data_18332 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18332 _Entry.Title ; E. coli Protein ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-03-16 _Entry.Accession_date 2012-03-16 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _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 Gerd Prehna . . . 18332 2 Guijin Zhang . . . 18332 3 Xiandi Gong . . . 18332 4 Marek Duszyk . . . 18332 5 Mark Okon . . . 18332 6 Lawrence McIntosh . P. . 18332 7 Joel Weiner . H. . 18332 8 Natalie Strynadka . CJ . 18332 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 18332 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'E. coli' . 18332 Secretion . 18332 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18332 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 239 18332 '15N chemical shifts' 67 18332 '1H chemical shifts' 462 18332 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 2 . . 2013-02-11 2012-03-16 update BMRB 'update entry citation' 18332 1 . . 2012-06-05 2010-03-16 original author 'original release' 18332 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2LQV 'BMRB Entry Tracking System' 18332 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18332 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22658749 _Citation.Full_citation . _Citation.Title 'A protein export pathway involving Escherichia coli porins.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Structure _Citation.Journal_name_full 'Structure (London, England : 1993)' _Citation.Journal_volume 20 _Citation.Journal_issue 7 _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 1154 _Citation.Page_last 1166 _Citation.Year 2012 _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 Gerd Prehna . . . 18332 1 2 Guijin Zhang . . . 18332 1 3 Xiandi Gong . . . 18332 1 4 Marek Duszyk . . . 18332 1 5 Mark Okon . . . 18332 1 6 Lawrence McIntosh . P. . 18332 1 7 Joel Weiner . H. . 18332 1 8 Natalie Strynadka . C.J. . 18332 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18332 _Assembly.ID 1 _Assembly.Name 'Escherichia coli Porins' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . 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 'Escherichia coli Porins' 1 $E_coli_protein A . yes native no no . . . 18332 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 'Escherichia coli Porins' 1 CYS 14 14 SG . 1 'Escherichia coli Porins' 1 CYS 87 87 SG 1 'Escherichia coli Porins' 35 CYS SG 1 'Escherichia coli Porins' 108 CYS SG 18332 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_E_coli_protein _Entity.Sf_category entity _Entity.Sf_framecode E_coli_protein _Entity.Entry_ID 18332 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name E_coli_protein _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; ANNETSKSVTFPKCEDLDAA GIAASVKRDYQQNRVARWAD DQKIVGQADPVAWVSLQDIQ GKDDKWSVPLTVRGKSADIH YQVSVDCKAGMAEYQRRLE ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 99 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state . _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 11054.386 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 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 2LQV . Yebf . . . . . 100.00 105 100.00 100.00 4.90e-65 . . . . 18332 1 2 no DBJ BAA15653 . "hypothetical protein [Escherichia coli str. K12 substr. W3110]" . . . . . 97.98 122 100.00 100.00 1.61e-63 . . . . 18332 1 3 no DBJ BAB35980 . "hypothetical protein [Escherichia coli O157:H7 str. Sakai]" . . . . . 97.98 122 98.97 98.97 1.57e-62 . . . . 18332 1 4 no DBJ BAG77546 . "conserved hypothetical protein [Escherichia coli SE11]" . . . . . 97.98 118 98.97 98.97 1.82e-62 . . . . 18332 1 5 no DBJ BAI25924 . "conserved predicted protein [Escherichia coli O26:H11 str. 11368]" . . . . . 97.98 118 98.97 98.97 1.82e-62 . . . . 18332 1 6 no DBJ BAI36219 . "conserved predicted protein [Escherichia coli O111:H- str. 11128]" . . . . . 97.98 118 98.97 98.97 1.82e-62 . . . . 18332 1 7 no EMBL CAP76337 . "Protein yebF [Escherichia coli LF82]" . . . . . 97.98 118 97.94 97.94 2.90e-61 . . . . 18332 1 8 no EMBL CAQ32323 . "predicted protein [Escherichia coli BL21(DE3)]" . . . . . 97.98 118 98.97 98.97 1.82e-62 . . . . 18332 1 9 no EMBL CAQ98773 . "conserved hypothetical protein [Escherichia coli IAI1]" . . . . . 97.98 122 98.97 98.97 1.57e-62 . . . . 18332 1 10 no EMBL CAR03207 . "conserved hypothetical protein [Escherichia coli S88]" . . . . . 97.98 122 98.97 98.97 1.57e-62 . . . . 18332 1 11 no EMBL CAR08244 . "conserved hypothetical protein [Escherichia coli ED1a]" . . . . . 97.98 122 98.97 98.97 1.57e-62 . . . . 18332 1 12 no GB AAA23859 . "putative [Escherichia coli]" . . . . . 97.98 122 100.00 100.00 1.61e-63 . . . . 18332 1 13 no GB AAC74917 . "extracellular Colicin M immunity family protein [Escherichia coli str. K-12 substr. MG1655]" . . . . . 97.98 118 100.00 100.00 2.45e-63 . . . . 18332 1 14 no GB AAG56837 . "orf, hypothetical protein [Escherichia coli O157:H7 str. EDL933]" . . . . . 97.98 122 98.97 98.97 1.40e-62 . . . . 18332 1 15 no GB AAN43416 . "conserved hypothetical protein [Shigella flexneri 2a str. 301]" . . . . . 97.98 118 97.94 97.94 1.51e-61 . . . . 18332 1 16 no GB AAN80718 . "Hypothetical lipoprotein yebF precursor [Escherichia coli CFT073]" . . . . . 97.98 122 98.97 98.97 1.57e-62 . . . . 18332 1 17 no REF NP_310584 . "hypothetical protein ECs2557 [Escherichia coli O157:H7 str. Sakai]" . . . . . 97.98 122 98.97 98.97 1.57e-62 . . . . 18332 1 18 no REF NP_416361 . "extracellular Colicin M immunity family protein [Escherichia coli str. K-12 substr. MG1655]" . . . . . 97.98 118 100.00 100.00 2.45e-63 . . . . 18332 1 19 no REF NP_707709 . "hypothetical protein SF1858 [Shigella flexneri 2a str. 301]" . . . . . 97.98 118 97.94 97.94 1.51e-61 . . . . 18332 1 20 no REF WP_000414411 . "hypothetical protein [Escherichia coli]" . . . . . 97.98 122 98.97 98.97 1.57e-62 . . . . 18332 1 21 no REF WP_000745667 . "hypothetical protein [Escherichia coli]" . . . . . 81.82 102 98.77 98.77 7.84e-50 . . . . 18332 1 22 no SP P33219 . "RecName: Full=Protein YebF; Flags: Precursor" . . . . . 97.98 118 100.00 100.00 2.45e-63 . . . . 18332 1 23 no SP Q322G8 . "RecName: Full=Protein YebF; Flags: Precursor" . . . . . 97.98 118 98.97 98.97 1.82e-62 . . . . 18332 1 24 no SP Q3Z2J8 . "RecName: Full=Protein YebF; Flags: Precursor" . . . . . 97.98 118 98.97 98.97 1.82e-62 . . . . 18332 1 25 no SP Q83KS1 . "RecName: Full=Protein YebF; Flags: Precursor" . . . . . 97.98 118 97.94 97.94 1.51e-61 . . . . 18332 1 26 no SP Q8CVZ5 . "RecName: Full=Protein YebF; Flags: Precursor" . . . . . 97.98 118 98.97 98.97 1.82e-62 . . . . 18332 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 22 ALA . 18332 1 2 23 ASN . 18332 1 3 24 ASN . 18332 1 4 25 GLU . 18332 1 5 26 THR . 18332 1 6 27 SER . 18332 1 7 28 LYS . 18332 1 8 29 SER . 18332 1 9 30 VAL . 18332 1 10 31 THR . 18332 1 11 32 PHE . 18332 1 12 33 PRO . 18332 1 13 34 LYS . 18332 1 14 35 CYS . 18332 1 15 36 GLU . 18332 1 16 37 ASP . 18332 1 17 38 LEU . 18332 1 18 39 ASP . 18332 1 19 40 ALA . 18332 1 20 41 ALA . 18332 1 21 42 GLY . 18332 1 22 43 ILE . 18332 1 23 44 ALA . 18332 1 24 45 ALA . 18332 1 25 46 SER . 18332 1 26 47 VAL . 18332 1 27 48 LYS . 18332 1 28 49 ARG . 18332 1 29 50 ASP . 18332 1 30 51 TYR . 18332 1 31 52 GLN . 18332 1 32 53 GLN . 18332 1 33 54 ASN . 18332 1 34 55 ARG . 18332 1 35 56 VAL . 18332 1 36 57 ALA . 18332 1 37 58 ARG . 18332 1 38 59 TRP . 18332 1 39 60 ALA . 18332 1 40 61 ASP . 18332 1 41 62 ASP . 18332 1 42 63 GLN . 18332 1 43 64 LYS . 18332 1 44 65 ILE . 18332 1 45 66 VAL . 18332 1 46 67 GLY . 18332 1 47 68 GLN . 18332 1 48 69 ALA . 18332 1 49 70 ASP . 18332 1 50 71 PRO . 18332 1 51 72 VAL . 18332 1 52 73 ALA . 18332 1 53 74 TRP . 18332 1 54 75 VAL . 18332 1 55 76 SER . 18332 1 56 77 LEU . 18332 1 57 78 GLN . 18332 1 58 79 ASP . 18332 1 59 80 ILE . 18332 1 60 81 GLN . 18332 1 61 82 GLY . 18332 1 62 83 LYS . 18332 1 63 84 ASP . 18332 1 64 85 ASP . 18332 1 65 86 LYS . 18332 1 66 87 TRP . 18332 1 67 88 SER . 18332 1 68 89 VAL . 18332 1 69 90 PRO . 18332 1 70 91 LEU . 18332 1 71 92 THR . 18332 1 72 93 VAL . 18332 1 73 94 ARG . 18332 1 74 95 GLY . 18332 1 75 96 LYS . 18332 1 76 97 SER . 18332 1 77 98 ALA . 18332 1 78 99 ASP . 18332 1 79 100 ILE . 18332 1 80 101 HIS . 18332 1 81 102 TYR . 18332 1 82 103 GLN . 18332 1 83 104 VAL . 18332 1 84 105 SER . 18332 1 85 106 VAL . 18332 1 86 107 ASP . 18332 1 87 108 CYS . 18332 1 88 109 LYS . 18332 1 89 110 ALA . 18332 1 90 111 GLY . 18332 1 91 112 MET . 18332 1 92 113 ALA . 18332 1 93 114 GLU . 18332 1 94 115 TYR . 18332 1 95 116 GLN . 18332 1 96 117 ARG . 18332 1 97 118 ARG . 18332 1 98 119 LEU . 18332 1 99 120 GLU . 