data_5778 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5778 _Entry.Title ; 1H, 15N and 13C chemical shift assignment of the Pleckstrin Homology domain of the Protein kinase B (PKB/Akt) ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2003-04-18 _Entry.Accession_date 2003-04-22 _Entry.Last_release_date 2004-04-07 _Entry.Original_release_date 2004-04-07 _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 Daniel Auguin . . . 5778 2 Philippe Barthe . . . 5778 3 Marie-Therese Auge-Senegas . . . 5778 4 Francois Hoh . . . 5778 5 Masayuki Noguchi . . . 5778 6 Christian Roumestand . . . 5778 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5778 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 650 5778 '15N chemical shifts' 86 5778 '13C chemical shifts' 303 5778 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 . . 2004-04-07 2003-04-18 original author . 5778 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5778 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22855807 _Citation.DOI . _Citation.PubMed_ID 12975590 _Citation.Full_citation . _Citation.Title ; Letter to the Editor: 1H, 15N and 13C Chemical Shift Assignment of the Pleckstrin Homology Domain of the Human Protein Kinase B (PKB/Akt) ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 27 _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 287 _Citation.Page_last 288 _Citation.Year 2003 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Daniel Auguin . . . 5778 1 2 Philippe Barthe . . . 5778 1 3 Marie-Therese Auge-Senegas . . . 5778 1 4 Francois Hoh . . . 5778 1 5 Masayuki Noguchi . . . 5778 1 6 Christian Roumestand . . . 5778 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID PKB 5778 1 Akt 5778 1 'PH domain' 5778 1 'NMR assignments' 5778 1 apoptosis 5778 1 proliferation 5778 1 stop_ save_ save_reference_1 _Citation.Sf_category citations _Citation.Sf_framecode reference_1 _Citation.Entry_ID 5778 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1801921 _Citation.Full_citation ; Jones PF, Jakubowicz T, Hemmings BA. Molecular cloning of a second form of rac protein kinase. Cell Regul. 1991 Dec;2(12):1001-9. ; _Citation.Title 'Molecular cloning of a second form of rac protein kinase.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Cell Regul.' _Citation.Journal_name_full 'Cell regulation' _Citation.Journal_volume 2 _Citation.Journal_issue 12 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1044-2030 _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 1001 _Citation.Page_last 1009 _Citation.Year 1991 _Citation.Details ; A novel serine/threonine protein kinase (termed rac-PK) has recently been identified and cloned from cDNA libraries derived from the human cell lines MCF-7 and WI38. A second form of this protein kinase, termed rac protein kinase beta, has been identified from cDNAs derived from the same cell lines. These two closely related forms show 90% homology, although the beta form with a predicted Mr 60,200 has a carboxyl terminal extension of 40 amino acids in comparison to the alpha form. This extension has a high serine content with 11 serine residues in the last 30 amino acids. The beta form of the protein has been shown by both in vitro translation and bacterial expression to be approximately 5000 Da larger than the alpha form. rac protein kinase beta is encoded by a 3.4-kb transcript and the alpha form is encoded by a 3.2-kb mRNA. Using gene-specific probes both transcripts were detected in all cell types analyzed, although levels of expression were different for the two forms. The catalytic domain of rac protein kinase beta shows a high degree of homology to both the protein kinase C and cyclic AMP-dependent protein kinase families, and hence rac protein kinases appear to represent a new subfamily of the second messenger serine/threonine protein kinases. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'P. F.' Jones P. F. . 5778 2 2 T. Jakubowicz T. . . 5778 2 3 'B. A.' Hemmings B. A. . 5778 2 stop_ save_ save_reference_2 _Citation.Sf_category citations _Citation.Sf_framecode reference_2 _Citation.Entry_ID 5778 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Pons, J.L., Malliavin, T.E. & Delsuc, M.A. (1996) J. Biomol. NMR 8, 445-452. ; _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_PKB-beta-PH _Assembly.Sf_category assembly _Assembly.Sf_framecode system_PKB-beta-PH _Assembly.Entry_ID 5778 _Assembly.ID 1 _Assembly.Name 'Pleckstrin Homology domain of the human Protein Kinase B beta' _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 2.7.1 _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 5778 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 'PKB-beta-PH monomer' 1 $PKB-beta-PH . . . native . . . . . 5778 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 60 60 SG . 1 . 1 CYS 77 77 SG . . . . . . . . . . 5778 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Pleckstrin Homology domain of the human Protein Kinase B beta' system 5778 1 PKB-beta-PH abbreviation 5778 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'binds to phosphatidylinositides' 5778 1 'regulates membrane-anchoring' 5778 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_PKB-beta-PH _Entity.Sf_category entity _Entity.Sf_framecode PKB-beta-PH _Entity.Entry_ID 5778 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Pleckstrin Homology domain of the human Protein Kinase B beta' _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 ; MNEVSVIKEGWLHKRGEYIK TWRPRYFLLKSDGSFIGYKE RPEAPDQTLPPLNNFSVAEC QLMKTERPRPNTFVIRCLQW TTVIERTFHVDSPDEREEWM RAIQMVANSLK ; _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 111 _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 13214 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details 'This sequence concerns the PH domain of the human PKB-beta (AKT2).' _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 1P6S . "Solution Structure Of The Pleckstrin Homology Domain Of Human Protein Kinase B Beta (PkbAKT)" . . . . . 100.00 111 100.00 100.00 1.12e-76 . . . . 5778 1 2 no DBJ BAA06280 . "RAC protein kinase beta [Rattus norvegicus]" . . . . . 100.00 481 99.10 100.00 2.75e-73 . . . . 5778 1 3 no DBJ BAE25779 . "unnamed protein product [Mus musculus]" . . . . . 100.00 481 100.00 100.00 1.26e-73 . . . . 5778 1 4 no DBJ BAE34668 . "unnamed protein product [Mus musculus]" . . . . . 100.00 481 100.00 100.00 1.26e-73 . . . . 5778 1 5 no DBJ BAG37185 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 481 100.00 100.00 9.96e-74 . . . . 5778 1 6 no DBJ BAH14135 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 288 100.00 100.00 5.53e-75 . . . . 5778 1 7 no GB AAA36585 . "rac protein kinase-beta [Homo sapiens]" . . . . . 100.00 520 100.00 100.00 1.06e-73 . . . . 5778 1 8 no GB AAA58364 . "protein serine/threonine kinase [Homo sapiens]" . . . . . 100.00 481 100.00 100.00 9.96e-74 . . . . 5778 1 9 no GB AAA83557 . "serine/threonine kinase [Mus musculus]" . . . . . 100.00 481 100.00 100.00 1.26e-73 . . . . 5778 1 10 no GB AAH26151 . "Thymoma viral proto-oncogene 2 [Mus musculus]" . . . . . 100.00 481 100.00 100.00 1.26e-73 . . . . 5778 1 11 no GB AAH32709 . "AKT2 protein, partial [Homo sapiens]" . . . . . 100.00 344 100.00 100.00 2.31e-75 . . . . 5778 1 12 no REF NP_001103678 . "RAC-beta serine/threonine-protein kinase [Mus musculus]" . . . . . 100.00 481 100.00 100.00 1.26e-73 . . . . 5778 1 13 no REF NP_001167450 . "RAC-beta serine/threonine-protein kinase [Papio anubis]" . . . . . 100.00 481 100.00 100.00 9.65e-74 . . . . 5778 1 14 no REF NP_001193075 . "RAC-beta serine/threonine-protein kinase [Bos taurus]" . . . . . 100.00 481 100.00 100.00 9.54e-74 . . . . 5778 1 15 no REF NP_001243708 . "RAC-beta serine/threonine-protein kinase [Sus scrofa]" . . . . . 100.00 481 100.00 100.00 8.95e-74 . . . . 5778 1 16 no REF NP_001252918 . "RAC-beta serine/threonine-protein kinase [Macaca mulatta]" . . . . . 100.00 481 100.00 100.00 9.65e-74 . . . . 5778 1 17 no SP P31751 . "RecName: Full=RAC-beta serine/threonine-protein kinase; AltName: Full=Protein kinase Akt-2; AltName: Full=Protein kinase B beta" . . . . . 100.00 481 100.00 100.00 9.96e-74 . . . . 5778 1 18 no SP P47197 . "RecName: Full=RAC-beta serine/threonine-protein kinase; AltName: Full=Protein kinase Akt-2; AltName: Full=Protein kinase B beta" . . . . . 100.00 481 99.10 100.00 2.75e-73 . . . . 5778 1 19 no SP Q60823 . "RecName: Full=RAC-beta serine/threonine-protein kinase; AltName: Full=Protein kinase Akt-2; AltName: Full=Protein kinase B beta" . . . . . 100.00 481 100.00 100.00 1.26e-73 . . . . 5778 1 20 no TPG DAA19835 . "TPA: v-akt murine thymoma viral oncogene homolog 2 [Bos taurus]" . . . . . 100.00 481 100.00 100.00 9.54e-74 . . . . 5778 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Pleckstrin Homology domain of the human Protein Kinase B beta' common 5778 1 PKB-beta-PH variant 5778 1 PKB-PH abbreviation 5778 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 . 5778 1 2 . ASN . 5778 1 3 . GLU . 5778 1 4 . VAL . 5778 1 5 . SER . 5778 1 6 . VAL . 5778 1 7 . ILE . 5778 1 8 . LYS . 5778 1 9 . GLU . 5778 1 10 . GLY . 5778 1 11 . TRP . 5778 1 12 . LEU . 5778 1 13 . HIS . 5778 1 14 . LYS . 5778 1 15 . ARG . 5778 1 16 . GLY . 5778 1 17 . GLU . 5778 1 18 . TYR . 5778 1 19 . ILE . 5778 1 20 . LYS . 5778 1 21 . THR . 5778 1 22 . TRP . 5778 1 23 . ARG . 5778 1 24 . PRO . 5778 1 25 . ARG . 5778 1 26 . TYR . 5778 1 27 . PHE . 5778 1 28 . LEU . 5778 1 29 . LEU . 5778 1 30 . LYS . 5778 1 31 . SER . 5778 1 32 . ASP . 5778 1 33 . GLY . 5778 1 34 . SER . 5778 1 35 . PHE . 5778 1 36 . ILE . 5778 1 37 . GLY . 5778 1 38 . TYR . 5778 1 39 . LYS . 5778 1 40 . GLU . 5778 1 41 . ARG . 5778 1 42 . PRO . 5778 1 43 . GLU . 5778 1 44 . ALA . 5778 1 45 . PRO . 5778 1 46 . ASP . 5778 1 47 . GLN . 5778 1 48 . THR . 5778 1 49 . LEU . 5778 1 50 . PRO . 5778 1 51 . PRO . 5778 1 52 . LEU . 5778 1 53 . ASN . 5778 1 54 . ASN . 5778 1 55 . PHE . 5778 1 56 . SER . 5778 1 57 . VAL . 5778 1 58 . ALA . 5778 1 59 . GLU . 5778 1 60 . CYS . 5778 1 61 . GLN . 5778 1 62 . LEU . 5778 1 63 . MET . 5778 1 64 . LYS . 5778 1 65 . THR . 5778 1 66 . GLU . 5778 1 67 . ARG . 5778 1 68 . PRO . 5778 1 69 . ARG . 5778 1 70 . PRO . 5778 1 71 . ASN . 5778 1 72 . THR . 5778 1 73 . PHE . 5778 1 74 . VAL . 5778 1 75 . ILE . 5778 1 76 . ARG . 5778 1 77 . CYS . 5778 1 78 . LEU . 5778 1 79 . GLN . 5778 1 80 . TRP . 5778 1 81 . THR . 5778 1 82 . THR . 5778 1 83 . VAL . 5778 1 84 . ILE . 5778 1 85 . GLU . 5778 1 86 . ARG . 5778 1 87 . THR . 5778 1 88 . PHE . 5778 1 89 . HIS . 5778 1 90 . VAL . 5778 1 91 . ASP . 5778 1 92 . SER . 5778 1 93 . PRO . 5778 1 94 . ASP . 5778 1 95 . GLU . 5778 1 96 . ARG . 