data_7278 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 7278 _Entry.Title ; Backbone amide chemical shifts for iG80b E. coli RNase H ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2006-08-28 _Entry.Accession_date 2006-08-29 _Entry.Last_release_date 2007-10-09 _Entry.Original_release_date 2007-10-09 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _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 Joel Butterwick . A. . 7278 2 Arthur Palmer . G. III 7278 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 7278 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 67 7278 '1H chemical shifts' 67 7278 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2007-10-09 2006-08-28 original author . 7278 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID . 5918 'non-mutant protein' 7278 . 7277 'dG85 ttRNH' 7278 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 7278 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 17088323 _Citation.Full_citation . _Citation.Title 'An inserted Gly residue fine tunes dynamics between mesophilc and thermophilic ribonucleases H' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full . _Citation.Journal_volume 15 _Citation.Journal_issue 12 _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 2697 _Citation.Page_last 2707 _Citation.Year 2006 _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 Joel Butterwick . A. . 7278 1 2 Arthur Palmer . G. III 7278 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 7278 _Assembly.ID 1 _Assembly.Name 'iG80b ecRNH' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 0 _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states no _Assembly.Ambiguous_chem_comp_sites no _Assembly.Molecules_in_chemical_exchange no _Assembly.Paramagnetic no _Assembly.Thiol_state 'all free' _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 'iG80b ecRNH' 1 $iG80b_ecRNH . . yes native no no . . . 7278 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_iG80b_ecRNH _Entity.Sf_category entity _Entity.Sf_framecode iG80b_ecRNH _Entity.Entry_ID 7278 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'iG80b ecRNH' _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 ; MLKQVEIFTDGSCLGNPGPG GYGAILRYRGREKTFSAGYT RTTNNRMELMAAIVALEALK EHCEVILSTDSQYVRQGITQ GWIHNWKKRGWKTADKKPVK NVDLWQRLDAALGQHQIKWE WVKGHAGHPENERCDELARA AAMNPTLEDTGYQVEV ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 156 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _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 1657 . "ribonuclease H" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 2 no BMRB 4012 . RNase_H1 . . . . . 100.00 155 97.44 97.44 1.11e-106 . . . . 7278 1 3 no PDB 1F21 . "Divalent Metal Cofactor Binding In The Kinetic Folding Trajectory Of E. Coli Ribonuclease Hi" . . . . . 100.00 155 97.44 97.44 1.11e-106 . . . . 7278 1 4 no PDB 1GOA . "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" . . . . . 100.00 156 100.00 100.00 4.06e-112 . . . . 7278 1 5 no PDB 1GOB . "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" . . . . . 100.00 155 98.72 98.72 6.85e-109 . . . . 