18332 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ALA 1 1 18332 1 . ASN 2 2 18332 1 . ASN 3 3 18332 1 . GLU 4 4 18332 1 . THR 5 5 18332 1 . SER 6 6 18332 1 . LYS 7 7 18332 1 . SER 8 8 18332 1 . VAL 9 9 18332 1 . THR 10 10 18332 1 . PHE 11 11 18332 1 . PRO 12 12 18332 1 . LYS 13 13 18332 1 . CYS 14 14 18332 1 . GLU 15 15 18332 1 . ASP 16 16 18332 1 . LEU 17 17 18332 1 . ASP 18 18 18332 1 . ALA 19 19 18332 1 . ALA 20 20 18332 1 . GLY 21 21 18332 1 . ILE 22 22 18332 1 . ALA 23 23 18332 1 . ALA 24 24 18332 1 . SER 25 25 18332 1 . VAL 26 26 18332 1 . LYS 27 27 18332 1 . ARG 28 28 18332 1 . ASP 29 29 18332 1 . TYR 30 30 18332 1 . GLN 31 31 18332 1 . GLN 32 32 18332 1 . ASN 33 33 18332 1 . ARG 34 34 18332 1 . VAL 35 35 18332 1 . ALA 36 36 18332 1 . ARG 37 37 18332 1 . TRP 38 38 18332 1 . ALA 39 39 18332 1 . ASP 40 40 18332 1 . ASP 41 41 18332 1 . GLN 42 42 18332 1 . LYS 43 43 18332 1 . ILE 44 44 18332 1 . VAL 45 45 18332 1 . GLY 46 46 18332 1 . GLN 47 47 18332 1 . ALA 48 48 18332 1 . ASP 49 49 18332 1 . PRO 50 50 18332 1 . VAL 51 51 18332 1 . ALA 52 52 18332 1 . TRP 53 53 18332 1 . VAL 54 54 18332 1 . SER 55 55 18332 1 . LEU 56 56 18332 1 . GLN 57 57 18332 1 . ASP 58 58 18332 1 . ILE 59 59 18332 1 . GLN 60 60 18332 1 . GLY 61 61 18332 1 . LYS 62 62 18332 1 . ASP 63 63 18332 1 . ASP 64 64 18332 1 . LYS 65 65 18332 1 . TRP 66 66 18332 1 . SER 67 67 18332 1 . VAL 68 68 18332 1 . PRO 69 69 18332 1 . LEU 70 70 18332 1 . THR 71 71 18332 1 . VAL 72 72 18332 1 . ARG 73 73 18332 1 . GLY 74 74 18332 1 . LYS 75 75 18332 1 . SER 76 76 18332 1 . ALA 77 77 18332 1 . ASP 78 78 18332 1 . ILE 79 79 18332 1 . HIS 80 80 18332 1 . TYR 81 81 18332 1 . GLN 82 82 18332 1 . VAL 83 83 18332 1 . SER 84 84 18332 1 . VAL 85 85 18332 1 . ASP 86 86 18332 1 . CYS 87 87 18332 1 . LYS 88 88 18332 1 . ALA 89 89 18332 1 . GLY 90 90 18332 1 . MET 91 91 18332 1 . ALA 92 92 18332 1 . GLU 93 93 18332 1 . TYR 94 94 18332 1 . GLN 95 95 18332 1 . ARG 96 96 18332 1 . ARG 97 97 18332 1 . LEU 98 98 18332 1 . GLU 99 99 18332 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 18332 _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 $E_coli_protein . 562 organism . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 18332 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 18332 _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 $E_coli_protein . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pT7-5 . . . . . . 18332 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18332 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '50 mM HEPES pH 6.5 100 mM NaCl 0.1 mM TCEP 0.1 mM PMSF' _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _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 'E coli protein' '[U-100% 13C; U-100% 15N]' . . 1 $E_coli_protein . . . 0.5 1 mM . . . . 18332 1 2 HEPES 'natural abundance' . . . . . . 50 . . mM . . . . 18332 1 3 'sodium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 18332 1 4 TCEP 'natural abundance' . . . . . . 0.1 . . mM . . . . 18332 1 5 PMSF 'natural abundance' . . . . . . 0.1 . . mM . . . . 18332 1 6 H2O 'natural abundance' . . . . . . 95 . . % . . . . 18332 1 7 D2O 'natural abundance' . . . . . . 5 . . % . . . . 18332 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 18332 _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 'ionic strength' 0.1 . M 18332 1 pH 6.5 . pH 18332 1 pressure 1 . atm 18332 1 temperature 273 . K 18332 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 18332 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 18332 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 18332 1 stop_ save_ save_NMRDraw _Software.Sf_category software _Software.Sf_framecode NMRDraw _Software.Entry_ID 18332 _Software.ID 2 _Software.Name NMRDraw _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Johnson, One Moon Scientific' . . 18332 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 18332 2 processing 18332 2 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 18332 _Software.ID 3 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 18332 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18332 3 'peak picking' 18332 3 stop_ save_ save_TALOS _Software.Sf_category software _Software.Sf_framecode TALOS _Software.Entry_ID 18332 _Software.ID 4 _Software.Name TALOS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Cornilescu, Delaglio and Bax' . . 18332 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'geometry optimization' 18332 4 'structure solution' 18332 4 stop_ save_ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 18332 _Software.ID 5 _Software.Name CYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 18332 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 18332 5 'structure solution' 18332 5 stop_ save_ save_CNSSOLVE _Software.Sf_category software _Software.Sf_framecode CNSSOLVE _Software.Entry_ID 18332 _Software.ID 6 _Software.Name CNSSOLVE _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 18332 6 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 18332 6 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 18332 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details cryoprobe _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Unity _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 18332 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details cryoprobe _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Unity _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18332 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Varian Unity . 500 cryoprobe . . 18332 1 2 spectrometer_2 Varian Unity . 600 cryoprobe . . 18332 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 18332 _Experiment_list.ID 1 _Experiment_list.Details 'two data sets, one at 25C and one at 35C, all other parameters the same' 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 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 2 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 3 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 4 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 5 '3D HCACO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 6 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 7 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 8 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 9 CCC-TOCSY-NNH no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 10 HCC-TOCSY-NNH no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 11 (HB)CB(CGCD)HD-aromatic no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 12 HBGCBGCCBGCACONNH no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 13 CT-HSQC no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18332 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 18332 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 external indirect 0.251449530 . . . . . . . . . 18332 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 external direct 1.000000000 . . . . . . . . . 18332 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 external indirect 0.101329118 . . . . . . . . . 18332 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_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 18332 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 18332 1 2 '3D CBCA(CO)NH' . . . 18332 1 3 '3D HNCACB' . . . 18332 1 4 '3D HNCO' . . . 18332 1 5 '3D HCACO' . . . 18332 1 6 '3D HCCH-TOCSY' . . . 18332 1 7 '3D 1H-15N NOESY' . . . 18332 1 9 CCC-TOCSY-NNH . . . 18332 1 10 HCC-TOCSY-NNH . . . 18332 1 11 (HB)CB(CGCD)HD-aromatic . . . 18332 1 12 HBGCBGCCBGCACONNH . . . 18332 1 13 CT-HSQC . . . 18332 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 2 2 ASN HB2 H 1 2.862 0 . 2 . . . A 23 ASN HB2 . 18332 1 2 . 1 1 2 2 ASN HB3 H 1 2.862 0 . 2 . . . A 23 ASN HB3 . 18332 1 3 . 1 1 2 2 ASN CA C 13 53.576 0.003 . 1 . . . A 23 ASN CA . 18332 1 4 . 1 1 2 2 ASN CB C 13 38.913 0.028 . 1 . . . A 23 ASN CB . 18332 1 5 . 1 1 3 3 ASN H H 1 8.546 0 . 1 . . . A 24 ASN H . 18332 1 6 . 1 1 3 3 ASN HB2 H 1 3.195 0 . 2 . . . A 24 ASN HB2 . 18332 1 7 . 1 1 3 3 ASN HB3 H 1 2.846 0 . 2 . . . A 24 ASN HB3 . 18332 1 8 . 1 1 3 3 ASN C C 13 175.201 0.017 . 1 . . . A 24 ASN C . 18332 1 9 . 1 1 3 3 ASN CA C 13 53.609 0 . 1 . . . A 24 ASN CA . 18332 1 10 . 1 1 3 3 ASN CB C 13 38.885 0 . 1 . . . A 24 ASN CB . 18332 1 11 . 1 1 3 3 ASN N N 15 119.074 0 . 1 . . . A 24 ASN N . 18332 1 12 . 1 1 4 4 GLU H H 1 8.431 0 . 1 . . . A 25 GLU H . 18332 1 13 . 1 1 4 4 GLU HA H 1 4.512 0 . 1 . . . A 25 GLU HA . 18332 1 14 . 1 1 4 4 GLU HB2 H 1 2.134 0 . 2 . . . A 25 GLU HB2 . 18332 1 15 . 1 1 4 4 GLU HB3 H 1 2.046 0 . 2 . . . A 25 GLU HB3 . 18332 1 16 . 1 1 4 4 GLU HG2 H 1 2.315 0 . 2 . . . A 25 GLU HG2 . 18332 1 17 . 1 1 4 4 GLU HG3 H 1 2.315 0 . 2 . . . A 25 GLU HG3 . 18332 1 18 . 1 1 4 4 GLU C C 13 176.957 0.025 . 1 . . . A 25 GLU C . 18332 1 19 . 1 1 4 4 GLU CA C 13 57.107 0.046 . 