data_1813 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 1813 _Entry.Title ; Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-13 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Kasibhatla Chandrasekhar . . . 1813 2 Gunter Krause . . . 1813 3 Arne Holmgren . . . 1813 4 H. Dyson . Jane . 1813 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 1813 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 101 1813 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 5 . . 2010-06-15 . revision BMRB 'Complete natural source information' 1813 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1813 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 1813 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1813 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 1813 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 1813 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Chandrasekhar, Kasibhatla, Krause, Gunter, Holmgren, Arne, Dyson, H. Jane, "Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin," FEBS Lett. 284 (2), 178-183 (1991). ; _Citation.Title ; Assignment of the 15N NMR spectra of reduced and oxidized Escherichia coli thioredoxin ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'FEBS Lett.' _Citation.Journal_name_full . _Citation.Journal_volume 284 _Citation.Journal_issue 2 _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 178 _Citation.Page_last 183 _Citation.Year 1991 _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 Kasibhatla Chandrasekhar . . . 1813 1 2 Gunter Krause . . . 1813 1 3 Arne Holmgren . . . 1813 1 4 H. Dyson . Jane . 1813 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_thioredoxin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_thioredoxin _Assembly.Entry_ID 1813 _Assembly.ID 1 _Assembly.Name thioredoxin _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 thioredoxin 1 $thioredoxin . . . . . . . . . 1813 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID thioredoxin system 1813 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_thioredoxin _Entity.Sf_category entity _Entity.Sf_framecode thioredoxin _Entity.Entry_ID 1813 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name thioredoxin _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 ; SDKIIHLTDDSFDTDVLKAD GAILVDFWAEWCGPCKMIAP ILDEIADEYQGKLTVAKLNI DQNPGTAPKYGIRGIPTLLL FKNGEVAATKVGALSKGQLK EFLDANLA ; _Entity.Polymer_seq_one_letter_code ; SDKIIHLTDDSFDTDVLKAD GAILVDFWAEWCGPCKMIAP ILDEIADEYQGKLTVAKLNI DQNPGTAPKYGIRGIPTLLL FKNGEVAATKVGALSKGQLK EFLDANLA ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 108 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _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 17700 . TRX_intact . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 2 no BMRB 1812 . thioredoxin . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 3 no PDB 1F6M . "Crystal Structure Of A Complex Between Thioredoxin Reductase, Thioredoxin, And The Nadp+ Analog, Aadp+" . . . . . 100.00 108 99.07 99.07 1.18e-69 . . . . 1813 1 4 no PDB 1KEB . "Crystal Structure Of Double Mutant M37l,P40s E.Coli Thioredoxin" . . . . . 