data_283 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 283 _Entry.Title ; Studies on the Solution Structure of Human Thioredoxin Using Heteronuclear 15N-1H Nuclear Magnetic Resonance Spectroscopy ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-13 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Julie Forman-Kay . D. . 283 2 Angela Gronenborn . M. . 283 3 Lewis Kay . E. . 283 4 Paul Wingfield . . . 283 5 G. Clore . Marius . 283 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 283 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 104 283 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 5 . . 2010-06-10 . revision BMRB 'Complete natural source information' 283 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 283 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 283 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 283 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 283 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 283 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Forman-Kay, Julie D., Gronenborn, Angela M., Kay, Lewis E., Wingfield, Paul, Clore, G. Marius, "Studies on the Solution Structure of Human Thioredoxin Using Heteronuclear 15N-1H Nuclear Magnetic Resonance Spectroscopy," Biochemistry 29 (6), 1566-1572 (1990). ; _Citation.Title ; Studies on the Solution Structure of Human Thioredoxin Using Heteronuclear 15N-1H Nuclear Magnetic Resonance Spectroscopy ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 29 _Citation.Journal_issue 6 _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 1566 _Citation.Page_last 1572 _Citation.Year 1990 _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 Julie Forman-Kay . D. . 283 1 2 Angela Gronenborn . M. . 283 1 3 Lewis Kay . E. . 283 1 4 Paul Wingfield . . . 283 1 5 G. Clore . Marius . 283 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_thioredoxin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_thioredoxin _Assembly.Entry_ID 283 _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 . . . . . . . . . 283 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID thioredoxin system 283 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_thioredoxin _Entity.Sf_category entity _Entity.Sf_framecode thioredoxin _Entity.Entry_ID 283 _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 ; MVKQIESKTAFQEALDAAGD KLVVVDFSATWCGPCKMIKP FFHSLSEKYSNVIFLEVDVD DCQDVASECEVKCTPTFQFF KKGQKVGEFSGANKEKLEAT INELV ; _Entity.Polymer_seq_one_letter_code ; MVKQIESKTAFQEALDAAGD KLVVVDFSATWCGPCKMIKP FFHSLSEKYSNVIFLEVDVD DCQDVASECEVKCTPTFQFF KKGQKVGEFSGANKEKLEAT INELV ; _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 105 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1400 . thioredoxin . . . . . 99.05 104 100.00 100.00 9.72e-68 . . . . 283 1 2 no BMRB 253 . thioredoxin . . . . . 100.00 105 100.00 100.00 1.00e-68 . . . . 