1 . . . A 25 GLU CA . 18332 1 20 . 1 1 4 4 GLU CB C 13 30.502 0.03 . 1 . . . A 25 GLU CB . 18332 1 21 . 1 1 4 4 GLU CG C 13 36.534 0 . 1 . . . A 25 GLU CG . 18332 1 22 . 1 1 4 4 GLU N N 15 120.681 0 . 1 . . . A 25 GLU N . 18332 1 23 . 1 1 5 5 THR H H 1 8.198 0 . 1 . . . A 26 THR H . 18332 1 24 . 1 1 5 5 THR HA H 1 4.332 0 . 1 . . . A 26 THR HA . 18332 1 25 . 1 1 5 5 THR HG21 H 1 1.258 0 . 1 . . . A 26 THR HG21 . 18332 1 26 . 1 1 5 5 THR HG22 H 1 1.258 0 . 1 . . . A 26 THR HG22 . 18332 1 27 . 1 1 5 5 THR HG23 H 1 1.258 0 . 1 . . . A 26 THR HG23 . 18332 1 28 . 1 1 5 5 THR C C 13 174.268 0.015 . 1 . . . A 26 THR C . 18332 1 29 . 1 1 5 5 THR CA C 13 61.97 0 . 1 . . . A 26 THR CA . 18332 1 30 . 1 1 5 5 THR CB C 13 70.089 0 . 1 . . . A 26 THR CB . 18332 1 31 . 1 1 5 5 THR CG2 C 13 21.885 0 . 1 . . . A 26 THR CG2 . 18332 1 32 . 1 1 5 5 THR N N 15 113.493 0 . 1 . . . A 26 THR N . 18332 1 33 . 1 1 6 6 SER H H 1 8.18 0 . 1 . . . A 27 SER H . 18332 1 34 . 1 1 6 6 SER HA H 1 5.077 0.001 . 1 . . . A 27 SER HA . 18332 1 35 . 1 1 6 6 SER HB2 H 1 3.9 0 . 2 . . . A 27 SER HB2 . 18332 1 36 . 1 1 6 6 SER HB3 H 1 3.037 0 . 2 . . . A 27 SER HB3 . 18332 1 37 . 1 1 6 6 SER C C 13 174.087 0 . 1 . . . A 27 SER C . 18332 1 38 . 1 1 6 6 SER CA C 13 57.821 0 . 1 . . . A 27 SER CA . 18332 1 39 . 1 1 6 6 SER CB C 13 64.827 0 . 1 . . . A 27 SER CB . 18332 1 40 . 1 1 6 6 SER N N 15 117.653 0 . 1 . . . A 27 SER N . 18332 1 41 . 1 1 8 8 SER HA H 1 5.455 0.003 . 1 . . . A 29 SER HA . 18332 1 42 . 1 1 8 8 SER HB2 H 1 3.87 0 . 2 . . . A 29 SER HB2 . 18332 1 43 . 1 1 8 8 SER HB3 H 1 3.87 0 . 2 . . . A 29 SER HB3 . 18332 1 44 . 1 1 8 8 SER C C 13 174.725 0 . 1 . . . A 29 SER C . 18332 1 45 . 1 1 8 8 SER CA C 13 57.885 0.041 . 1 . . . A 29 SER CA . 18332 1 46 . 1 1 8 8 SER CB C 13 63.99 0 . 1 . . . A 29 SER CB . 18332 1 47 . 1 1 9 9 VAL H H 1 9.435 0 . 1 . . . A 30 VAL H . 18332 1 48 . 1 1 9 9 VAL HA H 1 5.002 0.012 . 1 . . . A 30 VAL HA . 18332 1 49 . 1 1 9 9 VAL HB H 1 2.504 0 . 1 . . . A 30 VAL HB . 18332 1 50 . 1 1 9 9 VAL HG11 H 1 1.028 0 . 2 . . . A 30 VAL HG11 . 18332 1 51 . 1 1 9 9 VAL HG12 H 1 1.028 0 . 2 . . . A 30 VAL HG12 . 18332 1 52 . 1 1 9 9 VAL HG13 H 1 1.028 0 . 2 . . . A 30 VAL HG13 . 18332 1 53 . 1 1 9 9 VAL HG21 H 1 1.141 0.008 . 2 . . . A 30 VAL HG21 . 18332 1 54 . 1 1 9 9 VAL HG22 H 1 1.141 0.008 . 2 . . . A 30 VAL HG22 . 18332 1 55 . 1 1 9 9 VAL HG23 H 1 1.141 0.008 . 2 . . . A 30 VAL HG23 . 18332 1 56 . 1 1 9 9 VAL C C 13 175.3 0.004 . 1 . . . A 30 VAL C . 18332 1 57 . 1 1 9 9 VAL CA C 13 58.828 0.055 . 1 . . . A 30 VAL CA . 18332 1 58 . 1 1 9 9 VAL CB C 13 36.058 0.002 . 1 . . . A 30 VAL CB . 18332 1 59 . 1 1 9 9 VAL CG1 C 13 21.93 0 . 2 . . . A 30 VAL CG1 . 18332 1 60 . 1 1 9 9 VAL CG2 C 13 19.539 0.082 . 2 . . . A 30 VAL CG2 . 18332 1 61 . 1 1 9 9 VAL N N 15 118.961 0.024 . 1 . . . A 30 VAL N . 18332 1 62 . 1 1 10 10 THR H H 1 8.284 0.001 . 1 . . . A 31 THR H . 18332 1 63 . 1 1 10 10 THR HA H 1 4.726 0.023 . 1 . . . A 31 THR HA . 18332 1 64 . 1 1 10 10 THR HB H 1 4.202 0.018 . 1 . . . A 31 THR HB . 18332 1 65 . 1 1 10 10 THR HG21 H 1 1.084 0.018 . 1 . . . A 31 THR HG21 . 18332 1 66 . 1 1 10 10 THR HG22 H 1 1.084 0.018 . 1 . . . A 31 THR HG22 . 18332 1 67 . 1 1 10 10 THR HG23 H 1 1.084 0.018 . 1 . . . A 31 THR HG23 . 18332 1 68 . 1 1 10 10 THR C C 13 173.102 0.026 . 1 . . . A 31 THR C . 18332 1 69 . 1 1 10 10 THR CA C 13 63.291 0.042 . 1 . . . A 31 THR CA . 18332 1 70 . 1 1 10 10 THR CB C 13 69.49 0.057 . 1 . . . A 31 THR CB . 18332 1 71 . 1 1 10 10 THR CG2 C 13 22.472 0.04 . 1 . . . A 31 THR CG2 . 18332 1 72 . 1 1 10 10 THR N N 15 116.623 0.013 . 1 . . . A 31 THR N . 18332 1 73 . 1 1 11 11 PHE H H 1 8.029 0.002 . 1 . . . A 32 PHE H . 18332 1 74 . 1 1 11 11 PHE HA H 1 4.167 0 . 1 . . . A 32 PHE HA . 18332 1 75 . 1 1 11 11 PHE HB2 H 1 2.794 0 . 2 . . . A 32 PHE HB2 . 18332 1 76 . 1 1 11 11 PHE HB3 H 1 2.562 0 . 2 . . . A 32 PHE HB3 . 18332 1 77 . 1 1 11 11 PHE HD1 H 1 7.125 0.066 . 3 . . . A 32 PHE HD1 . 18332 1 78 . 1 1 11 11 PHE HD2 H 1 7.202 0.02 . 3 . . . A 32 PHE HD2 . 18332 1 79 . 1 1 11 11 PHE HE2 H 1 6.765 0.007 . 3 . . . A 32 PHE HE2 . 18332 1 80 . 1 1 11 11 PHE HZ H 1 7.36 0 . 1 . . . A 32 PHE HZ . 18332 1 81 . 1 1 11 11 PHE C C 13 172.082 0 . 1 . . . A 32 PHE C . 18332 1 82 . 1 1 11 11 PHE CA C 13 55.403 0 . 1 . . . A 32 PHE CA . 18332 1 83 . 1 1 11 11 PHE CB C 13 39.318 0.032 . 1 . . . A 32 PHE CB . 18332 1 84 . 1 1 11 11 PHE CD1 C 13 133.06 0 . 3 . . . A 32 PHE CD1 . 18332 1 85 . 1 1 11 11 PHE CD2 C 13 132.858 0.084 . 3 . . . A 32 PHE CD2 . 18332 1 86 . 1 1 11 11 PHE CE2 C 13 129.053 0.068 . 3 . . . A 32 PHE CE2 . 18332 1 87 . 1 1 11 11 PHE N N 15 129.214 0.04 . 1 . . . A 32 PHE N . 18332 1 88 . 1 1 12 12 PRO HA H 1 4.13 0 . 1 . . . A 33 PRO HA . 18332 1 89 . 1 1 12 12 PRO HB2 H 1 2.239 0 . 2 . . . A 33 PRO HB2 . 18332 1 90 . 1 1 12 12 PRO HB3 H 1 1.768 0 . 2 . . . A 33 PRO HB3 . 18332 1 91 . 1 1 12 12 PRO HG2 H 1 1.543 0 . 2 . . . A 33 PRO HG2 . 18332 1 92 . 1 1 12 12 PRO HG3 H 1 1.336 0 . 2 . . . A 33 PRO HG3 . 18332 1 93 . 1 1 12 12 PRO HD2 H 1 3.108 0 . 2 . . . A 33 PRO HD2 . 18332 1 94 . 1 1 12 12 PRO HD3 H 1 3.108 0 . 2 . . . A 33 PRO HD3 . 18332 1 95 . 1 1 12 12 PRO CA C 13 62.885 0 . 1 . . . A 33 PRO CA . 18332 1 96 . 1 1 12 12 PRO CB C 13 31.435 0 . 1 . . . A 33 PRO CB . 18332 1 97 . 1 1 12 12 PRO CG C 13 27.409 0 . 1 . . . A 33 PRO CG . 18332 1 98 . 1 1 12 12 PRO CD C 13 50.101 0 . 1 . . . A 33 PRO CD . 18332 1 99 . 1 1 13 13 LYS H H 1 7.98 0.004 . 1 . . . A 34 LYS H . 18332 1 100 . 1 1 13 13 LYS HA H 1 4.172 0 . 1 . . . A 34 LYS HA . 18332 1 101 . 1 1 13 13 LYS HB2 H 1 2.207 0 . 2 . . . A 34 LYS HB2 . 18332 1 102 . 1 1 13 13 LYS HB3 H 1 1.751 0 . 2 . . . A 34 LYS HB3 . 18332 1 103 . 1 1 13 13 LYS HG2 H 1 1.425 0 . 2 . . . A 34 LYS HG2 . 18332 1 104 . 1 1 13 13 LYS HG3 H 1 1.679 0 . 2 . . . A 34 LYS HG3 . 18332 1 105 . 1 1 13 13 LYS HD2 H 1 1.754 0 . 2 . . . A 34 LYS HD2 . 18332 1 106 . 1 1 13 13 LYS HD3 H 1 1.754 0 . 2 . . . A 34 LYS HD3 . 18332 1 107 . 1 1 13 13 LYS HE2 H 1 3.056 0 . 2 . . . A 34 LYS HE2 . 18332 1 108 . 1 1 13 13 LYS HE3 H 1 3.056 0.001 . 2 . . . A 34 LYS HE3 . 18332 1 109 . 1 1 13 13 LYS CA C 13 58.877 0.004 . 1 . . . A 34 LYS CA . 18332 1 110 . 1 1 13 13 LYS CB C 13 31.852 0.036 . 1 . . . A 34 LYS CB . 18332 1 111 . 1 1 13 13 LYS CG C 13 25.607 0 . 1 . . . A 34 LYS CG . 18332 1 112 . 1 1 13 13 LYS CD C 13 29.371 0 . 1 . . . A 34 LYS CD . 18332 1 113 . 1 1 13 13 LYS CE C 13 42.047 0 . 1 . . . A 34 LYS CE . 18332 1 114 . 1 1 13 13 LYS N N 15 120.291 0.032 . 1 . . . A 34 LYS N . 18332 1 115 . 1 1 14 14 CYS H H 1 8.056 0.006 . 1 . . . A 35 CYS H . 18332 1 116 . 1 1 14 14 CYS HA H 1 5.081 0.016 . 1 . . . A 35 CYS HA . 18332 1 117 . 1 1 14 14 CYS HB2 H 1 3.925 0 . 2 . . . A 35 CYS HB2 . 18332 1 118 . 1 1 14 14 CYS HB3 H 1 3.075 0 . 2 . . . A 35 CYS HB3 . 18332 1 119 . 1 1 14 14 CYS CA C 13 54.045 0.002 . 1 . . . A 35 CYS CA . 18332 1 120 . 1 1 14 14 CYS CB C 13 40.904 0.031 . 1 . . . A 35 CYS CB . 18332 1 121 . 1 1 14 14 CYS N N 15 116.206 0.024 . 1 . . . A 35 CYS N . 18332 1 122 . 1 1 15 15 GLU H H 1 8.949 0.003 . 1 . . . A 36 GLU H . 18332 1 123 . 1 1 15 15 GLU HA H 1 4.017 0 . 1 . . . A 36 GLU HA . 18332 1 124 . 1 1 15 15 GLU HB2 H 1 2.123 0 . 2 . . . A 36 GLU HB2 . 18332 1 125 . 1 1 15 15 GLU HB3 H 1 2.002 0 . 2 . . . A 36 GLU HB3 . 18332 1 126 . 1 1 15 15 GLU HG2 H 1 2.221 0 . 2 . . . A 36 GLU HG2 . 18332 1 127 . 1 1 15 15 GLU HG3 H 1 2.221 0 . 2 . . . A 36 GLU HG3 . 18332 1 128 . 1 1 15 15 GLU CA C 13 59.377 0.006 . 1 . . . A 36 GLU CA . 18332 1 129 . 1 1 15 15 GLU CB C 13 29.852 0.03 . 1 . . . A 36 GLU CB . 18332 1 130 . 1 1 15 15 GLU CG C 13 37.052 0 . 1 . . . A 36 GLU CG . 18332 1 131 . 1 1 15 15 GLU N N 15 122.11 0.036 . 1 . . . A 36 GLU N . 18332 1 132 . 1 1 16 16 ASP H H 1 8.947 0.002 . 1 . . . A 37 ASP H . 18332 1 133 . 1 1 16 16 ASP HA H 1 4.586 0 . 1 . . . A 37 ASP HA . 18332 1 134 . 1 1 16 16 ASP HB2 H 1 2.831 0 . 2 . . . A 37 ASP HB2 . 18332 1 135 . 1 1 16 16 ASP HB3 H 1 2.831 0 . 2 . . . A 37 ASP HB3 . 18332 1 136 . 1 1 16 16 ASP CA C 13 54.947 0 . 1 . . . A 37 ASP CA . 18332 1 137 . 1 1 16 16 ASP CB C 13 40.051 0 . 1 . . . A 37 ASP CB . 18332 1 138 . 1 1 16 16 ASP N N 15 115.46 0.027 . 1 . . . A 37 ASP N . 18332 1 139 . 1 1 17 17 LEU H H 1 7.468 0.004 . 1 . . . A 38 LEU H . 18332 1 140 . 1 1 17 17 LEU HA H 1 4.55 0.002 . 1 . . . A 38 LEU HA . 18332 1 141 . 1 1 17 17 LEU HB2 H 1 1.782 0 . 2 . . . A 38 LEU HB2 . 18332 1 142 . 1 1 17 17 LEU HB3 H 1 1.479 0 . 2 . . . A 38 LEU HB3 . 18332 1 143 . 1 1 17 17 LEU HG H 1 1.653 0 . 1 . . . A 38 LEU HG . 18332 1 144 . 1 1 17 17 LEU HD11 H 1 0.766 0 . 2 . . . A 38 LEU HD11 . 18332 1 145 . 1 1 17 17 LEU HD12 H 1 0.766 0 . 2 . . . A 38 LEU HD12 . 18332 1 146 . 1 1 17 17 LEU HD13 H 1 0.766 0 . 