 13 174.80 0.50 . 1 . . . . . . . . 4664 1 208 . 1 1 34 34 MET CB C 13 35.74 0.50 . 1 . . . . . . . . 4664 1 209 . 1 1 34 34 MET N N 15 119.05 0.25 . 1 . . . . . . . . 4664 1 210 . 1 1 35 35 ALA H H 1 7.33 0.03 . 1 . . . . . . . . 4664 1 211 . 1 1 35 35 ALA HA H 1 5.19 0.03 . 1 . . . . . . . . 4664 1 212 . 1 1 35 35 ALA HB1 H 1 1.78 0.03 . 1 . . . . . . . . 4664 1 213 . 1 1 35 35 ALA HB2 H 1 1.78 0.03 . 1 . . . . . . . . 4664 1 214 . 1 1 35 35 ALA HB3 H 1 1.78 0.03 . 1 . . . . . . . . 4664 1 215 . 1 1 35 35 ALA CA C 13 50.61 0.50 . 1 . . . . . . . . 4664 1 216 . 1 1 35 35 ALA C C 13 177.20 0.50 . 1 . . . . . . . . 4664 1 217 . 1 1 35 35 ALA CB C 13 23.82 0.50 . 1 . . . . . . . . 4664 1 218 . 1 1 35 35 ALA N N 15 126.73 0.25 . 1 . . . . . . . . 4664 1 219 . 1 1 36 36 MET H H 1 8.80 0.03 . 1 . . . . . . . . 4664 1 220 . 1 1 36 36 MET HA H 1 5.13 0.03 . 1 . . . . . . . . 4664 1 221 . 1 1 36 36 MET HB2 H 1 1.83 0.03 . 1 . . . . . . . . 4664 1 222 . 1 1 36 36 MET HB3 H 1 1.83 0.03 . 1 . . . . . . . . 4664 1 223 . 1 1 36 36 MET CA C 13 56.14 0.50 . 1 . . . . . . . . 4664 1 224 . 1 1 36 36 MET C C 13 173.50 0.50 . 1 . . . . . . . . 4664 1 225 . 1 1 36 36 MET CB C 13 39.48 0.50 . 1 . . . . . . . . 4664 1 226 . 1 1 36 36 MET N N 15 117.94 0.25 . 1 . . . . . . . . 4664 1 227 . 1 1 37 37 ALA H H 1 8.89 0.03 . 1 . . . . . . . . 4664 1 228 . 1 1 37 37 ALA HA H 1 5.32 0.03 . 1 . . . . . . . . 4664 1 229 . 1 1 37 37 ALA HB1 H 1 1.01 0.03 . 1 . . . . . . . . 4664 1 230 . 1 1 37 37 ALA HB2 H 1 1.01 0.03 . 1 . . . . . . . . 4664 1 231 . 1 1 37 37 ALA HB3 H 1 1.01 0.03 . 1 . . . . . . . . 4664 1 232 . 1 1 37 37 ALA CA C 13 51.08 0.50 . 1 . . . . . . . . 4664 1 233 . 1 1 37 37 ALA C C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 234 . 1 1 37 37 ALA CB C 13 24.27 0.50 . 1 . . . . . . . . 4664 1 235 . 1 1 37 37 ALA N N 15 122.70 0.25 . 1 . . . . . . . . 4664 1 236 . 1 1 38 38 ARG H H 1 9.14 0.03 . 1 . . . . . . . . 4664 1 237 . 1 1 38 38 ARG HA H 1 5.02 0.03 . 1 . . . . . . . . 4664 1 238 . 1 1 38 38 ARG CA C 13 55.29 0.50 . 1 . . . . . . . . 4664 1 239 . 1 1 38 38 ARG C C 13 176.20 0.50 . 1 . . . . . . . . 4664 1 240 . 1 1 38 38 ARG CB C 13 34.36 0.50 . 1 . . . . . . . . 4664 1 241 . 1 1 38 38 ARG N N 15 121.44 0.25 . 1 . . . . . . . . 4664 1 242 . 1 1 39 39 ILE H H 1 8.85 0.03 . 1 . . . . . . . . 4664 1 243 . 1 1 39 39 ILE HA H 1 4.92 0.03 . 1 . . . . . . . . 4664 1 244 . 1 1 39 39 ILE HB H 1 1.44 0.03 . 1 . . . . . . . . 4664 1 245 . 1 1 39 39 ILE CA C 13 60.11 0.50 . 1 . . . . . . . . 4664 1 246 . 1 1 39 39 ILE C C 13 176.10 0.50 . 1 . . . . . . . . 4664 1 247 . 1 1 39 39 ILE CB C 13 41.27 0.50 . 1 . . . . . . . . 4664 1 248 . 1 1 39 39 ILE N N 15 126.21 0.25 . 1 . . . . . . . . 4664 1 249 . 1 1 40 40 SER H H 1 8.66 0.03 . 1 . . . . . . . . 4664 1 250 . 1 1 40 40 SER HA H 1 4.55 0.03 . 1 . . . . . . . . 4664 1 251 . 1 1 40 40 SER HB2 H 1 3.69 0.03 . 2 . . . . . . . . 4664 1 252 . 1 1 40 40 SER HB3 H 1 3.57 0.03 . 2 . . . . . . . . 4664 1 253 . 1 1 40 40 SER CA C 13 57.95 0.50 . 1 . . . . . . . . 4664 1 254 . 1 1 40 40 SER C C 13 173.00 0.50 . 1 . . . . . . . . 4664 1 255 . 1 1 40 40 SER CB C 13 66.30 0.50 . 1 . . . . . . . . 4664 1 256 . 1 1 40 40 SER N N 15 121.80 0.25 . 1 . . . . . . . . 4664 1 257 . 1 1 41 41 PHE H H 1 8.96 0.03 . 1 . . . . . . . . 4664 1 258 . 1 1 41 41 PHE HA H 1 4.62 0.03 . 1 . . . . . . . . 4664 1 259 . 1 1 41 41 PHE HB2 H 1 3.17 0.03 . 2 . . . . . . . . 4664 1 260 . 1 1 41 41 PHE HB3 H 1 2.80 0.03 . 2 . . . . . . . . 4664 1 261 . 1 1 41 41 PHE CA C 13 59.92 0.50 . 1 . . . . . . . . 4664 1 262 . 1 1 41 41 PHE C C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 263 . 1 1 41 41 PHE CB C 13 40.97 0.50 . 1 . . . . . . . . 4664 1 264 . 1 1 41 41 PHE N N 15 123.14 0.25 . 1 . . . . . . . . 4664 1 265 . 1 1 42 42 LEU H H 1 8.42 0.03 . 1 . . . . . . . . 4664 1 266 . 1 1 42 42 LEU HA H 1 4.53 0.03 . 1 . . . . . . . . 4664 1 267 . 1 1 42 42 LEU HB2 H 1 1.55 0.03 . 2 . . . . . . . . 4664 1 268 . 1 1 42 42 LEU HB3 H 1 1.38 0.03 . 2 . . . . . . . . 4664 1 269 . 1 1 42 42 LEU CA C 13 55.45 0.50 . 1 . . . . . . . . 4664 1 270 . 1 1 42 42 LEU C C 13 177.30 0.50 . 1 . . . . . . . . 4664 1 271 . 1 1 42 42 LEU CB C 13 43.86 0.50 . 1 . . . . . . . . 4664 1 272 . 1 1 42 42 LEU N N 15 126.05 0.25 . 1 . . . . . . . . 4664 1 273 . 1 1 43 43 GLY H H 1 8.25 0.03 . 1 . . . . . . . . 4664 1 274 . 1 1 43 43 GLY HA2 H 1 4.03 0.03 . 1 . . . . . . . . 4664 1 275 . 1 1 43 43 GLY HA3 H 1 4.03 0.03 . 1 . . . . . . . . 4664 1 276 . 1 1 43 43 GLY CA C 13 45.94 0.50 . 1 . . . . . . . . 4664 1 277 . 1 1 43 43 GLY C C 13 174.80 0.50 . 1 . . . . . . . . 4664 1 278 . 1 1 43 43 GLY N N 15 109.65 0.25 . 1 . . . . . . . . 4664 1 279 . 1 1 44 44 GLU H H 1 8.81 0.03 . 1 . . . . . . . . 4664 1 280 . 1 1 44 44 GLU HA H 1 4.06 0.03 . 1 . . . . . . . . 4664 1 281 . 1 1 44 44 GLU HB2 H 1 1.93 0.03 . 1 . . . . . . . . 4664 1 282 . 1 1 44 44 GLU HB3 H 1 1.93 0.03 . 1 . . . . . . . . 4664 1 283 . 1 1 44 44 GLU CA C 13 59.55 0.50 . 1 . . . . . . . . 4664 1 284 . 1 1 44 44 GLU C C 13 178.30 0.50 . 1 . . . . . . . . 4664 1 285 . 1 1 44 44 GLU CB C 13 30.86 0.50 . 1 . . . . . . . . 4664 1 286 . 1 1 44 44 GLU N N 15 121.22 0.25 . 1 . . . . . . . . 4664 1 287 . 1 1 45 45 ASP H H 1 8.38 0.03 . 1 . . . . . . . . 4664 1 288 . 1 1 45 45 ASP HA H 1 4.82 0.03 . 1 . . . . . . . . 4664 1 289 . 1 1 45 45 ASP HB2 H 1 2.95 0.03 . 2 . . . . . . . . 4664 1 290 . 1 1 45 45 ASP HB3 H 1 2.74 0.03 . 2 . . . . . . . . 4664 1 291 . 1 1 45 45 ASP CA C 13 54.91 0.50 . 1 . . . . . . . . 4664 1 292 . 1 1 45 45 ASP C C 13 175.60 0.50 . 1 . . . . . . . . 4664 1 293 . 1 1 45 45 ASP CB C 13 42.81 0.50 . 1 . . . . . . . . 4664 1 294 . 1 1 45 45 ASP N N 15 115.82 0.25 . 1 . . . . . . . . 4664 1 295 . 1 1 46 46 GLU H H 1 7.38 0.03 . 1 . . . . . . . . 4664 1 296 . 1 1 46 46 GLU HA H 1 5.46 0.03 . 1 . . . . . . . . 4664 1 297 . 1 1 46 46 GLU HB2 H 1 1.94 0.03 . 1 . . . . . . . . 4664 1 298 . 1 1 46 46 GLU HB3 H 1 1.94 0.03 . 1 . . . . . . . . 4664 1 299 . 1 1 46 46 GLU CA C 13 56.45 0.50 . 1 . . . . . . . . 4664 1 300 . 1 1 46 46 GLU C C 13 176.04 0.50 . 1 . . . . . . . . 4664 1 301 . 1 1 46 46 GLU CB C 13 34.83 0.50 . 1 . . . . . . . . 4664 1 302 . 1 1 46 46 GLU N N 15 118.62 0.25 . 1 . . . . . . . . 4664 1 303 . 1 1 47 47 LEU H H 1 9.04 0.03 . 1 . . . . . . . . 4664 1 304 . 1 1 47 47 LEU HA H 1 4.80 0.03 . 1 . . . . . . . . 4664 1 305 . 1 1 47 47 LEU CA C 13 55.06 0.50 . 1 . . . . . . . . 4664 1 306 . 1 1 47 47 LEU C C 13 174.80 0.50 . 1 . . . . . . . . 4664 1 307 . 1 1 47 47 LEU N N 15 125.22 0.25 . 1 . . . . . . . . 4664 1 308 . 1 1 48 48 LYS H H 1 8.93 0.03 . 1 . . . . . . . . 4664 1 309 . 1 1 48 48 LYS HA H 1 4.88 0.03 . 1 . . . . . . . . 4664 1 310 . 1 1 48 48 LYS CA C 13 56.17 0.50 . 1 . . . . . . . . 4664 1 311 . 1 1 48 48 LYS C C 13 175.40 0.50 . 1 . . . . . . . . 4664 1 312 . 1 1 48 48 LYS CB C 13 35.63 0.50 . 1 . . . . . . . . 4664 1 313 . 1 1 48 48 LYS N N 15 125.15 0.25 . 1 . . . . . . . . 4664 1 314 . 1 1 49 49 VAL H H 1 8.80 0.03 . 