data_17944 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17944 _Entry.Title ; 13C, 15N Chemical shifts of the C-terminal fragment of E. coli thioredoxin reassembly using solid-state NMR spectroscopy ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2011-09-15 _Entry.Accession_date 2011-09-15 _Entry.Last_release_date 2011-10-28 _Entry.Original_release_date 2011-10-28 _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 . _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 Dabeiba Marulanda . . . 17944 2 Maria Tasayco . . . 17944 3 Ann McDermott . . . 17944 4 Marcela Cataldi . . . 17944 5 Vilma Arriaran . . . 17944 6 Tatyana Polenova . . . 17944 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 17944 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 152 17944 '15N chemical shifts' 34 17944 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2011-10-28 2011-09-15 original author . 17944 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 17944 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 15600367 _Citation.Full_citation . _Citation.Title 'Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Am. Chem. Soc.' _Citation.Journal_name_full . _Citation.Journal_volume 126 _Citation.Journal_issue 50 _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 16608 _Citation.Page_last 16620 _Citation.Year 2004 _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 Dabeiba Marulanda . . . 17944 1 2 Maria Tasayco . L. . 17944 1 3 Ann McDermott . . . 17944 1 4 M. Cataldi . . . 17944 1 5 V. Arriaran . . . 17944 1 6 Tatyana Polenova . . . 17944 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17944 _Assembly.ID 1 _Assembly.Name 'C-terminal Trx reassembly' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _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 'C-terminal fragment' 1 $C-terminal_of_Trx_reassembly A . yes native no no . . . 17944 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_C-terminal_of_Trx_reassembly _Entity.Sf_category entity _Entity.Sf_framecode C-terminal_of_Trx_reassembly _Entity.Entry_ID 17944 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name C-terminal_of_Trx_reassembly _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 ; GIPTLLLFKNGEVAATKVGA LSKGQLKEFLDANLA ; _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 35 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not available' _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 17700 . TRX_intact . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 2 no BMRB 1812 . thioredoxin . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 3 no BMRB 1813 . thioredoxin . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 4 no PDB 1F6M . "Crystal Structure Of A Complex Between Thioredoxin Reductase, Thioredoxin, And The Nadp+ Analog, Aadp+" . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 5 no PDB 1KEB . "Crystal Structure Of Double Mutant M37l,P40s E.Coli Thioredoxin" . . . . . 100.00 108 100.00 100.00 2.06e-13 . . . . 17944 1 6 no PDB 1M7T . "Solution Structure And Dynamics Of The Human-Escherichia Coli Thioredoxin Chimera: Insights Into Thermodynamic Stability" . . . . . 97.14 107 100.00 100.00 4.70e-13 . . . . 17944 1 7 no PDB 1OAZ . "Ige Fv Spe7 Complexed With A Recombinant Thioredoxin" . . . . . 100.00 123 100.00 100.00 2.10e-13 . . . . 17944 1 8 no PDB 1SKR . "T7 Dna Polymerase Complexed To Dna Primer/template And Ddatp" . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 9 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 2.04e-13 . . . . 17944 1 10 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 2.04e-13 . . . . 17944 1 11 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 2.04e-13 . . . . 17944 1 12 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 2.04e-13 . . . . 