data_17700 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17700 _Entry.Title ; 13C, 15N Chemical shifts of E. coli thioredoxin using solid-state nmr spectroscopy ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2011-06-13 _Entry.Accession_date 2011-06-13 _Entry.Last_release_date 2011-07-15 _Entry.Original_release_date 2011-07-15 _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 Sivakumar Paramasivam . . . 17700 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 17700 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 487 17700 '15N chemical shifts' 106 17700 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 . . 2011-07-15 2011-06-13 original author . 17700 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 17700 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 16853329 _Citation.Full_citation . _Citation.Title 'Resonance Assignments and Secondary Structure Analysis of E. coli Thioredoxin by Magic Angle Spinning Solid-State NMR Spectroscopy' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Phys. Chem. B' _Citation.Journal_name_full . _Citation.Journal_volume 109 _Citation.Journal_issue 38 _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 18135 _Citation.Page_last 18145 _Citation.Year 2005 _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 . . . 17700 1 2 'Maria Luisa' Tasayco . . . 17700 1 3 Marcela Cataldi . . . 17700 1 4 Vilma Arriaran . . . 17700 1 5 Tatyana Polenova . . . 17700 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17700 _Assembly.ID 1 _Assembly.Name 'TRX Intact' _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 'TRX Intact' 1 $TRX_intact A . yes native no no . . 'only protein chain' 17700 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_TRX_intact _Entity.Sf_category entity _Entity.Sf_framecode TRX_intact _Entity.Entry_ID 17700 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name TRX_intact _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 ; SDKIIHLTDDSFDTDVLKAD GAILVDFWAEWCGPCKMIAP ILDEIADEYQGKLTVAKLNI DQNPGTAPKYGIRGIPTLLL FKNGEVAATKVGALSKGQLK EFLDANLA ; _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 108 _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 1812 . thioredoxin . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 17700 1 2 no BMRB 1813 . thioredoxin . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 1 18 no PDB 1TXX . "Active-Site Variant Of E.Coli Thioredoxin" . . . . . 100.00 108 98.15 98.15 8.03e-68 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 1 22 no PDB 1XOA . "Thioredoxin (Oxidized Disulfide Form), Nmr, 20 Structures" . . . . . 99.07 108 100.00 100.00 5.43e-70 . . . . 17700 1 23 no PDB 1XOB . "Thioredoxin (Reduced Dithio Form), Nmr, 20 Structures" . . . . . 99.07 108 100.00 100.00 5.43e-70 . . . . 17700 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 . . . . 17700 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 . . . . 17700 1 26 no PDB 1ZZY . "Crystal Structure Of Thioredoxin Mutant L7v" . . . . . 100.00 108 99.07 100.00 2.48e-70 . . . . 17700 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 . . . . 17700 1 28 no PDB 2BTO . "Structure Of Btuba From Prosthecobacter Dejongeii" . . . . . 100.00 108 100.00 100.00 1.05e-70 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 1 32 no PDB 2FCH . "Crystal Structure Of Thioredoxin Mutant G74s" . . . . . 100.00 108 99.07 99.07 5.32e-70 . . . . 17700 1 33 no PDB 2FD3 . "Crystal Structure Of Thioredoxin Mutant P34h" . . . . . 100.00 108 99.07 99.07 1.39e-69 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 1 44 no PDB 2O8V . "Paps Reductase In A Covalent Complex With Thioredoxin C35a" . . . . . 100.00 128 99.07 99.07 3.11e-70 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 1 51 no DBJ BAA00903 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 52 no DBJ BAB38137 . "thioredoxin 1 [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 127 100.00 100.00 4.32e-71 . . . . 17700 1 53 no DBJ BAE77517 . "thioredoxin 1 [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 54 no DBJ BAG79587 . "thioredoxin [Escherichia coli SE11]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 55 no DBJ BAH61053 . "thioredoxin [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" . . . . . 100.00 113 97.22 98.15 7.23e-69 . . . . 17700 1 56 no EMBL CAA79851 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 57 no EMBL CAD09400 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 58 no EMBL CAP78228 . "Thioredoxin 1 [Escherichia coli LF82]" . . . . . 100.00 144 100.00 100.00 4.26e-71 . . . . 17700 1 59 no EMBL CAQ34125 . "thioredoxin 1 [Escherichia coli BL21(DE3)]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 60 no EMBL CAQ91183 . "thioredoxin 1 [Escherichia fergusonii ATCC 35469]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 61 no GB AAA24533 . "thioredoxin (trxA) [Escherichia coli]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 62 no GB AAA24534 . "thioredoxin [Escherichia coli]" . . . . . 100.00 127 100.00 100.00 4.32e-71 . . . . 17700 1 63 no GB AAA24693 . "thioredoxin [Escherichia coli]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 64 no GB AAA24694 . "thioredoxin (trxA) [Escherichia coli]" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 65 no GB AAA24696 . "thioredoxin [Escherichia coli]" . . . . . 100.93 110 99.08 99.08 3.90e-69 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 1 69 no REF NP_312741 . "thioredoxin [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 127 100.00 100.00 4.32e-71 . . . . 17700 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 . . . . 17700 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 . . . . 17700 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 . . . . 17700 1 73 no REF NP_709584 . "thioredoxin [Shigella flexneri 2a str. 301]" . . . . . 100.00 127 100.00 100.00 4.32e-71 . . . . 17700 1 74 no SP P0AA25 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 75 no SP P0AA26 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 76 no SP P0AA27 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 77 no SP P0AA28 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 1 78 no SP P0AA29 . "RecName: Full=Thioredoxin-1; Short=Trx-1" . . . . . 100.00 109 100.00 100.00 7.78e-71 . . . . 17700 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 . 17700 1 2 . ASP . 17700 1 3 . LYS . 17700 1 4 . ILE . 17700 1 5 . ILE . 17700 1 6 . HIS . 17700 1 7 . LEU . 17700 1 8 . THR . 17700 1 9 . ASP . 17700 1 10 . ASP . 17700 1 11 . SER . 17700 1 12 . PHE . 17700 1 13 . ASP . 17700 1 14 . THR . 17700 1 15 . ASP . 17700 1 16 . VAL . 17700 1 17 . LEU . 17700 1 18 . LYS . 17700 1 19 . ALA . 