data_18544 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18544 _Entry.Title ; Chemical shift assignments of DsbA(C33S)/DsbB 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 . . . 18544 2 Ming Tang . . . 18544 3 Deborah Berthold . . . 18544 4 Anna Nesbitt . . . 18544 5 Robert Gennis . . . 18544 6 Chad Rienstra . . . 18544 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18544 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 268 18544 '15N chemical shifts' 55 18544 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' 18544 1 . . 2013-04-02 2012-06-21 original author 'original release' 18544 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 16327 'DsbA, wild type oxidized' 18544 BMRB 18543 'DsbA(C33S) apo form' 18544 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18544 _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. . 18544 1 2 Ming Tang . . . 18544 1 3 Deborah Berthold . A. . 18544 1 4 Anna Nesbitt . E. . 18544 1 5 Robert Gennis . B. . 18544 1 6 Chad Rienstra . M. . 18544 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID DsbA/DsbB 18544 1 'Membrane Protein' 18544 1 'Solid-state NMR' 18544 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18544 _Assembly.ID 1 _Assembly.Name DsbA(C33S) _Assembly.BMRB_code . _Assembly.Number_of_components 2 _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 'DsbA(C33S) complex with wild-type DsbB' _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 . . . 18544 1 2 DsbB 2 $DsbB B . no native no no . . . 18544 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 DsbA(C33S) 1 CYS 30 30 SG . 2 DsbB 2 CYS 104 104 SG . DsbA(C33S) 30 CYS SG . DsbB 104 CYS SG 18544 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_DsbA(C33S) _Entity.Sf_category entity _Entity.Sf_framecode DsbA(C33S) _Entity.Entry_ID 18544 _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 disulfide bound' _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 . . . . 18544 1 2 no BMRB 17710 . DsbA . . . . . 99.47 188 99.47 99.47 9.64e-135 . . . . 18544 1 3 no BMRB 18396 . oxidized_DsbA . . . . . 100.00 189 98.94 99.47 1.05e-134 . . . . 18544 1 4 no BMRB 18543 . DsbA(C33S) . . . . . 100.00 189 100.00 100.00 4.19e-136 . . . . 18544 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 . . . . 18544 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 . . . . 18544 1 7 no PDB 1A2J . "Oxidized Dsba Crystal Form Ii" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18544 1 8 no PDB 1A2L . "Reduced Dsba At 2.7 Angstroms Resolution" . . . . . 100.00 189 99.47 99.47 2.54e-135 . . . . 18544 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 . . . . 18544 1 10 no PDB 1AC1 . "Dsba Mutant H32l" . . . . . 100.00 189 98.94 98.94 7.80e-134 . . . . 18544 1 11 no PDB 1ACV . "Dsba Mutant H32s" . . . . . 100.00 189 98.94 98.94 4.93e-134 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 1 16 no PDB 1TI1 . "Crystal Structure Of A Mutant Dsba" . . . . . 100.00 189 99.47 100.00 1.35e-135 . . . . 18544 1 17 no PDB 1U3A . "Mutant Dsba" . . . . . 100.00 189 99.47 100.00 1.35e-135 . . . . 18544 1 18 no PDB 2B3S . "Structure Of The Dsba Mutant (P31g-C33a)" . . . . . 100.00 189 98.94 99.47 3.43e-134 . . . . 18544 1 19 no PDB 2B6M . "Structure Of The Dsba Mutant (P31a-C33a)" . . . . . 100.00 189 98.94 99.47 1.50e-134 . . . . 18544 1 20 no PDB 2HI7 . "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" . . . . . 100.00 189 99.47 100.00 1.35e-135 . . . . 18544 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 . . . . 18544 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 . . . . 18544 1 23 no PDB 3DKS . "Dsba Substrate Complex" . . . . . 100.00 189 98.94 99.47 9.66e-135 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 1 32 no DBJ BAG79665 . "protein disulfide isomerase I [Escherichia coli SE11]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18544 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 . . . . 18544 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 . . . . 18544 1 35 no EMBL CAA44868 . "PpfA protein [Escherichia coli K-12]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18544 1 36 no EMBL CAA56736 . "dsbA [Escherichia coli K-12]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18544 1 37 no EMBL CAA90910 . "DsbA protein [Escherichia coli]" . . . . . 100.00 208 98.94 99.47 7.94e-135 . . . . 18544 1 38 no EMBL CAP78318 . "Thiol:disulfide interchange protein dsbA [Escherichia coli LF82]" . . . . . 100.00 208 98.94 99.47 7.94e-135 . . . . 18544 1 39 no EMBL CAQ34212 . "protein disulfide oxidoreductase [Escherichia coli BL21(DE3)]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18544 1 40 no GB AAA23715 . "putative [Escherichia coli]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18544 1 41 no GB AAB02995 . "dsbA [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 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 . . . . 18544 1 48 no REF WP_000725331 . "thiol-disulfide isomerase [Shigella boydii]" . . . . . 100.00 208 98.41 98.94 2.45e-134 . . . . 18544 1 49 no REF WP_000725332 . "thiol:disulfide interchange protein DsbA [Escherichia coli]" . . . . . 100.00 208 98.94 99.47 2.72e-135 . . . . 18544 1 50 no SP P0A4L5 . "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" . . . . . 100.00 208 98.94 99.47 7.94e-135 . . . . 18544 1 51 no SP P0A4L6 . "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" . . . . . 100.00 208 98.94 99.47 7.94e-135 . . . . 18544 1 52 no SP P0AEG4 . "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18544 1 53 no SP P0AEG5 . "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" . . . . . 100.00 208 99.47 99.47 2.21e-135 . . . . 18544 1 54 no SP P52235 . "RecName: Full=Thiol:disulfide interchange protein DsbA; Flags: Precursor" . . . . . 100.00 208 98.94 99.47 8.47e-135 . . . . 18544 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 . 18544 1 2 2 GLN . 18544 1 3 3 TYR . 18544 1 4 4 GLU . 18544 1 5 5 ASP . 18544 1 6 6 GLY . 18544 1 7 7 LYS . 18544 1 8 8 GLN . 18544 1 9 9 TYR . 18544 1 10 10 THR . 18544 1 11 11 THR . 18544 1 12 12 LEU . 18544 1 13 13 GLU . 18544 1 14 14 LYS . 18544 1 15 15 PRO . 18544 1 16 16 VAL . 18544 1 17 17 ALA . 18544 1 18 18 GLY . 18544 1 19 19 ALA . 18544 1 20 20 PRO . 18544 1 21 21 GLN . 18544 1 22 22 VAL . 18544 1 23 23 LEU . 18544 1 24 24 GLU . 18544 1 25 25 PHE . 18544 1 26 26 PHE . 18544 1 27 27 SER . 18544 1 28 28 PHE . 18544 1 29 29 PHE . 18544 1 30 30 CYS . 18544 1 31 31 PRO . 18544 1 32 32 HIS . 18544 1 33 33 SER . 18544 1 34 34 TYR . 18544 1 35 35 GLN . 18544 1 36 36 PHE . 18544 1 37 37 GLU . 18544 1 38 38 GLU . 18544 1 39 39 VAL . 18544 1 40 40 LEU . 18544 1 41 41 HIS . 18544 1 42 42 ILE . 18544 1 43 43 SER . 18544 1 44 44 ASP . 18544 1 45 45 ASN . 18544 1 46 46 VAL . 18544 1 47 47 LYS . 18544 1 48 48 LYS . 