data_1551 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 1551 _Entry.Title ; 1H NMR Identification of a B-Sheet Structure and Description of Folding Topology in Putidaredoxin ; _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 Thomas Pochapsky . C. . 1551 2 Xiao Ye . Mei . 1551 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 1551 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 222 1551 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 5 . . 2010-06-15 . revision BMRB 'Complete natural source information' 1551 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1551 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 1551 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1551 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 1551 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 1551 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Pochapsky, Thomas C., Ye, Xiao Mei, "1H NMR Identification of a B-Sheet Structure and Description of Folding Topology in Putidaredoxin," Biochemistry 30, 3850-3856 (1991). ; _Citation.Title ; 1H NMR Identification of a B-Sheet Structure and Description of Folding Topology in Putidaredoxin ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 30 _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 3850 _Citation.Page_last 3856 _Citation.Year 1991 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Thomas Pochapsky . C. . 1551 1 2 Xiao Ye . Mei . 1551 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_P450_reductase _Assembly.Sf_category assembly _Assembly.Sf_framecode system_P450_reductase _Assembly.Entry_ID 1551 _Assembly.ID 1 _Assembly.Name 'P450 reductase' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 'P450 reductase' 1 $P450_reductase . . . . . . . . . 1551 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'P450 reductase' system 1551 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_P450_reductase _Entity.Sf_category entity _Entity.Sf_framecode P450_reductase _Entity.Entry_ID 1551 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'P450 reductase' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; SKVVYVSHDGTRRQLDVADG VSLMQAAVSNGIYDIVGDCG GSASCATCHVYVNEAFTDKV PAANEREIGMLECVTAELKP NSRLCCQIIMTPELDGIVVD VPDRQW ; _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 106 _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 2015-11-26 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 2278 . putidaredoxin . . . . . 100.00 106 100.00 100.00 6.46e-71 . . . . 1551 1 2 no BMRB 4149 . putidaredoxin . . . . . 100.00 106 98.11 99.06 2.03e-69 . . . . 1551 1 3 no BMRB 4154 . putidaredoxin . . . . . 100.00 106 99.06 100.00 2.24e-70 . . . . 1551 1 4 no PDB 1GPX . "C85s Gapdx, Nmr, 20 Structures" . . . . . 100.00 106 98.11 99.06 2.03e-69 . . . . 1551 1 5 no PDB 1OQQ . "Crystal Structure Of C73sC85S MUTANT OF PUTIDAREDOXIN, A [2FE-2s] Ferredoxin From Pseudomonas Putida, At 1.47a Resolution" . . . . . 100.00 106 97.17 98.11 1.90e-68 . . . . 1551 1 6 no PDB 1OQR . "Crystal Structure Of C73s Mutant Of Putidaredoxin, A [2fe- 2s] Ferredoxin From Pseudomonas Putida, At 1.65a Resolution" . . . . . 