data_18543 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18543 _Entry.Title ; Chemical shift assignments of DsbA(C33S) by solid-state NMR ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-06-21 _Entry.Accession_date 2012-06-21 _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 SOLID-STATE _Entry.Details 'Solid-state NMR assignments of nanocrystalline DsbA(C33S) and membrane protein complex DsbA(C33S)/DsbB' _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 Lindsay Sperling . . . 18543 2 Ming Tang . . . 18543 3 Deborah Berthold . . . 18543 4 Anna Nesbitt . . . 18543 5 Robert Gennis . . . 18543 6 Chad Rienstra . . . 18543 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18543 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 518 18543 '15N chemical shifts' 128 18543 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 . . 2013-06-05 2012-06-21 update BMRB 'update entry citation' 18543 1 . . 2013-04-02 2012-06-21 original author 'original release' 18543 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 16327 'DsbA, wild type oxidized' 18543 BMRB 18544 'DsbA(C33S)/DsbB complex' 18543 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18543 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 23527473 _Citation.Full_citation . _Citation.Title 'Solid-State NMR Study of a 41 kDa Membrane Protein Complex DsbA/DsbB.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Phys. Chem. B' _Citation.Journal_name_full 'The journal of physical chemistry. B' _Citation.Journal_volume 117 _Citation.Journal_issue 20 _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 6052 _Citation.Page_last 6060 _Citation.Year 2013 _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 Lindsay Sperling . J. . 18543 1 2 Ming Tang . . . 18543 1 3 Deborah Berthold . A. . 18543 1 4 Anna Nesbitt . E. . 18543 1 5 Robert Gennis . B. . 18543 1 6 Chad Rienstra . M. . 18543 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID DsbA/DsbB 18543 1 'Membrane Protein' 18543 1 'Solid-state NMR' 18543 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18543 _Assembly.ID 1 _Assembly.Name 'DsbA(C33S) protein' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds yes _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass 41000 _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 DsbA(C33S) 1 $DsbA(C33S) A . yes native no no . . . 18543 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_DsbA(C33S) _Entity.Sf_category entity _Entity.Sf_framecode DsbA(C33S) _Entity.Entry_ID 18543 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name DsbA(C33S) _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 ; AQYEDGKQYTTLEKPVAGAP QVLEFFSFFCPHSYQFEEVL HISDNVKKKLPEGVKMTKYH VNFMGGDLGKDLTQAWAVAM ALGVEDKVTVPLFEGVQKTQ TIRSASDIRDVFINAGIKGE EYDAAWNSFVVKSLVAQQEK AAADVQLRGVPAMFVNGKYQ LNPQGMDTSNMDVFVQQYAD TVKYLSEKK ; _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 189 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 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 BMRB 16327 . DsbA . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 2 no BMRB 17710 . DsbA . . . . . 99.47 188 99.47 99.47 9.64e-135 . . . . 18543 1 3 no BMRB 18396 . oxidized_DsbA . . . . . 100.00 189 98.94 99.47 1.05e-134 . . . . 18543 1 4 no BMRB 18544 . DsbA(C33S) . . . . . 100.00 189 100.00 100.00 4.19e-136 . . . . 18543 1 5 no PDB 1A23 . "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Minimized Average Structure" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 6 no PDB 1A24 . "Solution Nmr Structure Of Reduced Dsba From Escherichia Coli, Family Of 20 Structures" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 7 no PDB 1A2J . "Oxidized Dsba Crystal Form Ii" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 8 no PDB 1A2L . "Reduced Dsba At 2.7 Angstroms Resolution" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 9 no PDB 1A2M . "Oxidized Dsba At 2.7 Angstroms Resolution, Crystal Form Iii" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 10 no PDB 1AC1 . "Dsba Mutant H32l" . . . . . 100.00 189 98.94 98.94 7.80e-134 . . . . 18543 1 11 no PDB 1ACV . "Dsba Mutant H32s" . . . . . 100.00 189 98.94 98.94 4.93e-134 . . . . 18543 1 12 no PDB 1BQ7 . "Dsba Mutant P151a, Role Of The Cis-Proline In The Active Site Of Dsba" . . . . . 100.00 189 98.94 98.94 2.82e-134 . . . . 18543 1 13 no PDB 1DSB . "Crystal Structure Of The Dsba Protein Required For Disulphide Bond Formation In Vivo" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 14 no PDB 1FVJ . "The 2.06 Angstrom Structure Of The H32y Mutant Of The Disulfide Bond Formation Protein (Dsba)" . . . . . 100.00 189 98.94 99.47 2.34e-134 . . . . 18543 1 15 no PDB 1FVK . "The 1.7 Angstrom Structure Of Wild Type Disulfide Bond Formation Protein (Dsba)" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 16 no PDB 1TI1 . "Crystal Structure Of A Mutant Dsba" . . . . . 100.00 189 99.47 100.00 1.35e-135 . . . . 18543 1 17 no PDB 1U3A . "Mutant Dsba" . . . . . 100.00 189 99.47 100.00 1.35e-135 . . . . 18543 1 18 no PDB 2B3S . "Structure Of The Dsba Mutant (P31g-C33a)" . . . . . 100.00 189 98.94 99.47 3.43e-134 . . . . 18543 1 19 no PDB 2B6M . "Structure Of The Dsba Mutant (P31a-C33a)" . . . . . 100.00 189 98.94 99.47 1.50e-134 . . . . 18543 1 20 no PDB 2HI7 . "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" . . . . . 100.00 189 99.47 100.00 1.35e-135 . . . . 18543 1 21 no PDB 2LEG . "Membrane Protein Complex Dsbb-Dsba Structure By Joint Calculations With Solid-State Nmr And X-Ray Experimental Data" . . . . . 100.00 189 99.47 100.00 1.35e-135 . . . . 18543 1 22 no PDB 2ZUP . "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" . . . . . 100.00 189 99.47 100.00 1.35e-135 . . . . 18543 1 23 no PDB 3DKS . "Dsba Substrate Complex" . . . . . 100.00 189 98.94 99.47 9.66e-135 . . . . 18543 1 24 no PDB 3E9J . "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" . . . . . 100.00 189 99.47 100.00 1.35e-135 . . . . 18543 1 25 no PDB 4TKY . "The Complex Structure Of E. Coli Dsba Bound To A Peptide At The Dsba/dsbb Interface" . . . . . 100.00 191 99.47 100.00 8.11e-136 . . . . 18543 1 26 no PDB 4WET . "Crystal Structure Of E.coli Dsba In Complex With Compound 16" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 27 no PDB 4WEY . "Crystal Structure Of E.coli Dsba In Complex With Compound 17" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 28 no PDB 4WF4 . "Crystal Structure Of E.coli Dsba Co-crystallised In Complex With Compound 4" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 29 no PDB 4WF5 . "Crystal Structure Of E.coli Dsba Soaked With Compound 4" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18543 1 30 no DBJ BAB38206 . "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 31 no DBJ BAE77448 . "periplasmic protein disulfide isomerase I [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 32 no DBJ BAG79665 . "protein disulfide isomerase I [Escherichia coli SE11]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 33 no DBJ BAI27892 . "periplasmic protein disulfide isomerase I [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 34 no DBJ BAI33015 . "periplasmic protein disulfide isomerase I [Escherichia coli O103:H2 str. 12009]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 35 no EMBL CAA44868 . "PpfA protein [Escherichia coli K-12]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 36 no EMBL CAA56736 . "dsbA [Escherichia coli K-12]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 37 no EMBL CAA90910 . "DsbA protein [Escherichia coli]" . . . . . 100.00 208 98.94 99.47 7.94e-135 . . . . 18543 1 38 no EMBL CAP78318 . "Thiol:disulfide interchange protein dsbA [Escherichia coli LF82]" . . . . . 100.00 208 98.94 99.47 7.94e-135 . . . . 18543 1 39 no EMBL CAQ34212 . "protein disulfide oxidoreductase [Escherichia coli BL21(DE3)]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 40 no GB AAA23715 . "putative [Escherichia coli]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 41 no GB AAB02995 . "dsbA [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 42 no GB AAC43519 . "thiol:disulfide interchange protein DsbA mutant PH31/32PP [Escherichia coli]" . . . . . 100.00 208 98.94 98.94 1.01e-133 . . . . 18543 1 43 no GB AAC43520 . "thiol:disulfide interchange protein DsbA mutant PH31/32TR [Escherichia coli]" . . . . . 100.00 208 98.41 98.41 2.99e-133 . . . . 18543 1 44 no GB AAC43521 . "thiol:disulfide interchange protein DsbA mutant PH31/32LQ [Escherichia coli]" . . . . . 100.00 208 98.41 98.41 5.70e-133 . . . . 