100.00 108 98.15 99.07 4.61e-69 . . . . 1813 1 5 no PDB 1SKR . "T7 Dna Polymerase Complexed To Dna Primer/template And Ddatp" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 6 no PDB 1SKS . "Binary 3' Complex Of T7 Dna Polymerase With A Dna PrimerTEMPLATE CONTAINING A CIS-Syn Thymine Dimer On The Template" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 7 no PDB 1SKW . "Binary 3' Complex Of T7 Dna Polymerase With A Dna PrimerTEMPLATE CONTAINING A DISORDERED CIS-Syn Thymine Dimer On The Template" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 8 no PDB 1SL0 . "Ternary 3' Complex Of T7 Dna Polymerase With A Dna PrimerTEMPLATE CONTAINING A DISORDERED CIS-Syn Thymine Dimer On The Template" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 9 no PDB 1SL1 . "Binary 5' Complex Of T7 Dna Polymerase With A Dna Primer/template Containing A Cis-syn Thymine Dimer On The Template" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 10 no PDB 1SL2 . "Ternary 5' Complex Of T7 Dna Polymerase With A Dna PrimerTEMPLATE CONTAINING A CIS-Syn Thymine Dimer On The Template And An Inc" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 11 no PDB 1T7P . "T7 Dna Polymerase Complexed To Dna PrimerTEMPLATE,A Nucleoside Triphosphate, And Its Processivity Factor Thioredoxin" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 12 no PDB 1T8E . "T7 Dna Polymerase Ternary Complex With Dctp At The Insertion Site." . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 13 no PDB 1THO . "Crystal Structure Of A Mutant Escherichia Coli Thioredoxin With An Arginine Insertion In The Active Site" . . . . . 100.93 109 99.08 99.08 5.98e-69 . . . . 1813 1 14 no PDB 1TK0 . "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Ddctp At The Insertion Site" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 15 no PDB 1TK5 . "T7 Dna Polymerase Binary Complex With 8 Oxo Guanosine In The Templating Strand" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 16 no PDB 1TK8 . "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Damp At The Elongation Site" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 17 no PDB 1TKD . "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Dcmp At The Elongation Site" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 18 no PDB 1TXX . "Active-Site Variant Of E.Coli Thioredoxin" . . . . . 100.00 108 98.15 98.15 8.03e-68 . . . . 1813 1 19 no PDB 1X9M . "T7 Dna Polymerase In Complex With An N-2- Acetylaminofluorene-adducted Dna" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 20 no PDB 1X9S . "T7 Dna Polymerase In Complex With A PrimerTEMPLATE DNA Containing A Disordered N-2 Aminofluorene On The Template, Crystallized " . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 21 no PDB 1X9W . "T7 Dna Polymerase In Complex With A Primer/template Dna Containing A Disordered N-2 Aminofluorene On The Template, Crystallized" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 22 no PDB 1XOA . "Thioredoxin (Oxidized Disulfide Form), Nmr, 20 Structures" . . . . . 99.07 108 100.00 100.00 5.43e-70 . . . . 1813 1 23 no PDB 1XOB . "Thioredoxin (Reduced Dithio Form), Nmr, 20 Structures" . . . . . 