17944 1 13 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 2.04e-13 . . . . 17944 1 14 no PDB 1SRX . "Three-Dimensional Structure Of Escherichia Coli Thioredoxin-S2 To 2.8 Angstroms Resolution" . . . . . 100.00 108 100.00 100.00 1.81e-13 . . . . 17944 1 15 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 2.04e-13 . . . . 17944 1 16 no PDB 1T8E . "T7 Dna Polymerase Ternary Complex With Dctp At The Insertion Site." . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 17 no PDB 1THO . "Crystal Structure Of A Mutant Escherichia Coli Thioredoxin With An Arginine Insertion In The Active Site" . . . . . 100.00 109 100.00 100.00 2.10e-13 . . . . 17944 1 18 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 2.04e-13 . . . . 17944 1 19 no PDB 1TK5 . "T7 Dna Polymerase Binary Complex With 8 Oxo Guanosine In The Templating Strand" . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 20 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 2.04e-13 . . . . 17944 1 21 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 2.04e-13 . . . . 17944 1 22 no PDB 1TXX . "Active-Site Variant Of E.Coli Thioredoxin" . . . . . 100.00 108 100.00 100.00 1.60e-13 . . . . 17944 1 23 no PDB 1X9M . "T7 Dna Polymerase In Complex With An N-2- Acetylaminofluorene-adducted Dna" . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 24 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 2.04e-13 . . . . 17944 1 25 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 2.04e-13 . . . . 17944 1 26 no PDB 1XOA . "Thioredoxin (Oxidized Disulfide Form), Nmr, 20 Structures" . . . . . 100.00 108 100.00 100.00 2.31e-13 . . . . 17944 1 27 no PDB 1XOB . "Thioredoxin (Reduced Dithio Form), Nmr, 20 Structures" . . . . . 100.00 108 100.00 100.00 2.31e-13 . . . . 17944 1 28 no PDB 1ZCP . "Crystal Structure Of A Catalytic Site Mutant E. Coli Trxa (Caca)" . . . . . 100.00 108 100.00 100.00 1.67e-13 . . . . 17944 1 29 no PDB 1ZYQ . "T7 Dna Polymerase In Complex With 8og And Incoming Ddatp" . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 30 no PDB 1ZZY . "Crystal Structure Of Thioredoxin Mutant L7v" . . . . . 100.00 108 100.00 100.00 1.99e-13 . . . . 17944 1 31 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 2.04e-13 . . . . 17944 1 32 no PDB 2BTO . "Structure Of Btuba From Prosthecobacter Dejongeii" . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 33 no PDB 2EIO . "Design Of Disulfide-Linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" . . . . . 100.00 108 97.14 97.14 3.16e-12 . . . . 17944 1 34 no PDB 2EIQ . "Design Of Disulfide-linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" . . . . . 100.00 108 97.14 97.14 9.93e-13 . . . . 17944 1 35 no PDB 2FCH . "Crystal Structure Of Thioredoxin Mutant G74s" . . . . . 97.14 108 100.00 100.00 1.15e-12 . . . . 17944 1 36 no PDB 2FD3 . "Crystal Structure Of Thioredoxin Mutant P34h" . . . . . 100.00 108 100.00 100.00 1.83e-13 . . . . 17944 1 37 no PDB 2H6X . "Crystal Structure Of Thioredoxin Wild Type In Hexagonal (P61) Space Group" . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 38 no PDB 2H6Y . "Crystal Structure Of Thioredoxin Mutant E48d In Hexagonal (P61) Space Group" . . . . . 100.00 108 100.00 100.00 1.97e-13 . . . . 17944 1 39 no PDB 2H6Z . "Crystal Structure Of Thioredoxin Mutant E44d In Hexagonal (P61) Space Group" . . . . . 100.00 108 100.00 100.00 1.97e-13 . . . . 17944 1 40 no PDB 2H70 . "Crystal Structure Of Thioredoxin Mutant D9e In Hexagonal (P61) Space Group" . . . . . 100.00 108 100.00 100.00 2.13e-13 . . . . 17944 1 41 no PDB 2H71 . "Crystal Structure Of Thioredoxin Mutant D47e In Hexagonal (P61) Space Group" . . . . . 100.00 108 100.00 100.00 2.13e-13 . . . . 