18543 1 45 no REF NP_312810 . "protein disulfide isomerase I [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 46 no REF NP_418297 . "periplasmic protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 47 no REF NP_709659 . "periplasmic protein disulfide isomerase I [Shigella flexneri 2a str. 301]" . . . . . 100.00 208 98.94 99.47 8.47e-135 . . . . 18543 1 48 no REF WP_000725331 . "thiol-disulfide isomerase [Shigella boydii]" . . . . . 100.00 208 98.41 98.94 2.45e-134 . . . . 18543 1 49 no REF WP_000725332 . "thiol:disulfide interchange protein DsbA [Escherichia coli]" . . . . . 100.00 208 98.94 99.47 2.72e-135 . . . . 18543 1 50 no SP P0A4L5 . "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" . . . . . 100.00 208 98.94 99.47 7.94e-135 . . . . 18543 1 51 no SP P0A4L6 . "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" . . . . . 100.00 208 98.94 99.47 7.94e-135 . . . . 18543 1 52 no SP P0AEG4 . "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 53 no SP P0AEG5 . "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18543 1 54 no SP P52235 . "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" . . . . . 100.00 208 98.94 99.47 8.47e-135 . . . . 18543 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 1 ALA . 18543 1 2 2 GLN . 18543 1 3 3 TYR . 18543 1 4 4 GLU . 18543 1 5 5 ASP . 18543 1 6 6 GLY . 18543 1 7 7 LYS . 18543 1 8 8 GLN . 18543 1 9 9 TYR . 18543 1 10 10 THR . 18543 1 11 11 THR . 18543 1 12 12 LEU . 18543 1 13 13 GLU . 18543 1 14 14 LYS . 18543 1 15 15 PRO . 18543 1 16 16 VAL . 18543 1 17 17 ALA . 18543 1 18 18 GLY . 18543 1 19 19 ALA . 18543 1 20 20 PRO . 18543 1 21 21 GLN . 18543 1 22 22 VAL . 18543 1 23 23 LEU . 18543 1 24 24 GLU . 18543 1 25 25 PHE . 18543 1 26 26 PHE . 18543 1 27 27 SER . 18543 1 28 28 PHE . 18543 1 29 29 PHE . 18543 1 30 30 CYS . 18543 1 31 31 PRO . 18543 1 32 32 HIS . 18543 1 33 33 SER . 18543 1 34 34 TYR . 18543 1 35 35 GLN . 18543 1 36 36 PHE . 18543 1 37 37 GLU . 18543 1 38 38 GLU . 18543 1 39 39 VAL . 18543 1 40 40 LEU . 18543 1 41 41 HIS . 18543 1 42 42 ILE . 18543 1 43 43 SER . 18543 1 44 44 ASP . 18543 1 45 45 ASN . 18543 1 46 46 VAL . 18543 1 47 47 LYS . 18543 1 48 48 LYS . 18543 1 49 49 LYS . 18543 1 50 50 LEU . 18543 1 51 51 PRO . 18543 1 52 52 GLU . 18543 1 53 53 GLY . 18543 1 54 54 VAL . 18543 1 55 55 LYS . 18543 1 56 56 MET . 18543 1 57 57 THR . 18543 1 58 58 LYS . 18543 1 59 59 TYR . 18543 1 60 60 HIS . 18543 1 61 61 VAL . 18543 1 62 62 ASN . 18543 1 63 63 PHE . 18543 1 64 64 MET . 18543 1 65 65 GLY . 18543 1 66 66 GLY . 18543 1 67 67 ASP . 18543 1 68 68 LEU . 18543 1 69 69 GLY . 18543 1 70 70 LYS . 18543 1 71 71 ASP . 18543 1 72 72 LEU . 18543 1 73 73 THR . 18543 1 74 74 GLN . 18543 1 75 75 ALA . 18543 1 76 76 TRP . 18543 1 77 77 ALA . 18543 1 78 78 VAL . 18543 1 79 79 ALA . 18543 1 80 80 MET . 18543 1 81 81 ALA . 18543 1 82 82 LEU . 18543 1 83 83 GLY . 18543 1 84 84 VAL . 18543 1 85 85 GLU . 18543 1 86 86 ASP . 18543 1 87 87 LYS . 18543 1 88 88 VAL . 18543 1 89 89 THR . 18543 1 90 90 VAL . 18543 1 91 91 PRO . 18543 1 92 92 LEU . 18543 1 93 93 PHE . 18543 1 94 94 GLU . 18543 1 95 95 GLY . 18543 1 96 96 VAL . 18543 1 97 97 GLN . 18543 1 98 98 LYS . 18543 1 99 99 THR . 18543 1 100 100 GLN . 18543 1 101 101 THR . 18543 1 102 102 ILE . 18543 1 103 103 ARG . 18543 1 104 104 SER . 18543 1 105 105 ALA . 18543 1 106 106 SER . 18543 1 107 107 ASP . 18543 1 108 108 ILE . 18543 1 109 109 ARG . 18543 1 110 110 ASP . 18543 1 111 111 VAL . 18543 1 112 112 PHE . 18543 1 113 113 ILE . 18543 1 114 114 ASN . 18543 1 115 115 ALA . 18543 1 116 116 GLY . 18543 1 117 117 ILE . 18543 1 118 118 LYS . 18543 1 119 119 GLY . 18543 1 120 120 GLU . 18543 1 121 121 GLU . 18543 1 122 122 TYR . 18543 1 123 123 ASP . 18543 1 124 124 ALA . 18543 1 125 125 ALA . 18543 1 126 126 TRP . 18543 1 127 127 ASN . 18543 1 128 128 SER . 18543 1 129 129 PHE . 18543 1 130 130 VAL . 18543 1 131 131 VAL . 18543 1 132 132 LYS . 18543 1 133 133 SER . 18543 1 134 134 LEU . 18543 1 135 135 VAL . 18543 1 136 136 ALA . 18543 1 137 137 GLN . 18543 1 138 138 GLN . 18543 1 139 139 GLU . 18543 1 140 140 LYS . 18543 1 141 141 ALA . 18543 1 142 142 ALA . 18543 1 143 143 ALA . 18543 1 144 144 ASP . 18543 1 145 145 VAL . 18543 1 146 146 GLN . 18543 1 147 147 LEU . 18543 1 148 148 ARG . 18543 1 149 149 GLY . 18543 1 150 150 VAL . 18543 1 151 151 PRO . 18543 1 152 152 ALA . 18543 1 153 153 MET . 18543 1 154 154 PHE . 18543 1 155 155 VAL . 18543 1 156 156 ASN . 18543 1 157 157 GLY . 18543 1 158 158 LYS . 18543 1 159 159 TYR . 18543 1 160 160 GLN . 18543 1 161 161 LEU . 18543 1 162 162 ASN . 18543 1 163 163 PRO . 18543 1 164 164 GLN . 18543 1 165 165 GLY . 18543 1 166 166 MET . 18543 1 167 167 ASP . 18543 1 168 168 THR . 18543 1 169 169 SER . 18543 1 170 170 ASN . 18543 1 171 171 MET . 18543 1 172 172 ASP . 18543 1 173 173 VAL . 18543 1 174 174 PHE . 18543 1 175 175 VAL . 18543 1 176 176 GLN . 18543 1 177 177 GLN . 18543 1 178 178 TYR . 18543 1 179 179 ALA . 18543 1 180 180 ASP . 18543 1 181 181 THR . 18543 1 182 182 VAL . 18543 1 183 183 LYS . 18543 1 184 184 TYR . 18543 1 185 185 LEU . 18543 1 186 186 SER . 18543 1 187 187 GLU . 18543 1 188 188 LYS . 18543 1 189 189 LYS . 18543 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 18543 1 . GLN 2 2 18543 1 . TYR 3 3 18543 1 . GLU 4 4 18543 1 . ASP 5 5 18543 1 . GLY 6 6 18543 1 . LYS 7 7 18543 1 . GLN 8 8 18543 1 . TYR 9 9 18543 1 . THR 10 10 18543 1 . THR 11 11 18543 1 . LEU 12 12 18543 1 . GLU 13 13 18543 1 . LYS 14 14 18543 1 . PRO 15 15 18543 1 . VAL 16 16 18543 1 . ALA 17 17 18543 1 . GLY 18 18 18543 1 . ALA 19 19 18543 1 . PRO 20 20 18543 1 . GLN 21 21 18543 1 . VAL 22 22 18543 1 . LEU 23 23 18543 1 . GLU 24 24 18543 1 . PHE 25 25 18543 1 . PHE 26 26 18543 1 . SER 27 27 18543 1 . PHE 28 28 18543 1 . PHE 29 29 18543 1 . CYS 30 30 18543 1 . PRO 31 31 18543 1 . HIS 32 32 18543 1 . SER 33 33 18543 1 . TYR 34 34 18543 1 . GLN 35 35 18543 1 . PHE 36 36 18543 1 . GLU 37 37 18543 1 . GLU 38 38 18543 1 . VAL 39 39 18543 1 . LEU 40 40 18543 1 . HIS 41 41 18543 1 . ILE 42 42 18543 1 . SER 43 43 18543 1 . ASP 44 44 18543 1 . ASN 45 45 18543 1 . VAL 46 46 18543 1 . LYS 47 47 18543 1 . LYS 48 48 18543 1 . LYS 49 49 18543 1 . LEU 50 50 18543 1 . PRO 51 51 18543 1 . GLU 52 52 18543 1 . GLY 53 53 18543 1 . VAL 54 54 18543 1 . LYS 55 55 18543 1 . MET 56 56 18543 1 . THR 57 57 18543 1 . LYS 58 58 18543 1 . TYR 59 59 18543 1 . HIS 60 60 18543 1 . VAL 61 61 18543 1 . ASN 62 62 18543 1 . PHE 63 63 18543 1 . MET 64 64 18543 1 . GLY 65 65 18543 1 . GLY 66 66 18543 1 . ASP 67 67 18543 1 . LEU 68 68 18543 1 . GLY 69 69 18543 1 . LYS 70 70 18543 1 . ASP 71 71 18543 1 . LEU 72 72 18543 1 . THR 73 73 18543 1 . GLN 74 74 18543 1 . ALA 75 75 18543 1 . TRP 76 76 18543 1 . ALA 77 77 18543 1 . VAL 78 78 18543 1 . ALA 79 79 18543 1 . MET 80 80 18543 1 . ALA 81 81 18543 1 . LEU 82 82 18543 1 . GLY 83 83 18543 1 . VAL 84 84 18543 1 . GLU 85 85 18543 1 . ASP 86 86 18543 1 . LYS 87 87 18543 1 . VAL 88 88 18543 1 . THR 89 89 18543 1 . VAL 90 90 18543 1 . PRO 91 91 18543 1 . LEU 92 92 18543 1 . PHE 93 93 18543 1 . GLU 94 94 18543 1 . GLY 95 95 18543 1 . VAL 96 96 18543 1 . GLN 97 97 18543 1 . LYS 98 98 18543 1 . THR 99 99 18543 1 . GLN 100 100 18543 1 . THR 101 101 18543 1 . ILE 102 102 18543 1 . ARG 103 103 18543 1 . SER 104 104 18543 1 . ALA 105 105 18543 1 . SER 106 106 18543 1 . ASP 107 107 18543 1 . ILE 108 108 18543 1 . ARG 109 109 18543 1 . ASP 110 110 18543 1 . VAL 111 111 18543 1 . PHE 112 112 18543 1 . ILE 113 113 18543 1 . ASN 114 114 18543 1 . ALA 115 115 18543 1 . GLY 116 116 18543 1 . ILE 117 117 18543 1 . LYS 118 118 18543 1 . GLY 119 119 18543 1 . GLU 120 120 18543 1 . GLU 121 121 18543 1 . TYR 122 122 18543 1 . ASP 123 123 18543 1 . ALA 124 124 18543 1 . ALA 125 125 18543 1 . TRP 126 126 18543 1 . ASN 127 127 18543 1 . SER 128 128 18543 1 . PHE 129 129 18543 1 . VAL 130 130 18543 1 . VAL 131 131 18543 1 . LYS 132 132 18543 1 . SER 133 133 18543 1 . LEU 134 134 18543 1 . VAL 135 135 18543 1 . ALA 136 136 18543 1 . GLN 137 137 18543 1 . GLN 138 138 18543 1 . GLU 139 139 18543 1 . LYS 140 140 18543 1 . ALA 141 141 18543 1 . ALA 142 142 18543 1 . ALA 143 143 18543 1 . ASP 144 144 18543 1 . VAL 145 145 18543 1 . GLN 146 146 18543 1 . LEU 147 147 18543 1 . ARG 148 148 18543 1 . GLY 149 149 18543 1 . VAL 150 150 18543 1 . PRO 151 151 18543 1 . ALA 152 152 18543 1 . MET 153 153 18543 1 . PHE 154 154 18543 1 . VAL 155 155 18543 1 . ASN 156 156 18543 1 . GLY 157 157 18543 1 . LYS 158 158 18543 1 . TYR 159 159 18543 1 . GLN 160 160 18543 1 . LEU 161 161 18543 1 . ASN 162 162 18543 1 . PRO 163 163 18543 1 . GLN 164 164 18543 1 . GLY 165 165 18543 1 . MET 166 166 18543 1 . ASP 167 167 18543 1 . THR 168 168 18543 1 . SER 169 169 18543 1 . ASN 170 170 18543 1 . MET 171 171 18543 1 . ASP 172 172 18543 1 . VAL 173 173 18543 1 . PHE 174 174 18543 1 . VAL 175 175 18543 1 . GLN 176 176 18543 1 . GLN 177 177 18543 1 . TYR 178 178 18543 1 . ALA 179 179 18543 1 . ASP 180 180 18543 1 . THR 181 181 18543 1 . VAL 182 182 18543 1 . LYS 183 183 18543 1 . TYR 184 184 18543 1 . LEU 185 185 18543 1 . SER 186 186 18543 1 . GLU 187 187 18543 1 . LYS 188 188 18543 1 . LYS 189 189 18543 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 18543 _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 $DsbA(C33S) . 