1 . . . . . . . . 4664 1 315 . 1 1 49 49 VAL HA H 1 4.43 0.03 . 1 . . . . . . . . 4664 1 316 . 1 1 49 49 VAL HB H 1 1.57 0.03 . 1 . . . . . . . . 4664 1 317 . 1 1 49 49 VAL CA C 13 61.58 0.50 . 1 . . . . . . . . 4664 1 318 . 1 1 49 49 VAL C C 13 174.70 0.50 . 1 . . . . . . . . 4664 1 319 . 1 1 49 49 VAL CB C 13 35.39 0.50 . 1 . . . . . . . . 4664 1 320 . 1 1 49 49 VAL N N 15 127.46 0.25 . 1 . . . . . . . . 4664 1 321 . 1 1 50 50 SER H H 1 8.26 0.03 . 1 . . . . . . . . 4664 1 322 . 1 1 50 50 SER HA H 1 4.76 0.03 . 1 . . . . . . . . 4664 1 323 . 1 1 50 50 SER HB2 H 1 3.83 0.03 . 2 . . . . . . . . 4664 1 324 . 1 1 50 50 SER HB3 H 1 3.41 0.03 . 2 . . . . . . . . 4664 1 325 . 1 1 50 50 SER CA C 13 57.17 0.50 . 1 . . . . . . . . 4664 1 326 . 1 1 50 50 SER C C 13 173.80 0.50 . 1 . . . . . . . . 4664 1 327 . 1 1 50 50 SER CB C 13 64.99 0.50 . 1 . . . . . . . . 4664 1 328 . 1 1 50 50 SER N N 15 121.67 0.25 . 1 . . . . . . . . 4664 1 329 . 1 1 51 51 TYR H H 1 8.90 0.03 . 1 . . . . . . . . 4664 1 330 . 1 1 51 51 TYR HA H 1 4.77 0.03 . 1 . . . . . . . . 4664 1 331 . 1 1 51 51 TYR HB2 H 1 3.18 0.03 . 2 . . . . . . . . 4664 1 332 . 1 1 51 51 TYR HB3 H 1 3.13 0.03 . 2 . . . . . . . . 4664 1 333 . 1 1 51 51 TYR CA C 13 58.11 0.50 . 1 . . . . . . . . 4664 1 334 . 1 1 51 51 TYR C C 13 177.90 0.50 . 1 . . . . . . . . 4664 1 335 . 1 1 51 51 TYR CB C 13 42.42 0.50 . 1 . . . . . . . . 4664 1 336 . 1 1 51 51 TYR N N 15 123.02 0.25 . 1 . . . . . . . . 4664 1 337 . 1 1 52 52 ALA H H 1 8.50 0.03 . 1 . . . . . . . . 4664 1 338 . 1 1 52 52 ALA HA H 1 4.81 0.03 . 1 . . . . . . . . 4664 1 339 . 1 1 52 52 ALA HB1 H 1 0.87 0.03 . 1 . . . . . . . . 4664 1 340 . 1 1 52 52 ALA HB2 H 1 0.87 0.03 . 1 . . . . . . . . 4664 1 341 . 1 1 52 52 ALA HB3 H 1 0.87 0.03 . 1 . . . . . . . . 4664 1 342 . 1 1 52 52 ALA CA C 13 52.98 0.50 . 1 . . . . . . . . 4664 1 343 . 1 1 52 52 ALA C C 13 175.90 0.50 . 1 . . . . . . . . 4664 1 344 . 1 1 52 52 ALA CB C 13 21.87 0.50 . 1 . . . . . . . . 4664 1 345 . 1 1 52 52 ALA N N 15 124.49 0.25 . 1 . . . . . . . . 4664 1 346 . 1 1 53 53 VAL H H 1 9.06 0.03 . 1 . . . . . . . . 4664 1 347 . 1 1 53 53 VAL HA H 1 4.64 0.03 . 1 . . . . . . . . 4664 1 348 . 1 1 53 53 VAL HB H 1 1.73 0.03 . 1 . . . . . . . . 4664 1 349 . 1 1 53 53 VAL CA C 13 59.29 0.50 . 1 . . . . . . . . 4664 1 350 . 1 1 53 53 VAL CB C 13 36.71 0.50 . 1 . . . . . . . . 4664 1 351 . 1 1 53 53 VAL N N 15 125.02 0.25 . 1 . . . . . . . . 4664 1 352 . 1 1 56 56 PRO CA C 13 66.40 0.50 . 1 . . . . . . . . 4664 1 353 . 1 1 56 56 PRO C C 13 178.20 0.50 . 1 . . . . . . . . 4664 1 354 . 1 1 56 56 PRO CB C 13 32.43 0.50 . 1 . . . . . . . . 4664 1 355 . 1 1 57 57 ASN H H 1 8.25 0.03 . 1 . . . . . . . . 4664 1 356 . 1 1 57 57 ASN HA H 1 4.65 0.03 . 1 . . . . . . . . 4664 1 357 . 1 1 57 57 ASN HB2 H 1 2.79 0.03 . 1 . . . . . . . . 4664 1 358 . 1 1 57 57 ASN HB3 H 1 2.79 0.03 . 1 . . . . . . . . 4664 1 359 . 1 1 57 57 ASN CA C 13 53.91 0.50 . 1 . . . . . . . . 4664 1 360 . 1 1 57 57 ASN C C 13 175.90 0.50 . 1 . . . . . . . . 4664 1 361 . 1 1 57 57 ASN CB C 13 39.21 0.50 . 1 . . . . . . . . 4664 1 362 . 1 1 57 57 ASN N N 15 114.85 0.25 . 1 . . . . . . . . 4664 1 363 . 1 1 58 58 GLY H H 1 7.70 0.03 . 1 . . . . . . . . 4664 1 364 . 1 1 58 58 GLY HA2 H 1 4.06 0.03 . 2 . . . . . . . . 4664 1 365 . 1 1 58 58 GLY HA3 H 1 3.94 0.03 . 2 . . . . . . . . 4664 1 366 . 1 1 58 58 GLY CA C 13 47.03 0.50 . 1 . . . . . . . . 4664 1 367 . 1 1 58 58 GLY N N 15 107.32 0.25 . 1 . . . . . . . . 4664 1 368 . 1 1 61 61 LYS HA H 1 5.40 0.03 . 1 . . . . . . . . 4664 1 369 . 1 1 61 61 LYS CA C 13 56.14 0.50 . 1 . . . . . . . . 4664 1 370 . 1 1 61 61 LYS C C 13 177.00 0.50 . 1 . . . . . . . . 4664 1 371 . 1 1 61 61 LYS CB C 13 36.25 0.50 . 1 . . . . . . . . 4664 1 372 . 1 1 62 62 TRP H H 1 7.95 0.03 . 1 . . . . . . . . 4664 1 373 . 1 1 62 62 TRP HA H 1 4.78 0.03 . 1 . . . . . . . . 4664 1 374 . 1 1 62 62 TRP HB2 H 1 3.15 0.03 . 1 . . . . . . . . 4664 1 375 . 1 1 62 62 TRP HB3 H 1 3.15 0.03 . 1 . . . . . . . . 4664 1 376 . 1 1 62 62 TRP CA C 13 57.88 0.50 . 1 . . . . . . . . 4664 1 377 . 1 1 62 62 TRP C C 13 172.80 0.50 . 1 . . . . . . . . 4664 1 378 . 1 1 62 62 TRP CB C 13 31.69 0.50 . 1 . . . . . . . . 4664 1 379 . 1 1 62 62 TRP N N 15 122.97 0.25 . 1 . . . . . . . . 4664 1 380 . 1 1 63 63 GLU H H 1 8.29 0.03 . 1 . . . . . . . . 4664 1 381 . 1 1 63 63 GLU HA H 1 5.53 0.03 . 1 . . . . . . . . 4664 1 382 . 1 1 63 63 GLU HB2 H 1 1.77 0.03 . 1 . . . . . . . . 4664 1 383 . 1 1 63 63 GLU HB3 H 1 1.77 0.03 . 1 . . . . . . . . 4664 1 384 . 1 1 63 63 GLU CA C 13 55.17 0.50 . 1 . . . . . . . . 4664 1 385 . 1 1 63 63 GLU C C 13 176.70 0.50 . 1 . . . . . . . . 4664 1 386 . 1 1 63 63 GLU CB C 13 35.01 0.50 . 1 . . . . . . . . 4664 1 387 . 1 1 63 63 GLU N N 15 118.12 0.25 . 1 . . . . . . . . 4664 1 388 . 1 1 64 64 THR H H 1 8.93 0.03 . 1 . . . . . . . . 4664 1 389 . 1 1 64 64 THR HA H 1 4.46 0.03 . 1 . . . . . . . . 4664 1 390 . 1 1 64 64 THR HB H 1 3.78 0.03 . 1 . . . . . . . . 4664 1 391 . 1 1 64 64 THR CA C 13 63.05 0.50 . 1 . . . . . . . . 4664 1 392 . 1 1 64 64 THR C C 13 172.80 0.50 . 1 . . . . . . . . 4664 1 393 . 1 1 64 64 THR CB C 13 73.12 0.50 . 1 . . . . . . . . 4664 1 394 . 1 1 64 64 THR N N 15 118.91 0.25 . 1 . . . . . . . . 4664 1 395 . 1 1 65 65 THR H H 1 8.36 0.03 . 1 . . . . . . . . 4664 1 396 . 1 1 65 65 THR HA H 1 5.13 0.03 . 1 . . . . . . . . 4664 1 397 . 1 1 65 65 THR HB H 1 3.91 0.03 . 1 . . . . . . . . 4664 1 398 . 1 1 65 65 THR CA C 13 62.69 0.50 . 1 . . . . . . . . 4664 1 399 . 1 1 65 65 THR C C 13 174.60 0.50 . 1 . . . . . . . . 4664 1 400 . 1 1 65 65 THR CB C 13 70.91 0.50 . 1 . . . . . . . . 4664 1 401 . 1 1 65 65 THR N N 15 120.74 0.25 . 1 . . . . . . . . 4664 1 402 . 1 1 66 66 PHE H H 1 8.24 0.03 . 1 . . . . . . . . 4664 1 403 . 1 1 66 66 PHE HA H 1 4.68 0.03 . 1 . . . . . . . . 4664 1 404 . 1 1 66 66 PHE CA C 13 62.43 0.50 . 1 . . . . . . . . 4664 1 405 . 1 1 66 66 PHE C C 13 175.30 0.50 . 1 . . . . . . . . 4664 1 406 . 1 1 66 66 PHE CB C 13 33.11 0.50 . 1 . . . . . . . . 4664 1 407 . 1 1 66 66 PHE N N 15 125.19 0.25 . 1 . . . . . . . . 4664 1 408 . 1 1 67 67 LYS H H 1 8.82 0.03 . 1 . . . . . . . . 4664 1 409 . 1 1 67 67 LYS HA H 1 5.41 0.03 . 1 . . . . . . . . 4664 1 410 . 1 1 67 67 LYS HB2 H 1 1.99 0.03 . 2 . . . . . . . . 4664 1 411 . 1 1 67 67 LYS HB3 H 1 1.83 0.03 . 2 . . . . . . . . 4664 1 412 . 1 1 67 67 LYS CA C 13 55.52 0.50 . 1 . . . . . . . . 4664 1 413 . 1 1 67 67 LYS C C 13 177.60 0.50 . 1 . . . . . . . . 4664 1 414 . 1 1 67 67 LYS CB C 13 37.22 0.50 . 1 . . . . . . . . 4664 1 415 . 1 1 67 67 LYS N N 15 120.68 0.25 . 1 . . . . . . . . 4664 1 416 . 1 1 68 68 LYS H H 1 8.83 0.03 . 1 . . . . . . . . 4664 1 417 . 1 1 68 68 LYS CA C 13 58.56 0.50 . 1 . . . . . . . . 4664 1 418 . 1 1 68 68 LYS C C 13 178.40 0.50 . 1 . . . . . . . . 4664 1 419 . 1 1 68 68 LYS CB C 13 35.23 0.50 . 1 . . . . . . . . 4664 1 420 . 1 1 68 68 LYS N N 15 129.88 0.25 . 1 . . . . . . . . 4664 1 421 . 1 1 69 69 THR H H 1 8.62 0.03 . 1 . . . . . . . . 4664 1 422 . 