data_5350 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5350 _Entry.Title ; 1H, 15N, and 13C resonance assignments of low molecular weight human cytoplasmic protein tyrosine phosphatase-A (HCPTP-A) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-04-22 _Entry.Accession_date 2002-04-22 _Entry.Last_release_date 2003-01-06 _Entry.Original_release_date 2003-01-06 _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 Vinit Rastogi . K. . 5350 2 Conrad Diven . F. . 5350 3 Genevieve Seabrook . M. . 5350 4 Frank Genbauffe . S. . 5350 5 Randy Bechard . T. . 5350 6 James Fandl . P. . 5350 7 Kevin Peters . G. . 5350 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5350 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 276 5350 '15N chemical shifts' 134 5350 '1H chemical shifts' 237 5350 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2003-01-06 2002-04-22 original author . 5350 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5350 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22223355 _Citation.DOI . _Citation.PubMed_ID 12238601 _Citation.Full_citation . _Citation.Title ; Letter to the Editor: 1H, 15N, and 13C Resonance Assignments of Low Molecular Weight Human Cytoplasmic Protein Tyrosine Phosphatase-A (HCPTP-A) ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 23 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 251 _Citation.Page_last 252 _Citation.Year 2002 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Vinit Rastogi . K. . 5350 1 2 Conrad Diven . F. . 5350 1 3 Genevieve Seabrook . M. . 5350 1 4 Frank Genbauffe . S. . 5350 1 5 Randy Bechard . T. . 5350 1 6 James Fandl . P. . 5350 1 7 Kevin Peters . G. . 5350 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID CSI 5350 1 'Protein Tyrosine Phosphatase (PTP)' 5350 1 'resonance assignment' 5350 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5350 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7727361 _Citation.Full_citation ; Logan TM, Zhou MM, Nettesheim DG, Meadows RP, Van Etten RL, Fesik SW. Solution structure of a low molecular weight protein tyrosine phosphatase. Biochemistry. 1994 Sep 20;33(37):11087-96. ; _Citation.Title 'Solution structure of a low molecular weight protein tyrosine phosphatase.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 33 _Citation.Journal_issue 37 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _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 11087 _Citation.Page_last 11096 _Citation.Year 1994 _Citation.Details ; Protein tyrosine phosphatases (PTPs) are important enzymes involved in signal transduction, cell cycle regulation, and the control of differentiation. Despite the importance of this class of enzymes in the control of critical cell processes, very little structural information is available for this family of proteins. In this paper, we present the first solution structure of a protein tyrosine phosphatase. This protein is a low molecular weight cytosolic PTP that was initially isolated from bovine heart. The structure that was determined from 1747 NMR-derived restraints consists of a central four-stranded parallel beta-sheet surrounded by four alpha-helices and a short 3(10) helix. The phosphate binding site, identified by chemical shift changes upon the addition of the competitive inhibitors phosphate and vanadate, is in a loop region connecting the C-terminal end of the first beta-strand with the first alpha-helix. Residues in the second, fourth, and fifth alpha-helices and in some of the loop regions connecting the elements of regular secondary structure also contribute to the binding site. The structure determined here is consistent with previous mutagenesis and chemical modification studies conducted on this protein. ; 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 'T. M.' Logan T. M. . 5350 2 2 'M. M.' Zhou M. M. . 5350 2 3 'D. G.' Nettesheim D. G. . 5350 2 4 'R. P.' Meadows R. P. . 5350 2 5 'R. L.' 'Van Etten' R. L. . 5350 2 6 'S. W.' Fesik S. W. . 5350 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_HCPTP-A _Assembly.Sf_category assembly _Assembly.Sf_framecode system_HCPTP-A _Assembly.Entry_ID 5350 _Assembly.ID 1 _Assembly.Name 'human cytoplasmic tyrosine phosphatase A' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all free' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number 3.1.3.2 _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 5350 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 HCPTP-A 1 $HCPTP-A . . . native . . . . . 5350 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'human cytoplasmic tyrosine phosphatase A' system 5350 1 HCPTP-A abbreviation 5350 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'protein tyrosine phosphatase' 5350 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HCPTP-A _Entity.Sf_category entity _Entity.Sf_framecode HCPTP-A _Entity.Entry_ID 5350 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'human cytoplasmic protein tyrosine phosphatase-A' _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 ; AEQATKSVLFVCLGNICRSP IAEAVFRKLVTDQNISENWR VDSAATSGYEIGNPPDYRGQ SCMKRHGIPMSHVARQITKE DFATFDYILCMDESNLRDLN RKSNQVKTCKAKIELLGSYD PQKQLIIEDPYYGNDSDFET VYQQCVRCCRAFLEKAH ; _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 free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 18890 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 3N8I . "Crystal Structure Of The A Isoform Of Human Cytoplasmic Protein Tyrosine Phosphatase (Hcptp-A) In Complex With 1-Naphtylacetic " . . . . . 100.00 157 100.00 100.00 1.10e-113 . . . . 5350 1 2 no PDB 5PNT . "Crystal Structure Of A Human Low Molecular Weight Phosphotyrosyl Phosphatase. Implications For Substrate Specificity" . . . . . 100.00 157 100.00 100.00 1.10e-113 . . . . 5350 1 3 no DBJ BAD93075 . "acid phosphatase 1 isoform c variant [Homo sapiens]" . . . . . 100.00 165 99.36 100.00 2.84e-113 . . . . 5350 1 4 no DBJ BAF84550 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 158 100.00 100.00 7.50e-114 . . . . 5350 1 5 no DBJ BAG11407 . "acid phosphatase 1 [synthetic construct]" . . . . . 100.00 158 99.36 100.00 4.60e-113 . . . . 5350 1 6 no EMBL CAH89780 . "hypothetical protein [Pongo abelii]" . . . . . 100.00 158 98.73 100.00 5.79e-113 . . . . 5350 1 7 no GB AAB20259 . "acid phosphatase isozyme Bf, ACP1 isozyme Bf {EC 3.1.3.2} [human, red cells, Peptide, 157 aa]" . . . . . 100.00 157 100.00 100.00 1.10e-113 . . . . 5350 1 8 no GB AAB22514 . "acid phosphatase isoenzyme Af [human, erythrocytes, Peptide, 157 aa]" . . . . . 100.00 157 99.36 100.00 5.02e-113 . . . . 5350 1 9 no GB AAB22515 . "acid phosphatase isoenzyme Cf [human, erythrocytes, Peptide, 157 aa]" . . . . . 100.00 157 100.00 100.00 1.10e-113 . . . . 5350 1 10 no GB AAB27085 . "adipocyte acid phosphatase alpha, partial [Homo sapiens]" . . . . . 87.90 146 99.28 100.00 2.03e-98 . . . . 5350 1 11 no GB AAB59354 . "cytoplasmic phosphotyrosyl protein phosphatase [Homo sapiens]" . . . . . 100.00 158 100.00 100.00 7.50e-114 . . . . 5350 1 12 no REF NP_001124815 . "low molecular weight phosphotyrosine protein phosphatase [Pongo abelii]" . . . . . 100.00 158 98.73 100.00 5.79e-113 . . . . 5350 1 13 no REF NP_004291 . "low molecular weight phosphotyrosine protein phosphatase isoform c [Homo sapiens]" . . . . . 100.00 158 100.00 100.00 7.50e-114 . . . . 5350 1 14 no REF XP_003278849 . "PREDICTED: low molecular weight phosphotyrosine protein phosphatase isoform 1 [Nomascus leucogenys]" . . . . . 100.00 158 99.36 100.00 1.43e-113 . . . . 