17944 1 42 no PDB 2H72 . "Crystal Structure Of Thioredoxin Mutant E85d In Hexagonal (P61) Space Group" . . . . . 100.00 108 97.14 100.00 5.74e-13 . . . . 17944 1 43 no PDB 2H73 . "Crystal Structure Of Thioredoxin Mutant D43e In Hexagonal (P61) Space Group" . . . . . 100.00 108 100.00 100.00 2.13e-13 . . . . 17944 1 44 no PDB 2H74 . "Crystal Structure Of Thioredoxin Mutant D2e In Hexagonal (P61) Space Group" . . . . . 100.00 108 100.00 100.00 2.13e-13 . . . . 17944 1 45 no PDB 2H75 . "Crystal Structure Of Thioredoxin Mutant D13e In Hexagonal (P61) Space Group" . . . . . 100.00 108 100.00 100.00 2.13e-13 . . . . 17944 1 46 no PDB 2H76 . "Crystal Structure Of Thioredoxin Mutant D10e In Hexagonal (P61) Space Group" . . . . . 100.00 108 100.00 100.00 2.13e-13 . . . . 17944 1 47 no PDB 2O8V . "Paps Reductase In A Covalent Complex With Thioredoxin C35a" . . . . . 100.00 128 100.00 100.00 1.45e-13 . . . . 17944 1 48 no PDB 2TIR . "Crystal Structure Analysis Of A Mutant Escherichia Coli Thioredoxin In Which Lysine 36 Is Replaced By Glutamic Acid" . . . . . 100.00 108 100.00 100.00 2.08e-13 . . . . 17944 1 49 no PDB 2TRX . "Crystal Structure Of Thioredoxin From Escherichia Coli At 1.68 Angstroms Resolution" . . . . . 100.00 108 100.00 100.00 2.04e-13 . . . . 17944 1 50 no PDB 3DXB . "Structure Of The Uhm Domain Of Puf60 Fused To Thioredoxin" . . . . . 100.00 222 100.00 100.00 1.05e-13 . . . . 17944 1 51 no PDB 3DYR . "Crystal Structure Of E. Coli Thioredoxin Mutant I76t In Its Oxidized Form" . . . . . 100.00 111 97.14 97.14 1.32e-12 . . . . 17944 1 52 no PDB 4HU7 . "E. Coli Thioredoxin Variant With Pro76 As Single Proline Residue" . . . . . 100.00 108 100.00 100.00 1.08e-13 . . . . 17944 1 53 no PDB 4HU9 . "E. Coli Thioredoxin Variant With (4s)-fluoropro76 As Single Proline Residue" . . . . . 100.00 108 97.14 97.14 2.19e-12 . . . . 17944 1 54 no PDB 4HUA . "E. Coli Thioredoxin Variant With (4r)-fluoropro76 As Single Proline Residue" . . . . . 100.00 108 97.14 97.14 2.19e-12 . . . . 17944 1 55 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 6.43e-13 . . . . 17944 1 56 no PDB 4KCB . "Crystal Structure Of Exo-1,5-alpha-l-arabinanase From Bovine Ruminal Metagenomic Library" . . . . . 100.00 447 100.00 100.00 2.58e-13 . . . . 17944 1 57 no PDB 4X43 . "Structure Of Proline-free E. Coli Thioredoxin" . . . . . 100.00 108 97.14 97.14 1.72e-12 . . . . 17944 1 58 no DBJ BAA00903 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 59 no DBJ BAB38137 . "thioredoxin 1 [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 127 100.00 100.00 2.07e-13 . . . . 17944 1 60 no DBJ BAE77517 . "thioredoxin 1 [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 61 no DBJ BAG79587 . "thioredoxin [Escherichia coli SE11]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 62 no DBJ BAH61053 . "thioredoxin [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" . . . . . 100.00 113 100.00 100.00 2.29e-13 . . . . 17944 1 63 no EMBL CAA79851 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 64 no EMBL CAD09400 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 65 no EMBL CAG77109 . "thioredoxin [Pectobacterium atrosepticum SCRI1043]" . . . . . 97.14 108 97.06 97.06 1.13e-11 . . . . 17944 1 66 no EMBL CAO95241 . "Thioredoxin 1 [Erwinia tasmaniensis Et1/99]" . . . . . 97.14 109 97.06 100.00 5.39e-12 . . . . 17944 1 67 no EMBL CAP78228 . "Thioredoxin 1 [Escherichia coli LF82]" . . . . . 100.00 144 100.00 100.00 2.14e-13 . . . . 17944 1 68 no GB AAA24533 . "thioredoxin (trxA) [Escherichia coli]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 69 no GB AAA24534 . "thioredoxin [Escherichia coli]" . . . . . 100.00 127 100.00 100.00 2.07e-13 . . . . 