5778 1 97 . GLU . 5778 1 98 . GLU . 5778 1 99 . TRP . 5778 1 100 . MET . 5778 1 101 . ARG . 5778 1 102 . ALA . 5778 1 103 . ILE . 5778 1 104 . GLN . 5778 1 105 . MET . 5778 1 106 . VAL . 5778 1 107 . ALA . 5778 1 108 . ASN . 5778 1 109 . SER . 5778 1 110 . LEU . 5778 1 111 . LYS . 5778 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 5778 1 . ASN 2 2 5778 1 . GLU 3 3 5778 1 . VAL 4 4 5778 1 . SER 5 5 5778 1 . VAL 6 6 5778 1 . ILE 7 7 5778 1 . LYS 8 8 5778 1 . GLU 9 9 5778 1 . GLY 10 10 5778 1 . TRP 11 11 5778 1 . LEU 12 12 5778 1 . HIS 13 13 5778 1 . LYS 14 14 5778 1 . ARG 15 15 5778 1 . GLY 16 16 5778 1 . GLU 17 17 5778 1 . TYR 18 18 5778 1 . ILE 19 19 5778 1 . LYS 20 20 5778 1 . THR 21 21 5778 1 . TRP 22 22 5778 1 . ARG 23 23 5778 1 . PRO 24 24 5778 1 . ARG 25 25 5778 1 . TYR 26 26 5778 1 . PHE 27 27 5778 1 . LEU 28 28 5778 1 . LEU 29 29 5778 1 . LYS 30 30 5778 1 . SER 31 31 5778 1 . ASP 32 32 5778 1 . GLY 33 33 5778 1 . SER 34 34 5778 1 . PHE 35 35 5778 1 . ILE 36 36 5778 1 . GLY 37 37 5778 1 . TYR 38 38 5778 1 . LYS 39 39 5778 1 . GLU 40 40 5778 1 . ARG 41 41 5778 1 . PRO 42 42 5778 1 . GLU 43 43 5778 1 . ALA 44 44 5778 1 . PRO 45 45 5778 1 . ASP 46 46 5778 1 . GLN 47 47 5778 1 . THR 48 48 5778 1 . LEU 49 49 5778 1 . PRO 50 50 5778 1 . PRO 51 51 5778 1 . LEU 52 52 5778 1 . ASN 53 53 5778 1 . ASN 54 54 5778 1 . PHE 55 55 5778 1 . SER 56 56 5778 1 . VAL 57 57 5778 1 . ALA 58 58 5778 1 . GLU 59 59 5778 1 . CYS 60 60 5778 1 . GLN 61 61 5778 1 . LEU 62 62 5778 1 . MET 63 63 5778 1 . LYS 64 64 5778 1 . THR 65 65 5778 1 . GLU 66 66 5778 1 . ARG 67 67 5778 1 . PRO 68 68 5778 1 . ARG 69 69 5778 1 . PRO 70 70 5778 1 . ASN 71 71 5778 1 . THR 72 72 5778 1 . PHE 73 73 5778 1 . VAL 74 74 5778 1 . ILE 75 75 5778 1 . ARG 76 76 5778 1 . CYS 77 77 5778 1 . LEU 78 78 5778 1 . GLN 79 79 5778 1 . TRP 80 80 5778 1 . THR 81 81 5778 1 . THR 82 82 5778 1 . VAL 83 83 5778 1 . ILE 84 84 5778 1 . GLU 85 85 5778 1 . ARG 86 86 5778 1 . THR 87 87 5778 1 . PHE 88 88 5778 1 . HIS 89 89 5778 1 . VAL 90 90 5778 1 . ASP 91 91 5778 1 . SER 92 92 5778 1 . PRO 93 93 5778 1 . ASP 94 94 5778 1 . GLU 95 95 5778 1 . ARG 96 96 5778 1 . GLU 97 97 5778 1 . GLU 98 98 5778 1 . TRP 99 99 5778 1 . MET 100 100 5778 1 . ARG 101 101 5778 1 . ALA 102 102 5778 1 . ILE 103 103 5778 1 . GLN 104 104 5778 1 . MET 105 105 5778 1 . VAL 106 106 5778 1 . ALA 107 107 5778 1 . ASN 108 108 5778 1 . SER 109 109 5778 1 . LEU 110 110 5778 1 . LYS 111 111 5778 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 5778 _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 $PKB-beta-PH . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5778 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 5778 _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 $PKB-beta-PH . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21 . . . . . . . . . . . . pGEX-2T . . . . . . . . . 5778 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5778 _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 'Pleckstrin Homology domain of the human Protein Kinase B beta' '[U-95% 13C; U-90% 15N]' . . 1 $PKB-beta-PH . . . 0.3 0.4 mM . . . . 5778 1 stop_ save_ ####################### # Sample conditions # ####################### save_cond_set_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_set_1 _Sample_condition_list.Entry_ID 5778 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.4 0.2 n/a 5778 1 temperature 286 1 K 5778 1 'ionic strength' 0.3 0.02 M 5778 1 stop_ save_ ############################ # Computer software used # ############################ save_GIFA _Software.Sf_category software _Software.Sf_framecode GIFA _Software.Entry_ID 5778 _Software.ID 1 _Software.Name GIFA _Software.Version 4.4 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'NMR processing' 5778 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $reference_2 5778 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 5778 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'A cryogenic probe equipped the 500 MHz spectrometer.' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 5778 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _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 5778 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 500 'A cryogenic probe equipped the 500 MHz spectrometer.' . . 5778 1 2 spectrometer_2 Bruker Avance . 600 . . . 5778 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 5778 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 HNCA . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_set_1 . . . . . . . . . . . . . . . . . . . . . 5778 1 2 HN(CO)CA . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_set_1 . . . . . . . . . . . . . . . . . . . . . 5778 1 3 HNCACB . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_set_1 . . . . . . . . . . . . . . . . . . . . . 5778 1 4 CBCA(CO)NH . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_set_1 . . . . . . . . . . . . . . . . . . . . . 5778 1 5 HNCO . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_set_1 . . . . . . . . . . . . . . . . . . . . . 5778 1 6 HN(CA)CO . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_set_1 . . . . . . . . . . . . . . . . . . . . . 5778 1 7 H(CC)H-TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_set_1 . . . . . . . . . . . . . . . . . . . . . 5778 1 8 '1H-15N NOESY' . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_set_1 . . . . . . . . . . . . . . . . . . . . . 5778 1 9 '1H-13C NOESY' . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_set_1 . . . . . . . . . . . . . . . . . . . . . 5778 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 5778 _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 . . . . . . . . . 5778 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5778 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5778 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 5778 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond_set_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 ; Several unassigned signals were observed that may correspond to local conformational exchange on an intermediate timescale arising from the bridge isomerization. ; _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 . 5778 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 MET H H 1 8.373 0.02 . 1 . . . . . . . . 5778 1 2 . 1 1 1 1 MET N N 15 121.72 0.05 . 1 . . . . . . . . 5778 1 3 . 1 1 1 1 MET CA C 13 55.32 0.05 . 1 . . . . . . . . 5778 1 4 . 1 1 1 1 MET HA H 1 4.386 0.02 . 1 . . . . . . . . 5778 1 5 . 1 1 1 1 MET C C 13 175.61 0.05 . 1 . . . . . . . . 5778 1 6 . 1 1 1 1 MET CB C 13 32.39 0.05 . 1 . . . . . . . . 5778 1 7 . 1 1 1 1 MET HB2 H 1 2.012 0.02 . 2 . . . . . . . . 5778 1 8 . 1 1 1 1 MET HB3 H 1 1.911 0.02 . 2 . . . . . . . . 5778 1 9 . 1 1 2 2 ASN H H 1 8.574 0.02 . 1 . . . . . . . . 5778 1 10 . 1 1 2 2 ASN N N 15 119.81 0.05 . 1 . . . . . . . . 5778 1 11 . 1 1 2 2 ASN CA C 13 53.08 0.05 . 1 . . . . . . . . 5778 1 12 . 1 1 2 2 ASN HA H 1 4.628 0.02 . 1 . . . . . . . . 5778 1 13 . 1 1 2 2 ASN C C 13 174.68 0.05 . 1 . . . . . . . . 5778 1 14 . 1 1 2 2 ASN CB C 13 38.55 0.05 . 1 . . . . . . . . 5778 1 15 . 1 1 2 2 ASN HB2 H 1 2.785 0.02 . 2 . . . . . . . . 5778 1 16 . 1 1 2 2 ASN HB3 H 1 2.696 0.02 . 2 . . . . . . . . 5778 1 17 . 1 1 2 2 ASN HD21 H 1 7.633 0.02 . 2 . . . . . . . . 5778 1 18 . 1 1 2 2 ASN HD22 H 1 6.938 0.02 . 2 . . . . . . . . 5778 1 19 . 1 1 3 3 GLU H H 1 8.274 0.02 . 1 . . . . . . . . 5778 1 20 . 1 1 3 3 GLU N N 15 121.29 0.05 . 1 . . . . . . . . 5778 1 21 . 1 1 3 3 GLU CA C 13 56.04 0.05 . 1 . . . . . . . . 5778 1 22 . 1 1 3 3 GLU HA H 1 4.254 0.02 . 1 . . . . . . . . 5778 1 23 . 1 1 3 3 GLU C C 13 175.69 0.05 . 1 . . . . . . . . 5778 1 24 . 1 1 3 3 GLU CB C 13 30.22 0.05 . 1 . . . . . . . . 5778 1 25 . 1 1 3 3 GLU HB2 H 1 1.965 0.02 . 2 . . . . . . . . 5778 1 26 . 1 1 3 3 GLU HB3 H 1 1.872 0.02 . 2 . . . . . . . . 5778 1 27 . 1 1 3 3 GLU HG2 H 1 2.193 0.02 . 2 . . . . . . . . 5778 1 28 . 1 1 3 3 GLU HG3 H 1 2.172 0.02 . 2 . . . . . . . . 5778 1 29 . 1 1 4 4 VAL H H 1 8.43 0.02 . 1 . . . . . . . . 5778 1 30 . 1 1 4 4 VAL N N 15 124.08 0.05 . 1 . . . . . . . . 5778 1 31 . 1 1 4 4 VAL CA C 13 62.41 0.05 . 1 . . . . . . . . 5778 1 32 . 1 1 4 4 VAL HA H 1 3.886 0.02 . 1 . . . . . . . . 5778 1 33 . 1 1 4 4 VAL C C 13 175.25 0.05 . 1 . . . . . . . . 5778 1 34 . 1 1 4 4 VAL CB C 13 32.28 0.05 . 1 . . . . . . . . 5778 1 35 . 1 1 4 4 VAL HB H 1 1.957 0.02 . 1 . . . . . . . . 5778 1 36 . 1 1 4 4 VAL HG11 H 1 0.955 0.02 . 1 . . . . . . . . 5778 1 37 . 1 1 4 4 VAL HG12 H 1 0.955 0.02 . 1 . . . . . . . . 5778 1 38 . 1 1 4 4 VAL HG13 H 1 0.955 0.02 . 1 . . . . . . . . 5778 1 39 . 1 1 4 4 VAL HG21 H 1 0.925 0.02 . 1 . . . . . . . . 5778 1 40 . 1 1 4 4 VAL HG22 H 1 0.925 0.02 . 1 . . . . . . . . 5778 1 41 . 1 1 4 4 VAL HG23 H 1 0.925 0.02 . 1 . . . . . . . . 5778 1 42 . 1 1 5 5 SER H H 1 8.684 0.02 . 1 . . . . . . . . 5778 1 43 . 1 1 5 5 SER N N 15 122.19 0.05 . 1 . . . . . . . . 5778 1 44 . 1 1 5 5 SER CA C 13 56.36 0.05 . 1 . . . . . . . . 5778 1 45 . 1 1 5 5 SER HA H 1 4.779 0.02 . 1 . . . . . . . . 5778 1 46 . 1 1 5 5 SER C C 13 173.32 0.05 . 1 . . . . . . . . 5778 1 47 . 1 1 5 5 SER CB C 13 65.76 0.05 . 1 . . . . . . . . 5778 1 48 . 1 1 5 5 SER HB2 H 1 3.746 0.02 . 2 . . . . . . . . 5778 1 49 . 1 1 5 5 SER HB3 H 1 3.718 0.02 . 2 . . . . . . . . 5778 1 50 . 1 1 6 6 VAL H H 1 8.853 0.02 . 1 . . . . . . . . 5778 1 51 . 1 1 6 6 VAL N N 15 121.77 0.05 . 1 . . . . . . . . 5778 1 52 . 1 1 6 6 VAL CA C 13 63.5 0.05 . 1 . . . . . . . . 5778 1 53 . 1 1 6 6 VAL HA H 1 3.979 0.02 . 1 . . . . . . . . 5778 1 54 . 1 1 6 6 VAL C C 13 175.72 0.05 . 1 . . . . . . . . 5778 1 55 . 1 1 6 6 VAL CB C 13 31.94 0.05 . 1 . . . . . . . . 5778 1 56 . 1 1 6 6 VAL HB H 1 2.033 0.02 . 1 . . . . . . . . 5778 1 57 . 1 1 6 6 VAL HG11 H 1 0.847 0.02 . 1 . . . . . . . . 5778 1 58 . 1 1 6 6 VAL HG12 H 1 0.847 0.02 . 1 . . . . . . . . 5778 1 59 . 1 1 6 6 VAL HG13 H 1 0.847 0.02 . 1 . . . . . . . . 5778 1 60 . 1 1 6 6 VAL HG21 H 1 0.953 0.02 . 1 . . . . . . . . 5778 1 61 . 1 1 6 6 VAL HG22 H 1 0.953 0.02 . 1 . . . . . . . . 5778 1 62 . 1 1 6 6 VAL HG23 H 1 0.953 0.02 . 1 . . . . . . . . 5778 1 63 . 1 1 7 7 ILE H H 1 9.391 0.02 . 1 . . . . . . . . 5778 1 64 . 1 1 7 7 ILE N N 15 130.58 0.05 . 1 . . . . . . . . 5778 1 65 . 1 1 7 7 ILE CA C 13 59.38 0.05 . 1 . . . . . . . . 5778 1 66 . 1 1 7 7 ILE HA H 1 3.948 0.02 . 1 . . . . . . . . 5778 1 67 . 1 1 7 7 ILE C C 13 175.71 0.05 . 1 . . . . . . . . 5778 1 68 . 1 1 7 7 ILE CB C 13 37.08 0.05 . 1 . . . . . . . . 5778 1 69 . 1 1 7 7 ILE HB H 1 1.542 0.02 . 1 . . . . . . . . 5778 1 70 . 1 1 7 7 ILE HG21 H 1 0.675 0.02 . 1 . . . . . . . . 5778 1 71 . 