5350 1 15 no REF XP_003807854 . "PREDICTED: low molecular weight phosphotyrosine protein phosphatase isoform X1 [Pan paniscus]" . . . . . 100.00 158 100.00 100.00 7.50e-114 . . . . 5350 1 16 no REF XP_003908262 . "PREDICTED: low molecular weight phosphotyrosine protein phosphatase isoform X1 [Papio anubis]" . . . . . 99.36 158 98.72 99.36 5.46e-111 . . . . 5350 1 17 no SP P24666 . "RecName: Full=Low molecular weight phosphotyrosine protein phosphatase; Short=LMW-PTP; Short=LMW-PTPase; AltName: Full=Adipocyt" . . . . . 100.00 158 100.00 100.00 7.50e-114 . . . . 5350 1 18 no SP Q5REM7 . "RecName: Full=Low molecular weight phosphotyrosine protein phosphatase; Short=LMW-PTP; Short=LMW-PTPase; AltName: Full=Low mole" . . . . . 100.00 158 98.73 100.00 5.79e-113 . . . . 5350 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'human cytoplasmic protein tyrosine phosphatase-A' common 5350 1 HCPTP-A abbreviation 5350 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . ALA . 5350 1 2 . GLU . 5350 1 3 . GLN . 5350 1 4 . ALA . 5350 1 5 . THR . 5350 1 6 . LYS . 5350 1 7 . SER . 5350 1 8 . VAL . 5350 1 9 . LEU . 5350 1 10 . PHE . 5350 1 11 . VAL . 5350 1 12 . CYS . 5350 1 13 . LEU . 5350 1 14 . GLY . 5350 1 15 . ASN . 5350 1 16 . ILE . 5350 1 17 . CYS . 5350 1 18 . ARG . 5350 1 19 . SER . 5350 1 20 . PRO . 5350 1 21 . ILE . 5350 1 22 . ALA . 5350 1 23 . GLU . 5350 1 24 . ALA . 5350 1 25 . VAL . 5350 1 26 . PHE . 5350 1 27 . ARG . 5350 1 28 . LYS . 5350 1 29 . LEU . 5350 1 30 . VAL . 5350 1 31 . THR . 5350 1 32 . ASP . 5350 1 33 . GLN . 5350 1 34 . ASN . 5350 1 35 . ILE . 5350 1 36 . SER . 5350 1 37 . GLU . 5350 1 38 . ASN . 5350 1 39 . TRP . 5350 1 40 . ARG . 5350 1 41 . VAL . 5350 1 42 . ASP . 5350 1 43 . SER . 5350 1 44 . ALA . 5350 1 45 . ALA . 5350 1 46 . THR . 5350 1 47 . SER . 5350 1 48 . GLY . 5350 1 49 . TYR . 5350 1 50 . GLU . 5350 1 51 . ILE . 5350 1 52 . GLY . 5350 1 53 . ASN . 5350 1 54 . PRO . 5350 1 55 . PRO . 5350 1 56 . ASP . 5350 1 57 . TYR . 5350 1 58 . ARG . 5350 1 59 . GLY . 5350 1 60 . GLN . 5350 1 61 . SER . 5350 1 62 . CYS . 5350 1 63 . MET . 5350 1 64 . LYS . 5350 1 65 . ARG . 5350 1 66 . HIS . 5350 1 67 . GLY . 5350 1 68 . ILE . 5350 1 69 . PRO . 5350 1 70 . MET . 5350 1 71 . SER . 5350 1 72 . HIS . 5350 1 73 . VAL . 5350 1 74 . ALA . 5350 1 75 . ARG . 5350 1 76 . GLN . 5350 1 77 . ILE . 5350 1 78 . THR . 5350 1 79 . LYS . 5350 1 80 . GLU . 5350 1 81 . ASP . 5350 1 82 . PHE . 5350 1 83 . ALA . 5350 1 84 . THR . 5350 1 85 . PHE . 5350 1 86 . ASP . 5350 1 87 . TYR . 5350 1 88 . ILE . 5350 1 89 . LEU . 5350 1 90 . CYS . 5350 1 91 . MET . 5350 1 92 . ASP . 5350 1 93 . GLU . 5350 1 94 . SER . 5350 1 95 . ASN . 5350 1 96 . LEU . 5350 1 97 . ARG . 5350 1 98 . ASP . 5350 1 99 . LEU . 5350 1 100 . ASN . 5350 1 101 . ARG . 5350 1 102 . LYS . 5350 1 103 . SER . 5350 1 104 . ASN . 5350 1 105 . GLN . 5350 1 106 . VAL . 5350 1 107 . LYS . 5350 1 108 . THR . 5350 1 109 . CYS . 5350 1 110 . LYS . 5350 1 111 . ALA . 5350 1 112 . LYS . 5350 1 113 . ILE . 5350 1 114 . GLU . 5350 1 115 . LEU . 5350 1 116 . LEU . 5350 1 117 . GLY . 5350 1 118 . SER . 5350 1 119 . TYR . 5350 1 120 . ASP . 5350 1 121 . PRO . 5350 1 122 . GLN . 5350 1 123 . LYS . 5350 1 124 . GLN . 5350 1 125 . LEU . 5350 1 126 . ILE . 5350 1 127 . ILE . 5350 1 128 . GLU . 5350 1 129 . ASP . 5350 1 130 . PRO . 5350 1 131 . TYR . 5350 1 132 . TYR . 5350 1 133 . GLY . 5350 1 134 . ASN . 5350 1 135 . ASP . 5350 1 136 . SER . 5350 1 137 . ASP . 5350 1 138 . PHE . 5350 1 139 . GLU . 5350 1 140 . THR . 5350 1 141 . VAL . 5350 1 142 . TYR . 5350 1 143 . GLN . 5350 1 144 . GLN . 5350 1 145 . CYS . 5350 1 146 . VAL . 5350 1 147 . ARG . 5350 1 148 . CYS . 5350 1 149 . CYS . 5350 1 150 . ARG . 5350 1 151 . ALA . 5350 1 152 . PHE . 5350 1 153 . LEU . 5350 1 154 . GLU . 5350 1 155 . LYS . 5350 1 156 . ALA . 5350 1 157 . HIS . 5350 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ALA 1 1 5350 1 . GLU 2 2 5350 1 . GLN 3 3 5350 1 . ALA 4 4 5350 1 . THR 5 5 5350 1 . LYS 6 6 5350 1 . SER 7 7 5350 1 . VAL 8 8 5350 1 . LEU 9 9 5350 1 . PHE 10 10 5350 1 . VAL 11 11 5350 1 . CYS 12 12 5350 1 . LEU 13 13 5350 1 . GLY 14 14 5350 1 . ASN 15 15 5350 1 . ILE 16 16 5350 1 . CYS 17 17 5350 1 . ARG 18 18 5350 1 . SER 19 19 5350 1 . PRO 20 20 5350 1 . ILE 21 21 5350 1 . ALA 22 22 5350 1 . GLU 23 23 5350 1 . ALA 24 24 5350 1 . VAL 25 25 5350 1 . PHE 26 26 5350 1 . ARG 27 27 5350 1 . LYS 28 28 5350 1 . LEU 29 29 5350 1 . VAL 30 30 5350 1 . THR 31 31 5350 1 . ASP 32 32 5350 1 . GLN 33 33 5350 1 . ASN 34 34 5350 1 . ILE 35 35 5350 1 . SER 36 36 5350 1 . GLU 37 37 5350 1 . ASN 38 38 5350 1 . TRP 39 39 5350 1 . ARG 40 40 5350 1 . VAL 41 41 5350 1 . ASP 42 42 5350 1 . SER 43 43 5350 1 . ALA 44 44 5350 1 . ALA 45 45 5350 1 . THR 46 46 5350 1 . SER 47 47 5350 1 . GLY 48 48 5350 1 . TYR 49 49 5350 1 . GLU 50 50 5350 1 . ILE 51 51 5350 1 . GLY 52 52 5350 1 . ASN 53 53 5350 1 . PRO 54 54 5350 1 . PRO 55 55 5350 1 . ASP 56 56 5350 1 . TYR 57 57 5350 1 . ARG 58 58 5350 1 . GLY 59 59 5350 1 . GLN 60 60 5350 1 . SER 61 61 5350 1 . CYS 62 62 5350 1 . MET 63 63 5350 1 . LYS 64 64 5350 1 . ARG 65 65 5350 1 . HIS 66 66 5350 1 . GLY 67 67 5350 1 . ILE 68 68 5350 1 . PRO 69 69 5350 1 . MET 70 70 5350 1 . SER 71 71 5350 1 . HIS 72 72 5350 1 . VAL 73 73 5350 1 . ALA 74 74 5350 1 . ARG 75 75 5350 1 . GLN 76 76 5350 1 . ILE 77 77 5350 1 . THR 78 78 5350 1 . LYS 79 79 5350 1 . GLU 80 80 5350 1 . ASP 81 81 5350 1 . PHE 82 82 5350 1 . ALA 83 83 5350 1 . THR 84 84 5350 1 . PHE 85 85 5350 1 . ASP 86 86 5350 1 . TYR 87 87 5350 1 . ILE 88 88 5350 1 . LEU 89 89 5350 1 . CYS 90 90 5350 1 . MET 91 91 5350 1 . ASP 92 92 5350 1 . GLU 93 93 5350 1 . SER 94 94 5350 1 . ASN 95 95 5350 1 . LEU 96 96 5350 1 . ARG 97 97 5350 1 . ASP 98 98 5350 1 . LEU 99 99 5350 1 . ASN 100 100 5350 1 . ARG 101 101 5350 1 . LYS 102 102 5350 1 . SER 103 103 5350 1 . ASN 104 104 5350 1 . GLN 105 105 5350 1 . VAL 106 106 5350 1 . LYS 107 107 5350 1 . THR 108 108 5350 1 . CYS 109 109 5350 1 . LYS 110 110 5350 1 . ALA 111 111 5350 1 . LYS 112 112 5350 1 . ILE 113 113 5350 1 . GLU 114 114 5350 1 . LEU 115 115 5350 1 . LEU 116 116 5350 1 . GLY 117 117 5350 1 . SER 118 118 5350 1 . TYR 119 119 5350 1 . ASP 120 120 5350 1 . PRO 121 121 5350 1 . GLN 122 122 5350 1 . LYS 123 123 5350 1 . GLN 124 124 5350 1 . LEU 125 125 5350 1 . ILE 126 126 5350 1 . ILE 127 127 5350 1 . GLU 128 128 5350 1 . ASP 129 129 5350 1 . PRO 130 130 5350 1 . TYR 131 131 5350 1 . TYR 132 132 5350 1 . GLY 133 133 5350 1 . ASN 134 134 5350 1 . ASP 135 135 5350 1 . SER 136 136 5350 1 . ASP 137 137 5350 1 . PHE 138 138 5350 1 . GLU 139 139 5350 1 . THR 140 140 5350 1 . VAL 141 141 5350 1 . TYR 142 142 5350 1 . GLN 143 143 5350 1 . GLN 144 144 5350 1 . CYS 145 145 5350 1 . VAL 146 146 5350 1 . ARG 147 147 5350 1 . CYS 148 148 5350 1 . CYS 149 149 5350 1 . ARG 150 150 5350 1 . ALA 151 151 5350 1 . PHE 152 152 5350 1 . LEU 153 153 5350 1 . GLU 154 154 5350 1 . LYS 155 155 5350 1 . ALA 156 156 5350 1 . HIS 157 157 5350 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 5350 _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 $HCPTP-A . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5350 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 5350 _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 $HCPTP-A . 'recombinant technology' 'Escherichia coli' 'E. Coli' . . Escherichia coli BL21 DE3 . . . . . . . . . . . . . . . . . . . . . 5350 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5350 _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 'human cytoplasmic protein tyrosine phosphatase-A' '[U-13C; U-15N]' . . 