100.00 106 98.11 99.06 2.03e-69 . . . . 1551 1 7 no PDB 1PDX . Putidaredoxin . . . . . 100.00 106 99.06 100.00 2.24e-70 . . . . 1551 1 8 no PDB 1PUT . "An Nmr-Derived Model For The Solution Structure Of Oxidized Putidaredoxin, A 2fe, 2-S Ferredoxin From Pseudomonas" . . . . . 100.00 106 100.00 100.00 6.46e-71 . . . . 1551 1 9 no PDB 1R7S . "Putidaredoxin (Fe2s2 Ferredoxin), C73g Mutant" . . . . . 100.00 106 98.11 99.06 6.25e-69 . . . . 1551 1 10 no PDB 1XLN . "Crystal Structure Of Oxidized C73sC85S PUTIDAREDOXIN, A [2fe-2s] Ferredoxin From Pseudomonas Putida" . . . . . 100.00 106 97.17 98.11 1.90e-68 . . . . 1551 1 11 no PDB 1XLO . "Structure Of Reduced C73s/c85s Putidaredoxin, A [2fe-2s] Ferredoxin From Pseudomonas Putida" . . . . . 100.00 106 97.17 98.11 1.90e-68 . . . . 1551 1 12 no PDB 1XLP . "Structure Of Oxidized C73s Putidaredoxin From Pseudomonas Putida" . . . . . 100.00 106 98.11 99.06 2.03e-69 . . . . 1551 1 13 no PDB 1XLQ . "Crystal Structure Of Reduced C73s Putidaredoxin From Pseudomonas Putida" . . . . . 100.00 106 98.11 99.06 2.03e-69 . . . . 1551 1 14 no PDB 1YJI . "Rdc-Refined Solution Nmr Structure Of Reduced Putidaredoxin" . . . . . 100.00 106 99.06 100.00 2.24e-70 . . . . 1551 1 15 no PDB 1YJJ . "Rdc-Refined Solution Nmr Structure Of Oxidized Putidaredoxin" . . . . . 100.00 106 99.06 100.00 2.24e-70 . . . . 1551 1 16 no PDB 2M56 . "The Structure Of The Complex Of Cytochrome P450cam And Its Electron Donor Putidaredoxin Determined By Paramagnetic Nmr Spectros" . . . . . 100.00 106 98.11 99.06 2.03e-69 . . . . 1551 1 17 no PDB 3LB8 . "Crystal Structure Of The Covalent Putidaredoxin Reductase- Putidaredoxin Complex" . . . . . 100.00 106 97.17 98.11 1.90e-68 . . . . 1551 1 18 no PDB 3W9C . "Crystal Structure Of The Electron Transfer Complex Of Cytochrome P450cam With Putidaredoxin" . . . . . 100.00 108 98.11 99.06 2.38e-69 . . . . 1551 1 19 no PDB 4JWS . "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" . . . . . 100.00 112 99.06 100.00 1.93e-70 . . . . 1551 1 20 no PDB 4JWU . "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" . . . . . 100.00 113 97.17 98.11 9.76e-68 . . . . 1551 1 21 no PDB 4JX1 . "Crystal Structure Of Reduced Cytochrome P450cam-putidaredoxin Complex Bound To Camphor And 5-exo-hydroxycamphor" . . . . . 100.00 113 97.17 98.11 9.76e-68 . . . . 1551 1 22 no DBJ BAA00414 . "putidaredoxin [Pseudomonas putida]" . . . . . 100.00 107 99.06 100.00 1.84e-70 . . . . 1551 1 23 no DBJ BAN13288 . "putidaredoxin [Pseudomonas putida]" . . . . . 100.00 107 99.06 100.00 1.84e-70 . . . . 1551 1 24 no GB AAA25759 . "putidaredoxin [Pseudomonas putida]" . . . . . 100.00 107 99.06 100.00 1.84e-70 . . . . 1551 1 25 no REF WP_032492635 . "putidaredoxin [Pseudomonas putida]" . . . . . 100.00 107 99.06 100.00 1.84e-70 . . . . 1551 1 26 no REF YP_009083114 . "putidaredoxin [Pseudomonas putida]" . . . . . 100.00 107 99.06 100.00 1.84e-70 . . . . 1551 1 27 no SP P00259 . "RecName: Full=Putidaredoxin; Short=PDX" . . . . . 100.00 107 99.06 100.00 1.84e-70 . . . . 1551 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'P450 reductase' common 1551 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 . 