1 1 7 7 ILE HG22 H 1 0.675 0.02 . 1 . . . . . . . . 5778 1 72 . 1 1 7 7 ILE HG23 H 1 0.675 0.02 . 1 . . . . . . . . 5778 1 73 . 1 1 7 7 ILE HG12 H 1 1.12 0.02 . 2 . . . . . . . . 5778 1 74 . 1 1 7 7 ILE CD1 C 13 8.45 0.05 . 1 . . . . . . . . 5778 1 75 . 1 1 7 7 ILE HD11 H 1 0.568 0.02 . 1 . . . . . . . . 5778 1 76 . 1 1 7 7 ILE HD12 H 1 0.568 0.02 . 1 . . . . . . . . 5778 1 77 . 1 1 7 7 ILE HD13 H 1 0.568 0.02 . 1 . . . . . . . . 5778 1 78 . 1 1 8 8 LYS H H 1 7.572 0.02 . 1 . . . . . . . . 5778 1 79 . 1 1 8 8 LYS N N 15 119.57 0.05 . 1 . . . . . . . . 5778 1 80 . 1 1 8 8 LYS CA C 13 55.49 0.05 . 1 . . . . . . . . 5778 1 81 . 1 1 8 8 LYS HA H 1 4.229 0.02 . 1 . . . . . . . . 5778 1 82 . 1 1 8 8 LYS C C 13 171.38 0.05 . 1 . . . . . . . . 5778 1 83 . 1 1 8 8 LYS CB C 13 35.98 0.05 . 1 . . . . . . . . 5778 1 84 . 1 1 8 8 LYS HB2 H 1 2.1 0.02 . 2 . . . . . . . . 5778 1 85 . 1 1 8 8 LYS HG2 H 1 1.666 0.02 . 2 . . . . . . . . 5778 1 86 . 1 1 8 8 LYS HG3 H 1 1.567 0.02 . 2 . . . . . . . . 5778 1 87 . 1 1 8 8 LYS HD2 H 1 1.805 0.02 . 2 . . . . . . . . 5778 1 88 . 1 1 8 8 LYS HE2 H 1 3.078 0.02 . 2 . . . . . . . . 5778 1 89 . 1 1 9 9 GLU H H 1 8.338 0.02 . 1 . . . . . . . . 5778 1 90 . 1 1 9 9 GLU N N 15 121.03 0.05 . 1 . . . . . . . . 5778 1 91 . 1 1 9 9 GLU CA C 13 53.22 0.05 . 1 . . . . . . . . 5778 1 92 . 1 1 9 9 GLU HA H 1 5.923 0.02 . 1 . . . . . . . . 5778 1 93 . 1 1 9 9 GLU C C 13 174.43 0.05 . 1 . . . . . . . . 5778 1 94 . 1 1 9 9 GLU HB2 H 1 2.147 0.02 . 2 . . . . . . . . 5778 1 95 . 1 1 9 9 GLU HB3 H 1 2.039 0.02 . 2 . . . . . . . . 5778 1 96 . 1 1 9 9 GLU HG2 H 1 2.652 0.02 . 2 . . . . . . . . 5778 1 97 . 1 1 9 9 GLU HG3 H 1 2.375 0.02 . 2 . . . . . . . . 5778 1 98 . 1 1 10 10 GLY H H 1 8.525 0.02 . 1 . . . . . . . . 5778 1 99 . 1 1 10 10 GLY N N 15 107.83 0.05 . 1 . . . . . . . . 5778 1 100 . 1 1 10 10 GLY CA C 13 44.96 0.05 . 1 . . . . . . . . 5778 1 101 . 1 1 10 10 GLY HA2 H 1 3.658 0.02 . 1 . . . . . . . . 5778 1 102 . 1 1 10 10 GLY HA3 H 1 4.579 0.02 . 1 . . . . . . . . 5778 1 103 . 1 1 10 10 GLY C C 13 170.45 0.05 . 1 . . . . . . . . 5778 1 104 . 1 1 11 11 TRP H H 1 8.767 0.02 . 1 . . . . . . . . 5778 1 105 . 1 1 11 11 TRP N N 15 118.84 0.05 . 1 . . . . . . . . 5778 1 106 . 1 1 11 11 TRP CA C 13 57.64 0.05 . 1 . . . . . . . . 5778 1 107 . 1 1 11 11 TRP HA H 1 4.964 0.02 . 1 . . . . . . . . 5778 1 108 . 1 1 11 11 TRP C C 13 177.26 0.05 . 1 . . . . . . . . 5778 1 109 . 1 1 11 11 TRP CB C 13 30.13 0.05 . 1 . . . . . . . . 5778 1 110 . 1 1 11 11 TRP HB2 H 1 3.186 0.02 . 2 . . . . . . . . 5778 1 111 . 1 1 11 11 TRP HB3 H 1 3.15 0.02 . 2 . . . . . . . . 5778 1 112 . 1 1 11 11 TRP HD1 H 1 7.596 0.02 . 1 . . . . . . . . 5778 1 113 . 1 1 11 11 TRP HE1 H 1 10.53 0.02 . 1 . . . . . . . . 5778 1 114 . 1 1 11 11 TRP HE3 H 1 7.431 0.02 . 1 . . . . . . . . 5778 1 115 . 1 1 11 11 TRP HZ2 H 1 6.483 0.02 . 1 . . . . . . . . 5778 1 116 . 1 1 11 11 TRP HZ3 H 1 6.863 0.02 . 1 . . . . . . . . 5778 1 117 . 1 1 11 11 TRP HH2 H 1 7.643 0.02 . 1 . . . . . . . . 5778 1 118 . 1 1 12 12 LEU H H 1 9.586 0.02 . 1 . . . . . . . . 5778 1 119 . 1 1 12 12 LEU N N 15 122.08 0.05 . 1 . . . . . . . . 5778 1 120 . 1 1 12 12 LEU CA C 13 53.88 0.05 . 1 . . . . . . . . 5778 1 121 . 1 1 12 12 LEU HA H 1 4.68 0.02 . 1 . . . . . . . . 5778 1 122 . 1 1 12 12 LEU C C 13 175.66 0.05 . 1 . . . . . . . . 5778 1 123 . 1 1 12 12 LEU CB C 13 47.68 0.05 . 1 . . . . . . . . 5778 1 124 . 1 1 12 12 LEU HB2 H 1 1.516 0.02 . 2 . . . . . . . . 5778 1 125 . 1 1 12 12 LEU HB3 H 1 1.215 0.02 . 2 . . . . . . . . 5778 1 126 . 1 1 12 12 LEU HG H 1 1.04 0.02 . 1 . . . . . . . . 5778 1 127 . 1 1 12 12 LEU CD1 C 13 24.74 0.05 . 1 . . . . . . . . 5778 1 128 . 1 1 12 12 LEU HD11 H 1 -0.61 0.02 . 1 . . . . . . . . 5778 1 129 . 1 1 12 12 LEU HD12 H 1 -0.61 0.02 . 1 . . . . . . . . 5778 1 130 . 1 1 12 12 LEU HD13 H 1 -0.61 0.02 . 1 . . . . . . . . 5778 1 131 . 1 1 12 12 LEU CD2 C 13 24.51 0.05 . 1 . . . . . . . . 5778 1 132 . 1 1 12 12 LEU HD21 H 1 -0.15 0.02 . 1 . . . . . . . . 5778 1 133 . 1 1 12 12 LEU HD22 H 1 -0.15 0.02 . 1 . . . . . . . . 5778 1 134 . 1 1 12 12 LEU HD23 H 1 -0.15 0.02 . 1 . . . . . . . . 5778 1 135 . 1 1 13 13 HIS H H 1 8.34 0.02 . 1 . . . . . . . . 5778 1 136 . 1 1 13 13 HIS N N 15 118.71 0.05 . 1 . . . . . . . . 5778 1 137 . 1 1 13 13 HIS CA C 13 55.39 0.05 . 1 . . . . . . . . 5778 1 138 . 1 1 13 13 HIS HA H 1 5.206 0.02 . 1 . . . . . . . . 5778 1 139 . 1 1 13 13 HIS HB2 H 1 2.843 0.02 . 2 . . . . . . . . 5778 1 140 . 1 1 13 13 HIS HB3 H 1 2.768 0.02 . 2 . . . . . . . . 5778 1 141 . 1 1 13 13 HIS HD2 H 1 6.627 0.02 . 1 . . . . . . . . 5778 1 142 . 1 1 13 13 HIS HE1 H 1 7.8 0.02 . 1 . . . . . . . . 5778 1 143 . 1 1 14 14 LYS HA H 1 4.02 0.02 . 1 . . . . . . . . 5778 1 144 . 1 1 14 14 LYS C C 13 175.23 0.05 . 1 . . . . . . . . 5778 1 145 . 1 1 14 14 LYS HB2 H 1 1.625 0.02 . 2 . . . . . . . . 5778 1 146 . 1 1 14 14 LYS HG2 H 1 1.236 0.02 . 2 . . . . . . . . 5778 1 147 . 1 1 14 14 LYS HG3 H 1 1.109 0.02 . 2 . . . . . . . . 5778 1 148 . 1 1 14 14 LYS HD2 H 1 1.463 0.02 . 2 . . . . . . . . 5778 1 149 . 1 1 14 14 LYS CE C 13 41.77 0.05 . 1 . . . . . . . . 5778 1 150 . 1 1 14 14 LYS HE2 H 1 2.842 0.02 . 2 . . . . . . . . 5778 1 151 . 1 1 15 15 ARG H H 1 8.074 0.02 . 1 . . . . . . . . 5778 1 152 . 1 1 15 15 ARG N N 15 131.98 0.05 . 1 . . . . . . . . 5778 1 153 . 1 1 15 15 ARG CA C 13 55.42 0.05 . 1 . . . . . . . . 5778 1 154 . 1 1 15 15 ARG HA H 1 3.755 0.02 . 1 . . . . . . . . 5778 1 155 . 1 1 15 15 ARG C C 13 176.7 0.05 . 1 . . . . . . . . 5778 1 156 . 1 1 15 15 ARG HB2 H 1 1.11 0.02 . 2 . . . . . . . . 5778 1 157 . 1 1 15 15 ARG HB3 H 1 0.851 0.02 . 2 . . . . . . . . 5778 1 158 . 1 1 15 15 ARG HG2 H 1 -0.04 0.02 . 2 . . . . . . . . 5778 1 159 . 1 1 15 15 ARG HG3 H 1 -0.26 0.02 . 2 . . . . . . . . 5778 1 160 . 1 1 15 15 ARG CD C 13 43.15 0.05 . 1 . . . . . . . . 5778 1 161 . 1 1 15 15 ARG HD2 H 1 2.447 0.02 . 2 . . . . . . . . 5778 1 162 . 1 1 15 15 ARG HD3 H 1 2.285 0.02 . 2 . . . . . . . . 5778 1 163 . 1 1 16 16 GLY H H 1 8.537 0.02 . 1 . . . . . . . . 5778 1 164 . 1 1 16 16 GLY N N 15 115.66 0.05 . 1 . . . . . . . . 5778 1 165 . 1 1 16 16 GLY CA C 13 46.07 0.05 . 1 . . . . . . . . 5778 1 166 . 1 1 16 16 GLY HA2 H 1 4.017 0.02 . 2 . . . . . . . . 5778 1 167 . 1 1 16 16 GLY HA3 H 1 3.958 0.02 . 2 . . . . . . . . 5778 1 168 . 1 1 16 16 GLY C C 13 172.99 0.05 . 1 . . . . . . . . 5778 1 169 . 1 1 17 17 GLU H H 1 8.4 0.02 . 1 . . . . . . . . 5778 1 170 . 1 1 17 17 GLU N N 15 121.36 0.05 . 1 . . . . . . . . 5778 1 171 . 1 1 17 17 GLU CA C 13 58.2 0.05 . 1 . . . . . . . . 5778 1 172 . 1 1 17 17 GLU HA H 1 3.815 0.02 . 1 . . . . . . . . 5778 1 173 . 1 1 17 17 GLU HB2 H 1 1.679 0.02 . 2 . . . . . . . . 5778 1 174 . 1 1 17 17 GLU HB3 H 1 1.523 0.02 . 2 . . . . . . . . 5778 1 175 . 1 1 17 17 GLU HG2 H 1 2.008 0.02 . 2 . . . . . . . . 5778 1 176 . 1 1 17 17 GLU HG3 H 1 1.98 0.02 . 2 . . . . . . . . 5778 1 177 . 1 1 18 18 TYR H H 1 8.288 0.02 . 1 . . . . . . . . 5778 1 178 . 1 1 18 18 TYR N N 15 117.46 0.05 . 1 . . . . . . . . 5778 1 179 . 1 1 18 18 TYR CA C 13 58.29 0.05 . 1 . . . . . . . . 5778 1 180 . 1 1 18 18 TYR HA H 1 4.501 0.02 . 1 . . . . . . . . 5778 1 181 . 1 1 18 18 TYR CB C 13 38.83 0.05 . 1 . . . . . . . . 5778 1 182 . 1 1 18 18 TYR HB2 H 1 3.101 0.02 . 2 . . . . . . . . 5778 1 183 . 1 1 18 18 TYR HB3 H 1 2.858 0.02 . 2 . . . . . . . . 5778 1 184 . 1 1 18 18 TYR HD1 H 1 7.103 0.02 . 3 . . . . . . . . 5778 1 185 . 1 1 18 18 TYR HE1 H 1 6.78 0.02 . 3 . . . . . . . . 5778 1 186 . 1 1 19 19 ILE H H 1 7.897 0.02 . 1 . . . . . . . . 5778 1 187 . 1 1 19 19 ILE N N 15 120.72 0.05 . 1 . . . . . . . . 5778 1 188 . 1 1 19 19 ILE CA C 13 60.54 0.05 . 1 . . . . . . . . 5778 1 189 . 1 1 19 19 ILE HA H 1 4.071 0.02 . 1 . . . . . . . . 5778 1 190 . 1 1 19 19 ILE CB C 13 38.11 0.05 . 1 . . . . . . . . 5778 1 191 . 1 1 19 19 ILE HB H 1 1.832 0.02 . 1 . . . . . . . . 5778 1 192 . 1 1 19 19 ILE CG2 C 13 17.28 0.05 . 1 . . . . . . . . 5778 1 193 . 1 1 19 19 ILE HG21 H 1 0.847 0.02 . 1 . . . . . . . . 5778 1 194 . 1 1 19 19 ILE HG22 H 1 0.847 0.02 . 1 . . . . . . . . 5778 1 195 . 1 1 19 19 ILE HG23 H 1 0.847 0.02 . 1 . . . . . . . . 5778 1 196 . 1 1 19 19 ILE HG12 H 1 1.396 0.02 . 2 . . . . . . . . 5778 1 197 . 1 1 19 19 ILE HG13 H 1 1.124 0.02 . 2 . . . . . . . . 5778 1 198 . 1 1 19 19 ILE CD1 C 13 12.61 0.05 . 1 . . . . . . . . 5778 1 199 . 1 1 19 19 ILE HD11 H 1 0.804 0.02 . 1 . . . . . . . . 5778 1 200 . 1 1 19 19 ILE HD12 H 1 0.804 0.02 . 1 . . . . . . . . 5778 1 201 . 1 1 19 19 ILE HD13 H 1 0.804 0.02 . 1 . . . . . . . . 5778 1 202 . 1 1 20 20 LYS CA C 13 56.00 0.05 . 1 . . . . . . . . 5778 1 203 . 1 1 20 20 LYS HA H 1 4.014 0.02 . 1 . . . . . . . . 5778 1 204 . 1 1 20 20 LYS C C 13 175.79 0.05 . 1 . . . . . . . . 5778 1 205 . 1 1 20 20 LYS CB C 13 30.41 0.05 . 1 . . . . . . . . 5778 1 206 . 1 1 20 20 LYS HB2 H 1 1.84 0.02 . 2 . . . . . . . . 5778 1 207 . 1 1 20 20 LYS HG2 H 1 1.613 0.02 . 2 . . . . . . . . 5778 1 208 . 1 1 20 20 LYS HG3 H 1 1.412 0.02 . 2 . . . . . . . . 5778 1 209 . 1 1 20 20 LYS HD2 H 1 1.725 0.02 . 2 . . . . . . . . 5778 1 210 . 1 1 20 20 LYS HE2 H 1 3.078 0.02 . 2 . . . . . . . . 5778 1 211 . 1 1 21 21 THR H H 1 7.678 0.02 . 1 . . . . . . . . 5778 1 212 . 1 1 21 21 THR N N 15 113.77 0.05 . 1 . . . . . . . . 5778 1 213 . 1 1 21 21 THR CA C 13 59.91 0.05 . 1 . . . . . . . . 5778 1 214 . 1 1 21 21 THR HA H 1 4.146 0.02 . 1 . . . . . . . . 5778 1 215 . 1 1 21 21 THR C C 13 173.59 0.05 . 1 . . . . . . . . 5778 1 216 . 1 1 21 21 THR CB C 13 70.33 0.05 . 1 . . . . . . . . 5778 1 217 . 1 1 21 21 THR HB H 1 4.383 0.02 . 1 . . . . . . . . 5778 1 218 . 1 1 21 21 THR CG2 C 13 21.6 0.05 . 1 . . . . . . . . 5778 1 219 . 1 1 21 21 THR HG21 H 1 1.102 0.02 . 1 . . . . . . . . 5778 1 220 . 1 1 21 21 THR HG22 H 1 1.102 0.02 . 1 . . . . . . . . 5778 1 221 . 1 1 21 21 THR HG23 H 1 1.102 0.02 . 1 . . . . . . . . 5778 1 222 . 1 1 22 22 TRP H H 1 8.765 0.02 . 1 . . . . . . . . 5778 1 223 . 1 1 22 22 TRP N N 15 123.84 0.05 . 1 . . . . . . . . 5778 1 224 . 1 1 22 22 TRP CA C 13 55.88 0.05 . 1 . . . . . . . . 5778 1 225 . 1 1 22 22 TRP HA H 1 4.849 0.02 . 1 . . . . . . . . 5778 1 226 . 1 1 22 22 TRP C C 13 176.19 0.05 . 1 . . . . . . . . 5778 1 227 . 1 1 22 22 TRP CB C 13 30.61 0.05 . 1 . . . . . . . . 5778 1 228 . 1 1 22 22 TRP HB2 H 1 3.036 0.02 . 2 . . . . . . . . 5778 1 229 . 1 1 22 22 TRP HB3 H 1 2.889 0.02 . 2 . . . . . . . . 5778 1 230 . 1 1 22 22 TRP HD1 H 1 7.294 0.02 . 1 . . . . . . . . 5778 1 231 . 1 1 22 22 TRP HE1 H 1 10.36 0.02 . 1 . . . . . . . . 5778 1 232 . 1 1 22 22 TRP HZ2 H 1 7.15 0.02 . 1 . . . . . . . . 5778 1 233 . 1 1 22 22 TRP HZ3 H 1 6.862 0.02 . 1 . . . . . . . . 5778 1 234 . 1 1 23 23 ARG H H 1 8.893 0.02 . 