data_62 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 62 _Entry.Title ; NMR Sequential Assignment of Escherichia coli Thioredoxin Utilizing Random Fractional Deuteriation ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-03-25 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 David LeMaster . M. . 62 2 Frederic Richards . M. . 62 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 62 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 357 62 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 4 . . 2010-06-10 . revision BMRB 'Complete natural source information' 62 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 62 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 62 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 62 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 62 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; LeMaster, David M., Richards, Frederic M., "NMR Sequential Assignment of Escherichia coli Thioredoxin Utilizing Random Fractional Deuteriation," Biochemistry 27, 142-150 (1988). ; _Citation.Title ; NMR Sequential Assignment of Escherichia coli Thioredoxin Utilizing Random Fractional Deuteriation ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 27 _Citation.Journal_issue . _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 142 _Citation.Page_last 150 _Citation.Year 1988 _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 David LeMaster . M. . 62 1 2 Frederic Richards . M. . 62 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_thioredoxin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_thioredoxin _Assembly.Entry_ID 62 _Assembly.ID 1 _Assembly.Name thioredoxin _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 thioredoxin 1 $thioredoxin . . . . . . . . . 62 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID thioredoxin system 62 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_thioredoxin _Entity.Sf_category entity _Entity.Sf_framecode thioredoxin _Entity.Entry_ID 62 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name thioredoxin _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can ; SDKIIHLTDDSFDTDVLKAD GAILVDFWAEWCGPCKMIAP ILDEIADEYQGKLTVAKLNI DQNPGTAPKYGIRGIPTLLL FKNGEVAATKVGAKSKGQLK EFLDANLA ; _Entity.Polymer_seq_one_letter_code ; SDKIIHLTDDSFDTDVLKAD GAILVDFWAEWCGPCKMIAP ILDEIADEYQGKLTVAKLNI DQNPGTAPKYGIRGIPTLLL FKNGEVAATKVGAKSKGQLK EFLDANLA ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 108 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 99.07 99.07 6.38e-70 . . . . 62 1 2 no BMRB 1812 . thioredoxin . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 3 no BMRB 1813 . thioredoxin . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 4 no BMRB 5715 . HHP-Trx . . . . . 100.00 111 99.07 99.07 8.72e-70 . . . . 62 1 5 no PDB 1F6M . "Crystal Structure Of A Complex Between Thioredoxin Reductase, Thioredoxin, And The Nadp+ Analog, Aadp+" . . . . . 100.00 108 98.15 98.15 8.47e-69 . . . . 62 1 6 no PDB 1KEB . "Crystal Structure Of Double Mutant M37l,P40s E.Coli Thioredoxin" . . . . . 100.00 108 97.22 98.15 2.41e-68 . . . . 62 1 7 no PDB 1SKR . "T7 Dna Polymerase Complexed To Dna Primer/template And Ddatp" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 8 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 99.07 99.07 6.38e-70 . . . . 62 1 9 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 99.07 99.07 6.38e-70 . . . . 62 1 10 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 99.07 99.07 6.38e-70 . . . . 62 1 11 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 99.07 99.07 6.38e-70 . . . . 62 1 12 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 99.07 99.07 6.38e-70 . . . . 62 1 13 no PDB 1T7P . "T7 Dna Polymerase Complexed To Dna PrimerTEMPLATE,A Nucleoside Triphosphate, And Its Processivity Factor Thioredoxin" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 14 no PDB 1T8E . "T7 Dna Polymerase Ternary Complex With Dctp At The Insertion Site." . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 15 no PDB 1THO . "Crystal Structure Of A Mutant Escherichia Coli Thioredoxin With An Arginine Insertion In The Active Site" . . . . . 100.93 109 98.17 98.17 3.45e-68 . . . . 62 1 16 no PDB 1TK0 . "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Ddctp At The Insertion Site" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 17 no PDB 1TK5 . "T7 Dna Polymerase Binary Complex With 8 Oxo Guanosine In The Templating Strand" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 18 no PDB 1TK8 . "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Damp At The Elongation Site" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 19 no PDB 1TKD . "T7 Dna Polymerase Ternary Complex With 8 Oxo Guanosine And Dcmp At The Elongation Site" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 20 no PDB 1TXX . "Active-Site Variant Of E.Coli Thioredoxin" . . . . . 