1551 1 2 . LYS . 1551 1 3 . VAL . 1551 1 4 . VAL . 1551 1 5 . TYR . 1551 1 6 . VAL . 1551 1 7 . SER . 1551 1 8 . HIS . 1551 1 9 . ASP . 1551 1 10 . GLY . 1551 1 11 . THR . 1551 1 12 . ARG . 1551 1 13 . ARG . 1551 1 14 . GLN . 1551 1 15 . LEU . 1551 1 16 . ASP . 1551 1 17 . VAL . 1551 1 18 . ALA . 1551 1 19 . ASP . 1551 1 20 . GLY . 1551 1 21 . VAL . 1551 1 22 . SER . 1551 1 23 . LEU . 1551 1 24 . MET . 1551 1 25 . GLN . 1551 1 26 . ALA . 1551 1 27 . ALA . 1551 1 28 . VAL . 1551 1 29 . SER . 1551 1 30 . ASN . 1551 1 31 . GLY . 1551 1 32 . ILE . 1551 1 33 . TYR . 1551 1 34 . ASP . 1551 1 35 . ILE . 1551 1 36 . VAL . 1551 1 37 . GLY . 1551 1 38 . ASP . 1551 1 39 . CYS . 1551 1 40 . GLY . 1551 1 41 . GLY . 1551 1 42 . SER . 1551 1 43 . ALA . 1551 1 44 . SER . 1551 1 45 . CYS . 1551 1 46 . ALA . 1551 1 47 . THR . 1551 1 48 . CYS . 1551 1 49 . HIS . 1551 1 50 . VAL . 1551 1 51 . TYR . 1551 1 52 . VAL . 1551 1 53 . ASN . 1551 1 54 . GLU . 1551 1 55 . ALA . 1551 1 56 . PHE . 1551 1 57 . THR . 1551 1 58 . ASP . 1551 1 59 . LYS . 1551 1 60 . VAL . 1551 1 61 . PRO . 1551 1 62 . ALA . 1551 1 63 . ALA . 1551 1 64 . ASN . 1551 1 65 . GLU . 1551 1 66 . ARG . 1551 1 67 . GLU . 1551 1 68 . ILE . 1551 1 69 . GLY . 1551 1 70 . MET . 1551 1 71 . LEU . 1551 1 72 . GLU . 1551 1 73 . CYS . 1551 1 74 . VAL . 1551 1 75 . THR . 1551 1 76 . ALA . 1551 1 77 . GLU . 1551 1 78 . LEU . 1551 1 79 . LYS . 1551 1 80 . PRO . 1551 1 81 . ASN . 1551 1 82 . SER . 1551 1 83 . ARG . 1551 1 84 . LEU . 1551 1 85 . CYS . 1551 1 86 . CYS . 1551 1 87 . GLN . 1551 1 88 . ILE . 1551 1 89 . ILE . 1551 1 90 . MET . 1551 1 91 . THR . 1551 1 92 . PRO . 1551 1 93 . GLU . 1551 1 94 . LEU . 1551 1 95 . ASP . 1551 1 96 . GLY . 1551 1 97 . ILE . 1551 1 98 . VAL . 1551 1 99 . VAL . 1551 1 100 . ASP . 1551 1 101 . VAL . 1551 1 102 . PRO . 1551 1 103 . ASP . 1551 1 104 . ARG . 1551 1 105 . GLN . 1551 1 106 . TRP . 1551 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 1551 1 . LYS 2 2 1551 1 . VAL 3 3 1551 1 . VAL 4 4 1551 1 . TYR 5 5 1551 1 . VAL 6 6 1551 1 . SER 7 7 1551 1 . HIS 8 8 1551 1 . ASP 9 9 1551 1 . GLY 10 10 1551 1 . THR 11 11 1551 1 . ARG 12 12 1551 1 . ARG 13 13 1551 1 . GLN 14 14 1551 1 . LEU 15 15 1551 1 . ASP 16 16 1551 1 . VAL 17 17 1551 1 . ALA 18 18 1551 1 . ASP 19 19 1551 1 . GLY 20 20 1551 1 . VAL 21 21 1551 1 . SER 22 22 1551 1 . LEU 23 23 1551 1 . MET 24 24 1551 1 . GLN 25 25 1551 1 . ALA 26 26 1551 1 . ALA 27 27 1551 1 . VAL 28 28 1551 1 . SER 29 29 1551 1 . ASN 30 30 1551 1 . GLY 31 31 1551 1 . ILE 32 32 1551 1 . TYR 33 33 1551 1 . ASP 34 34 1551 1 . ILE 35 35 1551 1 . VAL 36 36 1551 1 . GLY 37 37 1551 1 . ASP 38 38 1551 1 . CYS 39 39 1551 1 . GLY 40 40 1551 1 . GLY 41 41 1551 1 . SER 42 42 1551 1 . ALA 43 43 1551 1 . SER 44 44 1551 1 . CYS 45 45 1551 1 . ALA 46 46 1551 1 . THR 47 47 1551 1 . CYS 48 48 1551 1 . HIS 49 49 1551 1 . VAL 50 50 1551 1 . TYR 51 51 1551 1 . VAL 52 52 1551 1 . ASN 53 53 1551 1 . GLU 54 54 1551 1 . ALA 55 55 1551 1 . PHE 56 56 1551 1 . THR 57 57 1551 1 . ASP 58 58 1551 1 . LYS 59 59 1551 1 . VAL 60 60 1551 1 . PRO 61 61 1551 1 . ALA 62 62 