1 1 69 69 THR HA H 1 4.62 0.03 . 1 . . . . . . . . 4664 1 423 . 1 1 69 69 THR HB H 1 4.44 0.03 . 1 . . . . . . . . 4664 1 424 . 1 1 69 69 THR CA C 13 61.84 0.50 . 1 . . . . . . . . 4664 1 425 . 1 1 69 69 THR C C 13 175.70 0.50 . 1 . . . . . . . . 4664 1 426 . 1 1 69 69 THR CB C 13 70.62 0.50 . 1 . . . . . . . . 4664 1 427 . 1 1 69 69 THR N N 15 119.35 0.25 . 1 . . . . . . . . 4664 1 428 . 1 1 70 70 SER H H 1 8.24 0.03 . 1 . . . . . . . . 4664 1 429 . 1 1 70 70 SER HA H 1 4.35 0.03 . 1 . . . . . . . . 4664 1 430 . 1 1 70 70 SER HB2 H 1 3.98 0.03 . 2 . . . . . . . . 4664 1 431 . 1 1 70 70 SER HB3 H 1 3.79 0.03 . 2 . . . . . . . . 4664 1 432 . 1 1 70 70 SER CA C 13 59.21 0.50 . 1 . . . . . . . . 4664 1 433 . 1 1 70 70 SER C C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 434 . 1 1 70 70 SER CB C 13 64.34 0.50 . 1 . . . . . . . . 4664 1 435 . 1 1 70 70 SER N N 15 112.71 0.25 . 1 . . . . . . . . 4664 1 436 . 1 1 71 71 ASP H H 1 7.86 0.03 . 1 . . . . . . . . 4664 1 437 . 1 1 71 71 ASP HA H 1 4.29 0.03 . 1 . . . . . . . . 4664 1 438 . 1 1 71 71 ASP HB2 H 1 2.61 0.03 . 2 . . . . . . . . 4664 1 439 . 1 1 71 71 ASP HB3 H 1 2.03 0.03 . 2 . . . . . . . . 4664 1 440 . 1 1 71 71 ASP CA C 13 56.09 0.50 . 1 . . . . . . . . 4664 1 441 . 1 1 71 71 ASP C C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 442 . 1 1 71 71 ASP CB C 13 43.09 0.50 . 1 . . . . . . . . 4664 1 443 . 1 1 71 71 ASP N N 15 121.92 0.25 . 1 . . . . . . . . 4664 1 444 . 1 1 72 72 ASP H H 1 8.37 0.03 . 1 . . . . . . . . 4664 1 445 . 1 1 72 72 ASP HA H 1 4.37 0.03 . 1 . . . . . . . . 4664 1 446 . 1 1 72 72 ASP HB2 H 1 2.53 0.03 . 2 . . . . . . . . 4664 1 447 . 1 1 72 72 ASP HB3 H 1 2.45 0.03 . 2 . . . . . . . . 4664 1 448 . 1 1 72 72 ASP CA C 13 56.13 0.50 . 1 . . . . . . . . 4664 1 449 . 1 1 72 72 ASP C C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 450 . 1 1 72 72 ASP CB C 13 42.11 0.50 . 1 . . . . . . . . 4664 1 451 . 1 1 72 72 ASP N N 15 121.54 0.25 . 1 . . . . . . . . 4664 1 452 . 1 1 73 73 GLY H H 1 8.08 0.03 . 1 . . . . . . . . 4664 1 453 . 1 1 73 73 GLY HA2 H 1 3.96 0.03 . 2 . . . . . . . . 4664 1 454 . 1 1 73 73 GLY HA3 H 1 3.69 0.03 . 2 . . . . . . . . 4664 1 455 . 1 1 73 73 GLY CA C 13 45.47 0.50 . 1 . . . . . . . . 4664 1 456 . 1 1 73 73 GLY C C 13 173.90 0.50 . 1 . . . . . . . . 4664 1 457 . 1 1 73 73 GLY N N 15 109.82 0.25 . 1 . . . . . . . . 4664 1 458 . 1 1 74 74 GLU H H 1 8.70 0.03 . 1 . . . . . . . . 4664 1 459 . 1 1 74 74 GLU HA H 1 4.60 0.03 . 1 . . . . . . . . 4664 1 460 . 1 1 74 74 GLU CA C 13 55.66 0.50 . 1 . . . . . . . . 4664 1 461 . 1 1 74 74 GLU C C 13 174.50 0.50 . 1 . . . . . . . . 4664 1 462 . 1 1 74 74 GLU CB C 13 30.98 0.50 . 1 . . . . . . . . 4664 1 463 . 1 1 74 74 GLU N N 15 124.18 0.25 . 1 . . . . . . . . 4664 1 464 . 1 1 75 75 VAL H H 1 7.80 0.03 . 1 . . . . . . . . 4664 1 465 . 1 1 75 75 VAL HA H 1 4.91 0.03 . 1 . . . . . . . . 4664 1 466 . 1 1 75 75 VAL HB H 1 1.96 0.03 . 1 . . . . . . . . 4664 1 467 . 1 1 75 75 VAL CA C 13 62.42 0.50 . 1 . . . . . . . . 4664 1 468 . 1 1 75 75 VAL C C 13 175.10 0.50 . 1 . . . . . . . . 4664 1 469 . 1 1 75 75 VAL CB C 13 34.24 0.50 . 1 . . . . . . . . 4664 1 470 . 1 1 75 75 VAL N N 15 124.50 0.25 . 1 . . . . . . . . 4664 1 471 . 1 1 76 76 TYR H H 1 9.19 0.03 . 1 . . . . . . . . 4664 1 472 . 1 1 76 76 TYR HA H 1 5.15 0.03 . 1 . . . . . . . . 4664 1 473 . 1 1 76 76 TYR HB2 H 1 2.64 0.03 . 1 . . . . . . . . 4664 1 474 . 1 1 76 76 TYR HB3 H 1 2.64 0.03 . 1 . . . . . . . . 4664 1 475 . 1 1 76 76 TYR CA C 13 57.72 0.50 . 1 . . . . . . . . 4664 1 476 . 1 1 76 76 TYR C C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 477 . 1 1 76 76 TYR CB C 13 43.27 0.50 . 1 . . . . . . . . 4664 1 478 . 1 1 76 76 TYR N N 15 125.39 0.25 . 1 . . . . . . . . 4664 1 479 . 1 1 77 77 TYR H H 1 9.38 0.03 . 1 . . . . . . . . 4664 1 480 . 1 1 77 77 TYR HA H 1 5.79 0.03 . 1 . . . . . . . . 4664 1 481 . 1 1 77 77 TYR HB2 H 1 2.90 0.03 . 2 . . . . . . . . 4664 1 482 . 1 1 77 77 TYR HB3 H 1 2.88 0.03 . 2 . . . . . . . . 4664 1 483 . 1 1 77 77 TYR CA C 13 58.01 0.50 . 1 . . . . . . . . 4664 1 484 . 1 1 77 77 TYR C C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 485 . 1 1 77 77 TYR CB C 13 44.71 0.50 . 1 . . . . . . . . 4664 1 486 . 1 1 77 77 TYR N N 15 121.32 0.25 . 1 . . . . . . . . 4664 1 487 . 1 1 78 78 SER H H 1 8.46 0.03 . 1 . . . . . . . . 4664 1 488 . 1 1 78 78 SER HA H 1 4.74 0.03 . 1 . . . . . . . . 4664 1 489 . 1 1 78 78 SER HB2 H 1 3.09 0.03 . 2 . . . . . . . . 4664 1 490 . 1 1 78 78 SER HB3 H 1 2.66 0.03 . 2 . . . . . . . . 4664 1 491 . 1 1 78 78 SER CA C 13 55.65 0.50 . 1 . . . . . . . . 4664 1 492 . 1 1 78 78 SER C C 13 175.10 0.50 . 1 . . . . . . . . 4664 1 493 . 1 1 78 78 SER CB C 13 64.41 0.50 . 1 . . . . . . . . 4664 1 494 . 1 1 78 78 SER N N 15 125.58 0.25 . 1 . . . . . . . . 4664 1 495 . 1 1 79 79 GLU H H 1 8.60 0.03 . 1 . . . . . . . . 4664 1 496 . 1 1 79 79 GLU HA H 1 3.87 0.03 . 1 . . . . . . . . 4664 1 497 . 1 1 79 79 GLU HB2 H 1 2.06 0.03 . 1 . . . . . . . . 4664 1 498 . 1 1 79 79 GLU HB3 H 1 2.06 0.03 . 1 . . . . . . . . 4664 1 499 . 1 1 79 79 GLU CA C 13 59.61 0.50 . 1 . . . . . . . . 4664 1 500 . 1 1 79 79 GLU C C 13 179.60 0.50 . 1 . . . . . . . . 4664 1 501 . 1 1 79 79 GLU CB C 13 30.58 0.50 . 1 . . . . . . . . 4664 1 502 . 1 1 79 79 GLU N N 15 130.88 0.25 . 1 . . . . . . . . 4664 1 503 . 1 1 80 80 GLU H H 1 8.42 0.03 . 1 . . . . . . . . 4664 1 504 . 1 1 80 80 GLU HA H 1 3.91 0.03 . 1 . . . . . . . . 4664 1 505 . 1 1 80 80 GLU HB2 H 1 1.96 0.03 . 2 . . . . . . . . 4664 1 506 . 1 1 80 80 GLU HB3 H 1 1.86 0.03 . 2 . . . . . . . . 4664 1 507 . 1 1 80 80 GLU CA C 13 60.16 0.50 . 1 . . . . . . . . 4664 1 508 . 1 1 80 80 GLU C C 13 178.60 0.50 . 1 . . . . . . . . 4664 1 509 . 1 1 80 80 GLU CB C 13 30.45 0.50 . 1 . . . . . . . . 4664 1 510 . 1 1 80 80 GLU N N 15 119.71 0.25 . 1 . . . . . . . . 4664 1 511 . 1 1 81 81 ALA H H 1 7.28 0.03 . 1 . . . . . . . . 4664 1 512 . 1 1 81 81 ALA HA H 1 4.28 0.03 . 1 . . . . . . . . 4664 1 513 . 1 1 81 81 ALA HB1 H 1 1.30 0.03 . 1 . . . . . . . . 4664 1 514 . 1 1 81 81 ALA HB2 H 1 1.30 0.03 . 1 . . . . . . . . 4664 1 515 . 1 1 81 81 ALA HB3 H 1 1.30 0.03 . 1 . . . . . . . . 4664 1 516 . 1 1 81 81 ALA CA C 13 52.38 0.50 . 1 . . . . . . . . 4664 1 517 . 1 1 81 81 ALA C C 13 177.10 0.50 . 1 . . . . . . . . 4664 1 518 . 1 1 81 81 ALA CB C 13 20.75 0.50 . 1 . . . . . . . . 4664 1 519 . 1 1 81 81 ALA N N 15 118.49 0.25 . 1 . . . . . . . . 4664 1 520 . 1 1 82 82 LYS H H 1 7.74 0.03 . 1 . . . . . . . . 4664 1 521 . 1 1 82 82 LYS HA H 1 3.82 0.03 . 1 . . . . . . . . 4664 1 522 . 1 1 82 82 LYS CA C 13 57.08 0.50 . 1 . . . . . . . . 4664 1 523 . 1 1 82 82 LYS C C 13 176.10 0.50 . 1 . . . . . . . . 4664 1 524 . 1 1 82 82 LYS CB C 13 30.54 0.50 . 1 . . . . . . . . 4664 1 525 . 1 1 82 82 LYS N N 15 119.08 0.25 . 1 . . . . . . . . 4664 1 526 . 1 1 83 83 LYS H H 1 7.07 0.03 . 1 . . . . . . . . 4664 1 527 . 1 1 83 83 LYS HA H 1 5.38 0.03 . 1 . . . . . . . . 4664 1 528 . 1 1 83 83 LYS CA C 13 55.50 0.50 . 1 . . . . . . . . 