7278 1 6 no PDB 1GOC . "Cooperative Stabilization Of Escherichia Coli Ribonuclease Hi By Insertion Of Gly-80b And Gly-77-> Ala Substitution" . . . . . 100.00 156 99.36 99.36 2.18e-111 . . . . 7278 1 7 no PDB 1KVA . "E. Coli Ribonuclease Hi D134a Mutant" . . . . . 100.00 155 98.72 98.72 1.57e-108 . . . . 7278 1 8 no PDB 1KVB . "E. Coli Ribonuclease Hi D134h Mutant" . . . . . 100.00 155 98.72 98.72 2.11e-108 . . . . 7278 1 9 no PDB 1KVC . "E. Coli Ribonuclease Hi D134n Mutant" . . . . . 100.00 155 98.72 99.36 6.70e-109 . . . . 7278 1 10 no PDB 1LAV . "Stabilization Of Escherichia Coli Ribonuclease Hi By Cavity- Filling Mutations Within A Hydrophobic Core" . . . . . 100.00 155 98.72 99.36 3.96e-109 . . . . 7278 1 11 no PDB 1LAW . "Stabilization Of Escherichia Coli Ribonuclease Hi By Cavity- Filling Mutations Within A Hydrophobic Core" . . . . . 100.00 155 98.72 99.36 2.15e-109 . . . . 7278 1 12 no PDB 1RBR . "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" . . . . . 100.00 155 98.72 98.72 4.44e-108 . . . . 7278 1 13 no PDB 1RBS . "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" . . . . . 100.00 155 98.72 98.72 2.57e-108 . . . . 7278 1 14 no PDB 1RBT . "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" . . . . . 100.00 155 98.72 98.72 1.93e-108 . . . . 7278 1 15 no PDB 1RBU . "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" . . . . . 100.00 155 98.72 98.72 9.61e-109 . . . . 7278 1 16 no PDB 1RBV . "Structural Study Of Mutants Of Escherichia Coli Ribonuclease Hi With Enhanced Thermostability" . . . . . 100.00 155 98.72 98.72 9.71e-109 . . . . 7278 1 17 no PDB 1RCH . "Solution Nmr Structure Of Ribonuclease Hi From Escherichia Coli, 8 Structures" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 18 no PDB 1RDA . "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" . . . . . 100.00 155 98.72 99.36 6.70e-109 . . . . 7278 1 19 no PDB 1RDB . "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" . . . . . 100.00 155 98.72 99.36 3.79e-109 . . . . 7278 1 20 no PDB 1RDC . "Crystal Structures Of Ribonuclease Hi Active Site Mutants From Escherichia Coli" . . . . . 100.00 155 98.72 99.36 6.70e-109 . . . . 7278 1 21 no PDB 1RDD . "Crystal Structure Of Escherichia Coli Rnase Hi In Complex With Mg2+ At 2.8 Angstroms Resolution: Proof For A Single Mg2+ Site" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 22 no PDB 1RNH . "Structure Of Ribonuclease H Phased At 2 Angstroms Resolution By Mad Analysis Of The Selenomethionyl Protein" . . . . . 99.36 155 97.42 97.42 1.93e-105 . . . . 7278 1 23 no PDB 1WSE . "Co-Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48a) With Mn2+" . . . . . 100.00 155 98.08 98.08 5.28e-108 . . . . 7278 1 24 no PDB 1WSF . "Co-crystal Structure Of E.coli Rnase Hi Active Site Mutant (d134a*) With Mn2+" . . . . . 100.00 155 98.08 98.08 9.64e-108 . . . . 7278 1 25 no PDB 1WSG . "Co-Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48aD134N) WITH MN2+" . . . . . 100.00 155 97.44 98.08 2.39e-107 . . . . 7278 1 26 no PDB 1WSH . "Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48aK87A)" . . . . . 100.00 155 98.08 98.08 5.28e-108 . . . . 