17944 1 70 no GB AAA24693 . "thioredoxin [Escherichia coli]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 71 no GB AAA24694 . "thioredoxin (trxA) [Escherichia coli]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 72 no GB AAA24696 . "thioredoxin [Escherichia coli]" . . . . . 102.86 110 97.22 97.22 1.05e-11 . . . . 17944 1 73 no PIR AF0922 . "thioredoxin [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 74 no PIR B91218 . "thioredoxin 1 [imported] - Escherichia coli (strain O157:H7, substrain RIMD 0509952)" . . . . . 100.00 127 100.00 100.00 2.07e-13 . . . . 17944 1 75 no PIR C86064 . "thioredoxin 1 [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" . . . . . 100.00 127 100.00 100.00 2.07e-13 . . . . 17944 1 76 no REF NP_312741 . "thioredoxin [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 127 100.00 100.00 2.07e-13 . . . . 17944 1 77 no REF NP_418228 . "thioredoxin 1 [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 78 no REF NP_457831 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 79 no REF NP_462806 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 80 no REF NP_709584 . "thioredoxin [Shigella flexneri 2a str. 301]" . . . . . 100.00 127 100.00 100.00 2.07e-13 . . . . 17944 1 81 no SP P0AA25 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 82 no SP P0AA26 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 83 no SP P0AA27 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 84 no SP P0AA28 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 1 85 no SP P0AA29 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 1.99e-13 . . . . 17944 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 74 GLY . 17944 1 2 75 ILE . 17944 1 3 76 PRO . 17944 1 4 77 THR . 17944 1 5 78 LEU . 17944 1 6 79 LEU . 17944 1 7 80 LEU . 17944 1 8 81 PHE . 17944 1 9 82 LYS . 17944 1 10 83 ASN . 17944 1 11 84 GLY . 17944 1 12 85 GLU . 17944 1 13 86 VAL . 17944 1 14 87 ALA . 17944 1 15 88 ALA . 17944 1 16 89 THR . 17944 1 17 90 LYS . 17944 1 18 91 VAL . 17944 1 19 92 GLY . 17944 1 20 93 ALA . 17944 1 21 94 LEU . 17944 1 22 95 SER . 17944 1 23 96 LYS . 17944 1 24 97 GLY . 17944 1 25 98 GLN . 17944 1 26 99 LEU . 17944 1 27 100 LYS . 17944 1 28 101 GLU . 17944 1 29 102 PHE . 17944 1 30 103 LEU . 17944 1 31 104 ASP . 17944 1 32 105 ALA . 17944 1 33 106 ASN . 17944 1 34 107 LEU . 17944 1 35 108 ALA . 17944 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 . GLY 1 1 17944 1 . ILE 2 2 17944 1 . PRO 3 3 17944 1 . THR 4 4 17944 1 . LEU 5 5 17944 1 . LEU 6 6 17944 1 . LEU 7 7 17944 1 . PHE 8 8 17944 1 . LYS 9 9 17944 1 . ASN 10 10 17944 1 . GLY 11 11 17944 1 . GLU 12 12 17944 1 . VAL 13 13 17944 1 . ALA 14 14 17944 1 . ALA 15 15 17944 1 . THR 16 16 17944 1 . LYS 17 17 17944 1 . VAL 18 18 17944 1 . GLY 19 19 17944 1 . ALA 20 20 17944 1 . LEU 21 21 17944 1 . SER 22 22 17944 1 . LYS 23 23 17944 1 . GLY 24 24 17944 1 . GLN 25 25 17944 1 . LEU 26 26 17944 1 . LYS 27 27 17944 1 . GLU 28 28 17944 1 . PHE 29 29 17944 1 . LEU 30 30 17944 1 . ASP 31 31 17944 1 . ALA 32 32 17944 1 . ASN 33 33 17944 1 . LEU 34 34 17944 1 . ALA 35 35 17944 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 17944 _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 $C-terminal_of_Trx_reassembly . 562 organism . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli . . . . . . . . . . . . . . . . Trx . . . . 17944 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 17944 _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 $C-terminal_of_Trx_reassembly . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pTK100 . . . . . . 17944 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 17944 _Sample.ID 1 _Sample.Type solid _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system H2O _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 'C-terminal of Trx reassembly' '[U-100% 13C; U-100% 15N]' . . 