100.00 108 97.22 97.22 4.64e-67 . . . . 62 1 21 no PDB 1X9M . "T7 Dna Polymerase In Complex With An N-2- Acetylaminofluorene-adducted Dna" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 22 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 99.07 99.07 6.38e-70 . . . . 62 1 23 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 99.07 99.07 6.38e-70 . . . . 62 1 24 no PDB 1XOA . "Thioredoxin (Oxidized Disulfide Form), Nmr, 20 Structures" . . . . . 99.07 108 99.07 99.07 4.08e-69 . . . . 62 1 25 no PDB 1XOB . "Thioredoxin (Reduced Dithio Form), Nmr, 20 Structures" . . . . . 99.07 108 99.07 99.07 4.08e-69 . . . . 62 1 26 no PDB 1ZYQ . "T7 Dna Polymerase In Complex With 8og And Incoming Ddatp" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 27 no PDB 1ZZY . "Crystal Structure Of Thioredoxin Mutant L7v" . . . . . 100.00 108 98.15 99.07 1.68e-69 . . . . 62 1 28 no PDB 2AJQ . "Structure Of Replicative Dna Polymerase Provides Insigts Into The Mechanisms For Processivity, Frameshifting And Editing" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 29 no PDB 2BTO . "Structure Of Btuba From Prosthecobacter Dejongeii" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 30 no PDB 2EIO . "Design Of Disulfide-Linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" . . . . . 100.00 108 98.15 98.15 1.49e-68 . . . . 62 1 31 no PDB 2EIQ . "Design Of Disulfide-linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" . . . . . 100.00 108 98.15 98.15 5.30e-69 . . . . 62 1 32 no PDB 2EIR . "Design Of Disulfide-Linked Thioredoxin Dimers And Multimers Through Analysis Of Crystal Contacts" . . . . . 100.00 108 97.22 97.22 6.03e-68 . . . . 62 1 33 no PDB 2FCH . "Crystal Structure Of Thioredoxin Mutant G74s" . . . . . 100.00 108 98.15 98.15 2.97e-69 . . . . 62 1 34 no PDB 2FD3 . "Crystal Structure Of Thioredoxin Mutant P34h" . . . . . 100.00 108 98.15 98.15 7.59e-69 . . . . 62 1 35 no PDB 2H6X . "Crystal Structure Of Thioredoxin Wild Type In Hexagonal (P61) Space Group" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 36 no PDB 2H6Y . "Crystal Structure Of Thioredoxin Mutant E48d In Hexagonal (P61) Space Group" . . . . . 100.00 108 98.15 99.07 3.35e-69 . . . . 62 1 37 no PDB 2H6Z . "Crystal Structure Of Thioredoxin Mutant E44d In Hexagonal (P61) Space Group" . . . . . 100.00 108 98.15 99.07 3.35e-69 . . . . 62 1 38 no PDB 2H70 . "Crystal Structure Of Thioredoxin Mutant D9e In Hexagonal (P61) Space Group" . . . . . 100.00 108 98.15 99.07 2.14e-69 . . . . 62 1 39 no PDB 2H71 . "Crystal Structure Of Thioredoxin Mutant D47e In Hexagonal (P61) Space Group" . . . . . 100.00 108 98.15 99.07 2.14e-69 . . . . 62 1 40 no PDB 2H72 . "Crystal Structure Of Thioredoxin Mutant E85d In Hexagonal (P61) Space Group" . . . . . 100.00 108 98.15 99.07 3.35e-69 . . . . 62 1 41 no PDB 2H73 . "Crystal Structure Of Thioredoxin Mutant D43e In Hexagonal (P61) Space Group" . . . . . 100.00 108 98.15 99.07 2.14e-69 . . . . 62 1 42 no PDB 2H74 . "Crystal Structure Of Thioredoxin Mutant D2e In Hexagonal (P61) Space Group" . . . . . 100.00 108 98.15 99.07 2.14e-69 . . . . 62 1 43 no PDB 2H75 . "Crystal Structure Of Thioredoxin Mutant D13e In Hexagonal (P61) Space Group" . . . . . 100.00 108 98.15 99.07 2.14e-69 . . . . 62 1 44 no PDB 2H76 . "Crystal Structure Of Thioredoxin Mutant D10e In Hexagonal (P61) Space Group" . . . . . 100.00 108 98.15 99.07 2.14e-69 . . . . 62 1 45 no PDB 2O8V . "Paps Reductase In A Covalent Complex With Thioredoxin C35a" . . . . . 100.00 128 98.15 98.15 2.51e-69 . . . . 62 1 46 no PDB 2TIR . "Crystal Structure Analysis Of A Mutant Escherichia Coli Thioredoxin In Which Lysine 36 Is Replaced By Glutamic Acid" . . . . . 100.00 108 98.15 99.07 2.26e-69 . . . . 62 1 47 no PDB 2TRX . "Crystal Structure Of Thioredoxin From Escherichia Coli At 1.68 Angstroms Resolution" . . . . . 100.00 108 99.07 99.07 6.38e-70 . . . . 62 1 48 no PDB 3DXB . "Structure Of The Uhm Domain Of Puf60 Fused To Thioredoxin" . . . . . 100.00 222 99.07 99.07 8.87e-70 . . . . 62 1 49 no PDB 3DYR . "Crystal Structure Of E. Coli Thioredoxin Mutant I76t In Its Oxidized Form" . . . . . 100.00 111 98.15 98.15 2.43e-69 . . . . 62 1 50 no PDB 4KCA . "Crystal Structure Of Endo-1,5-alpha-l-arabinanase From A Bovine Ruminal Metagenomic Library" . . . . . 100.00 692 99.07 99.07 5.47e-65 . . . . 62 1 51 no PDB 4KCB . "Crystal Structure Of Exo-1,5-alpha-l-arabinanase From Bovine Ruminal Metagenomic Library" . . . . . 100.00 447 99.07 99.07 7.16e-68 . . . . 62 1 52 no DBJ BAA00903 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 53 no DBJ BAB38137 . "thioredoxin 1 [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 127 99.07 99.07 2.44e-70 . . . . 