7278 1 27 no PDB 1WSI . "Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (E48aK87AD134N)" . . . . . 100.00 155 97.44 98.08 2.39e-107 . . . . 7278 1 28 no PDB 1WSJ . "Crystal Structure Of E.Coli Rnase Hi Active Site Mutant (K87aH124A)" . . . . . 100.00 155 98.08 98.08 1.38e-107 . . . . 7278 1 29 no PDB 2RN2 . "Structural Details Of Ribonuclease H From Escherichia Coli As Refined To An Atomic Resolution" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 30 no PDB 3AA2 . "A52i E. Coli Rnase Hi" . . . . . 100.00 155 98.72 98.72 8.33e-109 . . . . 7278 1 31 no PDB 3AA3 . "A52l E. Coli Rnase Hi" . . . . . 100.00 155 98.72 98.72 8.52e-109 . . . . 7278 1 32 no PDB 3AA4 . "A52v E.Coli Rnase Hi" . . . . . 100.00 155 98.72 98.72 5.87e-109 . . . . 7278 1 33 no PDB 3AA5 . "A52f E.Coli Rnase Hi" . . . . . 100.00 155 98.72 98.72 9.50e-109 . . . . 7278 1 34 no DBJ BAA77885 . "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K-12 substr. W3110]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 35 no DBJ BAB33633 . "RNase HI [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 36 no DBJ BAG75734 . "ribonuclease H [Escherichia coli SE11]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 37 no DBJ BAI23570 . "ribonuclease HI [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 38 no DBJ BAI29084 . "ribonuclease HI [Escherichia coli O103:H2 str. 12009]" . . . . . 100.00 155 98.72 99.36 6.70e-109 . . . . 7278 1 39 no EMBL CAA23620 . "ribonuclease H [Escherichia coli]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 40 no EMBL CAA27660 . "unnamed protein product [Escherichia coli]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 41 no EMBL CAP74778 . "ribonuclease HI [Escherichia coli LF82]" . . . . . 100.00 155 98.72 98.72 1.39e-108 . . . . 7278 1 42 no EMBL CAQ30729 . "RNase HI, degrades RNA of DNA-RNA hybrids, participates in DNA replication [Escherichia coli BL21(DE3)]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 43 no EMBL CAQ87812 . "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia fergusonii ATCC 35469]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 44 no GB AAA24565 . "ribonuclease H [Escherichia coli]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 45 no GB AAB08636 . "ribonuclease H [Escherichia coli]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 46 no GB AAC73319 . "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 47 no GB AAG54510 . "RNase HI, degrades RNA of DNA-RNA hybrids, participates in DNA replication [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 48 no GB AAN41862 . "RNase HI [Shigella flexneri 2a str. 301]" . . . . . 100.00 192 99.36 99.36 6.09e-110 . . . . 7278 1 49 no REF NP_285902 . "ribonuclease H [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 50 no REF NP_308237 . "ribonuclease H [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 51 no REF NP_414750 . "ribonuclease HI, degrades RNA of DNA-RNA hybrids [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 52 no REF NP_706155 . "RNase HI [Shigella flexneri 2a str. 301]" . . . . . 100.00 192 99.36 99.36 6.09e-110 . . . . 7278 1 53 no REF NP_752197 . "ribonuclease H [Escherichia coli CFT073]" . . . . . 