2 . . . A 38 LEU HD13 . 18332 1 147 . 1 1 17 17 LEU HD21 H 1 0.766 0 . 2 . . . A 38 LEU HD21 . 18332 1 148 . 1 1 17 17 LEU HD22 H 1 0.766 0 . 2 . . . A 38 LEU HD22 . 18332 1 149 . 1 1 17 17 LEU HD23 H 1 0.766 0 . 2 . . . A 38 LEU HD23 . 18332 1 150 . 1 1 17 17 LEU CA C 13 54.8 0.1 . 1 . . . A 38 LEU CA . 18332 1 151 . 1 1 17 17 LEU CB C 13 43.291 0.022 . 1 . . . A 38 LEU CB . 18332 1 152 . 1 1 17 17 LEU CG C 13 26.593 0 . 1 . . . A 38 LEU CG . 18332 1 153 . 1 1 17 17 LEU CD1 C 13 25.597 0 . 2 . . . A 38 LEU CD1 . 18332 1 154 . 1 1 17 17 LEU CD2 C 13 22.78 0 . 2 . . . A 38 LEU CD2 . 18332 1 155 . 1 1 17 17 LEU N N 15 119.514 0.05 . 1 . . . A 38 LEU N . 18332 1 156 . 1 1 18 18 ASP H H 1 7.645 0.001 . 1 . . . A 39 ASP H . 18332 1 157 . 1 1 18 18 ASP HA H 1 4.831 0 . 1 . . . A 39 ASP HA . 18332 1 158 . 1 1 18 18 ASP HB2 H 1 3.192 0 . 2 . . . A 39 ASP HB2 . 18332 1 159 . 1 1 18 18 ASP HB3 H 1 2.846 0 . 2 . . . A 39 ASP HB3 . 18332 1 160 . 1 1 18 18 ASP CA C 13 51.261 0 . 1 . . . A 39 ASP CA . 18332 1 161 . 1 1 18 18 ASP CB C 13 41.863 0 . 1 . . . A 39 ASP CB . 18332 1 162 . 1 1 18 18 ASP N N 15 118.819 0.009 . 1 . . . A 39 ASP N . 18332 1 163 . 1 1 19 19 ALA H H 1 8.457 0.003 . 1 . . . A 40 ALA H . 18332 1 164 . 1 1 19 19 ALA HA H 1 3.202 0 . 1 . . . A 40 ALA HA . 18332 1 165 . 1 1 19 19 ALA HB1 H 1 1.43 0 . 1 . . . A 40 ALA HB1 . 18332 1 166 . 1 1 19 19 ALA HB2 H 1 1.43 0 . 1 . . . A 40 ALA HB2 . 18332 1 167 . 1 1 19 19 ALA HB3 H 1 1.43 0 . 1 . . . A 40 ALA HB3 . 18332 1 168 . 1 1 19 19 ALA CA C 13 55.69 0.002 . 1 . . . A 40 ALA CA . 18332 1 169 . 1 1 19 19 ALA CB C 13 18.317 0.041 . 1 . . . A 40 ALA CB . 18332 1 170 . 1 1 19 19 ALA N N 15 120.945 0.027 . 1 . . . A 40 ALA N . 18332 1 171 . 1 1 20 20 ALA H H 1 7.944 0.002 . 1 . . . A 41 ALA H . 18332 1 172 . 1 1 20 20 ALA HA H 1 3.921 0 . 1 . . . A 41 ALA HA . 18332 1 173 . 1 1 20 20 ALA HB1 H 1 1.417 0 . 1 . . . A 41 ALA HB1 . 18332 1 174 . 1 1 20 20 ALA HB2 H 1 1.417 0 . 1 . . . A 41 ALA HB2 . 18332 1 175 . 1 1 20 20 ALA HB3 H 1 1.417 0 . 1 . . . A 41 ALA HB3 . 18332 1 176 . 1 1 20 20 ALA CA C 13 55.042 0.069 . 1 . . . A 41 ALA CA . 18332 1 177 . 1 1 20 20 ALA CB C 13 17.773 0.115 . 1 . . . A 41 ALA CB . 18332 1 178 . 1 1 20 20 ALA N N 15 117.582 0.005 . 1 . . . A 41 ALA N . 18332 1 179 . 1 1 21 21 GLY H H 1 8.278 0.003 . 1 . . . A 42 GLY H . 18332 1 180 . 1 1 21 21 GLY HA2 H 1 3.933 0 . 2 . . . A 42 GLY HA2 . 18332 1 181 . 1 1 21 21 GLY HA3 H 1 3.768 0 . 2 . . . A 42 GLY HA3 . 18332 1 182 . 1 1 21 21 GLY CA C 13 47.069 0.02 . 1 . . . A 42 GLY CA . 18332 1 183 . 1 1 21 21 GLY N N 15 109.614 0.015 . 1 . . . A 42 GLY N . 18332 1 184 . 1 1 22 22 ILE H H 1 8.631 0.001 . 1 . . . A 43 ILE H . 18332 1 185 . 1 1 22 22 ILE HA H 1 3.731 0 . 1 . . . A 43 ILE HA . 18332 1 186 . 1 1 22 22 ILE HB H 1 1.188 0 . 1 . . . A 43 ILE HB . 18332 1 187 . 1 1 22 22 ILE HG12 H 1 0.647 0 . 2 . . . A 43 ILE HG12 . 18332 1 188 . 1 1 22 22 ILE HG13 H 1 -0.16 0 . 2 . . . A 43 ILE HG13 . 18332 1 189 . 1 1 22 22 ILE HG21 H 1 0.224 0 . 1 . . . A 43 ILE HG21 . 18332 1 190 . 1 1 22 22 ILE HG22 H 1 0.224 0 . 1 . . . A 43 ILE HG22 . 18332 1 191 . 1 1 22 22 ILE HG23 H 1 0.224 0 . 1 . . . A 43 ILE HG23 . 18332 1 192 . 1 1 22 22 ILE HD11 H 1 0.393 0 . 1 . . . A 43 ILE HD11 . 18332 1 193 . 1 1 22 22 ILE HD12 H 1 0.393 0 . 1 . . . A 43 ILE HD12 . 18332 1 194 . 1 1 22 22 ILE HD13 H 1 0.393 0 . 1 . . . A 43 ILE HD13 . 18332 1 195 . 1 1 22 22 ILE CA C 13 61.614 0.017 . 1 . . . A 43 ILE CA . 18332 1 196 . 1 1 22 22 ILE CB C 13 35.84 0.004 . 1 . . . A 43 ILE CB . 18332 1 197 . 1 1 22 22 ILE CG1 C 13 26.384 0 . 1 . . . A 43 ILE CG1 . 18332 1 198 . 1 1 22 22 ILE CG2 C 13 17.602 0 . 1 . . . A 43 ILE CG2 . 18332 1 199 . 1 1 22 22 ILE CD1 C 13 11.874 0 . 1 . . . A 43 ILE CD1 . 18332 1 200 . 1 1 22 22 ILE N N 15 126.734 0.017 . 1 . . . A 43 ILE N . 18332 1 201 . 1 1 23 23 ALA H H 1 8.347 0.002 . 1 . . . A 44 ALA H . 18332 1 202 . 1 1 23 23 ALA HA H 1 3.676 0 . 1 . . . A 44 ALA HA . 18332 1 203 . 1 1 23 23 ALA HB1 H 1 1.37 0 . 1 . . . A 44 ALA HB1 . 18332 1 204 . 1 1 23 23 ALA HB2 H 1 1.37 0 . 1 . . . A 44 ALA HB2 . 18332 1 205 . 1 1 23 23 ALA HB3 H 1 1.37 0 . 1 . . . A 44 ALA HB3 . 18332 1 206 . 1 1 23 23 ALA CA C 13 55.788 0.001 . 1 . . . A 44 ALA CA . 18332 1 207 . 1 1 23 23 ALA CB C 13 18.707 0.062 . 1 . . . A 44 ALA CB . 18332 1 208 . 1 1 23 23 ALA N N 15 123.871 0.021 . 1 . . . A 44 ALA N . 18332 1 209 . 1 1 24 24 ALA H H 1 7.593 0.002 . 1 . . . A 45 ALA H . 18332 1 210 . 1 1 24 24 ALA HA H 1 4.047 0 . 1 . . . A 45 ALA HA . 18332 1 211 . 1 1 24 24 ALA HB1 H 1 1.539 0 . 1 . . . A 45 ALA HB1 . 18332 1 212 . 1 1 24 24 ALA HB2 H 1 1.539 0 . 1 . . . A 45 ALA HB2 . 18332 1 213 . 1 1 24 24 ALA HB3 H 1 1.539 0 . 1 . . . A 45 ALA HB3 . 18332 1 214 . 1 1 24 24 ALA CA C 13 55.068 0.065 . 1 . . . A 45 ALA CA . 18332 1 215 . 1 1 24 24 ALA CB C 13 18.177 0.12 . 1 . . . A 45 ALA CB . 18332 1 216 . 1 1 24 24 ALA N N 15 117.86 0.016 . 1 . . . A 45 ALA N . 18332 1 217 . 1 1 25 25 SER H H 1 8.086 0.002 . 1 . . . A 46 SER H . 18332 1 218 . 1 1 25 25 SER HA H 1 4.103 0 . 1 . . . A 46 SER HA . 18332 1 219 . 1 1 25 25 SER HB2 H 1 3.919 0 . 2 . . . A 46 SER HB2 . 18332 1 220 . 1 1 25 25 SER HB3 H 1 3.919 0 . 2 . . . A 46 SER HB3 . 18332 1 221 . 1 1 25 25 SER CA C 13 62.044 0.081 . 1 . . . A 46 SER CA . 18332 1 222 . 1 1 25 25 SER CB C 13 63.061 0.027 . 1 . . . A 46 SER CB . 18332 1 223 . 1 1 25 25 SER N N 15 115.177 0.008 . 1 . . . A 46 SER N . 18332 1 224 . 1 1 26 26 VAL H H 1 8.733 0.013 . 1 . . . A 47 VAL H . 18332 1 225 . 1 1 26 26 VAL HA H 1 3.831 0 . 1 . . . A 47 VAL HA . 18332 1 226 . 1 1 26 26 VAL HB H 1 2.038 0 . 1 . . . A 47 VAL HB . 18332 1 227 . 1 1 26 26 VAL HG11 H 1 0.77 0 . 2 . . . A 47 VAL HG11 . 18332 1 228 . 1 1 26 26 VAL HG12 H 1 0.77 0 . 2 . . . A 47 VAL HG12 . 18332 1 229 . 1 1 26 26 VAL HG13 H 1 0.77 0 . 2 . . . A 47 VAL HG13 . 18332 1 230 . 1 1 26 26 VAL HG21 H 1 0.77 0 . 2 . . . A 47 VAL HG21 . 18332 1 231 . 1 1 26 26 VAL HG22 H 1 0.77 0 . 2 . . . A 47 VAL HG22 . 18332 1 232 . 1 1 26 26 VAL HG23 H 1 0.77 0 . 2 . . . A 47 VAL HG23 . 18332 1 233 . 1 1 26 26 VAL CA C 13 67.401 0 . 1 . . . A 47 VAL CA . 18332 1 234 . 1 1 26 26 VAL CB C 13 31.775 0 . 1 . . . A 47 VAL CB . 18332 1 235 . 1 1 26 26 VAL CG1 C 13 19.265 0 . 2 . . . A 47 VAL CG1 . 18332 1 236 . 1 1 26 26 VAL CG2 C 13 18.26 0 . 2 . . . A 47 VAL CG2 . 18332 1 237 . 1 1 26 26 VAL N N 15 123.762 0.013 . 1 . . . A 47 VAL N . 18332 1 238 . 1 1 27 27 LYS H H 1 7.931 0.007 . 1 . . . A 48 LYS H . 18332 1 239 . 1 1 27 27 LYS HA H 1 3.729 0.005 . 1 . . . A 48 LYS HA . 18332 1 240 . 1 1 27 27 LYS HB2 H 1 1.924 0 . 2 . . . A 48 LYS HB2 . 18332 1 241 . 1 1 27 27 LYS HB3 H 1 1.924 0 . 2 . . . A 48 LYS HB3 . 18332 1 242 . 1 1 27 27 LYS HG2 H 1 1.534 0 . 2 . . . A 48 LYS HG2 . 18332 1 243 . 1 1 27 27 LYS HG3 H 1 1.261 0 . 2 . . . A 48 LYS HG3 . 18332 1 244 . 1 1 27 27 LYS HD2 H 1 1.786 0 . 2 . . . A 48 LYS HD2 . 18332 1 245 . 1 1 27 27 LYS HD3 H 1 1.706 0 . 2 . . . A 48 LYS HD3 . 18332 1 246 . 1 1 27 27 LYS HE2 H 1 3.041 0 . 2 . . . A 48 LYS HE2 . 18332 1 247 . 1 1 27 27 LYS HE3 H 1 3.041 0 . 2 . . . A 48 LYS HE3 . 18332 1 248 . 1 1 27 27 LYS CA C 13 61.242 0.097 . 1 . . . A 48 LYS CA . 18332 1 249 . 1 1 27 27 LYS CB C 13 32.696 0.06 . 1 . . . A 48 LYS CB . 18332 1 250 . 1 1 27 27 LYS CG C 13 25.601 0 . 1 . . . A 48 LYS CG . 18332 1 251 . 1 1 27 27 LYS CD C 13 29.88 0 . 1 . . . A 48 LYS CD . 18332 1 252 . 1 1 27 27 LYS CE C 13 41.799 0 . 1 . . . A 48 LYS CE . 18332 1 253 . 1 1 27 27 LYS N N 15 118.412 0.048 . 1 . . . A 48 LYS N . 18332 1 254 . 1 1 28 28 ARG H H 1 7.941 0.008 . 1 . . . A 49 ARG H . 18332 1 255 . 1 1 28 28 ARG HA H 1 4.123 0 . 1 . . . A 49 ARG HA . 18332 1 256 . 1 1 28 28 ARG HB2 H 1 1.871 0 . 2 . . . A 49 ARG HB2 . 18332 1 257 . 1 1 28 28 ARG HB3 H 1 1.871 0 . 2 . . . A 49 ARG HB3 . 18332 1 258 . 1 1 28 28 ARG HG2 H 1 1.495 0 . 2 . . . A 49 ARG HG2 . 18332 1 259 . 1 1 28 28 ARG HG3 H 1 1.495 0 . 2 . . . A 49 ARG HG3 . 18332 1 260 . 1 1 28 28 ARG HD2 H 1 3.18 0 . 2 . . . A 49 ARG HD2 . 18332 1 261 . 1 1 28 28 ARG HD3 H 1 3.18 0 . 2 . . . A 49 ARG HD3 . 18332 1 262 . 1 1 28 28 ARG CA C 13 59.414 0.041 . 1 . . . A 49 ARG CA . 18332 1 263 . 1 1 28 28 ARG CB C 13 30.338 0.016 . 1 . . . A 49 ARG CB . 18332 1 264 . 1 1 28 28 ARG CG C 13 27.321 0 . 1 . . . A 49 ARG CG . 18332 1 265 . 1 1 28 28 ARG CD C 13 43.427 0 . 1 . . . A 49 ARG CD . 18332 1 266 . 1 1 28 28 ARG N N 15 116.894 0.086 . 1 . . . A 49 ARG N . 18332 1 267 . 1 1 29 29 ASP H H 1 8.25 0.003 . 1 . . . A 50 ASP H . 18332 1 268 . 1 1 29 29 ASP HA H 1 4.161 0 . 1 . . . A 50 ASP HA . 18332 1 269 . 1 1 29 29 ASP HB2 H 1 2.974 0 . 2 . . . A 50 ASP HB2 . 18332 1 270 . 1 1 29 29 ASP HB3 H 1 2.649 0 . 2 . . . A 50 ASP HB3 . 18332 1 271 . 1 1 29 29 ASP CA C 13 58.581 0.023 . 