99.07 108 100.00 100.00 5.43e-70 . . . . 1813 1 24 no PDB 1ZCP . "Crystal Structure Of A Catalytic Site Mutant E. Coli Trxa (Caca)" . . . . . 100.00 108 97.22 97.22 3.32e-67 . . . . 1813 1 25 no PDB 1ZYQ . "T7 Dna Polymerase In Complex With 8og And Incoming Ddatp" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 26 no PDB 1ZZY . "Crystal Structure Of Thioredoxin Mutant L7v" . . . . . 100.00 108 99.07 100.00 2.48e-70 . . . . 1813 1 27 no PDB 2AJQ . "Structure Of Replicative Dna Polymerase Provides Insigts Into The Mechanisms For Processivity, Frameshifting And Editing" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 28 no PDB 2BTO . "Structure Of Btuba From Prosthecobacter Dejongeii" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 29 no PDB 2EIO . "Design Of Disulfide-Linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" . . . . . 100.00 108 99.07 99.07 2.61e-69 . . . . 1813 1 30 no PDB 2EIQ . "Design Of Disulfide-linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" . . . . . 100.00 108 99.07 99.07 8.05e-70 . . . . 1813 1 31 no PDB 2EIR . "Design Of Disulfide-Linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" . . . . . 100.00 108 98.15 98.15 1.15e-68 . . . . 1813 1 32 no PDB 2FCH . "Crystal Structure Of Thioredoxin Mutant G74s" . . . . . 100.00 108 99.07 99.07 5.32e-70 . . . . 1813 1 33 no PDB 2FD3 . "Crystal Structure Of Thioredoxin Mutant P34h" . . . . . 100.00 108 99.07 99.07 1.39e-69 . . . . 1813 1 34 no PDB 2H6X . "Crystal Structure Of Thioredoxin Wild Type In Hexagonal (P61) Space Group" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 35 no PDB 2H6Y . "Crystal Structure Of Thioredoxin Mutant E48d In Hexagonal (P61) Space Group" . . . . . 100.00 108 99.07 100.00 4.42e-70 . . . . 1813 1 36 no PDB 2H6Z . "Crystal Structure Of Thioredoxin Mutant E44d In Hexagonal (P61) Space Group" . . . . . 100.00 108 99.07 100.00 4.42e-70 . . . . 1813 1 37 no PDB 2H70 . "Crystal Structure Of Thioredoxin Mutant D9e In Hexagonal (P61) Space Group" . . . . . 100.00 108 99.07 100.00 3.33e-70 . . . . 1813 1 38 no PDB 2H71 . "Crystal Structure Of Thioredoxin Mutant D47e In Hexagonal (P61) Space Group" . . . . . 100.00 108 99.07 100.00 3.33e-70 . . . . 1813 1 39 no PDB 2H72 . "Crystal Structure Of Thioredoxin Mutant E85d In Hexagonal (P61) Space Group" . . . . . 100.00 108 99.07 100.00 4.42e-70 . . . . 1813 1 40 no PDB 2H73 . "Crystal Structure Of Thioredoxin Mutant D43e In Hexagonal (P61) Space Group" . . . . . 100.00 108 99.07 100.00 3.33e-70 . . . . 1813 1 41 no PDB 2H74 . "Crystal Structure Of Thioredoxin Mutant D2e In Hexagonal (P61) Space Group" . . . . . 100.00 108 99.07 100.00 3.33e-70 . . . . 1813 1 42 no PDB 2H75 . "Crystal Structure Of Thioredoxin Mutant D13e In Hexagonal (P61) Space Group" . . . . . 100.00 108 99.07 100.00 3.33e-70 . . . . 1813 1 43 no PDB 2H76 . "Crystal Structure Of Thioredoxin Mutant D10e In Hexagonal (P61) Space Group" . . . . . 100.00 108 99.07 100.00 3.33e-70 . . . . 1813 1 44 no PDB 2O8V . "Paps Reductase In A Covalent Complex With Thioredoxin C35a" . . . . . 100.00 128 99.07 99.07 3.11e-70 . . . . 