1 $HCPTP-A . . 1.0 . . mM . . . . 5350 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 5350 _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* 5.1 0.2 n/a 5350 1 temperature 298 0.1 K 5350 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 5350 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 5350 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5350 _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 INOVA . 800 . . . 5350 1 2 spectrometer_2 Varian INOVA . 600 . . . 5350 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 5350 _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 'Pulsed field gradients for coherence selection and artifact suppression and' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 5350 1 2 'gradient sensitivity enhancement schemes were applied where appropriate.' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 5350 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 5350 _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 1.000000000 . . . . . . . . . 5350 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5350 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5350 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 5350 _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 . 5350 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 ALA CA C 13 51.850 0.200 . 1 . . . . . . . . 5350 1 2 . 1 1 1 1 ALA C C 13 173.670 0.200 . 1 . . . . . . . . 5350 1 3 . 1 1 2 2 GLU N N 15 120.660 0.050 . 1 . . . . . . . . 5350 1 4 . 1 1 2 2 GLU H H 1 8.740 0.010 . 1 . . . . . . . . 5350 1 5 . 1 1 2 2 GLU HA H 1 4.770 0.010 . 1 . . . . . . . . 5350 1 6 . 1 1 2 2 GLU CA C 13 56.490 0.200 . 1 . . . . . . . . 5350 1 7 . 1 1 2 2 GLU C C 13 176.070 0.200 . 1 . . . . . . . . 5350 1 8 . 1 1 3 3 GLN N N 15 121.790 0.050 . 1 . . . . . . . . 5350 1 9 . 1 1 3 3 GLN H H 1 8.510 0.010 . 1 . . . . . . . . 5350 1 10 . 1 1 3 3 GLN HA H 1 4.330 0.010 . 1 . . . . . . . . 5350 1 11 . 1 1 3 3 GLN CA C 13 55.580 0.200 . 1 . . . . . . . . 5350 1 12 . 1 1 3 3 GLN C C 13 175.270 0.200 . 1 . . . . . . . . 5350 1 13 . 1 1 4 4 ALA N N 15 125.980 0.050 . 1 . . . . . . . . 5350 1 14 . 1 1 4 4 ALA H H 1 8.390 0.010 . 1 . . . . . . . . 5350 1 15 . 1 1 4 4 ALA HA H 1 4.380 0.010 . 1 . . . . . . . . 5350 1 16 . 1 1 4 4 ALA CA C 13 52.510 0.200 . 1 . . . . . . . . 5350 1 17 . 1 1 4 4 ALA C C 13 177.500 0.200 . 1 . . . . . . . . 5350 1 18 . 1 1 5 5 THR N N 15 114.730 0.050 . 1 . . . . . . . . 5350 1 19 . 1 1 5 5 THR H H 1 8.010 0.010 . 1 . . . . . . . . 5350 1 20 . 1 1 5 5 THR HA H 1 4.230 0.010 . 1 . . . . . . . . 5350 1 21 . 1 1 5 5 THR CA C 13 61.970 0.200 . 1 . . . . . . . . 5350 1 22 . 1 1 5 5 THR C C 13 174.230 0.200 . 1 . . . . . . . . 5350 1 23 . 1 1 6 6 LYS N N 15 125.290 0.050 . 1 . . . . . . . . 5350 1 24 . 1 1 6 6 LYS H H 1 7.850 0.010 . 1 . . . . . . . . 5350 1 25 . 1 1 6 6 LYS HA H 1 4.570 0.010 . 1 . . . . . . . . 5350 1 26 . 1 1 6 6 LYS CA C 13 54.950 0.200 . 1 . . . . . . . . 5350 1 27 . 1 1 6 6 LYS C C 13 175.160 0.200 . 1 . . . . . . . . 5350 1 28 . 1 1 7 7 SER N N 15 114.620 0.050 . 1 . . . . . . . . 5350 1 29 . 1 1 7 7 SER H H 1 9.030 0.010 . 1 . . . . . . . . 5350 1 30 . 1 1 7 7 SER HA H 1 6.100 0.010 . 1 . . . . . . . . 5350 1 31 . 1 1 7 7 SER CA C 13 56.720 0.200 . 1 . . . . . . . . 5350 1 32 . 1 1 7 7 SER C C 13 173.460 0.200 . 1 . . . . . . . . 5350 1 33 . 1 1 8 8 VAL N N 15 121.880 0.050 . 1 . . . . . . . . 5350 1 34 . 1 1 8 8 VAL H H 1 9.250 0.010 . 1 . . . . . . . . 5350 1 35 . 1 1 8 8 VAL HA H 1 5.160 0.010 . 1 . . . . . . . . 5350 1 36 . 1 1 8 8 VAL CA C 13 59.310 0.200 . 1 . . . . . . . . 5350 1 37 . 1 1 8 8 VAL C C 13 169.320 0.200 . 1 . . . . . . . . 5350 1 38 . 1 1 9 9 LEU N N 15 128.450 0.050 . 1 . . . . . . . . 5350 1 39 . 1 1 9 9 LEU H H 1 7.980 0.010 . 1 . . . . . . . . 5350 1 40 . 1 1 9 9 LEU CA C 13 51.120 0.200 . 1 . . . . . . . . 5350 1 41 . 1 1 10 10 PHE N N 15 125.300 0.050 . 1 . . . . . . . . 5350 1 42 . 1 1 10 10 PHE H H 1 8.200 0.010 . 1 . . . . . . . . 5350 1 43 . 1 1 10 10 PHE HA H 1 5.160 0.010 . 1 . . . . . . . . 5350 1 44 . 1 1 10 10 PHE CA C 13 56.930 0.200 . 1 . . . . . . . . 5350 1 45 . 1 1 12 12 CYS CA C 13 57.480 0.200 . 1 . . . . . . . . 5350 1 46 . 1 1 12 12 CYS C C 13 175.060 0.200 . 1 . . . . . . . . 5350 1 47 . 1 1 13 13 LEU N N 15 118.810 0.050 . 1 . . . . . . . . 5350 1 48 . 1 1 13 13 LEU H H 1 7.100 0.010 . 1 . . . . . . . . 5350 1 49 . 1 1 13 13 LEU CA C 13 57.680 0.200 . 1 . . . . . . . . 5350 1 50 . 1 1 13 13 LEU C C 13 178.060 0.200 . 1 . . . . . . . . 5350 1 51 . 1 1 14 14 GLY N N 15 103.110 0.050 . 1 . . . . . . . . 5350 1 52 . 1 1 14 14 GLY H H 1 8.560 0.010 . 1 . . . . . . . . 5350 1 53 . 1 1 14 14 GLY HA2 H 1 4.250 0.010 . 2 . . . . . . . . 5350 1 54 . 1 1 14 14 GLY CA C 13 45.670 0.200 . 1 . . . . . . . . 5350 1 55 . 1 1 14 14 GLY C C 13 174.650 0.200 . 1 . . . . . . . . 5350 1 56 . 1 1 15 15 ASN N N 15 118.750 0.050 . 1 . . . . . . . . 5350 1 57 . 1 1 15 15 ASN H H 1 9.130 0.010 . 1 . . . . . . . . 5350 1 58 . 1 1 15 15 ASN CA C 13 54.880 0.200 . 1 . . . . . . . . 5350 1 59 . 1 1 15 15 ASN C C 13 172.000 0.200 . 1 . . . . . . . . 5350 1 60 . 1 1 16 16 ILE N N 15 103.100 0.050 . 1 . . . . . . . . 5350 1 61 . 1 1 16 16 ILE H H 1 7.550 0.010 . 1 . . . . . . . . 5350 1 62 . 1 1 16 16 ILE HA H 1 5.030 0.010 . 1 . . . . . . . . 5350 1 63 . 1 1 16 16 ILE CA C 13 63.000 0.200 . 1 . . . . . . . . 5350 1 64 . 1 1 16 16 ILE C C 13 177.780 0.200 . 1 . . . . . . . . 5350 1 65 . 1 1 17 17 CYS N N 15 122.220 0.050 . 1 . . . . . . . . 5350 1 66 . 1 1 17 17 CYS H H 1 9.580 0.010 . 1 . . . . . . . . 5350 1 67 . 1 1 17 17 CYS HA H 1 4.770 0.010 . 1 . . . . . . . . 5350 1 68 . 1 1 17 17 CYS CA C 13 59.690 0.200 . 1 . . . . . . . . 5350 1 69 . 1 1 17 17 CYS C C 13 175.280 0.200 . 1 . . . . . . . . 5350 1 70 . 1 1 18 18 ARG N N 15 118.740 0.050 . 1 . . . . . . . . 5350 1 71 . 1 1 18 18 ARG H H 1 9.860 0.010 . 1 . . . . . . . . 5350 1 72 . 1 1 18 18 ARG CA C 13 60.260 0.200 . 1 . . . . . . . . 5350 1 73 . 1 1 18 18 ARG C C 13 176.870 0.200 . 1 . . . . . . . . 5350 1 74 . 1 1 19 19 SER N N 15 117.360 0.050 . 1 . . . . . . . . 5350 1 75 . 1 1 19 19 SER H H 1 10.050 0.010 . 1 . . . . . . . . 5350 1 76 . 1 1 19 19 SER CA C 13 64.290 0.200 . 1 . . . . . . . . 5350 1 77 . 1 1 20 20 PRO CA C 13 65.740 0.200 . 1 . . . . . . . . 5350 1 78 . 1 1 20 20 PRO C C 13 179.360 0.200 . 1 . . . . . . . . 5350 1 79 . 1 1 21 21 ILE N N 15 118.450 0.050 . 1 . . . . . . . . 5350 1 80 . 1 1 21 21 ILE H H 1 6.510 0.010 . 1 . . . . . . . . 5350 1 81 . 1 1 21 21 ILE HA H 1 3.860 0.010 . 1 . . . . . . . . 5350 1 82 . 1 1 21 21 ILE CA C 13 65.600 0.200 . 1 . . . . . . . . 5350 1 83 . 1 1 21 21 ILE C C 13 176.300 0.200 . 1 . . . . . . . . 5350 1 84 . 1 1 22 22 ALA N N 15 122.680 0.050 . 1 . . . . . . . . 5350 1 85 . 1 1 22 22 ALA H H 1 7.830 0.010 . 1 . . . . . . . . 5350 1 86 . 1 1 22 22 ALA HA H 1 5.150 0.010 . 1 . . . . . . . . 5350 1 87 . 1 1 22 22 ALA CA C 13 57.000 0.200 . 1 . . . . . . . . 5350 1 88 . 1 1 22 22 ALA C C 13 176.810 0.200 . 1 . . . . . . . . 5350 1 89 . 1 1 23 23 GLU N N 15 115.000 0.050 . 1 . . . . . . . . 5350 1 90 . 1 1 23 23 GLU H H 1 7.850 0.010 . 1 . . . . . . . . 5350 1 91 . 1 1 23 23 GLU HA H 1 3.800 0.010 . 1 . . . . . . . . 5350 1 92 . 1 1 23 23 GLU CA C 13 58.860 0.200 . 1 . . . . . . . . 5350 1 93 . 1 1 23 23 GLU C C 13 176.880 0.200 . 1 . . . . . . . . 5350 1 94 . 1 1 24 24 ALA N N 15 121.320 0.050 . 1 . . . . . . . . 