100.00 155 98.72 99.36 6.27e-109 . . . . 7278 1 54 no SP A7ZHV1 . "RecName: Full=Ribonuclease H; Short=RNase H [Escherichia coli E24377A]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 55 no SP A7ZWF6 . "RecName: Full=Ribonuclease H; Short=RNase H [Escherichia coli HS]" . . . . . 100.00 155 98.72 99.36 6.70e-109 . . . . 7278 1 56 no SP B1IPU4 . "RecName: Full=Ribonuclease H; Short=RNase H [Escherichia coli ATCC 8739]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 57 no SP B1LHM3 . "RecName: Full=Ribonuclease H; Short=RNase H [Escherichia coli SMS-3-5]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 1 58 no SP B1XD78 . "RecName: Full=Ribonuclease H; Short=RNase H [Escherichia coli str. K-12 substr. DH10B]" . . . . . 100.00 155 99.36 99.36 1.45e-109 . . . . 7278 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 . 7278 1 2 . LEU . 7278 1 3 . LYS . 7278 1 4 . GLN . 7278 1 5 . VAL . 7278 1 6 . GLU . 7278 1 7 . ILE . 7278 1 8 . PHE . 7278 1 9 . THR . 7278 1 10 . ASP . 7278 1 11 . GLY . 7278 1 12 . SER . 7278 1 13 . CYS . 7278 1 14 . LEU . 7278 1 15 . GLY . 7278 1 16 . ASN . 7278 1 17 . PRO . 7278 1 18 . GLY . 7278 1 19 . PRO . 7278 1 20 . GLY . 7278 1 21 . GLY . 7278 1 22 . TYR . 7278 1 23 . GLY . 7278 1 24 . ALA . 7278 1 25 . ILE . 7278 1 26 . LEU . 7278 1 27 . ARG . 7278 1 28 . TYR . 7278 1 29 . ARG . 7278 1 30 . GLY . 7278 1 31 . ARG . 7278 1 32 . GLU . 7278 1 33 . LYS . 7278 1 34 . THR . 7278 1 35 . PHE . 7278 1 36 . SER . 7278 1 37 . ALA . 7278 1 38 . GLY . 7278 1 39 . TYR . 7278 1 40 . THR . 7278 1 41 . ARG . 7278 1 42 . THR . 7278 1 43 . THR . 7278 1 44 . ASN . 7278 1 45 . ASN . 7278 1 46 . ARG . 7278 1 47 . MET . 7278 1 48 . GLU . 7278 1 49 . LEU . 7278 1 50 . MET . 7278 1 51 . ALA . 7278 1 52 . ALA . 7278 1 53 . ILE . 7278 1 54 . VAL . 7278 1 55 . ALA . 7278 1 56 . LEU . 7278 1 57 . GLU . 7278 1 58 . ALA . 7278 1 59 . LEU . 7278 1 60 . LYS . 7278 1 61 . GLU . 7278 1 62 . HIS . 7278 1 63 . CYS . 7278 1 64 . GLU . 7278 1 65 . VAL . 7278 1 66 . ILE . 7278 1 67 . LEU . 7278 1 68 . SER . 7278 1 69 . THR . 7278 1 70 . ASP . 7278 1 71 . SER . 7278 1 72 . GLN . 7278 1 73 . TYR . 7278 1 74 . VAL . 7278 1 75 . ARG . 7278 1 76 . GLN . 7278 1 77 . GLY . 7278 1 78 . ILE . 7278 1 79 . THR . 7278 1 80 . GLN . 7278 1 81 . GLY . 7278 1 82 . TRP . 7278 1 83 . ILE . 7278 1 84 . HIS . 7278 1 85 . ASN . 7278 1 86 . TRP . 7278 1 87 . LYS . 7278 1 88 . LYS . 7278 1 89 . ARG . 7278 1 90 . GLY . 7278 1 91 . TRP . 7278 1 92 . LYS . 7278 1 93 . THR . 7278 1 94 . ALA . 7278 1 95 . ASP . 7278 1 96 . LYS . 7278 1 97 . LYS . 7278 1 98 . PRO . 7278 1 99 . VAL . 7278 1 100 . LYS . 7278 1 101 . ASN . 7278 1 102 . VAL . 7278 1 103 . ASP . 7278 1 104 . LEU . 7278 1 105 . TRP . 7278 1 106 . GLN . 7278 1 107 . ARG . 7278 1 108 . LEU . 7278 1 109 . ASP . 7278 1 110 . ALA . 7278 1 111 . ALA . 7278 1 112 . LEU . 7278 1 113 . GLY . 7278 1 114 . GLN . 7278 1 115 . HIS . 7278 1 116 . GLN . 7278 1 117 . ILE . 7278 1 118 . LYS . 7278 1 119 . TRP . 7278 1 120 . GLU . 7278 1 121 . TRP . 7278 1 122 . VAL . 7278 1 123 . LYS . 7278 1 124 . GLY . 7278 1 125 . HIS . 7278 1 126 . ALA . 7278 1 127 . GLY . 