18544 1 49 49 LYS . 18544 1 50 50 LEU . 18544 1 51 51 PRO . 18544 1 52 52 GLU . 18544 1 53 53 GLY . 18544 1 54 54 VAL . 18544 1 55 55 LYS . 18544 1 56 56 MET . 18544 1 57 57 THR . 18544 1 58 58 LYS . 18544 1 59 59 TYR . 18544 1 60 60 HIS . 18544 1 61 61 VAL . 18544 1 62 62 ASN . 18544 1 63 63 PHE . 18544 1 64 64 MET . 18544 1 65 65 GLY . 18544 1 66 66 GLY . 18544 1 67 67 ASP . 18544 1 68 68 LEU . 18544 1 69 69 GLY . 18544 1 70 70 LYS . 18544 1 71 71 ASP . 18544 1 72 72 LEU . 18544 1 73 73 THR . 18544 1 74 74 GLN . 18544 1 75 75 ALA . 18544 1 76 76 TRP . 18544 1 77 77 ALA . 18544 1 78 78 VAL . 18544 1 79 79 ALA . 18544 1 80 80 MET . 18544 1 81 81 ALA . 18544 1 82 82 LEU . 18544 1 83 83 GLY . 18544 1 84 84 VAL . 18544 1 85 85 GLU . 18544 1 86 86 ASP . 18544 1 87 87 LYS . 18544 1 88 88 VAL . 18544 1 89 89 THR . 18544 1 90 90 VAL . 18544 1 91 91 PRO . 18544 1 92 92 LEU . 18544 1 93 93 PHE . 18544 1 94 94 GLU . 18544 1 95 95 GLY . 18544 1 96 96 VAL . 18544 1 97 97 GLN . 18544 1 98 98 LYS . 18544 1 99 99 THR . 18544 1 100 100 GLN . 18544 1 101 101 THR . 18544 1 102 102 ILE . 18544 1 103 103 ARG . 18544 1 104 104 SER . 18544 1 105 105 ALA . 18544 1 106 106 SER . 18544 1 107 107 ASP . 18544 1 108 108 ILE . 18544 1 109 109 ARG . 18544 1 110 110 ASP . 18544 1 111 111 VAL . 18544 1 112 112 PHE . 18544 1 113 113 ILE . 18544 1 114 114 ASN . 18544 1 115 115 ALA . 18544 1 116 116 GLY . 18544 1 117 117 ILE . 18544 1 118 118 LYS . 18544 1 119 119 GLY . 18544 1 120 120 GLU . 18544 1 121 121 GLU . 18544 1 122 122 TYR . 18544 1 123 123 ASP . 18544 1 124 124 ALA . 18544 1 125 125 ALA . 18544 1 126 126 TRP . 18544 1 127 127 ASN . 18544 1 128 128 SER . 18544 1 129 129 PHE . 18544 1 130 130 VAL . 18544 1 131 131 VAL . 18544 1 132 132 LYS . 18544 1 133 133 SER . 18544 1 134 134 LEU . 18544 1 135 135 VAL . 18544 1 136 136 ALA . 18544 1 137 137 GLN . 18544 1 138 138 GLN . 18544 1 139 139 GLU . 18544 1 140 140 LYS . 18544 1 141 141 ALA . 18544 1 142 142 ALA . 18544 1 143 143 ALA . 18544 1 144 144 ASP . 18544 1 145 145 VAL . 18544 1 146 146 GLN . 18544 1 147 147 LEU . 18544 1 148 148 ARG . 18544 1 149 149 GLY . 18544 1 150 150 VAL . 18544 1 151 151 PRO . 18544 1 152 152 ALA . 18544 1 153 153 MET . 18544 1 154 154 PHE . 18544 1 155 155 VAL . 18544 1 156 156 ASN . 18544 1 157 157 GLY . 18544 1 158 158 LYS . 18544 1 159 159 TYR . 18544 1 160 160 GLN . 18544 1 161 161 LEU . 18544 1 162 162 ASN . 18544 1 163 163 PRO . 18544 1 164 164 GLN . 18544 1 165 165 GLY . 18544 1 166 166 MET . 18544 1 167 167 ASP . 18544 1 168 168 THR . 18544 1 169 169 SER . 18544 1 170 170 ASN . 18544 1 171 171 MET . 18544 1 172 172 ASP . 18544 1 173 173 VAL . 18544 1 174 174 PHE . 18544 1 175 175 VAL . 18544 1 176 176 GLN . 18544 1 177 177 GLN . 18544 1 178 178 TYR . 18544 1 179 179 ALA . 18544 1 180 180 ASP . 18544 1 181 181 THR . 18544 1 182 182 VAL . 18544 1 183 183 LYS . 18544 1 184 184 TYR . 18544 1 185 185 LEU . 18544 1 186 186 SER . 18544 1 187 187 GLU . 18544 1 188 188 LYS . 18544 1 189 189 LYS . 18544 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 18544 1 . GLN 2 2 18544 1 . TYR 3 3 18544 1 . GLU 4 4 18544 1 . ASP 5 5 18544 1 . GLY 6 6 18544 1 . LYS 7 7 18544 1 . GLN 8 8 18544 1 . TYR 9 9 18544 1 . THR 10 10 18544 1 . THR 11 11 18544 1 . LEU 12 12 18544 1 . GLU 13 13 18544 1 . LYS 14 14 18544 1 . PRO 15 15 18544 1 . VAL 16 16 18544 1 . ALA 17 17 18544 1 . GLY 18 18 18544 1 . ALA 19 19 18544 1 . PRO 20 20 18544 1 . GLN 21 21 18544 1 . VAL 22 22 18544 1 . LEU 23 23 18544 1 . GLU 24 24 18544 1 . PHE 25 25 18544 1 . PHE 26 26 18544 1 . SER 27 27 18544 1 . PHE 28 28 18544 1 . PHE 29 29 18544 1 . CYS 30 30 18544 1 . PRO 31 31 18544 1 . HIS 32 32 18544 1 . SER 33 33 18544 1 . TYR 34 34 18544 1 . GLN 35 35 18544 1 . PHE 36 36 18544 1 . GLU 37 37 18544 1 . GLU 38 38 18544 1 . VAL 39 39 18544 1 . LEU 40 40 18544 1 . HIS 41 41 18544 1 . ILE 42 42 18544 1 . SER 43 43 18544 1 . ASP 44 44 18544 1 . ASN 45 45 18544 1 . VAL 46 46 18544 1 . LYS 47 47 18544 1 . LYS 48 48 18544 1 . LYS 49 49 18544 1 . LEU 50 50 18544 1 . PRO 51 51 18544 1 . GLU 52 52 18544 1 . GLY 53 53 18544 1 . VAL 54 54 18544 1 . LYS 55 55 18544 1 . MET 56 56 18544 1 . THR 57 57 18544 1 . LYS 58 58 18544 1 . TYR 59 59 18544 1 . HIS 60 60 18544 1 . VAL 61 61 18544 1 . ASN 62 62 18544 1 . PHE 63 63 18544 1 . MET 64 64 18544 1 . GLY 65 65 18544 1 . GLY 66 66 18544 1 . ASP 67 67 18544 1 . LEU 68 68 18544 1 . GLY 69 69 18544 1 . LYS 70 70 18544 1 . ASP 71 71 18544 1 . LEU 72 72 18544 1 . THR 73 73 18544 1 . GLN 74 74 18544 1 . ALA 75 75 18544 1 . TRP 76 76 18544 1 . ALA 77 77 18544 1 . VAL 78 78 18544 1 . ALA 79 79 18544 1 . MET 80 80 18544 1 . ALA 81 81 18544 1 . LEU 82 82 18544 1 . GLY 83 83 18544 1 . VAL 84 84 18544 1 . GLU 85 85 18544 1 . ASP 86 86 18544 1 . LYS 87 87 18544 1 . VAL 88 88 18544 1 . THR 89 89 18544 1 . VAL 90 90 18544 1 . PRO 91 91 18544 1 . LEU 92 92 18544 1 . PHE 93 93 18544 1 . GLU 94 94 18544 1 . GLY 95 95 18544 1 . VAL 96 96 18544 1 . GLN 97 97 18544 1 . LYS 98 98 18544 1 . THR 99 99 18544 1 . GLN 100 100 18544 1 . THR 101 101 18544 1 . ILE 102 102 18544 1 . ARG 103 103 18544 1 . SER 104 104 18544 1 . ALA 105 105 18544 1 . SER 106 106 18544 1 . ASP 107 107 18544 1 . ILE 108 108 18544 1 . ARG 109 109 18544 1 . ASP 110 110 18544 1 . VAL 111 111 18544 1 . PHE 112 112 18544 1 . ILE 113 113 18544 1 . ASN 114 114 18544 1 . ALA 115 115 18544 1 . GLY 116 116 18544 1 . ILE 117 117 18544 1 . LYS 118 118 18544 1 . GLY 119 119 18544 1 . GLU 120 120 18544 1 . GLU 121 121 18544 1 . TYR 122 122 18544 1 . ASP 123 123 18544 1 . ALA 124 124 18544 1 . ALA 125 125 18544 1 . TRP 126 126 18544 1 . ASN 127 127 18544 1 . SER 128 128 18544 1 . PHE 129 129 18544 1 . VAL 130 130 18544 1 . VAL 131 131 18544 1 . LYS 132 132 18544 1 . SER 133 133 18544 1 . LEU 134 134 18544 1 . VAL 135 135 18544 1 . ALA 136 136 18544 1 . GLN 137 137 18544 1 . GLN 138 138 18544 1 . GLU 139 139 18544 1 . LYS 140 140 18544 1 . ALA 141 141 18544 1 . ALA 142 142 18544 1 . ALA 143 143 18544 1 . ASP 144 144 18544 1 . VAL 145 145 18544 1 . GLN 146 146 18544 1 . LEU 147 147 18544 1 . ARG 148 148 18544 1 . GLY 149 149 18544 1 . VAL 150 150 18544 1 . PRO 151 151 18544 1 . ALA 152 152 18544 1 . MET 153 153 18544 1 . PHE 154 154 18544 1 . VAL 155 155 18544 1 . ASN 156 156 18544 1 . GLY 157 157 18544 1 . LYS 158 158 18544 1 . TYR 159 159 18544 1 . GLN 160 160 18544 1 . LEU 161 161 18544 1 . ASN 162 162 18544 1 . PRO 163 163 18544 1 . GLN 164 164 18544 1 . GLY 165 165 18544 1 . MET 166 166 18544 1 . ASP 167 167 18544 1 . THR 168 168 18544 1 . SER 169 169 18544 1 . ASN 170 170 18544 1 . MET 171 171 18544 1 . ASP 172 172 18544 1 . VAL 173 173 18544 1 . PHE 174 174 18544 1 . VAL 175 175 18544 1 . GLN 176 176 18544 1 . GLN 177 177 18544 1 . TYR 178 178 18544 1 . ALA 179 179 18544 1 . ASP 180 180 18544 1 . THR 181 181 18544 1 . VAL 182 182 18544 1 . LYS 183 183 18544 1 . TYR 184 184 18544 1 . LEU 185 185 18544 1 . SER 186 186 18544 1 . GLU 187 187 18544 1 . LYS 188 188 18544 1 . LYS 189 189 18544 1 stop_ save_ save_DsbB _Entity.Sf_category entity _Entity.Sf_framecode DsbB _Entity.Entry_ID 18544 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name DsbB _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 ; MLRFLNQASQGRGAWLLMAF TALALELTALWFQHVMLLKP CVLCIYERVALFGVLGAALI GAIAPKTPLRYVAMVIWLYS AFRGVQLTYEHTMLQLYPSP FATCDFMVRFPEWLPLDKWV PQVFVASGDCAERQWDFLGL EMPQWLLGIFIAYLIVAVLV VISQPFKAKKRDLFGR ; _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 176 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'free and disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation 'DsbA C33S' _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 2015-01-30 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 15546 . DsbB . . . . . 