1 $C-terminal_of_Trx_reassembly . . 'PEG precipitate' . . mg . . . . 17944 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 17944 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 10 . mM 17944 1 pH 3.5 . pH 17944 1 pressure 1 . atm 17944 1 temperature 273 . K 17944 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 17944 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 17944 1 Goddard . . 17944 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 17944 1 processing 17944 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 17944 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 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 17944 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 750 . . . 17944 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 17944 _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 '2D 13C-13C DARR' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17944 1 2 '2D 15N-13C NCA' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17944 1 3 '2D 15N-13C NCO' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17944 1 4 '2D 15N-13C NCACX' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17944 1 5 '2D 15N-13C NCOCX' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17944 1 stop_ save_ save_NMR_spectrometer_expt _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spectrometer_expt _NMR_spec_expt.Entry_ID 17944 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name . _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $spectrometer_1 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $NMRPipe _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . 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 17944 _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 . . . . . . . . . 17944 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 17944 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 17944 _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 0.2 _Assigned_chem_shift_list.Chem_shift_15N_err 0.2 _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 13C-13C DARR' . . . 17944 1 2 '2D 15N-13C NCA' . . . 17944 1 3 '2D 15N-13C NCO' . . . 17944 1 4 '2D 15N-13C NCACX' . . . 17944 1 5 '2D 15N-13C NCOCX' . . . 17944 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 GLY C C 13 169.8 0.2 . 1 . . . . 74 GLY C . 17944 1 2 . 1 1 1 1 GLY CA C 13 43.30 0.2 . 1 . . . . 74 GLY CA . 17944 1 3 . 1 1 1 1 GLY N N 15 104.7 0.2 . 1 . . . . 74 GLY N . 17944 1 4 . 1 1 2 2 ILE C C 13 173.7 0.2 . 1 . . . . 75 ILE C . 17944 1 5 . 1 1 2 2 ILE CA C 13 59.40 0.2 . 1 . . . . 75 ILE CA . 17944 1 6 . 1 1 2 2 ILE CB C 13 38.60 0.2 . 1 . . . . 75 ILE CB . 17944 1 7 . 1 1 2 2 ILE CG1 C 13 24.50 0.2 . 1 . . . . 75 ILE CG1 . 17944 1 8 . 1 1 2 2 ILE CG2 C 13 20.40 0.2 . 1 . . . . 75 ILE CG2 . 17944 1 9 . 1 1 2 2 ILE CD1 C 13 16.60 0.2 . 1 . . . . 75 ILE CD1 . 17944 1 10 . 1 1 2 2 ILE N N 15 114.4 0.2 . 1 . . . . 75 ILE N . 17944 1 11 . 1 1 3 3 PRO C C 13 177.9 0.2 . 1 . . . . 76 PRO C . 17944 1 12 . 1 1 3 3 PRO CA C 13 62.80 0.2 . 1 . . . . 76 PRO CA . 17944 1 13 . 1 1 3 3 PRO CB C 13 34.80 0.2 . 1 . . . . 76 PRO CB . 17944 1 14 . 1 1 3 3 PRO CG C 13 24.70 0.2 . 1 . . . . 76 PRO CG . 17944 1 15 . 1 1 3 3 PRO CD C 13 51.60 0.2 . 1 . . . . 76 PRO CD . 17944 1 16 . 1 1 3 3 PRO N N 15 136.4 0.2 . 1 . . . . 76 PRO N . 17944 1 17 . 1 1 4 4 THR C C 13 171.3 0.2 . 1 . . . . 77 THR C . 17944 1 18 . 1 1 4 4 THR CA C 13 64.00 0.2 . 1 . . . . 77 THR CA . 17944 1 19 . 1 1 4 4 THR CB C 13 75.40 0.2 . 1 . . . . 77 THR CB . 17944 1 20 . 1 1 4 4 THR CG2 C 13 20.90 0.2 . 1 . . . . 77 THR CG2 . 17944 1 21 . 1 1 4 4 THR N N 15 120.2 0.2 . 1 . . . . 77 THR N . 17944 1 22 . 1 1 5 5 LEU C C 13 175.3 0.2 . 1 . . . . 78 LEU C . 17944 1 23 . 1 1 5 5 LEU CA C 13 52.60 0.2 . 1 . . . . 