7278 1 128 . HIS . 7278 1 129 . PRO . 7278 1 130 . GLU . 7278 1 131 . ASN . 7278 1 132 . GLU . 7278 1 133 . ARG . 7278 1 134 . CYS . 7278 1 135 . ASP . 7278 1 136 . GLU . 7278 1 137 . LEU . 7278 1 138 . ALA . 7278 1 139 . ARG . 7278 1 140 . ALA . 7278 1 141 . ALA . 7278 1 142 . ALA . 7278 1 143 . MET . 7278 1 144 . ASN . 7278 1 145 . PRO . 7278 1 146 . THR . 7278 1 147 . LEU . 7278 1 148 . GLU . 7278 1 149 . ASP . 7278 1 150 . THR . 7278 1 151 . GLY . 7278 1 152 . TYR . 7278 1 153 . GLN . 7278 1 154 . VAL . 7278 1 155 . GLU . 7278 1 156 . VAL . 7278 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 7278 1 . LEU 2 2 7278 1 . LYS 3 3 7278 1 . GLN 4 4 7278 1 . VAL 5 5 7278 1 . GLU 6 6 7278 1 . ILE 7 7 7278 1 . PHE 8 8 7278 1 . THR 9 9 7278 1 . ASP 10 10 7278 1 . GLY 11 11 7278 1 . SER 12 12 7278 1 . CYS 13 13 7278 1 . LEU 14 14 7278 1 . GLY 15 15 7278 1 . ASN 16 16 7278 1 . PRO 17 17 7278 1 . GLY 18 18 7278 1 . PRO 19 19 7278 1 . GLY 20 20 7278 1 . GLY 21 21 7278 1 . TYR 22 22 7278 1 . GLY 23 23 7278 1 . ALA 24 24 7278 1 . ILE 25 25 7278 1 . LEU 26 26 7278 1 . ARG 27 27 7278 1 . TYR 28 28 7278 1 . ARG 29 29 7278 1 . GLY 30 30 7278 1 . ARG 31 31 7278 1 . GLU 32 32 7278 1 . LYS 33 33 7278 1 . THR 34 34 7278 1 . PHE 35 35 7278 1 . SER 36 36 7278 1 . ALA 37 37 7278 1 . GLY 38 38 7278 1 . TYR 39 39 7278 1 . THR 40 40 7278 1 . ARG 41 41 7278 1 . THR 42 42 7278 1 . THR 43 43 7278 1 . ASN 44 44 7278 1 . ASN 45 45 7278 1 . ARG 46 46 7278 1 . MET 47 47 7278 1 . GLU 48 48 7278 1 . LEU 49 49 7278 1 . MET 50 50 7278 1 . ALA 51 51 7278 1 . ALA 52 52 7278 1 . ILE 53 53 7278 1 . VAL 54 54 7278 1 . ALA 55 55 7278 1 . LEU 56 56 7278 1 . GLU 57 57 7278 1 . ALA 58 58 7278 1 . LEU 59 59 7278 1 . LYS 60 60 7278 1 . GLU 61 61 7278 1 . HIS 62 62 7278 1 . CYS 63 63 7278 1 . GLU 64 64 7278 1 . VAL 65 65 7278 1 . ILE 66 66 7278 1 . LEU 67 67 7278 1 . SER 68 68 7278 1 . THR 69 69 7278 1 . ASP 70 70 7278 1 . SER 71 71 7278 1 . GLN 72 72 7278 1 . TYR 73 73 7278 1 . VAL 74 74 7278 1 . ARG 75 75 7278 1 . GLN 76 76 7278 1 . GLY 77 77 7278 1 . ILE 78 78 7278 1 . THR 79 79 7278 1 . GLN 80 80 7278 1 . GLY 81 81 7278 1 . TRP 82 82 7278 1 . ILE 83 83 7278 1 . HIS 84 84 7278 1 . ASN 85 85 7278 1 . TRP 86 86 7278 1 . LYS 87 87 7278 1 . LYS 88 88 7278 1 . ARG 89 89 7278 1 . GLY 90 90 7278 1 . TRP 91 91 7278 1 . LYS 92 92 7278 1 . THR 93 93 7278 1 . ALA 94 94 7278 1 . ASP 95 95 7278 1 . LYS 96 96 7278 1 . LYS 97 97 7278 1 . PRO 98 98 7278 1 . VAL 99 99 7278 1 . LYS 100 100 7278 1 . ASN 101 101 7278 1 . VAL 102 102 7278 1 . ASP 103 103 7278 1 . LEU 104 104 7278 1 . TRP 105 105 7278 1 . GLN 106 106 7278 1 . ARG 107 107 7278 1 . LEU 108 108 7278 1 . ASP 109 109 7278 1 . ALA 110 110 7278 1 . ALA 111 111 7278 1 . LEU 112 112 7278 1 . GLY 113 113 7278 1 . GLN 114 114 7278 1 . HIS 115 115 7278 1 . GLN 116 116 7278 1 . ILE 117 117 7278 1 . LYS 118 118 7278 1 . TRP 119 119 7278 1 . GLU 120 120 7278 1 . TRP 121 121 7278 1 . VAL 122 122 7278 1 . LYS 123 123 7278 1 . GLY 124 124 7278 1 . HIS 125 125 7278 1 . ALA 126 126 7278 1 . GLY 127 127 7278 1 . HIS 128 128 7278 1 . PRO 129 129 7278 1 . GLU 130 130 7278 1 . ASN 131 131 7278 