562 organism . 'Escherichia coli' Enterobacteria . . Bacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 18543 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 18543 _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 $DsbA(C33S) . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pQE70 . . . . . . 18543 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18543 _Sample.ID 1 _Sample.Type solid _Sample.Sub_type . _Sample.Details 'nanocrystalline DsbA(C33S)' _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% 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 DsbA(C33S) '[U-100% 13C; U-100% 15N]' . . 1 $DsbA(C33S) . . 15 . . mg . . . . 18543 1 2 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18543 1 3 D2O [U-2H] . . . . . . 10 . . % . . . . 18543 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 18543 _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 . pH 18543 1 pressure 1 . atm 18543 1 temperature 263 . K 18543 1 stop_ save_ save_sample_conditions_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_2 _Sample_condition_list.Entry_ID 18543 _Sample_condition_list.ID 2 _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 . pH 18543 2 pressure 1 . atm 18543 2 temperature 253 . K 18543 2 stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Software.Sf_category software _Software.Sf_framecode VNMRJ _Software.Entry_ID 18543 _Software.ID 1 _Software.Name VNMRJ _Software.Version 3.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Varian . . 18543 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 18543 1 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 18543 _Software.ID 2 _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' . . 18543 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 18543 2 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 18543 _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 . . 18543 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18543 3 'data analysis' 18543 3 'peak picking' 18543 3 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 18543 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model VXRS _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 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 18543 _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 VXRS . 500 . . . 18543 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 18543 _Experiment_list.ID 1 _Experiment_list.Details 'Magic angle spinning solid-state NMR' 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 '3D NCACX' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18543 1 2 '3D NCOCX' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18543 1 3 '2D CC' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18543 1 4 '2D TEDOR' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18543 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 18543 _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 na indirect 0.251449530 other other . . . . . . . 18543 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 other other . . . . . . . 18543 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_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode Assigned_chem_shift_1 _Assigned_chem_shift_list.Entry_ID 18543 _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 0.3 _Assigned_chem_shift_list.Chem_shift_15N_err 0.3 _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 '3D NCACX' . . . 18543 1 2 '3D NCOCX' . . . 18543 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 ALA CA C 13 51.458 0.30 . 1 . . . . 1 ALA CA . 18543 1 2 . 1 1 1 1 ALA CB C 13 19.737 0.30 . 1 . . . . 1 ALA CB . 18543 1 3 . 1 1 2 2 GLN C C 13 179.750 0.30 . 1 . . . . 2 GLN C . 18543 1 4 . 1 1 2 2 GLN CA C 13 59.815 0.30 . 1 . . . . 2 GLN CA . 18543 1 5 . 1 1 2 2 GLN CB C 13 29.891 0.30 . 1 . . . . 2 GLN CB . 18543 1 6 . 1 1 2 2 GLN CG C 13 32.485 0.30 . 1 . . . . 2 GLN CG . 18543 1 7 . 1 1 2 2 GLN N N 15 121.171 0.30 . 1 . . . . 2 GLN N . 18543 1 8 . 1 1 3 3 TYR C C 13 176.938 0.30 . 1 . . . . 3 TYR C . 18543 1 9 . 1 1 3 3 TYR CA C 13 57.911 0.30 . 1 . . . . 3 TYR CA . 18543 1 10 . 1 1 3 3 TYR CB C 13 40.489 0.30 . 1 . . . . 3 TYR CB . 18543 1 11 . 1 1 3 3 TYR N N 15 121.707 0.30 . 1 . . . . 3 TYR N . 18543 1 12 . 1 1 4 4 GLU C C 13 174.586 0.30 . 1 . . . . 4 GLU C . 18543 1 13 . 1 1 4 4 GLU CA C 13 54.912 0.30 . 1 . . . . 4 GLU CA . 18543 1 14 . 1 1 4 4 GLU CB C 13 33.806 0.30 . 1 . . . . 4 GLU CB . 18543 1 15 . 1 1 4 4 GLU N N 15 122.755 0.30 . 1 . . . . 4 GLU N . 18543 1 16 . 1 1 5 5 ASP C C 13 177.361 0.30 . 1 . . . . 5 ASP C . 18543 1 17 . 1 1 5 5 ASP CA C 13 55.296 0.30 . 1 . . . . 5 ASP CA . 18543 1 18 . 1 1 5 5 ASP CB C 13 41.388 0.30 . 1 . . . . 5 ASP CB . 18543 1 19 . 1 1 5 5 ASP CG C 13 179.726 0.30 . 1 . . . . 5 ASP CG . 18543 1 20 . 1 1 5 5 ASP N N 15 125.539 0.30 . 1 . . . . 5 ASP N . 18543 1 21 . 1 1 6 6 GLY C C 13 173.482 0.30 . 1 . . . . 6 GLY C . 18543 1 22 . 1 1 6 6 GLY CA C 13 44.911 0.30 . 1 . . . . 6 GLY CA . 18543 1 23 . 1 1 6 6 GLY N N 15 116.854 0.30 . 1 . . . . 6 GLY N . 18543 1 24 . 1 1 7 7 LYS C C 13 175.438 0.30 . 1 . . . . 7 LYS C . 18543 1 25 . 1 1 7 7 LYS CA C 13 56.798 0.30 . 1 . . . . 7 LYS CA . 18543 1 26 . 1 1 7 7 LYS CB C 13 32.206 0.30 . 1 . . . . 7 LYS CB . 18543 1 27 . 1 1 7 7 LYS N N 15 122.043 0.30 . 1 . . . . 7 LYS N . 18543 1 28 . 1 1 8 8 GLN C C 13 174.182 0.30 . 1 . . . . 8 GLN C . 18543 1 29 . 1 1 8 8 GLN CA C 13 59.412 0.30 . 1 . . . . 8 GLN CA . 18543 1 30 . 1 1 8 8 GLN CB C 13 27.100 0.30 . 1 . . . . 8 GLN CB . 18543 1 31 . 1 1 8 8 GLN CG C 13 34.022 0.30 . 1 . . . . 8 GLN CG . 18543 1 32 . 1 1 8 8 GLN N N 15 115.615 0.30 . 1 . . . . 8 GLN N . 18543 1 33 . 1 1 9 9 TYR C C 13 172.132 0.30 . 1 . . . . 9 TYR C . 18543 1 34 . 1 1 9 9 TYR CA C 13 55.102 0.30 . 1 . . . . 9 TYR CA . 18543 1 35 . 1 1 9 9 TYR CB C 13 41.562 0.30 . 1 . . . . 9 TYR CB . 18543 1 36 . 1 1 9 9 TYR CD1 C 13 132.294 0.30 . 3 . . . . 9 TYR CD1 . 18543 1 37 . 1 1 9 9 TYR CE1 C 13 116.886 0.30 . 1 . . . . 9 TYR CE . 18543 1 38 . 1 1 9 9 TYR CE2 C 13 116.886 0.30 . 1 . . . . 9 TYR CE . 18543 1 39 . 1 1 9 9 TYR CZ C 13 158.147 0.30 . 1 . . . . 9 TYR CZ . 18543 1 40 . 1 1 9 9 TYR N N 15 111.606 0.30 . 1 . . . . 9 TYR N . 18543 1 41 . 1 1 10 10 THR C C 13 174.496 0.30 . 1 . . . . 10 THR C . 18543 1 42 . 1 1 10 10 THR CA C 13 60.258 0.30 . 1 . . . . 10 THR CA . 18543 1 43 . 1 1 10 10 THR CB C 13 71.482 0.30 . 1 . . . . 10 THR CB . 18543 1 44 . 1 1 10 10 THR CG2 C 13 22.083 0.30 . 1 . . . . 10 THR CG2 . 18543 1 45 . 1 1 10 10 THR N N 15 111.517 0.30 . 1 . . . . 10 THR N . 18543 1 46 . 1 1 11 11 THR C C 13 175.324 0.30 . 1 . . . . 11 THR C . 18543 1 47 . 1 1 11 11 THR CA C 13 62.815 0.30 . 1 . . . . 11 THR CA . 18543 1 48 . 1 1 11 11 THR CB C 13 69.609 0.30 . 1 . . . . 11 THR CB . 18543 1 49 . 1 1 11 11 THR CG2 C 13 21.782 0.30 . 1 . . . . 11 THR CG2 . 18543 1 50 . 1 1 11 11 THR N N 15 120.997 0.30 . 1 . . . . 11 THR N . 18543 1 51 . 1 1 12 12 LEU C C 13 177.401 0.30 . 1 . . . . 12 LEU C . 18543 1 52 . 1 1 12 12 LEU CA C 13 55.832 0.30 . 1 . . . . 12 LEU CA . 18543 1 53 . 1 1 12 12 LEU CB C 13 41.606 0.30 . 1 . . . . 12 LEU CB . 18543 1 54 . 1 1 12 12 LEU CG C 13 28.533 0.30 . 1 . . . . 12 LEU CG . 18543 1 55 . 1 1 12 12 LEU CD1 C 13 24.601 0.30 . 1 . . . . 12 LEU CD1 . 18543 1 56 . 1 1 12 12 LEU CD2 C 13 23.474 0.30 . 2 . . . . 12 LEU CD2 . 18543 1 57 . 1 1 12 12 LEU N N 15 129.187 0.30 . 1 . . . . 12 LEU N . 18543 1 58 . 1 1 13 13 GLU C C 13 176.790 0.30 . 1 . . . . 13 GLU C . 18543 1 59 . 1 1 13 13 GLU CA C 13 58.721 0.30 . 1 . . . . 13 GLU CA . 18543 1 60 . 1 1 13 13 GLU CB C 13 29.775 0.30 . 1 . . . . 13 GLU CB . 18543 1 61 . 1 1 13 13 GLU N N 15 123.113 0.30 . 1 . . . . 13 GLU N . 18543 1 62 . 1 1 14 14 LYS C C 13 172.429 0.30 . 1 . . . . 14 LYS C . 18543 1 63 . 1 1 14 14 LYS CA C 13 52.304 0.30 . 1 . . . . 14 LYS CA . 18543 1 64 . 