78 LEU CA . 17944 1 24 . 1 1 5 5 LEU CB C 13 44.10 0.2 . 1 . . . . 78 LEU CB . 17944 1 25 . 1 1 5 5 LEU CG C 13 26.90 0.2 . 1 . . . . 78 LEU CG . 17944 1 26 . 1 1 5 5 LEU N N 15 126.1 0.2 . 1 . . . . 78 LEU N . 17944 1 27 . 1 1 6 6 LEU C C 13 175.6 0.2 . 1 . . . . 79 LEU C . 17944 1 28 . 1 1 6 6 LEU CA C 13 52.90 0.2 . 1 . . . . 79 LEU CA . 17944 1 29 . 1 1 6 6 LEU CB C 13 45.50 0.2 . 1 . . . . 79 LEU CB . 17944 1 30 . 1 1 6 6 LEU CG C 13 27.10 0.2 . 1 . . . . 79 LEU CG . 17944 1 31 . 1 1 6 6 LEU N N 15 125.7 0.2 . 1 . . . . 79 LEU N . 17944 1 32 . 1 1 7 7 LEU C C 13 174.4 0.2 . 1 . . . . 80 LEU C . 17944 1 33 . 1 1 7 7 LEU CA C 13 52.00 0.2 . 1 . . . . 80 LEU CA . 17944 1 34 . 1 1 7 7 LEU CB C 13 44.50 0.2 . 1 . . . . 80 LEU CB . 17944 1 35 . 1 1 7 7 LEU CG C 13 27.20 0.2 . 1 . . . . 80 LEU CG . 17944 1 36 . 1 1 7 7 LEU CD1 C 13 26.80 0.2 . . . . . . 80 LEU CD1 . 17944 1 37 . 1 1 7 7 LEU CD2 C 13 23.60 0.2 . . . . . . 80 LEU CD2 . 17944 1 38 . 1 1 7 7 LEU N N 15 120.0 0.2 . 1 . . . . 80 LEU N . 17944 1 39 . 1 1 8 8 PHE C C 13 176.9 0.2 . 1 . . . . 81 PHE C . 17944 1 40 . 1 1 8 8 PHE CA C 13 56.80 0.2 . 1 . . . . 81 PHE CA . 17944 1 41 . 1 1 8 8 PHE CB C 13 41.70 0.2 . 1 . . . . 81 PHE CB . 17944 1 42 . 1 1 8 8 PHE CG C 13 140.8 0.2 . 1 . . . . 81 PHE CG . 17944 1 43 . 1 1 8 8 PHE CD1 C 13 136.4 0.2 . . . . . . 81 PHE CD1 . 17944 1 44 . 1 1 8 8 PHE CD2 C 13 131.8 0.2 . . . . . . 81 PHE CD2 . 17944 1 45 . 1 1 8 8 PHE CE1 C 13 133.7 0.2 . . . . . . 81 PHE CE1 . 17944 1 46 . 1 1 8 8 PHE CE2 C 13 133.7 0.2 . . . . . . 81 PHE CE2 . 17944 1 47 . 1 1 8 8 PHE N N 15 128.1 0.2 . 1 . . . . 81 PHE N . 17944 1 48 . 1 1 9 9 LYS C C 13 178.7 0.2 . 1 . . . . 82 LYS C . 17944 1 49 . 1 1 9 9 LYS CA C 13 55.80 0.2 . 1 . . . . 82 LYS CA . 17944 1 50 . 1 1 9 9 LYS CB C 13 35.40 0.2 . 1 . . . . 82 LYS CB . 17944 1 51 . 1 1 9 9 LYS CG C 13 25.20 0.2 . 1 . . . . 82 LYS CG . 17944 1 52 . 1 1 9 9 LYS CD C 13 30.10 0.2 . 1 . . . . 82 LYS CD . 17944 1 53 . 1 1 9 9 LYS CE C 13 41.90 0.2 . 1 . . . . 82 LYS CE . 17944 1 54 . 1 1 9 9 LYS N N 15 116.7 0.2 . 1 . . . . 82 LYS N . 17944 1 55 . 1 1 10 10 ASN C C 13 176.1 0.2 . 1 . . . . 83 ASN C . 17944 1 56 . 1 1 10 10 ASN CA C 13 54.30 0.2 . 1 . . . . 83 ASN CA . 17944 1 57 . 1 1 10 10 ASN CB C 13 37.50 0.2 . 1 . . . . 83 ASN CB . 17944 1 58 . 1 1 10 10 ASN N N 15 123.9 0.2 . 1 . . . . 83 ASN N . 17944 1 59 . 1 1 11 11 GLY C C 13 173.9 0.2 . 1 . . . . 84 GLY C . 17944 1 60 . 1 1 11 11 GLY CA C 13 46.30 0.2 . 1 . . . . 84 GLY CA . 17944 1 61 . 1 1 11 11 GLY N N 15 104.2 0.2 . 1 . . . . 84 GLY N . 17944 1 62 . 1 1 12 12 GLU C C 13 177.2 0.2 . 1 . . . . 85 GLU C . 17944 1 63 . 1 1 12 12 GLU CA C 13 55.30 0.2 . 1 . . . . 85 GLU CA . 17944 1 64 . 1 1 12 12 GLU CB C 13 35.50 0.2 . 1 . . . . 85 GLU CB . 17944 1 65 . 1 1 12 12 GLU CG C 13 38.10 0.2 . 1 . . . . 85 GLU CG . 17944 1 66 . 1 1 12 12 GLU CD C 13 183.9 0.2 . 1 . . . . 85 GLU CD . 17944 1 67 . 1 1 12 12 GLU N N 15 117.3 0.2 . 1 . . . . 85 GLU N . 17944 1 68 . 1 1 13 13 VAL C C 13 175.5 0.2 . 1 . . . . 86 VAL C . 17944 1 69 . 1 1 13 13 VAL CA C 13 64.40 0.2 . 1 . . . . 86 VAL CA . 17944 1 70 . 1 1 13 13 VAL CB C 13 29.10 0.2 . 1 . . . . 86 VAL CB . 17944 1 71 . 1 1 13 13 VAL CG1 C 13 22.20 0.2 . . . . . . 86 VAL CG1 . 17944 1 72 . 1 1 13 13 VAL CG2 C 13 22.20 0.2 . . . . . . 86 VAL CG2 . 17944 1 73 . 1 1 13 13 VAL N N 15 124.3 0.2 . 1 . . . . 86 VAL N . 17944 1 74 . 1 1 14 14 ALA C C 13 176.6 0.2 . 1 . . . . 87 ALA C . 17944 1 75 . 1 1 14 14 ALA CA C 13 51.90 0.2 . 1 . . . . 87 ALA CA . 17944 1 76 . 1 1 14 14 ALA CB C 13 20.80 0.2 . 1 . . . . 87 ALA CB . 17944 1 77 . 1 1 14 14 ALA N N 15 135.8 0.2 . 1 . . . . 87 ALA N . 17944 1 78 . 1 1 15 15 ALA C C 13 175.1 0.2 . 1 . . . . 88 ALA C . 17944 1 79 . 1 1 15 15 ALA CA C 13 52.70 0.2 . 