100.00 186 99.43 99.43 7.23e-122 . . . . 18544 2 2 no BMRB 15966 . Disulfide_bond_formation_protein_B . . . . . 100.00 183 98.30 98.30 4.28e-120 . . . . 18544 2 3 no BMRB 17710 . DsbB . . . . . 100.00 176 99.43 99.43 1.19e-121 . . . . 18544 2 4 no BMRB 18395 . DsbB . . . . . 100.00 176 100.00 100.00 9.91e-123 . . . . 18544 2 5 no BMRB 18493 . DsbB . . . . . 100.00 176 99.43 99.43 1.19e-121 . . . . 18544 2 6 no PDB 2HI7 . "Crystal Structure Of Dsba-Dsbb-Ubiquinone Complex" . . . . . 100.00 176 99.43 99.43 1.19e-121 . . . . 18544 2 7 no PDB 2K73 . "Solution Nmr Structure Of Integral Membrane Protein Dsbb" . . . . . 100.00 183 98.30 98.30 4.28e-120 . . . . 18544 2 8 no PDB 2K74 . "Solution Nmr Structure Of Dsbb-Ubiquinone Complex" . . . . . 100.00 183 98.30 98.30 4.28e-120 . . . . 18544 2 9 no PDB 2LEG . "Membrane Protein Complex Dsbb-Dsba Structure By Joint Calculations With Solid-State Nmr And X-Ray Experimental Data" . . . . . 100.00 176 99.43 99.43 1.19e-121 . . . . 18544 2 10 no PDB 2LTQ . "High Resolution Structure Of Dsbb C41s By Joint Calculation With Solid-state Nmr And X-ray Data" . . . . . 100.00 176 99.43 99.43 1.19e-121 . . . . 18544 2 11 no PDB 2ZUP . "Updated Crystal Structure Of Dsbb-Dsba Complex From E. Coli" . . . . . 100.00 176 99.43 99.43 1.19e-121 . . . . 18544 2 12 no PDB 2ZUQ . "Crystal Structure Of Dsbb-Fab Complex" . . . . . 100.00 176 99.43 99.43 1.19e-121 . . . . 18544 2 13 no PDB 3E9J . "Structure Of The Charge-Transfer Intermediate Of The Transmembrane Redox Catalyst Dsbb" . . . . . 100.00 182 100.00 100.00 6.13e-123 . . . . 18544 2 14 no DBJ BAA07408 . "disulfide oxidoreductase [Shigella flexneri]" . . . . . 100.00 176 97.16 97.73 1.41e-118 . . . . 18544 2 15 no DBJ BAA36032 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. W3110]" . . . . . 100.00 176 98.86 98.86 3.86e-121 . . . . 18544 2 16 no DBJ BAB35103 . "protein-disulfide oxidoreductase [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 176 98.86 98.86 3.86e-121 . . . . 18544 2 17 no DBJ BAG76757 . "disulfide bond formation protein [Escherichia coli SE11]" . . . . . 100.00 176 97.73 98.30 1.17e-119 . . . . 18544 2 18 no DBJ BAI24997 . "oxidoreductase DsbB [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 176 98.30 98.86 8.48e-121 . . . . 18544 2 19 no EMBL CAP75720 . "Disulfide bond formation protein B [Escherichia coli LF82]" . . . . . 100.00 176 97.73 98.30 6.07e-120 . . . . 18544 2 20 no EMBL CAQ31687 . "DsbB[reduced] [Escherichia coli BL21(DE3)]" . . . . . 100.00 176 98.86 98.86 3.86e-121 . . . . 18544 2 21 no EMBL CAQ98064 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli IAI1]" . . . . . 100.00 176 98.86 98.86 3.86e-121 . . . . 18544 2 22 no EMBL CAR02574 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli S88]" . . . . . 100.00 176 97.73 98.30 6.07e-120 . . . . 18544 2 23 no EMBL CAR07527 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli ED1a]" . . . . . 100.00 176 97.16 97.73 2.16e-119 . . . . 18544 2 24 no GB AAA23711 . "oxido-reductase [Escherichia coli]" . . . . . 100.00 178 98.86 98.86 3.51e-121 . . . . 18544 2 25 no GB AAB25233 . "DsbB=disulfide bond formation protein [Escherichia coli, Peptide, 176 aa]" . . . . . 100.00 176 98.86 98.86 3.86e-121 . . . . 18544 2 26 no GB AAC74269 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 176 98.86 98.86 3.86e-121 . . . . 18544 2 27 no GB AAG56036 . "reoxidizes DsbA protein following formation of disulfide bond in P-ring of flagella [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 176 98.30 98.30 2.67e-120 . . . . 18544 2 28 no GB AAN42789 . "disulfide bond formation protein dsbB [Shigella flexneri 2a str. 301]" . . . . . 100.00 176 98.30 98.86 8.48e-121 . . . . 18544 2 29 no PIR H85696 . "hypothetical protein dsbB [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" . . . . . 100.00 176 98.30 98.30 2.67e-120 . . . . 18544 2 30 no REF NP_287424 . "disulfide bond formation protein B [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 176 98.30 98.30 2.67e-120 . . . . 18544 2 31 no REF NP_309707 . "disulfide bond formation protein B [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 176 98.86 98.86 3.86e-121 . . . . 18544 2 32 no REF NP_415703 . "oxidoreductase that catalyzes reoxidation of DsbA protein disulfide isomerase I [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 176 98.86 98.86 3.86e-121 . . . . 18544 2 33 no REF NP_707082 . "disulfide bond formation protein B [Shigella flexneri 2a str. 301]" . . . . . 100.00 176 98.30 98.86 8.48e-121 . . . . 18544 2 34 no REF NP_753538 . "disulfide bond formation protein B [Escherichia coli CFT073]" . . . . . 100.00 176 97.73 98.30 6.07e-120 . . . . 18544 2 35 no SP A1AAA8 . "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli APEC O1]" . . . . . 100.00 176 97.73 98.30 6.07e-120 . . . . 18544 2 36 no SP P0A6M2 . "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli K-12]" . . . . . 100.00 176 98.86 98.86 3.86e-121 . . . . 18544 2 37 no SP P0A6M3 . "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli O157:H7]" . . . . . 100.00 176 98.86 98.86 3.86e-121 . . . . 18544 2 38 no SP P59343 . "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Escherichia coli CFT073]" . . . . . 100.00 176 97.73 98.30 6.07e-120 . . . . 18544 2 39 no SP Q0T5L6 . "RecName: Full=Disulfide bond formation protein B; AltName: Full=Disulfide oxidoreductase [Shigella flexneri 5 str. 8401]" . . . . . 100.00 176 98.30 98.86 8.48e-121 . . . . 18544 2 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 MET . 18544 2 2 2 LEU . 18544 2 3 3 ARG . 18544 2 4 4 PHE . 18544 2 5 5 LEU . 18544 2 6 6 ASN . 18544 2 7 7 GLN . 18544 2 8 8 ALA . 18544 2 9 9 SER . 18544 2 10 10 GLN . 18544 2 11 11 GLY . 18544 2 12 12 ARG . 18544 2 13 13 GLY . 18544 2 14 14 ALA . 18544 2 15 15 TRP . 18544 2 16 16 LEU . 18544 2 17 17 LEU . 