1813 1 45 no PDB 2TIR . "Crystal Structure Analysis Of A Mutant Escherichia Coli Thioredoxin In Which Lysine 36 Is Replaced By Glutamic Acid" . . . . . 100.00 108 99.07 100.00 3.18e-70 . . . . 1813 1 46 no PDB 2TRX . "Crystal Structure Of Thioredoxin From Escherichia Coli At 1.68 Angstroms Resolution" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 1813 1 47 no PDB 3DXB . "Structure Of The Uhm Domain Of Puf60 Fused To Thioredoxin" . . . . . 100.00 222 100.00 100.00 1.21e-70 . . . . 1813 1 48 no PDB 3DYR . "Crystal Structure Of E. Coli Thioredoxin Mutant I76t In Its Oxidized Form" . . . . . 100.00 111 99.07 99.07 3.50e-70 . . . . 1813 1 49 no PDB 4KCA . "Crystal Structure Of Endo-1,5-alpha-l-arabinanase From A Bovine Ruminal Metagenomic Library" . . . . . 100.00 692 100.00 100.00 9.70e-66 . . . . 1813 1 50 no PDB 4KCB . "Crystal Structure Of Exo-1,5-alpha-l-arabinanase From Bovine Ruminal Metagenomic Library" . . . . . 100.00 447 100.00 100.00 4.30e-69 . . . . 1813 1 51 no DBJ BAA00903 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 52 no DBJ BAB38137 . "thioredoxin 1 [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 127 100.00 100.00 4.32e-71 . . . . 1813 1 53 no DBJ BAE77517 . "thioredoxin 1 [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 54 no DBJ BAG79587 . "thioredoxin [Escherichia coli SE11]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 55 no DBJ BAH61053 . "thioredoxin [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" . . . . . 100.00 113 97.22 98.15 7.23e-69 . . . . 1813 1 56 no EMBL CAA79851 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 57 no EMBL CAD09400 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 58 no EMBL CAP78228 . "Thioredoxin 1 [Escherichia coli LF82]" . . . . . 100.00 144 100.00 100.00 4.26e-71 . . . . 1813 1 59 no EMBL CAQ34125 . "thioredoxin 1 [Escherichia coli BL21(DE3)]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 60 no EMBL CAQ91183 . "thioredoxin 1 [Escherichia fergusonii ATCC 35469]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 61 no GB AAA24533 . "thioredoxin (trxA) [Escherichia coli]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 62 no GB AAA24534 . "thioredoxin [Escherichia coli]" . . . . . 100.00 127 100.00 100.00 4.32e-71 . . . . 1813 1 63 no GB AAA24693 . "thioredoxin [Escherichia coli]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 64 no GB AAA24694 . "thioredoxin (trxA) [Escherichia coli]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 65 no GB AAA24696 . "thioredoxin [Escherichia coli]" . . . . . 100.93 110 99.08 99.08 3.90e-69 . . . . 1813 1 66 no PIR AF0922 . "thioredoxin [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 67 no PIR B91218 . "thioredoxin 1 [imported] - Escherichia coli (strain O157:H7, substrain RIMD 0509952)" . . . . . 100.00 127 100.00 100.00 4.32e-71 . . . . 1813 1 68 no PIR C86064 . "thioredoxin 1 [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" . . . . . 100.00 127 100.00 100.00 4.32e-71 . . . . 1813 1 69 no REF NP_312741 . "thioredoxin [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 127 100.00 100.00 4.32e-71 . . . . 