1 . . . A 50 ASP CA . 18332 1 272 . 1 1 29 29 ASP CB C 13 43.769 0.01 . 1 . . . A 50 ASP CB . 18332 1 273 . 1 1 29 29 ASP N N 15 119.598 0.03 . 1 . . . A 50 ASP N . 18332 1 274 . 1 1 30 30 TYR H H 1 8.68 0.005 . 1 . . . A 51 TYR H . 18332 1 275 . 1 1 30 30 TYR HB2 H 1 2.867 0 . 2 . . . A 51 TYR HB2 . 18332 1 276 . 1 1 30 30 TYR HB3 H 1 2.809 0 . 2 . . . A 51 TYR HB3 . 18332 1 277 . 1 1 30 30 TYR HD1 H 1 7.051 0.004 . 3 . . . A 51 TYR HD1 . 18332 1 278 . 1 1 30 30 TYR HD2 H 1 7.075 0.01 . 3 . . . A 51 TYR HD2 . 18332 1 279 . 1 1 30 30 TYR HE1 H 1 6.502 0.018 . 3 . . . A 51 TYR HE1 . 18332 1 280 . 1 1 30 30 TYR HE2 H 1 6.771 0 . 3 . . . A 51 TYR HE2 . 18332 1 281 . 1 1 30 30 TYR CA C 13 62.615 0 . 1 . . . A 51 TYR CA . 18332 1 282 . 1 1 30 30 TYR CB C 13 38.668 0.042 . 1 . . . A 51 TYR CB . 18332 1 283 . 1 1 30 30 TYR CD1 C 13 133.171 0 . 3 . . . A 51 TYR CD1 . 18332 1 284 . 1 1 30 30 TYR CD2 C 13 130.497 0.099 . 3 . . . A 51 TYR CD2 . 18332 1 285 . 1 1 30 30 TYR CE1 C 13 118.363 0.043 . 3 . . . A 51 TYR CE1 . 18332 1 286 . 1 1 30 30 TYR CE2 C 13 118.283 0 . 3 . . . A 51 TYR CE2 . 18332 1 287 . 1 1 30 30 TYR N N 15 119.757 0.038 . 1 . . . A 51 TYR N . 18332 1 288 . 1 1 31 31 GLN H H 1 8.287 0 . 1 . . . A 52 GLN H . 18332 1 289 . 1 1 31 31 GLN HA H 1 4.126 0 . 1 . . . A 52 GLN HA . 18332 1 290 . 1 1 31 31 GLN HB2 H 1 2.846 0 . 2 . . . A 52 GLN HB2 . 18332 1 291 . 1 1 31 31 GLN HB3 H 1 2.717 0 . 2 . . . A 52 GLN HB3 . 18332 1 292 . 1 1 31 31 GLN HG2 H 1 2.241 0 . 2 . . . A 52 GLN HG2 . 18332 1 293 . 1 1 31 31 GLN HG3 H 1 2.241 0 . 2 . . . A 52 GLN HG3 . 18332 1 294 . 1 1 31 31 GLN C C 13 178.235 0 . 1 . . . A 52 GLN C . 18332 1 295 . 1 1 31 31 GLN CA C 13 59.256 0 . 1 . . . A 52 GLN CA . 18332 1 296 . 1 1 31 31 GLN N N 15 115.572 0 . 1 . . . A 52 GLN N . 18332 1 297 . 1 1 32 32 GLN H H 1 8.848 0.007 . 1 . . . A 53 GLN H . 18332 1 298 . 1 1 32 32 GLN HB2 H 1 1.958 0 . 2 . . . A 53 GLN HB2 . 18332 1 299 . 1 1 32 32 GLN HB3 H 1 1.958 0 . 2 . . . A 53 GLN HB3 . 18332 1 300 . 1 1 32 32 GLN HG2 H 1 2.444 0 . 2 . . . A 53 GLN HG2 . 18332 1 301 . 1 1 32 32 GLN HG3 H 1 2.259 0 . 2 . . . A 53 GLN HG3 . 18332 1 302 . 1 1 32 32 GLN C C 13 177.224 0 . 1 . . . A 53 GLN C . 18332 1 303 . 1 1 32 32 GLN CA C 13 57.673 0 . 1 . . . A 53 GLN CA . 18332 1 304 . 1 1 32 32 GLN CB C 13 29.425 0.117 . 1 . . . A 53 GLN CB . 18332 1 305 . 1 1 32 32 GLN N N 15 114.416 0.037 . 1 . . . A 53 GLN N . 18332 1 306 . 1 1 45 45 VAL HA H 1 4.239 0 . 1 . . . A 66 VAL HA . 18332 1 307 . 1 1 45 45 VAL HB H 1 2.427 0 . 1 . . . A 66 VAL HB . 18332 1 308 . 1 1 45 45 VAL HG11 H 1 1.014 0 . 2 . . . A 66 VAL HG11 . 18332 1 309 . 1 1 45 45 VAL HG12 H 1 1.014 0 . 2 . . . A 66 VAL HG12 . 18332 1 310 . 1 1 45 45 VAL HG13 H 1 1.014 0 . 2 . . . A 66 VAL HG13 . 18332 1 311 . 1 1 45 45 VAL HG21 H 1 1.108 0 . 2 . . . A 66 VAL HG21 . 18332 1 312 . 1 1 45 45 VAL HG22 H 1 1.108 0 . 2 . . . A 66 VAL HG22 . 18332 1 313 . 1 1 45 45 VAL HG23 H 1 1.108 0 . 2 . . . A 66 VAL HG23 . 18332 1 314 . 1 1 45 45 VAL CA C 13 63.712 0 . 1 . . . A 66 VAL CA . 18332 1 315 . 1 1 45 45 VAL CB C 13 32.252 0 . 1 . . . A 66 VAL CB . 18332 1 316 . 1 1 45 45 VAL CG1 C 13 22.023 0 . 2 . . . A 66 VAL CG1 . 18332 1 317 . 1 1 45 45 VAL CG2 C 13 20.272 0 . 2 . . . A 66 VAL CG2 . 18332 1 318 . 1 1 46 46 GLY H H 1 8.027 0 . 1 . . . A 67 GLY H . 18332 1 319 . 1 1 46 46 GLY CA C 13 45.91 0 . 1 . . . A 67 GLY CA . 18332 1 320 . 1 1 46 46 GLY N N 15 108.542 0.002 . 1 . . . A 67 GLY N . 18332 1 321 . 1 1 50 50 PRO HA H 1 4.129 0 . 1 . . . A 71 PRO HA . 18332 1 322 . 1 1 50 50 PRO HB2 H 1 2.055 0 . 2 . . . A 71 PRO HB2 . 18332 1 323 . 1 1 50 50 PRO HB3 H 1 2.055 0 . 2 . . . A 71 PRO HB3 . 18332 1 324 . 1 1 50 50 PRO HG2 H 1 1.565 0 . 2 . . . A 71 PRO HG2 . 18332 1 325 . 1 1 50 50 PRO HG3 H 1 1.466 0 . 2 . . . A 71 PRO HG3 . 18332 1 326 . 1 1 50 50 PRO HD2 H 1 3.116 0 . 2 . . . A 71 PRO HD2 . 18332 1 327 . 1 1 50 50 PRO HD3 H 1 3.116 0 . 2 . . . A 71 PRO HD3 . 18332 1 328 . 1 1 50 50 PRO C C 13 176.009 0 . 1 . . . A 71 PRO C . 18332 1 329 . 1 1 50 50 PRO CA C 13 62.889 0 . 1 . . . A 71 PRO CA . 18332 1 330 . 1 1 50 50 PRO CB C 13 32.769 0 . 1 . . . A 71 PRO CB . 18332 1 331 . 1 1 50 50 PRO CG C 13 27.433 0 . 1 . . . A 71 PRO CG . 18332 1 332 . 1 1 51 51 VAL H H 1 8.537 0 . 1 . . . A 72 VAL H . 18332 1 333 . 1 1 51 51 VAL HA H 1 4.166 0 . 1 . . . A 72 VAL HA . 18332 1 334 . 1 1 51 51 VAL HB H 1 1.872 0 . 1 . . . A 72 VAL HB . 18332 1 335 . 1 1 51 51 VAL HG11 H 1 0.895 0 . 2 . . . A 72 VAL HG11 . 18332 1 336 . 1 1 51 51 VAL HG12 H 1 0.895 0 . 2 . . . A 72 VAL HG12 . 18332 1 337 . 1 1 51 51 VAL HG13 H 1 0.895 0 . 2 . . . A 72 VAL HG13 . 18332 1 338 . 1 1 51 51 VAL HG21 H 1 0.895 0 . 2 . . . A 72 VAL HG21 . 18332 1 339 . 1 1 51 51 VAL HG22 H 1 0.895 0 . 2 . . . A 72 VAL HG22 . 18332 1 340 . 1 1 51 51 VAL HG23 H 1 0.895 0 . 2 . . . A 72 VAL HG23 . 18332 1 341 . 1 1 51 51 VAL C C 13 174.364 0.008 . 1 . . . A 72 VAL C . 18332 1 342 . 1 1 51 51 VAL CA C 13 62.794 0.053 . 1 . . . A 72 VAL CA . 18332 1 343 . 1 1 51 51 VAL CB C 13 32.947 0.072 . 1 . . . A 72 VAL CB . 18332 1 344 . 1 1 51 51 VAL CG1 C 13 21.413 0 . 2 . . . A 72 VAL CG1 . 18332 1 345 . 1 1 51 51 VAL CG2 C 13 21.413 0 . 2 . . . A 72 VAL CG2 . 18332 1 346 . 1 1 51 51 VAL N N 15 123.129 0 . 1 . . . A 72 VAL N . 18332 1 347 . 1 1 52 52 ALA H H 1 8.272 0 . 1 . . . A 73 ALA H . 18332 1 348 . 1 1 52 52 ALA HA H 1 5.437 0 . 1 . . . A 73 ALA HA . 18332 1 349 . 1 1 52 52 ALA HB1 H 1 1.292 0 . 1 . . . A 73 ALA HB1 . 18332 1 350 . 1 1 52 52 ALA HB2 H 1 1.292 0 . 1 . . . A 73 ALA HB2 . 18332 1 351 . 1 1 52 52 ALA HB3 H 1 1.292 0 . 1 . . . A 73 ALA HB3 . 18332 1 352 . 1 1 52 52 ALA C C 13 176.104 0.01 . 1 . . . A 73 ALA C . 18332 1 353 . 1 1 52 52 ALA CA C 13 50.307 0.027 . 1 . . . A 73 ALA CA . 18332 1 354 . 1 1 52 52 ALA CB C 13 21.672 0.006 . 1 . . . A 73 ALA CB . 18332 1 355 . 1 1 52 52 ALA N N 15 128.689 0 . 1 . . . A 73 ALA N . 18332 1 356 . 1 1 53 53 TRP H H 1 9.301 0 . 1 . . . A 74 TRP H . 18332 1 357 . 1 1 53 53 TRP HA H 1 4.89 0 . 1 . . . A 74 TRP HA . 18332 1 358 . 1 1 53 53 TRP HB2 H 1 3.232 0 . 2 . . . A 74 TRP HB2 . 18332 1 359 . 1 1 53 53 TRP HB3 H 1 3.132 0 . 2 . . . A 74 TRP HB3 . 18332 1 360 . 1 1 53 53 TRP HD1 H 1 7.123 0.001 . 1 . . . A 74 TRP HD1 . 18332 1 361 . 1 1 53 53 TRP HE1 H 1 10.082 0.001 . 1 . . . A 74 TRP HE1 . 18332 1 362 . 1 1 53 53 TRP HE3 H 1 7.496 0.001 . 1 . . . A 74 TRP HE3 . 18332 1 363 . 1 1 53 53 TRP HH2 H 1 7.197 0 . 1 . . . A 74 TRP HH2 . 18332 1 364 . 1 1 53 53 TRP C C 13 174.515 0 . 1 . . . A 74 TRP C . 18332 1 365 . 1 1 53 53 TRP CA C 13 56.883 0 . 1 . . . A 74 TRP CA . 18332 1 366 . 1 1 53 53 TRP CB C 13 32.12 0.051 . 1 . . . A 74 TRP CB . 18332 1 367 . 1 1 53 53 TRP CD1 C 13 127.103 0.065 . 1 . . . A 74 TRP CD1 . 18332 1 368 . 1 1 53 53 TRP CE3 C 13 120.589 0.104 . 1 . . . A 74 TRP CE3 . 18332 1 369 . 1 1 53 53 TRP CH2 C 13 124.449 0 . 1 . . . A 74 TRP CH2 . 18332 1 370 . 1 1 53 53 TRP N N 15 122.55 0 . 1 . . . A 74 TRP N . 18332 1 371 . 1 1 53 53 TRP NE1 N 15 129.79 0 . 1 . . . A 74 TRP NE1 . 18332 1 372 . 1 1 54 54 VAL HA H 1 4.424 0 . 1 . . . A 75 VAL HA . 18332 1 373 . 1 1 54 54 VAL HB H 1 1.722 0 . 1 . . . A 75 VAL HB . 18332 1 374 . 1 1 54 54 VAL HG11 H 1 0.833 0 . 2 . . . A 75 VAL HG11 . 18332 1 375 . 1 1 54 54 VAL HG12 H 1 0.833 0 . 2 . . . A 75 VAL HG12 . 18332 1 376 . 1 1 54 54 VAL HG13 H 1 0.833 0 . 2 . . . A 75 VAL HG13 . 18332 1 377 . 1 1 54 54 VAL HG21 H 1 0.747 0 . 2 . . . A 75 VAL HG21 . 18332 1 378 . 1 1 54 54 VAL HG22 H 1 0.747 0 . 2 . . . A 75 VAL HG22 . 18332 1 379 . 1 1 54 54 VAL HG23 H 1 0.747 0 . 2 . . . A 75 VAL HG23 . 18332 1 380 . 1 1 54 54 VAL C C 13 174.906 0 . 1 . . . A 75 VAL C . 18332 1 381 . 1 1 54 54 VAL CA C 13 60.326 0 . 1 . . . A 75 VAL CA . 18332 1 382 . 1 1 54 54 VAL CB C 13 34.985 0 . 1 . . . A 75 VAL CB . 18332 1 383 . 1 1 54 54 VAL CG1 C 13 21.667 0 . 2 . . . A 75 VAL CG1 . 18332 1 384 . 1 1 54 54 VAL CG2 C 13 21.667 0 . 2 . . . A 75 VAL CG2 . 18332 1 385 . 1 1 55 55 SER H H 1 7.855 0.011 . 1 . . . A 76 SER H . 18332 1 386 . 1 1 55 55 SER HA H 1 4.427 0 . 1 . . . A 76 SER HA . 18332 1 387 . 1 1 55 55 SER HB2 H 1 4.005 0 . 2 . . . A 76 SER HB2 . 18332 1 388 . 1 1 55 55 SER HB3 H 1 3.849 0 . 2 . . . A 76 SER HB3 . 18332 1 389 . 1 1 55 55 SER CA C 13 55.979 0 . 1 . . . A 76 SER CA . 18332 1 390 . 1 1 55 55 SER CB C 13 62.223 0 . 1 . . . A 76 SER CB . 18332 1 391 . 1 1 55 55 SER N N 15 121.442 0.059 . 1 . . . A 76 SER N . 18332 1 392 . 1 1 56 56 LEU H H 1 8.256 0.002 . 1 . . . A 77 LEU H . 18332 1 393 . 1 1 56 56 LEU HA H 1 3.829 0 . 1 . . . A 77 LEU HA . 18332 1 394 . 1 1 56 56 LEU HB2 H 1 1.71 0 . 2 . . . A 77 LEU HB2 . 18332 1 395 . 1 1 56 56 LEU HB3 H 1 1.59 0 . 2 . . . A 77 LEU HB3 . 18332 1 396 . 1 1 56 56 LEU HD11 H 1 0.903 0 . 2 . . . A 77 LEU HD11 . 