1 . . . . 88 ALA CA . 17944 1 80 . 1 1 15 15 ALA CB C 13 22.50 0.2 . 1 . . . . 88 ALA CB . 17944 1 81 . 1 1 15 15 ALA N N 15 114.5 0.2 . 1 . . . . 88 ALA N . 17944 1 82 . 1 1 16 16 THR C C 13 173.6 0.2 . 1 . . . . 89 THR C . 17944 1 83 . 1 1 16 16 THR CA C 13 62.40 0.2 . 1 . . . . 89 THR CA . 17944 1 84 . 1 1 16 16 THR CB C 13 71.40 0.2 . 1 . . . . 89 THR CB . 17944 1 85 . 1 1 16 16 THR CG2 C 13 21.40 0.2 . 1 . . . . 89 THR CG2 . 17944 1 86 . 1 1 16 16 THR N N 15 117.3 0.2 . 1 . . . . 89 THR N . 17944 1 87 . 1 1 17 17 LYS C C 13 173.8 0.2 . 1 . . . . 90 LYS C . 17944 1 88 . 1 1 17 17 LYS CA C 13 53.80 0.2 . 1 . . . . 90 LYS CA . 17944 1 89 . 1 1 17 17 LYS CB C 13 33.00 0.2 . 1 . . . . 90 LYS CB . 17944 1 90 . 1 1 17 17 LYS CG C 13 26.20 0.2 . 1 . . . . 90 LYS CG . 17944 1 91 . 1 1 17 17 LYS CD C 13 27.00 0.2 . 1 . . . . 90 LYS CD . 17944 1 92 . 1 1 17 17 LYS CE C 13 41.90 0.2 . 1 . . . . 90 LYS CE . 17944 1 93 . 1 1 17 17 LYS N N 15 127.5 0.2 . 1 . . . . 90 LYS N . 17944 1 94 . 1 1 18 18 VAL C C 13 177.3 0.2 . 1 . . . . 91 VAL C . 17944 1 95 . 1 1 18 18 VAL CA C 13 62.20 0.2 . 1 . . . . 91 VAL CA . 17944 1 96 . 1 1 18 18 VAL CB C 13 33.50 0.2 . 1 . . . . 91 VAL CB . 17944 1 97 . 1 1 18 18 VAL CG1 C 13 21.20 0.2 . . . . . . 91 VAL CG1 . 17944 1 98 . 1 1 18 18 VAL CG2 C 13 21.20 0.2 . . . . . . 91 VAL CG2 . 17944 1 99 . 1 1 18 18 VAL N N 15 132.1 0.2 . 1 . . . . 91 VAL N . 17944 1 100 . 1 1 19 19 GLY C C 13 171.7 0.2 . 1 . . . . 92 GLY C . 17944 1 101 . 1 1 19 19 GLY CA C 13 44.00 0.2 . 1 . . . . 92 GLY CA . 17944 1 102 . 1 1 19 19 GLY N N 15 114.9 0.2 . 1 . . . . 92 GLY N . 17944 1 103 . 1 1 20 20 ALA C C 13 175.1 0.2 . 1 . . . . 93 ALA C . 17944 1 104 . 1 1 20 20 ALA CA C 13 52.80 0.2 . 1 . . . . 93 ALA CA . 17944 1 105 . 1 1 20 20 ALA CB C 13 19.30 0.2 . 1 . . . . 93 ALA CB . 17944 1 106 . 1 1 20 20 ALA N N 15 125.8 0.2 . 1 . . . . 93 ALA N . 17944 1 107 . 1 1 21 21 LEU CA C 13 54.70 0.2 . 1 . . . . 94 LEU CA . 17944 1 108 . 1 1 21 21 LEU CB C 13 43.60 0.2 . 1 . . . . 94 LEU CB . 17944 1 109 . 1 1 21 21 LEU CG C 13 26.70 0.2 . 1 . . . . 94 LEU CG . 17944 1 110 . 1 1 21 21 LEU CD1 C 13 26.90 0.2 . . . . . . 94 LEU CD1 . 17944 1 111 . 1 1 21 21 LEU CD2 C 13 24.00 0.2 . . . . . . 94 LEU CD2 . 17944 1 112 . 1 1 21 21 LEU N N 15 124.0 0.2 . 1 . . . . 94 LEU N . 17944 1 113 . 1 1 22 22 SER C C 13 175.4 0.2 . 1 . . . . 95 SER C . 17944 1 114 . 1 1 22 22 SER CA C 13 56.10 0.2 . 1 . . . . 95 SER CA . 17944 1 115 . 1 1 22 22 SER CB C 13 66.40 0.2 . 1 . . . . 95 SER CB . 17944 1 116 . 1 1 22 22 SER N N 15 114.5 0.2 . 1 . . . . 95 SER N . 17944 1 117 . 1 1 23 23 LYS C C 13 178.8 0.2 . 1 . . . . 96 LYS C . 17944 1 118 . 1 1 23 23 LYS CA C 13 61.00 0.2 . 1 . . . . 96 LYS CA . 17944 1 119 . 1 1 23 23 LYS CB C 13 33.60 0.2 . 1 . . . . 96 LYS CB . 17944 1 120 . 1 1 23 23 LYS CG C 13 24.50 0.2 . 1 . . . . 96 LYS CG . 17944 1 121 . 1 1 23 23 LYS CD C 13 29.00 0.2 . 1 . . . . 96 LYS CD . 17944 1 122 . 1 1 23 23 LYS CE C 13 42.70 0.2 . 1 . . . . 96 LYS CE . 17944 1 123 . 1 1 23 23 LYS N N 15 120.9 0.2 . 1 . . . . 96 LYS N . 17944 1 124 . 1 1 24 24 GLY C C 13 177.0 0.2 . 1 . . . . 97 GLY C . 17944 1 125 . 1 1 24 24 GLY CA C 13 46.90 0.2 . 1 . . . . 97 GLY CA . 17944 1 126 . 1 1 24 24 GLY N N 15 106.1 0.2 . 1 . . . . 97 GLY N . 17944 1 127 . 1 1 25 25 GLN C C 13 179.8 0.2 . 1 . . . . 98 GLN C . 17944 1 128 . 1 1 25 25 GLN CA C 13 58.20 0.2 . 1 . . . . 98 GLN CA . 17944 1 129 . 1 1 25 25 GLN CB C 13 29.50 0.2 . 1 . . . . 98 GLN CB . 17944 1 130 . 1 1 25 25 GLN CG C 13 34.60 0.2 . 1 . . . . 98 GLN CG . 17944 1 131 . 1 1 25 25 GLN N N 15 121.8 0.2 . 1 . . . . 98 GLN N . 17944 1 132 . 1 1 26 26 LEU C C 13 177.9 0.2 . 1 . . . . 99 LEU C . 17944 1 133 . 1 1 26 26 LEU CA C 13 57.90 0.2 . 1 . . . . 99 LEU CA . 