18544 2 18 18 MET . 18544 2 19 19 ALA . 18544 2 20 20 PHE . 18544 2 21 21 THR . 18544 2 22 22 ALA . 18544 2 23 23 LEU . 18544 2 24 24 ALA . 18544 2 25 25 LEU . 18544 2 26 26 GLU . 18544 2 27 27 LEU . 18544 2 28 28 THR . 18544 2 29 29 ALA . 18544 2 30 30 LEU . 18544 2 31 31 TRP . 18544 2 32 32 PHE . 18544 2 33 33 GLN . 18544 2 34 34 HIS . 18544 2 35 35 VAL . 18544 2 36 36 MET . 18544 2 37 37 LEU . 18544 2 38 38 LEU . 18544 2 39 39 LYS . 18544 2 40 40 PRO . 18544 2 41 41 CYS . 18544 2 42 42 VAL . 18544 2 43 43 LEU . 18544 2 44 44 CYS . 18544 2 45 45 ILE . 18544 2 46 46 TYR . 18544 2 47 47 GLU . 18544 2 48 48 ARG . 18544 2 49 49 VAL . 18544 2 50 50 ALA . 18544 2 51 51 LEU . 18544 2 52 52 PHE . 18544 2 53 53 GLY . 18544 2 54 54 VAL . 18544 2 55 55 LEU . 18544 2 56 56 GLY . 18544 2 57 57 ALA . 18544 2 58 58 ALA . 18544 2 59 59 LEU . 18544 2 60 60 ILE . 18544 2 61 61 GLY . 18544 2 62 62 ALA . 18544 2 63 63 ILE . 18544 2 64 64 ALA . 18544 2 65 65 PRO . 18544 2 66 66 LYS . 18544 2 67 67 THR . 18544 2 68 68 PRO . 18544 2 69 69 LEU . 18544 2 70 70 ARG . 18544 2 71 71 TYR . 18544 2 72 72 VAL . 18544 2 73 73 ALA . 18544 2 74 74 MET . 18544 2 75 75 VAL . 18544 2 76 76 ILE . 18544 2 77 77 TRP . 18544 2 78 78 LEU . 18544 2 79 79 TYR . 18544 2 80 80 SER . 18544 2 81 81 ALA . 18544 2 82 82 PHE . 18544 2 83 83 ARG . 18544 2 84 84 GLY . 18544 2 85 85 VAL . 18544 2 86 86 GLN . 18544 2 87 87 LEU . 18544 2 88 88 THR . 18544 2 89 89 TYR . 18544 2 90 90 GLU . 18544 2 91 91 HIS . 18544 2 92 92 THR . 18544 2 93 93 MET . 18544 2 94 94 LEU . 18544 2 95 95 GLN . 18544 2 96 96 LEU . 18544 2 97 97 TYR . 18544 2 98 98 PRO . 18544 2 99 99 SER . 18544 2 100 100 PRO . 18544 2 101 101 PHE . 18544 2 102 102 ALA . 18544 2 103 103 THR . 18544 2 104 104 CYS . 18544 2 105 105 ASP . 18544 2 106 106 PHE . 18544 2 107 107 MET . 18544 2 108 108 VAL . 18544 2 109 109 ARG . 18544 2 110 110 PHE . 18544 2 111 111 PRO . 18544 2 112 112 GLU . 18544 2 113 113 TRP . 18544 2 114 114 LEU . 18544 2 115 115 PRO . 18544 2 116 116 LEU . 18544 2 117 117 ASP . 18544 2 118 118 LYS . 18544 2 119 119 TRP . 18544 2 120 120 VAL . 18544 2 121 121 PRO . 18544 2 122 122 GLN . 18544 2 123 123 VAL . 18544 2 124 124 PHE . 18544 2 125 125 VAL . 18544 2 126 126 ALA . 18544 2 127 127 SER . 18544 2 128 128 GLY . 18544 2 129 129 ASP . 18544 2 130 130 CYS . 18544 2 131 131 ALA . 18544 2 132 132 GLU . 18544 2 133 133 ARG . 18544 2 134 134 GLN . 18544 2 135 135 TRP . 18544 2 136 136 ASP . 18544 2 137 137 PHE . 18544 2 138 138 LEU . 18544 2 139 139 GLY . 18544 2 140 140 LEU . 18544 2 141 141 GLU . 18544 2 142 142 MET . 18544 2 143 143 PRO . 18544 2 144 144 GLN . 18544 2 145 145 TRP . 18544 2 146 146 LEU . 18544 2 147 147 LEU . 18544 2 148 148 GLY . 18544 2 149 149 ILE . 18544 2 150 150 PHE . 18544 2 151 151 ILE . 18544 2 152 152 ALA . 18544 2 153 153 TYR . 18544 2 154 154 LEU . 18544 2 155 155 ILE . 18544 2 156 156 VAL . 18544 2 157 157 ALA . 18544 2 158 158 VAL . 18544 2 159 159 LEU . 18544 2 160 160 VAL . 18544 2 161 161 VAL . 18544 2 162 162 ILE . 18544 2 163 163 SER . 18544 2 164 164 GLN . 18544 2 165 165 PRO . 18544 2 166 166 PHE . 18544 2 167 167 LYS . 18544 2 168 168 ALA . 18544 2 169 169 LYS . 18544 2 170 170 LYS . 18544 2 171 171 ARG . 18544 2 172 172 ASP . 18544 2 173 173 LEU . 18544 2 174 174 PHE . 18544 2 175 175 GLY . 18544 2 176 176 ARG . 18544 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 18544 2 . LEU 2 2 18544 2 . ARG 3 3 18544 2 . PHE 4 4 18544 2 . LEU 5 5 18544 2 . ASN 6 6 18544 2 . GLN 7 7 18544 2 . ALA 8 8 18544 2 . SER 9 9 18544 2 . GLN 10 10 18544 2 . GLY 11 11 18544 2 . ARG 12 12 18544 2 . GLY 13 13 18544 2 . ALA 14 14 18544 2 . TRP 15 15 18544 2 . LEU 16 16 18544 2 . LEU 17 17 18544 2 . MET 18 18 18544 2 . ALA 19 19 18544 2 . PHE 20 20 18544 2 . THR 21 21 18544 2 . ALA 22 22 18544 2 . LEU 23 23 18544 2 . ALA 24 24 18544 2 . LEU 25 25 18544 2 . GLU 26 26 18544 2 . LEU 27 27 18544 2 . THR 28 28 18544 2 . ALA 29 29 18544 2 . LEU 30 30 18544 2 . TRP 31 31 18544 2 . PHE 32 32 18544 2 . GLN 33 33 18544 2 . HIS 34 34 18544 2 . VAL 35 35 18544 2 . MET 36 36 18544 2 . LEU 37 37 18544 2 . LEU 38 38 18544 2 . LYS 39 39 18544 2 . PRO 40 40 18544 2 . CYS 41 41 18544 2 . VAL 42 42 18544 2 . LEU 43 43 18544 2 . CYS 44 44 18544 2 . ILE 45 45 18544 2 . TYR 46 46 18544 2 . GLU 47 47 18544 2 . ARG 48 48 18544 2 . VAL 49 49 18544 2 . ALA 50 50 18544 2 . LEU 51 51 18544 2 . PHE 52 52 18544 2 . GLY 53 53 18544 2 . VAL 54 54 18544 2 . LEU 55 55 18544 2 . GLY 56 56 18544 2 . ALA 57 57 18544 2 . ALA 58 58 18544 2 . LEU 59 59 18544 2 . ILE 60 60 18544 2 . GLY 61 61 18544 2 . ALA 62 62 18544 2 . ILE 63 63 18544 2 . ALA 64 64 18544 2 . PRO 65 65 18544 2 . LYS 66 66 18544 2 . THR 67 67 18544 2 . PRO 68 68 18544 2 . LEU 69 69 18544 2 . ARG 70 70 18544 2 . TYR 71 71 18544 2 . VAL 72 72 18544 2 . ALA 73 73 18544 2 . MET 74 74 18544 2 . VAL 75 75 18544 2 . ILE 76 76 18544 2 . TRP 77 77 18544 2 . LEU 78 78 18544 2 . TYR 79 79 18544 2 . SER 80 80 18544 2 . ALA 81 81 18544 2 . PHE 82 82 18544 2 . ARG 83 83 18544 2 . GLY 84 84 18544 2 . VAL 85 85 18544 2 . GLN 86 86 18544 2 . LEU 87 87 18544 2 . THR 88 88 18544 2 . TYR 89 89 18544 2 . GLU 90 90 18544 2 . HIS 91 91 18544 2 . THR 92 92 18544 2 . MET 93 93 18544 2 . LEU 94 94 18544 2 . GLN 95 95 18544 2 . LEU 96 96 18544 2 . TYR 97 97 18544 2 . PRO 98 98 18544 2 . SER 99 99 18544 2 . PRO 100 100 18544 2 . PHE 101 101 18544 2 . ALA 102 102 18544 2 . THR 103 103 18544 2 . CYS 104 104 18544 2 . ASP 105 105 18544 2 . PHE 106 106 18544 2 . MET 107 107 18544 2 . VAL 108 108 18544 2 . ARG 109 109 18544 2 . PHE 110 110 18544 2 . PRO 111 111 18544 2 . GLU 112 112 18544 2 . TRP 113 113 18544 2 . LEU 114 114 18544 2 . PRO 115 115 18544 2 . LEU 116 116 18544 2 . ASP 117 117 18544 2 . LYS 118 118 18544 2 . TRP 119 119 18544 2 . VAL 120 120 18544 2 . PRO 121 121 18544 2 . GLN 122 122 18544 2 . VAL 123 123 18544 2 . PHE 124 124 18544 2 . VAL 125 125 18544 2 . ALA 126 126 18544 2 . SER 127 127 18544 2 . GLY 128 128 18544 2 . ASP 129 129 18544 2 . CYS 130 130 18544 2 . ALA 131 131 18544 2 . GLU 132 132 18544 2 . ARG 133 133 18544 2 . GLN 134 134 18544 2 . TRP 135 135 18544 2 . ASP 136 136 18544 2 . PHE 137 137 18544 2 . LEU 138 138 18544 2 . GLY 139 139 18544 2 . LEU 140 140 18544 2 . GLU 141 141 18544 2 . MET 142 142 18544 2 . PRO 143 143 18544 2 . GLN 144 144 18544 2 . TRP 145 145 18544 2 . LEU 146 146 18544 2 . LEU 147 147 18544 2 . GLY 148 148 18544 2 . ILE 149 149 18544 2 . PHE 150 150 18544 2 . ILE 151 151 18544 2 . ALA 152 152 18544 2 . TYR 153 153 18544 2 . LEU 154 154 18544 2 . ILE 155 155 18544 2 . VAL 156 156 18544 2 . ALA 157 157 18544 2 . VAL 158 158 18544 2 . LEU 159 159 18544 2 . VAL 160 160 18544 2 . VAL 161 161 18544 2 . ILE 162 162 18544 2 . SER 163 163 18544 2 . GLN 164 164 18544 2 . PRO 165 165 18544 2 . PHE 166 166 18544 2 . LYS 167 167 18544 2 . ALA 168 168 18544 2 . LYS 169 169 18544 2 . LYS 170 170 18544 2 . ARG 171 171 18544 2 . ASP 172 172 18544 2 . LEU 173 173 18544 2 . PHE 174 174 18544 2 . GLY 175 175 18544 2 . ARG 176 176 18544 2 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 18544 _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 . . . . . . . . . . . . . . . . . . . . . 