4664 1 529 . 1 1 83 83 LYS CB C 13 40.04 0.50 . 1 . . . . . . . . 4664 1 530 . 1 1 83 83 LYS N N 15 119.10 0.25 . 1 . . . . . . . . 4664 1 531 . 1 1 86 86 GLU CA C 13 54.75 0.50 . 1 . . . . . . . . 4664 1 532 . 1 1 86 86 GLU C C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 533 . 1 1 86 86 GLU CB C 13 34.32 0.50 . 1 . . . . . . . . 4664 1 534 . 1 1 87 87 VAL H H 1 8.69 0.03 . 1 . . . . . . . . 4664 1 535 . 1 1 87 87 VAL HA H 1 4.14 0.03 . 1 . . . . . . . . 4664 1 536 . 1 1 87 87 VAL HB H 1 2.20 0.03 . 1 . . . . . . . . 4664 1 537 . 1 1 87 87 VAL CA C 13 63.37 0.50 . 1 . . . . . . . . 4664 1 538 . 1 1 87 87 VAL C C 13 177.00 0.50 . 1 . . . . . . . . 4664 1 539 . 1 1 87 87 VAL CB C 13 31.97 0.50 . 1 . . . . . . . . 4664 1 540 . 1 1 87 87 VAL N N 15 126.00 0.25 . 1 . . . . . . . . 4664 1 541 . 1 1 88 88 LEU H H 1 8.93 0.03 . 1 . . . . . . . . 4664 1 542 . 1 1 88 88 LEU CA C 13 56.94 0.50 . 1 . . . . . . . . 4664 1 543 . 1 1 88 88 LEU C C 13 178.20 0.50 . 1 . . . . . . . . 4664 1 544 . 1 1 88 88 LEU CB C 13 44.10 0.50 . 1 . . . . . . . . 4664 1 545 . 1 1 88 88 LEU N N 15 128.80 0.25 . 1 . . . . . . . . 4664 1 546 . 1 1 89 89 ASP H H 1 7.02 0.03 . 1 . . . . . . . . 4664 1 547 . 1 1 89 89 ASP HA H 1 4.70 0.03 . 1 . . . . . . . . 4664 1 548 . 1 1 89 89 ASP HB2 H 1 2.73 0.03 . 1 . . . . . . . . 4664 1 549 . 1 1 89 89 ASP HB3 H 1 2.73 0.03 . 1 . . . . . . . . 4664 1 550 . 1 1 89 89 ASP CA C 13 55.88 0.50 . 1 . . . . . . . . 4664 1 551 . 1 1 89 89 ASP C C 13 175.00 0.50 . 1 . . . . . . . . 4664 1 552 . 1 1 89 89 ASP CB C 13 46.51 0.50 . 1 . . . . . . . . 4664 1 553 . 1 1 89 89 ASP N N 15 114.58 0.25 . 1 . . . . . . . . 4664 1 554 . 1 1 90 90 THR H H 1 7.99 0.03 . 1 . . . . . . . . 4664 1 555 . 1 1 90 90 THR HA H 1 3.75 0.03 . 1 . . . . . . . . 4664 1 556 . 1 1 90 90 THR HB H 1 3.83 0.03 . 1 . . . . . . . . 4664 1 557 . 1 1 90 90 THR CA C 13 61.49 0.50 . 1 . . . . . . . . 4664 1 558 . 1 1 90 90 THR C C 13 179.86 0.50 . 1 . . . . . . . . 4664 1 559 . 1 1 90 90 THR CB C 13 69.15 0.50 . 1 . . . . . . . . 4664 1 560 . 1 1 90 90 THR N N 15 120.53 0.25 . 1 . . . . . . . . 4664 1 561 . 1 1 91 91 ASP H H 1 6.70 0.03 . 1 . . . . . . . . 4664 1 562 . 1 1 91 91 ASP HA H 1 4.76 0.03 . 1 . . . . . . . . 4664 1 563 . 1 1 91 91 ASP CA C 13 53.80 0.50 . 1 . . . . . . . . 4664 1 564 . 1 1 91 91 ASP C C 13 177.70 0.50 . 1 . . . . . . . . 4664 1 565 . 1 1 91 91 ASP CB C 13 41.90 0.50 . 1 . . . . . . . . 4664 1 566 . 1 1 91 91 ASP N N 15 123.00 0.25 . 1 . . . . . . . . 4664 1 567 . 1 1 92 92 TYR H H 1 9.30 0.03 . 1 . . . . . . . . 4664 1 568 . 1 1 92 92 TYR CA C 13 62.08 0.50 . 1 . . . . . . . . 4664 1 569 . 1 1 92 92 TYR C C 13 174.90 0.50 . 1 . . . . . . . . 4664 1 570 . 1 1 92 92 TYR CB C 13 36.77 0.50 . 1 . . . . . . . . 4664 1 571 . 1 1 92 92 TYR N N 15 115.90 0.25 . 1 . . . . . . . . 4664 1 572 . 1 1 93 93 LYS H H 1 7.99 0.03 . 1 . . . . . . . . 4664 1 573 . 1 1 93 93 LYS HA H 1 4.59 0.03 . 1 . . . . . . . . 4664 1 574 . 1 1 93 93 LYS HB2 H 1 1.62 0.03 . 1 . . . . . . . . 4664 1 575 . 1 1 93 93 LYS HB3 H 1 1.62 0.03 . 1 . . . . . . . . 4664 1 576 . 1 1 93 93 LYS CA C 13 59.30 0.50 . 1 . . . . . . . . 4664 1 577 . 1 1 93 93 LYS C C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 578 . 1 1 93 93 LYS CB C 13 37.84 0.50 . 1 . . . . . . . . 4664 1 579 . 1 1 93 93 LYS N N 15 113.37 0.25 . 1 . . . . . . . . 4664 1 580 . 1 1 94 94 SER H H 1 11.29 0.03 . 1 . . . . . . . . 4664 1 581 . 1 1 94 94 SER HA H 1 4.78 0.03 . 1 . . . . . . . . 4664 1 582 . 1 1 94 94 SER HB2 H 1 4.17 0.03 . 2 . . . . . . . . 4664 1 583 . 1 1 94 94 SER HB3 H 1 3.81 0.03 . 2 . . . . . . . . 4664 1 584 . 1 1 94 94 SER CA C 13 61.05 0.50 . 1 . . . . . . . . 4664 1 585 . 1 1 94 94 SER C C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 586 . 1 1 94 94 SER CB C 13 68.64 0.50 . 1 . . . . . . . . 4664 1 587 . 1 1 94 94 SER N N 15 120.95 0.25 . 1 . . . . . . . . 4664 1 588 . 1 1 95 95 TYR H H 1 8.40 0.03 . 1 . . . . . . . . 4664 1 589 . 1 1 95 95 TYR HA H 1 6.08 0.03 . 1 . . . . . . . . 4664 1 590 . 1 1 95 95 TYR HB2 H 1 3.22 0.03 . 2 . . . . . . . . 4664 1 591 . 1 1 95 95 TYR HB3 H 1 3.08 0.03 . 2 . . . . . . . . 4664 1 592 . 1 1 95 95 TYR CA C 13 58.52 0.50 . 1 . . . . . . . . 4664 1 593 . 1 1 95 95 TYR C C 13 174.60 0.50 . 1 . . . . . . . . 4664 1 594 . 1 1 95 95 TYR CB C 13 42.75 0.50 . 1 . . . . . . . . 4664 1 595 . 1 1 95 95 TYR N N 15 123.50 0.25 . 1 . . . . . . . . 4664 1 596 . 1 1 96 96 ALA H H 1 9.01 0.03 . 1 . . . . . . . . 4664 1 597 . 1 1 96 96 ALA HA H 1 4.53 0.03 . 1 . . . . . . . . 4664 1 598 . 1 1 96 96 ALA HB1 H 1 0.90 0.03 . 1 . . . . . . . . 4664 1 599 . 1 1 96 96 ALA HB2 H 1 0.90 0.03 . 1 . . . . . . . . 4664 1 600 . 1 1 96 96 ALA HB3 H 1 0.90 0.03 . 1 . . . . . . . . 4664 1 601 . 1 1 96 96 ALA CA C 13 53.37 0.50 . 1 . . . . . . . . 4664 1 602 . 1 1 96 96 ALA C C 13 175.70 0.50 . 1 . . . . . . . . 4664 1 603 . 1 1 96 96 ALA CB C 13 24.23 0.50 . 1 . . . . . . . . 4664 1 604 . 1 1 96 96 ALA N N 15 121.67 0.25 . 1 . . . . . . . . 4664 1 605 . 1 1 97 97 VAL H H 1 9.26 0.03 . 1 . . . . . . . . 4664 1 606 . 1 1 97 97 VAL HA H 1 4.95 0.03 . 1 . . . . . . . . 4664 1 607 . 1 1 97 97 VAL HB H 1 2.09 0.03 . 1 . . . . . . . . 4664 1 608 . 1 1 97 97 VAL CA C 13 63.45 0.50 . 1 . . . . . . . . 4664 1 609 . 1 1 97 97 VAL C C 13 175.00 0.50 . 1 . . . . . . . . 4664 1 610 . 1 1 97 97 VAL CB C 13 33.48 0.50 . 1 . . . . . . . . 4664 1 611 . 1 1 97 97 VAL N N 15 122.55 0.25 . 1 . . . . . . . . 4664 1 612 . 1 1 98 98 ILE H H 1 9.50 0.03 . 1 . . . . . . . . 4664 1 613 . 1 1 98 98 ILE HA H 1 5.07 0.03 . 1 . . . . . . . . 4664 1 614 . 1 1 98 98 ILE HB H 1 1.91 0.03 . 1 . . . . . . . . 4664 1 615 . 1 1 98 98 ILE CA C 13 58.91 0.50 . 1 . . . . . . . . 4664 1 616 . 1 1 98 98 ILE C C 13 175.20 0.50 . 1 . . . . . . . . 4664 1 617 . 1 1 98 98 ILE CB C 13 42.54 0.50 . 1 . . . . . . . . 4664 1 618 . 1 1 98 98 ILE N N 15 131.11 0.25 . 1 . . . . . . . . 4664 1 619 . 1 1 99 99 TYR H H 1 9.47 0.03 . 1 . . . . . . . . 4664 1 620 . 1 1 99 99 TYR HA H 1 5.19 0.03 . 1 . . . . . . . . 4664 1 621 . 1 1 99 99 TYR HB2 H 1 2.59 0.03 . 1 . . . . . . . . 4664 1 622 . 1 1 99 99 TYR HB3 H 1 2.59 0.03 . 1 . . . . . . . . 4664 1 623 . 1 1 99 99 TYR CA C 13 57.79 0.50 . 1 . . . . . . . . 4664 1 624 . 1 1 99 99 TYR C C 13 174.80 0.50 . 1 . . . . . . . . 4664 1 625 . 1 1 99 99 TYR CB C 13 42.17 0.50 . 1 . . . . . . . . 4664 1 626 . 1 1 99 99 TYR N N 15 128.87 0.25 . 1 . . . . . . . . 4664 1 627 . 1 1 100 100 ALA H H 1 9.53 0.03 . 1 . . . . . . . . 4664 1 628 . 1 1 100 100 ALA HA H 1 5.63 0.03 . 1 . . . . . . . . 4664 1 629 . 1 1 100 100 ALA HB1 H 1 1.42 0.03 . 1 . . . . . . . . 4664 1 630 . 1 1 100 100 ALA HB2 H 1 1.42 0.03 . 1 . . . . . . . . 4664 1 631 . 1 1 100 100 ALA HB3 H 1 1.42 0.03 . 1 . . . . . . . . 4664 1 632 . 1 1 100 100 ALA CA C 13 51.41 0.50 . 1 . . . . . . . . 4664 1 633 . 1 1 100 100 ALA C C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 634 . 1 1 100 100 ALA CB C 13 24.85 0.50 . 1 . . . . . . . . 4664 1 635 . 1 1 100 100 ALA N N 15 135.26 0.25 . 