18332 1 397 . 1 1 56 56 LEU HD12 H 1 0.903 0 . 2 . . . A 77 LEU HD12 . 18332 1 398 . 1 1 56 56 LEU HD13 H 1 0.903 0 . 2 . . . A 77 LEU HD13 . 18332 1 399 . 1 1 56 56 LEU HD21 H 1 0.83 0 . 2 . . . A 77 LEU HD21 . 18332 1 400 . 1 1 56 56 LEU HD22 H 1 0.83 0 . 2 . . . A 77 LEU HD22 . 18332 1 401 . 1 1 56 56 LEU HD23 H 1 0.83 0 . 2 . . . A 77 LEU HD23 . 18332 1 402 . 1 1 56 56 LEU CA C 13 58.257 0.006 . 1 . . . A 77 LEU CA . 18332 1 403 . 1 1 56 56 LEU CB C 13 41.844 0.024 . 1 . . . A 77 LEU CB . 18332 1 404 . 1 1 56 56 LEU CG C 13 27.361 0 . 1 . . . A 77 LEU CG . 18332 1 405 . 1 1 56 56 LEU CD1 C 13 24.567 0 . 2 . . . A 77 LEU CD1 . 18332 1 406 . 1 1 56 56 LEU CD2 C 13 24.567 0 . 2 . . . A 77 LEU CD2 . 18332 1 407 . 1 1 56 56 LEU N N 15 129.932 0.013 . 1 . . . A 77 LEU N . 18332 1 408 . 1 1 57 57 GLN H H 1 8.614 0.005 . 1 . . . A 78 GLN H . 18332 1 409 . 1 1 57 57 GLN HA H 1 4.186 0 . 1 . . . A 78 GLN HA . 18332 1 410 . 1 1 57 57 GLN HB2 H 1 2.1 0 . 2 . . . A 78 GLN HB2 . 18332 1 411 . 1 1 57 57 GLN HB3 H 1 2.1 0 . 2 . . . A 78 GLN HB3 . 18332 1 412 . 1 1 57 57 GLN HG2 H 1 2.42 0 . 2 . . . A 78 GLN HG2 . 18332 1 413 . 1 1 57 57 GLN HG3 H 1 2.42 0 . 2 . . . A 78 GLN HG3 . 18332 1 414 . 1 1 57 57 GLN HE21 H 1 7.639 0 . 2 . . . A 78 GLN HE21 . 18332 1 415 . 1 1 57 57 GLN HE22 H 1 6.878 0 . 2 . . . A 78 GLN HE22 . 18332 1 416 . 1 1 57 57 GLN CA C 13 57.73 0.047 . 1 . . . A 78 GLN CA . 18332 1 417 . 1 1 57 57 GLN CB C 13 28.156 0.033 . 1 . . . A 78 GLN CB . 18332 1 418 . 1 1 57 57 GLN CG C 13 33.567 0 . 1 . . . A 78 GLN CG . 18332 1 419 . 1 1 57 57 GLN N N 15 115.179 0.03 . 1 . . . A 78 GLN N . 18332 1 420 . 1 1 57 57 GLN NE2 N 15 112.442 0.019 . 1 . . . A 78 GLN NE2 . 18332 1 421 . 1 1 58 58 ASP H H 1 7.486 0.002 . 1 . . . A 79 ASP H . 18332 1 422 . 1 1 58 58 ASP HA H 1 4.901 0 . 1 . . . A 79 ASP HA . 18332 1 423 . 1 1 58 58 ASP HB2 H 1 3.049 0 . 2 . . . A 79 ASP HB2 . 18332 1 424 . 1 1 58 58 ASP HB3 H 1 2.563 0 . 2 . . . A 79 ASP HB3 . 18332 1 425 . 1 1 58 58 ASP CA C 13 54.261 0.008 . 1 . . . A 79 ASP CA . 18332 1 426 . 1 1 58 58 ASP CB C 13 43.008 0.025 . 1 . . . A 79 ASP CB . 18332 1 427 . 1 1 58 58 ASP N N 15 116.803 0.013 . 1 . . . A 79 ASP N . 18332 1 428 . 1 1 59 59 ILE H H 1 7.278 0.003 . 1 . . . A 80 ILE H . 18332 1 429 . 1 1 59 59 ILE HA H 1 4.344 0 . 1 . . . A 80 ILE HA . 18332 1 430 . 1 1 59 59 ILE HB H 1 1.964 0 . 1 . . . A 80 ILE HB . 18332 1 431 . 1 1 59 59 ILE HG12 H 1 2.137 0 . 2 . . . A 80 ILE HG12 . 18332 1 432 . 1 1 59 59 ILE HG13 H 1 1.123 0 . 2 . . . A 80 ILE HG13 . 18332 1 433 . 1 1 59 59 ILE HG21 H 1 1.123 0 . 1 . . . A 80 ILE HG21 . 18332 1 434 . 1 1 59 59 ILE HG22 H 1 1.123 0 . 1 . . . A 80 ILE HG22 . 18332 1 435 . 1 1 59 59 ILE HG23 H 1 1.123 0 . 1 . . . A 80 ILE HG23 . 18332 1 436 . 1 1 59 59 ILE HD11 H 1 0.903 0 . 1 . . . A 80 ILE HD11 . 18332 1 437 . 1 1 59 59 ILE HD12 H 1 0.903 0 . 1 . . . A 80 ILE HD12 . 18332 1 438 . 1 1 59 59 ILE HD13 H 1 0.903 0 . 1 . . . A 80 ILE HD13 . 18332 1 439 . 1 1 59 59 ILE CA C 13 63.397 0.006 . 1 . . . A 80 ILE CA . 18332 1 440 . 1 1 59 59 ILE CB C 13 38.796 0.019 . 1 . . . A 80 ILE CB . 18332 1 441 . 1 1 59 59 ILE CG1 C 13 29.225 0 . 1 . . . A 80 ILE CG1 . 18332 1 442 . 1 1 59 59 ILE CG2 C 13 18.227 0 . 1 . . . A 80 ILE CG2 . 18332 1 443 . 1 1 59 59 ILE CD1 C 13 15.652 0 . 1 . . . A 80 ILE CD1 . 18332 1 444 . 1 1 59 59 ILE N N 15 121.887 0.036 . 1 . . . A 80 ILE N . 18332 1 445 . 1 1 60 60 GLN H H 1 8.318 0.005 . 1 . . . A 81 GLN H . 18332 1 446 . 1 1 60 60 GLN HA H 1 4.983 0 . 1 . . . A 81 GLN HA . 18332 1 447 . 1 1 60 60 GLN HB2 H 1 2.16 0 . 2 . . . A 81 GLN HB2 . 18332 1 448 . 1 1 60 60 GLN HB3 H 1 1.937 0 . 2 . . . A 81 GLN HB3 . 18332 1 449 . 1 1 60 60 GLN HG2 H 1 2.408 0 . 2 . . . A 81 GLN HG2 . 18332 1 450 . 1 1 60 60 GLN HG3 H 1 2.408 0 . 2 . . . A 81 GLN HG3 . 18332 1 451 . 1 1 60 60 GLN HE21 H 1 7.481 0 . 2 . . . A 81 GLN HE21 . 18332 1 452 . 1 1 60 60 GLN HE22 H 1 6.787 0 . 2 . . . A 81 GLN HE22 . 18332 1 453 . 1 1 60 60 GLN CA C 13 54.165 0.007 . 1 . . . A 81 GLN CA . 18332 1 454 . 1 1 60 60 GLN CB C 13 32.639 0.015 . 1 . . . A 81 GLN CB . 18332 1 455 . 1 1 60 60 GLN CG C 13 33.606 0 . 1 . . . A 81 GLN CG . 18332 1 456 . 1 1 60 60 GLN N N 15 126.14 0.017 . 1 . . . A 81 GLN N . 18332 1 457 . 1 1 60 60 GLN NE2 N 15 112.142 0.008 . 1 . . . A 81 GLN NE2 . 18332 1 458 . 1 1 61 61 GLY H H 1 8.484 0.004 . 1 . . . A 82 GLY H . 18332 1 459 . 1 1 61 61 GLY HA2 H 1 4.161 0 . 2 . . . A 82 GLY HA2 . 18332 1 460 . 1 1 61 61 GLY HA3 H 1 3.108 0 . 2 . . . A 82 GLY HA3 . 18332 1 461 . 1 1 61 61 GLY CA C 13 45.844 0.016 . 1 . . . A 82 GLY CA . 18332 1 462 . 1 1 61 61 GLY N N 15 111.215 0.016 . 1 . . . A 82 GLY N . 18332 1 463 . 1 1 62 62 LYS H H 1 7.669 0.004 . 1 . . . A 83 LYS H . 18332 1 464 . 1 1 62 62 LYS HA H 1 3.986 0.017 . 1 . . . A 83 LYS HA . 18332 1 465 . 1 1 62 62 LYS HB2 H 1 1.66 0 . 2 . . . A 83 LYS HB2 . 18332 1 466 . 1 1 62 62 LYS HB3 H 1 1.66 0 . 2 . . . A 83 LYS HB3 . 18332 1 467 . 1 1 62 62 LYS HG2 H 1 1.221 0 . 2 . . . A 83 LYS HG2 . 18332 1 468 . 1 1 62 62 LYS HG3 H 1 1.221 0 . 2 . . . A 83 LYS HG3 . 18332 1 469 . 1 1 62 62 LYS HD2 H 1 1.561 0 . 2 . . . A 83 LYS HD2 . 18332 1 470 . 1 1 62 62 LYS HD3 H 1 1.561 0 . 2 . . . A 83 LYS HD3 . 18332 1 471 . 1 1 62 62 LYS HE2 H 1 2.946 0 . 2 . . . A 83 LYS HE2 . 18332 1 472 . 1 1 62 62 LYS HE3 H 1 2.946 0 . 2 . . . A 83 LYS HE3 . 18332 1 473 . 1 1 62 62 LYS CA C 13 56.248 0.007 . 1 . . . A 83 LYS CA . 18332 1 474 . 1 1 62 62 LYS CB C 13 34.501 0.038 . 1 . . . A 83 LYS CB . 18332 1 475 . 1 1 62 62 LYS CG C 13 24.037 0 . 1 . . . A 83 LYS CG . 18332 1 476 . 1 1 62 62 LYS CD C 13 29.206 0.359 . 1 . . . A 83 LYS CD . 18332 1 477 . 1 1 62 62 LYS CE C 13 42.087 0 . 1 . . . A 83 LYS CE . 18332 1 478 . 1 1 62 62 LYS N N 15 119.467 0.011 . 1 . . . A 83 LYS N . 18332 1 479 . 1 1 63 63 ASP H H 1 9.052 0.006 . 1 . . . A 84 ASP H . 18332 1 480 . 1 1 63 63 ASP HA H 1 4.181 0 . 1 . . . A 84 ASP HA . 18332 1 481 . 1 1 63 63 ASP HB2 H 1 2.812 0 . 2 . . . A 84 ASP HB2 . 18332 1 482 . 1 1 63 63 ASP HB3 H 1 2.584 0 . 2 . . . A 84 ASP HB3 . 18332 1 483 . 1 1 63 63 ASP CA C 13 56.029 0.074 . 1 . . . A 84 ASP CA . 18332 1 484 . 1 1 63 63 ASP CB C 13 39.258 0.026 . 1 . . . A 84 ASP CB . 18332 1 485 . 1 1 63 63 ASP N N 15 124.24 0.011 . 1 . . . A 84 ASP N . 18332 1 486 . 1 1 64 64 ASP H H 1 8.261 0.001 . 1 . . . A 85 ASP H . 18332 1 487 . 1 1 64 64 ASP HA H 1 4.24 0 . 1 . . . A 85 ASP HA . 18332 1 488 . 1 1 64 64 ASP HB2 H 1 3.034 0 . 2 . . . A 85 ASP HB2 . 18332 1 489 . 1 1 64 64 ASP HB3 H 1 2.831 0 . 2 . . . A 85 ASP HB3 . 18332 1 490 . 1 1 64 64 ASP CA C 13 56.115 0.026 . 1 . . . A 85 ASP CA . 18332 1 491 . 1 1 64 64 ASP CB C 13 40.468 0 . 1 . . . A 85 ASP CB . 18332 1 492 . 1 1 64 64 ASP N N 15 110.367 0.005 . 1 . . . A 85 ASP N . 18332 1 493 . 1 1 65 65 LYS H H 1 7.46 0.004 . 1 . . . A 86 LYS H . 18332 1 494 . 1 1 65 65 LYS HA H 1 5.352 0 . 1 . . . A 86 LYS HA . 18332 1 495 . 1 1 65 65 LYS HB2 H 1 1.746 0 . 2 . . . A 86 LYS HB2 . 18332 1 496 . 1 1 65 65 LYS HB3 H 1 1.746 0 . 2 . . . A 86 LYS HB3 . 18332 1 497 . 1 1 65 65 LYS HG2 H 1 1.47 0 . 2 . . . A 86 LYS HG2 . 18332 1 498 . 1 1 65 65 LYS HG3 H 1 1.319 0 . 2 . . . A 86 LYS HG3 . 18332 1 499 . 1 1 65 65 LYS HD2 H 1 1.649 0 . 2 . . . A 86 LYS HD2 . 18332 1 500 . 1 1 65 65 LYS HD3 H 1 1.649 0 . 2 . . . A 86 LYS HD3 . 18332 1 501 . 1 1 65 65 LYS HE2 H 1 2.997 0 . 2 . . . A 86 LYS HE2 . 18332 1 502 . 1 1 65 65 LYS HE3 H 1 2.997 0 . 2 . . . A 86 LYS HE3 . 18332 1 503 . 1 1 65 65 LYS CA C 13 55.218 0.064 . 1 . . . A 86 LYS CA . 18332 1 504 . 1 1 65 65 LYS CB C 13 34.418 0.036 . 1 . . . A 86 LYS CB . 18332 1 505 . 1 1 65 65 LYS CG C 13 25.488 0 . 1 . . . A 86 LYS CG . 18332 1 506 . 1 1 65 65 LYS CD C 13 29.402 0 . 1 . . . A 86 LYS CD . 18332 1 507 . 1 1 65 65 LYS CE C 13 42.285 0 . 1 . . . A 86 LYS CE . 18332 1 508 . 1 1 65 65 LYS N N 15 119.587 0.014 . 1 . . . A 86 LYS N . 18332 1 509 . 1 1 66 66 TRP H H 1 8.903 0.006 . 1 . . . A 87 TRP H . 18332 1 510 . 1 1 66 66 TRP HA H 1 5.307 0 . 1 . . . A 87 TRP HA . 18332 1 511 . 1 1 66 66 TRP HB2 H 1 3.045 0 . 2 . . . A 87 TRP HB2 . 18332 1 512 . 1 1 66 66 TRP HB3 H 1 2.628 0 . 2 . . . A 87 TRP HB3 . 18332 1 513 . 1 1 66 66 TRP HD1 H 1 6.872 0.002 . 1 . . . A 87 TRP HD1 . 18332 1 514 . 1 1 66 66 TRP HE1 H 1 10.705 0.003 . 1 . . . A 87 TRP HE1 . 18332 1 515 . 1 1 66 66 TRP HE3 H 1 7.217 0.003 . 1 . . . A 87 TRP HE3 . 18332 1 516 . 1 1 66 66 TRP HZ2 H 1 7.484 0.007 . 1 . . . A 87 TRP HZ2 . 18332 1 517 . 1 1 66 66 TRP HZ3 H 1 6.912 0.012 . 1 . . . A 87 TRP HZ3 . 18332 1 518 . 1 1 66 66 TRP HH2 H 1 7.091 0.004 . 1 . . . A 87 TRP HH2 . 18332 1 519 . 1 1 66 66 TRP C C 13 175.839 0.012 . 1 . . . A 87 TRP C . 18332 1 520 . 1 1 66 66 TRP CA C 13 55.834 0.049 . 1 . . . A 87 TRP CA . 18332 1 521 . 