5350 1 95 . 1 1 24 24 ALA H H 1 7.620 0.010 . 1 . . . . . . . . 5350 1 96 . 1 1 24 24 ALA HA H 1 3.990 0.010 . 1 . . . . . . . . 5350 1 97 . 1 1 24 24 ALA CA C 13 55.090 0.200 . 1 . . . . . . . . 5350 1 98 . 1 1 24 24 ALA C C 13 181.230 0.200 . 1 . . . . . . . . 5350 1 99 . 1 1 25 25 VAL N N 15 120.460 0.050 . 1 . . . . . . . . 5350 1 100 . 1 1 25 25 VAL H H 1 8.900 0.010 . 1 . . . . . . . . 5350 1 101 . 1 1 25 25 VAL HA H 1 4.640 0.010 . 1 . . . . . . . . 5350 1 102 . 1 1 25 25 VAL CA C 13 66.830 0.200 . 1 . . . . . . . . 5350 1 103 . 1 1 25 25 VAL C C 13 177.210 0.200 . 1 . . . . . . . . 5350 1 104 . 1 1 26 26 PHE N N 15 121.680 0.050 . 1 . . . . . . . . 5350 1 105 . 1 1 26 26 PHE H H 1 8.700 0.010 . 1 . . . . . . . . 5350 1 106 . 1 1 26 26 PHE CA C 13 63.410 0.200 . 1 . . . . . . . . 5350 1 107 . 1 1 26 26 PHE C C 13 176.880 0.200 . 1 . . . . . . . . 5350 1 108 . 1 1 27 27 ARG N N 15 116.630 0.050 . 1 . . . . . . . . 5350 1 109 . 1 1 27 27 ARG H H 1 8.870 0.010 . 1 . . . . . . . . 5350 1 110 . 1 1 27 27 ARG CA C 13 59.980 0.200 . 1 . . . . . . . . 5350 1 111 . 1 1 27 27 ARG C C 13 179.240 0.200 . 1 . . . . . . . . 5350 1 112 . 1 1 28 28 LYS N N 15 119.100 0.050 . 1 . . . . . . . . 5350 1 113 . 1 1 28 28 LYS H H 1 8.520 0.010 . 1 . . . . . . . . 5350 1 114 . 1 1 28 28 LYS HA H 1 4.900 0.010 . 1 . . . . . . . . 5350 1 115 . 1 1 28 28 LYS CA C 13 60.010 0.200 . 1 . . . . . . . . 5350 1 116 . 1 1 28 28 LYS C C 13 179.570 0.200 . 1 . . . . . . . . 5350 1 117 . 1 1 29 29 LEU N N 15 121.560 0.050 . 1 . . . . . . . . 5350 1 118 . 1 1 29 29 LEU H H 1 7.900 0.010 . 1 . . . . . . . . 5350 1 119 . 1 1 29 29 LEU HA H 1 4.640 0.010 . 1 . . . . . . . . 5350 1 120 . 1 1 29 29 LEU CA C 13 58.460 0.200 . 1 . . . . . . . . 5350 1 121 . 1 1 29 29 LEU C C 13 180.000 0.200 . 1 . . . . . . . . 5350 1 122 . 1 1 30 30 VAL N N 15 109.960 0.050 . 1 . . . . . . . . 5350 1 123 . 1 1 30 30 VAL H H 1 7.920 0.010 . 1 . . . . . . . . 5350 1 124 . 1 1 30 30 VAL HA H 1 3.630 0.010 . 1 . . . . . . . . 5350 1 125 . 1 1 30 30 VAL CA C 13 64.980 0.200 . 1 . . . . . . . . 5350 1 126 . 1 1 30 30 VAL C C 13 178.200 0.200 . 1 . . . . . . . . 5350 1 127 . 1 1 31 31 THR N N 15 119.750 0.050 . 1 . . . . . . . . 5350 1 128 . 1 1 31 31 THR H H 1 7.920 0.010 . 1 . . . . . . . . 5350 1 129 . 1 1 31 31 THR HA H 1 4.120 0.010 . 1 . . . . . . . . 5350 1 130 . 1 1 31 31 THR CA C 13 67.120 0.200 . 1 . . . . . . . . 5350 1 131 . 1 1 31 31 THR C C 13 178.230 0.200 . 1 . . . . . . . . 5350 1 132 . 1 1 32 32 ASP N N 15 125.340 0.050 . 1 . . . . . . . . 5350 1 133 . 1 1 32 32 ASP H H 1 8.950 0.010 . 1 . . . . . . . . 5350 1 134 . 1 1 32 32 ASP HA H 1 6.100 0.010 . 1 . . . . . . . . 5350 1 135 . 1 1 32 32 ASP CA C 13 57.300 0.200 . 1 . . . . . . . . 5350 1 136 . 1 1 32 32 ASP C C 13 178.020 0.200 . 1 . . . . . . . . 5350 1 137 . 1 1 33 33 GLN N N 15 115.100 0.050 . 1 . . . . . . . . 5350 1 138 . 1 1 33 33 GLN H H 1 7.480 0.010 . 1 . . . . . . . . 5350 1 139 . 1 1 33 33 GLN HA H 1 4.330 0.010 . 1 . . . . . . . . 5350 1 140 . 1 1 33 33 GLN CA C 13 55.830 0.200 . 1 . . . . . . . . 5350 1 141 . 1 1 33 33 GLN C C 13 174.660 0.200 . 1 . . . . . . . . 5350 1 142 . 1 1 34 34 ASN N N 15 115.620 0.050 . 1 . . . . . . . . 5350 1 143 . 1 1 34 34 ASN H H 1 8.060 0.010 . 1 . . . . . . . . 5350 1 144 . 1 1 34 34 ASN HA H 1 4.770 0.010 . 1 . . . . . . . . 5350 1 145 . 1 1 34 34 ASN CA C 13 54.790 0.200 . 1 . . . . . . . . 5350 1 146 . 1 1 34 34 ASN C C 13 175.420 0.200 . 1 . . . . . . . . 5350 1 147 . 1 1 35 35 ILE N N 15 110.060 0.050 . 1 . . . . . . . . 5350 1 148 . 1 1 35 35 ILE H H 1 8.250 0.010 . 1 . . . . . . . . 5350 1 149 . 1 1 35 35 ILE HA H 1 4.910 0.010 . 1 . . . . . . . . 5350 1 150 . 1 1 35 35 ILE CA C 13 61.000 0.200 . 1 . . . . . . . . 5350 1 151 . 1 1 35 35 ILE C C 13 177.330 0.200 . 1 . . . . . . . . 5350 1 152 . 1 1 36 36 SER N N 15 118.940 0.050 . 1 . . . . . . . . 5350 1 153 . 1 1 36 36 SER H H 1 8.060 0.010 . 1 . . . . . . . . 5350 1 154 . 1 1 36 36 SER HA H 1 3.990 0.010 . 1 . . . . . . . . 5350 1 155 . 1 1 36 36 SER CA C 13 59.400 0.200 . 1 . . . . . . . . 5350 1 156 . 1 1 36 36 SER C C 13 176.010 0.200 . 1 . . . . . . . . 5350 1 157 . 1 1 37 37 GLU N N 15 116.590 0.050 . 1 . . . . . . . . 5350 1 158 . 1 1 37 37 GLU H H 1 8.240 0.010 . 1 . . . . . . . . 5350 1 159 . 1 1 37 37 GLU CA C 13 58.000 0.200 . 1 . . . . . . . . 5350 1 160 . 1 1 37 37 GLU C C 13 176.680 0.200 . 1 . . . . . . . . 5350 1 161 . 1 1 38 38 ASN N N 15 116.070 0.050 . 1 . . . . . . . . 5350 1 162 . 1 1 38 38 ASN H H 1 7.960 0.010 . 1 . . . . . . . . 5350 1 163 . 1 1 38 38 ASN HA H 1 4.800 0.010 . 1 . . . . . . . . 5350 1 164 . 1 1 38 38 ASN CA C 13 53.640 0.200 . 1 . . . . . . . . 5350 1 165 . 1 1 38 38 ASN C C 13 173.810 0.200 . 1 . . . . . . . . 5350 1 166 . 1 1 39 39 TRP N N 15 119.430 0.050 . 1 . . . . . . . . 5350 1 167 . 1 1 39 39 TRP H H 1 7.830 0.010 . 1 . . . . . . . . 5350 1 168 . 1 1 39 39 TRP HA H 1 5.540 0.010 . 1 . . . . . . . . 5350 1 169 . 1 1 39 39 TRP CA C 13 56.760 0.200 . 1 . . . . . . . . 5350 1 170 . 1 1 39 39 TRP C C 13 175.370 0.200 . 1 . . . . . . . . 5350 1 171 . 1 1 40 40 ARG N N 15 125.010 0.050 . 1 . . . . . . . . 5350 1 172 . 1 1 40 40 ARG H H 1 9.190 0.010 . 1 . . . . . . . . 5350 1 173 . 1 1 40 40 ARG HA H 1 4.900 0.010 . 1 . . . . . . . . 5350 1 174 . 1 1 40 40 ARG CA C 13 55.400 0.200 . 1 . . . . . . . . 5350 1 175 . 1 1 40 40 ARG C C 13 174.690 0.200 . 1 . . . . . . . . 5350 1 176 . 1 1 41 41 VAL N N 15 125.440 0.050 . 1 . . . . . . . . 5350 1 177 . 1 1 41 41 VAL H H 1 8.820 0.010 . 1 . . . . . . . . 5350 1 178 . 1 1 41 41 VAL HA H 1 5.580 0.010 . 1 . . . . . . . . 5350 1 179 . 1 1 41 41 VAL CA C 13 60.050 0.200 . 1 . . . . . . . . 5350 1 180 . 1 1 41 41 VAL C C 13 173.990 0.200 . 1 . . . . . . . . 5350 1 181 . 1 1 42 42 ASP N N 15 124.520 0.050 . 1 . . . . . . . . 5350 1 182 . 1 1 42 42 ASP H H 1 8.480 0.010 . 1 . . . . . . . . 5350 1 183 . 1 1 42 42 ASP HA H 1 5.220 0.010 . 1 . . . . . . . . 5350 1 184 . 1 1 42 42 ASP CA C 13 52.550 0.200 . 1 . . . . . . . . 5350 1 185 . 1 1 42 42 ASP C C 13 174.260 0.200 . 1 . . . . . . . . 5350 1 186 . 1 1 43 43 SER N N 15 114.600 0.050 . 1 . . . . . . . . 5350 1 187 . 1 1 43 43 SER H H 1 8.990 0.010 . 1 . . . . . . . . 5350 1 188 . 1 1 43 43 SER HA H 1 5.440 0.010 . 1 . . . . . . . . 5350 1 189 . 1 1 43 43 SER CA C 13 58.130 0.200 . 1 . . . . . . . . 5350 1 190 . 1 1 43 43 SER C C 13 176.530 0.200 . 1 . . . . . . . . 5350 1 191 . 1 1 44 44 ALA N N 15 118.090 0.050 . 1 . . . . . . . . 5350 1 192 . 1 1 44 44 ALA H H 1 8.530 0.010 . 1 . . . . . . . . 5350 1 193 . 1 1 44 44 ALA HA H 1 4.760 0.010 . 1 . . . . . . . . 5350 1 194 . 1 1 44 44 ALA CA C 13 51.070 0.200 . 1 . . . . . . . . 5350 1 195 . 1 1 44 44 ALA C C 13 174.070 0.200 . 1 . . . . . . . . 5350 1 196 . 1 1 45 45 ALA N N 15 119.040 0.050 . 1 . . . . . . . . 5350 1 197 . 1 1 45 45 ALA H H 1 9.060 0.010 . 1 . . . . . . . . 5350 1 198 . 1 1 45 45 ALA HA H 1 4.380 0.010 . 1 . . . . . . . . 5350 1 199 . 1 1 45 45 ALA CA C 13 49.230 0.200 . 1 . . . . . . . . 5350 1 200 . 1 1 45 45 ALA C C 13 179.430 0.200 . 1 . . . . . . . . 5350 1 201 . 1 1 46 46 THR N N 15 108.890 0.050 . 1 . . . . . . . . 5350 1 202 . 1 1 46 46 THR H H 1 8.730 0.010 . 1 . . . . . . . . 5350 1 203 . 1 1 46 46 THR HA H 1 4.230 0.010 . 1 . . . . . . . . 5350 1 204 . 1 1 46 46 THR CA C 13 64.480 0.200 . 1 . . . . . . . . 5350 1 205 . 1 1 46 46 THR C C 13 175.970 0.200 . 1 . . . . . . . . 5350 1 206 . 1 1 47 47 SER N N 15 118.480 0.050 . 1 . . . . . . . . 5350 1 207 . 