1551 1 . ALA 63 63 1551 1 . ASN 64 64 1551 1 . GLU 65 65 1551 1 . ARG 66 66 1551 1 . GLU 67 67 1551 1 . ILE 68 68 1551 1 . GLY 69 69 1551 1 . MET 70 70 1551 1 . LEU 71 71 1551 1 . GLU 72 72 1551 1 . CYS 73 73 1551 1 . VAL 74 74 1551 1 . THR 75 75 1551 1 . ALA 76 76 1551 1 . GLU 77 77 1551 1 . LEU 78 78 1551 1 . LYS 79 79 1551 1 . PRO 80 80 1551 1 . ASN 81 81 1551 1 . SER 82 82 1551 1 . ARG 83 83 1551 1 . LEU 84 84 1551 1 . CYS 85 85 1551 1 . CYS 86 86 1551 1 . GLN 87 87 1551 1 . ILE 88 88 1551 1 . ILE 89 89 1551 1 . MET 90 90 1551 1 . THR 91 91 1551 1 . PRO 92 92 1551 1 . GLU 93 93 1551 1 . LEU 94 94 1551 1 . ASP 95 95 1551 1 . GLY 96 96 1551 1 . ILE 97 97 1551 1 . VAL 98 98 1551 1 . VAL 99 99 1551 1 . ASP 100 100 1551 1 . VAL 101 101 1551 1 . PRO 102 102 1551 1 . ASP 103 103 1551 1 . ARG 104 104 1551 1 . GLN 105 105 1551 1 . TRP 106 106 1551 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 1551 _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 $P450_reductase . 303 organism . 'Pseudomonas putida' . . . Bacteria . Pseudomonas putida generic . . . . . . . . . . . . . . . . . . . . 1551 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 1551 _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 $P450_reductase . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1551 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 1551 _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 1551 _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 7.4 . na 1551 1 temperature 290 . K 1551 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 1551 _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 1551 _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' . . 1551 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 1551 _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 . . . . . . . . . . . . . . . . 1551 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 1551 _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 . DSS . . . . . ppm 0 . . . . . . . . . . . . 1551 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 1551 _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 . 1551 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 SER HA H 1 3.88 . . 1 . . . . . . . . 1551 1 2 . 1 1 1 1 SER HB2 H 1 3.57 . . 2 . . . . . . . . 1551 1 3 . 1 1 1 1 SER HB3 H 1 3.4 . . 2 . . . . . . . . 1551 1 4 . 1 1 2 2 LYS H H 1 9.15 . . 1 . . . . . . . . 1551 1 5 . 1 1 2 2 LYS HA H 1 4.58 . . 1 . . . . . . . . 1551 1 6 . 1 1 2 2 LYS HB2 H 1 1.55 . . 2 . . . . . . . . 1551 1 7 . 1 1 2 2 LYS HB3 H 1 1.29 . . 2 . . . . . . . . 1551 1 8 . 1 1 2 2 LYS HG2 H 1 1.12 . . 2 . . . . . . . . 1551 1 9 . 1 1 2 2 LYS HG3 H 1 1 . . 2 . . . . . . . . 1551 1 10 . 1 1 2 2 LYS HD2 H 1 1.38 . . 2 . . . . . . . . 1551 1 11 . 1 1 2 2 LYS HD3 H 1 1.25 . . 2 . . . . . . . . 1551 1 12 . 1 1 2 2 LYS HE2 H 1 2.65 . . 2 . . . . . . . . 1551 1 13 . 1 1 2 2 LYS HE3 H 1 2.82 . . 2 . . . . . . . . 1551 1 14 . 1 1 3 3 VAL H H 1 8.48 . . 1 . . . . . . . . 1551 1 15 . 1 1 3 3 VAL HA H 1 4.18 . . 1 . . . . . . . . 1551 1 16 . 1 1 3 3 VAL HB H 1 1.38 . . 1 . . . . . . . . 1551 1 17 . 1 1 3 3 VAL HG11 H 1 .04 . . 