1813 1 70 no REF NP_418228 . "thioredoxin 1 [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 71 no REF NP_457831 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 72 no REF NP_462806 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 73 no REF NP_709584 . "thioredoxin [Shigella flexneri 2a str. 301]" . . . . . 100.00 127 100.00 100.00 4.32e-71 . . . . 1813 1 74 no SP P0AA25 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 75 no SP P0AA26 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 76 no SP P0AA27 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 77 no SP P0AA28 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 78 no SP P0AA29 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 1813 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID thioredoxin common 1813 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 . SER . 1813 1 2 . ASP . 1813 1 3 . LYS . 1813 1 4 . ILE . 1813 1 5 . ILE . 1813 1 6 . HIS . 1813 1 7 . LEU . 1813 1 8 . THR . 1813 1 9 . ASP . 1813 1 10 . ASP . 1813 1 11 . SER . 1813 1 12 . PHE . 1813 1 13 . ASP . 1813 1 14 . THR . 1813 1 15 . ASP . 1813 1 16 . VAL . 1813 1 17 . LEU . 1813 1 18 . LYS . 1813 1 19 . ALA . 1813 1 20 . ASP . 1813 1 21 . GLY . 1813 1 22 . ALA . 1813 1 23 . ILE . 1813 1 24 . LEU . 1813 1 25 . VAL . 1813 1 26 . ASP . 1813 1 27 . PHE . 1813 1 28 . TRP . 1813 1 29 . ALA . 1813 1 30 . GLU . 1813 1 31 . TRP . 1813 1 32 . CYS . 1813 1 33 . GLY . 1813 1 34 . PRO . 1813 1 35 . CYS . 1813 1 36 . LYS . 1813 1 37 . MET . 1813 1 38 . ILE . 1813 1 39 . ALA . 1813 1 40 . PRO . 1813 1 41 . ILE . 1813 1 42 . LEU . 1813 1 43 . ASP . 1813 1 44 . GLU . 1813 1 45 . ILE . 1813 1 46 . ALA . 1813 1 47 . ASP . 1813 1 48 . GLU . 1813 1 49 . TYR . 1813 1 50 . GLN . 1813 1 51 . GLY . 1813 1 52 . LYS . 1813 1 53 . LEU . 1813 1 54 . THR . 1813 1 55 . VAL . 1813 1 56 . ALA . 1813 1 57 . LYS . 1813 1 58 . LEU . 1813 1 59 . ASN . 1813 1 60 . ILE . 1813 1 61 . ASP . 1813 1 62 . GLN . 1813 1 63 . ASN . 1813 1 64 . PRO . 1813 1 65 . GLY . 1813 1 66 . THR . 1813 1 67 . ALA . 1813 1 68 . PRO . 1813 1 69 . LYS . 1813 1 70 . TYR . 1813 1 71 . GLY . 1813 1 72 . ILE . 1813 1 73 . ARG . 1813 1 74 . GLY . 1813 1 75 . ILE . 1813 1 76 . PRO . 1813 1 77 . THR . 1813 1 78 . LEU . 1813 1 79 . LEU . 1813 1 80 . LEU . 1813 1 81 . PHE . 1813 1 82 . LYS . 1813 1 83 . ASN . 1813 1 84 . GLY . 1813 1 85 . GLU . 1813 1 86 . VAL . 1813 1 87 . ALA . 1813 1 88 . ALA . 1813 1 89 . THR . 1813 1 90 . LYS . 1813 1 91 . VAL . 1813 1 92 . GLY . 1813 1 93 . ALA . 1813 1 94 . LEU . 1813 1 95 . SER . 1813 1 96 . LYS . 1813 1 97 . GLY . 1813 1 98 . GLN . 1813 1 99 . LEU . 1813 1 100 . LYS . 1813 1 101 . GLU . 1813 1 102 . PHE . 1813 1 103 . LEU . 1813 1 104 . ASP . 1813 1 105 . ALA . 1813 1 106 . ASN . 1813 1 107 . LEU . 1813 1 108 . ALA . 