17700 1 20 . ASP . 17700 1 21 . GLY . 17700 1 22 . ALA . 17700 1 23 . ILE . 17700 1 24 . LEU . 17700 1 25 . VAL . 17700 1 26 . ASP . 17700 1 27 . PHE . 17700 1 28 . TRP . 17700 1 29 . ALA . 17700 1 30 . GLU . 17700 1 31 . TRP . 17700 1 32 . CYS . 17700 1 33 . GLY . 17700 1 34 . PRO . 17700 1 35 . CYS . 17700 1 36 . LYS . 17700 1 37 . MET . 17700 1 38 . ILE . 17700 1 39 . ALA . 17700 1 40 . PRO . 17700 1 41 . ILE . 17700 1 42 . LEU . 17700 1 43 . ASP . 17700 1 44 . GLU . 17700 1 45 . ILE . 17700 1 46 . ALA . 17700 1 47 . ASP . 17700 1 48 . GLU . 17700 1 49 . TYR . 17700 1 50 . GLN . 17700 1 51 . GLY . 17700 1 52 . LYS . 17700 1 53 . LEU . 17700 1 54 . THR . 17700 1 55 . VAL . 17700 1 56 . ALA . 17700 1 57 . LYS . 17700 1 58 . LEU . 17700 1 59 . ASN . 17700 1 60 . ILE . 17700 1 61 . ASP . 17700 1 62 . GLN . 17700 1 63 . ASN . 17700 1 64 . PRO . 17700 1 65 . GLY . 17700 1 66 . THR . 17700 1 67 . ALA . 17700 1 68 . PRO . 17700 1 69 . LYS . 17700 1 70 . TYR . 17700 1 71 . GLY . 17700 1 72 . ILE . 17700 1 73 . ARG . 17700 1 74 . GLY . 17700 1 75 . ILE . 17700 1 76 . PRO . 17700 1 77 . THR . 17700 1 78 . LEU . 17700 1 79 . LEU . 17700 1 80 . LEU . 17700 1 81 . PHE . 17700 1 82 . LYS . 17700 1 83 . ASN . 17700 1 84 . GLY . 17700 1 85 . GLU . 17700 1 86 . VAL . 17700 1 87 . ALA . 17700 1 88 . ALA . 17700 1 89 . THR . 17700 1 90 . LYS . 17700 1 91 . VAL . 17700 1 92 . GLY . 17700 1 93 . ALA . 17700 1 94 . LEU . 17700 1 95 . SER . 17700 1 96 . LYS . 17700 1 97 . GLY . 17700 1 98 . GLN . 17700 1 99 . LEU . 17700 1 100 . LYS . 17700 1 101 . GLU . 17700 1 102 . PHE . 17700 1 103 . LEU . 17700 1 104 . ASP . 17700 1 105 . ALA . 17700 1 106 . ASN . 17700 1 107 . LEU . 17700 1 108 . ALA . 17700 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 17700 1 . ASP 2 2 17700 1 . LYS 3 3 17700 1 . ILE 4 4 17700 1 . ILE 5 5 17700 1 . HIS 6 6 17700 1 . LEU 7 7 17700 1 . THR 8 8 17700 1 . ASP 9 9 17700 1 . ASP 10 10 17700 1 . SER 11 11 17700 1 . PHE 12 12 17700 1 . ASP 13 13 17700 1 . THR 14 14 17700 1 . ASP 15 15 17700 1 . VAL 16 16 17700 1 . LEU 17 17 17700 1 . LYS 18 18 17700 1 . ALA 19 19 17700 1 . ASP 20 20 17700 1 . GLY 21 21 17700 1 . ALA 22 22 17700 1 . ILE 23 23 17700 1 . LEU 24 24 17700 1 . VAL 25 25 17700 1 . ASP 26 26 17700 1 . PHE 27 27 17700 1 . TRP 28 28 17700 1 . ALA 29 29 17700 1 . GLU 30 30 17700 1 . TRP 31 31 17700 1 . CYS 32 32 17700 1 . GLY 33 33 17700 1 . PRO 34 34 17700 1 . CYS 35 35 17700 1 . LYS 36 36 17700 1 . MET 37 37 17700 1 . ILE 38 38 17700 1 . ALA 39 39 17700 1 . PRO 40 40 17700 1 . ILE 41 41 17700 1 . LEU 42 42 17700 1 . ASP 43 43 17700 1 . GLU 44 44 17700 1 . ILE 45 45 17700 1 . ALA 46 46 17700 1 . ASP 47 47 17700 1 . GLU 48 48 17700 1 . TYR 49 49 17700 1 . GLN 50 50 17700 1 . GLY 51 51 17700 1 . LYS 52 52 17700 1 . LEU 53 53 17700 1 . THR 54 54 17700 1 . VAL 55 55 17700 1 . ALA 56 56 17700 1 . LYS 57 57 17700 1 . LEU 58 58 17700 1 . ASN 59 59 17700 1 . ILE 60 60 17700 1 . ASP 61 61 17700 1 . GLN 62 62 17700 1 . ASN 63 63 17700 1 . PRO 64 64 17700 1 . GLY 65 65 17700 1 . THR 66 66 17700 1 . ALA 67 67 17700 1 . PRO 68 68 17700 1 . LYS 69 69 17700 1 . TYR 70 70 17700 1 . GLY 71 71 17700 1 . ILE 72 72 17700 1 . ARG 73 73 17700 1 . GLY 74 74 17700 1 . ILE 75 75 17700 1 . PRO 76 76 17700 1 . THR 77 77 17700 1 . LEU 78 78 17700 1 . LEU 79 79 17700 1 . LEU 80 80 17700 1 . PHE 81 81 17700 1 . LYS 82 82 17700 1 . ASN 83 83 17700 1 . GLY 84 84 17700 1 . GLU 85 85 17700 1 . VAL 86 86 17700 1 . ALA 87 87 17700 1 . ALA 88 88 17700 1 . THR 89 89 17700 1 . LYS 90 90 17700 1 . VAL 91 91 17700 1 . GLY 92 92 17700 1 . ALA 93 93 17700 1 . LEU 94 94 17700 1 . SER 95 95 17700 1 . LYS 96 96 17700 1 . GLY 97 97 17700 1 . GLN 98 98 17700 1 . LEU 99 99 17700 1 . LYS 100 100 17700 1 . GLU 101 101 17700 1 . PHE 102 102 17700 1 . LEU 103 103 17700 1 . ASP 104 104 17700 1 . ALA 105 105 17700 1 . ASN 106 106 17700 1 . LEU 107 107 17700 1 . ALA 108 108 17700 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 17700 _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 $TRX_intact . 562 plasmid . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli JF521 . . . . . . . . . . . . . . . Trx . . . . 17700 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 17700 _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 $TRX_intact . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli JF521 . . . . . . . . . . . . . . . pTK100 . . . . . . 17700 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 17700 _Sample.ID 1 _Sample.Type solid _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system water _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 'TRX Intact' '[U-100% 13C; U-100% 15N]' . . 1 $TRX_intact . . . . . mM . . . . 17700 1 2 H2O 'natural abundance' . . . . . . 100 . . % . . . . 17700 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 17700 _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' . . M 17700 1 pH 7 . pH 17700 1 pressure 1 . atm 17700 1 temperature 273 . K 17700 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe_and_SPARKY _Software.Sf_category software _Software.Sf_framecode NMRPipe_and_SPARKY _Software.Entry_ID 17700 _Software.ID 1 _Software.Name NMRPipe_and_SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Zhengrong and Bax' . . 17700 1 Goddard . . 17700 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 17700 1 processing 17700 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 17700 _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 17700 _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 . . . 17700 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 17700 _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 C-C DARR' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17700 1 2 '2D N-CA SPECIFIC CP' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17700 1 3 '2D N-CO SPECIFIC CP' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17700 1 4 '2D N-CA-CX' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17700 1 5 '2D N-CO-CX' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17700 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 17700 _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 . indirect 0.251449530 . . . . . . . . . 17700 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . . . . . . . 17700 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 17700 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D C-C DARR' . . . 17700 1 2 '2D N-CA SPECIFIC CP' . . . 17700 1 3 '2D N-CO SPECIFIC CP' . . . 17700 1 4 '2D N-CA-CX' . . . 17700 1 5 '2D N-CO-CX' . . . 17700 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 SER C C 13 175.2 . . 1 . . . . 1 SER C . 