62 1 54 no DBJ BAE77517 . "thioredoxin 1 [Escherichia coli str. K-12 substr. W3110]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 55 no DBJ BAG79587 . "thioredoxin [Escherichia coli SE11]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 56 no DBJ BAI27964 . "thioredoxin 1 [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 57 no EMBL CAA79851 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 58 no EMBL CAD09400 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 59 no EMBL CAP78228 . "Thioredoxin 1 [Escherichia coli LF82]" . . . . . 100.00 144 99.07 99.07 2.43e-70 . . . . 62 1 60 no EMBL CAQ34125 . "thioredoxin 1 [Escherichia coli BL21(DE3)]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 61 no EMBL CAQ91183 . "thioredoxin 1 [Escherichia fergusonii ATCC 35469]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 62 no GB AAA24533 . "thioredoxin (trxA) [Escherichia coli]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 63 no GB AAA24534 . "thioredoxin [Escherichia coli]" . . . . . 100.00 127 99.07 99.07 2.44e-70 . . . . 62 1 64 no GB AAA24693 . "thioredoxin [Escherichia coli]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 65 no GB AAA24694 . "thioredoxin (trxA) [Escherichia coli]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 66 no GB AAA24696 . "thioredoxin [Escherichia coli]" . . . . . 100.93 110 98.17 98.17 2.46e-68 . . . . 62 1 67 no PIR AF0922 . "thioredoxin [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 68 no PIR B91218 . "thioredoxin 1 [imported] - Escherichia coli (strain O157:H7, substrain RIMD 0509952)" . . . . . 100.00 127 99.07 99.07 2.44e-70 . . . . 62 1 69 no PIR C86064 . "thioredoxin 1 [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" . . . . . 100.00 127 99.07 99.07 2.44e-70 . . . . 62 1 70 no REF NP_290411 . "thioredoxin [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 127 99.07 99.07 2.44e-70 . . . . 62 1 71 no REF NP_312741 . "thioredoxin [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 127 99.07 99.07 2.44e-70 . . . . 62 1 72 no REF NP_418228 . "thioredoxin 1 [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 73 no REF NP_457831 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 74 no REF NP_462806 . "thioredoxin [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 75 no SP P0AA25 . "RecName: Full=Thioredoxin-1; Short=Trx-1 [Escherichia coli K-12]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 76 no SP P0AA26 . "RecName: Full=Thioredoxin-1; Short=Trx-1 [Escherichia coli CFT073]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 77 no SP P0AA27 . "RecName: Full=Thioredoxin-1; Short=Trx-1 [Escherichia coli O157:H7]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 78 no SP P0AA28 . "RecName: Full=Thioredoxin-1; Short=Trx-1 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 79 no SP P0AA29 . "RecName: Full=Thioredoxin-1; Short=Trx-1 [Salmonella enterica subsp. enterica serovar Typhi]" . . . . . 100.00 109 99.07 99.07 4.85e-70 . . . . 62 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID thioredoxin common 62 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 . 62 1 2 . ASP . 62 1 3 . LYS . 62 1 4 . ILE . 62 1 5 . ILE . 62 1 6 . HIS . 62 1 7 . LEU . 62 1 8 . THR . 62 1 9 . ASP . 62 1 10 . ASP . 62 1 11 . SER . 62 1 12 . PHE . 62 1 13 . ASP . 62 1 14 . THR . 62 1 15 . ASP . 62 1 16 . VAL . 62 1 17 . LEU . 62 1 18 . LYS . 62 1 19 . ALA . 62 1 20 . ASP . 62 1 21 . GLY . 62 1 22 . ALA . 62 1 23 . ILE . 62 1 24 . LEU . 62 1 25 . VAL . 62 1 26 . ASP . 62 1 27 . PHE . 62 1 28 . TRP . 62 1 29 . ALA . 62 1 30 . GLU . 62 1 31 . TRP . 62 1 32 . CYS . 62 1 33 . GLY . 62 1 34 . PRO . 62 1 35 . CYS . 62 1 36 . LYS . 62 1 37 . MET . 62 1 38 . ILE . 62 1 39 . ALA . 62 1 40 . PRO . 62 1 41 . ILE . 62 1 42 . LEU . 62 1 43 . ASP . 62 1 44 . GLU . 62 1 45 . ILE . 62 1 46 . ALA . 62 1 47 . ASP . 62 1 48 . GLU . 62 1 49 . TYR . 62 1 50 . GLN . 62 1 51 . GLY . 62 1 52 . LYS . 62 1 53 . LEU . 62 1 54 . THR . 62 1 55 . VAL . 62 1 56 . ALA . 62 1 57 . LYS . 62 1 58 . LEU . 62 1 59 . ASN . 62 1 60 . ILE . 62 1 61 . ASP . 62 1 62 . GLN . 62 1 63 . ASN . 62 1 64 . PRO . 62 1 65 . GLY . 62 1 66 . THR . 62 1 67 . ALA . 62 1 68 . PRO . 62 1 69 . LYS . 62 1 70 . TYR . 62 1 71 . GLY . 62 1 72 . ILE . 62 1 73 . ARG . 62 1 74 . GLY . 62 1 75 . ILE . 62 1 76 . PRO . 62 1 77 . THR . 62 1 78 . LEU . 62 1 79 . LEU . 62 1 80 . LEU . 62 1 81 . PHE . 62 1 82 . LYS . 62 1 83 . ASN . 62 1 84 . GLY . 62 1 85 . GLU . 62 1 86 . VAL . 62 1 87 . ALA . 62 1 88 . ALA . 62 1 89 . THR . 62 1 90 . LYS . 62 1 91 . VAL . 62 1 92 . GLY . 62 1 93 . ALA . 62 1 94 . LYS . 62 1 95 . SER . 62 1 96 . LYS . 62 1 97 . GLY . 62 1 98 . GLN . 62 1 99 . LEU . 62 1 100 . LYS . 62 1 101 . GLU . 62 1 102 . PHE . 62 1 103 . LEU . 62 1 104 . ASP . 62 1 105 . ALA . 62 1 106 . ASN . 62 1 107 . LEU . 62 1 108 . ALA . 