1813 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 . SER 1 1 1813 1 . ASP 2 2 1813 1 . LYS 3 3 1813 1 . ILE 4 4 1813 1 . ILE 5 5 1813 1 . HIS 6 6 1813 1 . LEU 7 7 1813 1 . THR 8 8 1813 1 . ASP 9 9 1813 1 . ASP 10 10 1813 1 . SER 11 11 1813 1 . PHE 12 12 1813 1 . ASP 13 13 1813 1 . THR 14 14 1813 1 . ASP 15 15 1813 1 . VAL 16 16 1813 1 . LEU 17 17 1813 1 . LYS 18 18 1813 1 . ALA 19 19 1813 1 . ASP 20 20 1813 1 . GLY 21 21 1813 1 . ALA 22 22 1813 1 . ILE 23 23 1813 1 . LEU 24 24 1813 1 . VAL 25 25 1813 1 . ASP 26 26 1813 1 . PHE 27 27 1813 1 . TRP 28 28 1813 1 . ALA 29 29 1813 1 . GLU 30 30 1813 1 . TRP 31 31 1813 1 . CYS 32 32 1813 1 . GLY 33 33 1813 1 . PRO 34 34 1813 1 . CYS 35 35 1813 1 . LYS 36 36 1813 1 . MET 37 37 1813 1 . ILE 38 38 1813 1 . ALA 39 39 1813 1 . PRO 40 40 1813 1 . ILE 41 41 1813 1 . LEU 42 42 1813 1 . ASP 43 43 1813 1 . GLU 44 44 1813 1 . ILE 45 45 1813 1 . ALA 46 46 1813 1 . ASP 47 47 1813 1 . GLU 48 48 1813 1 . TYR 49 49 1813 1 . GLN 50 50 1813 1 . GLY 51 51 1813 1 . LYS 52 52 1813 1 . LEU 53 53 1813 1 . THR 54 54 1813 1 . VAL 55 55 1813 1 . ALA 56 56 1813 1 . LYS 57 57 1813 1 . LEU 58 58 1813 1 . ASN 59 59 1813 1 . ILE 60 60 1813 1 . ASP 61 61 1813 1 . GLN 62 62 1813 1 . ASN 63 63 1813 1 . PRO 64 64 1813 1 . GLY 65 65 1813 1 . THR 66 66 1813 1 . ALA 67 67 1813 1 . PRO 68 68 1813 1 . LYS 69 69 1813 1 . TYR 70 70 1813 1 . GLY 71 71 1813 1 . ILE 72 72 1813 1 . ARG 73 73 1813 1 . GLY 74 74 1813 1 . ILE 75 75 1813 1 . PRO 76 76 1813 1 . THR 77 77 1813 1 . LEU 78 78 1813 1 . LEU 79 79 1813 1 . LEU 80 80 1813 1 . PHE 81 81 1813 1 . LYS 82 82 1813 1 . ASN 83 83 1813 1 . GLY 84 84 1813 1 . GLU 85 85 1813 1 . VAL 86 86 1813 1 . ALA 87 87 1813 1 . ALA 88 88 1813 1 . THR 89 89 1813 1 . LYS 90 90 1813 1 . VAL 91 91 1813 1 . GLY 92 92 1813 1 . ALA 93 93 1813 1 . LEU 94 94 1813 1 . SER 95 95 1813 1 . LYS 96 96 1813 1 . GLY 97 97 1813 1 . GLN 98 98 1813 1 . LEU 99 99 1813 1 . LYS 100 100 1813 1 . GLU 101 101 1813 1 . PHE 102 102 1813 1 . LEU 103 103 1813 1 . ASP 104 104 1813 1 . ALA 105 105 1813 1 . ASN 106 106 1813 1 . LEU 107 107 1813 1 . ALA 108 108 1813 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 1813 _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 $thioredoxin . 562 organism . 'Escherichia coli' 'E. coli' . . Eubacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 1813 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 1813 _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 $thioredoxin . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1813 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 1813 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 1813 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 5.7 . na 1813 1 temperature 308 . K 1813 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 1813 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 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 1813 _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 unknown unknown . 0 'spectrometer information not available' . . 1813 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 1813 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 1813 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 1813 _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 N . 'liquid NH3' . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 1813 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_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 1813 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 1813 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 3 3 LYS N N 15 119.8 . . 