1 1 14 14 LYS CB C 13 32.905 0.30 . 1 . . . . 14 LYS CB . 18543 1 65 . 1 1 14 14 LYS CG C 13 24.440 0.30 . 1 . . . . 14 LYS CG . 18543 1 66 . 1 1 14 14 LYS N N 15 117.657 0.30 . 1 . . . . 14 LYS N . 18543 1 67 . 1 1 15 15 PRO C C 13 176.412 0.30 . 1 . . . . 15 PRO C . 18543 1 68 . 1 1 15 15 PRO CA C 13 62.328 0.30 . 1 . . . . 15 PRO CA . 18543 1 69 . 1 1 15 15 PRO CB C 13 32.653 0.30 . 1 . . . . 15 PRO CB . 18543 1 70 . 1 1 15 15 PRO CG C 13 27.202 0.30 . 1 . . . . 15 PRO CG . 18543 1 71 . 1 1 15 15 PRO CD C 13 50.734 0.30 . 1 . . . . 15 PRO CD . 18543 1 72 . 1 1 15 15 PRO N N 15 135.650 0.30 . 1 . . . . 15 PRO N . 18543 1 73 . 1 1 16 16 VAL C C 13 176.008 0.30 . 1 . . . . 16 VAL C . 18543 1 74 . 1 1 16 16 VAL CA C 13 61.443 0.30 . 1 . . . . 16 VAL CA . 18543 1 75 . 1 1 16 16 VAL CB C 13 32.778 0.30 . 1 . . . . 16 VAL CB . 18543 1 76 . 1 1 16 16 VAL CG1 C 13 21.534 0.30 . 2 . . . . 16 VAL CG1 . 18543 1 77 . 1 1 16 16 VAL CG2 C 13 21.555 0.30 . 2 . . . . 16 VAL CG2 . 18543 1 78 . 1 1 16 16 VAL N N 15 123.263 0.30 . 1 . . . . 16 VAL N . 18543 1 79 . 1 1 17 17 ALA C C 13 178.952 0.30 . 1 . . . . 17 ALA C . 18543 1 80 . 1 1 17 17 ALA CA C 13 52.406 0.30 . 1 . . . . 17 ALA CA . 18543 1 81 . 1 1 17 17 ALA CB C 13 18.886 0.30 . 1 . . . . 17 ALA CB . 18543 1 82 . 1 1 17 17 ALA N N 15 132.328 0.30 . 1 . . . . 17 ALA N . 18543 1 83 . 1 1 18 18 GLY C C 13 174.000 0.30 . 1 . . . . 18 GLY C . 18543 1 84 . 1 1 18 18 GLY CA C 13 45.612 0.30 . 1 . . . . 18 GLY CA . 18543 1 85 . 1 1 18 18 GLY N N 15 110.605 0.30 . 1 . . . . 18 GLY N . 18543 1 86 . 1 1 19 19 ALA C C 13 175.143 0.30 . 1 . . . . 19 ALA C . 18543 1 87 . 1 1 19 19 ALA CA C 13 50.243 0.30 . 1 . . . . 19 ALA CA . 18543 1 88 . 1 1 19 19 ALA CB C 13 17.254 0.30 . 1 . . . . 19 ALA CB . 18543 1 89 . 1 1 19 19 ALA N N 15 122.370 0.30 . 1 . . . . 19 ALA N . 18543 1 90 . 1 1 20 20 PRO CA C 13 62.310 0.30 . 1 . . . . 20 PRO CA . 18543 1 91 . 1 1 20 20 PRO CB C 13 31.986 0.30 . 1 . . . . 20 PRO CB . 18543 1 92 . 1 1 20 20 PRO CG C 13 27.823 0.30 . 1 . . . . 20 PRO CG . 18543 1 93 . 1 1 20 20 PRO CD C 13 50.189 0.30 . 1 . . . . 20 PRO CD . 18543 1 94 . 1 1 20 20 PRO N N 15 134.046 0.30 . 1 . . . . 20 PRO N . 18543 1 95 . 1 1 21 21 GLN C C 13 176.824 0.30 . 1 . . . . 21 GLN C . 18543 1 96 . 1 1 21 21 GLN CA C 13 60.088 0.30 . 1 . . . . 21 GLN CA . 18543 1 97 . 1 1 21 21 GLN CB C 13 29.558 0.30 . 1 . . . . 21 GLN CB . 18543 1 98 . 1 1 21 21 GLN CG C 13 31.832 0.30 . 1 . . . . 21 GLN CG . 18543 1 99 . 1 1 21 21 GLN N N 15 121.846 0.30 . 1 . . . . 21 GLN N . 18543 1 100 . 1 1 22 22 VAL C C 13 172.959 0.30 . 1 . . . . 22 VAL C . 18543 1 101 . 1 1 22 22 VAL CA C 13 62.723 0.30 . 1 . . . . 22 VAL CA . 18543 1 102 . 1 1 22 22 VAL CB C 13 33.562 0.30 . 1 . . . . 22 VAL CB . 18543 1 103 . 1 1 22 22 VAL CG1 C 13 22.959 0.30 . 2 . . . . 22 VAL CG1 . 18543 1 104 . 1 1 22 22 VAL CG2 C 13 21.328 0.30 . 2 . . . . 22 VAL CG2 . 18543 1 105 . 1 1 22 22 VAL N N 15 116.011 0.30 . 1 . . . . 22 VAL N . 18543 1 106 . 1 1 23 23 LEU C C 13 173.441 0.30 . 1 . . . . 23 LEU C . 18543 1 107 . 1 1 23 23 LEU CA C 13 52.768 0.30 . 1 . . . . 23 LEU CA . 18543 1 108 . 1 1 23 23 LEU CB C 13 46.120 0.30 . 1 . . . . 23 LEU CB . 18543 1 109 . 1 1 23 23 LEU CG C 13 26.470 0.30 . 1 . . . . 23 LEU CG . 18543 1 110 . 1 1 23 23 LEU CD1 C 13 22.358 0.30 . 1 . . . . 23 LEU CD . 18543 1 111 . 1 1 23 23 LEU CD2 C 13 22.358 0.30 . 1 . . . . 23 LEU CD . 18543 1 112 . 1 1 23 23 LEU N N 15 128.870 0.30 . 1 . . . . 23 LEU N . 18543 1 113 . 1 1 26 26 PHE C C 13 170.243 0.30 . 1 . . . . 26 PHE C . 18543 1 114 . 1 1 26 26 PHE CA C 13 54.800 0.30 . 1 . . . . 26 PHE CA . 18543 1 115 . 1 1 27 27 SER C C 13 177.315 0.30 . 1 . . . . 27 SER C . 18543 1 116 . 1 1 27 27 SER CA C 13 54.926 0.30 . 1 . . . . 27 SER CA . 18543 1 117 . 1 1 27 27 SER CB C 13 65.327 0.30 . 1 . . . . 27 SER CB . 18543 1 118 . 1 1 27 27 SER N N 15 108.245 0.30 . 1 . . . . 27 SER N . 18543 1 119 . 1 1 28 28 PHE N N 15 131.123 0.30 . 1 . . . . 28 PHE N . 18543 1 120 . 1 1 31 31 PRO CA C 13 66.300 0.30 . 1 . . . . 31 PRO CA . 18543 1 121 . 1 1 31 31 PRO CB C 13 32.265 0.30 . 1 . . . . 31 PRO CB . 18543 1 122 . 1 1 31 31 PRO CG C 13 27.034 0.30 . 1 . . . . 31 PRO CG . 18543 1 123 . 1 1 31 31 PRO CD C 13 51.602 0.30 . 1 . . . . 31 PRO CD . 18543 1 124 . 1 1 31 31 PRO N N 15 146.652 0.30 . 1 . . . . 31 PRO N . 18543 1 125 . 1 1 32 32 HIS CA C 13 58.600 0.30 . 1 . . . . 32 HIS CA . 18543 1 126 . 1 1 32 32 HIS CB C 13 29.688 0.30 . 1 . . . . 32 HIS CB . 18543 1 127 . 1 1 32 32 HIS N N 15 120.465 0.30 . 1 . . . . 32 HIS N . 18543 1 128 . 1 1 33 33 SER CA C 13 63.509 0.30 . 1 . . . . 33 SER CA . 18543 1 129 . 1 1 33 33 SER CB C 13 65.105 0.30 . 1 . . . . 33 SER CB . 18543 1 130 . 1 1 39 39 VAL C C 13 176.841 0.30 . 1 . . . . 39 VAL C . 18543 1 131 . 1 1 39 39 VAL CA C 13 63.965 0.30 . 1 . . . . 39 VAL CA . 18543 1 132 . 1 1 39 39 VAL CB C 13 32.407 0.30 . 1 . . . . 39 VAL CB . 18543 1 133 . 1 1 39 39 VAL CG1 C 13 20.848 0.30 . 2 . . . . 39 VAL CG1 . 18543 1 134 . 1 1 39 39 VAL N N 15 116.596 0.30 . 1 . . . . 39 VAL N . 18543 1 135 . 1 1 40 40 LEU C C 13 177.017 0.30 . 1 . . . . 40 LEU C . 18543 1 136 . 1 1 40 40 LEU CA C 13 55.158 0.30 . 1 . . . . 40 LEU CA . 18543 1 137 . 1 1 40 40 LEU CB C 13 42.718 0.30 . 1 . . . . 40 LEU CB . 18543 1 138 . 1 1 40 40 LEU CG C 13 27.163 0.30 . 1 . . . . 40 LEU CG . 18543 1 139 . 1 1 40 40 LEU CD1 C 13 26.036 0.30 . 1 . . . . 40 LEU CD . 18543 1 140 . 1 1 40 40 LEU CD2 C 13 26.036 0.30 . 1 . . . . 40 LEU CD . 18543 1 141 . 1 1 40 40 LEU N N 15 114.924 0.30 . 1 . . . . 40 LEU N . 18543 1 142 . 1 1 44 44 ASP C C 13 178.435 0.30 . 1 . . . . 44 ASP C . 18543 1 143 . 1 1 44 44 ASP CA C 13 57.423 0.30 . 1 . . . . 44 ASP CA . 18543 1 144 . 1 1 44 44 ASP CB C 13 40.196 0.30 . 1 . . . . 44 ASP CB . 18543 1 145 . 1 1 44 44 ASP N N 15 120.797 0.30 . 1 . . . . 44 ASP N . 18543 1 146 . 1 1 46 46 VAL C C 13 177.949 0.30 . 1 . . . . 46 VAL C . 18543 1 147 . 1 1 46 46 VAL CA C 13 67.000 0.30 . 1 . . . . 46 VAL CA . 18543 1 148 . 1 1 46 46 VAL CB C 13 31.500 0.30 . 1 . . . . 46 VAL CB . 18543 1 149 . 1 1 46 46 VAL CG1 C 13 23.800 0.30 . 2 . . . . 46 VAL CG1 . 18543 1 150 . 1 1 46 46 VAL CG2 C 13 22.500 0.30 . 2 . . . . 46 VAL CG2 . 18543 1 151 . 1 1 46 46 VAL N N 15 120.200 0.30 . 1 . . . . 46 VAL N . 18543 1 152 . 1 1 47 47 LYS C C 13 179.295 0.30 . 1 . . . . 47 LYS C . 18543 1 153 . 1 1 47 47 LYS CA C 13 60.497 0.30 . 1 . . . . 47 LYS CA . 18543 1 154 . 1 1 47 47 LYS CB C 13 32.153 0.30 . 1 . . . . 47 LYS CB . 18543 1 155 . 1 1 47 47 LYS CG C 13 25.063 0.30 . 1 . . . . 47 LYS CG . 18543 1 156 . 1 1 47 47 LYS N N 15 120.454 0.30 . 1 . . . . 47 LYS N . 18543 1 157 . 1 1 48 48 LYS C C 13 177.599 0.30 . 1 . . . . 48 LYS C . 18543 1 158 . 1 1 48 48 LYS CA C 13 58.474 0.30 . 1 . . . . 48 LYS CA . 18543 1 159 . 1 1 48 48 LYS CB C 13 32.926 0.30 . 1 . . . . 48 LYS CB . 18543 1 160 . 1 1 48 48 LYS CG C 13 25.527 0.30 . 1 . . . . 48 LYS CG . 18543 1 161 . 1 1 48 48 LYS N N 15 115.412 0.30 . 1 . . . . 48 LYS N . 18543 1 162 . 1 1 49 49 LYS C C 13 176.229 0.30 . 1 . . . . 49 LYS C . 18543 1 163 . 1 1 49 49 LYS CA C 13 55.461 0.30 . 1 . . . . 49 LYS CA . 18543 1 164 . 1 1 49 49 LYS CB C 13 34.277 0.30 . 1 . . . . 49 LYS CB . 18543 1 165 . 1 1 49 49 LYS CG C 13 25.915 0.30 . 1 . . . . 49 LYS CG . 18543 1 166 . 1 1 49 49 LYS N N 15 116.509 0.30 . 1 . . . . 49 LYS N . 18543 1 167 . 1 1 50 50 LEU CA C 13 53.330 0.30 . 1 . . . . 50 LEU CA . 18543 1 168 . 1 1 50 50 LEU CB C 13 41.271 0.30 . 1 . . . . 50 LEU CB . 18543 1 169 . 1 1 50 50 LEU CG C 13 25.864 0.30 . 1 . . . . 50 LEU CG . 18543 1 170 . 1 1 50 50 LEU N N 15 120.267 0.30 . 1 . . . . 50 LEU N . 18543 1 171 . 1 1 51 51 PRO CA C 13 65.437 0.30 . 1 . . . . 51 PRO CA . 18543 1 172 . 1 1 51 51 PRO CB C 13 32.376 0.30 . 1 . . . . 51 PRO CB . 18543 1 173 . 1 1 51 51 PRO CG C 13 28.377 0.30 . 1 . . . . 51 PRO CG . 18543 1 174 . 1 1 51 51 PRO CD C 13 52.693 0.30 . 1 . . . . 51 PRO CD . 18543 1 175 . 1 1 51 51 PRO N N 15 152.954 0.30 . 1 . . . . 51 PRO N . 18543 1 176 . 1 1 52 52 GLU C C 13 179.651 0.30 . 1 . . . . 52 GLU C . 18543 1 177 . 1 1 52 52 GLU CA C 13 59.344 0.30 . 1 . . . . 52 GLU CA . 18543 1 178 . 1 1 52 52 GLU CB C 13 28.114 0.30 . 1 . . . . 52 GLU CB . 18543 1 179 . 1 1 52 52 GLU CG C 13 34.438 0.30 . 1 . . . . 52 GLU CG . 18543 1 180 . 1 1 52 52 GLU N N 15 119.551 0.30 . 1 . . . . 52 GLU N . 18543 1 181 . 1 1 53 53 GLY C C 13 174.200 0.30 . 1 . . . . 53 GLY C . 18543 1 182 . 1 1 53 53 GLY CA C 13 45.678 0.30 . 1 . . . . 53 GLY CA . 18543 1 183 . 1 1 53 53 GLY N N 15 110.735 0.30 . 1 . . . . 