62 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 62 1 . ASP 2 2 62 1 . LYS 3 3 62 1 . ILE 4 4 62 1 . ILE 5 5 62 1 . HIS 6 6 62 1 . LEU 7 7 62 1 . THR 8 8 62 1 . ASP 9 9 62 1 . ASP 10 10 62 1 . SER 11 11 62 1 . PHE 12 12 62 1 . ASP 13 13 62 1 . THR 14 14 62 1 . ASP 15 15 62 1 . VAL 16 16 62 1 . LEU 17 17 62 1 . LYS 18 18 62 1 . ALA 19 19 62 1 . ASP 20 20 62 1 . GLY 21 21 62 1 . ALA 22 22 62 1 . ILE 23 23 62 1 . LEU 24 24 62 1 . VAL 25 25 62 1 . ASP 26 26 62 1 . PHE 27 27 62 1 . TRP 28 28 62 1 . ALA 29 29 62 1 . GLU 30 30 62 1 . TRP 31 31 62 1 . CYS 32 32 62 1 . GLY 33 33 62 1 . PRO 34 34 62 1 . CYS 35 35 62 1 . LYS 36 36 62 1 . MET 37 37 62 1 . ILE 38 38 62 1 . ALA 39 39 62 1 . PRO 40 40 62 1 . ILE 41 41 62 1 . LEU 42 42 62 1 . ASP 43 43 62 1 . GLU 44 44 62 1 . ILE 45 45 62 1 . ALA 46 46 62 1 . ASP 47 47 62 1 . GLU 48 48 62 1 . TYR 49 49 62 1 . GLN 50 50 62 1 . GLY 51 51 62 1 . LYS 52 52 62 1 . LEU 53 53 62 1 . THR 54 54 62 1 . VAL 55 55 62 1 . ALA 56 56 62 1 . LYS 57 57 62 1 . LEU 58 58 62 1 . ASN 59 59 62 1 . ILE 60 60 62 1 . ASP 61 61 62 1 . GLN 62 62 62 1 . ASN 63 63 62 1 . PRO 64 64 62 1 . GLY 65 65 62 1 . THR 66 66 62 1 . ALA 67 67 62 1 . PRO 68 68 62 1 . LYS 69 69 62 1 . TYR 70 70 62 1 . GLY 71 71 62 1 . ILE 72 72 62 1 . ARG 73 73 62 1 . GLY 74 74 62 1 . ILE 75 75 62 1 . PRO 76 76 62 1 . THR 77 77 62 1 . LEU 78 78 62 1 . LEU 79 79 62 1 . LEU 80 80 62 1 . PHE 81 81 62 1 . LYS 82 82 62 1 . ASN 83 83 62 1 . GLY 84 84 62 1 . GLU 85 85 62 1 . VAL 86 86 62 1 . ALA 87 87 62 1 . ALA 88 88 62 1 . THR 89 89 62 1 . LYS 90 90 62 1 . VAL 91 91 62 1 . GLY 92 92 62 1 . ALA 93 93 62 1 . LYS 94 94 62 1 . SER 95 95 62 1 . LYS 96 96 62 1 . GLY 97 97 62 1 . GLN 98 98 62 1 . LEU 99 99 62 1 . LYS 100 100 62 1 . GLU 101 101 62 1 . PHE 102 102 62 1 . LEU 103 103 62 1 . ASP 104 104 62 1 . ALA 105 105 62 1 . ASN 106 106 62 1 . LEU 107 107 62 1 . ALA 108 108 62 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 62 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $thioredoxin . 562 organism . 'Escherichia coli' 'E. coli' . . Eubacteria . Escherichia coli K12 . . . . . . . . . . . . . . . . . . . . 62 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 62 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $thioredoxin . 'not available' 'Escherichia coli' . . . Escherichia coli MG1655 . . . . . . . . . . . . . . . . . . . . . . 62 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 62 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 62 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 5.7 . na 62 1 temperature 303 . K 62 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 62 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 62 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 62 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 62 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 62 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 62 _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 H . p-dioxane . . . . . ppm 3.74 . . . . . . 1 $entry_citation . . 1 $entry_citation 62 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 62 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 62 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 3 3 LYS H H 1 8.41 . . 1 . . . . . . . . 62 1 2 . 1 1 3 3 LYS HA H 1 4.32 . . 1 . . . . . . . . 62 1 3 . 1 1 3 3 LYS HB2 H 1 1.92 . . 2 . . . . . . . . 62 1 4 . 1 1 3 3 LYS HB3 H 1 1.68 . . 2 . . . . . . . . 62 1 5 . 1 1 4 4 ILE H H 1 7.55 . . 1 . . . . . . . . 62 1 6 . 1 1 4 4 ILE HA H 1 4.38 . . 1 . . . . . . . . 62 1 7 . 1 1 4 4 ILE HB H 1 1.74 . . 1 . . . . . . . . 62 1 8 . 1 1 5 5 ILE H H 1 8.46 . . 1 . . . . . . . . 62 1 9 . 1 1 5 5 ILE HA H 1 4.23 . . 1 . . . . . . . . 62 1 10 . 1 1 5 5 ILE HB H 1 1.74 . . 1 . . . . . . . . 62 1 11 . 1 1 6 6 HIS H H 1 8.99 . . 1 . . . . . . . . 62 1 12 . 1 1 6 6 HIS HA H 1 4.93 . . 1 . . . . . . . . 62 1 13 . 1 1 6 6 HIS HB2 H 1 3.21 . . 2 . . . . . . . . 62 1 14 . 1 1 6 6 HIS HB3 H 1 3.16 . . 2 . . . . . . . . 62 1 15 . 1 1 7 7 LEU H H 1 8.7 . . 1 . . . . . . . . 62 1 16 . 1 1 7 7 LEU HA H 1 4.43 . . 1 . . . . . . . . 62 1 17 . 1 1 7 7 LEU HB2 H 1 1.81 . . 1 . . . . . . . . 62 1 18 . 1 1 7 7 LEU HB3 H 1 1.81 . . 1 . . . . . . . . 62 1 19 . 1 1 8 8 THR H H 1 8.12 . . 1 . . . . . . . . 62 1 20 . 1 1 8 8 THR HA H 1 4.82 . . 1 . . . . . . . . 62 1 21 . 1 1 8 8 THR HB H 1 4.52 . . 1 . . . . . . . . 62 1 22 . 1 1 9 9 ASP H H 1 8.26 . . 1 . . . . . . . . 62 1 23 . 1 1 9 9 ASP HA H 1 4.74 . . 1 . . . . . . . . 62 1 24 . 1 1 9 9 ASP HB2 H 1 2.75 . . 2 . . . . . . . . 62 1 25 . 1 1 9 9 ASP HB3 H 1 2.8 . . 2 . . . . . . . . 62 1 26 . 1 1 10 10 ASP H H 1 8.26 . . 1 . . . . . . . . 62 1 27 . 1 1 10 10 ASP HA H 1 4.59 . . 1 . . . . . . . . 62 1 28 . 1 1 10 10 ASP HB2 H 1 2.65 . . 2 . . . . . . . . 62 1 29 . 1 1 10 10 ASP HB3 H 1 2.71 . . 2 . . . . . . . . 62 1 30 . 1 1 11 11 SER H H 1 8.26 . . 