2 . . . . . . . . 1551 1 18 . 1 1 3 3 VAL HG12 H 1 .04 . . 2 . . . . . . . . 1551 1 19 . 1 1 3 3 VAL HG13 H 1 .04 . . 2 . . . . . . . . 1551 1 20 . 1 1 3 3 VAL HG21 H 1 .45 . . 2 . . . . . . . . 1551 1 21 . 1 1 3 3 VAL HG22 H 1 .45 . . 2 . . . . . . . . 1551 1 22 . 1 1 3 3 VAL HG23 H 1 .45 . . 2 . . . . . . . . 1551 1 23 . 1 1 4 4 VAL H H 1 8.5 . . 1 . . . . . . . . 1551 1 24 . 1 1 4 4 VAL HA H 1 4.4 . . 1 . . . . . . . . 1551 1 25 . 1 1 4 4 VAL HB H 1 1.78 . . 1 . . . . . . . . 1551 1 26 . 1 1 4 4 VAL HG11 H 1 .495 . . 2 . . . . . . . . 1551 1 27 . 1 1 4 4 VAL HG12 H 1 .495 . . 2 . . . . . . . . 1551 1 28 . 1 1 4 4 VAL HG13 H 1 .495 . . 2 . . . . . . . . 1551 1 29 . 1 1 4 4 VAL HG21 H 1 .53 . . 2 . . . . . . . . 1551 1 30 . 1 1 4 4 VAL HG22 H 1 .53 . . 2 . . . . . . . . 1551 1 31 . 1 1 4 4 VAL HG23 H 1 .53 . . 2 . . . . . . . . 1551 1 32 . 1 1 5 5 TYR H H 1 8.84 . . 1 . . . . . . . . 1551 1 33 . 1 1 5 5 TYR HA H 1 4.72 . . 1 . . . . . . . . 1551 1 34 . 1 1 5 5 TYR HB2 H 1 2.72 . . 2 . . . . . . . . 1551 1 35 . 1 1 5 5 TYR HB3 H 1 2.23 . . 2 . . . . . . . . 1551 1 36 . 1 1 5 5 TYR HD1 H 1 6.48 . . 1 . . . . . . . . 1551 1 37 . 1 1 5 5 TYR HD2 H 1 6.48 . . 1 . . . . . . . . 1551 1 38 . 1 1 5 5 TYR HE1 H 1 6.05 . . 1 . . . . . . . . 1551 1 39 . 1 1 5 5 TYR HE2 H 1 6.05 . . 1 . . . . . . . . 1551 1 40 . 1 1 5 5 TYR HH H 1 8.02 . . 1 . . . . . . . . 1551 1 41 . 1 1 6 6 VAL H H 1 9.5 . . 1 . . . . . . . . 1551 1 42 . 1 1 6 6 VAL HA H 1 4.68 . . 1 . . . . . . . . 1551 1 43 . 1 1 6 6 VAL HB H 1 2.18 . . 1 . . . . . . . . 1551 1 44 . 1 1 6 6 VAL HG11 H 1 .56 . . 2 . . . . . . . . 1551 1 45 . 1 1 6 6 VAL HG12 H 1 .56 . . 2 . . . . . . . . 1551 1 46 . 1 1 6 6 VAL HG13 H 1 .56 . . 2 . . . . . . . . 1551 1 47 . 1 1 6 6 VAL HG21 H 1 .715 . . 2 . . . . . . . . 1551 1 48 . 1 1 6 6 VAL HG22 H 1 .715 . . 2 . . . . . . . . 1551 1 49 . 1 1 6 6 VAL HG23 H 1 .715 . . 2 . . . . . . . . 1551 1 50 . 1 1 14 14 GLN H H 1 8.55 . . 1 . . . . . . . . 1551 1 51 . 1 1 14 14 GLN HA H 1 5.095 . . 1 . . . . . . . . 1551 1 52 . 1 1 14 14 GLN HB2 H 1 1.68 . . 1 . . . . . . . . 1551 1 53 . 1 1 14 14 GLN HB3 H 1 1.68 . . 1 . . . . . . . . 1551 1 54 . 1 1 14 14 GLN HG2 H 1 1.82 . . 2 . . . . . . . . 1551 1 55 . 1 1 14 14 GLN HG3 H 1 1.97 . . 2 . . . . . . . . 1551 1 56 . 1 1 15 15 LEU H H 1 9.19 . . 1 . . . . . . . . 1551 1 57 . 1 1 15 15 LEU HA H 1 4.54 . . 1 . . . . . . . . 1551 1 58 . 1 1 15 15 LEU HB2 H 1 1.23 . . 2 . . . . . . . . 1551 1 59 . 1 1 15 15 LEU HB3 H 1 1.31 . . 2 . . . . . . . . 1551 1 60 . 1 1 15 15 LEU HG H 1 1.31 . . 1 . . . . . . . . 1551 1 61 . 1 1 15 15 LEU HD11 H 1 .52 . . 2 . . . . . . . . 1551 1 62 . 1 1 15 15 LEU HD12 H 1 .52 . . 2 . . . . . . . . 1551 1 63 . 1 1 15 15 LEU HD13 H 1 .52 . . 2 . . . . . . . . 1551 1 64 . 1 1 15 15 LEU HD21 H 1 .6 . . 2 . . . . . . . . 1551 1 65 . 1 1 15 15 LEU HD22 H 1 .6 . . 2 . . . . . . . . 1551 1 66 . 1 1 15 15 LEU HD23 H 1 .6 . . 2 . . . . . . . . 1551 1 67 . 1 1 16 16 ASP H H 1 8.19 . . 1 . . . . . . . . 1551 1 68 . 1 1 16 16 ASP HA H 1 4.71 . . 1 . . . . . . . . 1551 1 69 . 1 1 16 16 ASP HB2 H 1 2.14 . . 2 . . . . . . . . 1551 1 70 . 