1 . . . . . . . . 5778 1 235 . 1 1 23 23 ARG N N 15 122.2 0.05 . 1 . . . . . . . . 5778 1 236 . 1 1 23 23 ARG CA C 13 53.00 0.05 . 1 . . . . . . . . 5778 1 237 . 1 1 23 23 ARG HA H 1 5.167 0.02 . 1 . . . . . . . . 5778 1 238 . 1 1 23 23 ARG C C 13 173.65 0.05 . 1 . . . . . . . . 5778 1 239 . 1 1 23 23 ARG CB C 13 31.79 0.05 . 1 . . . . . . . . 5778 1 240 . 1 1 23 23 ARG HB2 H 1 1.852 0.02 . 2 . . . . . . . . 5778 1 241 . 1 1 23 23 ARG HB3 H 1 1.815 0.02 . 2 . . . . . . . . 5778 1 242 . 1 1 23 23 ARG CG C 13 26.85 0.05 . 1 . . . . . . . . 5778 1 243 . 1 1 23 23 ARG HG2 H 1 1.655 0.02 . 2 . . . . . . . . 5778 1 244 . 1 1 23 23 ARG CD C 13 43.02 0.05 . 1 . . . . . . . . 5778 1 245 . 1 1 23 23 ARG HD2 H 1 3.319 0.02 . 2 . . . . . . . . 5778 1 246 . 1 1 23 23 ARG HD3 H 1 3.286 0.02 . 2 . . . . . . . . 5778 1 247 . 1 1 24 24 PRO CA C 13 61.95 0.05 . 1 . . . . . . . . 5778 1 248 . 1 1 24 24 PRO HA H 1 5.046 0.02 . 1 . . . . . . . . 5778 1 249 . 1 1 24 24 PRO C C 13 177.71 0.05 . 1 . . . . . . . . 5778 1 250 . 1 1 24 24 PRO CB C 13 31.68 0.05 . 1 . . . . . . . . 5778 1 251 . 1 1 24 24 PRO HB2 H 1 2.267 0.02 . 2 . . . . . . . . 5778 1 252 . 1 1 24 24 PRO HB3 H 1 2.006 0.02 . 2 . . . . . . . . 5778 1 253 . 1 1 24 24 PRO HG2 H 1 2.037 0.02 . 2 . . . . . . . . 5778 1 254 . 1 1 24 24 PRO HD2 H 1 3.825 0.02 . 2 . . . . . . . . 5778 1 255 . 1 1 24 24 PRO HD3 H 1 3.815 0.02 . 2 . . . . . . . . 5778 1 256 . 1 1 25 25 ARG H H 1 9.708 0.02 . 1 . . . . . . . . 5778 1 257 . 1 1 25 25 ARG N N 15 126.46 0.05 . 1 . . . . . . . . 5778 1 258 . 1 1 25 25 ARG CA C 13 54.18 0.05 . 1 . . . . . . . . 5778 1 259 . 1 1 25 25 ARG HA H 1 4.839 0.02 . 1 . . . . . . . . 5778 1 260 . 1 1 25 25 ARG C C 13 172.11 0.05 . 1 . . . . . . . . 5778 1 261 . 1 1 25 25 ARG CB C 13 36.12 0.05 . 1 . . . . . . . . 5778 1 262 . 1 1 25 25 ARG HB2 H 1 2.013 0.02 . 2 . . . . . . . . 5778 1 263 . 1 1 25 25 ARG HG2 H 1 1.542 0.02 . 2 . . . . . . . . 5778 1 264 . 1 1 25 25 ARG HG3 H 1 1.513 0.02 . 2 . . . . . . . . 5778 1 265 . 1 1 25 25 ARG HD2 H 1 3.193 0.02 . 2 . . . . . . . . 5778 1 266 . 1 1 25 25 ARG HD3 H 1 3.163 0.02 . 2 . . . . . . . . 5778 1 267 . 1 1 26 26 TYR H H 1 8.746 0.02 . 1 . . . . . . . . 5778 1 268 . 1 1 26 26 TYR N N 15 126.85 0.05 . 1 . . . . . . . . 5778 1 269 . 1 1 26 26 TYR CA C 13 57.99 0.05 . 1 . . . . . . . . 5778 1 270 . 1 1 26 26 TYR HA H 1 3.891 0.02 . 1 . . . . . . . . 5778 1 271 . 1 1 26 26 TYR C C 13 174.29 0.05 . 1 . . . . . . . . 5778 1 272 . 1 1 26 26 TYR CB C 13 37.95 0.05 . 1 . . . . . . . . 5778 1 273 . 1 1 26 26 TYR HB2 H 1 3.162 0.02 . 2 . . . . . . . . 5778 1 274 . 1 1 26 26 TYR HB3 H 1 3.025 0.02 . 2 . . . . . . . . 5778 1 275 . 1 1 26 26 TYR HD1 H 1 7.446 0.02 . 3 . . . . . . . . 5778 1 276 . 1 1 26 26 TYR HE1 H 1 6.649 0.02 . 3 . . . . . . . . 5778 1 277 . 1 1 27 27 PHE H H 1 8.545 0.02 . 1 . . . . . . . . 5778 1 278 . 1 1 27 27 PHE N N 15 128.44 0.05 . 1 . . . . . . . . 5778 1 279 . 1 1 27 27 PHE CA C 13 55.76 0.05 . 1 . . . . . . . . 5778 1 280 . 1 1 27 27 PHE HA H 1 5.593 0.02 . 1 . . . . . . . . 5778 1 281 . 1 1 27 27 PHE C C 13 174.92 0.05 . 1 . . . . . . . . 5778 1 282 . 1 1 27 27 PHE CB C 13 44.07 0.05 . 1 . . . . . . . . 5778 1 283 . 1 1 27 27 PHE HB2 H 1 2.3 0.02 . 2 . . . . . . . . 5778 1 284 . 1 1 27 27 PHE HB3 H 1 2.183 0.02 . 2 . . . . . . . . 5778 1 285 . 1 1 27 27 PHE HD1 H 1 6.23 0.02 . 3 . . . . . . . . 5778 1 286 . 1 1 27 27 PHE HE1 H 1 6.636 0.02 . 3 . . . . . . . . 5778 1 287 . 1 1 28 28 LEU H H 1 9.254 0.02 . 1 . . . . . . . . 5778 1 288 . 1 1 28 28 LEU N N 15 117.43 0.05 . 1 . . . . . . . . 5778 1 289 . 1 1 28 28 LEU CA C 13 55.06 0.05 . 1 . . . . . . . . 5778 1 290 . 1 1 28 28 LEU HA H 1 4.925 0.02 . 1 . . . . . . . . 5778 1 291 . 1 1 28 28 LEU C C 13 174.43 0.05 . 1 . . . . . . . . 5778 1 292 . 1 1 28 28 LEU CB C 13 45.07 0.05 . 1 . . . . . . . . 5778 1 293 . 1 1 28 28 LEU HB2 H 1 1.733 0.02 . 2 . . . . . . . . 5778 1 294 . 1 1 28 28 LEU HG H 1 1.45 0.02 . 1 . . . . . . . . 5778 1 295 . 1 1 28 28 LEU CD1 C 13 26.89 0.05 . 2 . . . . . . . . 5778 1 296 . 1 1 28 28 LEU HD11 H 1 0.963 0.02 . 2 . . . . . . . . 5778 1 297 . 1 1 28 28 LEU HD12 H 1 0.963 0.02 . 2 . . . . . . . . 5778 1 298 . 1 1 28 28 LEU HD13 H 1 0.963 0.02 . 2 . . . . . . . . 5778 1 299 . 1 1 28 28 LEU HD21 H 1 1.083 0.02 . 2 . . . . . . . . 5778 1 300 . 1 1 28 28 LEU HD22 H 1 1.083 0.02 . 2 . . . . . . . . 5778 1 301 . 1 1 28 28 LEU HD23 H 1 1.083 0.02 . 2 . . . . . . . . 5778 1 302 . 1 1 29 29 LEU H H 1 9.225 0.02 . 1 . . . . . . . . 5778 1 303 . 1 1 29 29 LEU N N 15 123.85 0.05 . 1 . . . . . . . . 5778 1 304 . 1 1 29 29 LEU CA C 13 53.00 0.05 . 1 . . . . . . . . 5778 1 305 . 1 1 29 29 LEU HA H 1 5.49 0.02 . 1 . . . . . . . . 5778 1 306 . 1 1 29 29 LEU C C 13 175.62 0.05 . 1 . . . . . . . . 5778 1 307 . 1 1 29 29 LEU CB C 13 44.45 0.05 . 1 . . . . . . . . 5778 1 308 . 1 1 29 29 LEU HB2 H 1 1.459 0.02 . 2 . . . . . . . . 5778 1 309 . 1 1 29 29 LEU HG H 1 1.531 0.02 . 1 . . . . . . . . 5778 1 310 . 1 1 29 29 LEU HD11 H 1 0.796 0.02 . 2 . . . . . . . . 5778 1 311 . 1 1 29 29 LEU HD12 H 1 0.796 0.02 . 2 . . . . . . . . 5778 1 312 . 1 1 29 29 LEU HD13 H 1 0.796 0.02 . 2 . . . . . . . . 5778 1 313 . 1 1 29 29 LEU HD21 H 1 0.669 0.02 . 2 . . . . . . . . 5778 1 314 . 1 1 29 29 LEU HD22 H 1 0.669 0.02 . 2 . . . . . . . . 5778 1 315 . 1 1 29 29 LEU HD23 H 1 0.669 0.02 . 2 . . . . . . . . 5778 1 316 . 1 1 30 30 LYS H H 1 9.41 0.02 . 1 . . . . . . . . 5778 1 317 . 1 1 30 30 LYS N N 15 126.00 0.05 . 1 . . . . . . . . 5778 1 318 . 1 1 30 30 LYS CA C 13 54.72 0.05 . 1 . . . . . . . . 5778 1 319 . 1 1 30 30 LYS HA H 1 5.398 0.02 . 1 . . . . . . . . 5778 1 320 . 1 1 30 30 LYS C C 13 177.98 0.05 . 1 . . . . . . . . 5778 1 321 . 1 1 30 30 LYS CB C 13 35.47 0.05 . 1 . . . . . . . . 5778 1 322 . 1 1 30 30 LYS HB2 H 1 2.222 0.02 . 2 . . . . . . . . 5778 1 323 . 1 1 30 30 LYS HB3 H 1 1.807 0.02 . 2 . . . . . . . . 5778 1 324 . 1 1 30 30 LYS HG2 H 1 1.593 0.02 . 2 . . . . . . . . 5778 1 325 . 1 1 30 30 LYS HG3 H 1 1.498 0.02 . 2 . . . . . . . . 5778 1 326 . 1 1 30 30 LYS HE2 H 1 2.815 0.02 . 2 . . . . . . . . 5778 1 327 . 1 1 31 31 SER H H 1 9.194 0.02 . 1 . . . . . . . . 5778 1 328 . 1 1 31 31 SER N N 15 114.39 0.05 . 1 . . . . . . . . 5778 1 329 . 1 1 31 31 SER CA C 13 60.9 0.05 . 1 . . . . . . . . 5778 1 330 . 1 1 31 31 SER HA H 1 4.171 0.02 . 1 . . . . . . . . 5778 1 331 . 1 1 31 31 SER C C 13 173.57 0.05 . 1 . . . . . . . . 5778 1 332 . 1 1 31 31 SER CB C 13 62.65 0.05 . 1 . . . . . . . . 5778 1 333 . 1 1 31 31 SER HB2 H 1 3.844 0.02 . 2 . . . . . . . . 5778 1 334 . 1 1 31 31 SER HB3 H 1 3.877 0.02 . 2 . . . . . . . . 5778 1 335 . 1 1 32 32 ASP H H 1 7.6 0.02 . 1 . . . . . . . . 5778 1 336 . 1 1 32 32 ASP N N 15 118.31 0.05 . 1 . . . . . . . . 5778 1 337 . 1 1 32 32 ASP CA C 13 52.93 0.05 . 1 . . . . . . . . 5778 1 338 . 1 1 32 32 ASP HA H 1 4.617 0.02 . 1 . . . . . . . . 5778 1 339 . 1 1 32 32 ASP C C 13 176.91 0.05 . 1 . . . . . . . . 5778 1 340 . 1 1 32 32 ASP CB C 13 40.29 0.05 . 1 . . . . . . . . 5778 1 341 . 1 1 32 32 ASP HB2 H 1 3.101 0.02 . 1 . . . . . . . . 5778 1 342 . 1 1 32 32 ASP HB3 H 1 2.563 0.02 . 1 . . . . . . . . 5778 1 343 . 1 1 33 33 GLY H H 1 8.349 0.02 . 1 . . . . . . . . 5778 1 344 . 1 1 33 33 GLY N N 15 108.37 0.05 . 1 . . . . . . . . 5778 1 345 . 1 1 33 33 GLY CA C 13 44.95 0.05 . 1 . . . . . . . . 5778 1 346 . 1 1 33 33 GLY HA2 H 1 3.33 0.02 . 1 . . . . . . . . 5778 1 347 . 1 1 33 33 GLY HA3 H 1 4.143 0.02 . 1 . . . . . . . . 5778 1 348 . 1 1 33 33 GLY C C 13 172.3 0.05 . 1 . . . . . . . . 5778 1 349 . 1 1 34 34 SER H H 1 8.127 0.02 . 1 . . . . . . . . 5778 1 350 . 1 1 34 34 SER N N 15 116.94 0.05 . 1 . . . . . . . . 5778 1 351 . 1 1 34 34 SER CA C 13 59.91 0.05 . 1 . . . . . . . . 5778 1 352 . 1 1 34 34 SER HA H 1 4.377 0.02 . 1 . . . . . . . . 5778 1 353 . 1 1 34 34 SER C C 13 171.38 0.05 . 1 . . . . . . . . 5778 1 354 . 1 1 34 34 SER CB C 13 63.23 0.05 . 1 . . . . . . . . 5778 1 355 . 1 1 34 34 SER HB2 H 1 3.877 0.02 . 2 . . . . . . . . 5778 1 356 . 1 1 34 34 SER HB3 H 1 3.84 0.02 . 2 . . . . . . . . 5778 1 357 . 1 1 35 35 PHE H H 1 8.789 0.02 . 1 . . . . . . . . 5778 1 358 . 1 1 35 35 PHE N N 15 129.55 0.05 . 1 . . . . . . . . 5778 1 359 . 1 1 35 35 PHE CA C 13 54.71 0.05 . 1 . . . . . . . . 5778 1 360 . 1 1 35 35 PHE HA H 1 5.737 0.02 . 1 . . . . . . . . 5778 1 361 . 1 1 35 35 PHE C C 13 173.64 0.05 . 1 . . . . . . . . 5778 1 362 . 1 1 35 35 PHE CB C 13 40.17 0.05 . 1 . . . . . . . . 5778 1 363 . 1 1 35 35 PHE HB2 H 1 2.602 0.02 . 2 . . . . . . . . 5778 1 364 . 1 1 35 35 PHE HB3 H 1 2.488 0.02 . 2 . . . . . . . . 5778 1 365 . 1 1 35 35 PHE HD1 H 1 6.977 0.02 . 3 . . . . . . . . 5778 1 366 . 1 1 35 35 PHE HE1 H 1 6.46 0.02 . 3 . . . . . . . . 5778 1 367 . 1 1 35 35 PHE HZ H 1 5.6 0.02 . 1 . . . . . . . . 5778 1 368 . 1 1 36 36 ILE H H 1 8.615 0.02 . 1 . . . . . . . . 5778 1 369 . 1 1 36 36 ILE N N 15 122.2 0.05 . 1 . . . . . . . . 5778 1 370 . 1 1 36 36 ILE CA C 13 59.05 0.05 . 1 . . . . . . . . 5778 1 371 . 1 1 36 36 ILE HA H 1 4.649 0.02 . 1 . . . . . . . . 5778 1 372 . 1 1 36 36 ILE C C 13 173.38 0.05 . 1 . . . . . . . . 5778 1 373 . 1 1 36 36 ILE CB C 13 40.78 0.05 . 1 . . . . . . . . 5778 1 374 . 1 1 36 36 ILE HB H 1 1.62 0.02 . 1 . . . . . . . . 5778 1 375 . 1 1 36 36 ILE HG21 H 1 0.74 0.02 . 1 . . . . . . . . 5778 1 376 . 1 1 36 36 ILE HG22 H 1 0.74 0.02 . 1 . . . . . . . . 5778 1 377 . 1 1 36 36 ILE HG23 H 1 0.74 0.02 . 1 . . . . . . . . 5778 1 378 . 1 1 36 36 ILE CG1 C 13 13.85 0.05 . 1 . . . . . . . . 5778 1 379 . 1 1 36 36 ILE HG12 H 1 0.91 0.02 . 2 . . . . . . . . 5778 1 380 . 1 1 36 36 ILE CD1 C 13 17.94 0.05 . 1 . . . . . . . . 5778 1 381 . 1 1 36 36 ILE HD11 H 1 0.762 0.02 . 1 . . . . . . . . 5778 1 382 . 1 1 36 36 ILE HD12 H 1 0.762 0.02 . 1 . . . . . . . . 5778 1 383 . 1 1 36 36 ILE HD13 H 1 0.762 0.02 . 1 . . . . . . . . 5778 1 384 . 1 1 37 37 GLY H H 1 8.267 0.02 . 1 . . . . . . . . 5778 1 385 . 1 1 37 37 GLY N N 15 111.53 0.05 . 1 . . . . . . . . 5778 1 386 . 1 1 37 37 GLY CA C 13 42.43 0.05 . 1 . . . . . . . . 5778 1 387 . 1 1 37 37 GLY HA2 H 1 3.994 0.02 . 2 . . . . . . . . 5778 1 388 . 1 1 37 37 GLY HA3 H 1 3.958 0.02 . 2 . . . . . . . . 5778 1 389 . 1 1 37 37 GLY C C 13 171.98 0.05 . 1 . . . . . . . . 5778 1 390 . 1 1 38 38 TYR H H 1 8.834 0.02 . 1 . . . . . . . . 5778 1 391 . 1 1 38 38 TYR N N 15 120.69 0.05 . 1 . . . . . . . . 5778 1 392 . 1 1 38 38 TYR CA C 13 56.58 0.05 . 1 . . . . . . . . 5778 1 393 . 1 1 38 38 TYR HA H 1 4.6 0.02 . 1 . . . . . . . . 5778 1 394 . 1 1 38 38 TYR C C 13 175.43 0.05 . 1 . . . . . . . . 5778 1 395 . 1 1 38 38 TYR CB C 13 43.49 0.05 . 1 . . . . . . . . 5778 1 396 . 1 1 38 38 TYR HB2 H 1 3.323 0.02 . 