1 . . . . . . . . 4664 1 636 . 1 1 101 101 THR H H 1 9.35 0.03 . 1 . . . . . . . . 4664 1 637 . 1 1 101 101 THR HA H 1 5.33 0.03 . 1 . . . . . . . . 4664 1 638 . 1 1 101 101 THR HB H 1 3.94 0.03 . 1 . . . . . . . . 4664 1 639 . 1 1 101 101 THR CA C 13 62.05 0.50 . 1 . . . . . . . . 4664 1 640 . 1 1 101 101 THR C C 13 174.60 0.50 . 1 . . . . . . . . 4664 1 641 . 1 1 101 101 THR CB C 13 73.12 0.50 . 1 . . . . . . . . 4664 1 642 . 1 1 101 101 THR N N 15 117.35 0.25 . 1 . . . . . . . . 4664 1 643 . 1 1 102 102 ARG H H 1 8.91 0.03 . 1 . . . . . . . . 4664 1 644 . 1 1 102 102 ARG HA H 1 5.17 0.03 . 1 . . . . . . . . 4664 1 645 . 1 1 102 102 ARG CA C 13 55.38 0.50 . 1 . . . . . . . . 4664 1 646 . 1 1 102 102 ARG C C 13 175.00 0.50 . 1 . . . . . . . . 4664 1 647 . 1 1 102 102 ARG CB C 13 36.22 0.50 . 1 . . . . . . . . 4664 1 648 . 1 1 102 102 ARG N N 15 126.75 0.25 . 1 . . . . . . . . 4664 1 649 . 1 1 103 103 VAL H H 1 7.74 0.03 . 1 . . . . . . . . 4664 1 650 . 1 1 103 103 VAL HA H 1 4.68 0.03 . 1 . . . . . . . . 4664 1 651 . 1 1 103 103 VAL CA C 13 62.43 0.50 . 1 . . . . . . . . 4664 1 652 . 1 1 103 103 VAL C C 13 176.70 0.50 . 1 . . . . . . . . 4664 1 653 . 1 1 103 103 VAL CB C 13 33.31 0.50 . 1 . . . . . . . . 4664 1 654 . 1 1 103 103 VAL N N 15 123.16 0.25 . 1 . . . . . . . . 4664 1 655 . 1 1 104 104 LYS H H 1 8.88 0.03 . 1 . . . . . . . . 4664 1 656 . 1 1 104 104 LYS HA H 1 4.33 0.03 . 1 . . . . . . . . 4664 1 657 . 1 1 104 104 LYS HB2 H 1 1.41 0.03 . 1 . . . . . . . . 4664 1 658 . 1 1 104 104 LYS HB3 H 1 1.41 0.03 . 1 . . . . . . . . 4664 1 659 . 1 1 104 104 LYS CA C 13 55.97 0.50 . 1 . . . . . . . . 4664 1 660 . 1 1 104 104 LYS CB C 13 36.55 0.50 . 1 . . . . . . . . 4664 1 661 . 1 1 104 104 LYS N N 15 130.93 0.25 . 1 . . . . . . . . 4664 1 662 . 1 1 105 105 ASP H H 1 9.39 0.03 . 1 . . . . . . . . 4664 1 663 . 1 1 105 105 ASP HA H 1 4.66 0.03 . 1 . . . . . . . . 4664 1 664 . 1 1 105 105 ASP CA C 13 56.45 0.50 . 1 . . . . . . . . 4664 1 665 . 1 1 105 105 ASP C C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 666 . 1 1 105 105 ASP CB C 13 40.53 0.50 . 1 . . . . . . . . 4664 1 667 . 1 1 105 105 ASP N N 15 130.04 0.25 . 1 . . . . . . . . 4664 1 668 . 1 1 106 106 GLY H H 1 8.24 0.03 . 1 . . . . . . . . 4664 1 669 . 1 1 106 106 GLY HA2 H 1 4.02 0.03 . 2 . . . . . . . . 4664 1 670 . 1 1 106 106 GLY HA3 H 1 3.45 0.03 . 2 . . . . . . . . 4664 1 671 . 1 1 106 106 GLY CA C 13 46.34 0.50 . 1 . . . . . . . . 4664 1 672 . 1 1 106 106 GLY C C 13 174.60 0.50 . 1 . . . . . . . . 4664 1 673 . 1 1 106 106 GLY N N 15 103.63 0.25 . 1 . . . . . . . . 4664 1 674 . 1 1 107 107 ARG H H 1 7.78 0.03 . 1 . . . . . . . . 4664 1 675 . 1 1 107 107 ARG HA H 1 4.58 0.03 . 1 . . . . . . . . 4664 1 676 . 1 1 107 107 ARG HB2 H 1 1.73 0.03 . 1 . . . . . . . . 4664 1 677 . 1 1 107 107 ARG HB3 H 1 1.73 0.03 . 1 . . . . . . . . 4664 1 678 . 1 1 107 107 ARG CA C 13 55.40 0.50 . 1 . . . . . . . . 4664 1 679 . 1 1 107 107 ARG C C 13 175.60 0.50 . 1 . . . . . . . . 4664 1 680 . 1 1 107 107 ARG CB C 13 33.35 0.50 . 1 . . . . . . . . 4664 1 681 . 1 1 107 107 ARG N N 15 122.00 0.25 . 1 . . . . . . . . 4664 1 682 . 1 1 108 108 THR H H 1 8.56 0.03 . 1 . . . . . . . . 4664 1 683 . 1 1 108 108 THR HA H 1 4.40 0.03 . 1 . . . . . . . . 4664 1 684 . 1 1 108 108 THR HB H 1 3.86 0.03 . 1 . . . . . . . . 4664 1 685 . 1 1 108 108 THR CA C 13 64.18 0.50 . 1 . . . . . . . . 4664 1 686 . 1 1 108 108 THR C C 13 174.40 0.50 . 1 . . . . . . . . 4664 1 687 . 1 1 108 108 THR CB C 13 69.73 0.50 . 1 . . . . . . . . 4664 1 688 . 1 1 108 108 THR N N 15 119.62 0.25 . 1 . . . . . . . . 4664 1 689 . 1 1 109 109 LEU H H 1 9.13 0.03 . 1 . . . . . . . . 4664 1 690 . 1 1 109 109 LEU HA H 1 4.63 0.03 . 1 . . . . . . . . 4664 1 691 . 1 1 109 109 LEU CA C 13 54.27 0.50 . 1 . . . . . . . . 4664 1 692 . 1 1 109 109 LEU C C 13 176.70 0.50 . 1 . . . . . . . . 4664 1 693 . 1 1 109 109 LEU N N 15 129.73 0.25 . 1 . . . . . . . . 4664 1 694 . 1 1 110 110 HIS H H 1 8.39 0.03 . 1 . . . . . . . . 4664 1 695 . 1 1 110 110 HIS HA H 1 5.94 0.03 . 1 . . . . . . . . 4664 1 696 . 1 1 110 110 HIS HB2 H 1 2.96 0.03 . 2 . . . . . . . . 4664 1 697 . 1 1 110 110 HIS HB3 H 1 2.89 0.03 . 2 . . . . . . . . 4664 1 698 . 1 1 110 110 HIS CA C 13 55.28 0.50 . 1 . . . . . . . . 4664 1 699 . 1 1 110 110 HIS C C 13 176.10 0.50 . 1 . . . . . . . . 4664 1 700 . 1 1 110 110 HIS CB C 13 34.39 0.50 . 1 . . . . . . . . 4664 1 701 . 1 1 110 110 HIS N N 15 116.91 0.25 . 1 . . . . . . . . 4664 1 702 . 1 1 111 111 MET H H 1 9.01 0.03 . 1 . . . . . . . . 4664 1 703 . 1 1 111 111 MET HA H 1 4.49 0.03 . 1 . . . . . . . . 4664 1 704 . 1 1 111 111 MET HB2 H 1 1.83 0.03 . 1 . . . . . . . . 4664 1 705 . 1 1 111 111 MET HB3 H 1 1.83 0.03 . 1 . . . . . . . . 4664 1 706 . 1 1 111 111 MET CA C 13 56.25 0.50 . 1 . . . . . . . . 4664 1 707 . 1 1 111 111 MET C C 13 174.90 0.50 . 1 . . . . . . . . 4664 1 708 . 1 1 111 111 MET CB C 13 37.58 0.50 . 1 . . . . . . . . 4664 1 709 . 1 1 111 111 MET N N 15 124.18 0.25 . 1 . . . . . . . . 4664 1 710 . 1 1 112 112 MET H H 1 9.06 0.03 . 1 . . . . . . . . 4664 1 711 . 1 1 112 112 MET HA H 1 5.58 0.03 . 1 . . . . . . . . 4664 1 712 . 1 1 112 112 MET HB2 H 1 2.05 0.03 . 1 . . . . . . . . 4664 1 713 . 1 1 112 112 MET HB3 H 1 2.05 0.03 . 1 . . . . . . . . 4664 1 714 . 1 1 112 112 MET CA C 13 55.32 0.50 . 1 . . . . . . . . 4664 1 715 . 1 1 112 112 MET C C 13 176.50 0.50 . 1 . . . . . . . . 4664 1 716 . 1 1 112 112 MET CB C 13 37.15 0.50 . 1 . . . . . . . . 4664 1 717 . 1 1 112 112 MET N N 15 123.86 0.25 . 1 . . . . . . . . 4664 1 718 . 1 1 113 113 ARG H H 1 9.37 0.03 . 1 . . . . . . . . 4664 1 719 . 1 1 113 113 ARG HA H 1 5.00 0.03 . 1 . . . . . . . . 4664 1 720 . 1 1 113 113 ARG CA C 13 55.67 0.50 . 1 . . . . . . . . 4664 1 721 . 1 1 113 113 ARG C C 13 175.00 0.50 . 1 . . . . . . . . 4664 1 722 . 1 1 113 113 ARG CB C 13 38.27 0.50 . 1 . . . . . . . . 4664 1 723 . 1 1 113 113 ARG N N 15 120.04 0.25 . 1 . . . . . . . . 4664 1 724 . 1 1 114 114 LEU H H 1 7.96 0.03 . 1 . . . . . . . . 4664 1 725 . 1 1 114 114 LEU HA H 1 4.99 0.03 . 1 . . . . . . . . 4664 1 726 . 1 1 114 114 LEU HB2 H 1 2.24 0.03 . 1 . . . . . . . . 4664 1 727 . 1 1 114 114 LEU HB3 H 1 2.24 0.03 . 1 . . . . . . . . 4664 1 728 . 1 1 114 114 LEU CA C 13 54.25 0.50 . 1 . . . . . . . . 4664 1 729 . 1 1 114 114 LEU C C 13 175.33 0.50 . 1 . . . . . . . . 4664 1 730 . 1 1 114 114 LEU CB C 13 43.89 0.50 . 1 . . . . . . . . 4664 1 731 . 1 1 114 114 LEU N N 15 125.31 0.25 . 1 . . . . . . . . 4664 1 732 . 1 1 115 115 TYR H H 1 9.54 0.03 . 1 . . . . . . . . 4664 1 733 . 1 1 115 115 TYR CA C 13 58.11 0.50 . 1 . . . . . . . . 4664 1 734 . 1 1 115 115 TYR C C 13 177.70 0.50 . 1 . . . . . . . . 4664 1 735 . 1 1 115 115 TYR N N 15 126.76 0.25 . 1 . . . . . . . . 4664 1 736 . 1 1 116 116 SER H H 1 9.85 0.03 . 1 . . . . . . . . 4664 1 737 . 1 1 116 116 SER HA H 1 5.73 0.03 . 1 . . . . . . . . 4664 1 738 . 1 1 116 116 SER HB2 H 1 3.89 0.03 . 2 . . . . . . . . 4664 1 739 . 1 1 116 116 SER HB3 H 1 3.59 0.03 . 