17944 1 134 . 1 1 26 26 LEU CB C 13 40.80 0.2 . 1 . . . . 99 LEU CB . 17944 1 135 . 1 1 26 26 LEU CG C 13 27.50 0.2 . 1 . . . . 99 LEU CG . 17944 1 136 . 1 1 26 26 LEU CD2 C 13 22.70 0.2 . . . . . . 99 LEU CD2 . 17944 1 137 . 1 1 26 26 LEU N N 15 124.0 0.2 . 1 . . . . 99 LEU N . 17944 1 138 . 1 1 27 27 LYS C C 13 178.5 0.2 . 1 . . . . 100 LYS C . 17944 1 139 . 1 1 27 27 LYS CA C 13 60.60 0.2 . 1 . . . . 100 LYS CA . 17944 1 140 . 1 1 27 27 LYS CB C 13 30.80 0.2 . 1 . . . . 100 LYS CB . 17944 1 141 . 1 1 27 27 LYS CG C 13 25.40 0.2 . 1 . . . . 100 LYS CG . 17944 1 142 . 1 1 27 27 LYS CD C 13 27.30 0.2 . 1 . . . . 100 LYS CD . 17944 1 143 . 1 1 27 27 LYS CE C 13 42.60 0.2 . 1 . . . . 100 LYS CE . 17944 1 144 . 1 1 27 27 LYS N N 15 118.9 0.2 . 1 . . . . 100 LYS N . 17944 1 145 . 1 1 28 28 GLU C C 13 179.5 0.2 . 1 . . . . 101 GLU C . 17944 1 146 . 1 1 28 28 GLU CA C 13 59.90 0.2 . 1 . . . . 101 GLU CA . 17944 1 147 . 1 1 28 28 GLU CB C 13 28.50 0.2 . 1 . . . . 101 GLU CB . 17944 1 148 . 1 1 28 28 GLU CG C 13 34.50 0.2 . 1 . . . . 101 GLU CG . 17944 1 149 . 1 1 28 28 GLU CD C 13 181.8 0.2 . 1 . . . . 101 GLU CD . 17944 1 150 . 1 1 28 28 GLU N N 15 118.7 0.2 . 1 . . . . 101 GLU N . 17944 1 151 . 1 1 29 29 PHE C C 13 177.4 0.2 . 1 . . . . 102 PHE C . 17944 1 152 . 1 1 29 29 PHE CA C 13 60.40 0.2 . 1 . . . . 102 PHE CA . 17944 1 153 . 1 1 29 29 PHE CB C 13 39.60 0.2 . 1 . . . . 102 PHE CB . 17944 1 154 . 1 1 29 29 PHE CG C 13 138.2 0.2 . 1 . . . . 102 PHE CG . 17944 1 155 . 1 1 29 29 PHE CD2 C 13 135.7 0.2 . . . . . . 102 PHE CD2 . 17944 1 156 . 1 1 29 29 PHE N N 15 120.4 0.2 . 1 . . . . 102 PHE N . 17944 1 157 . 1 1 30 30 LEU C C 13 177.4 0.2 . 1 . . . . 103 LEU C . 17944 1 158 . 1 1 30 30 LEU CA C 13 57.8 0.2 . 1 . . . . 103 LEU CA . 17944 1 159 . 1 1 30 30 LEU CB C 13 40.90 0.2 . 1 . . . . 103 LEU CB . 17944 1 160 . 1 1 30 30 LEU CG C 13 26.20 0.2 . 1 . . . . 103 LEU CG . 17944 1 161 . 1 1 30 30 LEU CD1 C 13 23.20 0.2 . . . . . . 103 LEU CD1 . 17944 1 162 . 1 1 30 30 LEU CD2 C 13 27.50 0.2 . . . . . . 103 LEU CD2 . 17944 1 163 . 1 1 30 30 LEU N N 15 119.9 0.2 . 1 . . . . 103 LEU N . 17944 1 164 . 1 1 31 31 ASP C C 13 179.2 0.2 . 1 . . . . 104 ASP C . 17944 1 165 . 1 1 31 31 ASP CA C 13 57.50 0.2 . 1 . . . . 104 ASP CA . 17944 1 166 . 1 1 31 31 ASP CB C 13 39.20 0.2 . 1 . . . . 104 ASP CB . 17944 1 167 . 1 1 31 31 ASP CG C 13 180.7 0.2 . 1 . . . . 104 ASP CG . 17944 1 168 . 1 1 31 31 ASP N N 15 120.8 0.2 . 1 . . . . 104 ASP N . 17944 1 169 . 1 1 32 32 ALA C C 13 179.1 0.2 . 1 . . . . 105 ALA C . 17944 1 170 . 1 1 32 32 ALA CA C 13 53.80 0.2 . 1 . . . . 105 ALA CA . 17944 1 171 . 1 1 32 32 ALA CB C 13 19.20 0.2 . 1 . . . . 105 ALA CB . 17944 1 172 . 1 1 32 32 ALA N N 15 120.9 0.2 . 1 . . . . 105 ALA N . 17944 1 173 . 1 1 33 33 ASN C C 13 178.3 0.2 . 1 . . . . 106 ASN C . 17944 1 174 . 1 1 33 33 ASN CA C 13 54.20 0.2 . 1 . . . . 106 ASN CA . 17944 1 175 . 1 1 33 33 ASN CB C 13 41.60 0.2 . 1 . . . . 106 ASN CB . 17944 1 176 . 1 1 33 33 ASN CG C 13 183.1 0.2 . 1 . . . . 106 ASN CG . 17944 1 177 . 1 1 33 33 ASN N N 15 112.7 0.2 . 1 . . . . 106 ASN N . 17944 1 178 . 1 1 34 34 LEU CA C 13 54.60 0.2 . 1 . . . . 107 LEU CA . 17944 1 179 . 1 1 34 34 LEU CB C 13 43.20 0.2 . 1 . . . . 107 LEU CB . 17944 1 180 . 1 1 34 34 LEU CG C 13 26.80 0.2 . 1 . . . . 107 LEU CG . 17944 1 181 . 1 1 34 34 LEU CD1 C 13 23.50 0.2 . . . . . . 107 LEU CD1 . 17944 1 182 . 1 1 34 34 LEU CD2 C 13 26.80 0.2 . . . . . . 107 LEU CD2 . 17944 1 183 . 1 1 34 34 LEU N N 15 121.0 0.2 . 1 . . . . 107 LEU N . 17944 1 184 . 1 1 35 35 ALA C C 13 178.0 0.2 . 1 . . . . 108 ALA C . 17944 1 185 . 1 1 35 35 ALA CA C 13 54.40 0.2 . 1 . . . . 108 ALA CA . 17944 1 186 . 1 1 35 35 ALA CB C 13 19.30 0.2 . 1 . . . . 108 ALA CB . 17944 1 stop_ save_