53 GLY N . 18543 1 184 . 1 1 54 54 VAL C C 13 174.617 0.30 . 1 . . . . 54 VAL C . 18543 1 185 . 1 1 54 54 VAL CA C 13 62.455 0.30 . 1 . . . . 54 VAL CA . 18543 1 186 . 1 1 54 54 VAL CB C 13 32.060 0.30 . 1 . . . . 54 VAL CB . 18543 1 187 . 1 1 54 54 VAL CG1 C 13 22.073 0.30 . 2 . . . . 54 VAL CG1 . 18543 1 188 . 1 1 54 54 VAL N N 15 121.881 0.30 . 1 . . . . 54 VAL N . 18543 1 189 . 1 1 57 57 THR C C 13 171.806 0.30 . 1 . . . . 57 THR C . 18543 1 190 . 1 1 57 57 THR CA C 13 62.875 0.30 . 1 . . . . 57 THR CA . 18543 1 191 . 1 1 57 57 THR CB C 13 70.478 0.30 . 1 . . . . 57 THR CB . 18543 1 192 . 1 1 57 57 THR CG2 C 13 22.783 0.30 . 1 . . . . 57 THR CG2 . 18543 1 193 . 1 1 57 57 THR N N 15 124.982 0.30 . 1 . . . . 57 THR N . 18543 1 194 . 1 1 59 59 TYR CA C 13 52.104 0.30 . 1 . . . . 59 TYR CA . 18543 1 195 . 1 1 61 61 VAL C C 13 176.453 0.30 . 1 . . . . 61 VAL C . 18543 1 196 . 1 1 61 61 VAL CA C 13 57.799 0.30 . 1 . . . . 61 VAL CA . 18543 1 197 . 1 1 61 61 VAL CB C 13 33.749 0.30 . 1 . . . . 61 VAL CB . 18543 1 198 . 1 1 61 61 VAL N N 15 110.625 0.30 . 1 . . . . 61 VAL N . 18543 1 199 . 1 1 65 65 GLY C C 13 176.579 0.30 . 1 . . . . 65 GLY C . 18543 1 200 . 1 1 65 65 GLY CA C 13 47.542 0.30 . 1 . . . . 65 GLY CA . 18543 1 201 . 1 1 66 66 GLY CA C 13 45.600 0.30 . 1 . . . . 66 GLY CA . 18543 1 202 . 1 1 67 67 ASP C C 13 178.257 0.30 . 1 . . . . 67 ASP C . 18543 1 203 . 1 1 67 67 ASP CA C 13 57.751 0.30 . 1 . . . . 67 ASP CA . 18543 1 204 . 1 1 67 67 ASP CB C 13 39.841 0.30 . 1 . . . . 67 ASP CB . 18543 1 205 . 1 1 67 67 ASP N N 15 128.168 0.30 . 1 . . . . 67 ASP N . 18543 1 206 . 1 1 68 68 LEU C C 13 179.000 0.30 . 1 . . . . 68 LEU C . 18543 1 207 . 1 1 68 68 LEU CA C 13 57.200 0.30 . 1 . . . . 68 LEU CA . 18543 1 208 . 1 1 68 68 LEU CB C 13 42.377 0.30 . 1 . . . . 68 LEU CB . 18543 1 209 . 1 1 68 68 LEU CG C 13 27.309 0.30 . 1 . . . . 68 LEU CG . 18543 1 210 . 1 1 68 68 LEU N N 15 120.300 0.30 . 1 . . . . 68 LEU N . 18543 1 211 . 1 1 69 69 GLY C C 13 176.007 0.30 . 1 . . . . 69 GLY C . 18543 1 212 . 1 1 69 69 GLY CA C 13 48.134 0.30 . 1 . . . . 69 GLY CA . 18543 1 213 . 1 1 69 69 GLY N N 15 106.875 0.30 . 1 . . . . 69 GLY N . 18543 1 214 . 1 1 70 70 LYS CA C 13 59.800 0.30 . 1 . . . . 70 LYS CA . 18543 1 215 . 1 1 70 70 LYS CG C 13 25.300 0.30 . 1 . . . . 70 LYS CG . 18543 1 216 . 1 1 70 70 LYS N N 15 121.113 0.30 . 1 . . . . 70 LYS N . 18543 1 217 . 1 1 72 72 LEU CB C 13 42.505 0.30 . 1 . . . . 72 LEU CB . 18543 1 218 . 1 1 72 72 LEU CG C 13 28.272 0.30 . 1 . . . . 72 LEU CG . 18543 1 219 . 1 1 73 73 THR C C 13 176.502 0.30 . 1 . . . . 73 THR C . 18543 1 220 . 1 1 73 73 THR CA C 13 67.105 0.30 . 1 . . . . 73 THR CA . 18543 1 221 . 1 1 73 73 THR CB C 13 68.438 0.30 . 1 . . . . 73 THR CB . 18543 1 222 . 1 1 73 73 THR CG2 C 13 22.447 0.30 . 1 . . . . 73 THR CG2 . 18543 1 223 . 1 1 73 73 THR N N 15 119.711 0.30 . 1 . . . . 73 THR N . 18543 1 224 . 1 1 74 74 GLN C C 13 177.512 0.30 . 1 . . . . 74 GLN C . 18543 1 225 . 1 1 74 74 GLN CA C 13 59.465 0.30 . 1 . . . . 74 GLN CA . 18543 1 226 . 1 1 74 74 GLN CB C 13 25.947 0.30 . 1 . . . . 74 GLN CB . 18543 1 227 . 1 1 74 74 GLN CG C 13 30.989 0.30 . 1 . . . . 74 GLN CG . 18543 1 228 . 1 1 74 74 GLN CD C 13 177.356 0.30 . 1 . . . . 74 GLN CD . 18543 1 229 . 1 1 74 74 GLN N N 15 125.222 0.30 . 1 . . . . 74 GLN N . 18543 1 230 . 1 1 74 74 GLN NE2 N 15 107.938 0.30 . 1 . . . . 74 GLN NE2 . 18543 1 231 . 1 1 75 75 ALA C C 13 179.736 0.30 . 1 . . . . 75 ALA C . 18543 1 232 . 1 1 75 75 ALA CA C 13 54.856 0.30 . 1 . . . . 75 ALA CA . 18543 1 233 . 1 1 75 75 ALA CB C 13 20.057 0.30 . 1 . . . . 75 ALA CB . 18543 1 234 . 1 1 75 75 ALA N N 15 123.350 0.30 . 1 . . . . 75 ALA N . 18543 1 235 . 1 1 76 76 TRP C C 13 177.913 0.30 . 1 . . . . 76 TRP C . 18543 1 236 . 1 1 76 76 TRP CA C 13 59.249 0.30 . 1 . . . . 76 TRP CA . 18543 1 237 . 1 1 76 76 TRP CB C 13 29.371 0.30 . 1 . . . . 76 TRP CB . 18543 1 238 . 1 1 76 76 TRP N N 15 120.686 0.30 . 1 . . . . 76 TRP N . 18543 1 239 . 1 1 77 77 ALA C C 13 178.995 0.30 . 1 . . . . 77 ALA C . 18543 1 240 . 1 1 77 77 ALA CA C 13 55.110 0.30 . 1 . . . . 77 ALA CA . 18543 1 241 . 1 1 77 77 ALA CB C 13 20.271 0.30 . 1 . . . . 77 ALA CB . 18543 1 242 . 1 1 77 77 ALA N N 15 120.437 0.30 . 1 . . . . 77 ALA N . 18543 1 243 . 1 1 78 78 VAL C C 13 177.465 0.30 . 1 . . . . 78 VAL C . 18543 1 244 . 1 1 78 78 VAL CA C 13 67.215 0.30 . 1 . . . . 78 VAL CA . 18543 1 245 . 1 1 78 78 VAL CB C 13 30.271 0.30 . 1 . . . . 78 VAL CB . 18543 1 246 . 1 1 78 78 VAL CG1 C 13 23.754 0.30 . 2 . . . . 78 VAL CG1 . 18543 1 247 . 1 1 78 78 VAL CG2 C 13 22.314 0.30 . 2 . . . . 78 VAL CG2 . 18543 1 248 . 1 1 78 78 VAL N N 15 119.708 0.30 . 1 . . . . 78 VAL N . 18543 1 249 . 1 1 79 79 ALA C C 13 179.909 0.30 . 1 . . . . 79 ALA C . 18543 1 250 . 1 1 79 79 ALA CA C 13 54.954 0.30 . 1 . . . . 79 ALA CA . 18543 1 251 . 1 1 79 79 ALA CB C 13 17.777 0.30 . 1 . . . . 79 ALA CB . 18543 1 252 . 1 1 79 79 ALA N N 15 121.045 0.30 . 1 . . . . 79 ALA N . 18543 1 253 . 1 1 80 80 MET C C 13 179.384 0.30 . 1 . . . . 80 MET C . 18543 1 254 . 1 1 80 80 MET CA C 13 58.561 0.30 . 1 . . . . 80 MET CA . 18543 1 255 . 1 1 80 80 MET CB C 13 34.424 0.30 . 1 . . . . 80 MET CB . 18543 1 256 . 1 1 80 80 MET CG C 13 31.166 0.30 . 1 . . . . 80 MET CG . 18543 1 257 . 1 1 80 80 MET N N 15 115.866 0.30 . 1 . . . . 80 MET N . 18543 1 258 . 1 1 81 81 ALA C C 13 180.077 0.30 . 1 . . . . 81 ALA C . 18543 1 259 . 1 1 81 81 ALA CA C 13 54.659 0.30 . 1 . . . . 81 ALA CA . 18543 1 260 . 1 1 81 81 ALA CB C 13 18.093 0.30 . 1 . . . . 81 ALA CB . 18543 1 261 . 1 1 81 81 ALA N N 15 123.576 0.30 . 1 . . . . 81 ALA N . 18543 1 262 . 1 1 82 82 LEU C C 13 177.539 0.30 . 1 . . . . 82 LEU C . 18543 1 263 . 1 1 82 82 LEU CA C 13 54.567 0.30 . 1 . . . . 82 LEU CA . 18543 1 264 . 1 1 82 82 LEU CB C 13 43.050 0.30 . 1 . . . . 82 LEU CB . 18543 1 265 . 1 1 82 82 LEU CG C 13 26.746 0.30 . 1 . . . . 82 LEU CG . 18543 1 266 . 1 1 82 82 LEU CD1 C 13 21.965 0.30 . 1 . . . . 82 LEU CD . 18543 1 267 . 1 1 82 82 LEU CD2 C 13 21.965 0.30 . 1 . . . . 82 LEU CD . 18543 1 268 . 1 1 82 82 LEU N N 15 113.424 0.30 . 1 . . . . 82 LEU N . 18543 1 269 . 1 1 83 83 GLY C C 13 176.806 0.30 . 1 . . . . 83 GLY C . 18543 1 270 . 1 1 83 83 GLY CA C 13 47.162 0.30 . 1 . . . . 83 GLY CA . 18543 1 271 . 1 1 83 83 GLY N N 15 110.919 0.30 . 1 . . . . 83 GLY N . 18543 1 272 . 1 1 84 84 VAL C C 13 176.659 0.30 . 1 . . . . 84 VAL C . 18543 1 273 . 1 1 84 84 VAL CA C 13 59.287 0.30 . 1 . . . . 84 VAL CA . 18543 1 274 . 1 1 84 84 VAL CB C 13 31.548 0.30 . 1 . . . . 84 VAL CB . 18543 1 275 . 1 1 84 84 VAL CG1 C 13 20.423 0.30 . 2 . . . . 84 VAL CG1 . 18543 1 276 . 1 1 84 84 VAL CG2 C 13 19.175 0.30 . 2 . . . . 84 VAL CG2 . 18543 1 277 . 1 1 84 84 VAL N N 15 108.499 0.30 . 1 . . . . 84 VAL N . 18543 1 278 . 1 1 85 85 GLU C C 13 179.571 0.30 . 1 . . . . 85 GLU C . 18543 1 279 . 1 1 85 85 GLU CA C 13 61.714 0.30 . 1 . . . . 85 GLU CA . 18543 1 280 . 1 1 85 85 GLU CB C 13 29.523 0.30 . 1 . . . . 85 GLU CB . 18543 1 281 . 1 1 85 85 GLU CG C 13 36.201 0.30 . 1 . . . . 85 GLU CG . 18543 1 282 . 1 1 85 85 GLU CD C 13 183.923 0.30 . 1 . . . . 85 GLU CD . 18543 1 283 . 1 1 85 85 GLU N N 15 126.358 0.30 . 1 . . . . 85 GLU N . 18543 1 284 . 1 1 86 86 ASP C C 13 177.332 0.30 . 1 . . . . 86 ASP C . 18543 1 285 . 1 1 86 86 ASP CA C 13 56.098 0.30 . 1 . . . . 86 ASP CA . 18543 1 286 . 1 1 86 86 ASP CB C 13 39.714 0.30 . 1 . . . . 86 ASP CB . 18543 1 287 . 1 1 86 86 ASP CG C 13 180.132 0.30 . 1 . . . . 86 ASP CG . 18543 1 288 . 1 1 86 86 ASP N N 15 116.172 0.30 . 1 . . . . 86 ASP N . 18543 1 289 . 1 1 87 87 LYS C C 13 177.969 0.30 . 1 . . . . 87 LYS C . 18543 1 290 . 1 1 87 87 LYS CA C 13 57.262 0.30 . 1 . . . . 87 LYS CA . 18543 1 291 . 1 1 87 87 LYS CB C 13 34.053 0.30 . 1 . . . . 87 LYS CB . 18543 1 292 . 1 1 87 87 LYS CG C 13 25.164 0.30 . 1 . . . . 87 LYS CG . 18543 1 293 . 1 1 87 87 LYS CD C 13 29.327 0.30 . 1 . . . . 87 LYS CD . 18543 1 294 . 1 1 87 87 LYS CE C 13 39.843 0.30 . 1 . . . . 87 LYS CE . 18543 1 295 . 1 1 87 87 LYS N N 15 117.216 0.30 . 1 . . . . 87 LYS N . 18543 1 296 . 1 1 88 88 VAL C C 13 176.109 0.30 . 1 . . . . 88 VAL C . 18543 1 297 . 1 1 88 88 VAL CA C 13 60.914 0.30 . 1 . . . . 88 VAL CA . 18543 1 298 . 1 1 88 88 VAL CB C 13 32.866 0.30 . 1 . . . . 88 VAL CB . 18543 1 299 . 1 1 88 88 VAL CG1 C 13 19.422 0.30 . 2 . . . . 88 VAL CG1 . 18543 1 300 . 1 1 88 88 VAL CG2 C 13 17.633 0.30 . 2 . . . . 88 VAL CG2 . 18543 1 301 . 1 1 88 88 VAL N N 15 103.704 0.30 . 1 . . . . 88 VAL N . 18543 1 302 . 1 1 89 89 THR C C 13 175.041 0.30 . 1 . . . . 89 THR C . 