17700 1 2 . 1 1 1 1 SER CA C 13 55.80 . . 1 . . . . 1 SER CA . 17700 1 3 . 1 1 1 1 SER CB C 13 64.90 . . 1 . . . . 1 SER CB . 17700 1 4 . 1 1 1 1 SER N N 15 105.0 . . 1 . . . . 1 SER N . 17700 1 5 . 1 1 2 2 ASP C C 13 177.4 . . 1 . . . . 2 ASP C . 17700 1 6 . 1 1 2 2 ASP CA C 13 50.80 . . 1 . . . . 2 ASP CA . 17700 1 7 . 1 1 2 2 ASP CB C 13 40.00 . . 1 . . . . 2 ASP CB . 17700 1 8 . 1 1 2 2 ASP CG C 13 178.6 . . 1 . . . . 2 ASP CG . 17700 1 9 . 1 1 3 3 LYS C C 13 174.6 . . 1 . . . . 3 LYS C . 17700 1 10 . 1 1 3 3 LYS CA C 13 54.00 . . 1 . . . . 3 LYS CA . 17700 1 11 . 1 1 3 3 LYS CB C 13 31.10 . . 1 . . . . 3 LYS CB . 17700 1 12 . 1 1 3 3 LYS CG C 13 22.50 . . 1 . . . . 3 LYS CG . 17700 1 13 . 1 1 3 3 LYS CD C 13 26.70 . . 1 . . . . 3 LYS CD . 17700 1 14 . 1 1 3 3 LYS CE C 13 40.10 . . 1 . . . . 3 LYS CE . 17700 1 15 . 1 1 3 3 LYS N N 15 118.1 . . 1 . . . . 3 LYS N . 17700 1 16 . 1 1 4 4 ILE C C 13 177.0 . . 1 . . . . 4 ILE C . 17700 1 17 . 1 1 4 4 ILE CA C 13 59.60 . . 1 . . . . 4 ILE CA . 17700 1 18 . 1 1 4 4 ILE CB C 13 37.10 . . 1 . . . . 4 ILE CB . 17700 1 19 . 1 1 4 4 ILE CG1 C 13 27.70 . . 1 . . . . 4 ILE CG1 . 17700 1 20 . 1 1 4 4 ILE CG2 C 13 16.30 . . 1 . . . . 4 ILE CG2 . 17700 1 21 . 1 1 4 4 ILE CD1 C 13 13.20 . . 1 . . . . 4 ILE CD1 . 17700 1 22 . 1 1 4 4 ILE N N 15 119.2 . . 1 . . . . 4 ILE N . 17700 1 23 . 1 1 5 5 ILE C C 13 176.0 . . 1 . . . . 5 ILE C . 17700 1 24 . 1 1 5 5 ILE CA C 13 60.20 . . 1 . . . . 5 ILE CA . 17700 1 25 . 1 1 5 5 ILE CB C 13 38.00 . . 1 . . . . 5 ILE CB . 17700 1 26 . 1 1 5 5 ILE CG1 C 13 26.00 . . 1 . . . . 5 ILE CG1 . 17700 1 27 . 1 1 5 5 ILE CG2 C 13 16.40 . . 1 . . . . 5 ILE CG2 . 17700 1 28 . 1 1 5 5 ILE CD1 C 13 13.30 . . 1 . . . . 5 ILE CD1 . 17700 1 29 . 1 1 5 5 ILE N N 15 127.1 . . 1 . . . . 5 ILE N . 17700 1 30 . 1 1 6 6 HIS C C 13 174.5 . . 1 . . . . 6 HIS C . 17700 1 31 . 1 1 6 6 HIS CA C 13 53.40 . . 1 . . . . 6 HIS CA . 17700 1 32 . 1 1 6 6 HIS CB C 13 26.00 . . 1 . . . . 6 HIS CB . 17700 1 33 . 1 1 6 6 HIS CG C 13 132.2 . . 1 . . . . 6 HIS CG . 17700 1 34 . 1 1 6 6 HIS CD2 C 13 121.6 . . 1 . . . . 6 HIS CD2 . 17700 1 35 . 1 1 6 6 HIS N N 15 127.3 . . 1 . . . . 6 HIS N . 17700 1 36 . 1 1 7 7 LEU C C 13 174.6 . . 1 . . . . 7 LEU C . 17700 1 37 . 1 1 7 7 LEU CA C 13 53.50 . . 1 . . . . 7 LEU CA . 17700 1 38 . 1 1 7 7 LEU CB C 13 43.80 . . 1 . . . . 7 LEU CB . 17700 1 39 . 1 1 7 7 LEU CG C 13 26.00 . . 1 . . . . 7 LEU CG . 17700 1 40 . 1 1 7 7 LEU CD1 C 13 27.00 . . . . . . . 7 LEU CD1 . 17700 1 41 . 1 1 7 7 LEU CD2 C 13 23.20 . . . . . . . 7 LEU CD2 . 17700 1 42 . 1 1 7 7 LEU N N 15 124.7 . . 1 . . . . 7 LEU N . 17700 1 43 . 1 1 8 8 THR C C 13 178.5 . . 1 . . . . 8 THR C . 17700 1 44 . 1 1 8 8 THR CA C 13 57.90 . . 1 . . . . 8 THR CA . 17700 1 45 . 1 1 8 8 THR CB C 13 71.60 . . 1 . . . . 8 THR CB . 17700 1 46 . 1 1 8 8 THR CG2 C 13 21.90 . . 1 . . . . 8 THR CG2 . 17700 1 47 . 1 1 8 8 THR N N 15 107.5 . . 1 . . . . 8 THR N . 17700 1 48 . 1 1 9 9 ASP C C 13 178.6 . . 1 . . . . 9 ASP C . 17700 1 49 . 1 1 9 9 ASP CA C 13 57.10 . . 1 . . . . 9 ASP CA . 17700 1 50 . 1 1 9 9 ASP CB C 13 39.60 . . 1 . . . . 9 ASP CB . 17700 1 51 . 1 1 9 9 ASP CG C 13 186.5 . . 1 . . . . 9 ASP CG . 17700 1 52 . 1 1 9 9 ASP N N 15 118.5 . . 1 . . . . 9 ASP N . 17700 1 53 . 1 1 10 10 ASP C C 13 177.8 . . 1 . . . . 10 ASP C . 17700 1 54 . 1 1 10 10 ASP CA C 13 55.50 . . 1 . . . . 10 ASP CA . 17700 1 55 . 1 1 10 10 ASP CB C 13 39.40 . . 1 . . . . 10 ASP CB . 17700 1 56 . 1 1 10 10 ASP N N 15 116.3 . . 1 . . . . 10 ASP N . 17700 1 57 . 1 1 11 11 SER C C 13 174.1 . . 1 . . . . 11 SER C . 17700 1 58 . 1 1 11 11 SER CA C 13 58.20 . . 1 . . . . 11 SER CA . 17700 1 59 . 1 1 11 11 SER CB C 13 63.80 . . 1 . . . . 11 SER CB . 17700 1 60 . 1 1 11 11 SER N N 15 117.5 . . 1 . . . . 11 SER N . 17700 1 61 . 1 1 12 12 PHE C C 13 176.0 . . 1 . . . . 12 PHE C . 17700 1 62 . 1 1 12 12 PHE CA C 13 62.40 . . 1 . . . . 12 PHE CA . 17700 1 63 . 1 1 12 12 PHE CB C 13 40.10 . . 1 . . . . 12 PHE CB . 17700 1 64 . 1 1 12 12 PHE CG C 13 139.1 . . 1 . . . . 12 PHE CG . 17700 1 65 . 1 1 12 12 PHE N N 15 124.4 . . 1 . . . . 12 PHE N . 17700 1 66 . 1 1 13 13 ASP C C 13 177.8 . . 1 . . . . 13 ASP C . 17700 1 67 . 1 1 13 13 ASP CA C 13 57.10 . . 1 . . . . 13 ASP CA . 17700 1 68 . 1 1 13 13 ASP CB C 13 38.10 . . 1 . . . . 13 ASP CB . 17700 1 69 . 1 1 13 13 ASP CG C 13 179.3 . . 1 . . . . 13 ASP CG . 17700 1 70 . 1 1 13 13 ASP N N 15 117.5 . . 1 . . . . 13 ASP N . 17700 1 71 . 1 1 14 14 THR C C 13 174.3 . . 1 . . . . 14 THR C . 17700 1 72 . 1 1 14 14 THR CA C 13 65.40 . . 1 . . . . 14 THR CA . 17700 1 73 . 1 1 14 14 THR CB C 13 68.30 . . 1 . . . . 14 THR CB . 17700 1 74 . 1 1 14 14 THR CG2 C 13 21.50 . . 1 . . . . 14 THR CG2 . 17700 1 75 . 1 1 14 14 THR N N 15 112.0 . . 1 . . . . 14 THR N . 17700 1 76 . 1 1 15 15 ASP C C 13 176.3 . . 1 . . . . 15 ASP C . 17700 1 77 . 1 1 15 15 ASP CA C 13 55.20 . . 1 . . . . 15 ASP CA . 17700 1 78 . 1 1 15 15 ASP CB C 13 39.70 . . 1 . . . . 15 ASP CB . 17700 1 79 . 1 1 15 15 ASP CG C 13 177.9 . . 1 . . . . 15 ASP CG . 17700 1 80 . 1 1 15 15 ASP N N 15 118.5 . . 1 . . . . 15 ASP N . 17700 1 81 . 1 1 16 16 VAL C C 13 176.5 . . 1 . . . . 16 VAL C . 17700 1 82 . 1 1 16 16 VAL CA C 13 62.20 . . 1 . . . . 16 VAL CA . 17700 1 83 . 1 1 16 16 VAL CB C 13 31.60 . . 1 . . . . 16 VAL CB . 17700 1 84 . 1 1 16 16 VAL CG1 C 13 19.10 . . . . . . . 16 VAL CG1 . 17700 1 85 . 1 1 16 16 VAL CG2 C 13 21.60 . . . . . . . 16 VAL CG2 . 17700 1 86 . 1 1 16 16 VAL N N 15 113.0 . . 1 . . . . 16 VAL N . 17700 1 87 . 1 1 17 17 LEU C C 13 177.7 . . 1 . . . . 17 LEU C . 17700 1 88 . 1 1 17 17 LEU CA C 13 56.90 . . 1 . . . . 17 LEU CA . 17700 1 89 . 1 1 17 17 LEU CB C 13 37.20 . . 1 . . . . 17 LEU CB . 17700 1 90 . 1 1 17 17 LEU CG C 13 24.50 . . 1 . . . . 17 LEU CG . 17700 1 91 . 1 1 17 17 LEU CD1 C 13 23.40 . . . . . . . 17 LEU CD1 . 17700 1 92 . 1 1 17 17 LEU CD2 C 13 20.10 . . . . . . . 17 LEU CD2 . 17700 1 93 . 1 1 17 17 LEU N N 15 116.5 . . 1 . . . . 17 LEU N . 17700 1 94 . 1 1 18 18 LYS C C 13 176.5 . . 1 . . . . 18 LYS C . 17700 1 95 . 1 1 18 18 LYS CA C 13 55.20 . . 1 . . . . 18 LYS CA . 17700 1 96 . 1 1 18 18 LYS CB C 13 29.20 . . 1 . . . . 18 LYS CB . 17700 1 97 . 1 1 18 18 LYS CG C 13 25.10 . . 1 . . . . 18 LYS CG . 17700 1 98 . 1 1 18 18 LYS CD C 13 27.70 . . 1 . . . . 18 LYS CD . 17700 1 99 . 1 1 18 18 LYS CE C 13 41.30 . . 1 . . . . 18 LYS CE . 17700 1 100 . 1 1 18 18 LYS N N 15 114.9 . . 1 . . . . 18 LYS N . 17700 1 101 . 1 1 19 19 ALA C C 13 177.0 . . 1 . . . . 19 ALA C . 17700 1 102 . 1 1 19 19 ALA CA C 13 51.10 . . 1 . . . . 19 ALA CA . 17700 1 103 . 1 1 19 19 ALA CB C 13 19.60 . . 1 . . . . 19 ALA CB . 17700 1 104 . 