1 . . . . . . . . 62 1 31 . 1 1 11 11 SER HA H 1 4.63 . . 1 . . . . . . . . 62 1 32 . 1 1 11 11 SER HB2 H 1 4.36 . . 1 . . . . . . . . 62 1 33 . 1 1 11 11 SER HB3 H 1 4.36 . . 1 . . . . . . . . 62 1 34 . 1 1 12 12 PHE H H 1 7.73 . . 1 . . . . . . . . 62 1 35 . 1 1 12 12 PHE HA H 1 3.69 . . 1 . . . . . . . . 62 1 36 . 1 1 12 12 PHE HB2 H 1 3.2 . . 2 . . . . . . . . 62 1 37 . 1 1 12 12 PHE HB3 H 1 3.33 . . 2 . . . . . . . . 62 1 38 . 1 1 13 13 ASP H H 1 8.76 . . 1 . . . . . . . . 62 1 39 . 1 1 13 13 ASP HA H 1 4.27 . . 1 . . . . . . . . 62 1 40 . 1 1 13 13 ASP HB2 H 1 2.74 . . 2 . . . . . . . . 62 1 41 . 1 1 13 13 ASP HB3 H 1 2.82 . . 2 . . . . . . . . 62 1 42 . 1 1 14 14 THR H H 1 7.82 . . 1 . . . . . . . . 62 1 43 . 1 1 14 14 THR HA H 1 3.8 . . 1 . . . . . . . . 62 1 44 . 1 1 14 14 THR HB H 1 4.08 . . 1 . . . . . . . . 62 1 45 . 1 1 15 15 ASP H H 1 8.46 . . 1 . . . . . . . . 62 1 46 . 1 1 15 15 ASP HA H 1 4.27 . . 1 . . . . . . . . 62 1 47 . 1 1 15 15 ASP HB2 H 1 2.27 . . 1 . . . . . . . . 62 1 48 . 1 1 15 15 ASP HB3 H 1 2.27 . . 1 . . . . . . . . 62 1 49 . 1 1 16 16 VAL H H 1 7.61 . . 1 . . . . . . . . 62 1 50 . 1 1 16 16 VAL HA H 1 3.79 . . 1 . . . . . . . . 62 1 51 . 1 1 16 16 VAL HB H 1 .7 . . 1 . . . . . . . . 62 1 52 . 1 1 17 17 LEU H H 1 7.02 . . 1 . . . . . . . . 62 1 53 . 1 1 17 17 LEU HA H 1 3.89 . . 1 . . . . . . . . 62 1 54 . 1 1 17 17 LEU HB2 H 1 1.58 . . 1 . . . . . . . . 62 1 55 . 1 1 17 17 LEU HB3 H 1 1.58 . . 1 . . . . . . . . 62 1 56 . 1 1 18 18 LYS H H 1 7.44 . . 1 . . . . . . . . 62 1 57 . 1 1 18 18 LYS HA H 1 4.4 . . 1 . . . . . . . . 62 1 58 . 1 1 18 18 LYS HB2 H 1 1.82 . . 1 . . . . . . . . 62 1 59 . 1 1 18 18 LYS HB3 H 1 1.82 . . 1 . . . . . . . . 62 1 60 . 1 1 19 19 ALA H H 1 6.64 . . 1 . . . . . . . . 62 1 61 . 1 1 19 19 ALA HA H 1 4.23 . . 1 . . . . . . . . 62 1 62 . 1 1 19 19 ALA HB1 H 1 1.27 . . 1 . . . . . . . . 62 1 63 . 1 1 19 19 ALA HB2 H 1 1.27 . . 1 . . . . . . . . 62 1 64 . 1 1 19 19 ALA HB3 H 1 1.27 . . 1 . . . . . . . . 62 1 65 . 1 1 20 20 ASP H H 1 8.52 . . 1 . . . . . . . . 62 1 66 . 1 1 20 20 ASP HA H 1 4.74 . . 1 . . . . . . . . 62 1 67 . 1 1 20 20 ASP HB2 H 1 2.62 . . 2 . . . . . . . . 62 1 68 . 1 1 20 20 ASP HB3 H 1 2.69 . . 2 . . . . . . . . 62 1 69 . 1 1 21 21 GLY H H 1 8.16 . . 1 . . . . . . . . 62 1 70 . 1 1 21 21 GLY HA2 H 1 4.02 . . 1 . . . . . . . . 62 1 71 . 1 1 21 21 GLY HA3 H 1 4.02 . . 1 . . . . . . . . 62 1 72 . 1 1 22 22 ALA H H 1 8.45 . . 1 . . . . . . . . 62 1 73 . 1 1 22 22 ALA HA H 1 5.2 . . 1 . . . . . . . . 62 1 74 . 1 1 22 22 ALA HB1 H 1 1.41 . . 1 . . . . . . . . 62 1 75 . 1 1 22 22 ALA HB2 H 1 1.41 . . 1 . . . . . . . . 62 1 76 . 1 1 22 22 ALA HB3 H 1 1.41 . . 1 . . . . . . . . 62 1 77 . 1 1 23 23 ILE H H 1 9.02 . . 1 . . . . . . . . 62 1 78 . 1 1 23 23 ILE HA H 1 5.16 . . 1 . . . . . . . . 62 1 79 . 1 1 23 23 ILE HB H 1 1.74 . . 1 . . . . . . . . 62 1 80 . 1 1 24 24 LEU H H 1 9.26 . . 1 . . . . . . . . 62 1 81 . 1 1 24 24 LEU HA H 1 5.24 . . 1 . . . . . . . . 62 1 82 . 1 1 24 24 LEU HB2 H 1 2.03 . . 1 . . . . . . . . 62 1 83 . 1 1 24 24 LEU HB3 H 1 2.03 . . 1 . . . . . . . . 62 1 84 . 1 1 25 25 VAL H H 1 9.8 . . 1 . . . . . . . . 62 1 85 . 1 1 25 25 VAL HA H 1 4.55 . . 1 . . . . . . . . 62 1 86 . 1 1 25 25 VAL HB H 1 2.24 . . 1 . . . . . . . . 62 1 87 . 1 1 26 26 ASP H H 1 8.91 . . 1 . . . . . . . . 62 1 88 . 1 1 26 26 ASP HA H 1 5.24 . . 1 . . . . . . . . 62 1 89 . 1 1 26 26 ASP HB2 H 1 2.87 . . 1 . . . . . . . . 62 1 90 . 1 1 26 26 ASP HB3 H 1 2.87 . . 1 . . . . . . . . 62 1 91 . 1 1 27 27 PHE H H 1 9 . . 1 . . . . . . . . 62 1 92 . 1 1 27 27 PHE HA H 1 5.33 . . 1 . . . . . . . . 62 1 93 . 1 1 27 27 PHE HB2 H 1 2.79 . . 2 . . . . . . . . 62 1 94 . 1 1 27 27 PHE HB3 H 1 3.33 . . 2 . . . . . . . . 62 1 95 . 1 1 28 28 TRP H H 1 8.66 . . 1 . . . . . . . . 62 1 96 . 1 1 28 28 TRP HA H 1 5.17 . . 1 . . . . . . . . 62 1 97 . 1 1 28 28 TRP HB2 H 1 3.08 . . 2 . . . . . . . . 62 1 98 . 1 1 28 28 TRP HB3 H 1 3.16 . . 2 . . . . . . . . 62 1 99 . 1 1 29 29 ALA H H 1 6.59 . . 1 . . . . . . . . 62 1 100 . 1 1 29 29 ALA HA H 1 3.33 . . 1 . . . . . . . . 62 1 101 . 1 1 29 29 ALA HB1 H 1 .35 . . 1 . . . . . . . . 62 1 102 . 1 1 29 29 ALA HB2 H 1 .35 . . 1 . . . . . . . . 62 1 103 . 1 1 29 29 ALA HB3 H 1 .35 . . 1 . . . . . . . . 62 1 104 . 1 1 30 30 GLU H H 1 9.36 . . 1 . . . . . . . . 62 1 105 . 1 1 30 30 GLU HA H 1 4.2 . . 1 . . . . . . . . 62 1 106 . 1 1 30 30 GLU HB2 H 1 2.06 . . 2 . . . . . . . . 62 1 107 . 1 1 30 30 GLU HB3 H 1 2.1 . . 2 . . . . . . . . 62 1 108 . 1 1 31 31 TRP H H 1 6.69 . . 1 . . . . . . . . 62 1 109 . 1 1 31 31 TRP HA H 1 4.61 . . 1 . . . . . . . . 62 1 110 . 1 1 31 31 TRP HB2 H 1 3.22 . . 1 . . . . . . . . 62 1 111 . 1 1 31 31 TRP HB3 H 1 3.22 . . 1 . . . . . . . . 62 1 112 . 1 1 32 32 CYS H H 1 6.88 . . 1 . . . . . . . . 62 1 113 . 1 1 32 32 CYS HA H 1 4.74 . . 