1 1 16 16 ASP HB3 H 1 2.42 . . 2 . . . . . . . . 1551 1 71 . 1 1 17 17 VAL H H 1 9 . . 1 . . . . . . . . 1551 1 72 . 1 1 17 17 VAL HA H 1 3.81 . . 1 . . . . . . . . 1551 1 73 . 1 1 17 17 VAL HB H 1 1.58 . . 1 . . . . . . . . 1551 1 74 . 1 1 17 17 VAL HG11 H 1 .58 . . 2 . . . . . . . . 1551 1 75 . 1 1 17 17 VAL HG12 H 1 .58 . . 2 . . . . . . . . 1551 1 76 . 1 1 17 17 VAL HG13 H 1 .58 . . 2 . . . . . . . . 1551 1 77 . 1 1 17 17 VAL HG21 H 1 .66 . . 2 . . . . . . . . 1551 1 78 . 1 1 17 17 VAL HG22 H 1 .66 . . 2 . . . . . . . . 1551 1 79 . 1 1 17 17 VAL HG23 H 1 .66 . . 2 . . . . . . . . 1551 1 80 . 1 1 18 18 ALA H H 1 8.4 . . 1 . . . . . . . . 1551 1 81 . 1 1 18 18 ALA HA H 1 3.92 . . 1 . . . . . . . . 1551 1 82 . 1 1 18 18 ALA HB1 H 1 1.1 . . 1 . . . . . . . . 1551 1 83 . 1 1 18 18 ALA HB2 H 1 1.1 . . 1 . . . . . . . . 1551 1 84 . 1 1 18 18 ALA HB3 H 1 1.1 . . 1 . . . . . . . . 1551 1 85 . 1 1 50 50 VAL H H 1 8.19 . . 1 . . . . . . . . 1551 1 86 . 1 1 50 50 VAL HA H 1 4.115 . . 1 . . . . . . . . 1551 1 87 . 1 1 51 51 TYR H H 1 8.945 . . 1 . . . . . . . . 1551 1 88 . 1 1 51 51 TYR HA H 1 4.96 . . 1 . . . . . . . . 1551 1 89 . 1 1 51 51 TYR HB2 H 1 2.62 . . 2 . . . . . . . . 1551 1 90 . 1 1 51 51 TYR HB3 H 1 2.69 . . 2 . . . . . . . . 1551 1 91 . 1 1 51 51 TYR HD1 H 1 6.63 . . 1 . . . . . . . . 1551 1 92 . 1 1 51 51 TYR HD2 H 1 6.63 . . 1 . . . . . . . . 1551 1 93 . 1 1 51 51 TYR HE1 H 1 6.65 . . 1 . . . . . . . . 1551 1 94 . 1 1 51 51 TYR HE2 H 1 6.65 . . 1 . . . . . . . . 1551 1 95 . 1 1 52 52 VAL H H 1 8.615 . . 1 . . . . . . . . 1551 1 96 . 1 1 52 52 VAL HA H 1 3.63 . . 1 . . . . . . . . 1551 1 97 . 1 1 52 52 VAL HB H 1 1.89 . . 1 . . . . . . . . 1551 1 98 . 1 1 52 52 VAL HG11 H 1 .66 . . 2 . . . . . . . . 1551 1 99 . 1 1 52 52 VAL HG12 H 1 .66 . . 2 . . . . . . . . 1551 1 100 . 1 1 52 52 VAL HG13 H 1 .66 . . 2 . . . . . . . . 1551 1 101 . 1 1 52 52 VAL HG21 H 1 .81 . . 2 . . . . . . . . 1551 1 102 . 1 1 52 52 VAL HG22 H 1 .81 . . 2 . . . . . . . . 1551 1 103 . 1 1 52 52 VAL HG23 H 1 .81 . . 2 . . . . . . . . 1551 1 104 . 1 1 53 53 ASN H H 1 8.26 . . 1 . . . . . . . . 1551 1 105 . 1 1 53 53 ASN HA H 1 4.28 . . 1 . . . . . . . . 1551 1 106 . 1 1 53 53 ASN HB2 H 1 2.57 . . 2 . . . . . . . . 1551 1 107 . 1 1 53 53 ASN HB3 H 1 2.79 . . 2 . . . . . . . . 1551 1 108 . 1 1 53 53 ASN HD21 H 1 8.04 . . 1 . . . . . . . . 1551 1 109 . 1 1 53 53 ASN HD22 H 1 8.04 . . 1 . . . . . . . . 1551 1 110 . 1 1 56 56 PHE H H 1 8.66 . . 1 . . . . . . . . 1551 1 111 . 1 1 56 56 PHE HA H 1 4.26 . . 1 . . . . . . . . 1551 1 112 . 1 1 56 56 PHE HB2 H 1 2.98 . . 2 . . . . . . . . 1551 1 113 . 1 1 56 56 PHE HB3 H 1 2.57 . . 2 . . . . . . . . 1551 1 114 . 1 1 56 56 PHE HD1 H 1 6.96 . . 1 . . . . . . . . 1551 1 115 . 1 1 56 56 PHE HD2 H 1 6.96 . . 1 . . . . . . . . 1551 1 116 . 1 1 56 56 PHE HE1 H 1 7.1 . . 1 . . . . . . . . 1551 1 117 . 1 1 56 56 PHE HE2 H 1 7.1 . . 1 . . . . . . . . 1551 1 118 . 1 1 56 56 PHE HZ H 1 7 . . 1 . . . . . . . . 1551 1 119 . 1 1 76 76 ALA H H 1 7.62 . . 1 . . . . . . . . 1551 1 120 . 1 1 76 76 ALA HA H 1 4.38 . . 1 . . . . . . . . 1551 1 121 . 1 1 76 76 ALA HB1 H 1 1.41 . . 1 . . . . . . . . 