2 . . . . . . . . 4664 1 740 . 1 1 116 116 SER CA C 13 56.55 0.50 . 1 . . . . . . . . 4664 1 741 . 1 1 116 116 SER C C 13 176.40 0.50 . 1 . . . . . . . . 4664 1 742 . 1 1 116 116 SER CB C 13 67.66 0.50 . 1 . . . . . . . . 4664 1 743 . 1 1 116 116 SER N N 15 113.93 0.25 . 1 . . . . . . . . 4664 1 744 . 1 1 117 117 ARG H H 1 8.25 0.03 . 1 . . . . . . . . 4664 1 745 . 1 1 117 117 ARG HA H 1 3.60 0.03 . 1 . . . . . . . . 4664 1 746 . 1 1 117 117 ARG HB2 H 1 1.79 0.03 . 2 . . . . . . . . 4664 1 747 . 1 1 117 117 ARG HB3 H 1 1.28 0.03 . 2 . . . . . . . . 4664 1 748 . 1 1 117 117 ARG CA C 13 58.08 0.50 . 1 . . . . . . . . 4664 1 749 . 1 1 117 117 ARG C C 13 176.40 0.50 . 1 . . . . . . . . 4664 1 750 . 1 1 117 117 ARG CB C 13 32.45 0.50 . 1 . . . . . . . . 4664 1 751 . 1 1 117 117 ARG N N 15 131.38 0.25 . 1 . . . . . . . . 4664 1 752 . 1 1 118 118 SER H H 1 7.87 0.03 . 1 . . . . . . . . 4664 1 753 . 1 1 118 118 SER HA H 1 4.90 0.03 . 1 . . . . . . . . 4664 1 754 . 1 1 118 118 SER HB2 H 1 3.88 0.03 . 2 . . . . . . . . 4664 1 755 . 1 1 118 118 SER HB3 H 1 3.59 0.03 . 2 . . . . . . . . 4664 1 756 . 1 1 118 118 SER CA C 13 54.79 0.50 . 1 . . . . . . . . 4664 1 757 . 1 1 118 118 SER CB C 13 65.77 0.50 . 1 . . . . . . . . 4664 1 758 . 1 1 118 118 SER N N 15 111.94 0.25 . 1 . . . . . . . . 4664 1 759 . 1 1 119 119 PRO HA H 1 4.01 0.03 . 1 . . . . . . . . 4664 1 760 . 1 1 119 119 PRO HB2 H 1 2.23 0.03 . 2 . . . . . . . . 4664 1 761 . 1 1 119 119 PRO HB3 H 1 1.94 0.03 . 2 . . . . . . . . 4664 1 762 . 1 1 119 119 PRO CA C 13 64.97 0.50 . 1 . . . . . . . . 4664 1 763 . 1 1 119 119 PRO C C 13 176.50 0.50 . 1 . . . . . . . . 4664 1 764 . 1 1 119 119 PRO CB C 13 32.43 0.50 . 1 . . . . . . . . 4664 1 765 . 1 1 120 120 GLU H H 1 7.30 0.03 . 1 . . . . . . . . 4664 1 766 . 1 1 120 120 GLU HA H 1 4.17 0.03 . 1 . . . . . . . . 4664 1 767 . 1 1 120 120 GLU HB2 H 1 1.74 0.03 . 2 . . . . . . . . 4664 1 768 . 1 1 120 120 GLU HB3 H 1 1.69 0.03 . 2 . . . . . . . . 4664 1 769 . 1 1 120 120 GLU CA C 13 55.88 0.50 . 1 . . . . . . . . 4664 1 770 . 1 1 120 120 GLU C C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 771 . 1 1 120 120 GLU CB C 13 29.71 0.50 . 1 . . . . . . . . 4664 1 772 . 1 1 120 120 GLU N N 15 118.13 0.25 . 1 . . . . . . . . 4664 1 773 . 1 1 121 121 VAL H H 1 7.81 0.03 . 1 . . . . . . . . 4664 1 774 . 1 1 121 121 VAL HA H 1 4.07 0.03 . 1 . . . . . . . . 4664 1 775 . 1 1 121 121 VAL HB H 1 1.76 0.03 . 1 . . . . . . . . 4664 1 776 . 1 1 121 121 VAL CA C 13 61.71 0.50 . 1 . . . . . . . . 4664 1 777 . 1 1 121 121 VAL C C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 778 . 1 1 121 121 VAL CB C 13 34.22 0.50 . 1 . . . . . . . . 4664 1 779 . 1 1 121 121 VAL N N 15 125.71 0.25 . 1 . . . . . . . . 4664 1 780 . 1 1 122 122 SER H H 1 8.57 0.03 . 1 . . . . . . . . 4664 1 781 . 1 1 122 122 SER HA H 1 4.68 0.03 . 1 . . . . . . . . 4664 1 782 . 1 1 122 122 SER HB2 H 1 4.20 0.03 . 2 . . . . . . . . 4664 1 783 . 1 1 122 122 SER HB3 H 1 3.88 0.03 . 2 . . . . . . . . 4664 1 784 . 1 1 122 122 SER CA C 13 57.23 0.50 . 1 . . . . . . . . 4664 1 785 . 1 1 122 122 SER CB C 13 64.40 0.50 . 1 . . . . . . . . 4664 1 786 . 1 1 122 122 SER N N 15 125.18 0.25 . 1 . . . . . . . . 4664 1 787 . 1 1 123 123 PRO HA H 1 4.26 0.03 . 1 . . . . . . . . 4664 1 788 . 1 1 123 123 PRO HB2 H 1 2.29 0.03 . 2 . . . . . . . . 4664 1 789 . 1 1 123 123 PRO HB3 H 1 1.87 0.03 . 2 . . . . . . . . 4664 1 790 . 1 1 123 123 PRO CA C 13 65.91 0.50 . 1 . . . . . . . . 4664 1 791 . 1 1 123 123 PRO C C 13 180.40 0.50 . 1 . . . . . . . . 4664 1 792 . 1 1 123 123 PRO CB C 13 32.57 0.50 . 1 . . . . . . . . 4664 1 793 . 1 1 124 124 ALA H H 1 7.93 0.03 . 1 . . . . . . . . 4664 1 794 . 1 1 124 124 ALA HA H 1 4.01 0.03 . 1 . . . . . . . . 4664 1 795 . 1 1 124 124 ALA HB1 H 1 1.23 0.03 . 1 . . . . . . . . 4664 1 796 . 1 1 124 124 ALA HB2 H 1 1.23 0.03 . 1 . . . . . . . . 4664 1 797 . 1 1 124 124 ALA HB3 H 1 1.23 0.03 . 1 . . . . . . . . 4664 1 798 . 1 1 124 124 ALA CA C 13 55.92 0.50 . 1 . . . . . . . . 4664 1 799 . 1 1 124 124 ALA C C 13 180.90 0.50 . 1 . . . . . . . . 4664 1 800 . 1 1 124 124 ALA CB C 13 19.15 0.50 . 1 . . . . . . . . 4664 1 801 . 1 1 124 124 ALA N N 15 120.88 0.25 . 1 . . . . . . . . 4664 1 802 . 1 1 125 125 ALA H H 1 7.41 0.03 . 1 . . . . . . . . 4664 1 803 . 1 1 125 125 ALA HA H 1 3.37 0.03 . 1 . . . . . . . . 4664 1 804 . 1 1 125 125 ALA HB1 H 1 1.08 0.03 . 1 . . . . . . . . 4664 1 805 . 1 1 125 125 ALA HB2 H 1 1.08 0.03 . 1 . . . . . . . . 4664 1 806 . 1 1 125 125 ALA HB3 H 1 1.08 0.03 . 1 . . . . . . . . 4664 1 807 . 1 1 125 125 ALA CA C 13 55.59 0.50 . 1 . . . . . . . . 4664 1 808 . 1 1 125 125 ALA C C 13 180.20 0.50 . 1 . . . . . . . . 4664 1 809 . 1 1 125 125 ALA CB C 13 19.36 0.50 . 1 . . . . . . . . 4664 1 810 . 1 1 125 125 ALA N N 15 121.76 0.25 . 1 . . . . . . . . 4664 1 811 . 1 1 126 126 THR H H 1 7.73 0.03 . 1 . . . . . . . . 4664 1 812 . 1 1 126 126 THR HA H 1 4.08 0.03 . 1 . . . . . . . . 4664 1 813 . 1 1 126 126 THR HB H 1 3.52 0.03 . 1 . . . . . . . . 4664 1 814 . 1 1 126 126 THR CA C 13 67.66 0.50 . 1 . . . . . . . . 4664 1 815 . 1 1 126 126 THR C C 13 177.20 0.50 . 1 . . . . . . . . 4664 1 816 . 1 1 126 126 THR CB C 13 68.88 0.50 . 1 . . . . . . . . 4664 1 817 . 1 1 126 126 THR N N 15 113.98 0.25 . 1 . . . . . . . . 4664 1 818 . 1 1 127 127 ALA H H 1 7.80 0.03 . 1 . . . . . . . . 4664 1 819 . 1 1 127 127 ALA HA H 1 4.01 0.03 . 1 . . . . . . . . 4664 1 820 . 1 1 127 127 ALA HB1 H 1 1.36 0.03 . 1 . . . . . . . . 4664 1 821 . 1 1 127 127 ALA HB2 H 1 1.36 0.03 . 1 . . . . . . . . 4664 1 822 . 1 1 127 127 ALA HB3 H 1 1.36 0.03 . 1 . . . . . . . . 4664 1 823 . 1 1 127 127 ALA CA C 13 56.33 0.50 . 1 . . . . . . . . 4664 1 824 . 1 1 127 127 ALA C C 13 172.36 0.50 . 1 . . . . . . . . 4664 1 825 . 1 1 127 127 ALA CB C 13 18.76 0.50 . 1 . . . . . . . . 4664 1 826 . 1 1 127 127 ALA N N 15 123.92 0.25 . 1 . . . . . . . . 4664 1 827 . 1 1 128 128 ILE H H 1 7.55 0.03 . 1 . . . . . . . . 4664 1 828 . 1 1 128 128 ILE HA H 1 3.67 0.03 . 1 . . . . . . . . 4664 1 829 . 1 1 128 128 ILE HB H 1 1.62 0.03 . 1 . . . . . . . . 4664 1 830 . 1 1 128 128 ILE CA C 13 65.67 0.50 . 1 . . . . . . . . 4664 1 831 . 1 1 128 128 ILE C C 13 178.40 0.50 . 1 . . . . . . . . 4664 1 832 . 1 1 128 128 ILE CB C 13 39.51 0.50 . 1 . . . . . . . . 4664 1 833 . 1 1 128 128 ILE N N 15 121.69 0.25 . 1 . . . . . . . . 4664 1 834 . 1 1 129 129 PHE H H 1 8.16 0.03 . 1 . . . . . . . . 4664 1 835 . 1 1 129 129 PHE HA H 1 3.94 0.03 . 1 . . . . . . . . 4664 1 836 . 1 1 129 129 PHE HB2 H 1 3.20 0.03 . 2 . . . . . . . . 4664 1 837 . 1 1 129 129 PHE HB3 H 1 3.13 0.03 . 2 . . . . . . . . 4664 1 838 . 1 1 129 129 PHE CA C 13 63.35 0.50 . 1 . . . . . . . . 4664 1 839 . 1 1 129 129 PHE C C 13 177.10 0.50 . 1 . . . . . . . . 4664 1 840 . 1 1 129 129 PHE CB C 13 41.12 0.50 . 1 . . . . . . . . 4664 1 841 . 1 1 129 129 PHE N N 15 120.96 0.25 . 1 . . . . . . . . 4664 1 842 . 1 1 130 130 ARG H H 1 8.55 0.03 . 1 . . . . . . . . 4664 1 843 . 1 1 130 130 ARG HA H 1 3.48 0.03 . 1 . . . . . . . . 