1 . . . . . . . . 62 1 114 . 1 1 32 32 CYS HB2 H 1 2.78 . . 2 . . . . . . . . 62 1 115 . 1 1 32 32 CYS HB3 H 1 2.91 . . 2 . . . . . . . . 62 1 116 . 1 1 33 33 GLY H H 1 9.61 . . 1 . . . . . . . . 62 1 117 . 1 1 33 33 GLY HA2 H 1 4.07 . . 2 . . . . . . . . 62 1 118 . 1 1 33 33 GLY HA3 H 1 4.34 . . 2 . . . . . . . . 62 1 119 . 1 1 35 35 CYS H H 1 8.25 . . 1 . . . . . . . . 62 1 120 . 1 1 35 35 CYS HA H 1 4.43 . . 1 . . . . . . . . 62 1 121 . 1 1 35 35 CYS HB2 H 1 3.4 . . 1 . . . . . . . . 62 1 122 . 1 1 35 35 CYS HB3 H 1 3.4 . . 1 . . . . . . . . 62 1 123 . 1 1 36 36 LYS H H 1 7.97 . . 1 . . . . . . . . 62 1 124 . 1 1 36 36 LYS HA H 1 4.09 . . 1 . . . . . . . . 62 1 125 . 1 1 36 36 LYS HB2 H 1 2 . . 2 . . . . . . . . 62 1 126 . 1 1 36 36 LYS HB3 H 1 2.12 . . 2 . . . . . . . . 62 1 127 . 1 1 37 37 MET H H 1 7.66 . . 1 . . . . . . . . 62 1 128 . 1 1 37 37 MET HA H 1 4.29 . . 1 . . . . . . . . 62 1 129 . 1 1 37 37 MET HB2 H 1 2.22 . . 2 . . . . . . . . 62 1 130 . 1 1 37 37 MET HB3 H 1 2.24 . . 2 . . . . . . . . 62 1 131 . 1 1 38 38 ILE H H 1 7.23 . . 1 . . . . . . . . 62 1 132 . 1 1 38 38 ILE HA H 1 4.41 . . 1 . . . . . . . . 62 1 133 . 1 1 38 38 ILE HB H 1 1.96 . . 1 . . . . . . . . 62 1 134 . 1 1 39 39 ALA H H 1 7.23 . . 1 . . . . . . . . 62 1 135 . 1 1 39 39 ALA HA H 1 3.85 . . 1 . . . . . . . . 62 1 136 . 1 1 39 39 ALA HB1 H 1 1.34 . . 1 . . . . . . . . 62 1 137 . 1 1 39 39 ALA HB2 H 1 1.34 . . 1 . . . . . . . . 62 1 138 . 1 1 39 39 ALA HB3 H 1 1.34 . . 1 . . . . . . . . 62 1 139 . 1 1 41 41 ILE H H 1 6.71 . . 1 . . . . . . . . 62 1 140 . 1 1 41 41 ILE HA H 1 3.85 . . 1 . . . . . . . . 62 1 141 . 1 1 41 41 ILE HB H 1 2.03 . . 1 . . . . . . . . 62 1 142 . 1 1 42 42 LEU H H 1 7.94 . . 1 . . . . . . . . 62 1 143 . 1 1 42 42 LEU HA H 1 3.85 . . 1 . . . . . . . . 62 1 144 . 1 1 42 42 LEU HB2 H 1 1.9 . . 1 . . . . . . . . 62 1 145 . 1 1 42 42 LEU HB3 H 1 1.9 . . 1 . . . . . . . . 62 1 146 . 1 1 43 43 ASP H H 1 7.33 . . 1 . . . . . . . . 62 1 147 . 1 1 43 43 ASP HA H 1 4.31 . . 1 . . . . . . . . 62 1 148 . 1 1 43 43 ASP HB2 H 1 2.69 . . 2 . . . . . . . . 62 1 149 . 1 1 43 43 ASP HB3 H 1 2.8 . . 2 . . . . . . . . 62 1 150 . 1 1 44 44 GLU H H 1 7.29 . . 1 . . . . . . . . 62 1 151 . 1 1 44 44 GLU HA H 1 4.27 . . 1 . . . . . . . . 62 1 152 . 1 1 44 44 GLU HB2 H 1 2.07 . . 2 . . . . . . . . 62 1 153 . 1 1 44 44 GLU HB3 H 1 2.24 . . 2 . . . . . . . . 62 1 154 . 1 1 45 45 ILE H H 1 8.56 . . 1 . . . . . . . . 62 1 155 . 1 1 45 45 ILE HA H 1 3.99 . . 1 . . . . . . . . 62 1 156 . 1 1 45 45 ILE HB H 1 2.16 . . 1 . . . . . . . . 62 1 157 . 1 1 46 46 ALA H H 1 8.6 . . 1 . . . . . . . . 62 1 158 . 1 1 46 46 ALA HA H 1 3.97 . . 1 . . . . . . . . 62 1 159 . 1 1 46 46 ALA HB1 H 1 1.44 . . 1 . . . . . . . . 62 1 160 . 1 1 46 46 ALA HB2 H 1 1.44 . . 1 . . . . . . . . 62 1 161 . 1 1 46 46 ALA HB3 H 1 1.44 . . 1 . . . . . . . . 62 1 162 . 1 1 47 47 ASP H H 1 7.17 . . 1 . . . . . . . . 62 1 163 . 1 1 47 47 ASP HA H 1 4.57 . . 1 . . . . . . . . 62 1 164 . 1 1 47 47 ASP HB2 H 1 2.85 . . 1 . . . . . . . . 62 1 165 . 1 1 47 47 ASP HB3 H 1 2.85 . . 1 . . . . . . . . 62 1 166 . 1 1 48 48 GLU H H 1 8.58 . . 1 . . . . . . . . 62 1 167 . 1 1 48 48 GLU HA H 1 4.06 . . 1 . . . . . . . . 62 1 168 . 1 1 48 48 GLU HB2 H 1 2.02 . . 2 . . . . . . . . 62 1 169 . 1 1 48 48 GLU HB3 H 1 2.16 . . 2 . . . . . . . . 62 1 170 . 1 1 49 49 TYR H H 1 8.76 . . 1 . . . . . . . . 62 1 171 . 1 1 49 49 TYR HA H 1 4.4 . . 1 . . . . . . . . 62 1 172 . 1 1 49 49 TYR HB2 H 1 2.82 . . 1 . . . . . . . . 62 1 173 . 1 1 49 49 TYR HB3 H 1 2.82 . . 1 . . . . . . . . 62 1 174 . 1 1 50 50 GLN H H 1 7.12 . . 1 . . . . . . . . 62 1 175 . 1 1 50 50 GLN HA H 1 4.37 . . 1 . . . . . . . . 62 1 176 . 1 1 50 50 GLN HB2 H 1 2.27 . . 2 . . . . . . . . 62 1 177 . 1 1 50 50 GLN HB3 H 1 2.36 . . 2 . . . . . . . . 62 1 178 . 1 1 51 51 GLY H H 1 9.27 . . 1 . . . . . . . . 62 1 179 . 1 1 51 51 GLY HA2 H 1 3.76 . . 2 . . . . . . . . 62 1 180 . 1 1 51 51 GLY HA3 H 1 4.43 . . 2 . . . . . . . . 62 1 181 . 1 1 52 52 LYS H H 1 8.22 . . 1 . . . . . . . . 62 1 182 . 1 1 52 52 LYS HA H 1 4.65 . . 1 . . . . . . . . 62 1 183 . 1 1 52 52 LYS HB2 H 1 1.9 . . 1 . . . . . . . . 62 1 184 . 1 1 52 52 LYS HB3 H 1 1.9 . . 1 . . . . . . . . 62 1 185 . 1 1 53 53 LEU H H 1 7.89 . . 1 . . . . . . . . 62 1 186 . 1 1 53 53 LEU HA H 1 4.82 . . 1 . . . . . . . . 62 1 187 . 1 1 53 53 LEU HB2 H 1 1.79 . . 1 . . . . . . . . 62 1 188 . 1 1 53 53 LEU HB3 H 1 1.79 . . 1 . . . . . . . . 62 1 189 . 1 1 54 54 THR H H 1 8.17 . . 1 . . . . . . . . 62 1 190 . 1 1 54 54 THR HA H 1 4.66 . . 1 . . . . . . . . 62 1 191 . 1 1 54 54 THR HB H 1 3.97 . . 1 . . . . . . . . 62 1 192 . 1 1 55 55 VAL H H 1 9.96 . . 1 . . . . . . . . 62 1 193 . 1 1 55 55 VAL HA H 1 4.63 . . 1 . . . . . . . . 62 1 194 . 1 1 55 55 VAL HB H 1 2 . . 1 . . . . . . . . 62 1 195 . 