283 1 3 no BMRB 254 . thioredoxin . . . . . 99.05 104 100.00 100.00 9.72e-68 . . . . 283 1 4 no BMRB 255 . thioredoxin . . . . . 99.05 104 100.00 100.00 9.72e-68 . . . . 283 1 5 no BMRB 256 . thioredoxin . . . . . 99.05 104 100.00 100.00 9.72e-68 . . . . 283 1 6 no BMRB 257 . thioredoxin . . . . . 100.00 105 100.00 100.00 1.00e-68 . . . . 283 1 7 no BMRB 284 . thioredoxin . . . . . 99.05 104 100.00 100.00 9.72e-68 . . . . 283 1 8 no BMRB 2958 . thioredoxin . . . . . 100.00 105 100.00 100.00 1.00e-68 . . . . 283 1 9 no BMRB 2959 . thioredoxin . . . . . 99.05 104 100.00 100.00 9.72e-68 . . . . 283 1 10 no PDB 1AIU . "Human Thioredoxin (D60n Mutant, Reduced Form)" . . . . . 100.00 105 98.10 99.05 2.25e-67 . . . . 283 1 11 no PDB 1AUC . "Human Thioredoxin (Oxidized With Diamide)" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 12 no PDB 1ERT . "Human Thioredoxin (Reduced Form)" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 13 no PDB 1ERU . "Human Thioredoxin (Oxidized Form)" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 14 no PDB 1ERV . "Human Thioredoxin Mutant With Cys 73 Replaced By Ser (Reduced Form)" . . . . . 100.00 105 98.10 98.10 6.91e-67 . . . . 283 1 15 no PDB 1ERW . "Human Thioredoxin Double Mutant With Cys 32 Replaced By Ser And Cys 35 Replaced By Ser" . . . . . 100.00 105 97.14 97.14 5.67e-66 . . . . 283 1 16 no PDB 1TRS . "The High-Resolution Three-Dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.14 97.14 2.82e-66 . . . . 283 1 17 no PDB 1TRU . "The High-Resolution Three-Dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.14 97.14 2.82e-66 . . . . 283 1 18 no PDB 1TRV . "The High-resolution Three-dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.14 97.14 2.82e-66 . . . . 283 1 19 no PDB 1TRW . "The High-Resolution Three-Dimensional Solution Structures Of The Oxidized And Reduced States Of Human Thioredoxin" . . . . . 100.00 105 97.14 97.14 2.82e-66 . . . . 283 1 20 no PDB 2HSH . "Crystal Structure Of C73s Mutant Of Human Thioredoxin-1 Oxidized With H2o2" . . . . . 100.00 105 98.10 98.10 6.91e-67 . . . . 283 1 21 no PDB 2HXK . "Crystal Structure Of S-Nitroso Thioredoxin" . . . . . 100.00 105 97.14 97.14 1.67e-65 . . . . 283 1 22 no PDB 2IFQ . "Crystal Structure Of S-Nitroso Thioredoxin" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 23 no PDB 2IIY . "Crystal Structure Of S-Nitroso Thioredoxin" . . . . . 100.00 105 97.14 97.14 1.67e-65 . . . . 283 1 24 no PDB 3E3E . "Human Thioredoxin Double Mutant C35s,C73r" . . . . . 100.00 105 97.14 97.14 1.15e-65 . . . . 283 1 25 no PDB 3M9J . "Crystal Structure Of Human Thioredoxin C6973S DOUBLE MUTANT, REDUCED Form" . . . . . 100.00 105 97.14 97.14 5.67e-66 . . . . 283 1 26 no PDB 3M9K . "Crystal Structure Of Human Thioredoxin C6973S DOUBLE-Mutant, Oxidized Form" . . . . . 100.00 105 97.14 97.14 5.67e-66 . . . . 