1 . . . . . . . . 1813 1 2 . 1 1 4 4 ILE N N 15 120.8 . . 1 . . . . . . . . 1813 1 3 . 1 1 5 5 ILE N N 15 126.4 . . 1 . . . . . . . . 1813 1 4 . 1 1 6 6 HIS N N 15 126.3 . . 1 . . . . . . . . 1813 1 5 . 1 1 7 7 LEU N N 15 124.8 . . 1 . . . . . . . . 1813 1 6 . 1 1 8 8 THR N N 15 108.4 . . 1 . . . . . . . . 1813 1 7 . 1 1 9 9 ASP N N 15 120.1 . . 1 . . . . . . . . 1813 1 8 . 1 1 10 10 ASP N N 15 116.4 . . 1 . . . . . . . . 1813 1 9 . 1 1 11 11 SER N N 15 117.4 . . 1 . . . . . . . . 1813 1 10 . 1 1 12 12 PHE N N 15 125.5 . . 1 . . . . . . . . 1813 1 11 . 1 1 13 13 ASP N N 15 117.4 . . 1 . . . . . . . . 1813 1 12 . 1 1 14 14 THR N N 15 112.5 . . 1 . . . . . . . . 1813 1 13 . 1 1 15 15 ASP N N 15 118.7 . . 1 . . . . . . . . 1813 1 14 . 1 1 16 16 VAL N N 15 113.3 . . 1 . . . . . . . . 1813 1 15 . 1 1 17 17 LEU N N 15 116.5 . . 1 . . . . . . . . 1813 1 16 . 1 1 18 18 LYS N N 15 115.3 . . 1 . . . . . . . . 1813 1 17 . 1 1 19 19 ALA N N 15 122.5 . . 1 . . . . . . . . 1813 1 18 . 1 1 20 20 ASP N N 15 121.1 . . 1 . . . . . . . . 1813 1 19 . 1 1 21 21 GLY N N 15 108.7 . . 1 . . . . . . . . 1813 1 20 . 1 1 22 22 ALA N N 15 123.6 . . 1 . . . . . . . . 1813 1 21 . 1 1 23 23 ILE N N 15 123.8 . . 1 . . . . . . . . 1813 1 22 . 1 1 24 24 LEU N N 15 130.6 . . 1 . . . . . . . . 1813 1 23 . 1 1 25 25 VAL N N 15 126.8 . . 1 . . . . . . . . 1813 1 24 . 1 1 26 26 ASP N N 15 124.6 . . 1 . . . . . . . . 1813 1 25 . 1 1 27 27 PHE N N 15 128.6 . . 1 . . . . . . . . 1813 1 26 . 1 1 28 28 TRP N N 15 120 . . 1 . . . . . . . . 1813 1 27 . 1 1 29 29 ALA N N 15 116.7 . . 1 . . . . . . . . 1813 1 28 . 1 1 30 30 GLU N N 15 121.7 . . 1 . . . . . . . . 1813 1 29 . 1 1 31 31 TRP N N 15 111.7 . . 1 . . . . . . . . 1813 1 30 . 1 1 32 32 CYS N N 15 120.8 . . 1 . . . . . . . . 1813 1 31 . 1 1 33 33 GLY N N 15 121.6 . . 1 . . . . . . . . 1813 1 32 . 1 1 35 35 CYS N N 15 111.1 . . 1 . . . . . . . . 1813 1 33 . 1 1 36 36 LYS N N 15 121.7 . . 1 . . . . . . . . 1813 1 34 . 1 1 37 37 MET N N 15 117.7 . . 1 . . . . . . . . 1813 1 35 . 1 1 38 38 ILE N N 15 109.8 . . 1 . . . . . . . . 1813 1 36 . 1 1 39 39 ALA N N 15 125.4 . . 1 . . . . . . . . 1813 1 37 . 1 1 41 41 ILE N N 15 116.7 . . 1 . . . . . . . . 1813 1 38 . 1 1 42 42 LEU N N 15 119.6 . . 1 . . . . . . . . 1813 1 39 . 1 1 43 43 ASP N N 15 118.6 . . 1 . . . . . . . . 1813 1 40 . 1 1 44 44 GLU N N 15 118.5 . . 1 . . . . . . . . 1813 1 41 . 1 1 45 45 ILE N N 15 121 . . 1 . . . . . . . . 1813 1 42 . 1 1 46 46 ALA N N 15 122.5 . . 1 . . . . . . . . 1813 1 43 . 1 1 47 47 ASP N N 15 115.2 . . 1 . . . . . . . . 1813 1 44 . 1 1 48 48 GLU N N 15 120.6 . . 1 . . . . . . . . 1813 1 45 . 1 1 49 49 TYR N N 15 115.5 . . 1 . . . . . . . . 1813 1 46 . 1 1 50 50 GLN N N 15 121.5 . . 1 . . . . . . . . 1813 1 47 . 1 1 51 51 GLY N N 15 115.5 . . 1 . . . . . . . . 1813 1 48 . 1 1 52 52 LYS N N 15 118.2 . . 1 . . . . . . . . 1813 1 49 . 1 1 53 53 LEU N N 15 119.5 . . 1 . . . . . . . . 1813 1 50 . 1 1 54 54 THR N N 15 123.5 . . 1 . . . . . . . . 1813 1 51 . 