1 1 47 47 SER H H 1 8.150 0.010 . 1 . . . . . . . . 5350 1 208 . 1 1 47 47 SER HA H 1 4.070 0.010 . 1 . . . . . . . . 5350 1 209 . 1 1 47 47 SER CA C 13 57.560 0.200 . 1 . . . . . . . . 5350 1 210 . 1 1 47 47 SER C C 13 174.620 0.200 . 1 . . . . . . . . 5350 1 211 . 1 1 48 48 GLY N N 15 108.660 0.050 . 1 . . . . . . . . 5350 1 212 . 1 1 48 48 GLY H H 1 8.470 0.010 . 1 . . . . . . . . 5350 1 213 . 1 1 48 48 GLY CA C 13 44.870 0.200 . 1 . . . . . . . . 5350 1 214 . 1 1 48 48 GLY C C 13 176.270 0.200 . 1 . . . . . . . . 5350 1 215 . 1 1 49 49 TYR N N 15 118.680 0.050 . 1 . . . . . . . . 5350 1 216 . 1 1 49 49 TYR H H 1 7.580 0.010 . 1 . . . . . . . . 5350 1 217 . 1 1 49 49 TYR CA C 13 60.420 0.200 . 1 . . . . . . . . 5350 1 218 . 1 1 49 49 TYR C C 13 176.970 0.200 . 1 . . . . . . . . 5350 1 219 . 1 1 50 50 GLU N N 15 115.210 0.050 . 1 . . . . . . . . 5350 1 220 . 1 1 50 50 GLU H H 1 8.550 0.010 . 1 . . . . . . . . 5350 1 221 . 1 1 50 50 GLU HA H 1 4.480 0.010 . 1 . . . . . . . . 5350 1 222 . 1 1 50 50 GLU CA C 13 54.100 0.200 . 1 . . . . . . . . 5350 1 223 . 1 1 50 50 GLU C C 13 175.140 0.200 . 1 . . . . . . . . 5350 1 224 . 1 1 51 51 ILE N N 15 115.540 0.050 . 1 . . . . . . . . 5350 1 225 . 1 1 51 51 ILE H H 1 6.660 0.010 . 1 . . . . . . . . 5350 1 226 . 1 1 51 51 ILE CA C 13 63.670 0.200 . 1 . . . . . . . . 5350 1 227 . 1 1 51 51 ILE C C 13 176.870 0.200 . 1 . . . . . . . . 5350 1 228 . 1 1 52 52 GLY N N 15 112.140 0.050 . 1 . . . . . . . . 5350 1 229 . 1 1 52 52 GLY H H 1 8.780 0.010 . 1 . . . . . . . . 5350 1 230 . 1 1 52 52 GLY HA2 H 1 4.640 0.010 . 2 . . . . . . . . 5350 1 231 . 1 1 52 52 GLY CA C 13 44.860 0.200 . 1 . . . . . . . . 5350 1 232 . 1 1 52 52 GLY C C 13 174.120 0.200 . 1 . . . . . . . . 5350 1 233 . 1 1 53 53 ASN N N 15 120.410 0.050 . 1 . . . . . . . . 5350 1 234 . 1 1 53 53 ASN H H 1 8.110 0.010 . 1 . . . . . . . . 5350 1 235 . 1 1 53 53 ASN HA H 1 5.230 0.010 . 1 . . . . . . . . 5350 1 236 . 1 1 53 53 ASN CA C 13 51.640 0.200 . 1 . . . . . . . . 5350 1 237 . 1 1 55 55 PRO CA C 13 62.790 0.200 . 1 . . . . . . . . 5350 1 238 . 1 1 55 55 PRO C C 13 176.150 0.200 . 1 . . . . . . . . 5350 1 239 . 1 1 56 56 ASP N N 15 122.330 0.050 . 1 . . . . . . . . 5350 1 240 . 1 1 56 56 ASP H H 1 8.380 0.010 . 1 . . . . . . . . 5350 1 241 . 1 1 56 56 ASP HA H 1 4.250 0.010 . 1 . . . . . . . . 5350 1 242 . 1 1 56 56 ASP CA C 13 54.850 0.200 . 1 . . . . . . . . 5350 1 243 . 1 1 56 56 ASP C C 13 178.530 0.200 . 1 . . . . . . . . 5350 1 244 . 1 1 57 57 TYR N N 15 128.670 0.050 . 1 . . . . . . . . 5350 1 245 . 1 1 57 57 TYR H H 1 9.180 0.010 . 1 . . . . . . . . 5350 1 246 . 1 1 57 57 TYR CA C 13 61.450 0.200 . 1 . . . . . . . . 5350 1 247 . 1 1 57 57 TYR C C 13 176.410 0.200 . 1 . . . . . . . . 5350 1 248 . 1 1 58 58 ARG N N 15 119.290 0.050 . 1 . . . . . . . . 5350 1 249 . 1 1 58 58 ARG H H 1 9.060 0.010 . 1 . . . . . . . . 5350 1 250 . 1 1 58 58 ARG CA C 13 58.110 0.200 . 1 . . . . . . . . 5350 1 251 . 1 1 58 58 ARG C C 13 180.460 0.200 . 1 . . . . . . . . 5350 1 252 . 1 1 59 59 GLY N N 15 110.150 0.050 . 1 . . . . . . . . 5350 1 253 . 1 1 59 59 GLY H H 1 7.190 0.010 . 1 . . . . . . . . 5350 1 254 . 1 1 59 59 GLY HA2 H 1 4.250 0.010 . 2 . . . . . . . . 5350 1 255 . 1 1 59 59 GLY CA C 13 47.340 0.200 . 1 . . . . . . . . 5350 1 256 . 1 1 60 60 GLN CA C 13 59.630 0.200 . 1 . . . . . . . . 5350 1 257 . 1 1 60 60 GLN C C 13 179.150 0.200 . 1 . . . . . . . . 5350 1 258 . 1 1 61 61 SER N N 15 115.220 0.050 . 1 . . . . . . . . 5350 1 259 . 1 1 61 61 SER H H 1 8.300 0.010 . 1 . . . . . . . . 5350 1 260 . 1 1 61 61 SER HA H 1 3.990 0.010 . 1 . . . . . . . . 5350 1 261 . 1 1 61 61 SER CA C 13 61.510 0.200 . 1 . . . . . . . . 5350 1 262 . 1 1 65 65 ARG CA C 13 54.500 0.200 . 1 . . . . . . . . 5350 1 263 . 1 1 65 65 ARG C C 13 175.710 0.200 . 1 . . . . . . . . 5350 1 264 . 1 1 66 66 HIS N N 15 115.990 0.050 . 1 . . . . . . . . 5350 1 265 . 1 1 66 66 HIS H H 1 7.620 0.010 . 1 . . . . . . . . 5350 1 266 . 1 1 66 66 HIS CA C 13 55.800 0.200 . 1 . . . . . . . . 5350 1 267 . 1 1 66 66 HIS C C 13 173.700 0.200 . 1 . . . . . . . . 5350 1 268 . 1 1 67 67 GLY N N 15 110.330 0.050 . 1 . . . . . . . . 5350 1 269 . 1 1 67 67 GLY H H 1 7.900 0.010 . 1 . . . . . . . . 5350 1 270 . 1 1 67 67 GLY HA2 H 1 3.990 0.010 . 2 . . . . . . . . 5350 1 271 . 1 1 67 67 GLY CA C 13 46.810 0.200 . 1 . . . . . . . . 5350 1 272 . 1 1 67 67 GLY C C 13 174.300 0.200 . 1 . . . . . . . . 5350 1 273 . 1 1 68 68 ILE N N 15 121.280 0.050 . 1 . . . . . . . . 5350 1 274 . 1 1 68 68 ILE H H 1 8.130 0.010 . 1 . . . . . . . . 5350 1 275 . 1 1 68 68 ILE HA H 1 4.520 0.010 . 1 . . . . . . . . 5350 1 276 . 1 1 68 68 ILE CA C 13 57.660 0.200 . 1 . . . . . . . . 5350 1 277 . 1 1 69 69 PRO CA C 13 65.140 0.200 . 1 . . . . . . . . 5350 1 278 . 1 1 69 69 PRO C C 13 178.120 0.200 . 1 . . . . . . . . 5350 1 279 . 1 1 70 70 MET N N 15 114.120 0.050 . 1 . . . . . . . . 5350 1 280 . 1 1 70 70 MET H H 1 8.210 0.010 . 1 . . . . . . . . 5350 1 281 . 1 1 70 70 MET HA H 1 4.250 0.010 . 1 . . . . . . . . 5350 1 282 . 1 1 70 70 MET CA C 13 55.640 0.200 . 1 . . . . . . . . 5350 1 283 . 1 1 70 70 MET C C 13 174.200 0.200 . 1 . . . . . . . . 5350 1 284 . 1 1 71 71 SER N N 15 122.470 0.050 . 1 . . . . . . . . 5350 1 285 . 1 1 71 71 SER H H 1 8.790 0.010 . 1 . . . . . . . . 5350 1 286 . 1 1 71 71 SER HA H 1 4.770 0.010 . 1 . . . . . . . . 5350 1 287 . 1 1 71 71 SER CA C 13 57.300 0.200 . 1 . . . . . . . . 5350 1 288 . 1 1 71 71 SER C C 13 172.680 0.200 . 1 . . . . . . . . 5350 1 289 . 1 1 72 72 HIS N N 15 123.760 0.050 . 1 . . . . . . . . 5350 1 290 . 1 1 72 72 HIS H H 1 8.210 0.010 . 1 . . . . . . . . 5350 1 291 . 1 1 72 72 HIS HA H 1 4.770 0.010 . 1 . . . . . . . . 5350 1 292 . 1 1 72 72 HIS CA C 13 56.270 0.200 . 1 . . . . . . . . 5350 1 293 . 1 1 72 72 HIS C C 13 171.520 0.200 . 1 . . . . . . . . 5350 1 294 . 1 1 73 73 VAL N N 15 124.070 0.050 . 1 . . . . . . . . 5350 1 295 . 1 1 73 73 VAL H H 1 7.090 0.010 . 1 . . . . . . . . 5350 1 296 . 1 1 73 73 VAL HA H 1 3.960 0.010 . 1 . . . . . . . . 5350 1 297 . 1 1 73 73 VAL CA C 13 61.210 0.200 . 1 . . . . . . . . 5350 1 298 . 1 1 73 73 VAL C C 13 174.600 0.200 . 1 . . . . . . . . 5350 1 299 . 1 1 74 74 ALA N N 15 127.940 0.050 . 1 . . . . . . . . 5350 1 300 . 1 1 74 74 ALA H H 1 8.720 0.010 . 1 . . . . . . . . 5350 1 301 . 1 1 74 74 ALA HA H 1 4.640 0.010 . 1 . . . . . . . . 5350 1 302 . 1 1 74 74 ALA CA C 13 53.040 0.200 . 1 . . . . . . . . 5350 1 303 . 1 1 74 74 ALA C C 13 178.920 0.200 . 1 . . . . . . . . 5350 1 304 . 1 1 75 75 ARG N N 15 120.230 0.050 . 1 . . . . . . . . 5350 1 305 . 1 1 75 75 ARG H H 1 8.970 0.010 . 1 . . . . . . . . 5350 1 306 . 1 1 75 75 ARG HA H 1 4.770 0.010 . 1 . . . . . . . . 5350 1 307 . 1 1 75 75 ARG CA C 13 53.880 0.200 . 1 . . . . . . . . 5350 1 308 . 1 1 75 75 ARG C C 13 172.460 0.200 . 1 . . . . . . . . 5350 1 309 . 1 1 76 76 GLN N N 15 123.140 0.050 . 1 . . . . . . . . 5350 1 310 . 1 1 76 76 GLN H H 1 8.880 0.010 . 1 . . . . . . . . 5350 1 311 . 1 1 76 76 GLN HA H 1 4.090 0.010 . 1 . . . . . . . . 5350 1 312 . 1 1 76 76 GLN CA C 13 54.620 0.200 . 1 . . . . . . . . 5350 1 313 . 1 1 76 76 GLN C C 13 175.390 0.200 . 1 . . . . . . . . 5350 1 314 . 1 1 77 77 ILE N N 15 126.680 0.050 . 1 . . . . . . . . 5350 1 315 . 1 1 77 77 ILE H H 1 9.000 0.010 . 1 . . . . . . . . 5350 1 316 . 1 1 77 77 ILE CA C 13 61.780 0.200 . 1 . . . . . . . . 5350 1 317 . 1 1 77 77 ILE C C 13 173.310 0.200 . 1 . . . . . . . . 5350 1 318 . 1 1 78 78 THR N N 15 119.510 0.050 . 1 . . . . . . . . 5350 1 319 . 