283 1 27 no PDB 3QFA . "Crystal Structure Of The Human Thioredoxin Reductase-Thioredoxin Complex" . . . . . 99.05 116 97.12 97.12 1.75e-65 . . . . 283 1 28 no PDB 3QFB . "Crystal Structure Of The Human Thioredoxin Reductase-Thioredoxin Complex" . . . . . 99.05 116 97.12 97.12 1.75e-65 . . . . 283 1 29 no PDB 3TRX . "High-Resolution Three-Dimensional Structure Of Reduced Recombinant Human Thioredoxin In Solution" . . . . . 100.00 105 100.00 100.00 1.00e-68 . . . . 283 1 30 no PDB 4LL1 . "The Structure Of The Trx And Txnip Complex" . . . . . 100.00 105 98.10 98.10 6.27e-67 . . . . 283 1 31 no PDB 4LL4 . "The Structure Of The Trx And Txnip Complex" . . . . . 100.00 105 98.10 98.10 6.27e-67 . . . . 283 1 32 no PDB 4PUF . "Complex Between The Salmonella T3ss Effector Slrp And Its Human Target Thioredoxin-1" . . . . . 100.00 117 99.05 99.05 2.28e-68 . . . . 283 1 33 no PDB 4TRX . "High-Resolution Three-Dimensional Structure Of Reduced Recombinant Human Thioredoxin In Solution" . . . . . 100.00 105 100.00 100.00 1.00e-68 . . . . 283 1 34 no DBJ BAF82197 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 35 no EMBL CAA38410 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 36 no EMBL CAA54687 . "ATL-derived factor/thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 37 no EMBL CAG28593 . "TXN [Homo sapiens]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 38 no EMBL CAH91537 . "hypothetical protein [Pongo abelii]" . . . . . 100.95 106 98.11 98.11 5.31e-66 . . . . 283 1 39 no EMBL CEK46668 . "Thioredoxin-1 [synthetic construct]" . . . . . 100.00 125 99.05 99.05 1.82e-68 . . . . 283 1 40 no GB AAA74596 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.05 99.05 4.67e-68 . . . . 283 1 41 no GB AAF86466 . "thioredoxin 1 [Homo sapiens]" . . . . . 100.00 105 99.05 99.05 4.67e-68 . . . . 283 1 42 no GB AAF87085 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 43 no GB AAG34699 . "thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 44 no GB AAH03377 . "Thioredoxin [Homo sapiens]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 45 no REF NP_001125903 . "thioredoxin [Pongo abelii]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 46 no REF NP_003320 . "thioredoxin isoform 1 [Homo sapiens]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 47 no REF WP_052431332 . "hypothetical protein, partial [Acinetobacter sp. MII]" . . . . . 96.19 101 99.01 99.01 4.54e-65 . . . . 283 1 48 no REF XP_001142154 . "PREDICTED: thioredoxin [Pan troglodytes]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 49 no REF XP_003257823 . "PREDICTED: thioredoxin [Nomascus leucogenys]" . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 50 no SP P10599 . "RecName: Full=Thioredoxin; Short=Trx; AltName: Full=ATL-derived factor; Short=ADF; AltName: Full=Surface-associated sulphydryl " . . . . . 100.00 105 99.05 99.05 6.55e-68 . . . . 