1 1 55 55 VAL N N 15 129.9 . . 1 . . . . . . . . 1813 1 52 . 1 1 56 56 ALA N N 15 129.4 . . 1 . . . . . . . . 1813 1 53 . 1 1 57 57 LYS N N 15 118.4 . . 1 . . . . . . . . 1813 1 54 . 1 1 58 58 LEU N N 15 123.5 . . 1 . . . . . . . . 1813 1 55 . 1 1 59 59 ASN N N 15 126.7 . . 1 . . . . . . . . 1813 1 56 . 1 1 60 60 ILE N N 15 122.4 . . 1 . . . . . . . . 1813 1 57 . 1 1 61 61 ASP N N 15 122.2 . . 1 . . . . . . . . 1813 1 58 . 1 1 62 62 GLN N N 15 116.1 . . 1 . . . . . . . . 1813 1 59 . 1 1 63 63 ASN N N 15 116.4 . . 1 . . . . . . . . 1813 1 60 . 1 1 65 65 GLY N N 15 112.4 . . 1 . . . . . . . . 1813 1 61 . 1 1 66 66 THR N N 15 118.8 . . 1 . . . . . . . . 1813 1 62 . 1 1 67 67 ALA N N 15 124.2 . . 1 . . . . . . . . 1813 1 63 . 1 1 69 69 LYS N N 15 117.1 . . 1 . . . . . . . . 1813 1 64 . 1 1 70 70 TYR N N 15 114.7 . . 1 . . . . . . . . 1813 1 65 . 1 1 71 71 GLY N N 15 108.1 . . 1 . . . . . . . . 1813 1 66 . 1 1 72 72 ILE N N 15 119.3 . . 1 . . . . . . . . 1813 1 67 . 1 1 73 73 ARG N N 15 128.2 . . 1 . . . . . . . . 1813 1 68 . 1 1 74 74 GLY N N 15 108.4 . . 1 . . . . . . . . 1813 1 69 . 1 1 75 75 ILE N N 15 113.3 . . 1 . . . . . . . . 1813 1 70 . 1 1 77 77 THR N N 15 118.7 . . 1 . . . . . . . . 1813 1 71 . 1 1 78 78 LEU N N 15 127 . . 1 . . . . . . . . 1813 1 72 . 1 1 79 79 LEU N N 15 122 . . 1 . . . . . . . . 1813 1 73 . 1 1 80 80 LEU N N 15 125.4 . . 1 . . . . . . . . 1813 1 74 . 1 1 81 81 PHE N N 15 128.5 . . 1 . . . . . . . . 1813 1 75 . 1 1 82 82 LYS N N 15 117.5 . . 1 . . . . . . . . 1813 1 76 . 1 1 83 83 ASN N N 15 124.2 . . 1 . . . . . . . . 1813 1 77 . 1 1 84 84 GLY N N 15 104.4 . . 1 . . . . . . . . 1813 1 78 . 1 1 85 85 GLU N N 15 118.7 . . 1 . . . . . . . . 1813 1 79 . 1 1 86 86 VAL N N 15 123.1 . . 1 . . . . . . . . 1813 1 80 . 1 1 87 87 ALA N N 15 133.4 . . 1 . . . . . . . . 1813 1 81 . 1 1 88 88 ALA N N 15 117.4 . . 1 . . . . . . . . 1813 1 82 . 1 1 89 89 THR N N 15 115.4 . . 1 . . . . . . . . 1813 1 83 . 1 1 90 90 LYS N N 15 126.2 . . 1 . . . . . . . . 1813 1 84 . 1 1 91 91 VAL N N 15 125.6 . . 1 . . . . . . . . 1813 1 85 . 1 1 92 92 GLY N N 15 113.3 . . 1 . . . . . . . . 1813 1 86 . 1 1 93 93 ALA N N 15 118.3 . . 1 . . . . . . . . 1813 1 87 . 1 1 94 94 LEU N N 15 119.4 . . 1 . . . . . . . . 1813 1 88 . 1 1 95 95 SER N N 15 120.7 . . 1 . . . . . . . . 1813 1 89 . 1 1 96 96 LYS N N 15 121.6 . . 1 . . . . . . . . 1813 1 90 . 1 1 97 97 GLY N N 15 105.6 . . 1 . . . . . . . . 1813 1 91 . 1 1 98 98 GLN N N 15 120.9 . . 1 . . . . . . . . 1813 1 92 . 1 1 99 99 LEU N N 15 123.6 . . 1 . . . . . . . . 1813 1 93 . 1 1 100 100 LYS N N 15 119.8 . . 1 . . . . . . . . 1813 1 94 . 1 1 101 101 GLU N N 15 117.9 . . 1 . . . . . . . . 1813 1 95 . 1 1 102 102 PHE N N 15 120.3 . . 1 . . . . . . . . 1813 1 96 . 1 1 103 103 LEU N N 15 121.2 . . 1 . . . . . . . . 1813 1 97 . 1 1 104 104 ASP N N 15 120.2 . . 1 . . . . . . . . 1813 1 98 . 1 1 105 105 ALA N N 15 118.5 . . 1 . . . . . . . . 1813 1 99 . 1 1 106 106 ASN N N 15 113.2 . . 1 . . . . . . . . 1813 1 100 . 1 1 107 107 LEU N N 15 121 . . 1 . . . . . . . . 1813 1 101 . 1 1 108 108 ALA N N 15 128.9 . . 1 . . . . . . . . 1813 1 stop_ save_