1 1 78 78 THR H H 1 9.500 0.010 . 1 . . . . . . . . 5350 1 320 . 1 1 78 78 THR HA H 1 4.790 0.010 . 1 . . . . . . . . 5350 1 321 . 1 1 78 78 THR CA C 13 59.610 0.200 . 1 . . . . . . . . 5350 1 322 . 1 1 78 78 THR C C 13 175.720 0.200 . 1 . . . . . . . . 5350 1 323 . 1 1 79 79 LYS N N 15 118.670 0.050 . 1 . . . . . . . . 5350 1 324 . 1 1 79 79 LYS H H 1 8.770 0.010 . 1 . . . . . . . . 5350 1 325 . 1 1 79 79 LYS HA H 1 4.190 0.010 . 1 . . . . . . . . 5350 1 326 . 1 1 79 79 LYS CA C 13 59.620 0.200 . 1 . . . . . . . . 5350 1 327 . 1 1 79 79 LYS C C 13 180.900 0.200 . 1 . . . . . . . . 5350 1 328 . 1 1 80 80 GLU N N 15 120.370 0.050 . 1 . . . . . . . . 5350 1 329 . 1 1 80 80 GLU H H 1 7.950 0.010 . 1 . . . . . . . . 5350 1 330 . 1 1 80 80 GLU HA H 1 3.990 0.010 . 1 . . . . . . . . 5350 1 331 . 1 1 80 80 GLU CA C 13 59.440 0.200 . 1 . . . . . . . . 5350 1 332 . 1 1 80 80 GLU C C 13 177.470 0.200 . 1 . . . . . . . . 5350 1 333 . 1 1 81 81 ASP N N 15 119.840 0.050 . 1 . . . . . . . . 5350 1 334 . 1 1 81 81 ASP H H 1 8.030 0.010 . 1 . . . . . . . . 5350 1 335 . 1 1 81 81 ASP HA H 1 3.990 0.010 . 1 . . . . . . . . 5350 1 336 . 1 1 81 81 ASP CA C 13 58.460 0.200 . 1 . . . . . . . . 5350 1 337 . 1 1 81 81 ASP C C 13 178.190 0.200 . 1 . . . . . . . . 5350 1 338 . 1 1 82 82 PHE N N 15 118.960 0.050 . 1 . . . . . . . . 5350 1 339 . 1 1 82 82 PHE H H 1 8.120 0.010 . 1 . . . . . . . . 5350 1 340 . 1 1 82 82 PHE HA H 1 4.130 0.010 . 1 . . . . . . . . 5350 1 341 . 1 1 82 82 PHE CA C 13 59.830 0.200 . 1 . . . . . . . . 5350 1 342 . 1 1 82 82 PHE C C 13 175.920 0.200 . 1 . . . . . . . . 5350 1 343 . 1 1 83 83 ALA N N 15 119.840 0.050 . 1 . . . . . . . . 5350 1 344 . 1 1 83 83 ALA H H 1 7.470 0.010 . 1 . . . . . . . . 5350 1 345 . 1 1 83 83 ALA HA H 1 4.510 0.010 . 1 . . . . . . . . 5350 1 346 . 1 1 83 83 ALA CA C 13 53.150 0.200 . 1 . . . . . . . . 5350 1 347 . 1 1 83 83 ALA C C 13 177.860 0.200 . 1 . . . . . . . . 5350 1 348 . 1 1 84 84 THR N N 15 108.160 0.050 . 1 . . . . . . . . 5350 1 349 . 1 1 84 84 THR H H 1 7.600 0.010 . 1 . . . . . . . . 5350 1 350 . 1 1 84 84 THR HA H 1 4.220 0.010 . 1 . . . . . . . . 5350 1 351 . 1 1 84 84 THR CA C 13 63.100 0.200 . 1 . . . . . . . . 5350 1 352 . 1 1 84 84 THR C C 13 174.650 0.200 . 1 . . . . . . . . 5350 1 353 . 1 1 85 85 PHE N N 15 121.490 0.050 . 1 . . . . . . . . 5350 1 354 . 1 1 85 85 PHE H H 1 7.410 0.010 . 1 . . . . . . . . 5350 1 355 . 1 1 85 85 PHE HA H 1 4.730 0.010 . 1 . . . . . . . . 5350 1 356 . 1 1 85 85 PHE CA C 13 58.990 0.200 . 1 . . . . . . . . 5350 1 357 . 1 1 85 85 PHE C C 13 174.440 0.200 . 1 . . . . . . . . 5350 1 358 . 1 1 86 86 ASP N N 15 118.100 0.050 . 1 . . . . . . . . 5350 1 359 . 1 1 86 86 ASP H H 1 8.230 0.010 . 1 . . . . . . . . 5350 1 360 . 1 1 86 86 ASP HA H 1 4.250 0.010 . 1 . . . . . . . . 5350 1 361 . 1 1 86 86 ASP CA C 13 57.000 0.200 . 1 . . . . . . . . 5350 1 362 . 1 1 86 86 ASP C C 13 177.190 0.200 . 1 . . . . . . . . 5350 1 363 . 1 1 87 87 TYR N N 15 115.940 0.050 . 1 . . . . . . . . 5350 1 364 . 1 1 87 87 TYR H H 1 7.860 0.010 . 1 . . . . . . . . 5350 1 365 . 1 1 87 87 TYR HA H 1 5.170 0.010 . 1 . . . . . . . . 5350 1 366 . 1 1 87 87 TYR CA C 13 57.010 0.200 . 1 . . . . . . . . 5350 1 367 . 1 1 87 87 TYR C C 13 174.110 0.200 . 1 . . . . . . . . 5350 1 368 . 1 1 88 88 ILE N N 15 123.540 0.050 . 1 . . . . . . . . 5350 1 369 . 1 1 88 88 ILE H H 1 9.020 0.010 . 1 . . . . . . . . 5350 1 370 . 1 1 88 88 ILE HA H 1 4.510 0.010 . 1 . . . . . . . . 5350 1 371 . 1 1 88 88 ILE CA C 13 60.720 0.200 . 1 . . . . . . . . 5350 1 372 . 1 1 88 88 ILE C C 13 173.540 0.200 . 1 . . . . . . . . 5350 1 373 . 1 1 89 89 LEU N N 15 125.440 0.050 . 1 . . . . . . . . 5350 1 374 . 1 1 89 89 LEU H H 1 8.330 0.010 . 1 . . . . . . . . 5350 1 375 . 1 1 89 89 LEU HA H 1 5.560 0.010 . 1 . . . . . . . . 5350 1 376 . 1 1 89 89 LEU CA C 13 51.800 0.200 . 1 . . . . . . . . 5350 1 377 . 1 1 89 89 LEU C C 13 176.130 0.200 . 1 . . . . . . . . 5350 1 378 . 1 1 90 90 CYS N N 15 118.810 0.050 . 1 . . . . . . . . 5350 1 379 . 1 1 90 90 CYS H H 1 9.270 0.010 . 1 . . . . . . . . 5350 1 380 . 1 1 90 90 CYS HA H 1 6.280 0.010 . 1 . . . . . . . . 5350 1 381 . 1 1 90 90 CYS CA C 13 54.710 0.200 . 1 . . . . . . . . 5350 1 382 . 1 1 91 91 MET N N 15 128.100 0.050 . 1 . . . . . . . . 5350 1 383 . 1 1 91 91 MET H H 1 10.100 0.010 . 1 . . . . . . . . 5350 1 384 . 1 1 91 91 MET CA C 13 56.900 0.200 . 1 . . . . . . . . 5350 1 385 . 1 1 91 91 MET C C 13 176.590 0.200 . 1 . . . . . . . . 5350 1 386 . 1 1 92 92 ASP N N 15 117.720 0.050 . 1 . . . . . . . . 5350 1 387 . 1 1 92 92 ASP H H 1 7.990 0.010 . 1 . . . . . . . . 5350 1 388 . 1 1 92 92 ASP HA H 1 4.930 0.010 . 1 . . . . . . . . 5350 1 389 . 1 1 92 92 ASP CA C 13 52.520 0.200 . 1 . . . . . . . . 5350 1 390 . 1 1 93 93 GLU CA C 13 59.690 0.200 . 1 . . . . . . . . 5350 1 391 . 1 1 93 93 GLU C C 13 178.910 0.200 . 1 . . . . . . . . 5350 1 392 . 1 1 94 94 SER N N 15 118.680 0.050 . 1 . . . . . . . . 5350 1 393 . 1 1 94 94 SER H H 1 8.380 0.010 . 1 . . . . . . . . 5350 1 394 . 1 1 94 94 SER HA H 1 4.270 0.010 . 1 . . . . . . . . 5350 1 395 . 1 1 94 94 SER CA C 13 61.670 0.200 . 1 . . . . . . . . 5350 1 396 . 1 1 94 94 SER C C 13 176.910 0.200 . 1 . . . . . . . . 5350 1 397 . 1 1 95 95 ASN N N 15 120.580 0.050 . 1 . . . . . . . . 5350 1 398 . 1 1 95 95 ASN H H 1 8.680 0.010 . 1 . . . . . . . . 5350 1 399 . 1 1 95 95 ASN CA C 13 56.180 0.200 . 1 . . . . . . . . 5350 1 400 . 1 1 95 95 ASN C C 13 177.030 0.200 . 1 . . . . . . . . 5350 1 401 . 1 1 96 96 LEU N N 15 117.700 0.050 . 1 . . . . . . . . 5350 1 402 . 1 1 96 96 LEU H H 1 7.940 0.010 . 1 . . . . . . . . 5350 1 403 . 1 1 96 96 LEU HA H 1 4.120 0.010 . 1 . . . . . . . . 5350 1 404 . 1 1 98 98 ASP C C 13 179.210 0.200 . 1 . . . . . . . . 5350 1 405 . 1 1 99 99 LEU N N 15 119.950 0.050 . 1 . . . . . . . . 5350 1 406 . 1 1 99 99 LEU H H 1 8.790 0.010 . 1 . . . . . . . . 5350 1 407 . 1 1 99 99 LEU CA C 13 57.880 0.200 . 1 . . . . . . . . 5350 1 408 . 1 1 99 99 LEU C C 13 178.990 0.200 . 1 . . . . . . . . 5350 1 409 . 1 1 100 100 ASN N N 15 119.560 0.050 . 1 . . . . . . . . 5350 1 410 . 1 1 100 100 ASN H H 1 8.830 0.010 . 1 . . . . . . . . 5350 1 411 . 1 1 100 100 ASN HA H 1 4.510 0.010 . 1 . . . . . . . . 5350 1 412 . 1 1 100 100 ASN CA C 13 56.270 0.200 . 1 . . . . . . . . 5350 1 413 . 1 1 101 101 ARG CA C 13 59.450 0.200 . 1 . . . . . . . . 5350 1 414 . 1 1 101 101 ARG C C 13 179.330 0.200 . 1 . . . . . . . . 5350 1 415 . 1 1 102 102 LYS N N 15 119.610 0.050 . 1 . . . . . . . . 5350 1 416 . 1 1 102 102 LYS H H 1 8.050 0.010 . 1 . . . . . . . . 5350 1 417 . 1 1 102 102 LYS HA H 1 3.860 0.010 . 1 . . . . . . . . 5350 1 418 . 1 1 102 102 LYS CA C 13 59.080 0.200 . 1 . . . . . . . . 5350 1 419 . 1 1 102 102 LYS C C 13 179.200 0.200 . 1 . . . . . . . . 5350 1 420 . 1 1 103 103 SER N N 15 115.220 0.050 . 1 . . . . . . . . 5350 1 421 . 1 1 103 103 SER H H 1 8.420 0.010 . 1 . . . . . . . . 5350 1 422 . 1 1 103 103 SER CA C 13 61.020 0.200 . 1 . . . . . . . . 5350 1 423 . 1 1 103 103 SER C C 13 175.020 0.200 . 1 . . . . . . . . 5350 1 424 . 1 1 104 104 ASN N N 15 118.400 0.050 . 1 . . . . . . . . 5350 1 425 . 1 1 104 104 ASN H H 1 7.170 0.010 . 1 . . . . . . . . 5350 1 426 . 1 1 104 104 ASN HA H 1 4.630 0.010 . 1 . . . . . . . . 5350 1 427 . 1 1 104 104 ASN CA C 13 54.630 0.200 . 1 . . . . . . . . 5350 1 428 . 1 1 104 104 ASN C C 13 175.800 0.200 . 1 . . . . . . . . 5350 1 429 . 1 1 105 105 GLN N N 15 115.990 0.050 . 1 . . . . . . . . 5350 1 430 . 1 1 105 105 GLN H H 1 7.620 0.010 . 