18544 1 2 2 $DsbB . 562 organism . 'Escherichia coli' Enterobacteria . . Bacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 18544 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 18544 _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 . . . . . . 18544 1 2 2 $DsbB . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pQE70 . . . . . . 18544 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_DsbA(C33S)_DsbB _Sample.Sf_category sample _Sample.Sf_framecode sample_DsbA(C33S)_DsbB _Sample.Entry_ID 18544 _Sample.ID 1 _Sample.Type solid _Sample.Sub_type . _Sample.Details 'membrane protein complex DsbA(C33S)/DsbB' _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) . . 6 . . mg . . . . 18544 1 2 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18544 1 3 D2O [U-2D] . . . . . . 10 . . % . . . . 18544 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 18544 _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 18544 1 pressure 1 . atm 18544 1 temperature 263 . K 18544 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 18544 _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 18544 2 pressure 1 . atm 18544 2 temperature 253 . K 18544 2 stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Software.Sf_category software _Software.Sf_framecode VNMRJ _Software.Entry_ID 18544 _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 . . 18544 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 18544 1 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 18544 _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' . . 18544 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 18544 2 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 18544 _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 . . 18544 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18544 3 'data analysis' 18544 3 'peak picking' 18544 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 18544 _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 18544 _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 . . . 18544 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 18544 _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_DsbA(C33S)_DsbB solid . . 2 $sample_conditions_2 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18544 1 2 '3D NCOCX' no . . . . . . . . . . 1 $sample_DsbA(C33S)_DsbB solid . . 2 $sample_conditions_2 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18544 1 3 '2D CC' no . . . . . . . . . . 1 $sample_DsbA(C33S)_DsbB solid . . 2 $sample_conditions_2 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18544 1 4 '2D TEDOR' no . . . . . . . . . . 1 $sample_DsbA(C33S)_DsbB solid . . 2 $sample_conditions_2 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18544 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 18544 _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 . . . . . . . 18544 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 other other . . . . . . . 18544 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_chemical_shifts_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shifts_1 _Assigned_chem_shift_list.Entry_ID 18544 _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' . . . 18544 1 2 '3D NCOCX' . . . 18544 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 4 4 GLU CA C 13 55.400 0.30 . 1 . . . . 4 GLU CA . 18544 1 2 . 1 1 4 4 GLU CG C 13 36.800 0.30 . 1 . . . . 4 GLU CG . 18544 1 3 . 1 1 5 5 ASP N N 15 125.848 0.30 . 1 . . . . 5 ASP N . 18544 1 4 . 1 1 6 6 GLY C C 13 173.119 0.30 . 1 . . . . 6 GLY C . 18544 1 5 . 1 1 6 6 GLY CA C 13 44.770 0.30 . 1 . . . . 6 GLY CA . 18544 1 6 . 1 1 6 6 GLY N N 15 116.910 0.30 . 1 . . . . 6 GLY N . 18544 1 7 . 1 1 7 7 LYS CA C 13 57.384 0.30 . 1 . . . . 7 LYS CA . 18544 1 8 . 1 1 7 7 LYS CB C 13 32.099 0.30 . 1 . . . . 7 LYS CB . 18544 1 9 . 1 1 7 7 LYS CG C 13 25.144 0.30 . 1 . . . . 7 LYS CG . 18544 1 10 . 1 1 7 7 LYS N N 15 122.456 0.30 . 1 . . . . 7 LYS N . 18544 1 11 . 1 1 8 8 GLN C C 13 173.952 0.30 . 1 . . . . 8 GLN C . 18544 1 12 . 1 1 8 8 GLN CA C 13 59.315 0.30 . 1 . . . . 8 GLN CA . 18544 1 13 . 1 1 8 8 GLN CB C 13 26.993 0.30 . 1 . . . . 8 GLN CB . 18544 1 14 . 1 1 8 8 GLN CG C 13 33.620 0.30 . 1 . . . . 8 GLN CG . 18544 1 15 . 1 1 9 9 TYR C C 13 172.156 0.30 . 1 . . . . 9 TYR C . 18544 1 16 . 1 1 9 9 TYR CA C 13 54.800 0.30 . 1 . . . . 9 TYR CA . 18544 1 17 . 1 1 9 9 TYR N N 15 111.349 0.30 . 1 . . . . 9 TYR N . 18544 1 18 . 1 1 10 10 THR C C 13 174.517 0.30 . 1 . . . . 10 THR C . 18544 1 19 . 1 1 10 10 THR CA C 13 60.300 0.30 . 1 . . . . 10 THR CA . 18544 1 20 . 1 1 10 10 THR CB C 13 71.500 0.30 . 1 . . . . 10 THR CB . 18544 1 21 . 1 1 10 10 THR CG2 C 13 22.047 0.30 . 1 . . . . 10 THR CG2 . 18544 1 22 . 1 1 10 10 THR N N 15 111.374 0.30 . 1 . . . . 10 THR N . 18544 1 23 . 1 1 11 11 THR C C 13 175.401 0.30 . 1 . . . . 11 THR C . 18544 1 24 . 1 1 11 11 THR CA C 13 62.900 0.30 . 1 . . . . 11 THR CA . 18544 1 25 . 1 1 11 11 THR CB C 13 69.800 0.30 . 1 . . . . 11 THR CB . 18544 1 26 . 1 1 11 11 THR CG2 C 13 21.700 0.30 . 1 . . . . 11 THR CG2 . 18544 1 27 . 1 1 11 11 THR N N 15 120.544 0.30 . 1 . . . . 11 THR N . 18544 1 28 . 1 1 12 12 LEU CA C 13 56.100 0.30 . 1 . . . . 12 LEU CA . 18544 1 29 . 1 1 12 12 LEU CB C 13 41.538 0.30 . 1 . . . . 12 LEU CB . 18544 1 30 . 1 1 12 12 LEU CG C 13 28.644 0.30 . 1 . . . . 12 LEU CG . 18544 1 31 . 1 1 12 12 LEU CD1 C 13 24.311 0.30 . 2 . . . . 12 LEU CD1 . 18544 1 32 . 1 1 12 12 LEU CD2 C 13 23.548 0.30 . 2 . . . . 12 LEU CD2 . 18544 1 33 . 1 1 12 12 LEU N N 15 129.300 0.30 . 1 . . . . 12 LEU N . 18544 1 34 . 1 1 14 14 LYS N N 15 117.764 0.30 . 1 . . . . 14 LYS N . 18544 1 35 . 1 1 15 15 PRO CA C 13 62.478 0.30 . 1 . . . . 15 PRO CA . 18544 1 36 . 1 1 15 15 PRO CB C 13 32.620 0.30 . 1 . . . . 15 PRO CB . 18544 1 37 . 1 1 15 15 PRO CG C 13 27.385 0.30 . 1 . . . . 15 PRO CG . 18544 1 38 . 1 1 15 15 PRO CD C 13 50.787 0.30 . 1 . . . . 15 PRO CD . 18544 1 39 . 1 1 15 15 PRO N N 15 135.765 0.30 . 1 . . . . 15 PRO N . 18544 1 40 . 1 1 16 16 VAL C C 13 175.923 0.30 . 1 . . . . 16 VAL C . 18544 1 41 . 1 1 16 16 VAL CA C 13 61.330 0.30 . 1 . . . . 16 VAL CA . 18544 1 42 . 1 1 16 16 VAL CB C 13 32.858 0.30 . 1 . . . . 16 VAL CB . 18544 1 43 . 1 1 16 16 VAL CG1 C 13 21.698 0.30 . 2 . . . . 16 VAL CG1 . 18544 1 44 . 1 1 16 16 VAL CG2 C 13 21.698 0.30 . 2 . . . . 16 VAL CG2 . 18544 1 45 . 1 1 16 16 VAL N N 15 123.744 0.30 . 1 . . . . 