18543 1 303 . 1 1 89 89 THR CA C 13 69.428 0.30 . 1 . . . . 89 THR CA . 18543 1 304 . 1 1 89 89 THR CB C 13 69.707 0.30 . 1 . . . . 89 THR CB . 18543 1 305 . 1 1 89 89 THR CG2 C 13 21.382 0.30 . 1 . . . . 89 THR CG2 . 18543 1 306 . 1 1 89 89 THR N N 15 120.153 0.30 . 1 . . . . 89 THR N . 18543 1 307 . 1 1 90 90 VAL C C 13 175.895 0.30 . 1 . . . . 90 VAL C . 18543 1 308 . 1 1 90 90 VAL CA C 13 69.172 0.30 . 1 . . . . 90 VAL CA . 18543 1 309 . 1 1 90 90 VAL CB C 13 28.841 0.30 . 1 . . . . 90 VAL CB . 18543 1 310 . 1 1 90 90 VAL CG1 C 13 24.254 0.30 . 2 . . . . 90 VAL CG1 . 18543 1 311 . 1 1 90 90 VAL CG2 C 13 21.419 0.30 . 2 . . . . 90 VAL CG2 . 18543 1 312 . 1 1 90 90 VAL N N 15 120.200 0.30 . 1 . . . . 90 VAL N . 18543 1 313 . 1 1 91 91 PRO CA C 13 65.686 0.30 . 1 . . . . 91 PRO CA . 18543 1 314 . 1 1 91 91 PRO CB C 13 31.589 0.30 . 1 . . . . 91 PRO CB . 18543 1 315 . 1 1 91 91 PRO CG C 13 27.811 0.30 . 1 . . . . 91 PRO CG . 18543 1 316 . 1 1 91 91 PRO CD C 13 49.104 0.30 . 1 . . . . 91 PRO CD . 18543 1 317 . 1 1 91 91 PRO N N 15 134.100 0.30 . 1 . . . . 91 PRO N . 18543 1 318 . 1 1 92 92 LEU C C 13 177.880 0.30 . 1 . . . . 92 LEU C . 18543 1 319 . 1 1 92 92 LEU CA C 13 57.941 0.30 . 1 . . . . 92 LEU CA . 18543 1 320 . 1 1 92 92 LEU CB C 13 40.794 0.30 . 1 . . . . 92 LEU CB . 18543 1 321 . 1 1 92 92 LEU CG C 13 27.025 0.30 . 1 . . . . 92 LEU CG . 18543 1 322 . 1 1 92 92 LEU CD1 C 13 23.053 0.30 . 1 . . . . 92 LEU CD . 18543 1 323 . 1 1 92 92 LEU CD2 C 13 23.053 0.30 . 1 . . . . 92 LEU CD . 18543 1 324 . 1 1 92 92 LEU N N 15 120.185 0.30 . 1 . . . . 92 LEU N . 18543 1 325 . 1 1 94 94 GLU C C 13 180.303 0.30 . 1 . . . . 94 GLU C . 18543 1 326 . 1 1 94 94 GLU CA C 13 59.535 0.30 . 1 . . . . 94 GLU CA . 18543 1 327 . 1 1 94 94 GLU CB C 13 29.558 0.30 . 1 . . . . 94 GLU CB . 18543 1 328 . 1 1 94 94 GLU CD C 13 177.439 0.30 . 1 . . . . 94 GLU CD . 18543 1 329 . 1 1 94 94 GLU N N 15 115.917 0.30 . 1 . . . . 94 GLU N . 18543 1 330 . 1 1 95 95 GLY C C 13 175.813 0.30 . 1 . . . . 95 GLY C . 18543 1 331 . 1 1 95 95 GLY CA C 13 46.435 0.30 . 1 . . . . 95 GLY CA . 18543 1 332 . 1 1 95 95 GLY N N 15 107.985 0.30 . 1 . . . . 95 GLY N . 18543 1 333 . 1 1 96 96 VAL C C 13 177.899 0.30 . 1 . . . . 96 VAL C . 18543 1 334 . 1 1 96 96 VAL CA C 13 66.431 0.30 . 1 . . . . 96 VAL CA . 18543 1 335 . 1 1 96 96 VAL CB C 13 32.022 0.30 . 1 . . . . 96 VAL CB . 18543 1 336 . 1 1 96 96 VAL CG1 C 13 23.486 0.30 . 2 . . . . 96 VAL CG1 . 18543 1 337 . 1 1 96 96 VAL CG2 C 13 21.612 0.30 . 2 . . . . 96 VAL CG2 . 18543 1 338 . 1 1 96 96 VAL N N 15 119.865 0.30 . 1 . . . . 96 VAL N . 18543 1 339 . 1 1 97 97 GLN CA C 13 54.900 0.30 . 1 . . . . 97 GLN CA . 18543 1 340 . 1 1 97 97 GLN CD C 13 172.000 0.30 . 1 . . . . 97 GLN CD . 18543 1 341 . 1 1 97 97 GLN NE2 N 15 111.200 0.30 . 1 . . . . 97 GLN NE2 . 18543 1 342 . 1 1 99 99 THR C C 13 175.705 0.30 . 1 . . . . 99 THR C . 18543 1 343 . 1 1 99 99 THR CA C 13 62.151 0.30 . 1 . . . . 99 THR CA . 18543 1 344 . 1 1 99 99 THR CB C 13 68.734 0.30 . 1 . . . . 99 THR CB . 18543 1 345 . 1 1 99 99 THR CG2 C 13 22.288 0.30 . 1 . . . . 99 THR CG2 . 18543 1 346 . 1 1 99 99 THR N N 15 107.814 0.30 . 1 . . . . 99 THR N . 18543 1 347 . 1 1 100 100 GLN C C 13 175.203 0.30 . 1 . . . . 100 GLN C . 18543 1 348 . 1 1 100 100 GLN CA C 13 57.492 0.30 . 1 . . . . 100 GLN CA . 18543 1 349 . 1 1 100 100 GLN CB C 13 25.782 0.30 . 1 . . . . 100 GLN CB . 18543 1 350 . 1 1 100 100 GLN CG C 13 34.391 0.30 . 1 . . . . 100 GLN CG . 18543 1 351 . 1 1 100 100 GLN CD C 13 180.725 0.30 . 1 . . . . 100 GLN CD . 18543 1 352 . 1 1 100 100 GLN N N 15 114.569 0.30 . 1 . . . . 100 GLN N . 18543 1 353 . 1 1 101 101 THR C C 13 175.507 0.30 . 1 . . . . 101 THR C . 18543 1 354 . 1 1 101 101 THR CA C 13 60.965 0.30 . 1 . . . . 101 THR CA . 18543 1 355 . 1 1 101 101 THR CB C 13 68.644 0.30 . 1 . . . . 101 THR CB . 18543 1 356 . 1 1 101 101 THR CG2 C 13 22.759 0.30 . 1 . . . . 101 THR CG2 . 18543 1 357 . 1 1 101 101 THR N N 15 105.838 0.30 . 1 . . . . 101 THR N . 18543 1 358 . 1 1 102 102 ILE C C 13 174.014 0.30 . 1 . . . . 102 ILE C . 18543 1 359 . 1 1 102 102 ILE CA C 13 60.761 0.30 . 1 . . . . 102 ILE CA . 18543 1 360 . 1 1 102 102 ILE CB C 13 37.116 0.30 . 1 . . . . 102 ILE CB . 18543 1 361 . 1 1 102 102 ILE CG1 C 13 27.128 0.30 . 1 . . . . 102 ILE CG1 . 18543 1 362 . 1 1 102 102 ILE CG2 C 13 17.441 0.30 . 1 . . . . 102 ILE CG2 . 18543 1 363 . 1 1 102 102 ILE CD1 C 13 14.586 0.30 . 1 . . . . 102 ILE CD1 . 18543 1 364 . 1 1 102 102 ILE N N 15 121.067 0.30 . 1 . . . . 102 ILE N . 18543 1 365 . 1 1 103 103 ARG C C 13 175.372 0.30 . 1 . . . . 103 ARG C . 18543 1 366 . 1 1 103 103 ARG CA C 13 55.146 0.30 . 1 . . . . 103 ARG CA . 18543 1 367 . 1 1 103 103 ARG CB C 13 32.428 0.30 . 1 . . . . 103 ARG CB . 18543 1 368 . 1 1 103 103 ARG CG C 13 27.045 0.30 . 1 . . . . 103 ARG CG . 18543 1 369 . 1 1 103 103 ARG N N 15 125.864 0.30 . 1 . . . . 103 ARG N . 18543 1 370 . 1 1 104 104 SER C C 13 174.454 0.30 . 1 . . . . 104 SER C . 18543 1 371 . 1 1 104 104 SER CA C 13 56.762 0.30 . 1 . . . . 104 SER CA . 18543 1 372 . 1 1 104 104 SER CB C 13 67.126 0.30 . 1 . . . . 104 SER CB . 18543 1 373 . 1 1 104 104 SER N N 15 114.873 0.30 . 1 . . . . 104 SER N . 18543 1 374 . 1 1 105 105 ALA C C 13 180.877 0.30 . 1 . . . . 105 ALA C . 18543 1 375 . 1 1 105 105 ALA CA C 13 55.250 0.30 . 1 . . . . 105 ALA CA . 18543 1 376 . 1 1 105 105 ALA CB C 13 17.033 0.30 . 1 . . . . 105 ALA CB . 18543 1 377 . 1 1 105 105 ALA N N 15 123.572 0.30 . 1 . . . . 105 ALA N . 18543 1 378 . 1 1 106 106 SER C C 13 176.280 0.30 . 1 . . . . 106 SER C . 18543 1 379 . 1 1 106 106 SER CA C 13 61.351 0.30 . 1 . . . . 106 SER CA . 18543 1 380 . 1 1 106 106 SER CB C 13 62.196 0.30 . 1 . . . . 106 SER CB . 18543 1 381 . 1 1 106 106 SER N N 15 115.731 0.30 . 1 . . . . 106 SER N . 18543 1 382 . 1 1 107 107 ASP C C 13 179.080 0.30 . 1 . . . . 107 ASP C . 18543 1 383 . 1 1 107 107 ASP CA C 13 57.070 0.30 . 1 . . . . 107 ASP CA . 18543 1 384 . 1 1 107 107 ASP CB C 13 42.577 0.30 . 1 . . . . 107 ASP CB . 18543 1 385 . 1 1 107 107 ASP N N 15 120.249 0.30 . 1 . . . . 107 ASP N . 18543 1 386 . 1 1 108 108 ILE C C 13 176.989 0.30 . 1 . . . . 108 ILE C . 18543 1 387 . 1 1 108 108 ILE CA C 13 65.825 0.30 . 1 . . . . 108 ILE CA . 18543 1 388 . 1 1 108 108 ILE CB C 13 38.163 0.30 . 1 . . . . 108 ILE CB . 18543 1 389 . 1 1 108 108 ILE CG1 C 13 28.922 0.30 . 1 . . . . 108 ILE CG1 . 18543 1 390 . 1 1 108 108 ILE CG2 C 13 18.646 0.30 . 1 . . . . 108 ILE CG2 . 18543 1 391 . 1 1 108 108 ILE CD1 C 13 15.220 0.30 . 1 . . . . 108 ILE CD1 . 18543 1 392 . 1 1 108 108 ILE N N 15 119.990 0.30 . 1 . . . . 108 ILE N . 18543 1 393 . 1 1 109 109 ARG CA C 13 59.572 0.30 . 1 . . . . 109 ARG CA . 18543 1 394 . 1 1 109 109 ARG CD C 13 43.310 0.30 . 1 . . . . 109 ARG CD . 18543 1 395 . 1 1 110 110 ASP C C 13 179.249 0.30 . 1 . . . . 110 ASP C . 18543 1 396 . 1 1 110 110 ASP CA C 13 57.586 0.30 . 1 . . . . 110 ASP CA . 18543 1 397 . 1 1 110 110 ASP CB C 13 40.187 0.30 . 1 . . . . 110 ASP CB . 18543 1 398 . 1 1 110 110 ASP N N 15 117.237 0.30 . 1 . . . . 110 ASP N . 18543 1 399 . 1 1 111 111 VAL C C 13 179.159 0.30 . 1 . . . . 111 VAL C . 18543 1 400 . 1 1 111 111 VAL CA C 13 66.436 0.30 . 1 . . . . 111 VAL CA . 18543 1 401 . 1 1 111 111 VAL CB C 13 30.900 0.30 . 1 . . . . 111 VAL CB . 18543 1 402 . 1 1 111 111 VAL CG1 C 13 23.513 0.30 . 2 . . . . 111 VAL CG1 . 18543 1 403 . 1 1 111 111 VAL CG2 C 13 21.665 0.30 . 2 . . . . 111 VAL CG2 . 18543 1 404 . 1 1 111 111 VAL N N 15 120.156 0.30 . 1 . . . . 111 VAL N . 18543 1 405 . 1 1 113 113 ILE C C 13 182.271 0.30 . 1 . . . . 113 ILE C . 18543 1 406 . 1 1 113 113 ILE CA C 13 63.548 0.30 . 1 . . . . 113 ILE CA . 18543 1 407 . 1 1 113 113 ILE CB C 13 37.765 0.30 . 1 . . . . 113 ILE CB . 18543 1 408 . 1 1 113 113 ILE CG1 C 13 28.265 0.30 . 1 . . . . 113 ILE CG1 . 18543 1 409 . 1 1 113 113 ILE CG2 C 13 17.400 0.30 . 1 . . . . 113 ILE CG2 . 18543 1 410 . 1 1 113 113 ILE CD1 C 13 13.433 0.30 . 1 . . . . 113 ILE CD1 . 18543 1 411 . 1 1 113 113 ILE N N 15 122.071 0.30 . 1 . . . . 113 ILE N . 18543 1 412 . 1 1 114 114 ASN CA C 13 55.576 0.30 . 1 . . . . 114 ASN CA . 18543 1 413 . 1 1 114 114 ASN CB C 13 38.057 0.30 . 1 . . . . 114 ASN CB . 18543 1 414 . 1 1 114 114 ASN N N 15 120.304 0.30 . 1 . . . . 114 ASN N . 18543 1 415 . 1 1 115 115 ALA C C 13 176.949 0.30 . 1 . . . . 115 ALA C . 18543 1 416 . 1 1 115 115 ALA CA C 13 51.865 0.30 . 1 . . . . 115 ALA CA . 18543 1 417 . 1 1 115 115 ALA CB C 13 18.661 0.30 . 1 . . . . 115 ALA CB . 18543 1 418 . 1 1 115 115 ALA N N 15 120.866 0.30 . 