283 1 51 no SP Q5R9M3 . "RecName: Full=Thioredoxin; Short=Trx" . . . . . 100.95 106 98.11 98.11 5.31e-66 . . . . 283 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'N-met form' variant 283 1 thioredoxin common 283 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 . MET . 283 1 2 . VAL . 283 1 3 . LYS . 283 1 4 . GLN . 283 1 5 . ILE . 283 1 6 . GLU . 283 1 7 . SER . 283 1 8 . LYS . 283 1 9 . THR . 283 1 10 . ALA . 283 1 11 . PHE . 283 1 12 . GLN . 283 1 13 . GLU . 283 1 14 . ALA . 283 1 15 . LEU . 283 1 16 . ASP . 283 1 17 . ALA . 283 1 18 . ALA . 283 1 19 . GLY . 283 1 20 . ASP . 283 1 21 . LYS . 283 1 22 . LEU . 283 1 23 . VAL . 283 1 24 . VAL . 283 1 25 . VAL . 283 1 26 . ASP . 283 1 27 . PHE . 283 1 28 . SER . 283 1 29 . ALA . 283 1 30 . THR . 283 1 31 . TRP . 283 1 32 . CYS . 283 1 33 . GLY . 283 1 34 . PRO . 283 1 35 . CYS . 283 1 36 . LYS . 283 1 37 . MET . 283 1 38 . ILE . 283 1 39 . LYS . 283 1 40 . PRO . 283 1 41 . PHE . 283 1 42 . PHE . 283 1 43 . HIS . 283 1 44 . SER . 283 1 45 . LEU . 283 1 46 . SER . 283 1 47 . GLU . 283 1 48 . LYS . 283 1 49 . TYR . 283 1 50 . SER . 283 1 51 . ASN . 283 1 52 . VAL . 283 1 53 . ILE . 283 1 54 . PHE . 283 1 55 . LEU . 283 1 56 . GLU . 283 1 57 . VAL . 283 1 58 . ASP . 283 1 59 . VAL . 283 1 60 . ASP . 283 1 61 . ASP . 283 1 62 . CYS . 283 1 63 . GLN . 283 1 64 . ASP . 283 1 65 . VAL . 283 1 66 . ALA . 283 1 67 . SER . 283 1 68 . GLU . 283 1 69 . CYS . 283 1 70 . GLU . 283 1 71 . VAL . 283 1 72 . LYS . 283 1 73 . CYS . 283 1 74 . THR . 283 1 75 . PRO . 283 1 76 . THR . 283 1 77 . PHE . 283 1 78 . GLN . 283 1 79 . PHE . 283 1 80 . PHE . 283 1 81 . LYS . 283 1 82 . LYS . 283 1 83 . GLY . 283 1 84 . GLN . 283 1 85 . LYS . 283 1 86 . VAL . 283 1 87 . GLY . 283 1 88 . GLU . 283 1 89 . PHE . 283 1 90 . SER . 283 1 91 . GLY . 283 1 92 . ALA . 283 1 93 . ASN . 283 1 94 . LYS . 283 1 95 . GLU . 283 1 96 . LYS . 283 1 97 . LEU . 283 1 98 . GLU . 283 1 99 . ALA . 283 1 100 . THR . 283 1 101 . ILE . 283 1 102 . ASN . 283 1 103 . GLU . 283 1 104 . LEU . 283 1 105 . VAL . 283 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 . MET 1 1 283 1 . VAL 2 2 283 1 . LYS 3 3 283 1 . GLN 4 4 283 1 . ILE 5 5 283 1 . GLU 6 6 283 1 . SER 7 7 283 1 . LYS 8 8 283 1 . THR 9 9 283 1 . ALA 10 10 283 1 . PHE 11 11 283 1 . GLN 12 12 283 1 . GLU 13 13 283 1 . ALA 14 14 283 1 . LEU 15 15 283 1 . ASP 16 16 283 1 . ALA 17 17 283 1 . ALA 18 18 283 1 . GLY 19 19 283 1 . ASP 20 20 283 1 . LYS 21 21 283 1 . LEU 22 22 283 1 . VAL 23 23 283 1 . VAL 24 24 283 1 . VAL 25 25 283 1 . ASP 26 26 283 1 . PHE 27 27 283 1 . SER 28 28 283 1 . ALA 29 29 283 1 . THR 30 30 283 1 . TRP 31 31 283 1 . CYS 32 32 283 1 . GLY 33 33 283 1 . PRO 34 34 283 1 . CYS 35 35 283 1 . LYS 36 36 283 1 . MET 37 37 283 1 . ILE 38 38 283 1 . LYS 39 39 283 1 . PRO 40 40 283 1 . PHE 41 41 283 1 . PHE 42 42 283 1 . HIS 43 43 283 1 . SER 44 44 283 1 . LEU 45 45 283 1 . SER 46 46 283 1 . GLU 47 47 283 1 . LYS 48 48 283 1 . TYR 49 49 283 1 . SER 50 50 283 1 . ASN 51 51 283 1 . VAL 52 52 283 1 . ILE 53 53 283 1 . PHE 54 54 283 1 . LEU 55 55 283 1 . GLU 56 56 283 1 . VAL 57 57 283 1 . ASP 58 58 283 1 . VAL 59 59 283 1 . ASP 60 60 283 1 . ASP 61 61 283 1 . CYS 62 62 283 1 . GLN 63 63 283 1 . ASP 64 64 283 1 . VAL 65 65 283 1 . ALA 66 66 283 1 . SER 67 67 283 1 . GLU 68 68 283 1 . CYS 69 69 283 1 . GLU 70 70 283 1 . VAL 71 71 283 1 . LYS 72 72 283 1 . CYS 73 73 283 1 . THR 74 74 283 1 . PRO 75 75 283 1 . THR 76 76 283 1 . PHE 77 77 283 1 . GLN 78 78 283 1 . PHE 79 79 283 1 . PHE 80 80 283 1 . LYS 81 81 283 1 . LYS 82 82 283 1 . GLY 83 83 283 1 . GLN 84 84 283 1 . LYS 85 85 283 1 . VAL 86 86 283 1 . GLY 87 87 283 1 . GLU 88 88 283 1 . PHE 89 89 283 1 . SER 90 90 283 1 . GLY 91 91 283 1 . ALA 92 92 283 1 . ASN 93 93 283 1 . LYS 94 94 283 1 . GLU 95 95 283 1 . LYS 96 96 283 1 . LEU 97 97 283 1 . GLU 98 98 283 1 . ALA 99 99 283 1 . THR 100 100 283 1 . ILE 101 101 283 1 . ASN 102 102 283 1 . GLU 103 103 283 1 . LEU 104 104 283 1 . VAL 105 105 283 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 283 _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 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapeins . . . . . . . . . . . . . . . . . . . . . 283 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 283 _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' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 283 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 283 _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 283 _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 5.5 . na 283 1 temperature 313 . K 283 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 283 _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 283 _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' . . 283 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 283 _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 . . . . . . . . . . . . . . . . 283 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 283 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID N . 'liquid NH3' . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 283 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 283 _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 . 283 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 4 4 GLN NE2 N 15 112.3 . . 1 . . . . . . . . 283 1 2 . 1 1 4 4 GLN N N 15 126.9 . . 1 . . . . . . . . 283 1 3 . 1 1 5 5 ILE N N 15 127.7 . . 1 . . . . . . . . 283 1 4 . 1 1 6 6 GLU N N 15 123.4 . . 1 . . . . . . . . 283 1 5 . 1 1 7 7 SER N N 15 111.4 . . 1 . . . . . . . . 283 1 6 . 1 1 8 8 LYS N N 15 122.3 . . 1 . . . . . . . . 283 1 7 . 1 1 9 9 THR N N 15 115.3 . . 1 . . . . . . . . 283 1 8 . 1 1 10 10 ALA N N 15 123.7 . . 1 . . . . . . . . 283 1 9 . 1 1 11 11 PHE N N 15 120.5 . . 