1551 1 122 . 1 1 76 76 ALA HB2 H 1 1.41 . . 1 . . . . . . . . 1551 1 123 . 1 1 76 76 ALA HB3 H 1 1.41 . . 1 . . . . . . . . 1551 1 124 . 1 1 77 77 GLU H H 1 7.91 . . 1 . . . . . . . . 1551 1 125 . 1 1 77 77 GLU HA H 1 3.71 . . 1 . . . . . . . . 1551 1 126 . 1 1 77 77 GLU HB2 H 1 1.58 . . 2 . . . . . . . . 1551 1 127 . 1 1 77 77 GLU HB3 H 1 1.81 . . 2 . . . . . . . . 1551 1 128 . 1 1 77 77 GLU HG2 H 1 2.09 . . 2 . . . . . . . . 1551 1 129 . 1 1 77 77 GLU HG3 H 1 2.26 . . 2 . . . . . . . . 1551 1 130 . 1 1 78 78 LEU H H 1 8.49 . . 1 . . . . . . . . 1551 1 131 . 1 1 78 78 LEU HA H 1 4.41 . . 1 . . . . . . . . 1551 1 132 . 1 1 78 78 LEU HB2 H 1 1.58 . . 2 . . . . . . . . 1551 1 133 . 1 1 78 78 LEU HB3 H 1 1.59 . . 2 . . . . . . . . 1551 1 134 . 1 1 78 78 LEU HG H 1 1.17 . . 1 . . . . . . . . 1551 1 135 . 1 1 78 78 LEU HD11 H 1 .67 . . 2 . . . . . . . . 1551 1 136 . 1 1 78 78 LEU HD12 H 1 .67 . . 2 . . . . . . . . 1551 1 137 . 1 1 78 78 LEU HD13 H 1 .67 . . 2 . . . . . . . . 1551 1 138 . 1 1 78 78 LEU HD21 H 1 .82 . . 2 . . . . . . . . 1551 1 139 . 1 1 78 78 LEU HD22 H 1 .82 . . 2 . . . . . . . . 1551 1 140 . 1 1 78 78 LEU HD23 H 1 .82 . . 2 . . . . . . . . 1551 1 141 . 1 1 79 79 LYS H H 1 9.71 . . 1 . . . . . . . . 1551 1 142 . 1 1 79 79 LYS HA H 1 4.8 . . 1 . . . . . . . . 1551 1 143 . 1 1 79 79 LYS HB2 H 1 1.58 . . 2 . . . . . . . . 1551 1 144 . 1 1 79 79 LYS HB3 H 1 1.73 . . 2 . . . . . . . . 1551 1 145 . 1 1 79 79 LYS HG2 H 1 .93 . . 2 . . . . . . . . 1551 1 146 . 1 1 79 79 LYS HG3 H 1 1.07 . . 2 . . . . . . . . 1551 1 147 . 1 1 79 79 LYS HD2 H 1 1.81 . . 2 . . . . . . . . 1551 1 148 . 1 1 79 79 LYS HD3 H 1 1.95 . . 2 . . . . . . . . 1551 1 149 . 1 1 79 79 LYS HE2 H 1 2.28 . . 1 . . . . . . . . 1551 1 150 . 1 1 79 79 LYS HE3 H 1 2.28 . . 1 . . . . . . . . 1551 1 151 . 1 1 80 80 PRO HA H 1 4.24 . . 1 . . . . . . . . 1551 1 152 . 1 1 80 80 PRO HB2 H 1 1.76 . . 2 . . . . . . . . 1551 1 153 . 1 1 80 80 PRO HB3 H 1 2.28 . . 2 . . . . . . . . 1551 1 154 . 1 1 80 80 PRO HG2 H 1 1.83 . . 2 . . . . . . . . 1551 1 155 . 1 1 80 80 PRO HG3 H 1 2.14 . . 2 . . . . . . . . 1551 1 156 . 1 1 80 80 PRO HD2 H 1 3.7 . . 2 . . . . . . . . 1551 1 157 . 1 1 80 80 PRO HD3 H 1 3.52 . . 2 . . . . . . . . 1551 1 158 . 1 1 81 81 ASN H H 1 8.62 . . 1 . . . . . . . . 1551 1 159 . 1 1 81 81 ASN HA H 1 4.68 . . 1 . . . . . . . . 1551 1 160 . 1 1 81 81 ASN HB2 H 1 2.58 . . 2 . . . . . . . . 1551 1 161 . 1 1 81 81 ASN HB3 H 1 2.71 . . 2 . . . . . . . . 1551 1 162 . 1 1 81 81 ASN HD21 H 1 6.545 . . 2 . . . . . . . . 1551 1 163 . 1 1 81 81 ASN HD22 H 1 7.45 . . 2 . . . . . . . . 1551 1 164 . 1 1 82 82 SER H H 1 7.985 . . 1 . . . . . . . . 1551 1 165 . 1 1 82 82 SER HA H 1 5.03 . . 1 . . . . . . . . 1551 1 166 . 1 1 82 82 SER HB2 H 1 3.95 . . 2 . . . . . . . . 1551 1 167 . 1 1 82 82 SER HB3 H 1 4 . . 2 . . . . . . . . 1551 1 168 . 1 1 82 82 SER HG H 1 10.095 . . 1 . . . . . . . . 1551 1 169 . 1 1 83 83 ARG H H 1 9.375 . . 1 . . . . . . . . 1551 1 170 . 1 1 83 83 ARG HA H 1 4.65 . . 1 . . . . . . . . 1551 1 171 . 1 1 83 83 ARG HB2 H 1 1.02 . . 2 . . . . . . . . 1551 1 172 . 1 1 83 83 ARG HB3 H 1 1.05 . . 