2 . . . . . . . . 5778 1 397 . 1 1 38 38 TYR HB3 H 1 2.714 0.02 . 2 . . . . . . . . 5778 1 398 . 1 1 38 38 TYR HD1 H 1 7.018 0.02 . 3 . . . . . . . . 5778 1 399 . 1 1 38 38 TYR HE1 H 1 6.616 0.02 . 3 . . . . . . . . 5778 1 400 . 1 1 39 39 LYS H H 1 9.086 0.02 . 1 . . . . . . . . 5778 1 401 . 1 1 39 39 LYS N N 15 120.9 0.05 . 1 . . . . . . . . 5778 1 402 . 1 1 39 39 LYS CA C 13 58.99 0.05 . 1 . . . . . . . . 5778 1 403 . 1 1 39 39 LYS HA H 1 4.172 0.02 . 1 . . . . . . . . 5778 1 404 . 1 1 39 39 LYS C C 13 174.98 0.05 . 1 . . . . . . . . 5778 1 405 . 1 1 39 39 LYS CB C 13 33.32 0.05 . 1 . . . . . . . . 5778 1 406 . 1 1 39 39 LYS HB2 H 1 1.922 0.02 . 2 . . . . . . . . 5778 1 407 . 1 1 39 39 LYS HG2 H 1 1.666 0.02 . 2 . . . . . . . . 5778 1 408 . 1 1 39 39 LYS HG3 H 1 1.555 0.02 . 2 . . . . . . . . 5778 1 409 . 1 1 39 39 LYS HD2 H 1 1.766 0.02 . 2 . . . . . . . . 5778 1 410 . 1 1 39 39 LYS CE C 13 41.74 0.05 . 1 . . . . . . . . 5778 1 411 . 1 1 39 39 LYS HE2 H 1 3.039 0.02 . 2 . . . . . . . . 5778 1 412 . 1 1 40 40 GLU H H 1 7.467 0.02 . 1 . . . . . . . . 5778 1 413 . 1 1 40 40 GLU N N 15 112.04 0.05 . 1 . . . . . . . . 5778 1 414 . 1 1 40 40 GLU CA C 13 53.14 0.05 . 1 . . . . . . . . 5778 1 415 . 1 1 40 40 GLU HA H 1 4.757 0.02 . 1 . . . . . . . . 5778 1 416 . 1 1 40 40 GLU C C 13 173.96 0.05 . 1 . . . . . . . . 5778 1 417 . 1 1 40 40 GLU CB C 13 32.24 0.05 . 1 . . . . . . . . 5778 1 418 . 1 1 40 40 GLU HB2 H 1 2.073 0.02 . 2 . . . . . . . . 5778 1 419 . 1 1 40 40 GLU HB3 H 1 1.758 0.02 . 2 . . . . . . . . 5778 1 420 . 1 1 40 40 GLU HG2 H 1 2.16 0.02 . 2 . . . . . . . . 5778 1 421 . 1 1 40 40 GLU HG3 H 1 2.141 0.02 . 2 . . . . . . . . 5778 1 422 . 1 1 41 41 ARG H H 1 8.228 0.02 . 1 . . . . . . . . 5778 1 423 . 1 1 41 41 ARG N N 15 122.84 0.05 . 1 . . . . . . . . 5778 1 424 . 1 1 41 41 ARG CA C 13 54.29 0.05 . 1 . . . . . . . . 5778 1 425 . 1 1 41 41 ARG HA H 1 3.033 0.02 . 1 . . . . . . . . 5778 1 426 . 1 1 41 41 ARG CB C 13 30.49 0.05 . 1 . . . . . . . . 5778 1 427 . 1 1 41 41 ARG HB2 H 1 0.881 0.02 . 2 . . . . . . . . 5778 1 428 . 1 1 41 41 ARG HB3 H 1 0.112 0.02 . 2 . . . . . . . . 5778 1 429 . 1 1 41 41 ARG HG2 H 1 1.347 0.02 . 2 . . . . . . . . 5778 1 430 . 1 1 41 41 ARG HG3 H 1 0.628 0.02 . 2 . . . . . . . . 5778 1 431 . 1 1 41 41 ARG CD C 13 43.46 0.05 . 1 . . . . . . . . 5778 1 432 . 1 1 41 41 ARG HD2 H 1 2.774 0.02 . 2 . . . . . . . . 5778 1 433 . 1 1 41 41 ARG HD3 H 1 2.752 0.02 . 2 . . . . . . . . 5778 1 434 . 1 1 42 42 PRO CA C 13 62.46 0.05 . 1 . . . . . . . . 5778 1 435 . 1 1 42 42 PRO HA H 1 4.061 0.02 . 1 . . . . . . . . 5778 1 436 . 1 1 42 42 PRO C C 13 176.3 0.05 . 1 . . . . . . . . 5778 1 437 . 1 1 42 42 PRO CB C 13 31.27 0.05 . 1 . . . . . . . . 5778 1 438 . 1 1 42 42 PRO HB2 H 1 1.463 0.02 . 2 . . . . . . . . 5778 1 439 . 1 1 42 42 PRO HG2 H 1 1.579 0.02 . 2 . . . . . . . . 5778 1 440 . 1 1 42 42 PRO HD2 H 1 3.641 0.02 . 2 . . . . . . . . 5778 1 441 . 1 1 42 42 PRO HD3 H 1 3.55 0.02 . 2 . . . . . . . . 5778 1 442 . 1 1 43 43 GLU H H 1 8.466 0.02 . 1 . . . . . . . . 5778 1 443 . 1 1 43 43 GLU N N 15 123.46 0.05 . 1 . . . . . . . . 5778 1 444 . 1 1 43 43 GLU CA C 13 56.63 0.05 . 1 . . . . . . . . 5778 1 445 . 1 1 43 43 GLU HA H 1 4.06 0.02 . 1 . . . . . . . . 5778 1 446 . 1 1 43 43 GLU C C 13 175.5 0.05 . 1 . . . . . . . . 5778 1 447 . 1 1 43 43 GLU CB C 13 30.28 0.05 . 1 . . . . . . . . 5778 1 448 . 1 1 43 43 GLU HB2 H 1 1.967 0.02 . 2 . . . . . . . . 5778 1 449 . 1 1 43 43 GLU HB3 H 1 1.791 0.02 . 2 . . . . . . . . 5778 1 450 . 1 1 43 43 GLU HG2 H 1 2.175 0.02 . 2 . . . . . . . . 5778 1 451 . 1 1 43 43 GLU HG3 H 1 2.09 0.02 . 2 . . . . . . . . 5778 1 452 . 1 1 44 44 ALA H H 1 7.781 0.02 . 1 . . . . . . . . 5778 1 453 . 1 1 44 44 ALA N N 15 121.77 0.05 . 1 . . . . . . . . 5778 1 454 . 1 1 44 44 ALA CA C 13 50.28 0.05 . 1 . . . . . . . . 5778 1 455 . 1 1 44 44 ALA HA H 1 4.577 0.02 . 1 . . . . . . . . 5778 1 456 . 1 1 44 44 ALA CB C 13 19.13 0.05 . 1 . . . . . . . . 5778 1 457 . 1 1 44 44 ALA HB1 H 1 1.311 0.02 . 1 . . . . . . . . 5778 1 458 . 1 1 44 44 ALA HB2 H 1 1.311 0.02 . 1 . . . . . . . . 5778 1 459 . 1 1 44 44 ALA HB3 H 1 1.311 0.02 . 1 . . . . . . . . 5778 1 460 . 1 1 45 45 PRO CA C 13 64.1 0.05 . 1 . . . . . . . . 5778 1 461 . 1 1 45 45 PRO HA H 1 4.248 0.02 . 1 . . . . . . . . 5778 1 462 . 1 1 45 45 PRO C C 13 176.62 0.05 . 1 . . . . . . . . 5778 1 463 . 1 1 45 45 PRO CB C 13 31.27 0.05 . 1 . . . . . . . . 5778 1 464 . 1 1 45 45 PRO HB2 H 1 2.209 0.02 . 2 . . . . . . . . 5778 1 465 . 1 1 45 45 PRO HG2 H 1 1.965 0.02 . 2 . . . . . . . . 5778 1 466 . 1 1 45 45 PRO HG3 H 1 1.893 0.02 . 2 . . . . . . . . 5778 1 467 . 1 1 45 45 PRO CD C 13 50.28 0.05 . 1 . . . . . . . . 5778 1 468 . 1 1 45 45 PRO HD2 H 1 3.66 0.02 . 2 . . . . . . . . 5778 1 469 . 1 1 45 45 PRO HD3 H 1 3.627 0.02 . 2 . . . . . . . . 5778 1 470 . 1 1 46 46 ASP H H 1 8.162 0.02 . 1 . . . . . . . . 5778 1 471 . 1 1 46 46 ASP N N 15 116.15 0.05 . 1 . . . . . . . . 5778 1 472 . 1 1 46 46 ASP CA C 13 53.47 0.05 . 1 . . . . . . . . 5778 1 473 . 1 1 46 46 ASP HA H 1 4.519 0.02 . 1 . . . . . . . . 5778 1 474 . 1 1 46 46 ASP C C 13 175.75 0.05 . 1 . . . . . . . . 5778 1 475 . 1 1 46 46 ASP CB C 13 40.09 0.05 . 1 . . . . . . . . 5778 1 476 . 1 1 46 46 ASP HB2 H 1 2.692 0.02 . 2 . . . . . . . . 5778 1 477 . 1 1 46 46 ASP HB3 H 1 2.595 0.02 . 2 . . . . . . . . 5778 1 478 . 1 1 47 47 GLN H H 1 7.791 0.02 . 1 . . . . . . . . 5778 1 479 . 1 1 47 47 GLN N N 15 119.47 0.05 . 1 . . . . . . . . 5778 1 480 . 1 1 47 47 GLN CA C 13 55.48 0.05 . 1 . . . . . . . . 5778 1 481 . 1 1 47 47 GLN HA H 1 4.345 0.02 . 1 . . . . . . . . 5778 1 482 . 1 1 47 47 GLN C C 13 175.62 0.05 . 1 . . . . . . . . 5778 1 483 . 1 1 47 47 GLN CB C 13 29.00 0.05 . 1 . . . . . . . . 5778 1 484 . 1 1 47 47 GLN HB2 H 1 2.117 0.02 . 2 . . . . . . . . 5778 1 485 . 1 1 47 47 GLN HB3 H 1 1.933 0.02 . 2 . . . . . . . . 5778 1 486 . 1 1 47 47 GLN CG C 13 33.38 0.05 . 1 . . . . . . . . 5778 1 487 . 1 1 47 47 GLN HG2 H 1 2.271 0.02 . 2 . . . . . . . . 5778 1 488 . 1 1 47 47 GLN HG3 H 1 2.252 0.02 . 2 . . . . . . . . 5778 1 489 . 1 1 47 47 GLN HE21 H 1 7.408 0.02 . 2 . . . . . . . . 5778 1 490 . 1 1 47 47 GLN HE22 H 1 6.882 0.02 . 2 . . . . . . . . 5778 1 491 . 1 1 48 48 THR H H 1 8.221 0.02 . 1 . . . . . . . . 5778 1 492 . 1 1 48 48 THR N N 15 115.21 0.05 . 1 . . . . . . . . 5778 1 493 . 1 1 48 48 THR CA C 13 61.82 0.05 . 1 . . . . . . . . 5778 1 494 . 1 1 48 48 THR HA H 1 4.244 0.02 . 1 . . . . . . . . 5778 1 495 . 1 1 48 48 THR C C 13 174.31 0.05 . 1 . . . . . . . . 5778 1 496 . 1 1 48 48 THR CB C 13 69.29 0.05 . 1 . . . . . . . . 5778 1 497 . 1 1 48 48 THR HB H 1 4.154 0.02 . 1 . . . . . . . . 5778 1 498 . 1 1 48 48 THR CG2 C 13 21.32 0.05 . 1 . . . . . . . . 5778 1 499 . 1 1 48 48 THR HG21 H 1 1.117 0.02 . 1 . . . . . . . . 5778 1 500 . 1 1 48 48 THR HG22 H 1 1.117 0.02 . 1 . . . . . . . . 5778 1 501 . 1 1 48 48 THR HG23 H 1 1.117 0.02 . 1 . . . . . . . . 5778 1 502 . 1 1 49 49 LEU H H 1 7.985 0.02 . 1 . . . . . . . . 5778 1 503 . 1 1 49 49 LEU N N 15 126.72 0.05 . 1 . . . . . . . . 5778 1 504 . 1 1 49 49 LEU CA C 13 52.81 0.05 . 1 . . . . . . . . 5778 1 505 . 1 1 49 49 LEU HA H 1 4.63 0.02 . 1 . . . . . . . . 5778 1 506 . 1 1 49 49 LEU C C 13 174.17 0.05 . 1 . . . . . . . . 5778 1 507 . 1 1 49 49 LEU CB C 13 41.68 0.05 . 1 . . . . . . . . 5778 1 508 . 1 1 49 49 LEU HB2 H 1 1.565 0.02 . 2 . . . . . . . . 5778 1 509 . 1 1 49 49 LEU HG H 1 1.635 0.02 . 1 . . . . . . . . 5778 1 510 . 1 1 49 49 LEU CD1 C 13 23.53 0.05 . 2 . . . . . . . . 5778 1 511 . 1 1 49 49 LEU HD11 H 1 0.867 0.02 . 2 . . . . . . . . 5778 1 512 . 1 1 49 49 LEU HD12 H 1 0.867 0.02 . 2 . . . . . . . . 5778 1 513 . 1 1 49 49 LEU HD13 H 1 0.867 0.02 . 2 . . . . . . . . 5778 1 514 . 1 1 49 49 LEU HD21 H 1 0.842 0.02 . 2 . . . . . . . . 5778 1 515 . 1 1 49 49 LEU HD22 H 1 0.842 0.02 . 2 . . . . . . . . 5778 1 516 . 1 1 49 49 LEU HD23 H 1 0.842 0.02 . 2 . . . . . . . . 5778 1 517 . 1 1 50 50 PRO CA C 13 60.95 0.05 . 1 . . . . . . . . 5778 1 518 . 1 1 50 50 PRO HA H 1 4.745 0.02 . 1 . . . . . . . . 5778 1 519 . 1 1 50 50 PRO HB2 H 1 2.304 0.02 . 2 . . . . . . . . 5778 1 520 . 1 1 50 50 PRO HB3 H 1 1.826 0.02 . 2 . . . . . . . . 5778 1 521 . 1 1 50 50 PRO CG C 13 28.93 0.05 . 1 . . . . . . . . 5778 1 522 . 1 1 50 50 PRO HG2 H 1 2.093 0.02 . 2 . . . . . . . . 5778 1 523 . 1 1 50 50 PRO HG3 H 1 1.975 0.02 . 2 . . . . . . . . 5778 1 524 . 1 1 50 50 PRO HD2 H 1 3.881 0.02 . 2 . . . . . . . . 5778 1 525 . 1 1 50 50 PRO HD3 H 1 3.658 0.02 . 2 . . . . . . . . 5778 1 526 . 1 1 51 51 PRO CA C 13 62.28 0.05 . 1 . . . . . . . . 5778 1 527 . 1 1 51 51 PRO HA H 1 3.888 0.02 . 1 . . . . . . . . 5778 1 528 . 1 1 51 51 PRO C C 13 176.68 0.05 . 1 . . . . . . . . 5778 1 529 . 1 1 51 51 PRO CB C 13 31.58 0.05 . 1 . . . . . . . . 5778 1 530 . 1 1 51 51 PRO HB2 H 1 2.149 0.02 . 2 . . . . . . . . 5778 1 531 . 1 1 51 51 PRO HB3 H 1 1.792 0.02 . 2 . . . . . . . . 5778 1 532 . 1 1 51 51 PRO HG2 H 1 2.061 0.02 . 2 . . . . . . . . 5778 1 533 . 1 1 51 51 PRO HG3 H 1 2.032 0.02 . 2 . . . . . . . . 5778 1 534 . 1 1 51 51 PRO HD2 H 1 3.84 0.02 . 2 . . . . . . . . 5778 1 535 . 1 1 51 51 PRO HD3 H 1 3.604 0.02 . 2 . . . . . . . . 5778 1 536 . 1 1 52 52 LEU H H 1 8.152 0.02 . 1 . . . . . . . . 5778 1 537 . 1 1 52 52 LEU N N 15 121.85 0.05 . 1 . . . . . . . . 5778 1 538 . 1 1 52 52 LEU CA C 13 55.59 0.05 . 1 . . . . . . . . 5778 1 539 . 1 1 52 52 LEU HA H 1 4.207 0.02 . 1 . . . . . . . . 5778 1 540 . 1 1 52 52 LEU C C 13 177.01 0.05 . 1 . . . . . . . . 5778 1 541 . 1 1 52 52 LEU CB C 13 42.76 0.05 . 1 . . . . . . . . 5778 1 542 . 1 1 52 52 LEU HB2 H 1 1.639 0.02 . 2 . . . . . . . . 5778 1 543 . 1 1 52 52 LEU HB3 H 1 1.58 0.02 . 2 . . . . . . . . 5778 1 544 . 1 1 52 52 LEU HG H 1 1.352 0.02 . 1 . . . . . . . . 5778 1 545 . 1 1 52 52 LEU HD11 H 1 0.831 0.02 . 2 . . . . . . . . 5778 1 546 . 1 1 52 52 LEU HD12 H 1 0.831 0.02 . 2 . . . . . . . . 5778 1 547 . 1 1 52 52 LEU HD13 H 1 0.831 0.02 . 2 . . . . . . . . 5778 1 548 . 1 1 52 52 LEU HD21 H 1 0.801 0.02 . 2 . . . . . . . . 5778 1 549 . 1 1 52 52 LEU HD22 H 1 0.801 0.02 . 2 . . . . . . . . 5778 1 550 . 1 1 52 52 LEU HD23 H 1 0.801 0.02 . 2 . . . . . . . . 5778 1 551 . 1 1 53 53 ASN H H 1 7.605 0.02 . 1 . . . . . . . . 5778 1 552 . 1 1 53 53 ASN N N 15 114.51 0.05 . 1 . . . . . . . . 5778 1 553 . 1 1 53 53 ASN CA C 13 52.04 0.05 . 1 . . . . . . . . 5778 1 554 . 1 1 53 53 ASN HA H 1 4.904 0.02 . 1 . . . . . . . . 5778 1 555 . 1 1 53 53 ASN C C 13 173.23 0.05 . 1 . . . . . . . . 5778 1 556 . 1 1 53 53 ASN CB C 13 43.23 0.05 . 1 . . . . . . . . 5778 1 557 . 1 1 53 53 ASN HB2 H 1 2.592 0.02 . 2 . . . . . . . . 5778 1 558 . 1 1 53 53 ASN HB3 H 1 2.56 0.02 . 