1 1 19 19 ALA N N 15 121.8 . . 1 . . . . 19 ALA N . 17700 1 105 . 1 1 20 20 ASP C C 13 174.8 . . 1 . . . . 20 ASP C . 17700 1 106 . 1 1 20 20 ASP CA C 13 51.20 . . 1 . . . . 20 ASP CA . 17700 1 107 . 1 1 20 20 ASP CB C 13 39.90 . . 1 . . . . 20 ASP CB . 17700 1 108 . 1 1 20 20 ASP CG C 13 179.8 . . 1 . . . . 20 ASP CG . 17700 1 109 . 1 1 20 20 ASP N N 15 121.4 . . 1 . . . . 20 ASP N . 17700 1 110 . 1 1 21 21 GLY C C 13 172.2 . . 1 . . . . 21 GLY C . 17700 1 111 . 1 1 21 21 GLY CA C 13 43.40 . . 1 . . . . 21 GLY CA . 17700 1 112 . 1 1 21 21 GLY N N 15 107.2 . . 1 . . . . 21 GLY N . 17700 1 113 . 1 1 22 22 ALA C C 13 177.2 . . 1 . . . . 22 ALA C . 17700 1 114 . 1 1 22 22 ALA CA C 13 50.90 . . 1 . . . . 22 ALA CA . 17700 1 115 . 1 1 22 22 ALA CB C 13 19.90 . . 1 . . . . 22 ALA CB . 17700 1 116 . 1 1 22 22 ALA N N 15 122.7 . . 1 . . . . 22 ALA N . 17700 1 117 . 1 1 23 23 ILE C C 13 172.5 . . 1 . . . . 23 ILE C . 17700 1 118 . 1 1 23 23 ILE CA C 13 57.60 . . 1 . . . . 23 ILE CA . 17700 1 119 . 1 1 23 23 ILE CB C 13 40.30 . . 1 . . . . 23 ILE CB . 17700 1 120 . 1 1 23 23 ILE CG1 C 13 25.10 . . 1 . . . . 23 ILE CG1 . 17700 1 121 . 1 1 23 23 ILE CG2 C 13 12.40 . . 1 . . . . 23 ILE CG2 . 17700 1 122 . 1 1 23 23 ILE CD1 C 13 10.10 . . 1 . . . . 23 ILE CD1 . 17700 1 123 . 1 1 23 23 ILE N N 15 122.9 . . 1 . . . . 23 ILE N . 17700 1 124 . 1 1 24 24 LEU C C 13 172.7 . . 1 . . . . 24 LEU C . 17700 1 125 . 1 1 24 24 LEU CA C 13 52.00 . . 1 . . . . 24 LEU CA . 17700 1 126 . 1 1 24 24 LEU CB C 13 44.70 . . 1 . . . . 24 LEU CB . 17700 1 127 . 1 1 24 24 LEU CG C 13 25.90 . . 1 . . . . 24 LEU CG . 17700 1 128 . 1 1 24 24 LEU CD1 C 13 23.70 . . . . . . . 24 LEU CD1 . 17700 1 129 . 1 1 24 24 LEU N N 15 129.8 . . 1 . . . . 24 LEU N . 17700 1 130 . 1 1 25 25 VAL C C 13 176.3 . . 1 . . . . 25 VAL C . 17700 1 131 . 1 1 25 25 VAL CA C 13 60.60 . . 1 . . . . 25 VAL CA . 17700 1 132 . 1 1 25 25 VAL CB C 13 33.00 . . 1 . . . . 25 VAL CB . 17700 1 133 . 1 1 25 25 VAL CG1 C 13 22.60 . . . . . . . 25 VAL CG1 . 17700 1 134 . 1 1 25 25 VAL CG2 C 13 20.30 . . . . . . . 25 VAL CG2 . 17700 1 135 . 1 1 25 25 VAL N N 15 126.2 . . 1 . . . . 25 VAL N . 17700 1 136 . 1 1 26 26 ASP C C 13 174.2 . . 1 . . . . 26 ASP C . 17700 1 137 . 1 1 26 26 ASP CA C 13 50.90 . . 1 . . . . 26 ASP CA . 17700 1 138 . 1 1 26 26 ASP CB C 13 38.00 . . 1 . . . . 26 ASP CB . 17700 1 139 . 1 1 26 26 ASP CG C 13 183.5 . . 1 . . . . 26 ASP CG . 17700 1 140 . 1 1 26 26 ASP N N 15 124.1 . . 1 . . . . 26 ASP N . 17700 1 141 . 1 1 27 27 PHE C C 13 174.1 . . 1 . . . . 27 PHE C . 17700 1 142 . 1 1 27 27 PHE CA C 13 56.80 . . 1 . . . . 27 PHE CA . 17700 1 143 . 1 1 27 27 PHE CB C 13 38.50 . . 1 . . . . 27 PHE CB . 17700 1 144 . 1 1 27 27 PHE CG C 13 139.7 . . 1 . . . . 27 PHE CG . 17700 1 145 . 1 1 27 27 PHE CD1 C 13 131.3 . . . . . . . 27 PHE CD1 . 17700 1 146 . 1 1 27 27 PHE CD2 C 13 130.2 . . . . . . . 27 PHE CD2 . 17700 1 147 . 1 1 27 27 PHE N N 15 128.0 . . 1 . . . . 27 PHE N . 17700 1 148 . 1 1 28 28 TRP C C 13 174.7 . . 1 . . . . 28 TRP C . 17700 1 149 . 1 1 28 28 TRP CA C 13 54.40 . . 1 . . . . 28 TRP CA . 17700 1 150 . 1 1 28 28 TRP CB C 13 31.40 . . 1 . . . . 28 TRP CB . 17700 1 151 . 1 1 28 28 TRP CG C 13 109.6 . . 1 . . . . 28 TRP CG . 17700 1 152 . 1 1 28 28 TRP CD1 C 13 125.8 . . 1 . . . . 28 TRP CD1 . 17700 1 153 . 1 1 28 28 TRP CD2 C 13 126.9 . . 1 . . . . 28 TRP CD2 . 17700 1 154 . 1 1 28 28 TRP N N 15 119.6 . . 1 . . . . 28 TRP N . 17700 1 155 . 1 1 30 30 GLU C C 13 178.2 . . 1 . . . . 30 GLU C . 17700 1 156 . 1 1 30 30 GLU CA C 13 57.50 . . 1 . . . . 30 GLU CA . 17700 1 157 . 1 1 30 30 GLU CB C 13 28.70 . . 1 . . . . 30 GLU CB . 17700 1 158 . 1 1 30 30 GLU CG C 13 34.00 . . 1 . . . . 30 GLU CG . 17700 1 159 . 1 1 30 30 GLU CD C 13 181.9 . . 1 . . . . 30 GLU CD . 17700 1 160 . 1 1 30 30 GLU N N 15 120.8 . . 1 . . . . 30 GLU N . 17700 1 161 . 1 1 31 31 TRP C C 13 177.8 . . 1 . . . . 31 TRP C . 17700 1 162 . 1 1 31 31 TRP CA C 13 53.40 . . 1 . . . . 31 TRP CA . 17700 1 163 . 1 1 31 31 TRP CB C 13 27.80 . . 1 . . . . 31 TRP CB . 17700 1 164 . 1 1 31 31 TRP CG C 13 108.2 . . 1 . . . . 31 TRP CG . 17700 1 165 . 1 1 31 31 TRP CD1 C 13 127.8 . . 1 . . . . 31 TRP CD1 . 17700 1 166 . 1 1 31 31 TRP CD2 C 13 130.5 . . 1 . . . . 31 TRP CD2 . 17700 1 167 . 1 1 31 31 TRP CE2 C 13 136.6 . . 1 . . . . 31 TRP CE2 . 17700 1 168 . 1 1 31 31 TRP CZ2 C 13 115.6 . . 1 . . . . 31 TRP CZ2 . 17700 1 169 . 1 1 31 31 TRP CH2 C 13 124.3 . . 1 . . . . 31 TRP CH2 . 17700 1 170 . 1 1 31 31 TRP N N 15 110.6 . . 1 . . . . 31 TRP N . 17700 1 171 . 1 1 32 32 CYS C C 13 174.4 . . 1 . . . . 32 CYS C . 17700 1 172 . 1 1 32 32 CYS CA C 13 58.10 . . 1 . . . . 32 CYS CA . 17700 1 173 . 1 1 32 32 CYS CB C 13 27.90 . . 1 . . . . 32 CYS CB . 17700 1 174 . 1 1 32 32 CYS N N 15 121.0 . . 1 . . . . 32 CYS N . 17700 1 175 . 1 1 33 33 GLY C C 13 175.5 . . 1 . . . . 33 GLY C . 17700 1 176 . 1 1 33 33 GLY CA C 13 48.00 . . 1 . . . . 33 GLY CA . 17700 1 177 . 1 1 33 33 GLY N N 15 120.6 . . 1 . . . . 33 GLY N . 17700 1 178 . 1 1 34 34 PRO C C 13 179.4 . . 1 . . . . 34 PRO C . 17700 1 179 . 1 1 34 34 PRO CA C 13 64.00 . . 1 . . . . 34 PRO CA . 17700 1 180 . 1 1 34 34 PRO CB C 13 31.70 . . 1 . . . . 34 PRO CB . 17700 1 181 . 1 1 34 34 PRO CG C 13 29.10 . . 1 . . . . 34 PRO CG . 17700 1 182 . 1 1 34 34 PRO CD C 13 51.10 . . 1 . . . . 34 PRO CD . 17700 1 183 . 1 1 34 34 PRO N N 15 136.5 . . 1 . . . . 34 PRO N . 17700 1 184 . 1 1 35 35 CYS CA C 13 62.80 . . 1 . . . . 35 CYS CA . 17700 1 185 . 1 1 35 35 CYS CB C 13 25.80 . . 1 . . . . 35 CYS CB . 17700 1 186 . 1 1 35 35 CYS N N 15 111.3 . . 1 . . . . 35 CYS N . 17700 1 187 . 1 1 36 36 LYS C C 13 176.4 . . 1 . . . . 36 LYS C . 17700 1 188 . 1 1 36 36 LYS CA C 13 57.90 . . 1 . . . . 36 LYS CA . 17700 1 189 . 1 1 36 36 LYS CB C 13 31.50 . . 1 . . . . 36 LYS CB . 17700 1 190 . 1 1 36 36 LYS CG C 13 23.60 . . 1 . . . . 36 LYS CG . 17700 1 191 . 1 1 36 36 LYS CD C 13 25.60 . . 1 . . . . 36 LYS CD . 17700 1 192 . 1 1 36 36 LYS CE C 13 40.00 . . 1 . . . . 36 LYS CE . 17700 1 193 . 1 1 36 36 LYS N N 15 121.1 . . 1 . . . . 36 LYS N . 17700 1 194 . 1 1 37 37 MET C C 13 176.9 . . 1 . . . . 37 MET C . 17700 1 195 . 1 1 37 37 MET CA C 13 55.80 . . 1 . . . . 37 MET CA . 17700 1 196 . 1 1 37 37 MET CB C 13 30.50 . . 1 . . . . 37 MET CB . 17700 1 197 . 1 1 37 37 MET CG C 13 32.60 . . 1 . . . . 37 MET CG . 17700 1 198 . 1 1 37 37 MET CE C 13 19.60 . . 1 . . . . 37 MET CE . 17700 1 199 . 1 1 37 37 MET N N 15 117.2 . . 1 . . . . 37 MET N . 17700 1 200 . 1 1 38 38 ILE C C 13 176.1 . . 1 . . . . 38 ILE C . 17700 1 201 . 1 1 38 38 ILE CA C 13 61.00 . . 1 . . . . 38 ILE CA . 17700 1 202 . 1 1 38 38 ILE CB C 13 38.60 . . 