16 VAL N . 18544 1 46 . 1 1 17 17 ALA C C 13 178.981 0.30 . 1 . . . . 17 ALA C . 18544 1 47 . 1 1 17 17 ALA CA C 13 52.255 0.30 . 1 . . . . 17 ALA CA . 18544 1 48 . 1 1 17 17 ALA CB C 13 19.200 0.30 . 1 . . . . 17 ALA CB . 18544 1 49 . 1 1 17 17 ALA N N 15 132.800 0.30 . 1 . . . . 17 ALA N . 18544 1 50 . 1 1 18 18 GLY CA C 13 45.487 0.30 . 1 . . . . 18 GLY CA . 18544 1 51 . 1 1 18 18 GLY N N 15 111.191 0.30 . 1 . . . . 18 GLY N . 18544 1 52 . 1 1 19 19 ALA C C 13 175.340 0.30 . 1 . . . . 19 ALA C . 18544 1 53 . 1 1 19 19 ALA CA C 13 50.400 0.30 . 1 . . . . 19 ALA CA . 18544 1 54 . 1 1 19 19 ALA CB C 13 17.297 0.30 . 1 . . . . 19 ALA CB . 18544 1 55 . 1 1 19 19 ALA N N 15 122.097 0.30 . 1 . . . . 19 ALA N . 18544 1 56 . 1 1 20 20 PRO CA C 13 62.598 0.30 . 1 . . . . 20 PRO CA . 18544 1 57 . 1 1 20 20 PRO CB C 13 31.807 0.30 . 1 . . . . 20 PRO CB . 18544 1 58 . 1 1 20 20 PRO CG C 13 27.923 0.30 . 1 . . . . 20 PRO CG . 18544 1 59 . 1 1 20 20 PRO CD C 13 50.282 0.30 . 1 . . . . 20 PRO CD . 18544 1 60 . 1 1 20 20 PRO N N 15 134.142 0.30 . 1 . . . . 20 PRO N . 18544 1 61 . 1 1 22 22 VAL C C 13 172.928 0.30 . 1 . . . . 22 VAL C . 18544 1 62 . 1 1 22 22 VAL CA C 13 62.701 0.30 . 1 . . . . 22 VAL CA . 18544 1 63 . 1 1 22 22 VAL CB C 13 34.082 0.30 . 1 . . . . 22 VAL CB . 18544 1 64 . 1 1 22 22 VAL CG1 C 13 23.146 0.30 . 2 . . . . 22 VAL CG1 . 18544 1 65 . 1 1 22 22 VAL CG2 C 13 21.393 0.30 . 2 . . . . 22 VAL CG2 . 18544 1 66 . 1 1 23 23 LEU C C 13 173.410 0.30 . 1 . . . . 23 LEU C . 18544 1 67 . 1 1 23 23 LEU CA C 13 52.497 0.30 . 1 . . . . 23 LEU CA . 18544 1 68 . 1 1 23 23 LEU CB C 13 46.123 0.30 . 1 . . . . 23 LEU CB . 18544 1 69 . 1 1 23 23 LEU CG C 13 26.780 0.30 . 1 . . . . 23 LEU CG . 18544 1 70 . 1 1 23 23 LEU CD1 C 13 22.479 0.30 . 1 . . . . 23 LEU CD . 18544 1 71 . 1 1 23 23 LEU CD2 C 13 22.479 0.30 . 1 . . . . 23 LEU CD . 18544 1 72 . 1 1 23 23 LEU N N 15 129.000 0.30 . 1 . . . . 23 LEU N . 18544 1 73 . 1 1 26 26 PHE C C 13 170.362 0.30 . 1 . . . . 26 PHE C . 18544 1 74 . 1 1 26 26 PHE CA C 13 55.351 0.30 . 1 . . . . 26 PHE CA . 18544 1 75 . 1 1 27 27 SER C C 13 177.849 0.30 . 1 . . . . 27 SER C . 18544 1 76 . 1 1 27 27 SER CA C 13 54.816 0.30 . 1 . . . . 27 SER CA . 18544 1 77 . 1 1 27 27 SER CB C 13 65.276 0.30 . 1 . . . . 27 SER CB . 18544 1 78 . 1 1 27 27 SER N N 15 107.820 0.30 . 1 . . . . 27 SER N . 18544 1 79 . 1 1 28 28 PHE N N 15 131.179 0.30 . 1 . . . . 28 PHE N . 18544 1 80 . 1 1 39 39 VAL CA C 13 64.002 0.30 . 1 . . . . 39 VAL CA . 18544 1 81 . 1 1 39 39 VAL CB C 13 32.551 0.30 . 1 . . . . 39 VAL CB . 18544 1 82 . 1 1 39 39 VAL CG1 C 13 21.059 0.30 . 2 . . . . 39 VAL CG1 . 18544 1 83 . 1 1 39 39 VAL N N 15 116.500 0.30 . 1 . . . . 39 VAL N . 18544 1 84 . 1 1 40 40 LEU CA C 13 55.364 0.30 . 1 . . . . 40 LEU CA . 18544 1 85 . 1 1 40 40 LEU CG C 13 27.221 0.30 . 1 . . . . 40 LEU CG . 18544 1 86 . 1 1 46 46 VAL CA C 13 66.993 0.30 . 1 . . . . 46 VAL CA . 18544 1 87 . 1 1 46 46 VAL CB C 13 32.082 0.30 . 1 . . . . 46 VAL CB . 18544 1 88 . 1 1 46 46 VAL CG1 C 13 24.121 0.30 . 2 . . . . 46 VAL CG1 . 18544 1 89 . 1 1 46 46 VAL CG2 C 13 22.435 0.30 . 2 . . . . 46 VAL CG2 . 18544 1 90 . 1 1 50 50 LEU CB C 13 41.200 0.30 . 1 . . . . 50 LEU CB . 18544 1 91 . 1 1 51 51 PRO CA C 13 64.938 0.30 . 1 . . . . 51 PRO CA . 18544 1 92 . 1 1 51 51 PRO CB C 13 31.970 0.30 . 1 . . . . 51 PRO CB . 18544 1 93 . 1 1 51 51 PRO CG C 13 28.083 0.30 . 1 . . . . 51 PRO CG . 18544 1 94 . 1 1 51 51 PRO CD C 13 52.565 0.30 . 1 . . . . 51 PRO CD . 18544 1 95 . 1 1 51 51 PRO N N 15 153.189 0.30 . 1 . . . . 51 PRO N . 18544 1 96 . 1 1 53 53 GLY N N 15 111.404 0.30 . 1 . . . . 53 GLY N . 18544 1 97 . 1 1 54 54 VAL CA C 13 62.501 0.30 . 1 . . . . 54 VAL CA . 18544 1 98 . 1 1 54 54 VAL CB C 13 31.670 0.30 . 1 . . . . 54 VAL CB . 18544 1 99 . 1 1 54 54 VAL CG1 C 13 22.465 0.30 . 2 . . . . 54 VAL CG1 . 18544 1 100 . 1 1 57 57 THR CA C 13 62.966 0.30 . 1 . . . . 57 THR CA . 18544 1 101 . 1 1 57 57 THR CB C 13 70.475 0.30 . 1 . . . . 57 THR CB . 18544 1 102 . 1 1 57 57 THR CG2 C 13 22.331 0.30 . 1 . . . . 57 THR CG2 . 18544 1 103 . 1 1 59 59 TYR CA C 13 52.062 0.30 . 1 . . . . 59 TYR CA . 18544 1 104 . 1 1 59 59 TYR CB C 13 40.812 0.30 . 1 . . . . 59 TYR CB . 18544 1 105 . 1 1 66 66 GLY C C 13 177.086 0.30 . 1 . . . . 66 GLY C . 18544 1 106 . 1 1 66 66 GLY CA C 13 45.537 0.30 . 1 . . . . 66 GLY CA . 18544 1 107 . 1 1 67 67 ASP N N 15 129.097 0.30 . 1 . . . . 67 ASP N . 18544 1 108 . 1 1 68 68 LEU C C 13 179.175 0.30 . 1 . . . . 68 LEU C . 18544 1 109 . 1 1 68 68 LEU CA C 13 57.121 0.30 . 1 . . . . 68 LEU CA . 18544 1 110 . 1 1 69 69 GLY CA C 13 47.963 0.30 . 1 . . . . 69 GLY CA . 18544 1 111 . 1 1 69 69 GLY N N 15 106.917 0.30 . 1 . . . . 69 GLY N . 18544 1 112 . 1 1 72 72 LEU CA C 13 57.957 0.30 . 1 . . . . 72 LEU CA . 18544 1 113 . 1 1 72 72 LEU CG C 13 28.388 0.30 . 1 . . . . 72 LEU CG . 18544 1 114 . 1 1 73 73 THR C C 13 176.764 0.30 . 1 . . . . 73 THR C . 18544 1 115 . 1 1 73 73 THR CA C 13 66.744 0.30 . 1 . . . . 73 THR CA . 18544 1 116 . 1 1 73 73 THR CB C 13 68.496 0.30 . 1 . . . . 73 THR CB . 18544 1 117 . 1 1 74 74 GLN CA C 13 59.734 0.30 . 1 . . . . 74 GLN CA . 18544 1 118 . 1 1 74 74 GLN CB C 13 25.946 0.30 . 1 . . . . 74 GLN CB . 18544 1 119 . 1 1 74 74 GLN N N 15 125.801 0.30 . 1 . . . . 74 GLN N . 18544 1 120 . 1 1 75 75 ALA CA C 13 54.726 0.30 . 1 . . . . 75 ALA CA . 18544 1 121 . 1 1 75 75 ALA CB C 13 20.161 0.30 . 1 . . . . 75 ALA CB . 18544 1 122 . 1 1 75 75 ALA N N 15 123.401 0.30 . 1 . . . . 75 ALA N . 18544 1 123 . 1 1 77 77 ALA CA C 13 55.200 0.30 . 1 . . . . 77 ALA CA . 18544 1 124 . 1 1 77 77 ALA CB C 13 20.378 0.30 . 1 . . . . 77 ALA CB . 18544 1 125 . 1 1 77 77 ALA N N 15 120.096 0.30 . 1 . . . . 77 ALA N . 18544 1 126 . 1 1 78 78 VAL C C 13 177.000 0.30 . 1 . . . . 78 VAL C . 18544 1 127 . 1 1 78 78 VAL CA C 13 66.900 0.30 . 1 . . . . 78 VAL CA . 18544 1 128 . 1 1 78 78 VAL CB C 13 30.293 0.30 . 1 . . . . 78 VAL CB . 18544 1 129 . 1 1 78 78 VAL CG1 C 13 23.624 0.30 . 2 . . . . 78 VAL CG1 . 18544 1 130 . 1 1 78 78 VAL CG2 C 13 22.267 0.30 . 2 . . . . 78 VAL CG2 . 18544 1 131 . 1 1 78 78 VAL N N 15 119.679 0.30 . 1 . . . . 78 VAL N . 18544 1 132 . 1 1 79 79 ALA C C 13 179.796 0.30 . 1 . . . . 79 ALA C . 18544 1 133 . 1 1 79 79 ALA CA C 13 54.726 0.30 . 1 . . . . 79 ALA CA . 18544 1 134 . 1 1 79 79 ALA N N 15 120.811 0.30 . 1 . . . . 79 ALA N . 18544 1 135 . 1 1 80 80 MET C C 13 179.401 0.30 . 1 . . . . 80 MET C . 18544 1 136 . 1 1 80 80 MET CA C 13 58.153 0.30 . 1 . . . . 80 MET CA . 18544 1 137 . 1 1 80 80 MET CB C 13 34.573 0.30 . 1 . . . . 80 MET CB . 18544 1 138 . 1 1 80 80 MET CG C 13 31.003 0.30 . 1 . . . . 80 MET CG . 18544 1 139 . 1 1 80 80 MET N N 15 115.652 0.30 . 1 . . . . 80 MET N . 18544 1 140 . 1 1 81 81 ALA C C 13 180.222 0.30 . 1 . . . . 81 ALA C . 