1 . . . . 115 ALA N . 18543 1 419 . 1 1 116 116 GLY C C 13 173.774 0.30 . 1 . . . . 116 GLY C . 18543 1 420 . 1 1 116 116 GLY CA C 13 45.142 0.30 . 1 . . . . 116 GLY CA . 18543 1 421 . 1 1 116 116 GLY N N 15 105.391 0.30 . 1 . . . . 116 GLY N . 18543 1 422 . 1 1 117 117 ILE C C 13 175.152 0.30 . 1 . . . . 117 ILE C . 18543 1 423 . 1 1 117 117 ILE CA C 13 60.823 0.30 . 1 . . . . 117 ILE CA . 18543 1 424 . 1 1 117 117 ILE CB C 13 37.462 0.30 . 1 . . . . 117 ILE CB . 18543 1 425 . 1 1 117 117 ILE CG1 C 13 25.753 0.30 . 1 . . . . 117 ILE CG1 . 18543 1 426 . 1 1 117 117 ILE CG2 C 13 20.574 0.30 . 1 . . . . 117 ILE CG2 . 18543 1 427 . 1 1 117 117 ILE CD1 C 13 14.704 0.30 . 1 . . . . 117 ILE CD1 . 18543 1 428 . 1 1 117 117 ILE N N 15 125.335 0.30 . 1 . . . . 117 ILE N . 18543 1 429 . 1 1 118 118 LYS C C 13 179.153 0.30 . 1 . . . . 118 LYS C . 18543 1 430 . 1 1 118 118 LYS CA C 13 56.654 0.30 . 1 . . . . 118 LYS CA . 18543 1 431 . 1 1 118 118 LYS CB C 13 32.499 0.30 . 1 . . . . 118 LYS CB . 18543 1 432 . 1 1 118 118 LYS CG C 13 25.457 0.30 . 1 . . . . 118 LYS CG . 18543 1 433 . 1 1 118 118 LYS N N 15 126.118 0.30 . 1 . . . . 118 LYS N . 18543 1 434 . 1 1 119 119 GLY C C 13 175.015 0.30 . 1 . . . . 119 GLY C . 18543 1 435 . 1 1 119 119 GLY CA C 13 48.213 0.30 . 1 . . . . 119 GLY CA . 18543 1 436 . 1 1 119 119 GLY N N 15 113.905 0.30 . 1 . . . . 119 GLY N . 18543 1 437 . 1 1 120 120 GLU CA C 13 59.581 0.30 . 1 . . . . 120 GLU CA . 18543 1 438 . 1 1 120 120 GLU CB C 13 28.966 0.30 . 1 . . . . 120 GLU CB . 18543 1 439 . 1 1 120 120 GLU N N 15 117.303 0.30 . 1 . . . . 120 GLU N . 18543 1 440 . 1 1 123 123 ASP C C 13 179.880 0.30 . 1 . . . . 123 ASP C . 18543 1 441 . 1 1 123 123 ASP CA C 13 57.366 0.30 . 1 . . . . 123 ASP CA . 18543 1 442 . 1 1 123 123 ASP CB C 13 39.742 0.30 . 1 . . . . 123 ASP CB . 18543 1 443 . 1 1 123 123 ASP N N 15 118.922 0.30 . 1 . . . . 123 ASP N . 18543 1 444 . 1 1 124 124 ALA C C 13 181.181 0.30 . 1 . . . . 124 ALA C . 18543 1 445 . 1 1 124 124 ALA CA C 13 54.643 0.30 . 1 . . . . 124 ALA CA . 18543 1 446 . 1 1 124 124 ALA CB C 13 18.159 0.30 . 1 . . . . 124 ALA CB . 18543 1 447 . 1 1 124 124 ALA N N 15 121.027 0.30 . 1 . . . . 124 ALA N . 18543 1 448 . 1 1 125 125 ALA C C 13 181.029 0.30 . 1 . . . . 125 ALA C . 18543 1 449 . 1 1 125 125 ALA CA C 13 54.921 0.30 . 1 . . . . 125 ALA CA . 18543 1 450 . 1 1 125 125 ALA CB C 13 18.452 0.30 . 1 . . . . 125 ALA CB . 18543 1 451 . 1 1 125 125 ALA N N 15 119.653 0.30 . 1 . . . . 125 ALA N . 18543 1 452 . 1 1 126 126 TRP C C 13 175.882 0.30 . 1 . . . . 126 TRP C . 18543 1 453 . 1 1 126 126 TRP CA C 13 61.166 0.30 . 1 . . . . 126 TRP CA . 18543 1 454 . 1 1 127 127 ASN C C 13 174.615 0.30 . 1 . . . . 127 ASN C . 18543 1 455 . 1 1 127 127 ASN CA C 13 53.188 0.30 . 1 . . . . 127 ASN CA . 18543 1 456 . 1 1 127 127 ASN CB C 13 40.156 0.30 . 1 . . . . 127 ASN CB . 18543 1 457 . 1 1 127 127 ASN CG C 13 177.557 0.30 . 1 . . . . 127 ASN CG . 18543 1 458 . 1 1 127 127 ASN N N 15 110.518 0.30 . 1 . . . . 127 ASN N . 18543 1 459 . 1 1 128 128 SER C C 13 175.614 0.30 . 1 . . . . 128 SER C . 18543 1 460 . 1 1 128 128 SER CA C 13 59.100 0.30 . 1 . . . . 128 SER CA . 18543 1 461 . 1 1 128 128 SER CB C 13 65.612 0.30 . 1 . . . . 128 SER CB . 18543 1 462 . 1 1 128 128 SER N N 15 116.107 0.30 . 1 . . . . 128 SER N . 18543 1 463 . 1 1 130 130 VAL CA C 13 67.100 0.30 . 1 . . . . 130 VAL CA . 18543 1 464 . 1 1 131 131 VAL C C 13 177.700 0.30 . 1 . . . . 131 VAL C . 18543 1 465 . 1 1 131 131 VAL CA C 13 66.969 0.30 . 1 . . . . 131 VAL CA . 18543 1 466 . 1 1 131 131 VAL CB C 13 31.529 0.30 . 1 . . . . 131 VAL CB . 18543 1 467 . 1 1 131 131 VAL CG1 C 13 24.200 0.30 . 2 . . . . 131 VAL CG1 . 18543 1 468 . 1 1 131 131 VAL CG2 C 13 22.900 0.30 . 2 . . . . 131 VAL CG2 . 18543 1 469 . 1 1 131 131 VAL N N 15 120.594 0.30 . 1 . . . . 131 VAL N . 18543 1 470 . 1 1 133 133 SER CA C 13 61.228 0.30 . 1 . . . . 133 SER CA . 18543 1 471 . 1 1 133 133 SER CB C 13 62.422 0.30 . 1 . . . . 133 SER CB . 18543 1 472 . 1 1 134 134 LEU C C 13 181.386 0.30 . 1 . . . . 134 LEU C . 18543 1 473 . 1 1 134 134 LEU CA C 13 57.596 0.30 . 1 . . . . 134 LEU CA . 18543 1 474 . 1 1 134 134 LEU CB C 13 43.960 0.30 . 1 . . . . 134 LEU CB . 18543 1 475 . 1 1 134 134 LEU CG C 13 27.321 0.30 . 1 . . . . 134 LEU CG . 18543 1 476 . 1 1 134 134 LEU CD1 C 13 22.897 0.30 . 1 . . . . 134 LEU CD1 . 18543 1 477 . 1 1 134 134 LEU CD2 C 13 26.172 0.30 . 2 . . . . 134 LEU CD2 . 18543 1 478 . 1 1 134 134 LEU N N 15 123.770 0.30 . 1 . . . . 134 LEU N . 18543 1 479 . 1 1 135 135 VAL C C 13 177.053 0.30 . 1 . . . . 135 VAL C . 18543 1 480 . 1 1 135 135 VAL CA C 13 68.960 0.30 . 1 . . . . 135 VAL CA . 18543 1 481 . 1 1 135 135 VAL CB C 13 31.380 0.30 . 1 . . . . 135 VAL CB . 18543 1 482 . 1 1 135 135 VAL CG1 C 13 23.797 0.30 . 2 . . . . 135 VAL CG1 . 18543 1 483 . 1 1 135 135 VAL CG2 C 13 20.951 0.30 . 2 . . . . 135 VAL CG2 . 18543 1 484 . 1 1 135 135 VAL N N 15 123.151 0.30 . 1 . . . . 135 VAL N . 18543 1 485 . 1 1 136 136 ALA C C 13 181.298 0.30 . 1 . . . . 136 ALA C . 18543 1 486 . 1 1 136 136 ALA CA C 13 54.941 0.30 . 1 . . . . 136 ALA CA . 18543 1 487 . 1 1 136 136 ALA CB C 13 17.751 0.30 . 1 . . . . 136 ALA CB . 18543 1 488 . 1 1 136 136 ALA N N 15 121.086 0.30 . 1 . . . . 136 ALA N . 18543 1 489 . 1 1 137 137 GLN C C 13 179.218 0.30 . 1 . . . . 137 GLN C . 18543 1 490 . 1 1 137 137 GLN CA C 13 59.150 0.30 . 1 . . . . 137 GLN CA . 18543 1 491 . 1 1 137 137 GLN CB C 13 29.480 0.30 . 1 . . . . 137 GLN CB . 18543 1 492 . 1 1 137 137 GLN N N 15 118.446 0.30 . 1 . . . . 137 GLN N . 18543 1 493 . 1 1 140 140 LYS CA C 13 58.811 0.30 . 1 . . . . 140 LYS CA . 18543 1 494 . 1 1 140 140 LYS CB C 13 32.872 0.30 . 1 . . . . 140 LYS CB . 18543 1 495 . 1 1 140 140 LYS CG C 13 24.819 0.30 . 1 . . . . 140 LYS CG . 18543 1 496 . 1 1 140 140 LYS CD C 13 36.425 0.30 . 1 . . . . 140 LYS CD . 18543 1 497 . 1 1 140 140 LYS CE C 13 42.366 0.30 . 1 . . . . 140 LYS CE . 18543 1 498 . 1 1 140 140 LYS N N 15 122.187 0.30 . 1 . . . . 140 LYS N . 18543 1 499 . 1 1 141 141 ALA C C 13 179.440 0.30 . 1 . . . . 141 ALA C . 18543 1 500 . 1 1 141 141 ALA CA C 13 54.832 0.30 . 1 . . . . 141 ALA CA . 18543 1 501 . 1 1 141 141 ALA CB C 13 18.298 0.30 . 1 . . . . 141 ALA CB . 18543 1 502 . 1 1 142 142 ALA C C 13 178.825 0.30 . 1 . . . . 142 ALA C . 18543 1 503 . 1 1 142 142 ALA CA C 13 54.523 0.30 . 1 . . . . 142 ALA CA . 18543 1 504 . 1 1 142 142 ALA CB C 13 17.889 0.30 . 1 . . . . 142 ALA CB . 18543 1 505 . 1 1 142 142 ALA N N 15 116.973 0.30 . 1 . . . . 142 ALA N . 18543 1 506 . 1 1 143 143 ALA CA C 13 54.374 0.30 . 1 . . . . 143 ALA CA . 18543 1 507 . 1 1 143 143 ALA CB C 13 17.953 0.30 . 1 . . . . 143 ALA CB . 18543 1 508 . 1 1 143 143 ALA N N 15 120.256 0.30 . 1 . . . . 143 ALA N . 18543 1 509 . 1 1 144 144 ASP C C 13 178.286 0.30 . 1 . . . . 144 ASP C . 18543 1 510 . 1 1 144 144 ASP CA C 13 57.117 0.30 . 1 . . . . 144 ASP CA . 18543 1 511 . 1 1 144 144 ASP CB C 13 40.034 0.30 . 1 . . . . 144 ASP CB . 18543 1 512 . 1 1 145 145 VAL C C 13 174.268 0.30 . 1 . . . . 145 VAL C . 18543 1 513 . 1 1 145 145 VAL CA C 13 60.381 0.30 . 1 . . . . 145 VAL CA . 18543 1 514 . 1 1 145 145 VAL CB C 13 30.887 0.30 . 1 . . . . 145 VAL CB . 18543 1 515 . 1 1 145 145 VAL CG1 C 13 20.072 0.30 . 2 . . . . 145 VAL CG1 . 18543 1 516 . 1 1 145 145 VAL CG2 C 13 19.130 0.30 . 2 . . . . 145 VAL CG2 . 18543 1 517 . 1 1 145 145 VAL N N 15 108.467 0.30 . 1 . . . . 145 VAL N . 18543 1 518 . 1 1 146 146 GLN C C 13 175.328 0.30 . 1 . . . . 146 GLN C . 18543 1 519 . 1 1 146 146 GLN CA C 13 56.006 0.30 . 1 . . . . 146 GLN CA . 18543 1 520 . 1 1 147 147 LEU CB C 13 43.032 0.30 . 1 . . . . 147 LEU CB . 18543 1 521 . 1 1 147 147 LEU CG C 13 26.963 0.30 . 1 . . . . 147 LEU CG . 18543 1 522 . 1 1 148 148 ARG C C 13 175.716 0.30 . 1 . . . . 148 ARG C . 18543 1 523 . 1 1 148 148 ARG CA C 13 54.630 0.30 . 1 . . . . 148 ARG CA . 18543 1 524 . 1 1 148 148 ARG CB C 13 31.844 0.30 . 1 . . . . 148 ARG CB . 18543 1 525 . 1 1 149 149 GLY C C 13 170.860 0.30 . 1 . . . . 149 GLY C . 18543 1 526 . 1 1 149 149 GLY CA C 13 45.168 0.30 . 1 . . . . 149 GLY CA . 18543 1 527 . 1 1 149 149 GLY N N 15 105.616 0.30 . 1 . . . . 149 GLY N . 18543 1 528 . 1 1 150 150 VAL C C 13 173.007 0.30 . 1 . . . . 150 VAL C . 18543 1 529 . 1 1 150 150 VAL CA C 13 58.061 0.30 . 1 . . . . 150 VAL CA . 18543 1 530 . 1 1 150 150 VAL CB C 13 35.028 0.30 . 1 . . . . 150 VAL CB . 18543 1 531 . 1 1 150 150 VAL N N 15 110.477 0.30 . 1 . . . . 150 VAL N . 18543 1 532 . 1 1 152 152 ALA C C 13 174.774 0.30 . 1 . . . . 152 ALA C . 18543 1 533 . 