1 . . . . 38 ILE CB . 17700 1 203 . 1 1 38 38 ILE CG1 C 13 26.50 . . 1 . . . . 38 ILE CG1 . 17700 1 204 . 1 1 38 38 ILE CG2 C 13 16.50 . . 1 . . . . 38 ILE CG2 . 17700 1 205 . 1 1 38 38 ILE CD1 C 13 13.90 . . 1 . . . . 38 ILE CD1 . 17700 1 206 . 1 1 38 38 ILE N N 15 109.4 . . 1 . . . . 38 ILE N . 17700 1 207 . 1 1 39 39 ALA C C 13 176.5 . . 1 . . . . 39 ALA C . 17700 1 208 . 1 1 39 39 ALA CA C 13 56.50 . . 1 . . . . 39 ALA CA . 17700 1 209 . 1 1 39 39 ALA CB C 13 14.20 . . 1 . . . . 39 ALA CB . 17700 1 210 . 1 1 39 39 ALA N N 15 124.8 . . 1 . . . . 39 ALA N . 17700 1 211 . 1 1 40 40 PRO C C 13 179.1 . . 1 . . . . 40 PRO C . 17700 1 212 . 1 1 40 40 PRO CA C 13 64.60 . . 1 . . . . 40 PRO CA . 17700 1 213 . 1 1 40 40 PRO CB C 13 30.30 . . 1 . . . . 40 PRO CB . 17700 1 214 . 1 1 40 40 PRO CG C 13 27.60 . . 1 . . . . 40 PRO CG . 17700 1 215 . 1 1 40 40 PRO CD C 13 49.40 . . 1 . . . . 40 PRO CD . 17700 1 216 . 1 1 40 40 PRO N N 15 132.3 . . 1 . . . . 40 PRO N . 17700 1 217 . 1 1 41 41 ILE C C 13 177.9 . . 1 . . . . 41 ILE C . 17700 1 218 . 1 1 41 41 ILE CA C 13 63.50 . . 1 . . . . 41 ILE CA . 17700 1 219 . 1 1 41 41 ILE CB C 13 37.20 . . 1 . . . . 41 ILE CB . 17700 1 220 . 1 1 41 41 ILE CG1 C 13 27.50 . . 1 . . . . 41 ILE CG1 . 17700 1 221 . 1 1 41 41 ILE CG2 C 13 17.40 . . 1 . . . . 41 ILE CG2 . 17700 1 222 . 1 1 41 41 ILE CD1 C 13 12.20 . . 1 . . . . 41 ILE CD1 . 17700 1 223 . 1 1 41 41 ILE N N 15 117.3 . . 1 . . . . 41 ILE N . 17700 1 224 . 1 1 42 42 LEU C C 13 173.4 . . 1 . . . . 42 LEU C . 17700 1 225 . 1 1 42 42 LEU CA C 13 57.00 . . 1 . . . . 42 LEU CA . 17700 1 226 . 1 1 42 42 LEU CB C 13 38.60 . . 1 . . . . 42 LEU CB . 17700 1 227 . 1 1 42 42 LEU CG C 13 25.70 . . 1 . . . . 42 LEU CG . 17700 1 228 . 1 1 42 42 LEU CD1 C 13 23.70 . . . . . . . 42 LEU CD1 . 17700 1 229 . 1 1 42 42 LEU CD2 C 13 21.70 . . . . . . . 42 LEU CD2 . 17700 1 230 . 1 1 42 42 LEU N N 15 119.6 . . 1 . . . . 42 LEU N . 17700 1 231 . 1 1 43 43 ASP CA C 13 56.30 . . 1 . . . . 43 ASP CA . 17700 1 232 . 1 1 43 43 ASP CB C 13 38.00 . . 1 . . . . 43 ASP CB . 17700 1 233 . 1 1 43 43 ASP CG C 13 183.8 . . 1 . . . . 43 ASP CG . 17700 1 234 . 1 1 43 43 ASP N N 15 118.1 . . 1 . . . . 43 ASP N . 17700 1 235 . 1 1 44 44 GLU C C 13 179.1 . . 1 . . . . 44 GLU C . 17700 1 236 . 1 1 44 44 GLU CA C 13 57.90 . . 1 . . . . 44 GLU CA . 17700 1 237 . 1 1 44 44 GLU CB C 13 28.40 . . 1 . . . . 44 GLU CB . 17700 1 238 . 1 1 44 44 GLU CG C 13 33.80 . . 1 . . . . 44 GLU CG . 17700 1 239 . 1 1 44 44 GLU CD C 13 181.4 . . 1 . . . . 44 GLU CD . 17700 1 240 . 1 1 44 44 GLU N N 15 118.3 . . 1 . . . . 44 GLU N . 17700 1 241 . 1 1 45 45 ILE C C 13 176.2 . . 1 . . . . 45 ILE C . 17700 1 242 . 1 1 45 45 ILE CA C 13 61.40 . . 1 . . . . 45 ILE CA . 17700 1 243 . 1 1 45 45 ILE CB C 13 35.30 . . 1 . . . . 45 ILE CB . 17700 1 244 . 1 1 45 45 ILE CG1 C 13 29.20 . . 1 . . . . 45 ILE CG1 . 17700 1 245 . 1 1 45 45 ILE CG2 C 13 17.70 . . 1 . . . . 45 ILE CG2 . 17700 1 246 . 1 1 45 45 ILE CD1 C 13 10.10 . . 1 . . . . 45 ILE CD1 . 17700 1 247 . 1 1 45 45 ILE N N 15 122.7 . . 1 . . . . 45 ILE N . 17700 1 248 . 1 1 46 46 ALA C C 13 179.2 . . 1 . . . . 46 ALA C . 17700 1 249 . 1 1 46 46 ALA CA C 13 54.30 . . 1 . . . . 46 ALA CA . 17700 1 250 . 1 1 46 46 ALA CB C 13 17.70 . . 1 . . . . 46 ALA CB . 17700 1 251 . 1 1 46 46 ALA N N 15 121.6 . . 1 . . . . 46 ALA N . 17700 1 252 . 1 1 47 47 ASP C C 13 177.6 . . 1 . . . . 47 ASP C . 17700 1 253 . 1 1 47 47 ASP CA C 13 56.10 . . 1 . . . . 47 ASP CA . 17700 1 254 . 1 1 47 47 ASP CB C 13 40.50 . . 1 . . . . 47 ASP CB . 17700 1 255 . 1 1 47 47 ASP CG C 13 179.2 . . 1 . . . . 47 ASP CG . 17700 1 256 . 1 1 47 47 ASP N N 15 114.0 . . 1 . . . . 47 ASP N . 17700 1 257 . 1 1 48 48 GLU C C 13 177.3 . . 1 . . . . 48 GLU C . 17700 1 258 . 1 1 48 48 GLU CA C 13 58.30 . . 1 . . . . 48 GLU CA . 17700 1 259 . 1 1 48 48 GLU CB C 13 29.20 . . 1 . . . . 48 GLU CB . 17700 1 260 . 1 1 48 48 GLU CG C 13 35.10 . . 1 . . . . 48 GLU CG . 17700 1 261 . 1 1 48 48 GLU CD C 13 181.0 . . 1 . . . . 48 GLU CD . 17700 1 262 . 1 1 48 48 GLU N N 15 119.5 . . 1 . . . . 48 GLU N . 17700 1 263 . 1 1 49 49 TYR C C 13 176.5 . . 1 . . . . 49 TYR C . 17700 1 264 . 1 1 49 49 TYR CA C 13 55.60 . . 1 . . . . 49 TYR CA . 17700 1 265 . 1 1 49 49 TYR CB C 13 35.30 . . 1 . . . . 49 TYR CB . 17700 1 266 . 1 1 49 49 TYR CE1 C 13 117.9 . . . . . . . 49 TYR CE1 . 17700 1 267 . 1 1 49 49 TYR N N 15 114.9 . . 1 . . . . 49 TYR N . 17700 1 268 . 1 1 50 50 GLN C C 13 177.5 . . 1 . . . . 50 GLN C . 17700 1 269 . 1 1 50 50 GLN CA C 13 57.50 . . 1 . . . . 50 GLN CA . 17700 1 270 . 1 1 50 50 GLN CB C 13 26.50 . . 1 . . . . 50 GLN CB . 17700 1 271 . 1 1 50 50 GLN CG C 13 30.80 . . 1 . . . . 50 GLN CG . 17700 1 272 . 1 1 50 50 GLN CD C 13 183.1 . . 1 . . . . 50 GLN CD . 17700 1 273 . 1 1 50 50 GLN N N 15 121.3 . . 1 . . . . 50 GLN N . 17700 1 274 . 1 1 51 51 GLY C C 13 175.6 . . 1 . . . . 51 GLY C . 17700 1 275 . 1 1 51 51 GLY CA C 13 41.40 . . 1 . . . . 51 GLY CA . 17700 1 276 . 1 1 51 51 GLY N N 15 116.6 . . 1 . . . . 51 GLY N . 17700 1 277 . 1 1 52 52 LYS C C 13 176.5 . . 1 . . . . 52 LYS C . 17700 1 278 . 1 1 52 52 LYS CA C 13 55.40 . . 1 . . . . 52 LYS CA . 17700 1 279 . 1 1 52 52 LYS CB C 13 34.80 . . 1 . . . . 52 LYS CB . 17700 1 280 . 1 1 52 52 LYS CG C 13 24.00 . . 1 . . . . 52 LYS CG . 17700 1 281 . 1 1 52 52 LYS CD C 13 28.80 . . 1 . . . . 52 LYS CD . 17700 1 282 . 1 1 52 52 LYS CE C 13 40.90 . . 1 . . . . 52 LYS CE . 17700 1 283 . 1 1 52 52 LYS N N 15 116.4 . . 1 . . . . 52 LYS N . 17700 1 284 . 1 1 53 53 LEU C C 13 176.0 . . 1 . . . . 53 LEU C . 17700 1 285 . 1 1 53 53 LEU CA C 13 53.70 . . 1 . . . . 53 LEU CA . 17700 1 286 . 1 1 53 53 LEU CB C 13 45.70 . . 1 . . . . 53 LEU CB . 17700 1 287 . 1 1 53 53 LEU CG C 13 23.30 . . 1 . . . . 53 LEU CG . 17700 1 288 . 1 1 53 53 LEU CD1 C 13 25.50 . . . . . . . 53 LEU CD1 . 17700 1 289 . 1 1 53 53 LEU CD2 C 13 23.20 . . . . . . . 53 LEU CD2 . 17700 1 290 . 1 1 53 53 LEU N N 15 118.6 . . 1 . . . . 53 LEU N . 17700 1 291 . 1 1 54 54 THR C C 13 171.2 . . 1 . . . . 54 THR C . 17700 1 292 . 1 1 54 54 THR CA C 13 61.00 . . 1 . . . . 54 THR CA . 17700 1 293 . 1 1 54 54 THR CB C 13 69.40 . . 1 . . . . 54 THR CB . 17700 1 294 . 1 1 54 54 THR CG2 C 13 21.10 . . 1 . . . . 54 THR CG2 . 17700 1 295 . 1 1 54 54 THR N N 15 123.3 . . 1 . . . . 54 THR N . 17700 1 296 . 1 1 55 55 VAL C C 13 171.7 . . 1 . . . . 55 VAL C . 17700 1 297 . 1 1 55 55 VAL CA C 13 60.60 . . 1 . . . . 55 VAL CA . 17700 1 298 . 1 1 55 55 VAL CB C 13 32.00 . . 1 . . . . 55 VAL CB . 17700 1 299 . 1 1 55 55 VAL CG1 C 13 21.90 . . . . . . . 55 VAL CG1 . 17700 1 300 . 1 1 55 55 VAL CG2 C 13 21.30 . . . . . . . 