18544 1 141 . 1 1 81 81 ALA CA C 13 54.577 0.30 . 1 . . . . 81 ALA CA . 18544 1 142 . 1 1 81 81 ALA N N 15 123.461 0.30 . 1 . . . . 81 ALA N . 18544 1 143 . 1 1 82 82 LEU C C 13 177.575 0.30 . 1 . . . . 82 LEU C . 18544 1 144 . 1 1 82 82 LEU CA C 13 54.404 0.30 . 1 . . . . 82 LEU CA . 18544 1 145 . 1 1 82 82 LEU CB C 13 42.984 0.30 . 1 . . . . 82 LEU CB . 18544 1 146 . 1 1 82 82 LEU CG C 13 26.964 0.30 . 1 . . . . 82 LEU CG . 18544 1 147 . 1 1 82 82 LEU CD1 C 13 22.100 0.30 . 1 . . . . 82 LEU CD . 18544 1 148 . 1 1 82 82 LEU CD2 C 13 22.100 0.30 . 1 . . . . 82 LEU CD . 18544 1 149 . 1 1 82 82 LEU N N 15 113.178 0.30 . 1 . . . . 82 LEU N . 18544 1 150 . 1 1 83 83 GLY C C 13 176.909 0.30 . 1 . . . . 83 GLY C . 18544 1 151 . 1 1 83 83 GLY CA C 13 47.083 0.30 . 1 . . . . 83 GLY CA . 18544 1 152 . 1 1 83 83 GLY N N 15 111.275 0.30 . 1 . . . . 83 GLY N . 18544 1 153 . 1 1 84 84 VAL C C 13 176.749 0.30 . 1 . . . . 84 VAL C . 18544 1 154 . 1 1 84 84 VAL CA C 13 59.102 0.30 . 1 . . . . 84 VAL CA . 18544 1 155 . 1 1 84 84 VAL CB C 13 31.582 0.30 . 1 . . . . 84 VAL CB . 18544 1 156 . 1 1 84 84 VAL CG1 C 13 20.582 0.30 . 2 . . . . 84 VAL CG1 . 18544 1 157 . 1 1 84 84 VAL CG2 C 13 19.290 0.30 . 2 . . . . 84 VAL CG2 . 18544 1 158 . 1 1 84 84 VAL N N 15 108.375 0.30 . 1 . . . . 84 VAL N . 18544 1 159 . 1 1 85 85 GLU C C 13 179.245 0.30 . 1 . . . . 85 GLU C . 18544 1 160 . 1 1 85 85 GLU CA C 13 61.539 0.30 . 1 . . . . 85 GLU CA . 18544 1 161 . 1 1 85 85 GLU CB C 13 29.403 0.30 . 1 . . . . 85 GLU CB . 18544 1 162 . 1 1 85 85 GLU CG C 13 36.312 0.30 . 1 . . . . 85 GLU CG . 18544 1 163 . 1 1 85 85 GLU N N 15 126.854 0.30 . 1 . . . . 85 GLU N . 18544 1 164 . 1 1 86 86 ASP C C 13 177.583 0.30 . 1 . . . . 86 ASP C . 18544 1 165 . 1 1 86 86 ASP CA C 13 55.753 0.30 . 1 . . . . 86 ASP CA . 18544 1 166 . 1 1 87 87 LYS C C 13 178.039 0.30 . 1 . . . . 87 LYS C . 18544 1 167 . 1 1 87 87 LYS CA C 13 57.366 0.30 . 1 . . . . 87 LYS CA . 18544 1 168 . 1 1 87 87 LYS CB C 13 34.395 0.30 . 1 . . . . 87 LYS CB . 18544 1 169 . 1 1 87 87 LYS CG C 13 25.718 0.30 . 1 . . . . 87 LYS CG . 18544 1 170 . 1 1 87 87 LYS CD C 13 29.490 0.30 . 1 . . . . 87 LYS CD . 18544 1 171 . 1 1 88 88 VAL C C 13 175.866 0.30 . 1 . . . . 88 VAL C . 18544 1 172 . 1 1 88 88 VAL CA C 13 60.535 0.30 . 1 . . . . 88 VAL CA . 18544 1 173 . 1 1 88 88 VAL CB C 13 32.992 0.30 . 1 . . . . 88 VAL CB . 18544 1 174 . 1 1 88 88 VAL CG1 C 13 19.473 0.30 . 2 . . . . 88 VAL CG1 . 18544 1 175 . 1 1 88 88 VAL CG2 C 13 17.644 0.30 . 2 . . . . 88 VAL CG2 . 18544 1 176 . 1 1 88 88 VAL N N 15 103.481 0.30 . 1 . . . . 88 VAL N . 18544 1 177 . 1 1 89 89 THR CA C 13 69.137 0.30 . 1 . . . . 89 THR CA . 18544 1 178 . 1 1 89 89 THR CG2 C 13 21.426 0.30 . 1 . . . . 89 THR CG2 . 18544 1 179 . 1 1 90 90 VAL C C 13 176.028 0.30 . 1 . . . . 90 VAL C . 18544 1 180 . 1 1 90 90 VAL CA C 13 69.447 0.30 . 1 . . . . 90 VAL CA . 18544 1 181 . 1 1 90 90 VAL CB C 13 28.876 0.30 . 1 . . . . 90 VAL CB . 18544 1 182 . 1 1 90 90 VAL CG1 C 13 24.694 0.30 . 2 . . . . 90 VAL CG1 . 18544 1 183 . 1 1 90 90 VAL CG2 C 13 21.638 0.30 . 2 . . . . 90 VAL CG2 . 18544 1 184 . 1 1 91 91 PRO N N 15 134.083 0.30 . 1 . . . . 91 PRO N . 18544 1 185 . 1 1 92 92 LEU CA C 13 58.013 0.30 . 1 . . . . 92 LEU CA . 18544 1 186 . 1 1 92 92 LEU CB C 13 40.307 0.30 . 1 . . . . 92 LEU CB . 18544 1 187 . 1 1 92 92 LEU CG C 13 27.137 0.30 . 1 . . . . 92 LEU CG . 18544 1 188 . 1 1 92 92 LEU CD1 C 13 23.125 0.30 . 1 . . . . 92 LEU CD . 18544 1 189 . 1 1 92 92 LEU CD2 C 13 23.125 0.30 . 1 . . . . 92 LEU CD . 18544 1 190 . 1 1 94 94 GLU C C 13 180.235 0.30 . 1 . . . . 94 GLU C . 18544 1 191 . 1 1 94 94 GLU CA C 13 59.378 0.30 . 1 . . . . 94 GLU CA . 18544 1 192 . 1 1 95 95 GLY C C 13 175.565 0.30 . 1 . . . . 95 GLY C . 18544 1 193 . 1 1 95 95 GLY CA C 13 46.033 0.30 . 1 . . . . 95 GLY CA . 18544 1 194 . 1 1 95 95 GLY N N 15 107.790 0.30 . 1 . . . . 95 GLY N . 18544 1 195 . 1 1 96 96 VAL CA C 13 66.476 0.30 . 1 . . . . 96 VAL CA . 18544 1 196 . 1 1 96 96 VAL CB C 13 32.243 0.30 . 1 . . . . 96 VAL CB . 18544 1 197 . 1 1 96 96 VAL CG1 C 13 23.389 0.30 . 2 . . . . 96 VAL CG1 . 18544 1 198 . 1 1 99 99 THR CA C 13 62.078 0.30 . 1 . . . . 99 THR CA . 18544 1 199 . 1 1 99 99 THR CB C 13 68.727 0.30 . 1 . . . . 99 THR CB . 18544 1 200 . 1 1 99 99 THR CG2 C 13 22.368 0.30 . 1 . . . . 99 THR CG2 . 18544 1 201 . 1 1 100 100 GLN C C 13 175.004 0.30 . 1 . . . . 100 GLN C . 18544 1 202 . 1 1 100 100 GLN CA C 13 57.357 0.30 . 1 . . . . 100 GLN CA . 18544 1 203 . 1 1 100 100 GLN CB C 13 25.724 0.30 . 1 . . . . 100 GLN CB . 18544 1 204 . 1 1 100 100 GLN CG C 13 34.618 0.30 . 1 . . . . 100 GLN CG . 18544 1 205 . 1 1 101 101 THR C C 13 175.391 0.30 . 1 . . . . 101 THR C . 18544 1 206 . 1 1 101 101 THR CA C 13 60.592 0.30 . 1 . . . . 101 THR CA . 18544 1 207 . 1 1 101 101 THR CB C 13 68.865 0.30 . 1 . . . . 101 THR CB . 18544 1 208 . 1 1 101 101 THR CG2 C 13 22.960 0.30 . 1 . . . . 101 THR CG2 . 18544 1 209 . 1 1 101 101 THR N N 15 105.649 0.30 . 1 . . . . 101 THR N . 18544 1 210 . 1 1 102 102 ILE CA C 13 60.773 0.30 . 1 . . . . 102 ILE CA . 18544 1 211 . 1 1 102 102 ILE CB C 13 36.956 0.30 . 1 . . . . 102 ILE CB . 18544 1 212 . 1 1 102 102 ILE CG1 C 13 27.278 0.30 . 1 . . . . 102 ILE CG1 . 18544 1 213 . 1 1 102 102 ILE CG2 C 13 17.457 0.30 . 1 . . . . 102 ILE CG2 . 18544 1 214 . 1 1 102 102 ILE CD1 C 13 14.866 0.30 . 1 . . . . 102 ILE CD1 . 18544 1 215 . 1 1 103 103 ARG CA C 13 55.029 0.30 . 1 . . . . 103 ARG CA . 18544 1 216 . 1 1 103 103 ARG N N 15 125.129 0.30 . 1 . . . . 103 ARG N . 18544 1 217 . 1 1 104 104 SER CA C 13 56.499 0.30 . 1 . . . . 104 SER CA . 18544 1 218 . 1 1 104 104 SER CB C 13 67.404 0.30 . 1 . . . . 104 SER CB . 18544 1 219 . 1 1 104 104 SER N N 15 114.972 0.30 . 1 . . . . 104 SER N . 18544 1 220 . 1 1 105 105 ALA C C 13 181.000 0.30 . 1 . . . . 105 ALA C . 18544 1 221 . 1 1 105 105 ALA CA C 13 54.976 0.30 . 1 . . . . 105 ALA CA . 18544 1 222 . 1 1 105 105 ALA CB C 13 17.100 0.30 . 1 . . . . 105 ALA CB . 18544 1 223 . 1 1 105 105 ALA N N 15 123.500 0.30 . 1 . . . . 105 ALA N . 18544 1 224 . 1 1 106 106 SER CA C 13 61.336 0.30 . 1 . . . . 106 SER CA . 18544 1 225 . 1 1 106 106 SER CB C 13 62.542 0.30 . 1 . . . . 106 SER CB . 18544 1 226 . 1 1 106 106 SER N N 15 116.024 0.30 . 1 . . . . 106 SER N . 18544 1 227 . 1 1 107 107 ASP C C 13 178.883 0.30 . 1 . . . . 107 ASP C . 18544 1 228 . 1 1 108 108 ILE CA C 13 65.614 0.30 . 1 . . . . 108 ILE CA . 18544 1 229 . 1 1 108 108 ILE CB C 13 38.333 0.30 . 1 . . . . 108 ILE CB . 18544 1 230 . 1 1 108 108 ILE CG1 C 13 28.856 0.30 . 1 . . . . 108 ILE CG1 . 18544 1 231 . 1 1 108 108 ILE CG2 C 13 18.532 0.30 . 1 . . . . 108 ILE CG2 . 18544 1 232 . 1 1 108 108 ILE CD1 C 13 15.618 0.30 . 1 . . . . 108 ILE CD1 . 18544 1 233 . 1 1 108 108 ILE N N 15 120.080 0.30 . 1 . . . . 