1 . . . . . . . . 283 1 10 . 1 1 12 12 GLN NE2 N 15 113.4 . . 1 . . . . . . . . 283 1 11 . 1 1 12 12 GLN N N 15 117.3 . . 1 . . . . . . . . 283 1 12 . 1 1 13 13 GLU N N 15 117.6 . . 1 . . . . . . . . 283 1 13 . 1 1 14 14 ALA N N 15 121.7 . . 1 . . . . . . . . 283 1 14 . 1 1 15 15 LEU N N 15 117.2 . . 1 . . . . . . . . 283 1 15 . 1 1 16 16 ASP N N 15 119.7 . . 1 . . . . . . . . 283 1 16 . 1 1 17 17 ALA N N 15 121.3 . . 1 . . . . . . . . 283 1 17 . 1 1 18 18 ALA N N 15 119 . . 1 . . . . . . . . 283 1 18 . 1 1 19 19 GLY N N 15 105.8 . . 1 . . . . . . . . 283 1 19 . 1 1 20 20 ASP N N 15 128.5 . . 1 . . . . . . . . 283 1 20 . 1 1 21 21 LYS N N 15 119.3 . . 1 . . . . . . . . 283 1 21 . 1 1 22 22 LEU N N 15 122.8 . . 1 . . . . . . . . 283 1 22 . 1 1 23 23 VAL N N 15 126 . . 1 . . . . . . . . 283 1 23 . 1 1 24 24 VAL N N 15 126.8 . . 1 . . . . . . . . 283 1 24 . 1 1 25 25 VAL N N 15 126.7 . . 1 . . . . . . . . 283 1 25 . 1 1 26 26 ASP N N 15 123.5 . . 1 . . . . . . . . 283 1 26 . 1 1 27 27 PHE N N 15 125.4 . . 1 . . . . . . . . 283 1 27 . 1 1 28 28 SER N N 15 117.7 . . 1 . . . . . . . . 283 1 28 . 1 1 29 29 ALA N N 15 121.7 . . 1 . . . . . . . . 283 1 29 . 1 1 30 30 THR N N 15 116.2 . . 1 . . . . . . . . 283 1 30 . 1 1 32 32 CYS N N 15 122.6 . . 1 . . . . . . . . 283 1 31 . 1 1 34 34 PRO N N 15 128.8 . . 1 . . . . . . . . 283 1 32 . 1 1 35 35 CYS N N 15 113.8 . . 1 . . . . . . . . 283 1 33 . 1 1 36 36 LYS N N 15 120.7 . . 1 . . . . . . . . 283 1 34 . 1 1 37 37 MET N N 15 116.2 . . 1 . . . . . . . . 283 1 35 . 1 1 38 38 ILE N N 15 115.8 . . 1 . . . . . . . . 283 1 36 . 1 1 39 39 LYS N N 15 125.3 . . 1 . . . . . . . . 283 1 37 . 1 1 40 40 PRO N N 15 129.1 . . 1 . . . . . . . . 283 1 38 . 1 1 41 41 PHE N N 15 119.7 . . 1 . . . . . . . . 283 1 39 . 1 1 42 42 PHE N N 15 122.1 . . 1 . . . . . . . . 283 1 40 . 1 1 43 43 HIS N N 15 114.4 . . 1 . . . . . . . . 283 1 41 . 1 1 44 44 SER N N 15 119.4 . . 1 . . . . . . . . 283 1 42 . 1 1 45 45 LEU N N 15 123.4 . . 1 . . . . . . . . 283 1 43 . 1 1 46 46 SER N N 15 115.5 . . 1 . . . . . . . . 283 1 44 . 1 1 47 47 GLU N N 15 119.7 . . 1 . . . . . . . . 283 1 45 . 1 1 48 48 LYS N N 15 119.9 . . 1 . . . . . . . . 283 1 46 . 1 1 49 49 TYR N N 15 118.4 . . 1 . . . . . . . . 283 1 47 . 1 1 51 51 ASN ND2 N 15 112.2 . . 1 . . . . . . . . 283 1 48 . 1 1 51 51 ASN N N 15 118.3 . . 1 . . . . . . . . 283 1 49 . 1 1 52 52 VAL N N 15 120.9 . . 1 . . . . . . . . 283 1 50 . 1 1 53 53 ILE N N 15 127.9 . . 1 . . . . . . . . 283 1 51 . 1 1 54 54 PHE N N 15 126.6 . . 1 . . . . . . . . 283 1 52 . 1 1 55 55 LEU N N 15 122.2 . . 1 . . . . . . . . 283 1 53 . 1 1 56 56 GLU N N 15 121.3 . . 1 . . . . . . . . 283 1 54 . 1 1 57 57 VAL N N 15 125.7 . . 1 . . . . . . . . 283 1 55 . 1 1 59 59 VAL N N 15 119.8 . . 1 . . . . . . . . 283 1 56 . 1 1 60 60 ASP N N 15 119.4 . . 1 . . . . . . . . 283 1 57 . 1 1 61 61 ASP N N 15 120.8 . . 