55 VAL CG2 . 17700 1 301 . 1 1 55 55 VAL N N 15 129.4 . . 1 . . . . 55 VAL N . 17700 1 302 . 1 1 56 56 ALA C C 13 174.7 . . 1 . . . . 56 ALA C . 17700 1 303 . 1 1 56 56 ALA CA C 13 48.90 . . 1 . . . . 56 ALA CA . 17700 1 304 . 1 1 56 56 ALA CB C 13 23.50 . . 1 . . . . 56 ALA CB . 17700 1 305 . 1 1 56 56 ALA N N 15 128.3 . . 1 . . . . 56 ALA N . 17700 1 306 . 1 1 57 57 LYS C C 13 174.8 . . 1 . . . . 57 LYS C . 17700 1 307 . 1 1 57 57 LYS CA C 13 54.10 . . 1 . . . . 57 LYS CA . 17700 1 308 . 1 1 57 57 LYS CB C 13 44.30 . . 1 . . . . 57 LYS CB . 17700 1 309 . 1 1 57 57 LYS CG C 13 24.30 . . 1 . . . . 57 LYS CG . 17700 1 310 . 1 1 57 57 LYS CD C 13 26.40 . . 1 . . . . 57 LYS CD . 17700 1 311 . 1 1 57 57 LYS CE C 13 42.10 . . 1 . . . . 57 LYS CE . 17700 1 312 . 1 1 57 57 LYS N N 15 117.6 . . 1 . . . . 57 LYS N . 17700 1 313 . 1 1 58 58 LEU C C 13 172.5 . . 1 . . . . 58 LEU C . 17700 1 314 . 1 1 58 58 LEU CA C 13 52.60 . . 1 . . . . 58 LEU CA . 17700 1 315 . 1 1 58 58 LEU CB C 13 43.70 . . 1 . . . . 58 LEU CB . 17700 1 316 . 1 1 58 58 LEU CG C 13 27.70 . . 1 . . . . 58 LEU CG . 17700 1 317 . 1 1 58 58 LEU CD1 C 13 22.90 . . . . . . . 58 LEU CD1 . 17700 1 318 . 1 1 58 58 LEU N N 15 123.5 . . 1 . . . . 58 LEU N . 17700 1 319 . 1 1 59 59 ASN C C 13 175.2 . . 1 . . . . 59 ASN C . 17700 1 320 . 1 1 59 59 ASN CA C 13 50.90 . . 1 . . . . 59 ASN CA . 17700 1 321 . 1 1 59 59 ASN CB C 13 37.70 . . 1 . . . . 59 ASN CB . 17700 1 322 . 1 1 59 59 ASN CG C 13 176.9 . . 1 . . . . 59 ASN CG . 17700 1 323 . 1 1 59 59 ASN N N 15 126.4 . . 1 . . . . 59 ASN N . 17700 1 324 . 1 1 60 60 ILE C C 13 176.9 . . 1 . . . . 60 ILE C . 17700 1 325 . 1 1 60 60 ILE CA C 13 62.70 . . 1 . . . . 60 ILE CA . 17700 1 326 . 1 1 60 60 ILE CB C 13 37.00 . . 1 . . . . 60 ILE CB . 17700 1 327 . 1 1 60 60 ILE CG1 C 13 24.30 . . 1 . . . . 60 ILE CG1 . 17700 1 328 . 1 1 60 60 ILE CG2 C 13 18.80 . . 1 . . . . 60 ILE CG2 . 17700 1 329 . 1 1 60 60 ILE CD1 C 13 14.50 . . 1 . . . . 60 ILE CD1 . 17700 1 330 . 1 1 60 60 ILE N N 15 120.8 . . 1 . . . . 60 ILE N . 17700 1 331 . 1 1 61 61 ASP C C 13 176.3 . . 1 . . . . 61 ASP C . 17700 1 332 . 1 1 61 61 ASP CA C 13 55.70 . . 1 . . . . 61 ASP CA . 17700 1 333 . 1 1 61 61 ASP CB C 13 39.90 . . 1 . . . . 61 ASP CB . 17700 1 334 . 1 1 61 61 ASP CG C 13 179.5 . . 1 . . . . 61 ASP CG . 17700 1 335 . 1 1 61 61 ASP N N 15 122.1 . . 1 . . . . 61 ASP N . 17700 1 336 . 1 1 62 62 GLN C C 13 177.3 . . 1 . . . . 62 GLN C . 17700 1 337 . 1 1 62 62 GLN CA C 13 57.40 . . 1 . . . . 62 GLN CA . 17700 1 338 . 1 1 62 62 GLN CB C 13 28.40 . . 1 . . . . 62 GLN CB . 17700 1 339 . 1 1 62 62 GLN CG C 13 31.30 . . 1 . . . . 62 GLN CG . 17700 1 340 . 1 1 62 62 GLN CD C 13 181.1 . . 1 . . . . 62 GLN CD . 17700 1 341 . 1 1 62 62 GLN N N 15 116.3 . . 1 . . . . 62 GLN N . 17700 1 342 . 1 1 63 63 ASN C C 13 175.7 . . 1 . . . . 63 ASN C . 17700 1 343 . 1 1 63 63 ASN CA C 13 50.80 . . 1 . . . . 63 ASN CA . 17700 1 344 . 1 1 63 63 ASN CB C 13 40.00 . . 1 . . . . 63 ASN CB . 17700 1 345 . 1 1 63 63 ASN CG C 13 178.1 . . 1 . . . . 63 ASN CG . 17700 1 346 . 1 1 63 63 ASN N N 15 116.3 . . 1 . . . . 63 ASN N . 17700 1 347 . 1 1 64 64 PRO C C 13 177.7 . . 1 . . . . 64 PRO C . 17700 1 348 . 1 1 64 64 PRO CA C 13 62.90 . . 1 . . . . 64 PRO CA . 17700 1 349 . 1 1 64 64 PRO CB C 13 32.10 . . 1 . . . . 64 PRO CB . 17700 1 350 . 1 1 64 64 PRO CG C 13 25.10 . . 1 . . . . 64 PRO CG . 17700 1 351 . 1 1 64 64 PRO CD C 13 49.00 . . 1 . . . . 64 PRO CD . 17700 1 352 . 1 1 64 64 PRO N N 15 128.4 . . 1 . . . . 64 PRO N . 17700 1 353 . 1 1 65 65 GLY C C 13 173.7 . . 1 . . . . 65 GLY C . 17700 1 354 . 1 1 65 65 GLY CA C 13 45.40 . . 1 . . . . 65 GLY CA . 17700 1 355 . 1 1 65 65 GLY N N 15 111.9 . . 1 . . . . 65 GLY N . 17700 1 356 . 1 1 66 66 THR C C 13 175.4 . . 1 . . . . 66 THR C . 17700 1 357 . 1 1 66 66 THR CA C 13 68.90 . . 1 . . . . 66 THR CA . 17700 1 358 . 1 1 66 66 THR CB C 13 67.40 . . 1 . . . . 66 THR CB . 17700 1 359 . 1 1 66 66 THR CG2 C 13 19.40 . . 1 . . . . 66 THR CG2 . 17700 1 360 . 1 1 66 66 THR N N 15 117.6 . . 1 . . . . 66 THR N . 17700 1 361 . 1 1 67 67 ALA C C 13 176.1 . . 1 . . . . 67 ALA C . 17700 1 362 . 1 1 67 67 ALA CA C 13 56.30 . . 1 . . . . 67 ALA CA . 17700 1 363 . 1 1 67 67 ALA CB C 13 14.60 . . 1 . . . . 67 ALA CB . 17700 1 364 . 1 1 67 67 ALA N N 15 124.3 . . 1 . . . . 67 ALA N . 17700 1 365 . 1 1 68 68 PRO C C 13 179.1 . . 1 . . . . 68 PRO C . 17700 1 366 . 1 1 68 68 PRO CA C 13 64.80 . . 1 . . . . 68 PRO CA . 17700 1 367 . 1 1 68 68 PRO CB C 13 30.00 . . 1 . . . . 68 PRO CB . 17700 1 368 . 1 1 68 68 PRO CG C 13 28.10 . . 1 . . . . 68 PRO CG . 17700 1 369 . 1 1 68 68 PRO CD C 13 49.60 . . 1 . . . . 68 PRO CD . 17700 1 370 . 1 1 68 68 PRO N N 15 133.5 . . 1 . . . . 68 PRO N . 17700 1 371 . 1 1 69 69 LYS C C 13 178.0 . . 1 . . . . 69 LYS C . 17700 1 372 . 1 1 69 69 LYS CA C 13 57.10 . . 1 . . . . 69 LYS CA . 17700 1 373 . 1 1 69 69 LYS CB C 13 31.60 . . 1 . . . . 69 LYS CB . 17700 1 374 . 1 1 69 69 LYS CG C 13 21.50 . . 1 . . . . 69 LYS CG . 17700 1 375 . 1 1 69 69 LYS CD C 13 25.80 . . 1 . . . . 69 LYS CD . 17700 1 376 . 1 1 69 69 LYS CE C 13 39.90 . . 1 . . . . 69 LYS CE . 17700 1 377 . 1 1 69 69 LYS N N 15 117.1 . . 1 . . . . 69 LYS N . 17700 1 378 . 1 1 70 70 TYR C C 13 177.2 . . 1 . . . . 70 TYR C . 17700 1 379 . 1 1 70 70 TYR CA C 13 57.60 . . 1 . . . . 70 TYR CA . 17700 1 380 . 1 1 70 70 TYR CB C 13 38.90 . . 1 . . . . 70 TYR CB . 17700 1 381 . 1 1 70 70 TYR CG C 13 131.5 . . 1 . . . . 70 TYR CG . 17700 1 382 . 1 1 70 70 TYR CE2 C 13 116.8 . . . . . . . 70 TYR CE2 . 17700 1 383 . 1 1 70 70 TYR N N 15 114.6 . . 1 . . . . 70 TYR N . 17700 1 384 . 1 1 71 71 GLY C C 13 173.0 . . 1 . . . . 71 GLY C . 17700 1 385 . 1 1 71 71 GLY CA C 13 45.90 . . 1 . . . . 71 GLY CA . 17700 1 386 . 1 1 71 71 GLY N N 15 107.1 . . 1 . . . . 71 GLY N . 17700 1 387 . 1 1 72 72 ILE C C 13 176.1 . . 1 . . . . 72 ILE C . 17700 1 388 . 1 1 72 72 ILE CA C 13 60.50 . . 1 . . . . 72 ILE CA . 17700 1 389 . 1 1 72 72 ILE CB C 13 35.50 . . 1 . . . . 72 ILE CB . 17700 1 390 . 1 1 72 72 ILE CG1 C 13 26.00 . . 1 . . . . 72 ILE CG1 . 17700 1 391 . 1 1 72 72 ILE CG2 C 13 17.50 . . 1 . . . . 72 ILE CG2 . 17700 1 392 . 1 1 72 72 ILE CD1 C 13 14.10 . . 1 . . . . 72 ILE CD1 . 17700 1 393 . 1 1 72 72 ILE N N 15 120.9 . . 1 . . . . 72 ILE N . 17700 1 394 . 1 1 73 73 ARG C C 13 177.7 . . 1 . . . . 73 ARG C . 17700 1 395 . 1 1 73 73 ARG CA C 13 57.70 . . 1 . . . . 73 ARG CA . 17700 1 396 . 1 1 73 73 ARG CB C 13 30.70 . . 1 . . . . 73 ARG CB . 17700 1 397 . 1 1 73 73 ARG CG C 13 24.70 . . 1 . . . . 73 ARG CG . 17700 1 398 . 1 1 73 73 ARG CD C 13 41.20 . . 1 . . . . 73 ARG CD . 17700 1 399 . 1 1 73 73 ARG CZ C 13 158.3 . . 