1 1 66 66 TRP CB C 13 34.217 0.061 . 1 . . . A 87 TRP CB . 18332 1 522 . 1 1 66 66 TRP CD1 C 13 127.039 0.054 . 1 . . . A 87 TRP CD1 . 18332 1 523 . 1 1 66 66 TRP CE3 C 13 119.937 0.125 . 1 . . . A 87 TRP CE3 . 18332 1 524 . 1 1 66 66 TRP CZ2 C 13 114.62 0.04 . 1 . . . A 87 TRP CZ2 . 18332 1 525 . 1 1 66 66 TRP CZ3 C 13 120.499 0.156 . 1 . . . A 87 TRP CZ3 . 18332 1 526 . 1 1 66 66 TRP CH2 C 13 123.762 0.083 . 1 . . . A 87 TRP CH2 . 18332 1 527 . 1 1 66 66 TRP N N 15 121.49 0.039 . 1 . . . A 87 TRP N . 18332 1 528 . 1 1 66 66 TRP NE1 N 15 130.987 0 . 1 . . . A 87 TRP NE1 . 18332 1 529 . 1 1 67 67 SER H H 1 9.382 0.002 . 1 . . . A 88 SER H . 18332 1 530 . 1 1 67 67 SER HA H 1 5.236 0.026 . 1 . . . A 88 SER HA . 18332 1 531 . 1 1 67 67 SER HB2 H 1 3.878 0 . 2 . . . A 88 SER HB2 . 18332 1 532 . 1 1 67 67 SER HB3 H 1 3.732 0 . 2 . . . A 88 SER HB3 . 18332 1 533 . 1 1 67 67 SER CA C 13 57.197 0.009 . 1 . . . A 88 SER CA . 18332 1 534 . 1 1 67 67 SER CB C 13 63.945 0.005 . 1 . . . A 88 SER CB . 18332 1 535 . 1 1 67 67 SER N N 15 118.488 0.013 . 1 . . . A 88 SER N . 18332 1 536 . 1 1 68 68 VAL H H 1 9.36 0 . 1 . . . A 89 VAL H . 18332 1 537 . 1 1 68 68 VAL HA H 1 4.62 0 . 1 . . . A 89 VAL HA . 18332 1 538 . 1 1 68 68 VAL HB H 1 2.096 0 . 1 . . . A 89 VAL HB . 18332 1 539 . 1 1 68 68 VAL HG11 H 1 0.793 0 . 2 . . . A 89 VAL HG11 . 18332 1 540 . 1 1 68 68 VAL HG12 H 1 0.793 0 . 2 . . . A 89 VAL HG12 . 18332 1 541 . 1 1 68 68 VAL HG13 H 1 0.793 0 . 2 . . . A 89 VAL HG13 . 18332 1 542 . 1 1 68 68 VAL HG21 H 1 0.724 0 . 2 . . . A 89 VAL HG21 . 18332 1 543 . 1 1 68 68 VAL HG22 H 1 0.724 0 . 2 . . . A 89 VAL HG22 . 18332 1 544 . 1 1 68 68 VAL HG23 H 1 0.724 0 . 2 . . . A 89 VAL HG23 . 18332 1 545 . 1 1 68 68 VAL CA C 13 59.246 0 . 1 . . . A 89 VAL CA . 18332 1 546 . 1 1 68 68 VAL CB C 13 35.649 0 . 1 . . . A 89 VAL CB . 18332 1 547 . 1 1 68 68 VAL N N 15 127.693 0.012 . 1 . . . A 89 VAL N . 18332 1 548 . 1 1 69 69 PRO HA H 1 4.077 0 . 1 . . . A 90 PRO HA . 18332 1 549 . 1 1 69 69 PRO HB2 H 1 2.344 0 . 2 . . . A 90 PRO HB2 . 18332 1 550 . 1 1 69 69 PRO HB3 H 1 2.344 0 . 2 . . . A 90 PRO HB3 . 18332 1 551 . 1 1 69 69 PRO HG2 H 1 2.106 0 . 2 . . . A 90 PRO HG2 . 18332 1 552 . 1 1 69 69 PRO HG3 H 1 2.344 0 . 2 . . . A 90 PRO HG3 . 18332 1 553 . 1 1 69 69 PRO C C 13 174.726 0 . 1 . . . A 90 PRO C . 18332 1 554 . 1 1 69 69 PRO CA C 13 61.967 0 . 1 . . . A 90 PRO CA . 18332 1 555 . 1 1 69 69 PRO CB C 13 31.095 0 . 1 . . . A 90 PRO CB . 18332 1 556 . 1 1 69 69 PRO CG C 13 28.153 0 . 1 . . . A 90 PRO CG . 18332 1 557 . 1 1 70 70 LEU H H 1 8.767 0.015 . 1 . . . A 91 LEU H . 18332 1 558 . 1 1 70 70 LEU HA H 1 4.818 0 . 1 . . . A 91 LEU HA . 18332 1 559 . 1 1 70 70 LEU HB2 H 1 1.671 0 . 2 . . . A 91 LEU HB2 . 18332 1 560 . 1 1 70 70 LEU HB3 H 1 1.205 0 . 2 . . . A 91 LEU HB3 . 18332 1 561 . 1 1 70 70 LEU HG H 1 1.093 0 . 1 . . . A 91 LEU HG . 18332 1 562 . 1 1 70 70 LEU HD11 H 1 0.582 0 . 2 . . . A 91 LEU HD11 . 18332 1 563 . 1 1 70 70 LEU HD12 H 1 0.582 0 . 2 . . . A 91 LEU HD12 . 18332 1 564 . 1 1 70 70 LEU HD13 H 1 0.582 0 . 2 . . . A 91 LEU HD13 . 18332 1 565 . 1 1 70 70 LEU HD21 H 1 0.385 0 . 2 . . . A 91 LEU HD21 . 18332 1 566 . 1 1 70 70 LEU HD22 H 1 0.385 0 . 2 . . . A 91 LEU HD22 . 18332 1 567 . 1 1 70 70 LEU HD23 H 1 0.385 0 . 2 . . . A 91 LEU HD23 . 18332 1 568 . 1 1 70 70 LEU C C 13 173.906 0.043 . 1 . . . A 91 LEU C . 18332 1 569 . 1 1 70 70 LEU CA C 13 53.978 0 . 1 . . . A 91 LEU CA . 18332 1 570 . 1 1 70 70 LEU CB C 13 46.386 0 . 1 . . . A 91 LEU CB . 18332 1 571 . 1 1 70 70 LEU CG C 13 26.036 0 . 1 . . . A 91 LEU CG . 18332 1 572 . 1 1 70 70 LEU CD1 C 13 24.908 0.06 . 2 . . . A 91 LEU CD1 . 18332 1 573 . 1 1 70 70 LEU CD2 C 13 24.776 0 . 2 . . . A 91 LEU CD2 . 18332 1 574 . 1 1 70 70 LEU N N 15 126.522 0.083 . 1 . . . A 91 LEU N . 18332 1 575 . 1 1 71 71 THR H H 1 9.034 0 . 1 . . . A 92 THR H . 18332 1 576 . 1 1 71 71 THR HA H 1 5.105 0 . 1 . . . A 92 THR HA . 18332 1 577 . 1 1 71 71 THR HB H 1 5.105 0 . 1 . . . A 92 THR HB . 18332 1 578 . 1 1 72 72 VAL HA H 1 4.532 0 . 1 . . . A 93 VAL HA . 18332 1 579 . 1 1 72 72 VAL HB H 1 1.972 0 . 1 . . . A 93 VAL HB . 18332 1 580 . 1 1 72 72 VAL HG11 H 1 1.006 0 . 2 . . . A 93 VAL HG11 . 18332 1 581 . 1 1 72 72 VAL HG12 H 1 1.006 0 . 2 . . . A 93 VAL HG12 . 18332 1 582 . 1 1 72 72 VAL HG13 H 1 1.006 0 . 2 . . . A 93 VAL HG13 . 18332 1 583 . 1 1 72 72 VAL HG21 H 1 0.546 0 . 2 . . . A 93 VAL HG21 . 18332 1 584 . 1 1 72 72 VAL HG22 H 1 0.546 0 . 2 . . . A 93 VAL HG22 . 18332 1 585 . 1 1 72 72 VAL HG23 H 1 0.546 0 . 2 . . . A 93 VAL HG23 . 18332 1 586 . 1 1 72 72 VAL CA C 13 61.333 0 . 1 . . . A 93 VAL CA . 18332 1 587 . 1 1 72 72 VAL CB C 13 33.826 0 . 1 . . . A 93 VAL CB . 18332 1 588 . 1 1 72 72 VAL CG1 C 13 21.891 0 . 2 . . . A 93 VAL CG1 . 18332 1 589 . 1 1 72 72 VAL CG2 C 13 19.445 0 . 2 . . . A 93 VAL CG2 . 18332 1 590 . 1 1 73 73 ARG H H 1 8.833 0.004 . 1 . . . A 94 ARG H . 18332 1 591 . 1 1 73 73 ARG HA H 1 4.9 0 . 1 . . . A 94 ARG HA . 18332 1 592 . 1 1 73 73 ARG HB2 H 1 1.929 0 . 2 . . . A 94 ARG HB2 . 18332 1 593 . 1 1 73 73 ARG HB3 H 1 1.929 0 . 2 . . . A 94 ARG HB3 . 18332 1 594 . 1 1 73 73 ARG HG2 H 1 1.71 0 . 2 . . . A 94 ARG HG2 . 18332 1 595 . 1 1 73 73 ARG HG3 H 1 1.58 0 . 2 . . . A 94 ARG HG3 . 18332 1 596 . 1 1 73 73 ARG HD2 H 1 3.051 0 . 2 . . . A 94 ARG HD2 . 18332 1 597 . 1 1 73 73 ARG HD3 H 1 3.051 0 . 2 . . . A 94 ARG HD3 . 18332 1 598 . 1 1 73 73 ARG CA C 13 55.931 0.037 . 1 . . . A 94 ARG CA . 18332 1 599 . 1 1 73 73 ARG CB C 13 31.104 0.064 . 1 . . . A 94 ARG CB . 18332 1 600 . 1 1 73 73 ARG CG C 13 26.836 0 . 1 . . . A 94 ARG CG . 18332 1 601 . 1 1 73 73 ARG CD C 13 43.386 0 . 1 . . . A 94 ARG CD . 18332 1 602 . 1 1 73 73 ARG N N 15 126.565 0.021 . 1 . . . A 94 ARG N . 18332 1 603 . 1 1 74 74 GLY H H 1 8.562 0.004 . 1 . . . A 95 GLY H . 18332 1 604 . 1 1 74 74 GLY HA2 H 1 4.859 0.007 . 2 . . . A 95 GLY HA2 . 18332 1 605 . 1 1 74 74 GLY HA3 H 1 4.12 0 . 2 . . . A 95 GLY HA3 . 18332 1 606 . 1 1 74 74 GLY CA C 13 44.454 0.054 . 1 . . . A 95 GLY CA . 18332 1 607 . 1 1 74 74 GLY N N 15 112.938 0.11 . 1 . . . A 95 GLY N . 18332 1 608 . 1 1 75 75 LYS H H 1 8.074 0.006 . 1 . . . A 96 LYS H . 18332 1 609 . 1 1 75 75 LYS HA H 1 4.243 0 . 1 . . . A 96 LYS HA . 18332 1 610 . 1 1 75 75 LYS HB2 H 1 1.936 0 . 2 . . . A 96 LYS HB2 . 18332 1 611 . 1 1 75 75 LYS HB3 H 1 1.936 0 . 2 . . . A 96 LYS HB3 . 18332 1 612 . 1 1 75 75 LYS HG2 H 1 1.539 0 . 2 . . . A 96 LYS HG2 . 18332 1 613 . 1 1 75 75 LYS HG3 H 1 1.539 0 . 2 . . . A 96 LYS HG3 . 18332 1 614 . 1 1 75 75 LYS HD2 H 1 1.756 0 . 2 . . . A 96 LYS HD2 . 18332 1 615 . 1 1 75 75 LYS HD3 H 1 1.756 0 . 2 . . . A 96 LYS HD3 . 18332 1 616 . 1 1 75 75 LYS HE2 H 1 3.044 0 . 2 . . . A 96 LYS HE2 . 18332 1 617 . 1 1 75 75 LYS HE3 H 1 3.044 0 . 2 . . . A 96 LYS HE3 . 18332 1 618 . 1 1 75 75 LYS CA C 13 59.295 0.022 . 1 . . . A 96 LYS CA . 18332 1 619 . 1 1 75 75 LYS CB C 13 32.597 0.057 . 1 . . . A 96 LYS CB . 18332 1 620 . 1 1 75 75 LYS CG C 13 24.654 0 . 1 . . . A 96 LYS CG . 18332 1 621 . 1 1 75 75 LYS CD C 13 29.202 0 . 1 . . . A 96 LYS CD . 18332 1 622 . 1 1 75 75 LYS N N 15 119.229 0.015 . 1 . . . A 96 LYS N . 18332 1 623 . 1 1 76 76 SER H H 1 8.828 0.01 . 1 . . . A 97 SER H . 18332 1 624 . 1 1 76 76 SER HA H 1 4.625 0 . 1 . . . A 97 SER HA . 18332 1 625 . 1 1 76 76 SER HB2 H 1 3.865 0 . 2 . . . A 97 SER HB2 . 18332 1 626 . 1 1 76 76 SER HB3 H 1 3.865 0 . 2 . . . A 97 SER HB3 . 18332 1 627 . 1 1 76 76 SER CA C 13 58.593 0.1 . 1 . . . A 97 SER CA . 18332 1 628 . 1 1 76 76 SER CB C 13 64.106 0.025 . 1 . . . A 97 SER CB . 18332 1 629 . 1 1 76 76 SER N N 15 111.88 0.024 . 1 . . . A 97 SER N . 18332 1 630 . 1 1 77 77 ALA H H 1 7.341 0.002 . 1 . . . A 98 ALA H . 18332 1 631 . 1 1 77 77 ALA HA H 1 4.121 0 . 1 . . . A 98 ALA HA . 18332 1 632 . 1 1 77 77 ALA HB1 H 1 0.967 0 . 1 . . . A 98 ALA HB1 . 18332 1 633 . 1 1 77 77 ALA HB2 H 1 0.967 0 . 1 . . . A 98 ALA HB2 . 18332 1 634 . 1 1 77 77 ALA HB3 H 1 0.967 0 . 1 . . . A 98 ALA HB3 . 18332 1 635 . 1 1 77 77 ALA CA C 13 51.218 0.006 . 1 . . . A 98 ALA CA . 18332 1 636 . 1 1 77 77 ALA CB C 13 21.866 0.053 . 1 . . . A 98 ALA CB . 18332 1 637 . 1 1 77 77 ALA N N 15 122.995 0.013 . 1 . . . A 98 ALA N . 18332 1 638 . 1 1 78 78 ASP H H 1 8.206 0.003 . 1 . . . A 99 ASP H . 18332 1 639 . 1 1 78 78 ASP HA H 1 5.435 0 . 1 . . . A 99 ASP HA . 18332 1 640 . 1 1 78 78 ASP HB2 H 1 2.483 0 . 2 . . . A 99 ASP HB2 . 18332 1 641 . 1 1 78 78 ASP HB3 H 1 2.483 0 . 2 . . . A 99 ASP HB3 . 18332 1 642 . 1 1 78 78 ASP CA C 13 52.144 0 . 1 . . . A 99 ASP CA . 18332 1 643 . 1 1 78 78 ASP CB C 13 43.392 0 . 1 . . . A 99 ASP CB . 18332 1 644 . 1 1 78 78 ASP N N 15 115.649 0.006 . 1 . . . A 99 ASP N . 18332 1 645 . 1 1 79 79 ILE H H 1 9.039 0 . 1 . . . A 100 ILE H . 18332 1 646 . 