2 . . . . . . . . 1551 1 173 . 1 1 83 83 ARG HG2 H 1 1.22 . . 2 . . . . . . . . 1551 1 174 . 1 1 83 83 ARG HG3 H 1 1.56 . . 2 . . . . . . . . 1551 1 175 . 1 1 83 83 ARG HD2 H 1 3.08 . . 2 . . . . . . . . 1551 1 176 . 1 1 83 83 ARG HD3 H 1 3.39 . . 2 . . . . . . . . 1551 1 177 . 1 1 83 83 ARG HE H 1 10.29 . . 1 . . . . . . . . 1551 1 178 . 1 1 96 96 GLY H H 1 9.64 . . 1 . . . . . . . . 1551 1 179 . 1 1 96 96 GLY HA2 H 1 2.82 . . 2 . . . . . . . . 1551 1 180 . 1 1 96 96 GLY HA3 H 1 4.02 . . 2 . . . . . . . . 1551 1 181 . 1 1 97 97 ILE H H 1 7.77 . . 1 . . . . . . . . 1551 1 182 . 1 1 97 97 ILE HA H 1 1.03 . . 1 . . . . . . . . 1551 1 183 . 1 1 97 97 ILE HB H 1 .46 . . 1 . . . . . . . . 1551 1 184 . 1 1 97 97 ILE HG12 H 1 .64 . . 2 . . . . . . . . 1551 1 185 . 1 1 97 97 ILE HG13 H 1 1.34 . . 2 . . . . . . . . 1551 1 186 . 1 1 97 97 ILE HG21 H 1 1.1 . . 1 . . . . . . . . 1551 1 187 . 1 1 97 97 ILE HG22 H 1 1.1 . . 1 . . . . . . . . 1551 1 188 . 1 1 97 97 ILE HG23 H 1 1.1 . . 1 . . . . . . . . 1551 1 189 . 1 1 97 97 ILE HD11 H 1 .36 . . 1 . . . . . . . . 1551 1 190 . 1 1 97 97 ILE HD12 H 1 .36 . . 1 . . . . . . . . 1551 1 191 . 1 1 97 97 ILE HD13 H 1 .36 . . 1 . . . . . . . . 1551 1 192 . 1 1 98 98 VAL H H 1 4.88 . . 1 . . . . . . . . 1551 1 193 . 1 1 98 98 VAL HA H 1 4.48 . . 1 . . . . . . . . 1551 1 194 . 1 1 98 98 VAL HB H 1 1.39 . . 1 . . . . . . . . 1551 1 195 . 1 1 98 98 VAL HG11 H 1 .61 . . 2 . . . . . . . . 1551 1 196 . 1 1 98 98 VAL HG12 H 1 .61 . . 2 . . . . . . . . 1551 1 197 . 1 1 98 98 VAL HG13 H 1 .61 . . 2 . . . . . . . . 1551 1 198 . 1 1 98 98 VAL HG21 H 1 .75 . . 2 . . . . . . . . 1551 1 199 . 1 1 98 98 VAL HG22 H 1 .75 . . 2 . . . . . . . . 1551 1 200 . 1 1 98 98 VAL HG23 H 1 .75 . . 2 . . . . . . . . 1551 1 201 . 1 1 99 99 VAL H H 1 8.59 . . 1 . . . . . . . . 1551 1 202 . 1 1 99 99 VAL HA H 1 4.75 . . 1 . . . . . . . . 1551 1 203 . 1 1 99 99 VAL HB H 1 1.48 . . 1 . . . . . . . . 1551 1 204 . 1 1 99 99 VAL HG11 H 1 .3 . . 2 . . . . . . . . 1551 1 205 . 1 1 99 99 VAL HG12 H 1 .3 . . 2 . . . . . . . . 1551 1 206 . 1 1 99 99 VAL HG13 H 1 .3 . . 2 . . . . . . . . 1551 1 207 . 1 1 99 99 VAL HG21 H 1 .36 . . 2 . . . . . . . . 1551 1 208 . 1 1 99 99 VAL HG22 H 1 .36 . . 2 . . . . . . . . 1551 1 209 . 1 1 99 99 VAL HG23 H 1 .36 . . 2 . . . . . . . . 1551 1 210 . 1 1 100 100 ASP H H 1 8.825 . . 1 . . . . . . . . 1551 1 211 . 1 1 100 100 ASP HA H 1 5.28 . . 1 . . . . . . . . 1551 1 212 . 1 1 100 100 ASP HB2 H 1 2.5 . . 1 . . . . . . . . 1551 1 213 . 1 1 100 100 ASP HB3 H 1 2.5 . . 1 . . . . . . . . 1551 1 214 . 1 1 101 101 VAL H H 1 8.96 . . 1 . . . . . . . . 1551 1 215 . 1 1 101 101 VAL HA H 1 4.23 . . 1 . . . . . . . . 1551 1 216 . 1 1 101 101 VAL HB H 1 1.88 . . 1 . . . . . . . . 1551 1 217 . 1 1 101 101 VAL HG11 H 1 .58 . . 2 . . . . . . . . 1551 1 218 . 1 1 101 101 VAL HG12 H 1 .58 . . 2 . . . . . . . . 1551 1 219 . 1 1 101 101 VAL HG13 H 1 .58 . . 2 . . . . . . . . 1551 1 220 . 1 1 101 101 VAL HG21 H 1 .72 . . 2 . . . . . . . . 1551 1 221 . 1 1 101 101 VAL HG22 H 1 .72 . . 2 . . . . . . . . 1551 1 222 . 1 1 101 101 VAL HG23 H 1 .72 . . 2 . . . . . . . . 1551 1 stop_ save_