2 . . . . . . . . 5778 1 559 . 1 1 53 53 ASN HD21 H 1 7.71 0.02 . 2 . . . . . . . . 5778 1 560 . 1 1 53 53 ASN HD22 H 1 6.89 0.02 . 2 . . . . . . . . 5778 1 561 . 1 1 54 54 ASN H H 1 8.794 0.02 . 1 . . . . . . . . 5778 1 562 . 1 1 54 54 ASN N N 15 121.07 0.05 . 1 . . . . . . . . 5778 1 563 . 1 1 54 54 ASN CA C 13 52.77 0.05 . 1 . . . . . . . . 5778 1 564 . 1 1 54 54 ASN HA H 1 4.963 0.02 . 1 . . . . . . . . 5778 1 565 . 1 1 54 54 ASN C C 13 172.84 0.05 . 1 . . . . . . . . 5778 1 566 . 1 1 54 54 ASN CB C 13 39.04 0.05 . 1 . . . . . . . . 5778 1 567 . 1 1 54 54 ASN HB2 H 1 2.717 0.02 . 2 . . . . . . . . 5778 1 568 . 1 1 54 54 ASN HB3 H 1 2.465 0.02 . 2 . . . . . . . . 5778 1 569 . 1 1 54 54 ASN HD21 H 1 7.263 0.02 . 2 . . . . . . . . 5778 1 570 . 1 1 54 54 ASN HD22 H 1 6.591 0.02 . 2 . . . . . . . . 5778 1 571 . 1 1 55 55 PHE H H 1 8.288 0.02 . 1 . . . . . . . . 5778 1 572 . 1 1 55 55 PHE N N 15 122.31 0.05 . 1 . . . . . . . . 5778 1 573 . 1 1 55 55 PHE CA C 13 54.96 0.05 . 1 . . . . . . . . 5778 1 574 . 1 1 55 55 PHE HA H 1 5.154 0.02 . 1 . . . . . . . . 5778 1 575 . 1 1 55 55 PHE CB C 13 40.61 0.05 . 1 . . . . . . . . 5778 1 576 . 1 1 55 55 PHE HB2 H 1 3.329 0.02 . 2 . . . . . . . . 5778 1 577 . 1 1 55 55 PHE HB3 H 1 3.261 0.02 . 2 . . . . . . . . 5778 1 578 . 1 1 55 55 PHE HD1 H 1 7.2 0.02 . 3 . . . . . . . . 5778 1 579 . 1 1 55 55 PHE HE1 H 1 7.073 0.02 . 3 . . . . . . . . 5778 1 580 . 1 1 56 56 SER H H 1 8.713 0.02 . 1 . . . . . . . . 5778 1 581 . 1 1 56 56 SER N N 15 113.61 0.05 . 1 . . . . . . . . 5778 1 582 . 1 1 56 56 SER CA C 13 55.48 0.05 . 1 . . . . . . . . 5778 1 583 . 1 1 56 56 SER HA H 1 5.332 0.02 . 1 . . . . . . . . 5778 1 584 . 1 1 56 56 SER C C 13 177.02 0.05 . 1 . . . . . . . . 5778 1 585 . 1 1 56 56 SER CB C 13 64.11 0.05 . 1 . . . . . . . . 5778 1 586 . 1 1 56 56 SER HB2 H 1 3.848 0.02 . 2 . . . . . . . . 5778 1 587 . 1 1 56 56 SER HB3 H 1 3.747 0.02 . 2 . . . . . . . . 5778 1 588 . 1 1 57 57 VAL H H 1 8.943 0.02 . 1 . . . . . . . . 5778 1 589 . 1 1 57 57 VAL N N 15 118.58 0.05 . 1 . . . . . . . . 5778 1 590 . 1 1 57 57 VAL CA C 13 60.58 0.05 . 1 . . . . . . . . 5778 1 591 . 1 1 57 57 VAL HA H 1 5.323 0.02 . 1 . . . . . . . . 5778 1 592 . 1 1 57 57 VAL C C 13 174.66 0.05 . 1 . . . . . . . . 5778 1 593 . 1 1 57 57 VAL HB H 1 2.594 0.02 . 1 . . . . . . . . 5778 1 594 . 1 1 57 57 VAL HG11 H 1 0.783 0.02 . 1 . . . . . . . . 5778 1 595 . 1 1 57 57 VAL HG12 H 1 0.783 0.02 . 1 . . . . . . . . 5778 1 596 . 1 1 57 57 VAL HG13 H 1 0.783 0.02 . 1 . . . . . . . . 5778 1 597 . 1 1 57 57 VAL HG21 H 1 0.709 0.02 . 1 . . . . . . . . 5778 1 598 . 1 1 57 57 VAL HG22 H 1 0.709 0.02 . 1 . . . . . . . . 5778 1 599 . 1 1 57 57 VAL HG23 H 1 0.709 0.02 . 1 . . . . . . . . 5778 1 600 . 1 1 58 58 ALA H H 1 8.155 0.02 . 1 . . . . . . . . 5778 1 601 . 1 1 58 58 ALA N N 15 124.11 0.05 . 1 . . . . . . . . 5778 1 602 . 1 1 58 58 ALA CA C 13 53.98 0.05 . 1 . . . . . . . . 5778 1 603 . 1 1 58 58 ALA HA H 1 3.975 0.02 . 1 . . . . . . . . 5778 1 604 . 1 1 58 58 ALA C C 13 177.97 0.05 . 1 . . . . . . . . 5778 1 605 . 1 1 58 58 ALA CB C 13 18.16 0.05 . 1 . . . . . . . . 5778 1 606 . 1 1 58 58 ALA HB1 H 1 1.334 0.02 . 1 . . . . . . . . 5778 1 607 . 1 1 58 58 ALA HB2 H 1 1.334 0.02 . 1 . . . . . . . . 5778 1 608 . 1 1 58 58 ALA HB3 H 1 1.334 0.02 . 1 . . . . . . . . 5778 1 609 . 1 1 61 61 GLN CA C 13 54.44 0.05 . 1 . . . . . . . . 5778 1 610 . 1 1 61 61 GLN HA H 1 4.659 0.02 . 1 . . . . . . . . 5778 1 611 . 1 1 61 61 GLN C C 13 174.44 0.05 . 1 . . . . . . . . 5778 1 612 . 1 1 61 61 GLN CB C 13 31.56 0.05 . 1 . . . . . . . . 5778 1 613 . 1 1 61 61 GLN HB2 H 1 2.047 0.02 . 2 . . . . . . . . 5778 1 614 . 1 1 61 61 GLN HB3 H 1 1.833 0.02 . 2 . . . . . . . . 5778 1 615 . 1 1 61 61 GLN CG C 13 33.65 0.05 . 1 . . . . . . . . 5778 1 616 . 1 1 61 61 GLN HG2 H 1 2.332 0.02 . 2 . . . . . . . . 5778 1 617 . 1 1 61 61 GLN HG3 H 1 2.301 0.02 . 2 . . . . . . . . 5778 1 618 . 1 1 61 61 GLN HE21 H 1 7.535 0.02 . 2 . . . . . . . . 5778 1 619 . 1 1 61 61 GLN HE22 H 1 6.78 0.02 . 2 . . . . . . . . 5778 1 620 . 1 1 62 62 LEU H H 1 8.806 0.02 . 1 . . . . . . . . 5778 1 621 . 1 1 62 62 LEU N N 15 123.62 0.05 . 1 . . . . . . . . 5778 1 622 . 1 1 62 62 LEU CA C 13 53.57 0.05 . 1 . . . . . . . . 5778 1 623 . 1 1 62 62 LEU HA H 1 5.536 0.02 . 1 . . . . . . . . 5778 1 624 . 1 1 62 62 LEU C C 13 176.77 0.05 . 1 . . . . . . . . 5778 1 625 . 1 1 62 62 LEU CB C 13 45.93 0.05 . 1 . . . . . . . . 5778 1 626 . 1 1 62 62 LEU HB2 H 1 1.715 0.02 . 2 . . . . . . . . 5778 1 627 . 1 1 62 62 LEU HB3 H 1 1.32 0.02 . 2 . . . . . . . . 5778 1 628 . 1 1 62 62 LEU HG H 1 1.594 0.02 . 1 . . . . . . . . 5778 1 629 . 1 1 62 62 LEU CD1 C 13 25.75 0.05 . 2 . . . . . . . . 5778 1 630 . 1 1 62 62 LEU HD11 H 1 0.921 0.02 . 2 . . . . . . . . 5778 1 631 . 1 1 62 62 LEU HD12 H 1 0.921 0.02 . 2 . . . . . . . . 5778 1 632 . 1 1 62 62 LEU HD13 H 1 0.921 0.02 . 2 . . . . . . . . 5778 1 633 . 1 1 62 62 LEU HD21 H 1 0.846 0.02 . 2 . . . . . . . . 5778 1 634 . 1 1 62 62 LEU HD22 H 1 0.846 0.02 . 2 . . . . . . . . 5778 1 635 . 1 1 62 62 LEU HD23 H 1 0.846 0.02 . 2 . . . . . . . . 5778 1 636 . 1 1 63 63 MET H H 1 8.825 0.02 . 1 . . . . . . . . 5778 1 637 . 1 1 63 63 MET N N 15 120.04 0.05 . 1 . . . . . . . . 5778 1 638 . 1 1 63 63 MET CA C 13 54.49 0.05 . 1 . . . . . . . . 5778 1 639 . 1 1 63 63 MET HA H 1 4.804 0.02 . 1 . . . . . . . . 5778 1 640 . 1 1 63 63 MET C C 13 174.44 0.05 . 1 . . . . . . . . 5778 1 641 . 1 1 63 63 MET CB C 13 36.16 0.05 . 1 . . . . . . . . 5778 1 642 . 1 1 63 63 MET HB2 H 1 2.056 0.02 . 2 . . . . . . . . 5778 1 643 . 1 1 63 63 MET HB3 H 1 1.912 0.02 . 2 . . . . . . . . 5778 1 644 . 1 1 63 63 MET HG2 H 1 2.512 0.02 . 2 . . . . . . . . 5778 1 645 . 1 1 63 63 MET HG3 H 1 2.407 0.02 . 2 . . . . . . . . 5778 1 646 . 1 1 64 64 LYS H H 1 8.904 0.02 . 1 . . . . . . . . 5778 1 647 . 1 1 64 64 LYS N N 15 122.98 0.05 . 1 . . . . . . . . 5778 1 648 . 1 1 64 64 LYS CA C 13 55.75 0.05 . 1 . . . . . . . . 5778 1 649 . 1 1 64 64 LYS HA H 1 4.873 0.02 . 1 . . . . . . . . 5778 1 650 . 1 1 64 64 LYS C C 13 174.8 0.05 . 1 . . . . . . . . 5778 1 651 . 1 1 64 64 LYS CB C 13 34.85 0.05 . 1 . . . . . . . . 5778 1 652 . 1 1 64 64 LYS HB2 H 1 1.818 0.02 . 2 . . . . . . . . 5778 1 653 . 1 1 64 64 LYS HG2 H 1 1.448 0.02 . 2 . . . . . . . . 5778 1 654 . 1 1 64 64 LYS HG3 H 1 1.313 0.02 . 2 . . . . . . . . 5778 1 655 . 1 1 64 64 LYS HD2 H 1 1.778 0.02 . 2 . . . . . . . . 5778 1 656 . 1 1 64 64 LYS CE C 13 41.38 0.05 . 1 . . . . . . . . 5778 1 657 . 1 1 64 64 LYS HE2 H 1 2.914 0.02 . 2 . . . . . . . . 5778 1 658 . 1 1 65 65 THR H H 1 8.056 0.02 . 1 . . . . . . . . 5778 1 659 . 1 1 65 65 THR N N 15 115.65 0.05 . 1 . . . . . . . . 5778 1 660 . 1 1 65 65 THR CA C 13 59.89 0.05 . 1 . . . . . . . . 5778 1 661 . 1 1 65 65 THR HA H 1 4.696 0.02 . 1 . . . . . . . . 5778 1 662 . 1 1 65 65 THR C C 13 171.32 0.05 . 1 . . . . . . . . 5778 1 663 . 1 1 65 65 THR CB C 13 69.54 0.05 . 1 . . . . . . . . 5778 1 664 . 1 1 65 65 THR HB H 1 4.263 0.02 . 1 . . . . . . . . 5778 1 665 . 1 1 65 65 THR CG2 C 13 20.31 0.05 . 1 . . . . . . . . 5778 1 666 . 1 1 65 65 THR HG21 H 1 1.053 0.02 . 1 . . . . . . . . 5778 1 667 . 1 1 65 65 THR HG22 H 1 1.053 0.02 . 1 . . . . . . . . 5778 1 668 . 1 1 65 65 THR HG23 H 1 1.053 0.02 . 1 . . . . . . . . 5778 1 669 . 1 1 66 66 GLU H H 1 8.413 0.02 . 1 . . . . . . . . 5778 1 670 . 1 1 66 66 GLU N N 15 119.67 0.05 . 1 . . . . . . . . 5778 1 671 . 1 1 66 66 GLU CA C 13 52.82 0.05 . 1 . . . . . . . . 5778 1 672 . 1 1 66 66 GLU HA H 1 5.084 0.02 . 1 . . . . . . . . 5778 1 673 . 1 1 66 66 GLU C C 13 174.99 0.05 . 1 . . . . . . . . 5778 1 674 . 1 1 66 66 GLU CB C 13 28.78 0.05 . 1 . . . . . . . . 5778 1 675 . 1 1 66 66 GLU HB2 H 1 2.393 0.02 . 2 . . . . . . . . 5778 1 676 . 1 1 66 66 GLU HB3 H 1 2.205 0.02 . 2 . . . . . . . . 5778 1 677 . 1 1 66 66 GLU HG2 H 1 2.442 0.02 . 2 . . . . . . . . 5778 1 678 . 1 1 67 67 ARG H H 1 7.775 0.02 . 1 . . . . . . . . 5778 1 679 . 1 1 67 67 ARG N N 15 117.76 0.05 . 1 . . . . . . . . 5778 1 680 . 1 1 67 67 ARG CA C 13 51.92 0.05 . 1 . . . . . . . . 5778 1 681 . 1 1 67 67 ARG HA H 1 4.408 0.02 . 1 . . . . . . . . 5778 1 682 . 1 1 67 67 ARG C C 13 174.49 0.05 . 1 . . . . . . . . 5778 1 683 . 1 1 67 67 ARG CB C 13 31.95 0.05 . 1 . . . . . . . . 5778 1 684 . 1 1 67 67 ARG HB2 H 1 1.439 0.02 . 2 . . . . . . . . 5778 1 685 . 1 1 67 67 ARG HG2 H 1 1.693 0.02 . 2 . . . . . . . . 5778 1 686 . 1 1 67 67 ARG HG3 H 1 1.541 0.02 . 2 . . . . . . . . 5778 1 687 . 1 1 67 67 ARG HD2 H 1 3.101 0.02 . 2 . . . . . . . . 5778 1 688 . 1 1 67 67 ARG HD3 H 1 3.13 0.02 . 2 . . . . . . . . 5778 1 689 . 1 1 68 68 PRO CA C 13 63.71 0.05 . 1 . . . . . . . . 5778 1 690 . 1 1 68 68 PRO HA H 1 4.512 0.02 . 1 . . . . . . . . 5778 1 691 . 1 1 68 68 PRO C C 13 175.43 0.05 . 1 . . . . . . . . 5778 1 692 . 1 1 68 68 PRO CB C 13 34.32 0.05 . 1 . . . . . . . . 5778 1 693 . 1 1 68 68 PRO HB2 H 1 2.483 0.02 . 2 . . . . . . . . 5778 1 694 . 1 1 68 68 PRO HB3 H 1 1.867 0.02 . 2 . . . . . . . . 5778 1 695 . 1 1 68 68 PRO HG2 H 1 2.25 0.02 . 2 . . . . . . . . 5778 1 696 . 1 1 68 68 PRO HG3 H 1 2.126 0.02 . 2 . . . . . . . . 5778 1 697 . 1 1 68 68 PRO HD2 H 1 3.682 0.02 . 2 . . . . . . . . 5778 1 698 . 1 1 68 68 PRO HD3 H 1 3.566 0.02 . 2 . . . . . . . . 5778 1 699 . 1 1 69 69 ARG H H 1 7.457 0.02 . 1 . . . . . . . . 5778 1 700 . 1 1 69 69 ARG N N 15 119.97 0.05 . 1 . . . . . . . . 5778 1 701 . 1 1 69 69 ARG CA C 13 52.14 0.05 . 1 . . . . . . . . 5778 1 702 . 1 1 69 69 ARG HA H 1 4.695 0.02 . 1 . . . . . . . . 5778 1 703 . 1 1 69 69 ARG C C 13 172.37 0.05 . 1 . . . . . . . . 5778 1 704 . 1 1 69 69 ARG CB C 13 31.71 0.05 . 1 . . . . . . . . 5778 1 705 . 1 1 69 69 ARG HB2 H 1 1.148 0.02 . 2 . . . . . . . . 5778 1 706 . 1 1 69 69 ARG HG2 H 1 1.539 0.02 . 2 . . . . . . . . 5778 1 707 . 1 1 69 69 ARG HG3 H 1 1.239 0.02 . 2 . . . . . . . . 5778 1 708 . 1 1 69 69 ARG HD2 H 1 3.037 0.02 . 2 . . . . . . . . 5778 1 709 . 1 1 69 69 ARG HD3 H 1 3.004 0.02 . 2 . . . . . . . . 5778 1 710 . 1 1 70 70 PRO CA C 13 62.44 0.05 . 1 . . . . . . . . 5778 1 711 . 1 1 70 70 PRO HA H 1 4.59 0.02 . 1 . . . . . . . . 5778 1 712 . 1 1 70 70 PRO C C 13 175.8 0.05 . 1 . . . . . . . . 5778 1 713 . 1 1 70 70 PRO CB C 13 32.72 0.05 . 1 . . . . . . . . 5778 1 714 . 1 1 70 70 PRO HB2 H 1 2.376 0.02 . 2 . . . . . . . . 5778 1 715 . 1 1 70 70 PRO HB3 H 1 1.797 0.02 . 2 . . . . . . . . 5778 1 716 . 1 1 70 70 PRO HG2 H 1 2.013 0.02 . 2 . . . . . . . . 5778 1 717 . 1 1 70 70 PRO HG3 H 1 1.982 0.02 . 2 . . . . . . . . 5778 1 718 . 1 1 70 70 PRO HD2 H 1 3.38 0.02 . 2 . . . . . . . . 5778 1 719 . 1 1 70 70 PRO HD3 H 1 3.357 0.02 . 2 . . . . . . . . 5778 1 720 . 1 1 71 71 ASN H H 1 8.849 0.02 . 