1 1 152 152 ALA CA C 13 51.739 0.30 . 1 . . . . 152 ALA CA . 18543 1 534 . 1 1 152 152 ALA CB C 13 25.293 0.30 . 1 . . . . 152 ALA CB . 18543 1 535 . 1 1 153 153 MET C C 13 173.438 0.30 . 1 . . . . 153 MET C . 18543 1 536 . 1 1 153 153 MET CB C 13 37.158 0.30 . 1 . . . . 153 MET CB . 18543 1 537 . 1 1 153 153 MET CG C 13 32.455 0.30 . 1 . . . . 153 MET CG . 18543 1 538 . 1 1 153 153 MET N N 15 121.304 0.30 . 1 . . . . 153 MET N . 18543 1 539 . 1 1 155 155 VAL C C 13 176.081 0.30 . 1 . . . . 155 VAL C . 18543 1 540 . 1 1 155 155 VAL CA C 13 60.738 0.30 . 1 . . . . 155 VAL CA . 18543 1 541 . 1 1 155 155 VAL CB C 13 34.794 0.30 . 1 . . . . 155 VAL CB . 18543 1 542 . 1 1 155 155 VAL CG1 C 13 22.797 0.30 . 2 . . . . 155 VAL CG1 . 18543 1 543 . 1 1 155 155 VAL CG2 C 13 20.495 0.30 . 2 . . . . 155 VAL CG2 . 18543 1 544 . 1 1 155 155 VAL N N 15 123.034 0.30 . 1 . . . . 155 VAL N . 18543 1 545 . 1 1 156 156 ASN C C 13 174.193 0.30 . 1 . . . . 156 ASN C . 18543 1 546 . 1 1 156 156 ASN CA C 13 54.546 0.30 . 1 . . . . 156 ASN CA . 18543 1 547 . 1 1 156 156 ASN CB C 13 37.337 0.30 . 1 . . . . 156 ASN CB . 18543 1 548 . 1 1 156 156 ASN CG C 13 177.389 0.30 . 1 . . . . 156 ASN CG . 18543 1 549 . 1 1 156 156 ASN N N 15 127.219 0.30 . 1 . . . . 156 ASN N . 18543 1 550 . 1 1 157 157 GLY C C 13 172.478 0.30 . 1 . . . . 157 GLY C . 18543 1 551 . 1 1 157 157 GLY CA C 13 46.392 0.30 . 1 . . . . 157 GLY CA . 18543 1 552 . 1 1 157 157 GLY N N 15 105.259 0.30 . 1 . . . . 157 GLY N . 18543 1 553 . 1 1 158 158 LYS CA C 13 57.117 0.30 . 1 . . . . 158 LYS CA . 18543 1 554 . 1 1 158 158 LYS CB C 13 37.324 0.30 . 1 . . . . 158 LYS CB . 18543 1 555 . 1 1 158 158 LYS CG C 13 29.877 0.30 . 1 . . . . 158 LYS CG . 18543 1 556 . 1 1 158 158 LYS N N 15 114.470 0.30 . 1 . . . . 158 LYS N . 18543 1 557 . 1 1 159 159 TYR C C 13 174.853 0.30 . 1 . . . . 159 TYR C . 18543 1 558 . 1 1 160 160 GLN C C 13 175.490 0.30 . 1 . . . . 160 GLN C . 18543 1 559 . 1 1 160 160 GLN CA C 13 53.406 0.30 . 1 . . . . 160 GLN CA . 18543 1 560 . 1 1 160 160 GLN CB C 13 30.662 0.30 . 1 . . . . 160 GLN CB . 18543 1 561 . 1 1 160 160 GLN CG C 13 32.483 0.30 . 1 . . . . 160 GLN CG . 18543 1 562 . 1 1 160 160 GLN CD C 13 179.251 0.30 . 1 . . . . 160 GLN CD . 18543 1 563 . 1 1 160 160 GLN N N 15 124.898 0.30 . 1 . . . . 160 GLN N . 18543 1 564 . 1 1 160 160 GLN NE2 N 15 108.307 0.30 . 1 . . . . 160 GLN NE2 . 18543 1 565 . 1 1 161 161 LEU C C 13 177.480 0.30 . 1 . . . . 161 LEU C . 18543 1 566 . 1 1 161 161 LEU CA C 13 54.093 0.30 . 1 . . . . 161 LEU CA . 18543 1 567 . 1 1 161 161 LEU CB C 13 40.838 0.30 . 1 . . . . 161 LEU CB . 18543 1 568 . 1 1 161 161 LEU CG C 13 27.879 0.30 . 1 . . . . 161 LEU CG . 18543 1 569 . 1 1 161 161 LEU CD1 C 13 24.185 0.30 . 1 . . . . 161 LEU CD . 18543 1 570 . 1 1 161 161 LEU CD2 C 13 24.185 0.30 . 1 . . . . 161 LEU CD . 18543 1 571 . 1 1 161 161 LEU N N 15 131.282 0.30 . 1 . . . . 161 LEU N . 18543 1 572 . 1 1 162 162 ASN C C 13 172.167 0.30 . 1 . . . . 162 ASN C . 18543 1 573 . 1 1 162 162 ASN CA C 13 49.993 0.30 . 1 . . . . 162 ASN CA . 18543 1 574 . 1 1 162 162 ASN CB C 13 38.601 0.30 . 1 . . . . 162 ASN CB . 18543 1 575 . 1 1 162 162 ASN N N 15 118.500 0.30 . 1 . . . . 162 ASN N . 18543 1 576 . 1 1 163 163 PRO CA C 13 64.800 0.30 . 1 . . . . 163 PRO CA . 18543 1 577 . 1 1 163 163 PRO CB C 13 32.400 0.30 . 1 . . . . 163 PRO CB . 18543 1 578 . 1 1 163 163 PRO CG C 13 27.892 0.30 . 1 . . . . 163 PRO CG . 18543 1 579 . 1 1 163 163 PRO CD C 13 50.845 0.30 . 1 . . . . 163 PRO CD . 18543 1 580 . 1 1 163 163 PRO N N 15 137.100 0.30 . 1 . . . . 163 PRO N . 18543 1 581 . 1 1 164 164 GLN C C 13 177.104 0.30 . 1 . . . . 164 GLN C . 18543 1 582 . 1 1 164 164 GLN CA C 13 57.638 0.30 . 1 . . . . 164 GLN CA . 18543 1 583 . 1 1 164 164 GLN CB C 13 27.915 0.30 . 1 . . . . 164 GLN CB . 18543 1 584 . 1 1 165 165 GLY C C 13 173.932 0.30 . 1 . . . . 165 GLY C . 18543 1 585 . 1 1 165 165 GLY CA C 13 44.720 0.30 . 1 . . . . 165 GLY CA . 18543 1 586 . 1 1 165 165 GLY N N 15 106.700 0.30 . 1 . . . . 165 GLY N . 18543 1 587 . 1 1 166 166 MET N N 15 119.240 0.30 . 1 . . . . 166 MET N . 18543 1 588 . 1 1 168 168 THR C C 13 175.645 0.30 . 1 . . . . 168 THR C . 18543 1 589 . 1 1 168 168 THR CA C 13 60.794 0.30 . 1 . . . . 168 THR CA . 18543 1 590 . 1 1 168 168 THR CB C 13 68.554 0.30 . 1 . . . . 168 THR CB . 18543 1 591 . 1 1 168 168 THR N N 15 112.325 0.30 . 1 . . . . 168 THR N . 18543 1 592 . 1 1 169 169 SER CA C 13 61.352 0.30 . 1 . . . . 169 SER CA . 18543 1 593 . 1 1 169 169 SER CB C 13 63.344 0.30 . 1 . . . . 169 SER CB . 18543 1 594 . 1 1 173 173 VAL CA C 13 65.729 0.30 . 1 . . . . 173 VAL CA . 18543 1 595 . 1 1 173 173 VAL CB C 13 32.062 0.30 . 1 . . . . 173 VAL CB . 18543 1 596 . 1 1 173 173 VAL CG1 C 13 22.379 0.30 . 2 . . . . 173 VAL CG1 . 18543 1 597 . 1 1 173 173 VAL CG2 C 13 21.224 0.30 . 2 . . . . 173 VAL CG2 . 18543 1 598 . 1 1 173 173 VAL N N 15 121.383 0.30 . 1 . . . . 173 VAL N . 18543 1 599 . 1 1 174 174 PHE CB C 13 27.900 0.30 . 1 . . . . 174 PHE CB . 18543 1 600 . 1 1 175 175 VAL C C 13 177.693 0.30 . 1 . . . . 175 VAL C . 18543 1 601 . 1 1 175 175 VAL CA C 13 66.916 0.30 . 1 . . . . 175 VAL CA . 18543 1 602 . 1 1 175 175 VAL CB C 13 31.784 0.30 . 1 . . . . 175 VAL CB . 18543 1 603 . 1 1 175 175 VAL CG1 C 13 21.241 0.30 . 2 . . . . 175 VAL CG1 . 18543 1 604 . 1 1 175 175 VAL CG2 C 13 24.102 0.30 . 2 . . . . 175 VAL CG2 . 18543 1 605 . 1 1 175 175 VAL N N 15 117.001 0.30 . 1 . . . . 175 VAL N . 18543 1 606 . 1 1 176 176 GLN CA C 13 59.062 0.30 . 1 . . . . 176 GLN CA . 18543 1 607 . 1 1 176 176 GLN CB C 13 27.711 0.30 . 1 . . . . 176 GLN CB . 18543 1 608 . 1 1 176 176 GLN CG C 13 34.173 0.30 . 1 . . . . 176 GLN CG . 18543 1 609 . 1 1 176 176 GLN CD C 13 180.000 0.30 . 1 . . . . 176 GLN CD . 18543 1 610 . 1 1 176 176 GLN N N 15 116.511 0.30 . 1 . . . . 176 GLN N . 18543 1 611 . 1 1 176 176 GLN NE2 N 15 110.792 0.30 . 1 . . . . 176 GLN NE2 . 18543 1 612 . 1 1 177 177 GLN C C 13 179.997 0.30 . 1 . . . . 177 GLN C . 18543 1 613 . 1 1 177 177 GLN CA C 13 59.039 0.30 . 1 . . . . 177 GLN CA . 18543 1 614 . 1 1 177 177 GLN CB C 13 28.047 0.30 . 1 . . . . 177 GLN CB . 18543 1 615 . 1 1 177 177 GLN CG C 13 34.200 0.30 . 1 . . . . 177 GLN CG . 18543 1 616 . 1 1 178 178 TYR C C 13 178.114 0.30 . 1 . . . . 178 TYR C . 18543 1 617 . 1 1 178 178 TYR CA C 13 61.700 0.30 . 1 . . . . 178 TYR CA . 18543 1 618 . 1 1 178 178 TYR N N 15 126.422 0.30 . 1 . . . . 178 TYR N . 18543 1 619 . 1 1 179 179 ALA C C 13 179.720 0.30 . 1 . . . . 179 ALA C . 18543 1 620 . 1 1 179 179 ALA CA C 13 55.266 0.30 . 1 . . . . 179 ALA CA . 18543 1 621 . 1 1 179 179 ALA CB C 13 18.301 0.30 . 1 . . . . 179 ALA CB . 18543 1 622 . 1 1 180 180 ASP N N 15 118.836 0.30 . 1 . . . . 180 ASP N . 18543 1 623 . 1 1 181 181 THR CB C 13 67.457 0.30 . 1 . . . . 181 THR CB . 18543 1 624 . 1 1 181 181 THR CG2 C 13 21.804 0.30 . 1 . . . . 181 THR CG2 . 18543 1 625 . 1 1 182 182 VAL CA C 13 67.772 0.30 . 1 . . . . 182 VAL CA . 18543 1 626 . 1 1 182 182 VAL CB C 13 30.796 0.30 . 1 . . . . 182 VAL CB . 18543 1 627 . 1 1 182 182 VAL CG1 C 13 24.154 0.30 . 2 . . . . 182 VAL CG1 . 18543 1 628 . 1 1 182 182 VAL CG2 C 13 22.867 0.30 . 2 . . . . 182 VAL CG2 . 18543 1 629 . 1 1 182 182 VAL N N 15 121.432 0.30 . 1 . . . . 182 VAL N . 18543 1 630 . 1 1 184 184 TYR C C 13 177.858 0.30 . 1 . . . . 184 TYR C . 18543 1 631 . 1 1 184 184 TYR CA C 13 59.909 0.30 . 1 . . . . 184 TYR CA . 18543 1 632 . 1 1 185 185 LEU C C 13 178.477 0.30 . 1 . . . . 185 LEU C . 18543 1 633 . 1 1 185 185 LEU CA C 13 56.442 0.30 . 1 . . . . 185 LEU CA . 18543 1 634 . 1 1 185 185 LEU CB C 13 42.463 0.30 . 1 . . . . 185 LEU CB . 18543 1 635 . 1 1 185 185 LEU CG C 13 25.667 0.30 . 1 . . . . 185 LEU CG . 18543 1 636 . 1 1 185 185 LEU CD1 C 13 23.503 0.30 . 1 . . . . 185 LEU CD . 18543 1 637 . 1 1 185 185 LEU CD2 C 13 23.503 0.30 . 1 . . . . 185 LEU CD . 18543 1 638 . 1 1 185 185 LEU N N 15 118.123 0.30 . 1 . . . . 185 LEU N . 18543 1 639 . 1 1 186 186 SER CA C 13 61.946 0.30 . 1 . . . . 186 SER CA . 18543 1 640 . 1 1 186 186 SER CB C 13 62.533 0.30 . 1 . . . . 186 SER CB . 18543 1 641 . 1 1 186 186 SER N N 15 114.977 0.30 . 1 . . . . 186 SER N . 18543 1 642 . 1 1 187 187 GLU CA C 13 56.009 0.30 . 1 . . . . 187 GLU CA . 18543 1 643 . 1 1 187 187 GLU CB C 13 30.411 0.30 . 1 . . . . 187 GLU CB . 18543 1 644 . 1 1 187 187 GLU CG C 13 36.722 0.30 . 1 . . . . 187 GLU CG . 18543 1 645 . 1 1 187 187 GLU N N 15 119.458 0.30 . 1 . . . . 187 GLU N . 18543 1 646 . 1 1 188 188 LYS CA C 13 57.552 0.30 . 1 . . . . 188 LYS CA . 18543 1 stop_ save_