1 1 56 56 ALA H H 1 9.32 . . 1 . . . . . . . . 62 1 196 . 1 1 56 56 ALA HA H 1 5.41 . . 1 . . . . . . . . 62 1 197 . 1 1 56 56 ALA HB1 H 1 1.03 . . 1 . . . . . . . . 62 1 198 . 1 1 56 56 ALA HB2 H 1 1.03 . . 1 . . . . . . . . 62 1 199 . 1 1 56 56 ALA HB3 H 1 1.03 . . 1 . . . . . . . . 62 1 200 . 1 1 57 57 LYS H H 1 8.7 . . 1 . . . . . . . . 62 1 201 . 1 1 57 57 LYS HA H 1 5.14 . . 1 . . . . . . . . 62 1 202 . 1 1 57 57 LYS HB2 H 1 1.6 . . 1 . . . . . . . . 62 1 203 . 1 1 57 57 LYS HB3 H 1 1.6 . . 1 . . . . . . . . 62 1 204 . 1 1 58 58 LEU H H 1 8.83 . . 1 . . . . . . . . 62 1 205 . 1 1 58 58 LEU HA H 1 4.62 . . 1 . . . . . . . . 62 1 206 . 1 1 58 58 LEU HB2 H 1 1.32 . . 1 . . . . . . . . 62 1 207 . 1 1 58 58 LEU HB3 H 1 1.32 . . 1 . . . . . . . . 62 1 208 . 1 1 59 59 ASN H H 1 9.09 . . 1 . . . . . . . . 62 1 209 . 1 1 59 59 ASN HA H 1 4 . . 1 . . . . . . . . 62 1 210 . 1 1 59 59 ASN HB2 H 1 2.21 . . 2 . . . . . . . . 62 1 211 . 1 1 59 59 ASN HB3 H 1 2.69 . . 2 . . . . . . . . 62 1 212 . 1 1 60 60 ILE H H 1 8.56 . . 1 . . . . . . . . 62 1 213 . 1 1 60 60 ILE HA H 1 4.27 . . 1 . . . . . . . . 62 1 214 . 1 1 60 60 ILE HB H 1 2.24 . . 1 . . . . . . . . 62 1 215 . 1 1 61 61 ASP H H 1 7.8 . . 1 . . . . . . . . 62 1 216 . 1 1 61 61 ASP HA H 1 4.64 . . 1 . . . . . . . . 62 1 217 . 1 1 61 61 ASP HB2 H 1 2.71 . . 2 . . . . . . . . 62 1 218 . 1 1 61 61 ASP HB3 H 1 2.92 . . 2 . . . . . . . . 62 1 219 . 1 1 62 62 GLN H H 1 7.26 . . 1 . . . . . . . . 62 1 220 . 1 1 62 62 GLN HA H 1 4.23 . . 1 . . . . . . . . 62 1 221 . 1 1 62 62 GLN HB2 H 1 1.78 . . 2 . . . . . . . . 62 1 222 . 1 1 62 62 GLN HB3 H 1 2.22 . . 2 . . . . . . . . 62 1 223 . 1 1 63 63 ASN H H 1 7.41 . . 1 . . . . . . . . 62 1 224 . 1 1 63 63 ASN HA H 1 5.19 . . 1 . . . . . . . . 62 1 225 . 1 1 63 63 ASN HB2 H 1 2.72 . . 2 . . . . . . . . 62 1 226 . 1 1 63 63 ASN HB3 H 1 2.8 . . 2 . . . . . . . . 62 1 227 . 1 1 65 65 GLY H H 1 10.28 . . 1 . . . . . . . . 62 1 228 . 1 1 65 65 GLY HA2 H 1 3.7 . . 2 . . . . . . . . 62 1 229 . 1 1 65 65 GLY HA3 H 1 4 . . 2 . . . . . . . . 62 1 230 . 1 1 66 66 THR H H 1 7.9 . . 1 . . . . . . . . 62 1 231 . 1 1 66 66 THR HA H 1 3.8 . . 1 . . . . . . . . 62 1 232 . 1 1 66 66 THR HB H 1 3.78 . . 1 . . . . . . . . 62 1 233 . 1 1 67 67 ALA H H 1 9.76 . . 1 . . . . . . . . 62 1 234 . 1 1 67 67 ALA HA H 1 3.89 . . 1 . . . . . . . . 62 1 235 . 1 1 67 67 ALA HB1 H 1 1.34 . . 1 . . . . . . . . 62 1 236 . 1 1 67 67 ALA HB2 H 1 1.34 . . 1 . . . . . . . . 62 1 237 . 1 1 67 67 ALA HB3 H 1 1.34 . . 1 . . . . . . . . 62 1 238 . 1 1 69 69 LYS H H 1 7.4 . . 1 . . . . . . . . 62 1 239 . 1 1 69 69 LYS HA H 1 3.9 . . 1 . . . . . . . . 62 1 240 . 1 1 69 69 LYS HB2 H 1 1.49 . . 2 . . . . . . . . 62 1 241 . 1 1 69 69 LYS HB3 H 1 1.83 . . 2 . . . . . . . . 62 1 242 . 1 1 70 70 TYR H H 1 7.35 . . 1 . . . . . . . . 62 1 243 . 1 1 70 70 TYR HA H 1 4.44 . . 1 . . . . . . . . 62 1 244 . 1 1 70 70 TYR HB2 H 1 3.44 . . 1 . . . . . . . . 62 1 245 . 1 1 70 70 TYR HB3 H 1 3.44 . . 1 . . . . . . . . 62 1 246 . 1 1 71 71 GLY H H 1 7.55 . . 1 . . . . . . . . 62 1 247 . 1 1 71 71 GLY HA2 H 1 3.78 . . 2 . . . . . . . . 62 1 248 . 1 1 71 71 GLY HA3 H 1 3.85 . . 2 . . . . . . . . 62 1 249 . 1 1 72 72 ILE H H 1 7.17 . . 1 . . . . . . . . 62 1 250 . 1 1 72 72 ILE HA H 1 3.79 . . 1 . . . . . . . . 62 1 251 . 1 1 72 72 ILE HB H 1 1.53 . . 1 . . . . . . . . 62 1 252 . 1 1 73 73 ARG H H 1 8.6 . . 1 . . . . . . . . 62 1 253 . 1 1 73 73 ARG HA H 1 4.44 . . 1 . . . . . . . . 62 1 254 . 1 1 73 73 ARG HB2 H 1 1.63 . . 2 . . . . . . . . 62 1 255 . 1 1 73 73 ARG HB3 H 1 1.67 . . 2 . . . . . . . . 62 1 256 . 1 1 74 74 GLY H H 1 7.71 . . 1 . . . . . . . . 62 1 257 . 1 1 74 74 GLY HA2 H 1 3.79 . . 2 . . . . . . . . 62 1 258 . 1 1 74 74 GLY HA3 H 1 4.25 . . 2 . . . . . . . . 62 1 259 . 1 1 75 75 ILE H H 1 8.3 . . 1 . . . . . . . . 62 1 260 . 1 1 75 75 ILE HA H 1 4.74 . . 1 . . . . . . . . 62 1 261 . 1 1 75 75 ILE HB H 1 1.92 . . 1 . . . . . . . . 62 1 262 . 1 1 77 77 THR H H 1 7.8 . . 1 . . . . . . . . 62 1 263 . 1 1 77 77 THR HA H 1 4.93 . . 1 . . . . . . . . 62 1 264 . 1 1 77 77 THR HB H 1 3.9 . . 1 . . . . . . . . 62 1 265 . 1 1 78 78 LEU H H 1 9.3 . . 1 . . . . . . . . 62 1 266 . 1 1 78 78 LEU HA H 1 5.77 . . 1 . . . . . . . . 62 1 267 . 1 1 78 78 LEU HB2 H 1 1.7 . . 2 . . . . . . . . 62 1 268 . 1 1 78 78 LEU HB3 H 1 1.77 . . 2 . . . . . . . . 62 1 269 . 1 1 79 79 LEU H H 1 9.12 . . 1 . . . . . . . . 62 1 270 . 1 1 79 79 LEU HA H 1 5.14 . . 1 . . . . . . . . 62 1 271 . 1 1 79 79 LEU HB2 H 1 1.87 . . 1 . . . . . . . . 62 1 272 . 1 1 79 79 LEU HB3 H 1 1.87 . . 1 . . . . . . . . 62 1 273 . 1 1 80 80 LEU H H 1 8.89 . . 1 . . . . . . . . 62 1 274 . 1 1 80 80 LEU HA H 1 5.32 . . 1 . . . . . . . . 62 1 275 . 1 1 80 80 LEU HB2 H 1 1.96 . . 1 . . . . . . . . 62 1 276 . 1 1 80 80 LEU HB3 H 1 1.96 . . 1 . . . . . . . . 