1 . . . . . . . . 283 1 58 . 1 1 62 62 CYS N N 15 120.3 . . 1 . . . . . . . . 283 1 59 . 1 1 63 63 GLN NE2 N 15 111.4 . . 1 . . . . . . . . 283 1 60 . 1 1 63 63 GLN N N 15 122.3 . . 1 . . . . . . . . 283 1 61 . 1 1 64 64 ASP N N 15 118.2 . . 1 . . . . . . . . 283 1 62 . 1 1 65 65 VAL N N 15 121.9 . . 1 . . . . . . . . 283 1 63 . 1 1 66 66 ALA N N 15 120.2 . . 1 . . . . . . . . 283 1 64 . 1 1 67 67 SER N N 15 111.5 . . 1 . . . . . . . . 283 1 65 . 1 1 68 68 GLU N N 15 123.8 . . 1 . . . . . . . . 283 1 66 . 1 1 69 69 CYS N N 15 114.5 . . 1 . . . . . . . . 283 1 67 . 1 1 70 70 GLU N N 15 116.9 . . 1 . . . . . . . . 283 1 68 . 1 1 71 71 VAL N N 15 119.6 . . 1 . . . . . . . . 283 1 69 . 1 1 72 72 LYS N N 15 126.9 . . 1 . . . . . . . . 283 1 70 . 1 1 73 73 CYS N N 15 114.3 . . 1 . . . . . . . . 283 1 71 . 1 1 74 74 THR N N 15 112.2 . . 1 . . . . . . . . 283 1 72 . 1 1 76 76 THR N N 15 119 . . 1 . . . . . . . . 283 1 73 . 1 1 77 77 PHE N N 15 125.6 . . 1 . . . . . . . . 283 1 74 . 1 1 78 78 GLN NE2 N 15 105.8 . . 1 . . . . . . . . 283 1 75 . 1 1 78 78 GLN N N 15 118.8 . . 1 . . . . . . . . 283 1 76 . 1 1 79 79 PHE N N 15 119.7 . . 1 . . . . . . . . 283 1 77 . 1 1 80 80 PHE N N 15 122.5 . . 1 . . . . . . . . 283 1 78 . 1 1 81 81 LYS N N 15 118.7 . . 1 . . . . . . . . 283 1 79 . 1 1 82 82 LYS N N 15 128.3 . . 1 . . . . . . . . 283 1 80 . 1 1 83 83 GLY N N 15 104.2 . . 1 . . . . . . . . 283 1 81 . 1 1 84 84 GLN NE2 N 15 112.1 . . 1 . . . . . . . . 283 1 82 . 1 1 84 84 GLN N N 15 118.7 . . 1 . . . . . . . . 283 1 83 . 1 1 85 85 LYS N N 15 125.9 . . 1 . . . . . . . . 283 1 84 . 1 1 86 86 VAL N N 15 120.3 . . 1 . . . . . . . . 283 1 85 . 1 1 87 87 GLY N N 15 107.6 . . 1 . . . . . . . . 283 1 86 . 1 1 88 88 GLU N N 15 117.7 . . 1 . . . . . . . . 283 1 87 . 1 1 89 89 PHE N N 15 117.8 . . 1 . . . . . . . . 283 1 88 . 1 1 90 90 SER N N 15 116.1 . . 1 . . . . . . . . 283 1 89 . 1 1 91 91 GLY N N 15 107.8 . . 1 . . . . . . . . 283 1 90 . 1 1 92 92 ALA N N 15 122.9 . . 1 . . . . . . . . 283 1 91 . 1 1 93 93 ASN ND2 N 15 112.6 . . 1 . . . . . . . . 283 1 92 . 1 1 93 93 ASN N N 15 121.8 . . 1 . . . . . . . . 283 1 93 . 1 1 94 94 LYS N N 15 125.1 . . 1 . . . . . . . . 283 1 94 . 1 1 95 95 GLU N N 15 119.2 . . 1 . . . . . . . . 283 1 95 . 1 1 96 96 LYS N N 15 120.7 . . 1 . . . . . . . . 283 1 96 . 1 1 97 97 LEU N N 15 122.8 . . 1 . . . . . . . . 283 1 97 . 1 1 98 98 GLU N N 15 117.3 . . 1 . . . . . . . . 283 1 98 . 1 1 99 99 ALA N N 15 120.3 . . 1 . . . . . . . . 283 1 99 . 1 1 100 100 THR N N 15 115 . . 1 . . . . . . . . 283 1 100 . 1 1 102 102 ASN ND2 N 15 113 . . 1 . . . . . . . . 283 1 101 . 1 1 102 102 ASN N N 15 113.2 . . 1 . . . . . . . . 283 1 102 . 1 1 103 103 GLU N N 15 118 . . 1 . . . . . . . . 283 1 103 . 1 1 104 104 LEU N N 15 117.8 . . 1 . . . . . . . . 283 1 104 . 1 1 105 105 VAL N N 15 123.4 . . 1 . . . . . . . . 283 1 stop_ save_