4664 1 844 . 1 1 130 130 ARG HB2 H 1 1.88 0.03 . 2 . . . . . . . . 4664 1 845 . 1 1 130 130 ARG HB3 H 1 1.75 0.03 . 2 . . . . . . . . 4664 1 846 . 1 1 130 130 ARG CA C 13 61.04 0.50 . 1 . . . . . . . . 4664 1 847 . 1 1 130 130 ARG C C 13 180.40 0.50 . 1 . . . . . . . . 4664 1 848 . 1 1 130 130 ARG CB C 13 30.75 0.50 . 1 . . . . . . . . 4664 1 849 . 1 1 130 130 ARG N N 15 117.06 0.25 . 1 . . . . . . . . 4664 1 850 . 1 1 131 131 LYS H H 1 7.92 0.03 . 1 . . . . . . . . 4664 1 851 . 1 1 131 131 LYS HA H 1 3.95 0.03 . 1 . . . . . . . . 4664 1 852 . 1 1 131 131 LYS HB2 H 1 1.83 0.03 . 1 . . . . . . . . 4664 1 853 . 1 1 131 131 LYS HB3 H 1 1.83 0.03 . 1 . . . . . . . . 4664 1 854 . 1 1 131 131 LYS CA C 13 60.41 0.50 . 1 . . . . . . . . 4664 1 855 . 1 1 131 131 LYS C C 13 180.30 0.50 . 1 . . . . . . . . 4664 1 856 . 1 1 131 131 LYS CB C 13 33.42 0.50 . 1 . . . . . . . . 4664 1 857 . 1 1 131 131 LYS N N 15 122.91 0.25 . 1 . . . . . . . . 4664 1 858 . 1 1 132 132 LEU H H 1 8.35 0.03 . 1 . . . . . . . . 4664 1 859 . 1 1 132 132 LEU HA H 1 3.86 0.03 . 1 . . . . . . . . 4664 1 860 . 1 1 132 132 LEU HB2 H 1 1.63 0.03 . 1 . . . . . . . . 4664 1 861 . 1 1 132 132 LEU HB3 H 1 1.63 0.03 . 1 . . . . . . . . 4664 1 862 . 1 1 132 132 LEU CA C 13 58.58 0.50 . 1 . . . . . . . . 4664 1 863 . 1 1 132 132 LEU C C 13 180.60 0.50 . 1 . . . . . . . . 4664 1 864 . 1 1 132 132 LEU CB C 13 42.45 0.50 . 1 . . . . . . . . 4664 1 865 . 1 1 132 132 LEU N N 15 120.95 0.25 . 1 . . . . . . . . 4664 1 866 . 1 1 133 133 ALA H H 1 8.66 0.03 . 1 . . . . . . . . 4664 1 867 . 1 1 133 133 ALA HA H 1 3.89 0.03 . 1 . . . . . . . . 4664 1 868 . 1 1 133 133 ALA HB1 H 1 0.79 0.03 . 1 . . . . . . . . 4664 1 869 . 1 1 133 133 ALA HB2 H 1 0.79 0.03 . 1 . . . . . . . . 4664 1 870 . 1 1 133 133 ALA HB3 H 1 0.79 0.03 . 1 . . . . . . . . 4664 1 871 . 1 1 133 133 ALA CA C 13 56.04 0.50 . 1 . . . . . . . . 4664 1 872 . 1 1 133 133 ALA C C 13 171.89 0.50 . 1 . . . . . . . . 4664 1 873 . 1 1 133 133 ALA CB C 13 16.93 0.50 . 1 . . . . . . . . 4664 1 874 . 1 1 133 133 ALA N N 15 123.18 0.25 . 1 . . . . . . . . 4664 1 875 . 1 1 134 134 GLY H H 1 8.03 0.03 . 1 . . . . . . . . 4664 1 876 . 1 1 134 134 GLY HA2 H 1 3.81 0.03 . 1 . . . . . . . . 4664 1 877 . 1 1 134 134 GLY HA3 H 1 3.81 0.03 . 1 . . . . . . . . 4664 1 878 . 1 1 134 134 GLY CA C 13 48.08 0.50 . 1 . . . . . . . . 4664 1 879 . 1 1 134 134 GLY C C 13 179.20 0.50 . 1 . . . . . . . . 4664 1 880 . 1 1 134 134 GLY N N 15 108.18 0.25 . 1 . . . . . . . . 4664 1 881 . 1 1 135 135 GLU H H 1 7.63 0.03 . 1 . . . . . . . . 4664 1 882 . 1 1 135 135 GLU HA H 1 3.98 0.03 . 1 . . . . . . . . 4664 1 883 . 1 1 135 135 GLU HB2 H 1 1.95 0.03 . 1 . . . . . . . . 4664 1 884 . 1 1 135 135 GLU HB3 H 1 1.95 0.03 . 1 . . . . . . . . 4664 1 885 . 1 1 135 135 GLU CA C 13 59.38 0.50 . 1 . . . . . . . . 4664 1 886 . 1 1 135 135 GLU C C 13 178.40 0.50 . 1 . . . . . . . . 4664 1 887 . 1 1 135 135 GLU CB C 13 30.51 0.50 . 1 . . . . . . . . 4664 1 888 . 1 1 135 135 GLU N N 15 122.63 0.25 . 1 . . . . . . . . 4664 1 889 . 1 1 136 136 ARG H H 1 7.03 0.03 . 1 . . . . . . . . 4664 1 890 . 1 1 136 136 ARG HA H 1 4.05 0.03 . 1 . . . . . . . . 4664 1 891 . 1 1 136 136 ARG HB2 H 1 1.30 0.03 . 1 . . . . . . . . 4664 1 892 . 1 1 136 136 ARG HB3 H 1 1.30 0.03 . 1 . . . . . . . . 4664 1 893 . 1 1 136 136 ARG CA C 13 55.78 0.50 . 1 . . . . . . . . 4664 1 894 . 1 1 136 136 ARG C C 13 174.50 0.50 . 1 . . . . . . . . 4664 1 895 . 1 1 136 136 ARG CB C 13 29.48 0.50 . 1 . . . . . . . . 4664 1 896 . 1 1 136 136 ARG N N 15 118.75 0.25 . 1 . . . . . . . . 4664 1 897 . 1 1 137 137 ASN H H 1 7.47 0.03 . 1 . . . . . . . . 4664 1 898 . 1 1 137 137 ASN HA H 1 4.06 0.03 . 1 . . . . . . . . 4664 1 899 . 1 1 137 137 ASN HB2 H 1 2.79 0.03 . 2 . . . . . . . . 4664 1 900 . 1 1 137 137 ASN HB3 H 1 2.72 0.03 . 2 . . . . . . . . 4664 1 901 . 1 1 137 137 ASN CA C 13 55.79 0.50 . 1 . . . . . . . . 4664 1 902 . 1 1 137 137 ASN C C 13 175.20 0.50 . 1 . . . . . . . . 4664 1 903 . 1 1 137 137 ASN CB C 13 37.14 0.50 . 1 . . . . . . . . 4664 1 904 . 1 1 137 137 ASN N N 15 110.33 0.25 . 1 . . . . . . . . 4664 1 905 . 1 1 138 138 TYR H H 1 7.92 0.03 . 1 . . . . . . . . 4664 1 906 . 1 1 138 138 TYR HA H 1 5.22 0.03 . 1 . . . . . . . . 4664 1 907 . 1 1 138 138 TYR HB2 H 1 2.50 0.03 . 2 . . . . . . . . 4664 1 908 . 1 1 138 138 TYR HB3 H 1 2.45 0.03 . 2 . . . . . . . . 4664 1 909 . 1 1 138 138 TYR CA C 13 57.67 0.50 . 1 . . . . . . . . 4664 1 910 . 1 1 138 138 TYR C C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 911 . 1 1 138 138 TYR CB C 13 37.57 0.50 . 1 . . . . . . . . 4664 1 912 . 1 1 138 138 TYR N N 15 119.40 0.25 . 1 . . . . . . . . 4664 1 913 . 1 1 139 139 THR H H 1 7.64 0.03 . 1 . . . . . . . . 4664 1 914 . 1 1 139 139 THR HA H 1 4.34 0.03 . 1 . . . . . . . . 4664 1 915 . 1 1 139 139 THR HB H 1 4.63 0.03 . 1 . . . . . . . . 4664 1 916 . 1 1 139 139 THR CA C 13 61.40 0.50 . 1 . . . . . . . . 4664 1 917 . 1 1 139 139 THR C C 13 176.50 0.50 . 1 . . . . . . . . 4664 1 918 . 1 1 139 139 THR CB C 13 71.19 0.50 . 1 . . . . . . . . 4664 1 919 . 1 1 139 139 THR N N 15 115.69 0.25 . 1 . . . . . . . . 4664 1 920 . 1 1 140 140 ASP H H 1 8.52 0.03 . 1 . . . . . . . . 4664 1 921 . 1 1 140 140 ASP HA H 1 4.18 0.03 . 1 . . . . . . . . 4664 1 922 . 1 1 140 140 ASP HB2 H 1 2.61 0.03 . 1 . . . . . . . . 4664 1 923 . 1 1 140 140 ASP HB3 H 1 2.61 0.03 . 1 . . . . . . . . 4664 1 924 . 1 1 140 140 ASP CA C 13 59.04 0.50 . 1 . . . . . . . . 4664 1 925 . 1 1 140 140 ASP C C 13 179.40 0.50 . 1 . . . . . . . . 4664 1 926 . 1 1 140 140 ASP CB C 13 41.89 0.50 . 1 . . . . . . . . 4664 1 927 . 1 1 140 140 ASP N N 15 118.66 0.25 . 1 . . . . . . . . 4664 1 928 . 1 1 141 141 GLU H H 1 8.41 0.03 . 1 . . . . . . . . 4664 1 929 . 1 1 141 141 GLU HA H 1 4.19 0.03 . 1 . . . . . . . . 4664 1 930 . 1 1 141 141 GLU HB2 H 1 2.03 0.03 . 2 . . . . . . . . 4664 1 931 . 1 1 141 141 GLU HB3 H 1 1.97 0.03 . 2 . . . . . . . . 4664 1 932 . 1 1 141 141 GLU CA C 13 59.08 0.50 . 1 . . . . . . . . 4664 1 933 . 1 1 141 141 GLU C C 13 177.20 0.50 . 1 . . . . . . . . 4664 1 934 . 1 1 141 141 GLU CB C 13 30.12 0.50 . 1 . . . . . . . . 4664 1 935 . 1 1 141 141 GLU N N 15 117.55 0.25 . 1 . . . . . . . . 4664 1 936 . 1 1 142 142 MET H H 1 7.87 0.03 . 1 . . . . . . . . 4664 1 937 . 1 1 142 142 MET HA H 1 4.42 0.03 . 1 . . . . . . . . 4664 1 938 . 1 1 142 142 MET CA C 13 56.95 0.50 . 1 . . . . . . . . 4664 1 939 . 1 1 142 142 MET C C 13 173.90 0.50 . 1 . . . . . . . . 4664 1 940 . 1 1 142 142 MET CB C 13 33.63 0.50 . 1 . . . . . . . . 4664 1 941 . 1 1 142 142 MET N N 15 118.24 0.25 . 1 . . . . . . . . 4664 1 942 . 1 1 143 143 VAL H H 1 7.03 0.03 . 1 . . . . . . . . 4664 1 943 . 1 1 143 143 VAL HA H 1 4.71 0.03 . 1 . . . . . . . . 4664 1 944 . 1 1 143 143 VAL HB H 1 2.04 0.03 . 1 . . . . . . . . 4664 1 945 . 1 1 143 143 VAL CA C 13 62.32 0.50 . 1 . . . . . . . . 4664 1 946 . 1 1 143 143 VAL C C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 947 . 1 1 143 143 VAL CB C 13 34.49 0.50 . 1 . . . . . . . . 