62 1 277 . 1 1 81 81 PHE H H 1 10 . . 1 . . . . . . . . 62 1 278 . 1 1 81 81 PHE HA H 1 5.2 . . 1 . . . . . . . . 62 1 279 . 1 1 81 81 PHE HB2 H 1 2.87 . . 2 . . . . . . . . 62 1 280 . 1 1 81 81 PHE HB3 H 1 2.93 . . 2 . . . . . . . . 62 1 281 . 1 1 82 82 LYS H H 1 8.82 . . 1 . . . . . . . . 62 1 282 . 1 1 82 82 LYS HA H 1 4.62 . . 1 . . . . . . . . 62 1 283 . 1 1 82 82 LYS HB2 H 1 1.62 . . 2 . . . . . . . . 62 1 284 . 1 1 82 82 LYS HB3 H 1 1.77 . . 2 . . . . . . . . 62 1 285 . 1 1 83 83 ASN H H 1 9.41 . . 1 . . . . . . . . 62 1 286 . 1 1 83 83 ASN HA H 1 4.62 . . 1 . . . . . . . . 62 1 287 . 1 1 83 83 ASN HB2 H 1 2.86 . . 2 . . . . . . . . 62 1 288 . 1 1 83 83 ASN HB3 H 1 3.13 . . 2 . . . . . . . . 62 1 289 . 1 1 84 84 GLY H H 1 9.62 . . 1 . . . . . . . . 62 1 290 . 1 1 84 84 GLY HA2 H 1 3.79 . . 2 . . . . . . . . 62 1 291 . 1 1 84 84 GLY HA3 H 1 4.4 . . 2 . . . . . . . . 62 1 292 . 1 1 85 85 GLU H H 1 7.88 . . 1 . . . . . . . . 62 1 293 . 1 1 85 85 GLU HA H 1 4.95 . . 1 . . . . . . . . 62 1 294 . 1 1 85 85 GLU HB2 H 1 1.96 . . 2 . . . . . . . . 62 1 295 . 1 1 85 85 GLU HB3 H 1 2.11 . . 2 . . . . . . . . 62 1 296 . 1 1 86 86 VAL H H 1 8.84 . . 1 . . . . . . . . 62 1 297 . 1 1 86 86 VAL HA H 1 3.16 . . 1 . . . . . . . . 62 1 298 . 1 1 86 86 VAL HB H 1 1.87 . . 1 . . . . . . . . 62 1 299 . 1 1 87 87 ALA H H 1 9.68 . . 1 . . . . . . . . 62 1 300 . 1 1 87 87 ALA HA H 1 4.53 . . 1 . . . . . . . . 62 1 301 . 1 1 87 87 ALA HB1 H 1 1.33 . . 1 . . . . . . . . 62 1 302 . 1 1 87 87 ALA HB2 H 1 1.33 . . 1 . . . . . . . . 62 1 303 . 1 1 87 87 ALA HB3 H 1 1.33 . . 1 . . . . . . . . 62 1 304 . 1 1 88 88 ALA H H 1 7.72 . . 1 . . . . . . . . 62 1 305 . 1 1 88 88 ALA HA H 1 4.64 . . 1 . . . . . . . . 62 1 306 . 1 1 88 88 ALA HB1 H 1 1.34 . . 1 . . . . . . . . 62 1 307 . 1 1 88 88 ALA HB2 H 1 1.34 . . 1 . . . . . . . . 62 1 308 . 1 1 88 88 ALA HB3 H 1 1.34 . . 1 . . . . . . . . 62 1 309 . 1 1 89 89 THR H H 1 8.55 . . 1 . . . . . . . . 62 1 310 . 1 1 89 89 THR HA H 1 5.16 . . 1 . . . . . . . . 62 1 311 . 1 1 89 89 THR HB H 1 3.84 . . 1 . . . . . . . . 62 1 312 . 1 1 90 90 LYS H H 1 9.05 . . 1 . . . . . . . . 62 1 313 . 1 1 90 90 LYS HA H 1 4.52 . . 1 . . . . . . . . 62 1 314 . 1 1 90 90 LYS HB2 H 1 1.22 . . 1 . . . . . . . . 62 1 315 . 1 1 90 90 LYS HB3 H 1 1.22 . . 1 . . . . . . . . 62 1 316 . 1 1 91 91 VAL H H 1 8.66 . . 1 . . . . . . . . 62 1 317 . 1 1 91 91 VAL HA H 1 4.6 . . 1 . . . . . . . . 62 1 318 . 1 1 91 91 VAL HB H 1 1.95 . . 1 . . . . . . . . 62 1 319 . 1 1 92 92 GLY H H 1 8.19 . . 1 . . . . . . . . 62 1 320 . 1 1 92 92 GLY HA2 H 1 3.65 . . 2 . . . . . . . . 62 1 321 . 1 1 92 92 GLY HA3 H 1 4.4 . . 2 . . . . . . . . 62 1 322 . 1 1 93 93 ALA H H 1 8.22 . . 1 . . . . . . . . 62 1 323 . 1 1 93 93 ALA HA H 1 3.99 . . 1 . . . . . . . . 62 1 324 . 1 1 93 93 ALA HB1 H 1 1.37 . . 1 . . . . . . . . 62 1 325 . 1 1 93 93 ALA HB2 H 1 1.37 . . 1 . . . . . . . . 62 1 326 . 1 1 93 93 ALA HB3 H 1 1.37 . . 1 . . . . . . . . 62 1 327 . 1 1 94 94 LYS H H 1 6.78 . . 1 . . . . . . . . 62 1 328 . 1 1 94 94 LYS HA H 1 4.71 . . 1 . . . . . . . . 62 1 329 . 1 1 94 94 LYS HB2 H 1 1.56 . . 2 . . . . . . . . 62 1 330 . 1 1 94 94 LYS HB3 H 1 1.61 . . 2 . . . . . . . . 62 1 331 . 1 1 95 95 SER H H 1 8.42 . . 1 . . . . . . . . 62 1 332 . 1 1 95 95 SER HA H 1 4.64 . . 1 . . . . . . . . 62 1 333 . 1 1 95 95 SER HB2 H 1 3.96 . . 1 . . . . . . . . 62 1 334 . 1 1 95 95 SER HB3 H 1 3.96 . . 1 . . . . . . . . 62 1 335 . 1 1 96 96 LYS H H 1 9.34 . . 1 . . . . . . . . 62 1 336 . 1 1 96 96 LYS HA H 1 3.83 . . 1 . . . . . . . . 62 1 337 . 1 1 96 96 LYS HB2 H 1 1.88 . . 2 . . . . . . . . 62 1 338 . 1 1 96 96 LYS HB3 H 1 1.96 . . 2 . . . . . . . . 62 1 339 . 1 1 97 97 GLY H H 1 8.83 . . 1 . . . . . . . . 62 1 340 . 1 1 97 97 GLY HA2 H 1 3.8 . . 2 . . . . . . . . 62 1 341 . 1 1 97 97 GLY HA3 H 1 3.96 . . 2 . . . . . . . . 62 1 342 . 1 1 98 98 GLN H H 1 7.76 . . 1 . . . . . . . . 62 1 343 . 1 1 98 98 GLN HA H 1 4.16 . . 1 . . . . . . . . 62 1 344 . 1 1 98 98 GLN HB2 H 1 2.3 . . 2 . . . . . . . . 62 1 345 . 1 1 98 98 GLN HB3 H 1 2.47 . . 2 . . . . . . . . 62 1 346 . 1 1 99 99 LEU H H 1 8.6 . . 1 . . . . . . . . 62 1 347 . 1 1 99 99 LEU HA H 1 4.12 . . 1 . . . . . . . . 62 1 348 . 1 1 99 99 LEU HB2 H 1 1.48 . . 2 . . . . . . . . 62 1 349 . 1 1 99 99 LEU HB3 H 1 1.91 . . 2 . . . . . . . . 62 1 350 . 1 1 100 100 LYS H H 1 8.76 . . 1 . . . . . . . . 62 1 351 . 1 1 100 100 LYS HA H 1 3.97 . . 1 . . . . . . . . 62 1 352 . 1 1 100 100 LYS HB2 H 1 1.83 . . 2 . . . . . . . . 62 1 353 . 1 1 100 100 LYS HB3 H 1 2.02 . . 2 . . . . . . . . 62 1 354 . 1 1 101 101 GLU H H 1 7.86 . . 1 . . . . . . . . 62 1 355 . 1 1 101 101 GLU HA H 1 4.08 . . 1 . . . . . . . . 62 1 356 . 1 1 101 101 GLU HB2 H 1 2.11 . . 2 . . . . . . . . 62 1 357 . 1 1 101 101 GLU HB3 H 1 2.16 . . 2 . . . . . . . . 62 1 stop_ save_