1 . . . . . . . . 5778 1 721 . 1 1 71 71 ASN N N 15 112.69 0.05 . 1 . . . . . . . . 5778 1 722 . 1 1 71 71 ASN CA C 13 55.09 0.05 . 1 . . . . . . . . 5778 1 723 . 1 1 71 71 ASN HA H 1 4.062 0.02 . 1 . . . . . . . . 5778 1 724 . 1 1 71 71 ASN C C 13 174.44 0.05 . 1 . . . . . . . . 5778 1 725 . 1 1 71 71 ASN CB C 13 37.52 0.05 . 1 . . . . . . . . 5778 1 726 . 1 1 71 71 ASN HB2 H 1 3.243 0.02 . 2 . . . . . . . . 5778 1 727 . 1 1 71 71 ASN HB3 H 1 2.438 0.02 . 2 . . . . . . . . 5778 1 728 . 1 1 72 72 THR H H 1 7.58 0.02 . 1 . . . . . . . . 5778 1 729 . 1 1 72 72 THR N N 15 116.28 0.05 . 1 . . . . . . . . 5778 1 730 . 1 1 72 72 THR CA C 13 62.59 0.05 . 1 . . . . . . . . 5778 1 731 . 1 1 72 72 THR HA H 1 4.063 0.02 . 1 . . . . . . . . 5778 1 732 . 1 1 72 72 THR C C 13 175.76 0.05 . 1 . . . . . . . . 5778 1 733 . 1 1 72 72 THR CB C 13 69.79 0.05 . 1 . . . . . . . . 5778 1 734 . 1 1 72 72 THR HB H 1 5.419 0.02 . 1 . . . . . . . . 5778 1 735 . 1 1 72 72 THR CG2 C 13 22.99 0.05 . 1 . . . . . . . . 5778 1 736 . 1 1 72 72 THR HG21 H 1 1.246 0.02 . 1 . . . . . . . . 5778 1 737 . 1 1 72 72 THR HG22 H 1 1.246 0.02 . 1 . . . . . . . . 5778 1 738 . 1 1 72 72 THR HG23 H 1 1.246 0.02 . 1 . . . . . . . . 5778 1 739 . 1 1 73 73 PHE H H 1 9.637 0.02 . 1 . . . . . . . . 5778 1 740 . 1 1 73 73 PHE N N 15 123.41 0.05 . 1 . . . . . . . . 5778 1 741 . 1 1 73 73 PHE CA C 13 56.42 0.05 . 1 . . . . . . . . 5778 1 742 . 1 1 73 73 PHE HA H 1 5.603 0.02 . 1 . . . . . . . . 5778 1 743 . 1 1 73 73 PHE C C 13 171.22 0.05 . 1 . . . . . . . . 5778 1 744 . 1 1 73 73 PHE CB C 13 42.17 0.05 . 1 . . . . . . . . 5778 1 745 . 1 1 73 73 PHE HB2 H 1 3.146 0.02 . 2 . . . . . . . . 5778 1 746 . 1 1 73 73 PHE HB3 H 1 3.016 0.02 . 2 . . . . . . . . 5778 1 747 . 1 1 73 73 PHE HD1 H 1 6.847 0.02 . 3 . . . . . . . . 5778 1 748 . 1 1 73 73 PHE HE1 H 1 6.62 0.02 . 3 . . . . . . . . 5778 1 749 . 1 1 73 73 PHE HZ H 1 6.19 0.02 . 1 . . . . . . . . 5778 1 750 . 1 1 74 74 VAL H H 1 9.17 0.02 . 1 . . . . . . . . 5778 1 751 . 1 1 74 74 VAL N N 15 121.71 0.05 . 1 . . . . . . . . 5778 1 752 . 1 1 74 74 VAL CA C 13 60.08 0.05 . 1 . . . . . . . . 5778 1 753 . 1 1 74 74 VAL HA H 1 4.912 0.02 . 1 . . . . . . . . 5778 1 754 . 1 1 74 74 VAL C C 13 175.24 0.05 . 1 . . . . . . . . 5778 1 755 . 1 1 74 74 VAL CB C 13 35.28 0.05 . 1 . . . . . . . . 5778 1 756 . 1 1 74 74 VAL HB H 1 1.823 0.02 . 1 . . . . . . . . 5778 1 757 . 1 1 74 74 VAL HG11 H 1 0.766 0.02 . 1 . . . . . . . . 5778 1 758 . 1 1 74 74 VAL HG12 H 1 0.766 0.02 . 1 . . . . . . . . 5778 1 759 . 1 1 74 74 VAL HG13 H 1 0.766 0.02 . 1 . . . . . . . . 5778 1 760 . 1 1 74 74 VAL HG21 H 1 0.908 0.02 . 1 . . . . . . . . 5778 1 761 . 1 1 74 74 VAL HG22 H 1 0.908 0.02 . 1 . . . . . . . . 5778 1 762 . 1 1 74 74 VAL HG23 H 1 0.908 0.02 . 1 . . . . . . . . 5778 1 763 . 1 1 75 75 ILE H H 1 9.282 0.02 . 1 . . . . . . . . 5778 1 764 . 1 1 75 75 ILE N N 15 124.2 0.05 . 1 . . . . . . . . 5778 1 765 . 1 1 75 75 ILE CA C 13 59.81 0.05 . 1 . . . . . . . . 5778 1 766 . 1 1 75 75 ILE HA H 1 4.834 0.02 . 1 . . . . . . . . 5778 1 767 . 1 1 75 75 ILE HB H 1 1.835 0.02 . 1 . . . . . . . . 5778 1 768 . 1 1 75 75 ILE HG21 H 1 0.79 0.02 . 1 . . . . . . . . 5778 1 769 . 1 1 75 75 ILE HG22 H 1 0.79 0.02 . 1 . . . . . . . . 5778 1 770 . 1 1 75 75 ILE HG23 H 1 0.79 0.02 . 1 . . . . . . . . 5778 1 771 . 1 1 75 75 ILE HG12 H 1 0.97 0.02 . 2 . . . . . . . . 5778 1 772 . 1 1 75 75 ILE CD1 C 13 20.64 0.05 . 1 . . . . . . . . 5778 1 773 . 1 1 75 75 ILE HD11 H 1 0.747 0.02 . 1 . . . . . . . . 5778 1 774 . 1 1 75 75 ILE HD12 H 1 0.747 0.02 . 1 . . . . . . . . 5778 1 775 . 1 1 75 75 ILE HD13 H 1 0.747 0.02 . 1 . . . . . . . . 5778 1 776 . 1 1 80 80 TRP HD1 H 1 7.248 0.02 . 1 . . . . . . . . 5778 1 777 . 1 1 80 80 TRP HE1 H 1 10.20 0.02 . 1 . . . . . . . . 5778 1 778 . 1 1 87 87 THR H H 1 8.37 0.02 . 1 . . . . . . . . 5778 1 779 . 1 1 87 87 THR CA C 13 62.93 0.05 . 1 . . . . . . . . 5778 1 780 . 1 1 87 87 THR HA H 1 5.54 0.02 . 1 . . . . . . . . 5778 1 781 . 1 1 87 87 THR C C 13 171.72 0.05 . 1 . . . . . . . . 5778 1 782 . 1 1 87 87 THR CB C 13 69.54 0.05 . 1 . . . . . . . . 5778 1 783 . 1 1 87 87 THR HB H 1 4.575 0.02 . 1 . . . . . . . . 5778 1 784 . 1 1 87 87 THR HG21 H 1 1.091 0.02 . 1 . . . . . . . . 5778 1 785 . 1 1 87 87 THR HG22 H 1 1.091 0.02 . 1 . . . . . . . . 5778 1 786 . 1 1 87 87 THR HG23 H 1 1.091 0.02 . 1 . . . . . . . . 5778 1 787 . 1 1 88 88 PHE H H 1 8.781 0.02 . 1 . . . . . . . . 5778 1 788 . 1 1 88 88 PHE N N 15 123.67 0.05 . 1 . . . . . . . . 5778 1 789 . 1 1 88 88 PHE CA C 13 55.82 0.05 . 1 . . . . . . . . 5778 1 790 . 1 1 88 88 PHE HA H 1 5.517 0.02 . 1 . . . . . . . . 5778 1 791 . 1 1 88 88 PHE C C 13 173.85 0.05 . 1 . . . . . . . . 5778 1 792 . 1 1 88 88 PHE CB C 13 43.81 0.05 . 1 . . . . . . . . 5778 1 793 . 1 1 88 88 PHE HB2 H 1 3.053 0.02 . 2 . . . . . . . . 5778 1 794 . 1 1 88 88 PHE HB3 H 1 2.904 0.02 . 2 . . . . . . . . 5778 1 795 . 1 1 88 88 PHE HD1 H 1 6.853 0.02 . 3 . . . . . . . . 5778 1 796 . 1 1 88 88 PHE HE1 H 1 6.618 0.02 . 3 . . . . . . . . 5778 1 797 . 1 1 88 88 PHE HZ H 1 6.195 0.02 . 1 . . . . . . . . 5778 1 798 . 1 1 89 89 HIS H H 1 9.453 0.02 . 1 . . . . . . . . 5778 1 799 . 1 1 89 89 HIS N N 15 118.14 0.05 . 1 . . . . . . . . 5778 1 800 . 1 1 89 89 HIS CA C 13 55.49 0.05 . 1 . . . . . . . . 5778 1 801 . 1 1 89 89 HIS HA H 1 5.245 0.02 . 1 . . . . . . . . 5778 1 802 . 1 1 89 89 HIS C C 13 172.46 0.05 . 1 . . . . . . . . 5778 1 803 . 1 1 89 89 HIS CB C 13 32.6 0.05 . 1 . . . . . . . . 5778 1 804 . 1 1 89 89 HIS HB2 H 1 2.803 0.02 . 2 . . . . . . . . 5778 1 805 . 1 1 89 89 HIS HB3 H 1 2.539 0.02 . 2 . . . . . . . . 5778 1 806 . 1 1 89 89 HIS HD2 H 1 6.492 0.02 . 1 . . . . . . . . 5778 1 807 . 1 1 90 90 VAL H H 1 7.197 0.02 . 1 . . . . . . . . 5778 1 808 . 1 1 90 90 VAL N N 15 116.5 0.05 . 1 . . . . . . . . 5778 1 809 . 1 1 90 90 VAL CA C 13 58.89 0.05 . 1 . . . . . . . . 5778 1 810 . 1 1 90 90 VAL HA H 1 4.776 0.02 . 1 . . . . . . . . 5778 1 811 . 1 1 90 90 VAL C C 13 174.64 0.05 . 1 . . . . . . . . 5778 1 812 . 1 1 90 90 VAL CB C 13 33.85 0.05 . 1 . . . . . . . . 5778 1 813 . 1 1 90 90 VAL HB H 1 2.491 0.02 . 1 . . . . . . . . 5778 1 814 . 1 1 90 90 VAL CG1 C 13 24.26 0.05 . 1 . . . . . . . . 5778 1 815 . 1 1 90 90 VAL HG11 H 1 1.11 0.02 . 1 . . . . . . . . 5778 1 816 . 1 1 90 90 VAL HG12 H 1 1.11 0.02 . 1 . . . . . . . . 5778 1 817 . 1 1 90 90 VAL HG13 H 1 1.11 0.02 . 1 . . . . . . . . 5778 1 818 . 1 1 90 90 VAL HG21 H 1 1.044 0.02 . 1 . . . . . . . . 5778 1 819 . 1 1 90 90 VAL HG22 H 1 1.044 0.02 . 1 . . . . . . . . 5778 1 820 . 1 1 90 90 VAL HG23 H 1 1.044 0.02 . 1 . . . . . . . . 5778 1 821 . 1 1 91 91 ASP H H 1 8.536 0.02 . 1 . . . . . . . . 5778 1 822 . 1 1 91 91 ASP N N 15 117.35 0.05 . 1 . . . . . . . . 5778 1 823 . 1 1 91 91 ASP CA C 13 56.3 0.05 . 1 . . . . . . . . 5778 1 824 . 1 1 91 91 ASP HA H 1 4.61 0.02 . 1 . . . . . . . . 5778 1 825 . 1 1 91 91 ASP C C 13 175.69 0.05 . 1 . . . . . . . . 5778 1 826 . 1 1 91 91 ASP CB C 13 41.6 0.05 . 1 . . . . . . . . 5778 1 827 . 1 1 91 91 ASP HB2 H 1 2.83 0.02 . 2 . . . . . . . . 5778 1 828 . 1 1 91 91 ASP HB3 H 1 2.778 0.02 . 2 . . . . . . . . 5778 1 829 . 1 1 92 92 SER H H 1 7.449 0.02 . 1 . . . . . . . . 5778 1 830 . 1 1 92 92 SER N N 15 111.57 0.05 . 1 . . . . . . . . 5778 1 831 . 1 1 92 92 SER CA C 13 55.28 0.05 . 1 . . . . . . . . 5778 1 832 . 1 1 92 92 SER HA H 1 5.045 0.02 . 1 . . . . . . . . 5778 1 833 . 1 1 92 92 SER CB C 13 64.41 0.05 . 1 . . . . . . . . 5778 1 834 . 1 1 92 92 SER HB2 H 1 4.263 0.02 . 2 . . . . . . . . 5778 1 835 . 1 1 92 92 SER HB3 H 1 3.906 0.02 . 2 . . . . . . . . 5778 1 836 . 1 1 93 93 PRO CA C 13 64.97 0.05 . 1 . . . . . . . . 5778 1 837 . 1 1 93 93 PRO HA H 1 4.302 0.02 . 1 . . . . . . . . 5778 1 838 . 1 1 93 93 PRO C C 13 180.07 0.05 . 1 . . . . . . . . 5778 1 839 . 1 1 93 93 PRO CB C 13 31.26 0.05 . 1 . . . . . . . . 5778 1 840 . 1 1 93 93 PRO HB2 H 1 2.46 0.02 . 2 . . . . . . . . 5778 1 841 . 1 1 93 93 PRO HB3 H 1 2.121 0.02 . 2 . . . . . . . . 5778 1 842 . 1 1 93 93 PRO CG C 13 27.29 0.05 . 1 . . . . . . . . 5778 1 843 . 1 1 93 93 PRO HG2 H 1 2.176 0.02 . 2 . . . . . . . . 5778 1 844 . 1 1 93 93 PRO HD2 H 1 4.036 0.02 . 2 . . . . . . . . 5778 1 845 . 1 1 93 93 PRO HD3 H 1 3.878 0.02 . 2 . . . . . . . . 5778 1 846 . 1 1 94 94 ASP H H 1 8.459 0.02 . 1 . . . . . . . . 5778 1 847 . 1 1 94 94 ASP N N 15 119.66 0.05 . 1 . . . . . . . . 5778 1 848 . 1 1 94 94 ASP CA C 13 56.77 0.05 . 1 . . . . . . . . 5778 1 849 . 1 1 94 94 ASP HA H 1 4.401 0.02 . 1 . . . . . . . . 5778 1 850 . 1 1 94 94 ASP C C 13 178.15 0.05 . 1 . . . . . . . . 5778 1 851 . 1 1 94 94 ASP CB C 13 39.79 0.05 . 1 . . . . . . . . 5778 1 852 . 1 1 94 94 ASP HB2 H 1 2.673 0.02 . 2 . . . . . . . . 5778 1 853 . 1 1 94 94 ASP HB3 H 1 2.542 0.02 . 2 . . . . . . . . 5778 1 854 . 1 1 95 95 GLU H H 1 7.647 0.02 . 1 . . . . . . . . 5778 1 855 . 1 1 95 95 GLU N N 15 120.49 0.05 . 1 . . . . . . . . 5778 1 856 . 1 1 95 95 GLU CA C 13 58.69 0.05 . 1 . . . . . . . . 5778 1 857 . 1 1 95 95 GLU HA H 1 4.154 0.02 . 1 . . . . . . . . 5778 1 858 . 1 1 95 95 GLU C C 13 178.52 0.05 . 1 . . . . . . . . 5778 1 859 . 1 1 95 95 GLU CB C 13 30.32 0.05 . 1 . . . . . . . . 5778 1 860 . 1 1 95 95 GLU HB2 H 1 2.247 0.02 . 2 . . . . . . . . 5778 1 861 . 1 1 95 95 GLU HB3 H 1 2.149 0.02 . 2 . . . . . . . . 5778 1 862 . 1 1 95 95 GLU CG C 13 36.68 0.05 . 1 . . . . . . . . 5778 1 863 . 1 1 95 95 GLU HG2 H 1 2.512 0.02 . 2 . . . . . . . . 5778 1 864 . 1 1 95 95 GLU HG3 H 1 2.372 0.02 . 2 . . . . . . . . 5778 1 865 . 1 1 96 96 ARG H H 1 7.673 0.02 . 1 . . . . . . . . 5778 1 866 . 1 1 96 96 ARG N N 15 119.96 0.05 . 1 . . . . . . . . 5778 1 867 . 1 1 96 96 ARG CA C 13 60.64 0.05 . 1 . . . . . . . . 5778 1 868 . 1 1 96 96 ARG HA H 1 3.827 0.02 . 1 . . . . . . . . 5778 1 869 . 1 1 96 96 ARG C C 13 176.72 0.05 . 1 . . . . . . . . 5778 1 870 . 1 1 96 96 ARG CB C 13 29.00 0.05 . 1 . . . . . . . . 5778 1 871 . 1 1 96 96 ARG HB2 H 1 1.565 0.02 . 2 . . . . . . . . 5778 1 872 . 1 1 96 96 ARG HB3 H 1 1.535 0.02 . 2 . . . . . . . . 5778 1 873 . 1 1 96 96 ARG HG2 H 1 1.101 0.02 . 2 . . . . . . . . 5778 1 874 . 1 1 96 96 ARG HG3 H 1 1.036 0.02 . 2 . . . . . . . . 5778 1 875 . 1 1 97 97 GLU H H 1 7.934 0.02 . 1 . . . . . . . . 5778 1 876 . 1 1 97 97 GLU N N 15 119.11 0.05 . 1 . . . . . . . . 5778 1 877 . 1 1 97 97 GLU CA C 13 59.02 0.05 . 1 . . . . . . . . 5778 1 878 . 1 1 97 97 GLU HA H 1 3.855 0.02 . 1 . . . . . . . . 5778 1 879 . 1 1 97 97 GLU C C 13 178.48 0.05 . 1 . . . . . . . . 5778 1 880 . 1 1 97 97 GLU CB C 13 28.7 0.05 . 1 . . . . . . . . 5778 1 881 . 1 1 97 97 GLU HB2 H 1 2.16 0.02 . 2 . . . . . . . . 5778 1 882 . 1 1 97 97 GLU HB3 H 1 2.123 0.02 . 2 . . . . . . . . 