1 1 79 79 ILE HA H 1 4.177 0 . 1 . . . A 100 ILE HA . 18332 1 647 . 1 1 79 79 ILE HB H 1 1.847 0 . 1 . . . A 100 ILE HB . 18332 1 648 . 1 1 79 79 ILE HG12 H 1 1.438 0 . 2 . . . A 100 ILE HG12 . 18332 1 649 . 1 1 79 79 ILE HG13 H 1 1.151 0 . 2 . . . A 100 ILE HG13 . 18332 1 650 . 1 1 79 79 ILE HG21 H 1 0.861 0 . 1 . . . A 100 ILE HG21 . 18332 1 651 . 1 1 79 79 ILE HG22 H 1 0.861 0 . 1 . . . A 100 ILE HG22 . 18332 1 652 . 1 1 79 79 ILE HG23 H 1 0.861 0 . 1 . . . A 100 ILE HG23 . 18332 1 653 . 1 1 79 79 ILE HD11 H 1 0.861 0 . 1 . . . A 100 ILE HD11 . 18332 1 654 . 1 1 79 79 ILE HD12 H 1 0.861 0 . 1 . . . A 100 ILE HD12 . 18332 1 655 . 1 1 79 79 ILE HD13 H 1 0.861 0 . 1 . . . A 100 ILE HD13 . 18332 1 656 . 1 1 79 79 ILE CA C 13 60.56 0 . 1 . . . A 100 ILE CA . 18332 1 657 . 1 1 79 79 ILE CB C 13 41.095 0 . 1 . . . A 100 ILE CB . 18332 1 658 . 1 1 79 79 ILE CG1 C 13 27.478 0.016 . 1 . . . A 100 ILE CG1 . 18332 1 659 . 1 1 79 79 ILE CG2 C 13 17.511 0 . 1 . . . A 100 ILE CG2 . 18332 1 660 . 1 1 79 79 ILE CD1 C 13 12.991 0 . 1 . . . A 100 ILE CD1 . 18332 1 661 . 1 1 79 79 ILE N N 15 120.032 0 . 1 . . . A 100 ILE N . 18332 1 662 . 1 1 80 80 HIS HD2 H 1 6.951 0 . 1 . . . A 101 HIS HD2 . 18332 1 663 . 1 1 80 80 HIS HE1 H 1 8.187 0 . 1 . . . A 101 HIS HE1 . 18332 1 664 . 1 1 80 80 HIS CD2 C 13 118.602 0 . 1 . . . A 101 HIS CD2 . 18332 1 665 . 1 1 80 80 HIS CE1 C 13 136.46 0 . 1 . . . A 101 HIS CE1 . 18332 1 666 . 1 1 83 83 VAL HA H 1 4.779 0 . 1 . . . A 104 VAL HA . 18332 1 667 . 1 1 83 83 VAL HB H 1 1.907 0 . 1 . . . A 104 VAL HB . 18332 1 668 . 1 1 83 83 VAL HG11 H 1 0.425 0 . 2 . . . A 104 VAL HG11 . 18332 1 669 . 1 1 83 83 VAL HG12 H 1 0.425 0 . 2 . . . A 104 VAL HG12 . 18332 1 670 . 1 1 83 83 VAL HG13 H 1 0.425 0 . 2 . . . A 104 VAL HG13 . 18332 1 671 . 1 1 83 83 VAL HG21 H 1 -0.074 0 . 2 . . . A 104 VAL HG21 . 18332 1 672 . 1 1 83 83 VAL HG22 H 1 -0.074 0 . 2 . . . A 104 VAL HG22 . 18332 1 673 . 1 1 83 83 VAL HG23 H 1 -0.074 0 . 2 . . . A 104 VAL HG23 . 18332 1 674 . 1 1 83 83 VAL CA C 13 61.192 0 . 1 . . . A 104 VAL CA . 18332 1 675 . 1 1 83 83 VAL CB C 13 31.896 0 . 1 . . . A 104 VAL CB . 18332 1 676 . 1 1 83 83 VAL CG1 C 13 22.499 0 . 2 . . . A 104 VAL CG1 . 18332 1 677 . 1 1 83 83 VAL CG2 C 13 20.132 0 . 2 . . . A 104 VAL CG2 . 18332 1 678 . 1 1 84 84 SER H H 1 8.973 0.004 . 1 . . . A 105 SER H . 18332 1 679 . 1 1 84 84 SER HA H 1 5.393 0 . 1 . . . A 105 SER HA . 18332 1 680 . 1 1 84 84 SER HB2 H 1 3.887 0 . 2 . . . A 105 SER HB2 . 18332 1 681 . 1 1 84 84 SER HB3 H 1 3.887 0 . 2 . . . A 105 SER HB3 . 18332 1 682 . 1 1 84 84 SER CA C 13 56.419 0.029 . 1 . . . A 105 SER CA . 18332 1 683 . 1 1 84 84 SER CB C 13 63.496 0.009 . 1 . . . A 105 SER CB . 18332 1 684 . 1 1 84 84 SER N N 15 124.376 0.033 . 1 . . . A 105 SER N . 18332 1 685 . 1 1 85 85 VAL H H 1 9.254 0.001 . 1 . . . A 106 VAL H . 18332 1 686 . 1 1 85 85 VAL HA H 1 4.09 0 . 1 . . . A 106 VAL HA . 18332 1 687 . 1 1 85 85 VAL HB H 1 1.78 0 . 1 . . . A 106 VAL HB . 18332 1 688 . 1 1 85 85 VAL HG11 H 1 0.501 0 . 2 . . . A 106 VAL HG11 . 18332 1 689 . 1 1 85 85 VAL HG12 H 1 0.501 0 . 2 . . . A 106 VAL HG12 . 18332 1 690 . 1 1 85 85 VAL HG13 H 1 0.501 0 . 2 . . . A 106 VAL HG13 . 18332 1 691 . 1 1 85 85 VAL HG21 H 1 0.155 0 . 2 . . . A 106 VAL HG21 . 18332 1 692 . 1 1 85 85 VAL HG22 H 1 0.155 0 . 2 . . . A 106 VAL HG22 . 18332 1 693 . 1 1 85 85 VAL HG23 H 1 0.155 0 . 2 . . . A 106 VAL HG23 . 18332 1 694 . 1 1 85 85 VAL CA C 13 61.843 0.012 . 1 . . . A 106 VAL CA . 18332 1 695 . 1 1 85 85 VAL CB C 13 34.995 0.018 . 1 . . . A 106 VAL CB . 18332 1 696 . 1 1 85 85 VAL CG1 C 13 22.874 0 . 2 . . . A 106 VAL CG1 . 18332 1 697 . 1 1 85 85 VAL CG2 C 13 20.563 0 . 2 . . . A 106 VAL CG2 . 18332 1 698 . 1 1 85 85 VAL N N 15 127.349 0.013 . 1 . . . A 106 VAL N . 18332 1 699 . 1 1 86 86 ASP H H 1 8.877 0.001 . 1 . . . A 107 ASP H . 18332 1 700 . 1 1 86 86 ASP HA H 1 5.149 0 . 1 . . . A 107 ASP HA . 18332 1 701 . 1 1 86 86 ASP HB2 H 1 3.031 0 . 2 . . . A 107 ASP HB2 . 18332 1 702 . 1 1 86 86 ASP HB3 H 1 2.538 0 . 2 . . . A 107 ASP HB3 . 18332 1 703 . 1 1 86 86 ASP CA C 13 52.528 0.006 . 1 . . . A 107 ASP CA . 18332 1 704 . 1 1 86 86 ASP CB C 13 41.694 0.03 . 1 . . . A 107 ASP CB . 18332 1 705 . 1 1 86 86 ASP N N 15 126.522 0.018 . 1 . . . A 107 ASP N . 18332 1 706 . 1 1 87 87 CYS H H 1 8.989 0.001 . 1 . . . A 108 CYS H . 18332 1 707 . 1 1 87 87 CYS HA H 1 4.828 0 . 1 . . . A 108 CYS HA . 18332 1 708 . 1 1 87 87 CYS HB2 H 1 3.494 0.014 . 2 . . . A 108 CYS HB2 . 18332 1 709 . 1 1 87 87 CYS HB3 H 1 2.757 0.017 . 2 . . . A 108 CYS HB3 . 18332 1 710 . 1 1 87 87 CYS CA C 13 57.07 0.016 . 1 . . . A 108 CYS CA . 18332 1 711 . 1 1 87 87 CYS CB C 13 40.994 0.006 . 1 . . . A 108 CYS CB . 18332 1 712 . 1 1 87 87 CYS N N 15 120.863 0.011 . 1 . . . A 108 CYS N . 18332 1 713 . 1 1 88 88 LYS H H 1 8.374 0.002 . 1 . . . A 109 LYS H . 18332 1 714 . 1 1 88 88 LYS HA H 1 4.384 0 . 1 . . . A 109 LYS HA . 18332 1 715 . 1 1 88 88 LYS HB2 H 1 1.954 0 . 2 . . . A 109 LYS HB2 . 18332 1 716 . 1 1 88 88 LYS HB3 H 1 1.954 0 . 2 . . . A 109 LYS HB3 . 18332 1 717 . 1 1 88 88 LYS HG2 H 1 1.574 0 . 2 . . . A 109 LYS HG2 . 18332 1 718 . 1 1 88 88 LYS HG3 H 1 1.445 0 . 2 . . . A 109 LYS HG3 . 18332 1 719 . 1 1 88 88 LYS HD2 H 1 1.763 0 . 2 . . . A 109 LYS HD2 . 18332 1 720 . 1 1 88 88 LYS HD3 H 1 1.763 0 . 2 . . . A 109 LYS HD3 . 18332 1 721 . 1 1 88 88 LYS HE2 H 1 3.058 0 . 2 . . . A 109 LYS HE2 . 18332 1 722 . 1 1 88 88 LYS HE3 H 1 3.058 0 . 2 . . . A 109 LYS HE3 . 18332 1 723 . 1 1 88 88 LYS CA C 13 58.418 0.013 . 1 . . . A 109 LYS CA . 18332 1 724 . 1 1 88 88 LYS CB C 13 32.625 0.032 . 1 . . . A 109 LYS CB . 18332 1 725 . 1 1 88 88 LYS CG C 13 25.38 0.286 . 1 . . . A 109 LYS CG . 18332 1 726 . 1 1 88 88 LYS CD C 13 29.252 0 . 1 . . . A 109 LYS CD . 18332 1 727 . 1 1 88 88 LYS CE C 13 42.009 0 . 1 . . . A 109 LYS CE . 18332 1 728 . 1 1 88 88 LYS N N 15 118.8 0.015 . 1 . . . A 109 LYS N . 18332 1 729 . 1 1 89 89 ALA H H 1 7.777 0.005 . 1 . . . A 110 ALA H . 18332 1 730 . 1 1 89 89 ALA HA H 1 4.285 0 . 1 . . . A 110 ALA HA . 18332 1 731 . 1 1 89 89 ALA HB1 H 1 1.327 0 . 1 . . . A 110 ALA HB1 . 18332 1 732 . 1 1 89 89 ALA HB2 H 1 1.327 0 . 1 . . . A 110 ALA HB2 . 18332 1 733 . 1 1 89 89 ALA HB3 H 1 1.327 0 . 1 . . . A 110 ALA HB3 . 18332 1 734 . 1 1 89 89 ALA CA C 13 52.221 0.009 . 1 . . . A 110 ALA CA . 18332 1 735 . 1 1 89 89 ALA CB C 13 19.837 0.046 . 1 . . . A 110 ALA CB . 18332 1 736 . 1 1 89 89 ALA N N 15 119.495 0.027 . 1 . . . A 110 ALA N . 18332 1 737 . 1 1 90 90 GLY H H 1 8.084 0.001 . 1 . . . A 111 GLY H . 18332 1 738 . 1 1 90 90 GLY HA2 H 1 4.067 0 . 2 . . . A 111 GLY HA2 . 18332 1 739 . 1 1 90 90 GLY HA3 H 1 3.913 0 . 2 . . . A 111 GLY HA3 . 18332 1 740 . 1 1 90 90 GLY CA C 13 47.745 0.015 . 1 . . . A 111 GLY CA . 18332 1 741 . 1 1 90 90 GLY N N 15 107.111 0.01 . 1 . . . A 111 GLY N . 18332 1 742 . 1 1 91 91 MET H H 1 7.731 0.001 . 1 . . . A 112 MET H . 18332 1 743 . 1 1 91 91 MET HA H 1 5.426 0 . 1 . . . A 112 MET HA . 18332 1 744 . 1 1 91 91 MET HB2 H 1 2.126 0 . 2 . . . A 112 MET HB2 . 18332 1 745 . 1 1 91 91 MET HB3 H 1 1.837 0 . 2 . . . A 112 MET HB3 . 18332 1 746 . 1 1 91 91 MET HG2 H 1 2.582 0 . 2 . . . A 112 MET HG2 . 18332 1 747 . 1 1 91 91 MET HG3 H 1 2.42 0 . 2 . . . A 112 MET HG3 . 18332 1 748 . 1 1 91 91 MET CA C 13 53.755 0.014 . 1 . . . A 112 MET CA . 18332 1 749 . 1 1 91 91 MET CB C 13 37.293 0.011 . 1 . . . A 112 MET CB . 18332 1 750 . 1 1 91 91 MET CG C 13 31.761 0 . 1 . . . A 112 MET CG . 18332 1 751 . 1 1 91 91 MET N N 15 118.682 0.01 . 1 . . . A 112 MET N . 18332 1 752 . 1 1 92 92 ALA H H 1 9.225 0.015 . 1 . . . A 113 ALA H . 18332 1 753 . 1 1 92 92 ALA HA H 1 5.297 0 . 1 . . . A 113 ALA HA . 18332 1 754 . 1 1 92 92 ALA HB1 H 1 0.763 0 . 1 . . . A 113 ALA HB1 . 18332 1 755 . 1 1 92 92 ALA HB2 H 1 0.763 0 . 1 . . . A 113 ALA HB2 . 18332 1 756 . 1 1 92 92 ALA HB3 H 1 0.763 0 . 1 . . . A 113 ALA HB3 . 18332 1 757 . 1 1 92 92 ALA CA C 13 50.306 0.015 . 1 . . . A 113 ALA CA . 18332 1 758 . 1 1 92 92 ALA CB C 13 23.342 0.046 . 1 . . . A 113 ALA CB . 18332 1 759 . 1 1 92 92 ALA N N 15 123.295 0.043 . 1 . . . A 113 ALA N . 18332 1 760 . 1 1 93 93 GLU H H 1 8.84 0.004 . 1 . . . A 114 GLU H . 18332 1 761 . 1 1 93 93 GLU HA H 1 5.348 0 . 1 . . . A 114 GLU HA . 18332 1 762 . 1 1 93 93 GLU HB2 H 1 2.182 0 . 2 . . . A 114 GLU HB2 . 18332 1 763 . 1 1 93 93 GLU HB3 H 1 1.945 0 . 2 . . . A 114 GLU HB3 . 18332 1 764 . 1 1 93 93 GLU HG2 H 1 2.231 0 . 2 . . . A 114 GLU HG2 . 18332 1 765 . 1 1 93 93 GLU HG3 H 1 2.231 0 . 2 . . . A 114 GLU HG3 . 18332 1 766 . 1 1 93 93 GLU CA C 13 54.721 0 . 1 . . . A 114 GLU CA . 18332 1 767 . 1 1 93 93 GLU CB C 13 32.53 0 . 1 . . . A 114 GLU CB . 18332 1 768 . 1 1 93 93 GLU N N 15 120.553 0.043 . 1 . . . A 114 GLU N . 18332 1 stop_ save_