1 . GLU 132 132 7278 1 . ARG 133 133 7278 1 . CYS 134 134 7278 1 . ASP 135 135 7278 1 . GLU 136 136 7278 1 . LEU 137 137 7278 1 . ALA 138 138 7278 1 . ARG 139 139 7278 1 . ALA 140 140 7278 1 . ALA 141 141 7278 1 . ALA 142 142 7278 1 . MET 143 143 7278 1 . ASN 144 144 7278 1 . PRO 145 145 7278 1 . THR 146 146 7278 1 . LEU 147 147 7278 1 . GLU 148 148 7278 1 . ASP 149 149 7278 1 . THR 150 150 7278 1 . GLY 151 151 7278 1 . TYR 152 152 7278 1 . GLN 153 153 7278 1 . VAL 154 154 7278 1 . GLU 155 155 7278 1 . VAL 156 156 7278 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 7278 _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 $iG80b_ecRNH . 562 organism no 'Escherichia coli' 'E. coli' . . Eubacteria Protista Escherichia coli . . . . . . . . . . . . . . . . . . . . . 7278 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 7278 _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 $iG80b_ecRNH . 'recombinant technology' . . . . Escherichia coli BL21(DE3) . . . . . . . . . . . . . . . . . . . . . . 7278 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 7278 _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 . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'iG80b ecRNH' '[U-2H; U-15N]' . . 1 $iG80b_ecRNH . protein 1.0 . . mM 0.1 . . . 7278 1 stop_ save_ ####################### # Sample conditions # ####################### save_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions_1 _Sample_condition_list.Entry_ID 7278 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 100 1 mM 7278 1 pH 5.5 0.1 pH 7278 1 temperature 300 1 K 7278 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_700MHz_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode 700MHz_spectrometer _NMR_spectrometer.Entry_ID 7278 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AV _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ ############################# # NMR applied experiments # ############################# save_NMR_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode NMR_experiment_list _Experiment_list.Entry_ID 7278 _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 '1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . 1 $700MHz_spectrometer . . . . . . . . . . . . . . . . 7278 1 2 HMQC-NOESY-HSQC no . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . 1 $700MHz_spectrometer . . . . . . . . . . . . . . . . 7278 1 stop_ save_ save_1H-15N_HSQC _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode 1H-15N_HSQC _NMR_spec_expt.Entry_ID 7278 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $700MHz_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_HMQC-NOESY-HSQC _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode HMQC-NOESY-HSQC _NMR_spec_expt.Entry_ID 7278 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name HMQC-NOESY-HSQC _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $700MHz_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_referencing _Chem_shift_reference.Entry_ID 7278 _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 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . 1 $entry_citation . . 