4664 1 948 . 1 1 143 143 VAL N N 15 117.58 0.25 . 1 . . . . . . . . 4664 1 949 . 1 1 144 144 ALA H H 1 9.52 0.03 . 1 . . . . . . . . 4664 1 950 . 1 1 144 144 ALA HA H 1 4.74 0.03 . 1 . . . . . . . . 4664 1 951 . 1 1 144 144 ALA HB1 H 1 1.21 0.03 . 1 . . . . . . . . 4664 1 952 . 1 1 144 144 ALA HB2 H 1 1.21 0.03 . 1 . . . . . . . . 4664 1 953 . 1 1 144 144 ALA HB3 H 1 1.21 0.03 . 1 . . . . . . . . 4664 1 954 . 1 1 144 144 ALA CA C 13 51.49 0.50 . 1 . . . . . . . . 4664 1 955 . 1 1 144 144 ALA C C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 956 . 1 1 144 144 ALA CB C 13 22.72 0.50 . 1 . . . . . . . . 4664 1 957 . 1 1 144 144 ALA N N 15 131.82 0.25 . 1 . . . . . . . . 4664 1 958 . 1 1 145 145 MET H H 1 8.53 0.03 . 1 . . . . . . . . 4664 1 959 . 1 1 145 145 MET HA H 1 4.85 0.03 . 1 . . . . . . . . 4664 1 960 . 1 1 145 145 MET HB2 H 1 1.99 0.03 . 2 . . . . . . . . 4664 1 961 . 1 1 145 145 MET HB3 H 1 1.93 0.03 . 2 . . . . . . . . 4664 1 962 . 1 1 145 145 MET CA C 13 54.06 0.50 . 1 . . . . . . . . 4664 1 963 . 1 1 145 145 MET C C 13 177.90 0.50 . 1 . . . . . . . . 4664 1 964 . 1 1 145 145 MET CB C 13 30.13 0.50 . 1 . . . . . . . . 4664 1 965 . 1 1 145 145 MET N N 15 123.10 0.25 . 1 . . . . . . . . 4664 1 966 . 1 1 146 146 LEU H H 1 7.81 0.03 . 1 . . . . . . . . 4664 1 967 . 1 1 146 146 LEU CB C 13 42.96 0.50 . 1 . . . . . . . . 4664 1 968 . 1 1 146 146 LEU N N 15 126.17 0.25 . 1 . . . . . . . . 4664 1 969 . 1 1 147 147 PRO HA H 1 4.49 0.03 . 1 . . . . . . . . 4664 1 970 . 1 1 147 147 PRO HB2 H 1 2.31 0.03 . 2 . . . . . . . . 4664 1 971 . 1 1 147 147 PRO HB3 H 1 1.84 0.03 . 2 . . . . . . . . 4664 1 972 . 1 1 147 147 PRO CA C 13 63.23 0.50 . 1 . . . . . . . . 4664 1 973 . 1 1 147 147 PRO C C 13 177.30 0.50 . 1 . . . . . . . . 4664 1 974 . 1 1 147 147 PRO CB C 13 33.73 0.50 . 1 . . . . . . . . 4664 1 975 . 1 1 148 148 ARG H H 1 8.43 0.03 . 1 . . . . . . . . 4664 1 976 . 1 1 148 148 ARG HA H 1 4.18 0.03 . 1 . . . . . . . . 4664 1 977 . 1 1 148 148 ARG HB2 H 1 1.74 0.03 . 2 . . . . . . . . 4664 1 978 . 1 1 148 148 ARG HB3 H 1 1.68 0.03 . 2 . . . . . . . . 4664 1 979 . 1 1 148 148 ARG CA C 13 58.35 0.50 . 1 . . . . . . . . 4664 1 980 . 1 1 148 148 ARG C C 13 176.50 0.50 . 1 . . . . . . . . 4664 1 981 . 1 1 148 148 ARG CB C 13 32.54 0.50 . 1 . . . . . . . . 4664 1 982 . 1 1 148 148 ARG N N 15 121.39 0.25 . 1 . . . . . . . . 4664 1 983 . 1 1 149 149 GLN H H 1 7.66 0.03 . 1 . . . . . . . . 4664 1 984 . 1 1 149 149 GLN HA H 1 4.61 0.03 . 1 . . . . . . . . 4664 1 985 . 1 1 149 149 GLN HB2 H 1 2.06 0.03 . 1 . . . . . . . . 4664 1 986 . 1 1 149 149 GLN HB3 H 1 2.06 0.03 . 1 . . . . . . . . 4664 1 987 . 1 1 149 149 GLN CA C 13 55.72 0.50 . 1 . . . . . . . . 4664 1 988 . 1 1 149 149 GLN C C 13 175.30 0.50 . 1 . . . . . . . . 4664 1 989 . 1 1 149 149 GLN CB C 13 29.67 0.50 . 1 . . . . . . . . 4664 1 990 . 1 1 149 149 GLN N N 15 115.79 0.25 . 1 . . . . . . . . 4664 1 991 . 1 1 150 150 GLU H H 1 8.47 0.03 . 1 . . . . . . . . 4664 1 992 . 1 1 150 150 GLU HA H 1 4.38 0.03 . 1 . . . . . . . . 4664 1 993 . 1 1 150 150 GLU HB2 H 1 2.12 0.03 . 2 . . . . . . . . 4664 1 994 . 1 1 150 150 GLU HB3 H 1 1.63 0.03 . 2 . . . . . . . . 4664 1 995 . 1 1 150 150 GLU CA C 13 56.22 0.50 . 1 . . . . . . . . 4664 1 996 . 1 1 150 150 GLU C C 13 176.70 0.50 . 1 . . . . . . . . 4664 1 997 . 1 1 150 150 GLU CB C 13 32.42 0.50 . 1 . . . . . . . . 4664 1 998 . 1 1 150 150 GLU N N 15 118.54 0.25 . 1 . . . . . . . . 4664 1 999 . 1 1 151 151 GLU H H 1 7.92 0.03 . 1 . . . . . . . . 4664 1 1000 . 1 1 151 151 GLU HA H 1 4.17 0.03 . 1 . . . . . . . . 4664 1 1001 . 1 1 151 151 GLU HB2 H 1 1.99 0.03 . 1 . . . . . . . . 4664 1 1002 . 1 1 151 151 GLU HB3 H 1 1.99 0.03 . 1 . . . . . . . . 4664 1 1003 . 1 1 151 151 GLU CA C 13 59.47 0.50 . 1 . . . . . . . . 4664 1 1004 . 1 1 151 151 GLU C C 13 177.00 0.50 . 1 . . . . . . . . 4664 1 1005 . 1 1 151 151 GLU CB C 13 32.29 0.50 . 1 . . . . . . . . 4664 1 1006 . 1 1 151 151 GLU N N 15 119.93 0.25 . 1 . . . . . . . . 4664 1 1007 . 1 1 152 152 CYS H H 1 9.52 0.03 . 1 . . . . . . . . 4664 1 1008 . 1 1 152 152 CYS HA H 1 5.07 0.03 . 1 . . . . . . . . 4664 1 1009 . 1 1 152 152 CYS HB2 H 1 3.01 0.03 . 1 . . . . . . . . 4664 1 1010 . 1 1 152 152 CYS HB3 H 1 3.01 0.03 . 1 . . . . . . . . 4664 1 1011 . 1 1 152 152 CYS CA C 13 53.99 0.50 . 1 . . . . . . . . 4664 1 1012 . 1 1 152 152 CYS C C 13 173.80 0.50 . 1 . . . . . . . . 4664 1 1013 . 1 1 152 152 CYS CB C 13 35.04 0.50 . 1 . . . . . . . . 4664 1 1014 . 1 1 152 152 CYS N N 15 122.88 0.25 . 1 . . . . . . . . 4664 1 1015 . 1 1 153 153 THR H H 1 8.40 0.03 . 1 . . . . . . . . 4664 1 1016 . 1 1 153 153 THR HA H 1 4.80 0.03 . 1 . . . . . . . . 4664 1 1017 . 1 1 153 153 THR HB H 1 4.03 0.03 . 1 . . . . . . . . 4664 1 1018 . 1 1 153 153 THR CA C 13 59.86 0.50 . 1 . . . . . . . . 4664 1 1019 . 1 1 153 153 THR C C 13 173.90 0.50 . 1 . . . . . . . . 4664 1 1020 . 1 1 153 153 THR CB C 13 72.48 0.50 . 1 . . . . . . . . 4664 1 1021 . 1 1 153 153 THR N N 15 118.84 0.25 . 1 . . . . . . . . 4664 1 1022 . 1 1 154 154 VAL H H 1 6.85 0.03 . 1 . . . . . . . . 4664 1 1023 . 1 1 154 154 VAL HA H 1 4.04 0.03 . 1 . . . . . . . . 4664 1 1024 . 1 1 154 154 VAL HB H 1 1.91 0.03 . 1 . . . . . . . . 4664 1 1025 . 1 1 154 154 VAL CA C 13 62.03 0.50 . 1 . . . . . . . . 4664 1 1026 . 1 1 154 154 VAL C C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 1027 . 1 1 154 154 VAL CB C 13 33.32 0.50 . 1 . . . . . . . . 4664 1 1028 . 1 1 154 154 VAL N N 15 115.82 0.25 . 1 . . . . . . . . 4664 1 1029 . 1 1 155 155 ASP H H 1 8.29 0.03 . 1 . . . . . . . . 4664 1 1030 . 1 1 155 155 ASP HA H 1 4.42 0.03 . 1 . . . . . . . . 4664 1 1031 . 1 1 155 155 ASP HB2 H 1 2.59 0.03 . 2 . . . . . . . . 4664 1 1032 . 1 1 155 155 ASP HB3 H 1 2.34 0.03 . 2 . . . . . . . . 4664 1 1033 . 1 1 155 155 ASP CA C 13 55.77 0.50 . 1 . . . . . . . . 4664 1 1034 . 1 1 155 155 ASP C C 13 176.90 0.50 . 1 . . . . . . . . 4664 1 1035 . 1 1 155 155 ASP CB C 13 42.40 0.50 . 1 . . . . . . . . 4664 1 1036 . 1 1 155 155 ASP N N 15 124.82 0.25 . 1 . . . . . . . . 4664 1 1037 . 1 1 156 156 GLU H H 1 8.35 0.03 . 1 . . . . . . . . 4664 1 1038 . 1 1 156 156 GLU HA H 1 4.11 0.03 . 1 . . . . . . . . 4664 1 1039 . 1 1 156 156 GLU HB2 H 1 1.93 0.03 . 2 . . . . . . . . 4664 1 1040 . 1 1 156 156 GLU HB3 H 1 1.73 0.03 . 2 . . . . . . . . 4664 1 1041 . 1 1 156 156 GLU CA C 13 57.49 0.50 . 1 . . . . . . . . 4664 1 1042 . 1 1 156 156 GLU C C 13 176.45 0.50 . 1 . . . . . . . . 4664 1 1043 . 1 1 156 156 GLU CB C 13 31.50 0.50 . 1 . . . . . . . . 4664 1 1044 . 1 1 156 156 GLU N N 15 121.83 0.25 . 1 . . . . . . . . 4664 1 1045 . 1 1 157 157 VAL H H 1 7.52 0.03 . 1 . . . . . . . . 4664 1 1046 . 1 1 157 157 VAL HA H 1 3.88 0.03 . 1 . . . . . . . . 4664 1 1047 . 1 1 157 157 VAL HB H 1 1.94 0.03 . 1 . . . . . . . . 4664 1 1048 . 1 1 157 157 VAL CA C 13 64.39 0.50 . 1 . . . . . . . . 4664 1 1049 . 1 1 157 157 VAL CB C 13 34.33 0.50 . 1 . . . . . . . . 4664 1 1050 . 1 1 157 157 VAL N N 15 124.69 0.25 . 1 . . . . . . . . 4664 1 stop_ save_