1 . . . . 73 ARG CZ . 17700 1 400 . 1 1 73 73 ARG N N 15 128.4 . . 1 . . . . 73 ARG N . 17700 1 401 . 1 1 74 74 GLY C C 13 172.0 . . 1 . . . . 74 GLY C . 17700 1 402 . 1 1 74 74 GLY CA C 13 43.80 . . 1 . . . . 74 GLY CA . 17700 1 403 . 1 1 74 74 GLY N N 15 108.1 . . 1 . . . . 74 GLY N . 17700 1 404 . 1 1 75 75 ILE C C 13 175.8 . . 1 . . . . 75 ILE C . 17700 1 405 . 1 1 75 75 ILE CA C 13 56.90 . . 1 . . . . 75 ILE CA . 17700 1 406 . 1 1 75 75 ILE CB C 13 40.20 . . 1 . . . . 75 ILE CB . 17700 1 407 . 1 1 75 75 ILE CG1 C 13 21.60 . . 1 . . . . 75 ILE CG1 . 17700 1 408 . 1 1 75 75 ILE CG2 C 13 19.50 . . 1 . . . . 75 ILE CG2 . 17700 1 409 . 1 1 75 75 ILE CD1 C 13 17.10 . . 1 . . . . 75 ILE CD1 . 17700 1 410 . 1 1 75 75 ILE N N 15 113.5 . . 1 . . . . 75 ILE N . 17700 1 411 . 1 1 76 76 PRO C C 13 178.0 . . 1 . . . . 76 PRO C . 17700 1 412 . 1 1 76 76 PRO CA C 13 62.70 . . 1 . . . . 76 PRO CA . 17700 1 413 . 1 1 76 76 PRO CB C 13 32.40 . . 1 . . . . 76 PRO CB . 17700 1 414 . 1 1 76 76 PRO CG C 13 25.60 . . 1 . . . . 76 PRO CG . 17700 1 415 . 1 1 76 76 PRO CD C 13 49.10 . . 1 . . . . 76 PRO CD . 17700 1 416 . 1 1 76 76 PRO N N 15 130.9 . . 1 . . . . 76 PRO N . 17700 1 417 . 1 1 77 77 THR C C 13 171.6 . . 1 . . . . 77 THR C . 17700 1 418 . 1 1 77 77 THR CA C 13 62.80 . . 1 . . . . 77 THR CA . 17700 1 419 . 1 1 77 77 THR CB C 13 71.80 . . 1 . . . . 77 THR CB . 17700 1 420 . 1 1 77 77 THR CG2 C 13 21.80 . . 1 . . . . 77 THR CG2 . 17700 1 421 . 1 1 77 77 THR N N 15 118.7 . . 1 . . . . 77 THR N . 17700 1 422 . 1 1 78 78 LEU C C 13 173.9 . . 1 . . . . 78 LEU C . 17700 1 423 . 1 1 78 78 LEU CA C 13 52.20 . . 1 . . . . 78 LEU CA . 17700 1 424 . 1 1 78 78 LEU CB C 13 43.70 . . 1 . . . . 78 LEU CB . 17700 1 425 . 1 1 78 78 LEU CG C 13 26.50 . . 1 . . . . 78 LEU CG . 17700 1 426 . 1 1 78 78 LEU CD1 C 13 26.50 . . . . . . . 78 LEU CD1 . 17700 1 427 . 1 1 78 78 LEU CD2 C 13 22.50 . . . . . . . 78 LEU CD2 . 17700 1 428 . 1 1 78 78 LEU N N 15 127.5 . . 1 . . . . 78 LEU N . 17700 1 429 . 1 1 79 79 LEU C C 13 172.7 . . 1 . . . . 79 LEU C . 17700 1 430 . 1 1 79 79 LEU CA C 13 51.90 . . 1 . . . . 79 LEU CA . 17700 1 431 . 1 1 79 79 LEU CB C 13 44.40 . . 1 . . . . 79 LEU CB . 17700 1 432 . 1 1 79 79 LEU CG C 13 26.10 . . 1 . . . . 79 LEU CG . 17700 1 433 . 1 1 79 79 LEU CD1 C 13 24.20 . . . . . . . 79 LEU CD1 . 17700 1 434 . 1 1 79 79 LEU CD2 C 13 23.70 . . . . . . . 79 LEU CD2 . 17700 1 435 . 1 1 79 79 LEU N N 15 123.1 . . 1 . . . . 79 LEU N . 17700 1 436 . 1 1 80 80 LEU C C 13 174.1 . . 1 . . . . 80 LEU C . 17700 1 437 . 1 1 80 80 LEU CA C 13 51.90 . . 1 . . . . 80 LEU CA . 17700 1 438 . 1 1 80 80 LEU CB C 13 43.80 . . 1 . . . . 80 LEU CB . 17700 1 439 . 1 1 80 80 LEU CG C 13 25.90 . . 1 . . . . 80 LEU CG . 17700 1 440 . 1 1 80 80 LEU CD1 C 13 25.90 . . . . . . . 80 LEU CD1 . 17700 1 441 . 1 1 80 80 LEU CD2 C 13 22.90 . . . . . . . 80 LEU CD2 . 17700 1 442 . 1 1 80 80 LEU N N 15 125.5 . . 1 . . . . 80 LEU N . 17700 1 443 . 1 1 81 81 PHE C C 13 176.4 . . 1 . . . . 81 PHE C . 17700 1 444 . 1 1 81 81 PHE CA C 13 57.50 . . 1 . . . . 81 PHE CA . 17700 1 445 . 1 1 81 81 PHE CB C 13 39.60 . . 1 . . . . 81 PHE CB . 17700 1 446 . 1 1 81 81 PHE CG C 13 140.1 . . 1 . . . . 81 PHE CG . 17700 1 447 . 1 1 81 81 PHE CD1 C 13 132.6 . . . . . . . 81 PHE CD1 . 17700 1 448 . 1 1 81 81 PHE CD2 C 13 131.6 . . . . . . . 81 PHE CD2 . 17700 1 449 . 1 1 81 81 PHE N N 15 127.7 . . 1 . . . . 81 PHE N . 17700 1 450 . 1 1 82 82 LYS C C 13 176.7 . . 1 . . . . 82 LYS C . 17700 1 451 . 1 1 82 82 LYS CA C 13 55.30 . . 1 . . . . 82 LYS CA . 17700 1 452 . 1 1 82 82 LYS CB C 13 34.20 . . 1 . . . . 82 LYS CB . 17700 1 453 . 1 1 82 82 LYS CG C 13 23.70 . . 1 . . . . 82 LYS CG . 17700 1 454 . 1 1 82 82 LYS CD C 13 26.80 . . 1 . . . . 82 LYS CD . 17700 1 455 . 1 1 82 82 LYS CE C 13 41.10 . . 1 . . . . 82 LYS CE . 17700 1 456 . 1 1 82 82 LYS N N 15 117.3 . . 1 . . . . 82 LYS N . 17700 1 457 . 1 1 83 83 ASN C C 13 175.2 . . 1 . . . . 83 ASN C . 17700 1 458 . 1 1 83 83 ASN CA C 13 53.40 . . 1 . . . . 83 ASN CA . 17700 1 459 . 1 1 83 83 ASN CB C 13 33.50 . . 1 . . . . 83 ASN CB . 17700 1 460 . 1 1 83 83 ASN CG C 13 176.5 . . 1 . . . . 83 ASN CG . 17700 1 461 . 1 1 83 83 ASN N N 15 126.9 . . 1 . . . . 83 ASN N . 17700 1 462 . 1 1 84 84 GLY C C 13 173.5 . . 1 . . . . 84 GLY C . 17700 1 463 . 1 1 84 84 GLY CA C 13 45.60 . . 1 . . . . 84 GLY CA . 17700 1 464 . 1 1 84 84 GLY N N 15 104.1 . . 1 . . . . 84 GLY N . 17700 1 465 . 1 1 85 85 GLU C C 13 177.9 . . 1 . . . . 85 GLU C . 17700 1 466 . 1 1 85 85 GLU CA C 13 52.80 . . 1 . . . . 85 GLU CA . 17700 1 467 . 1 1 85 85 GLU CB C 13 31.90 . . 1 . . . . 85 GLU CB . 17700 1 468 . 1 1 85 85 GLU CG C 13 34.20 . . 1 . . . . 85 GLU CG . 17700 1 469 . 1 1 85 85 GLU CD C 13 181.9 . . 1 . . . . 85 GLU CD . 17700 1 470 . 1 1 85 85 GLU N N 15 118.6 . . 1 . . . . 85 GLU N . 17700 1 471 . 1 1 86 86 VAL C C 13 175.5 . . 1 . . . . 86 VAL C . 17700 1 472 . 1 1 86 86 VAL CA C 13 63.50 . . 1 . . . . 86 VAL CA . 17700 1 473 . 1 1 86 86 VAL CB C 13 30.90 . . 1 . . . . 86 VAL CB . 17700 1 474 . 1 1 86 86 VAL CG1 C 13 22.60 . . . . . . . 86 VAL CG1 . 17700 1 475 . 1 1 86 86 VAL CG2 C 13 22.40 . . . . . . . 86 VAL CG2 . 17700 1 476 . 1 1 86 86 VAL N N 15 123.1 . . 1 . . . . 86 VAL N . 17700 1 477 . 1 1 87 87 ALA C C 13 177.2 . . 1 . . . . 87 ALA C . 17700 1 478 . 1 1 87 87 ALA CA C 13 51.70 . . 1 . . . . 87 ALA CA . 17700 1 479 . 1 1 87 87 ALA CB C 13 19.60 . . 1 . . . . 87 ALA CB . 17700 1 480 . 1 1 87 87 ALA N N 15 133.3 . . 1 . . . . 87 ALA N . 17700 1 481 . 1 1 88 88 ALA C C 13 174.5 . . 1 . . . . 88 ALA C . 17700 1 482 . 1 1 88 88 ALA CA C 13 51.50 . . 1 . . . . 88 ALA CA . 17700 1 483 . 1 1 88 88 ALA CB C 13 21.60 . . 1 . . . . 88 ALA CB . 17700 1 484 . 1 1 88 88 ALA N N 15 118.4 . . 1 . . . . 88 ALA N . 17700 1 485 . 1 1 89 89 THR C C 13 171.3 . . 1 . . . . 89 THR C . 17700 1 486 . 1 1 89 89 THR CA C 13 63.20 . . 1 . . . . 89 THR CA . 17700 1 487 . 1 1 89 89 THR CB C 13 71.40 . . 1 . . . . 89 THR CB . 17700 1 488 . 1 1 89 89 THR CG2 C 13 21.90 . . 1 . . . . 89 THR CG2 . 17700 1 489 . 1 1 89 89 THR N N 15 116.4 . . 1 . . . . 89 THR N . 17700 1 490 . 1 1 90 90 LYS C C 13 173.3 . . 1 . . . . 90 LYS C . 17700 1 491 . 1 1 90 90 LYS CA C 13 53.20 . . 1 . . . . 90 LYS CA . 17700 1 492 . 1 1 90 90 LYS CB C 13 32.10 . . 1 . . . . 90 LYS CB . 17700 1 493 . 1 1 90 90 LYS CG C 13 22.30 . . 1 . . . . 90 LYS CG . 17700 1 494 . 1 1 90 90 LYS CD C 13 26.00 . . 1 . . . . 90 LYS CD . 17700 1 495 . 1 1 90 90 LYS CE C 13 39.50 . . 1 . . . . 90 LYS CE . 17700 1 496 . 1 1 90 90 LYS N N 15 126.7 . . 1 . . . . 90 LYS N . 17700 1 497 . 1 1 91 91 VAL C C 13 173.8 . . 1 . . . . 91 VAL C . 