108 ILE N . 18544 1 234 . 1 1 111 111 VAL CA C 13 66.402 0.30 . 1 . . . . 111 VAL CA . 18544 1 235 . 1 1 111 111 VAL CB C 13 30.739 0.30 . 1 . . . . 111 VAL CB . 18544 1 236 . 1 1 111 111 VAL CG1 C 13 23.631 0.30 . 2 . . . . 111 VAL CG1 . 18544 1 237 . 1 1 111 111 VAL CG2 C 13 21.740 0.30 . 2 . . . . 111 VAL CG2 . 18544 1 238 . 1 1 113 113 ILE C C 13 182.362 0.30 . 1 . . . . 113 ILE C . 18544 1 239 . 1 1 113 113 ILE CA C 13 63.762 0.30 . 1 . . . . 113 ILE CA . 18544 1 240 . 1 1 113 113 ILE CB C 13 37.970 0.30 . 1 . . . . 113 ILE CB . 18544 1 241 . 1 1 113 113 ILE CG1 C 13 28.281 0.30 . 1 . . . . 113 ILE CG1 . 18544 1 242 . 1 1 113 113 ILE CG2 C 13 17.371 0.30 . 1 . . . . 113 ILE CG2 . 18544 1 243 . 1 1 113 113 ILE CD1 C 13 13.802 0.30 . 1 . . . . 113 ILE CD1 . 18544 1 244 . 1 1 114 114 ASN CA C 13 55.695 0.30 . 1 . . . . 114 ASN CA . 18544 1 245 . 1 1 114 114 ASN CB C 13 37.871 0.30 . 1 . . . . 114 ASN CB . 18544 1 246 . 1 1 114 114 ASN N N 15 121.071 0.30 . 1 . . . . 114 ASN N . 18544 1 247 . 1 1 115 115 ALA C C 13 176.912 0.30 . 1 . . . . 115 ALA C . 18544 1 248 . 1 1 115 115 ALA CA C 13 51.607 0.30 . 1 . . . . 115 ALA CA . 18544 1 249 . 1 1 115 115 ALA CB C 13 19.099 0.30 . 1 . . . . 115 ALA CB . 18544 1 250 . 1 1 115 115 ALA N N 15 120.639 0.30 . 1 . . . . 115 ALA N . 18544 1 251 . 1 1 116 116 GLY C C 13 173.782 0.30 . 1 . . . . 116 GLY C . 18544 1 252 . 1 1 116 116 GLY CA C 13 44.896 0.30 . 1 . . . . 116 GLY CA . 18544 1 253 . 1 1 116 116 GLY N N 15 105.361 0.30 . 1 . . . . 116 GLY N . 18544 1 254 . 1 1 117 117 ILE CA C 13 60.988 0.30 . 1 . . . . 117 ILE CA . 18544 1 255 . 1 1 117 117 ILE CB C 13 37.546 0.30 . 1 . . . . 117 ILE CB . 18544 1 256 . 1 1 117 117 ILE CG1 C 13 25.886 0.30 . 1 . . . . 117 ILE CG1 . 18544 1 257 . 1 1 117 117 ILE CG2 C 13 20.655 0.30 . 1 . . . . 117 ILE CG2 . 18544 1 258 . 1 1 117 117 ILE N N 15 125.476 0.30 . 1 . . . . 117 ILE N . 18544 1 259 . 1 1 118 118 LYS C C 13 179.413 0.30 . 1 . . . . 118 LYS C . 18544 1 260 . 1 1 119 119 GLY N N 15 113.971 0.30 . 1 . . . . 119 GLY N . 18544 1 261 . 1 1 126 126 TRP CA C 13 61.507 0.30 . 1 . . . . 126 TRP CA . 18544 1 262 . 1 1 126 126 TRP CB C 13 28.525 0.30 . 1 . . . . 126 TRP CB . 18544 1 263 . 1 1 128 128 SER CA C 13 58.714 0.30 . 1 . . . . 128 SER CA . 18544 1 264 . 1 1 128 128 SER CB C 13 65.790 0.30 . 1 . . . . 128 SER CB . 18544 1 265 . 1 1 128 128 SER N N 15 116.192 0.30 . 1 . . . . 128 SER N . 18544 1 266 . 1 1 130 130 VAL CA C 13 67.300 0.30 . 1 . . . . 130 VAL CA . 18544 1 267 . 1 1 130 130 VAL CB C 13 30.374 0.30 . 1 . . . . 130 VAL CB . 18544 1 268 . 1 1 131 131 VAL CA C 13 67.185 0.30 . 1 . . . . 131 VAL CA . 18544 1 269 . 1 1 131 131 VAL CB C 13 31.455 0.30 . 1 . . . . 131 VAL CB . 18544 1 270 . 1 1 134 134 LEU CB C 13 44.075 0.30 . 1 . . . . 134 LEU CB . 18544 1 271 . 1 1 134 134 LEU CG C 13 27.321 0.30 . 1 . . . . 134 LEU CG . 18544 1 272 . 1 1 135 135 VAL CA C 13 68.701 0.30 . 1 . . . . 135 VAL CA . 18544 1 273 . 1 1 135 135 VAL CB C 13 31.453 0.30 . 1 . . . . 135 VAL CB . 18544 1 274 . 1 1 135 135 VAL CG1 C 13 23.885 0.30 . 2 . . . . 135 VAL CG1 . 18544 1 275 . 1 1 135 135 VAL CG2 C 13 21.404 0.30 . 2 . . . . 135 VAL CG2 . 18544 1 276 . 1 1 135 135 VAL N N 15 123.026 0.30 . 1 . . . . 135 VAL N . 18544 1 277 . 1 1 136 136 ALA N N 15 121.026 0.30 . 1 . . . . 136 ALA N . 18544 1 278 . 1 1 141 141 ALA C C 13 179.649 0.30 . 1 . . . . 141 ALA C . 18544 1 279 . 1 1 141 141 ALA CA C 13 55.149 0.30 . 1 . . . . 141 ALA CA . 18544 1 280 . 1 1 142 142 ALA CA C 13 53.949 0.30 . 1 . . . . 142 ALA CA . 18544 1 281 . 1 1 142 142 ALA N N 15 116.928 0.30 . 1 . . . . 142 ALA N . 18544 1 282 . 1 1 143 143 ALA CA C 13 54.391 0.30 . 1 . . . . 143 ALA CA . 18544 1 283 . 1 1 144 144 ASP C C 13 178.504 0.30 . 1 . . . . 144 ASP C . 18544 1 284 . 1 1 145 145 VAL CA C 13 60.384 0.30 . 1 . . . . 145 VAL CA . 18544 1 285 . 1 1 145 145 VAL CB C 13 31.107 0.30 . 1 . . . . 145 VAL CB . 18544 1 286 . 1 1 145 145 VAL CG1 C 13 20.126 0.30 . 2 . . . . 145 VAL CG1 . 18544 1 287 . 1 1 145 145 VAL CG2 C 13 19.018 0.30 . 2 . . . . 145 VAL CG2 . 18544 1 288 . 1 1 145 145 VAL N N 15 108.467 0.30 . 1 . . . . 145 VAL N . 18544 1 289 . 1 1 146 146 GLN CA C 13 55.921 0.30 . 1 . . . . 146 GLN CA . 18544 1 290 . 1 1 146 146 GLN CB C 13 26.233 0.30 . 1 . . . . 146 GLN CB . 18544 1 291 . 1 1 150 150 VAL CA C 13 58.211 0.30 . 1 . . . . 150 VAL CA . 18544 1 292 . 1 1 150 150 VAL CG1 C 13 26.026 0.30 . 2 . . . . 150 VAL CG1 . 18544 1 293 . 1 1 155 155 VAL CA C 13 60.944 0.30 . 1 . . . . 155 VAL CA . 18544 1 294 . 1 1 155 155 VAL CB C 13 34.790 0.30 . 1 . . . . 155 VAL CB . 18544 1 295 . 1 1 155 155 VAL CG1 C 13 22.864 0.30 . 2 . . . . 155 VAL CG1 . 18544 1 296 . 1 1 155 155 VAL CG2 C 13 20.493 0.30 . 2 . . . . 155 VAL CG2 . 18544 1 297 . 1 1 156 156 ASN C C 13 174.078 0.30 . 1 . . . . 156 ASN C . 18544 1 298 . 1 1 156 156 ASN CA C 13 54.605 0.30 . 1 . . . . 156 ASN CA . 18544 1 299 . 1 1 156 156 ASN CB C 13 37.382 0.30 . 1 . . . . 156 ASN CB . 18544 1 300 . 1 1 157 157 GLY C C 13 172.357 0.30 . 1 . . . . 157 GLY C . 18544 1 301 . 1 1 157 157 GLY CA C 13 45.960 0.30 . 1 . . . . 157 GLY CA . 18544 1 302 . 1 1 157 157 GLY N N 15 105.310 0.30 . 1 . . . . 157 GLY N . 18544 1 303 . 1 1 158 158 LYS N N 15 114.286 0.30 . 1 . . . . 158 LYS N . 18544 1 304 . 1 1 160 160 GLN C C 13 175.725 0.30 . 1 . . . . 160 GLN C . 18544 1 305 . 1 1 160 160 GLN CA C 13 53.355 0.30 . 1 . . . . 160 GLN CA . 18544 1 306 . 1 1 163 163 PRO CA C 13 64.860 0.30 . 1 . . . . 163 PRO CA . 18544 1 307 . 1 1 163 163 PRO CB C 13 32.407 0.30 . 1 . . . . 163 PRO CB . 18544 1 308 . 1 1 163 163 PRO CG C 13 27.992 0.30 . 1 . . . . 163 PRO CG . 18544 1 309 . 1 1 163 163 PRO CD C 13 50.954 0.30 . 1 . . . . 163 PRO CD . 18544 1 310 . 1 1 169 169 SER CA C 13 61.006 0.30 . 1 . . . . 169 SER CA . 18544 1 311 . 1 1 169 169 SER CB C 13 63.351 0.30 . 1 . . . . 169 SER CB . 18544 1 312 . 1 1 173 173 VAL CA C 13 65.799 0.30 . 1 . . . . 173 VAL CA . 18544 1 313 . 1 1 173 173 VAL CB C 13 32.254 0.30 . 1 . . . . 173 VAL CB . 18544 1 314 . 1 1 175 175 VAL CA C 13 66.812 0.30 . 1 . . . . 175 VAL CA . 18544 1 315 . 1 1 175 175 VAL CB C 13 31.600 0.30 . 1 . . . . 175 VAL CB . 18544 1 316 . 1 1 175 175 VAL CG1 C 13 21.371 0.30 . 2 . . . . 175 VAL CG1 . 18544 1 317 . 1 1 175 175 VAL N N 15 116.900 0.30 . 1 . . . . 175 VAL N . 18544 1 318 . 1 1 182 182 VAL CA C 13 67.775 0.30 . 1 . . . . 182 VAL CA . 18544 1 319 . 1 1 182 182 VAL CB C 13 30.882 0.30 . 1 . . . . 182 VAL CB . 18544 1 320 . 1 1 182 182 VAL CG1 C 13 24.195 0.30 . 2 . . . . 182 VAL CG1 . 18544 1 321 . 1 1 185 185 LEU CA C 13 56.749 0.30 . 1 . . . . 185 LEU CA . 18544 1 322 . 1 1 185 185 LEU CB C 13 42.215 0.30 . 1 . . . . 185 LEU CB . 18544 1 323 . 1 1 185 185 LEU CG C 13 25.753 0.30 . 1 . . . . 185 LEU CG . 18544 1 stop_ save_