1 . . . . . . . . 5350 1 431 . 1 1 105 105 GLN HA H 1 4.300 0.010 . 1 . . . . . . . . 5350 1 432 . 1 1 105 105 GLN CA C 13 55.840 0.200 . 1 . . . . . . . . 5350 1 433 . 1 1 105 105 GLN C C 13 175.930 0.200 . 1 . . . . . . . . 5350 1 434 . 1 1 106 106 VAL N N 15 114.650 0.050 . 1 . . . . . . . . 5350 1 435 . 1 1 106 106 VAL H H 1 7.150 0.010 . 1 . . . . . . . . 5350 1 436 . 1 1 106 106 VAL HA H 1 4.370 0.010 . 1 . . . . . . . . 5350 1 437 . 1 1 106 106 VAL CA C 13 60.440 0.200 . 1 . . . . . . . . 5350 1 438 . 1 1 106 106 VAL C C 13 175.690 0.200 . 1 . . . . . . . . 5350 1 439 . 1 1 107 107 LYS N N 15 123.300 0.050 . 1 . . . . . . . . 5350 1 440 . 1 1 107 107 LYS H H 1 8.610 0.010 . 1 . . . . . . . . 5350 1 441 . 1 1 107 107 LYS HA H 1 4.770 0.010 . 1 . . . . . . . . 5350 1 442 . 1 1 107 107 LYS CA C 13 58.840 0.200 . 1 . . . . . . . . 5350 1 443 . 1 1 107 107 LYS C C 13 177.390 0.200 . 1 . . . . . . . . 5350 1 444 . 1 1 108 108 THR N N 15 111.240 0.050 . 1 . . . . . . . . 5350 1 445 . 1 1 108 108 THR H H 1 7.530 0.010 . 1 . . . . . . . . 5350 1 446 . 1 1 108 108 THR HA H 1 4.380 0.010 . 1 . . . . . . . . 5350 1 447 . 1 1 108 108 THR CA C 13 60.950 0.200 . 1 . . . . . . . . 5350 1 448 . 1 1 108 108 THR C C 13 172.830 0.200 . 1 . . . . . . . . 5350 1 449 . 1 1 109 109 CYS N N 15 126.280 0.050 . 1 . . . . . . . . 5350 1 450 . 1 1 109 109 CYS H H 1 8.670 0.010 . 1 . . . . . . . . 5350 1 451 . 1 1 109 109 CYS HA H 1 4.380 0.010 . 1 . . . . . . . . 5350 1 452 . 1 1 109 109 CYS CA C 13 58.230 0.200 . 1 . . . . . . . . 5350 1 453 . 1 1 109 109 CYS C C 13 173.650 0.200 . 1 . . . . . . . . 5350 1 454 . 1 1 110 110 LYS N N 15 129.080 0.050 . 1 . . . . . . . . 5350 1 455 . 1 1 110 110 LYS H H 1 8.590 0.010 . 1 . . . . . . . . 5350 1 456 . 1 1 110 110 LYS HA H 1 4.360 0.010 . 1 . . . . . . . . 5350 1 457 . 1 1 110 110 LYS CA C 13 56.950 0.200 . 1 . . . . . . . . 5350 1 458 . 1 1 110 110 LYS C C 13 176.370 0.200 . 1 . . . . . . . . 5350 1 459 . 1 1 111 111 ALA N N 15 122.750 0.050 . 1 . . . . . . . . 5350 1 460 . 1 1 111 111 ALA H H 1 7.500 0.010 . 1 . . . . . . . . 5350 1 461 . 1 1 111 111 ALA HA H 1 4.120 0.010 . 1 . . . . . . . . 5350 1 462 . 1 1 111 111 ALA CA C 13 53.230 0.200 . 1 . . . . . . . . 5350 1 463 . 1 1 111 111 ALA C C 13 177.560 0.200 . 1 . . . . . . . . 5350 1 464 . 1 1 112 112 LYS N N 15 122.160 0.050 . 1 . . . . . . . . 5350 1 465 . 1 1 112 112 LYS H H 1 7.680 0.010 . 1 . . . . . . . . 5350 1 466 . 1 1 112 112 LYS HA H 1 4.380 0.010 . 1 . . . . . . . . 5350 1 467 . 1 1 112 112 LYS CA C 13 56.010 0.200 . 1 . . . . . . . . 5350 1 468 . 1 1 112 112 LYS C C 13 175.320 0.200 . 1 . . . . . . . . 5350 1 469 . 1 1 113 113 ILE N N 15 127.170 0.050 . 1 . . . . . . . . 5350 1 470 . 1 1 113 113 ILE H H 1 8.530 0.010 . 1 . . . . . . . . 5350 1 471 . 1 1 113 113 ILE HA H 1 5.050 0.010 . 1 . . . . . . . . 5350 1 472 . 1 1 113 113 ILE CA C 13 60.990 0.200 . 1 . . . . . . . . 5350 1 473 . 1 1 113 113 ILE C C 13 178.340 0.200 . 1 . . . . . . . . 5350 1 474 . 1 1 114 114 GLU N N 15 124.800 0.050 . 1 . . . . . . . . 5350 1 475 . 1 1 114 114 GLU H H 1 8.920 0.010 . 1 . . . . . . . . 5350 1 476 . 1 1 114 114 GLU HA H 1 4.790 0.010 . 1 . . . . . . . . 5350 1 477 . 1 1 114 114 GLU CA C 13 53.820 0.200 . 1 . . . . . . . . 5350 1 478 . 1 1 114 114 GLU C C 13 175.510 0.200 . 1 . . . . . . . . 5350 1 479 . 1 1 115 115 LEU N N 15 121.210 0.050 . 1 . . . . . . . . 5350 1 480 . 1 1 115 115 LEU H H 1 8.950 0.010 . 1 . . . . . . . . 5350 1 481 . 1 1 115 115 LEU HA H 1 4.640 0.010 . 1 . . . . . . . . 5350 1 482 . 1 1 115 115 LEU CA C 13 53.880 0.200 . 1 . . . . . . . . 5350 1 483 . 1 1 116 116 LEU N N 15 131.180 0.050 . 1 . . . . . . . . 5350 1 484 . 1 1 116 116 LEU H H 1 10.040 0.010 . 1 . . . . . . . . 5350 1 485 . 1 1 116 116 LEU HA H 1 5.820 0.010 . 1 . . . . . . . . 5350 1 486 . 1 1 116 116 LEU CA C 13 58.400 0.200 . 1 . . . . . . . . 5350 1 487 . 1 1 116 116 LEU C C 13 178.120 0.200 . 1 . . . . . . . . 5350 1 488 . 1 1 117 117 GLY N N 15 105.000 0.050 . 1 . . . . . . . . 5350 1 489 . 1 1 117 117 GLY H H 1 10.050 0.010 . 1 . . . . . . . . 5350 1 490 . 1 1 117 117 GLY CA C 13 46.400 0.200 . 1 . . . . . . . . 5350 1 491 . 1 1 117 117 GLY C C 13 176.950 0.200 . 1 . . . . . . . . 5350 1 492 . 1 1 118 118 SER N N 15 117.550 0.050 . 1 . . . . . . . . 5350 1 493 . 1 1 118 118 SER H H 1 7.930 0.010 . 1 . . . . . . . . 5350 1 494 . 1 1 118 118 SER HA H 1 4.050 0.010 . 1 . . . . . . . . 5350 1 495 . 1 1 118 118 SER CA C 13 61.650 0.200 . 1 . . . . . . . . 5350 1 496 . 1 1 123 123 LYS CA C 13 57.020 0.200 . 1 . . . . . . . . 5350 1 497 . 1 1 123 123 LYS C C 13 174.940 0.200 . 1 . . . . . . . . 5350 1 498 . 1 1 124 124 GLN N N 15 120.670 0.050 . 1 . . . . . . . . 5350 1 499 . 1 1 124 124 GLN H H 1 8.200 0.010 . 1 . . . . . . . . 5350 1 500 . 1 1 124 124 GLN HA H 1 4.030 0.010 . 1 . . . . . . . . 5350 1 501 . 1 1 124 124 GLN CA C 13 54.600 0.200 . 1 . . . . . . . . 5350 1 502 . 1 1 124 124 GLN C C 13 174.100 0.200 . 1 . . . . . . . . 5350 1 503 . 1 1 125 125 LEU N N 15 122.310 0.050 . 1 . . . . . . . . 5350 1 504 . 1 1 125 125 LEU H H 1 7.290 0.010 . 1 . . . . . . . . 5350 1 505 . 1 1 125 125 LEU HA H 1 3.730 0.010 . 1 . . . . . . . . 5350 1 506 . 1 1 125 125 LEU CA C 13 58.160 0.200 . 1 . . . . . . . . 5350 1 507 . 1 1 125 125 LEU C C 13 178.190 0.200 . 1 . . . . . . . . 5350 1 508 . 1 1 126 126 ILE N N 15 118.620 0.050 . 1 . . . . . . . . 5350 1 509 . 1 1 126 126 ILE H H 1 8.130 0.010 . 1 . . . . . . . . 5350 1 510 . 1 1 126 126 ILE HA H 1 4.070 0.010 . 1 . . . . . . . . 5350 1 511 . 1 1 126 126 ILE CA C 13 58.610 0.200 . 1 . . . . . . . . 5350 1 512 . 1 1 126 126 ILE C C 13 175.800 0.200 . 1 . . . . . . . . 5350 1 513 . 1 1 127 127 ILE N N 15 129.270 0.050 . 1 . . . . . . . . 5350 1 514 . 1 1 127 127 ILE H H 1 7.830 0.010 . 1 . . . . . . . . 5350 1 515 . 1 1 127 127 ILE CA C 13 61.230 0.200 . 1 . . . . . . . . 5350 1 516 . 1 1 127 127 ILE C C 13 175.140 0.200 . 1 . . . . . . . . 5350 1 517 . 1 1 128 128 GLU N N 15 127.870 0.050 . 1 . . . . . . . . 5350 1 518 . 1 1 128 128 GLU H H 1 8.980 0.010 . 1 . . . . . . . . 5350 1 519 . 1 1 128 128 GLU HA H 1 4.130 0.010 . 1 . . . . . . . . 5350 1 520 . 1 1 128 128 GLU CA C 13 56.480 0.200 . 1 . . . . . . . . 5350 1 521 . 1 1 128 128 GLU C C 13 177.240 0.200 . 1 . . . . . . . . 5350 1 522 . 1 1 129 129 ASP N N 15 124.720 0.050 . 1 . . . . . . . . 5350 1 523 . 1 1 129 129 ASP H H 1 8.860 0.010 . 1 . . . . . . . . 5350 1 524 . 1 1 129 129 ASP HA H 1 4.640 0.010 . 1 . . . . . . . . 5350 1 525 . 1 1 129 129 ASP CA C 13 52.270 0.200 . 1 . . . . . . . . 5350 1 526 . 1 1 130 130 PRO CA C 13 62.200 0.200 . 1 . . . . . . . . 5350 1 527 . 1 1 130 130 PRO C C 13 176.150 0.200 . 1 . . . . . . . . 5350 1 528 . 1 1 131 131 TYR N N 15 122.420 0.050 . 1 . . . . . . . . 5350 1 529 . 1 1 131 131 TYR H H 1 7.440 0.010 . 1 . . . . . . . . 5350 1 530 . 1 1 131 131 TYR HA H 1 3.860 0.010 . 1 . . . . . . . . 5350 1 531 . 1 1 131 131 TYR CA C 13 62.380 0.200 . 1 . . . . . . . . 5350 1 532 . 1 1 131 131 TYR C C 13 177.580 0.200 . 1 . . . . . . . . 5350 1 533 . 1 1 132 132 TYR N N 15 116.520 0.050 . 1 . . . . . . . . 5350 1 534 . 1 1 132 132 TYR H H 1 8.690 0.010 . 1 . . . . . . . . 5350 1 535 . 1 1 132 132 TYR HA H 1 4.640 0.010 . 1 . . . . . . . . 5350 1 536 . 1 1 132 132 TYR CA C 13 58.140 0.200 . 1 . . . . . . . . 5350 1 537 . 1 1 132 132 TYR C C 13 175.470 0.200 . 1 . . . . . . . . 5350 1 538 . 1 1 133 133 GLY N N 15 110.640 0.050 . 1 . . . . . . . . 5350 1 539 . 1 1 133 133 GLY H H 1 8.040 0.010 . 