17700 1 498 . 1 1 91 91 VAL CA C 13 60.80 . . 1 . . . . 91 VAL CA . 17700 1 499 . 1 1 91 91 VAL CB C 13 33.20 . . 1 . . . . 91 VAL CB . 17700 1 500 . 1 1 91 91 VAL CG1 C 13 22.20 . . . . . . . 91 VAL CG1 . 17700 1 501 . 1 1 91 91 VAL CG2 C 13 22.10 . . . . . . . 91 VAL CG2 . 17700 1 502 . 1 1 91 91 VAL N N 15 126.4 . . 1 . . . . 91 VAL N . 17700 1 503 . 1 1 92 92 GLY C C 13 170.1 . . 1 . . . . 92 GLY C . 17700 1 504 . 1 1 92 92 GLY CA C 13 40.20 . . 1 . . . . 92 GLY CA . 17700 1 505 . 1 1 92 92 GLY N N 15 113.9 . . 1 . . . . 92 GLY N . 17700 1 506 . 1 1 93 93 ALA C C 13 176.9 . . 1 . . . . 93 ALA C . 17700 1 507 . 1 1 93 93 ALA CA C 13 50.70 . . 1 . . . . 93 ALA CA . 17700 1 508 . 1 1 93 93 ALA CB C 13 19.70 . . 1 . . . . 93 ALA CB . 17700 1 509 . 1 1 93 93 ALA N N 15 118.8 . . 1 . . . . 93 ALA N . 17700 1 510 . 1 1 94 94 LEU C C 13 174.6 . . 1 . . . . 94 LEU C . 17700 1 511 . 1 1 94 94 LEU CA C 13 52.00 . . 1 . . . . 94 LEU CA . 17700 1 512 . 1 1 94 94 LEU CB C 13 42.60 . . 1 . . . . 94 LEU CB . 17700 1 513 . 1 1 94 94 LEU CG C 13 25.80 . . 1 . . . . 94 LEU CG . 17700 1 514 . 1 1 94 94 LEU CD1 C 13 25.80 . . . . . . . 94 LEU CD1 . 17700 1 515 . 1 1 94 94 LEU CD2 C 13 21.50 . . . . . . . 94 LEU CD2 . 17700 1 516 . 1 1 94 94 LEU N N 15 119.8 . . 1 . . . . 94 LEU N . 17700 1 517 . 1 1 95 95 SER C C 13 174.6 . . 1 . . . . 95 SER C . 17700 1 518 . 1 1 95 95 SER CA C 13 55.30 . . 1 . . . . 95 SER CA . 17700 1 519 . 1 1 95 95 SER CB C 13 65.50 . . 1 . . . . 95 SER CB . 17700 1 520 . 1 1 95 95 SER N N 15 118.5 . . 1 . . . . 95 SER N . 17700 1 521 . 1 1 96 96 LYS C C 13 177.7 . . 1 . . . . 96 LYS C . 17700 1 522 . 1 1 96 96 LYS CA C 13 60.00 . . 1 . . . . 96 LYS CA . 17700 1 523 . 1 1 96 96 LYS CB C 13 31.20 . . 1 . . . . 96 LYS CB . 17700 1 524 . 1 1 96 96 LYS CG C 13 24.60 . . 1 . . . . 96 LYS CG . 17700 1 525 . 1 1 96 96 LYS CD C 13 28.30 . . 1 . . . . 96 LYS CD . 17700 1 526 . 1 1 96 96 LYS CE C 13 40.40 . . 1 . . . . 96 LYS CE . 17700 1 527 . 1 1 96 96 LYS N N 15 120.6 . . 1 . . . . 96 LYS N . 17700 1 528 . 1 1 97 97 GLY C C 13 176.8 . . 1 . . . . 97 GLY C . 17700 1 529 . 1 1 97 97 GLY CA C 13 46.30 . . 1 . . . . 97 GLY CA . 17700 1 530 . 1 1 97 97 GLY N N 15 105.4 . . 1 . . . . 97 GLY N . 17700 1 531 . 1 1 98 98 GLN C C 13 178.0 . . 1 . . . . 98 GLN C . 17700 1 532 . 1 1 98 98 GLN CA C 13 58.10 . . 1 . . . . 98 GLN CA . 17700 1 533 . 1 1 98 98 GLN CB C 13 27.70 . . 1 . . . . 98 GLN CB . 17700 1 534 . 1 1 98 98 GLN CG C 13 31.20 . . 1 . . . . 98 GLN CG . 17700 1 535 . 1 1 98 98 GLN CD C 13 179.2 . . 1 . . . . 98 GLN CD . 17700 1 536 . 1 1 98 98 GLN N N 15 120.3 . . 1 . . . . 98 GLN N . 17700 1 537 . 1 1 99 99 LEU C C 13 176.0 . . 1 . . . . 99 LEU C . 17700 1 538 . 1 1 99 99 LEU CA C 13 57.20 . . 1 . . . . 99 LEU CA . 17700 1 539 . 1 1 99 99 LEU CB C 13 40.30 . . 1 . . . . 99 LEU CB . 17700 1 540 . 1 1 99 99 LEU CG C 13 26.40 . . 1 . . . . 99 LEU CG . 17700 1 541 . 1 1 99 99 LEU CD1 C 13 25.70 . . . . . . . 99 LEU CD1 . 17700 1 542 . 1 1 99 99 LEU CD2 C 13 21.90 . . . . . . . 99 LEU CD2 . 17700 1 543 . 1 1 99 99 LEU N N 15 123.2 . . 1 . . . . 99 LEU N . 17700 1 544 . 1 1 100 100 LYS C C 13 177.1 . . 1 . . . . 100 LYS C . 17700 1 545 . 1 1 100 100 LYS CA C 13 59.90 . . 1 . . . . 100 LYS CA . 17700 1 546 . 1 1 100 100 LYS CB C 13 30.70 . . 1 . . . . 100 LYS CB . 17700 1 547 . 1 1 100 100 LYS CD C 13 25.70 . . 1 . . . . 100 LYS CD . 17700 1 548 . 1 1 100 100 LYS CE C 13 41.70 . . 1 . . . . 100 LYS CE . 17700 1 549 . 1 1 100 100 LYS N N 15 119.0 . . 1 . . . . 100 LYS N . 17700 1 550 . 1 1 101 101 GLU C C 13 179.3 . . 1 . . . . 101 GLU C . 17700 1 551 . 1 1 101 101 GLU CA C 13 58.00 . . 1 . . . . 101 GLU CA . 17700 1 552 . 1 1 101 101 GLU CB C 13 28.60 . . 1 . . . . 101 GLU CB . 17700 1 553 . 1 1 101 101 GLU CG C 13 33.80 . . 1 . . . . 101 GLU CG . 17700 1 554 . 1 1 101 101 GLU CD C 13 182.1 . . 1 . . . . 101 GLU CD . 17700 1 555 . 1 1 101 101 GLU N N 15 117.1 . . 1 . . . . 101 GLU N . 17700 1 556 . 1 1 102 102 PHE C C 13 176.5 . . 1 . . . . 102 PHE C . 17700 1 557 . 1 1 102 102 PHE CA C 13 59.30 . . 1 . . . . 102 PHE CA . 17700 1 558 . 1 1 102 102 PHE CB C 13 38.20 . . 1 . . . . 102 PHE CB . 17700 1 559 . 1 1 102 102 PHE CG C 13 137.7 . . 1 . . . . 102 PHE CG . 17700 1 560 . 1 1 102 102 PHE CD1 C 13 131.7 . . . . . . . 102 PHE CD1 . 17700 1 561 . 1 1 102 102 PHE N N 15 120.3 . . 1 . . . . 102 PHE N . 17700 1 562 . 1 1 103 103 LEU C C 13 176.6 . . 1 . . . . 103 LEU C . 17700 1 563 . 1 1 103 103 LEU CA C 13 55.80 . . 1 . . . . 103 LEU CA . 17700 1 564 . 1 1 103 103 LEU CB C 13 39.80 . . 1 . . . . 103 LEU CB . 17700 1 565 . 1 1 103 103 LEU CG C 13 22.40 . . 1 . . . . 103 LEU CG . 17700 1 566 . 1 1 103 103 LEU CD1 C 13 22.30 . . . . . . . 103 LEU CD1 . 17700 1 567 . 1 1 103 103 LEU CD2 C 13 18.40 . . . . . . . 103 LEU CD2 . 17700 1 568 . 1 1 103 103 LEU N N 15 121.1 . . 1 . . . . 103 LEU N . 17700 1 569 . 1 1 104 104 ASP C C 13 176.4 . . 1 . . . . 104 ASP C . 17700 1 570 . 1 1 104 104 ASP CA C 13 55.60 . . 1 . . . . 104 ASP CA . 17700 1 571 . 1 1 104 104 ASP CB C 13 39.40 . . 1 . . . . 104 ASP CB . 17700 1 572 . 1 1 104 104 ASP CG C 13 180.8 . . 1 . . . . 104 ASP CG . 17700 1 573 . 1 1 104 104 ASP N N 15 119.9 . . 1 . . . . 104 ASP N . 17700 1 574 . 1 1 105 105 ALA C C 13 177.7 . . 1 . . . . 105 ALA C . 17700 1 575 . 1 1 105 105 ALA CA C 13 53.10 . . 1 . . . . 105 ALA CA . 17700 1 576 . 1 1 105 105 ALA CB C 13 18.30 . . 1 . . . . 105 ALA CB . 17700 1 577 . 1 1 105 105 ALA N N 15 117.6 . . 1 . . . . 105 ALA N . 17700 1 578 . 1 1 106 106 ASN C C 13 175.4 . . 1 . . . . 106 ASN C . 17700 1 579 . 1 1 106 106 ASN CA C 13 53.80 . . 1 . . . . 106 ASN CA . 17700 1 580 . 1 1 106 106 ASN CB C 13 41.70 . . 1 . . . . 106 ASN CB . 17700 1 581 . 1 1 106 106 ASN CG C 13 176.0 . . 1 . . . . 106 ASN CG . 17700 1 582 . 1 1 106 106 ASN N N 15 112.2 . . 1 . . . . 106 ASN N . 17700 1 583 . 1 1 107 107 LEU C C 13 173.7 . . 1 . . . . 107 LEU C . 17700 1 584 . 1 1 107 107 LEU CA C 13 52.20 . . 1 . . . . 107 LEU CA . 17700 1 585 . 1 1 107 107 LEU CB C 13 44.60 . . 1 . . . . 107 LEU CB . 17700 1 586 . 1 1 107 107 LEU CG C 13 23.60 . . 1 . . . . 107 LEU CG . 17700 1 587 . 1 1 107 107 LEU CD1 C 13 23.60 . . . . . . . 107 LEU CD1 . 17700 1 588 . 1 1 107 107 LEU CD2 C 13 26.00 . . . . . . . 107 LEU CD2 . 17700 1 589 . 1 1 107 107 LEU N N 15 121.1 . . 1 . . . . 107 LEU N . 17700 1 590 . 1 1 108 108 ALA C C 13 178.4 . . 1 . . . . 108 ALA C . 17700 1 591 . 1 1 108 108 ALA CA C 13 53.50 . . 1 . . . . 108 ALA CA . 17700 1 592 . 1 1 108 108 ALA CB C 13 18.90 . . 1 . . . . 108 ALA CB . 17700 1 593 . 1 1 108 108 ALA N N 15 127.7 . . 1 . . . . 108 ALA N . 17700 1 stop_ save_