5778 1 883 . 1 1 97 97 GLU HG2 H 1 2.33 0.02 . 2 . . . . . . . . 5778 1 884 . 1 1 98 98 GLU H H 1 7.871 0.02 . 1 . . . . . . . . 5778 1 885 . 1 1 98 98 GLU N N 15 117.32 0.05 . 1 . . . . . . . . 5778 1 886 . 1 1 98 98 GLU CA C 13 59.24 0.05 . 1 . . . . . . . . 5778 1 887 . 1 1 98 98 GLU HA H 1 3.88 0.02 . 1 . . . . . . . . 5778 1 888 . 1 1 98 98 GLU C C 13 180.19 0.05 . 1 . . . . . . . . 5778 1 889 . 1 1 98 98 GLU CB C 13 29.31 0.05 . 1 . . . . . . . . 5778 1 890 . 1 1 98 98 GLU HB2 H 1 2.16 0.02 . 2 . . . . . . . . 5778 1 891 . 1 1 98 98 GLU HB3 H 1 2.082 0.02 . 2 . . . . . . . . 5778 1 892 . 1 1 98 98 GLU CG C 13 35.31 0.05 . 1 . . . . . . . . 5778 1 893 . 1 1 98 98 GLU HG2 H 1 2.339 0.02 . 2 . . . . . . . . 5778 1 894 . 1 1 99 99 TRP H H 1 8.08 0.02 . 1 . . . . . . . . 5778 1 895 . 1 1 99 99 TRP N N 15 119.81 0.05 . 1 . . . . . . . . 5778 1 896 . 1 1 99 99 TRP CA C 13 61.74 0.05 . 1 . . . . . . . . 5778 1 897 . 1 1 99 99 TRP HA H 1 3.847 0.02 . 1 . . . . . . . . 5778 1 898 . 1 1 99 99 TRP C C 13 177.78 0.05 . 1 . . . . . . . . 5778 1 899 . 1 1 99 99 TRP HB2 H 1 2.829 0.02 . 2 . . . . . . . . 5778 1 900 . 1 1 99 99 TRP HB3 H 1 2.608 0.02 . 2 . . . . . . . . 5778 1 901 . 1 1 99 99 TRP HD1 H 1 7.172 0.02 . 1 . . . . . . . . 5778 1 902 . 1 1 99 99 TRP HE1 H 1 11.06 0.02 . 1 . . . . . . . . 5778 1 903 . 1 1 99 99 TRP HZ2 H 1 6.784 0.02 . 1 . . . . . . . . 5778 1 904 . 1 1 99 99 TRP HZ3 H 1 6.816 0.02 . 1 . . . . . . . . 5778 1 905 . 1 1 99 99 TRP HH2 H 1 6.478 0.02 . 1 . . . . . . . . 5778 1 906 . 1 1 100 100 MET H H 1 8.294 0.02 . 1 . . . . . . . . 5778 1 907 . 1 1 100 100 MET N N 15 116.09 0.05 . 1 . . . . . . . . 5778 1 908 . 1 1 100 100 MET CA C 13 59.9 0.05 . 1 . . . . . . . . 5778 1 909 . 1 1 100 100 MET HA H 1 3.441 0.02 . 1 . . . . . . . . 5778 1 910 . 1 1 100 100 MET C C 13 177.59 0.05 . 1 . . . . . . . . 5778 1 911 . 1 1 100 100 MET HB2 H 1 1.809 0.02 . 2 . . . . . . . . 5778 1 912 . 1 1 100 100 MET HG2 H 1 2.317 0.02 . 2 . . . . . . . . 5778 1 913 . 1 1 101 101 ARG H H 1 8.388 0.02 . 1 . . . . . . . . 5778 1 914 . 1 1 101 101 ARG N N 15 118.27 0.05 . 1 . . . . . . . . 5778 1 915 . 1 1 101 101 ARG CA C 13 58.91 0.05 . 1 . . . . . . . . 5778 1 916 . 1 1 101 101 ARG HA H 1 3.867 0.02 . 1 . . . . . . . . 5778 1 917 . 1 1 101 101 ARG C C 13 178.64 0.05 . 1 . . . . . . . . 5778 1 918 . 1 1 101 101 ARG CB C 13 29.92 0.05 . 1 . . . . . . . . 5778 1 919 . 1 1 101 101 ARG HB2 H 1 1.801 0.02 . 2 . . . . . . . . 5778 1 920 . 1 1 101 101 ARG HB3 H 1 1.697 0.02 . 2 . . . . . . . . 5778 1 921 . 1 1 101 101 ARG HG2 H 1 1.514 0.02 . 2 . . . . . . . . 5778 1 922 . 1 1 101 101 ARG CD C 13 42.95 0.05 . 1 . . . . . . . . 5778 1 923 . 1 1 101 101 ARG HD2 H 1 3.117 0.02 . 2 . . . . . . . . 5778 1 924 . 1 1 101 101 ARG HD3 H 1 3.089 0.02 . 2 . . . . . . . . 5778 1 925 . 1 1 102 102 ALA H H 1 7.55 0.02 . 1 . . . . . . . . 5778 1 926 . 1 1 102 102 ALA N N 15 121.87 0.05 . 1 . . . . . . . . 5778 1 927 . 1 1 102 102 ALA CA C 13 55.13 0.05 . 1 . . . . . . . . 5778 1 928 . 1 1 102 102 ALA HA H 1 3.959 0.02 . 1 . . . . . . . . 5778 1 929 . 1 1 102 102 ALA C C 13 178.54 0.05 . 1 . . . . . . . . 5778 1 930 . 1 1 102 102 ALA CB C 13 18.05 0.05 . 1 . . . . . . . . 5778 1 931 . 1 1 102 102 ALA HB1 H 1 1.131 0.02 . 1 . . . . . . . . 5778 1 932 . 1 1 102 102 ALA HB2 H 1 1.131 0.02 . 1 . . . . . . . . 5778 1 933 . 1 1 102 102 ALA HB3 H 1 1.131 0.02 . 1 . . . . . . . . 5778 1 934 . 1 1 103 103 ILE H H 1 8.298 0.02 . 1 . . . . . . . . 5778 1 935 . 1 1 103 103 ILE N N 15 117.18 0.05 . 1 . . . . . . . . 5778 1 936 . 1 1 103 103 ILE CA C 13 65.9 0.05 . 1 . . . . . . . . 5778 1 937 . 1 1 103 103 ILE HA H 1 3.308 0.02 . 1 . . . . . . . . 5778 1 938 . 1 1 103 103 ILE C C 13 176.85 0.05 . 1 . . . . . . . . 5778 1 939 . 1 1 103 103 ILE CB C 13 37.9 0.05 . 1 . . . . . . . . 5778 1 940 . 1 1 103 103 ILE HB H 1 1.594 0.02 . 1 . . . . . . . . 5778 1 941 . 1 1 103 103 ILE HG21 H 1 0.705 0.02 . 1 . . . . . . . . 5778 1 942 . 1 1 103 103 ILE HG22 H 1 0.705 0.02 . 1 . . . . . . . . 5778 1 943 . 1 1 103 103 ILE HG23 H 1 0.705 0.02 . 1 . . . . . . . . 5778 1 944 . 1 1 103 103 ILE HG12 H 1 0.837 0.02 . 2 . . . . . . . . 5778 1 945 . 1 1 103 103 ILE CD1 C 13 14.35 0.05 . 1 . . . . . . . . 5778 1 946 . 1 1 103 103 ILE HD11 H 1 0.507 0.02 . 1 . . . . . . . . 5778 1 947 . 1 1 103 103 ILE HD12 H 1 0.507 0.02 . 1 . . . . . . . . 5778 1 948 . 1 1 103 103 ILE HD13 H 1 0.507 0.02 . 1 . . . . . . . . 5778 1 949 . 1 1 104 104 GLN H H 1 8.116 0.02 . 1 . . . . . . . . 5778 1 950 . 1 1 104 104 GLN N N 15 117.77 0.05 . 1 . . . . . . . . 5778 1 951 . 1 1 104 104 GLN CA C 13 58.3 0.05 . 1 . . . . . . . . 5778 1 952 . 1 1 104 104 GLN HA H 1 3.823 0.02 . 1 . . . . . . . . 5778 1 953 . 1 1 104 104 GLN C C 13 177.7 0.05 . 1 . . . . . . . . 5778 1 954 . 1 1 104 104 GLN CB C 13 28.89 0.05 . 1 . . . . . . . . 5778 1 955 . 1 1 104 104 GLN HB2 H 1 2.049 0.02 . 2 . . . . . . . . 5778 1 956 . 1 1 104 104 GLN HB3 H 1 1.976 0.02 . 2 . . . . . . . . 5778 1 957 . 1 1 104 104 GLN HG2 H 1 2.306 0.02 . 2 . . . . . . . . 5778 1 958 . 1 1 104 104 GLN HG3 H 1 2.268 0.02 . 2 . . . . . . . . 5778 1 959 . 1 1 104 104 GLN HE21 H 1 7.242 0.02 . 2 . . . . . . . . 5778 1 960 . 1 1 104 104 GLN HE22 H 1 7.114 0.02 . 2 . . . . . . . . 5778 1 961 . 1 1 105 105 MET H H 1 8.163 0.02 . 1 . . . . . . . . 5778 1 962 . 1 1 105 105 MET N N 15 119.13 0.05 . 1 . . . . . . . . 5778 1 963 . 1 1 105 105 MET CA C 13 58.94 0.05 . 1 . . . . . . . . 5778 1 964 . 1 1 105 105 MET HA H 1 4.045 0.02 . 1 . . . . . . . . 5778 1 965 . 1 1 105 105 MET C C 13 179.54 0.05 . 1 . . . . . . . . 5778 1 966 . 1 1 105 105 MET HB2 H 1 2.25 0.02 . 2 . . . . . . . . 5778 1 967 . 1 1 105 105 MET HB3 H 1 2.145 0.02 . 2 . . . . . . . . 5778 1 968 . 1 1 105 105 MET CG C 13 31.4 0.05 . 1 . . . . . . . . 5778 1 969 . 1 1 105 105 MET HG2 H 1 2.634 0.02 . 2 . . . . . . . . 5778 1 970 . 1 1 105 105 MET HG3 H 1 2.429 0.02 . 2 . . . . . . . . 5778 1 971 . 1 1 106 106 VAL H H 1 8.144 0.02 . 1 . . . . . . . . 5778 1 972 . 1 1 106 106 VAL N N 15 121.13 0.05 . 1 . . . . . . . . 5778 1 973 . 1 1 106 106 VAL CA C 13 66.15 0.05 . 1 . . . . . . . . 5778 1 974 . 1 1 106 106 VAL HA H 1 3.585 0.02 . 1 . . . . . . . . 5778 1 975 . 1 1 106 106 VAL C C 13 179.11 0.05 . 1 . . . . . . . . 5778 1 976 . 1 1 106 106 VAL CB C 13 31.13 0.05 . 1 . . . . . . . . 5778 1 977 . 1 1 106 106 VAL HB H 1 2.016 0.02 . 1 . . . . . . . . 5778 1 978 . 1 1 106 106 VAL HG11 H 1 0.824 0.02 . 1 . . . . . . . . 5778 1 979 . 1 1 106 106 VAL HG12 H 1 0.824 0.02 . 1 . . . . . . . . 5778 1 980 . 1 1 106 106 VAL HG13 H 1 0.824 0.02 . 1 . . . . . . . . 5778 1 981 . 1 1 106 106 VAL CG2 C 13 24.26 0.05 . 1 . . . . . . . . 5778 1 982 . 1 1 106 106 VAL HG21 H 1 0.977 0.02 . 1 . . . . . . . . 5778 1 983 . 1 1 106 106 VAL HG22 H 1 0.977 0.02 . 1 . . . . . . . . 5778 1 984 . 1 1 106 106 VAL HG23 H 1 0.977 0.02 . 1 . . . . . . . . 5778 1 985 . 1 1 107 107 ALA H H 1 8.875 0.02 . 1 . . . . . . . . 5778 1 986 . 1 1 107 107 ALA N N 15 123.68 0.05 . 1 . . . . . . . . 5778 1 987 . 1 1 107 107 ALA CA C 13 56.01 0.05 . 1 . . . . . . . . 5778 1 988 . 1 1 107 107 ALA HA H 1 3.859 0.02 . 1 . . . . . . . . 5778 1 989 . 1 1 107 107 ALA C C 13 180.99 0.05 . 1 . . . . . . . . 5778 1 990 . 1 1 107 107 ALA CB C 13 18.02 0.05 . 1 . . . . . . . . 5778 1 991 . 1 1 107 107 ALA HB1 H 1 1.523 0.02 . 1 . . . . . . . . 5778 1 992 . 1 1 107 107 ALA HB2 H 1 1.523 0.02 . 1 . . . . . . . . 5778 1 993 . 1 1 107 107 ALA HB3 H 1 1.523 0.02 . 1 . . . . . . . . 5778 1 994 . 1 1 108 108 ASN H H 1 8.684 0.02 . 1 . . . . . . . . 5778 1 995 . 1 1 108 108 ASN N N 15 116.6 0.05 . 1 . . . . . . . . 5778 1 996 . 1 1 108 108 ASN CA C 13 55.14 0.05 . 1 . . . . . . . . 5778 1 997 . 1 1 108 108 ASN HA H 1 4.447 0.02 . 1 . . . . . . . . 5778 1 998 . 1 1 108 108 ASN C C 13 177.28 0.05 . 1 . . . . . . . . 5778 1 999 . 1 1 108 108 ASN CB C 13 37.33 0.05 . 1 . . . . . . . . 5778 1 1000 . 1 1 108 108 ASN HB2 H 1 2.838 0.02 . 2 . . . . . . . . 5778 1 1001 . 1 1 108 108 ASN HB3 H 1 2.941 0.02 . 2 . . . . . . . . 5778 1 1002 . 1 1 108 108 ASN HD21 H 1 7.633 0.02 . 2 . . . . . . . . 5778 1 1003 . 1 1 108 108 ASN HD22 H 1 7.073 0.02 . 2 . . . . . . . . 5778 1 1004 . 1 1 109 109 SER H H 1 7.98 0.02 . 1 . . . . . . . . 5778 1 1005 . 1 1 109 109 SER N N 15 116.33 0.05 . 1 . . . . . . . . 5778 1 1006 . 1 1 109 109 SER CA C 13 60.2 0.05 . 1 . . . . . . . . 5778 1 1007 . 1 1 109 109 SER HA H 1 4.429 0.02 . 1 . . . . . . . . 5778 1 1008 . 1 1 109 109 SER C C 13 174.21 0.05 . 1 . . . . . . . . 5778 1 1009 . 1 1 109 109 SER CB C 13 63.23 0.05 . 1 . . . . . . . . 5778 1 1010 . 1 1 109 109 SER HB2 H 1 4.072 0.02 . 2 . . . . . . . . 5778 1 1011 . 1 1 109 109 SER HB3 H 1 4.036 0.02 . 2 . . . . . . . . 5778 1 1012 . 1 1 110 110 LEU H H 1 7.202 0.02 . 1 . . . . . . . . 5778 1 1013 . 1 1 110 110 LEU N N 15 122.09 0.05 . 1 . . . . . . . . 5778 1 1014 . 1 1 110 110 LEU CA C 13 54.71 0.05 . 1 . . . . . . . . 5778 1 1015 . 1 1 110 110 LEU HA H 1 4.437 0.02 . 1 . . . . . . . . 5778 1 1016 . 1 1 110 110 LEU C C 13 176.36 0.05 . 1 . . . . . . . . 5778 1 1017 . 1 1 110 110 LEU CB C 13 41.78 0.05 . 1 . . . . . . . . 5778 1 1018 . 1 1 110 110 LEU HB2 H 1 1.941 0.02 . 2 . . . . . . . . 5778 1 1019 . 1 1 110 110 LEU HB3 H 1 1.699 0.02 . 2 . . . . . . . . 5778 1 1020 . 1 1 110 110 LEU HG H 1 1.739 0.02 . 1 . . . . . . . . 5778 1 1021 . 1 1 110 110 LEU CD1 C 13 25.61 0.05 . 2 . . . . . . . . 5778 1 1022 . 1 1 110 110 LEU HD11 H 1 0.778 0.02 . 2 . . . . . . . . 5778 1 1023 . 1 1 110 110 LEU HD12 H 1 0.778 0.02 . 2 . . . . . . . . 5778 1 1024 . 1 1 110 110 LEU HD13 H 1 0.778 0.02 . 2 . . . . . . . . 5778 1 1025 . 1 1 110 110 LEU HD21 H 1 0.703 0.02 . 2 . . . . . . . . 5778 1 1026 . 1 1 110 110 LEU HD22 H 1 0.703 0.02 . 2 . . . . . . . . 5778 1 1027 . 1 1 110 110 LEU HD23 H 1 0.703 0.02 . 2 . . . . . . . . 5778 1 1028 . 1 1 111 111 LYS H H 1 7.301 0.02 . 1 . . . . . . . . 5778 1 1029 . 1 1 111 111 LYS N N 15 125.88 0.05 . 1 . . . . . . . . 5778 1 1030 . 1 1 111 111 LYS CA C 13 58.01 0.05 . 1 . . . . . . . . 5778 1 1031 . 1 1 111 111 LYS HA H 1 4.088 0.02 . 1 . . . . . . . . 5778 1 1032 . 1 1 111 111 LYS CB C 13 33.55 0.05 . 1 . . . . . . . . 5778 1 1033 . 1 1 111 111 LYS HB2 H 1 1.864 0.02 . 2 . . . . . . . . 5778 1 1034 . 1 1 111 111 LYS HB3 H 1 1.713 0.02 . 2 . . . . . . . . 5778 1 1035 . 1 1 111 111 LYS HG2 H 1 1.559 0.02 . 2 . . . . . . . . 5778 1 1036 . 1 1 111 111 LYS HG3 H 1 1.471 0.02 . 2 . . . . . . . . 5778 1 1037 . 1 1 111 111 LYS HD2 H 1 1.765 0.02 . 2 . . . . . . . . 5778 1 1038 . 1 1 111 111 LYS CE C 13 41.77 0.05 . 1 . . . . . . . . 5778 1 1039 . 1 1 111 111 LYS HE2 H 1 3.005 0.02 . 2 . . . . . . . . 5778 1 stop_ save_