1 . . . . . . . . 5350 1 540 . 1 1 133 133 GLY HA2 H 1 4.380 0.010 . 2 . . . . . . . . 5350 1 541 . 1 1 133 133 GLY CA C 13 44.240 0.200 . 1 . . . . . . . . 5350 1 542 . 1 1 133 133 GLY C C 13 173.360 0.200 . 1 . . . . . . . . 5350 1 543 . 1 1 134 134 ASN N N 15 120.260 0.050 . 1 . . . . . . . . 5350 1 544 . 1 1 134 134 ASN H H 1 9.460 0.010 . 1 . . . . . . . . 5350 1 545 . 1 1 134 134 ASN HA H 1 5.290 0.010 . 1 . . . . . . . . 5350 1 546 . 1 1 134 134 ASN CA C 13 51.190 0.200 . 1 . . . . . . . . 5350 1 547 . 1 1 134 134 ASN C C 13 171.310 0.200 . 1 . . . . . . . . 5350 1 548 . 1 1 135 135 ASP N N 15 117.950 0.050 . 1 . . . . . . . . 5350 1 549 . 1 1 135 135 ASP H H 1 8.520 0.010 . 1 . . . . . . . . 5350 1 550 . 1 1 135 135 ASP HA H 1 4.770 0.010 . 1 . . . . . . . . 5350 1 551 . 1 1 135 135 ASP CA C 13 58.110 0.200 . 1 . . . . . . . . 5350 1 552 . 1 1 136 136 SER CA C 13 59.250 0.200 . 1 . . . . . . . . 5350 1 553 . 1 1 136 136 SER C C 13 178.840 0.200 . 1 . . . . . . . . 5350 1 554 . 1 1 137 137 ASP N N 15 122.170 0.050 . 1 . . . . . . . . 5350 1 555 . 1 1 137 137 ASP H H 1 7.870 0.010 . 1 . . . . . . . . 5350 1 556 . 1 1 137 137 ASP HA H 1 5.160 0.010 . 1 . . . . . . . . 5350 1 557 . 1 1 137 137 ASP CA C 13 57.010 0.200 . 1 . . . . . . . . 5350 1 558 . 1 1 137 137 ASP C C 13 178.600 0.200 . 1 . . . . . . . . 5350 1 559 . 1 1 138 138 PHE N N 15 118.530 0.050 . 1 . . . . . . . . 5350 1 560 . 1 1 138 138 PHE H H 1 7.790 0.010 . 1 . . . . . . . . 5350 1 561 . 1 1 138 138 PHE HA H 1 3.740 0.010 . 1 . . . . . . . . 5350 1 562 . 1 1 138 138 PHE CA C 13 63.430 0.200 . 1 . . . . . . . . 5350 1 563 . 1 1 138 138 PHE C C 13 176.650 0.200 . 1 . . . . . . . . 5350 1 564 . 1 1 139 139 GLU N N 15 120.180 0.050 . 1 . . . . . . . . 5350 1 565 . 1 1 139 139 GLU H H 1 7.920 0.010 . 1 . . . . . . . . 5350 1 566 . 1 1 139 139 GLU HA H 1 3.990 0.010 . 1 . . . . . . . . 5350 1 567 . 1 1 139 139 GLU CA C 13 58.900 0.200 . 1 . . . . . . . . 5350 1 568 . 1 1 139 139 GLU C C 13 178.620 0.200 . 1 . . . . . . . . 5350 1 569 . 1 1 140 140 THR N N 15 118.010 0.050 . 1 . . . . . . . . 5350 1 570 . 1 1 140 140 THR H H 1 8.160 0.010 . 1 . . . . . . . . 5350 1 571 . 1 1 140 140 THR CA C 13 67.310 0.200 . 1 . . . . . . . . 5350 1 572 . 1 1 140 140 THR C C 13 175.610 0.200 . 1 . . . . . . . . 5350 1 573 . 1 1 141 141 VAL N N 15 120.820 0.050 . 1 . . . . . . . . 5350 1 574 . 1 1 141 141 VAL H H 1 7.730 0.010 . 1 . . . . . . . . 5350 1 575 . 1 1 141 141 VAL CA C 13 66.900 0.200 . 1 . . . . . . . . 5350 1 576 . 1 1 141 141 VAL C C 13 177.210 0.200 . 1 . . . . . . . . 5350 1 577 . 1 1 142 142 TYR N N 15 121.450 0.050 . 1 . . . . . . . . 5350 1 578 . 1 1 142 142 TYR H H 1 8.690 0.010 . 1 . . . . . . . . 5350 1 579 . 1 1 142 142 TYR CA C 13 62.450 0.200 . 1 . . . . . . . . 5350 1 580 . 1 1 142 142 TYR C C 13 175.650 0.200 . 1 . . . . . . . . 5350 1 581 . 1 1 143 143 GLN N N 15 117.850 0.050 . 1 . . . . . . . . 5350 1 582 . 1 1 143 143 GLN H H 1 8.470 0.010 . 1 . . . . . . . . 5350 1 583 . 1 1 143 143 GLN CA C 13 58.850 0.010 . 1 . . . . . . . . 5350 1 584 . 1 1 143 143 GLN C C 13 180.020 0.200 . 1 . . . . . . . . 5350 1 585 . 1 1 144 144 GLN N N 15 118.260 0.050 . 1 . . . . . . . . 5350 1 586 . 1 1 144 144 GLN H H 1 8.700 0.010 . 1 . . . . . . . . 5350 1 587 . 1 1 144 144 GLN CA C 13 60.790 0.200 . 1 . . . . . . . . 5350 1 588 . 1 1 144 144 GLN C C 13 178.820 0.200 . 1 . . . . . . . . 5350 1 589 . 1 1 145 145 CYS N N 15 117.510 0.050 . 1 . . . . . . . . 5350 1 590 . 1 1 145 145 CYS H H 1 8.720 0.010 . 1 . . . . . . . . 5350 1 591 . 1 1 145 145 CYS CA C 13 66.020 0.200 . 1 . . . . . . . . 5350 1 592 . 1 1 145 145 CYS C C 13 176.930 0.200 . 1 . . . . . . . . 5350 1 593 . 1 1 146 146 VAL N N 15 120.790 0.050 . 1 . . . . . . . . 5350 1 594 . 1 1 146 146 VAL H H 1 8.420 0.010 . 1 . . . . . . . . 5350 1 595 . 1 1 146 146 VAL CA C 13 67.770 0.200 . 1 . . . . . . . . 5350 1 596 . 1 1 146 146 VAL C C 13 177.440 0.200 . 1 . . . . . . . . 5350 1 597 . 1 1 147 147 ARG N N 15 115.510 0.050 . 1 . . . . . . . . 5350 1 598 . 1 1 147 147 ARG H H 1 7.430 0.010 . 1 . . . . . . . . 5350 1 599 . 1 1 147 147 ARG CA C 13 60.340 0.200 . 1 . . . . . . . . 5350 1 600 . 1 1 147 147 ARG C C 13 180.640 0.200 . 1 . . . . . . . . 5350 1 601 . 1 1 148 148 CYS N N 15 116.350 0.050 . 1 . . . . . . . . 5350 1 602 . 1 1 148 148 CYS H H 1 8.490 0.010 . 1 . . . . . . . . 5350 1 603 . 1 1 148 148 CYS CA C 13 64.070 0.200 . 1 . . . . . . . . 5350 1 604 . 1 1 148 148 CYS C C 13 175.440 0.200 . 1 . . . . . . . . 5350 1 605 . 1 1 149 149 CYS N N 15 116.270 0.050 . 1 . . . . . . . . 5350 1 606 . 1 1 149 149 CYS H H 1 8.870 0.010 . 1 . . . . . . . . 5350 1 607 . 1 1 149 149 CYS CA C 13 65.260 0.200 . 1 . . . . . . . . 5350 1 608 . 1 1 149 149 CYS C C 13 176.140 0.200 . 1 . . . . . . . . 5350 1 609 . 1 1 150 150 ARG N N 15 117.810 0.050 . 1 . . . . . . . . 5350 1 610 . 1 1 150 150 ARG H H 1 7.850 0.010 . 1 . . . . . . . . 5350 1 611 . 1 1 150 150 ARG HA H 1 3.780 0.010 . 1 . . . . . . . . 5350 1 612 . 1 1 150 150 ARG CA C 13 60.230 0.200 . 1 . . . . . . . . 5350 1 613 . 1 1 150 150 ARG C C 13 178.200 0.200 . 1 . . . . . . . . 5350 1 614 . 1 1 151 151 ALA N N 15 120.930 0.050 . 1 . . . . . . . . 5350 1 615 . 1 1 151 151 ALA H H 1 7.260 0.010 . 1 . . . . . . . . 5350 1 616 . 1 1 151 151 ALA HA H 1 4.290 0.010 . 1 . . . . . . . . 5350 1 617 . 1 1 151 151 ALA CA C 13 55.240 0.200 . 1 . . . . . . . . 5350 1 618 . 1 1 151 151 ALA C C 13 179.900 0.200 . 1 . . . . . . . . 5350 1 619 . 1 1 152 152 PHE N N 15 120.290 0.050 . 1 . . . . . . . . 5350 1 620 . 1 1 152 152 PHE H H 1 8.480 0.010 . 1 . . . . . . . . 5350 1 621 . 1 1 152 152 PHE HA H 1 4.250 0.010 . 1 . . . . . . . . 5350 1 622 . 1 1 152 152 PHE CA C 13 60.900 0.200 . 1 . . . . . . . . 5350 1 623 . 1 1 152 152 PHE C C 13 176.450 0.200 . 1 . . . . . . . . 5350 1 624 . 1 1 153 153 LEU N N 15 118.180 0.050 . 1 . . . . . . . . 5350 1 625 . 1 1 153 153 LEU H H 1 7.760 0.010 . 1 . . . . . . . . 5350 1 626 . 1 1 153 153 LEU HA H 1 3.730 0.010 . 1 . . . . . . . . 5350 1 627 . 1 1 153 153 LEU CA C 13 57.270 0.200 . 1 . . . . . . . . 5350 1 628 . 1 1 153 153 LEU C C 13 178.850 0.200 . 1 . . . . . . . . 5350 1 629 . 1 1 154 154 GLU N N 15 117.210 0.050 . 1 . . . . . . . . 5350 1 630 . 1 1 154 154 GLU H H 1 7.480 0.010 . 1 . . . . . . . . 5350 1 631 . 1 1 154 154 GLU HA H 1 4.000 0.010 . 1 . . . . . . . . 5350 1 632 . 1 1 154 154 GLU CA C 13 58.700 0.200 . 1 . . . . . . . . 5350 1 633 . 1 1 154 154 GLU C C 13 177.850 0.200 . 1 . . . . . . . . 5350 1 634 . 1 1 155 155 LYS N N 15 118.100 0.050 . 1 . . . . . . . . 5350 1 635 . 1 1 155 155 LYS H H 1 7.660 0.010 . 1 . . . . . . . . 5350 1 636 . 1 1 155 155 LYS HA H 1 4.250 0.010 . 1 . . . . . . . . 5350 1 637 . 1 1 155 155 LYS CA C 13 56.940 0.200 . 1 . . . . . . . . 5350 1 638 . 1 1 155 155 LYS C C 13 175.690 0.200 . 1 . . . . . . . . 5350 1 639 . 1 1 156 156 ALA N N 15 125.900 0.050 . 1 . . . . . . . . 5350 1 640 . 1 1 156 156 ALA H H 1 8.020 0.010 . 1 . . . . . . . . 5350 1 641 . 1 1 156 156 ALA HA H 1 4.250 0.010 . 1 . . . . . . . . 5350 1 642 . 1 1 156 156 ALA CA C 13 52.840 0.200 . 1 . . . . . . . . 5350 1 643 . 1 1 156 156 ALA C C 13 177.210 0.200 . 1 . . . . . . . . 5350 1 644 . 1 1 157 157 HIS N N 15 122.750 0.050 . 1 . . . . . . . . 5350 1 645 . 1 1 157 157 HIS H H 1 8.220 0.010 . 1 . . . . . . . . 5350 1 646 . 1 1 157 157 HIS HA H 1 4.620 0.010 . 1 . . . . . . . . 5350 1 647 . 1 1 157 157 HIS CA C 13 57.270 0.200 . 1 . . . . . . . . 5350 1 stop_ save_