1 $entry_citation 7278 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . 1 $entry_citation . . 1 $entry_citation 7278 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_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 7278 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_referencing _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 '1H-15N HSQC' 1 $sample_1 isotropic 7278 1 2 HMQC-NOESY-HSQC 1 $sample_1 isotropic 7278 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 2 2 LEU H H 1 8.698 0.01 . 1 . . . . 2 L HN . 7278 1 2 . 1 1 2 2 LEU N N 15 125.722 0.1 . 1 . . . . 2 L N . 7278 1 3 . 1 1 3 3 LYS H H 1 8.720 0.01 . 1 . . . . 3 K HN . 7278 1 4 . 1 1 3 3 LYS N N 15 124.362 0.1 . 1 . . . . 3 K N . 7278 1 5 . 1 1 4 4 GLN H H 1 8.300 0.01 . 1 . . . . 4 Q HN . 7278 1 6 . 1 1 4 4 GLN N N 15 123.183 0.1 . 1 . . . . 4 Q N . 7278 1 7 . 1 1 5 5 VAL H H 1 8.763 0.01 . 1 . . . . 5 V HN . 7278 1 8 . 1 1 5 5 VAL N N 15 122.661 0.1 . 1 . . . . 5 V N . 7278 1 9 . 1 1 6 6 GLU H H 1 8.627 0.01 . 1 . . . . 6 E HN . 7278 1 10 . 1 1 6 6 GLU N N 15 124.813 0.1 . 1 . . . . 6 E N . 7278 1 11 . 1 1 7 7 ILE H H 1 8.549 0.01 . 1 . . . . 7 I HN . 7278 1 12 . 1 1 7 7 ILE N N 15 122.330 0.1 . 1 . . . . 7 I N . 7278 1 13 . 1 1 8 8 PHE H H 1 9.190 0.01 . 1 . . . . 8 F HN . 7278 1 14 . 1 1 8 8 PHE N N 15 128.929 0.1 . 1 . . . . 8 F N . 7278 1 15 . 1 1 9 9 THR H H 1 8.102 0.01 . 1 . . . . 9 T HN . 7278 1 16 . 1 1 9 9 THR N N 15 110.369 0.1 . 1 . . . . 9 T N . 7278 1 17 . 1 1 10 10 ASP H H 1 9.072 0.01 . 1 . . . . 10 D HN . 7278 1 18 . 1 1 10 10 ASP N N 15 121.772 0.1 . 1 . . . . 10 D N . 7278 1 19 . 1 1 11 11 GLY H H 1 8.684 0.01 . 1 . . . . 11 G HN . 7278 1 20 . 1 1 11 11 GLY N N 15 107.621 0.1 . 1 . . . . 11 G N . 7278 1 21 . 1 1 12 12 SER H H 1 8.821 0.01 . 1 . . . . 12 S HN . 7278 1 22 . 1 1 12 12 SER N N 15 114.518 0.1 . 1 . . . . 12 S N . 7278 1 23 . 1 1 13 13 CYS H H 1 8.467 0.01 . 1 . . . . 13 C HN . 7278 1 24 . 1 1 13 13 CYS N N 15 123.754 0.1 . 1 . . . . 13 C N . 7278 1 25 . 1 1 14 14 LEU H H 1 9.047 0.01 . 1 . . . . 14 L HN . 7278 1 26 . 1 1 14 14 LEU N N 15 128.999 0.1 . 1 . . . . 14 L N . 7278 1 27 . 1 1 15 15 GLY H H 1 7.830 0.01 . 1 . . . . 15 G HN . 7278 1 28 . 1 1 15 15 GLY N N 15 108.403 0.1 . 1 . . . . 15 G N . 7278 1 29 . 1 1 18 18 GLY H H 1 8.308 0.01 . 1 . . . . 18 G HN . 7278 1 30 . 1 1 18 18 GLY N N 15 105.967 0.1 . 1 . . . . 18 G N . 7278 1 31 . 1 1 20 20 GLY H H 1 8.948 0.01 . 1 . . . . 20 G HN . 7278 1 32 . 1 1 20 20 GLY N N 15 108.908 0.1 . 1 . . . . 20 G N . 7278 1 33 . 1 1 21 21 GLY H H 1 9.051 0.01 . 1 . . . . 21 G HN . 7278 1 34 . 1 1 21 21 GLY N N 15 107.236 0.1 . 1 . . . . 21 G N . 7278 1 35 . 1 1 22 22 TYR H H 1 7.870 0.01 . 1 . . . . 22 Y HN . 7278 1 36 . 1 1 22 22 TYR N N 15 113.783 0.1 . 1 . . . . 22 Y N . 7278 1 37 . 1 1 23 23 GLY H H 1 9.034 0.01 . 1 . . . . 23 G HN . 7278 1 38 . 1 1 23 23 GLY N N 15 106.776 0.1 . 1 . . . . 23 G N . 7278 1 39 . 1 1 24 24 ALA H H 1 9.515 0.01 . 1 . . . . 24 A HN . 7278 1 40 . 1 1 24 24 ALA N N 15 126.729 0.1 . 1 . . . . 24 A N . 7278 1 41 . 1 1 25 25 ILE H H 1 9.120 0.01 . 1 . . . . 25 I HN . 7278 1 42 . 1 1 25 25 ILE N N 15 121.551 0.1 . 1 . . . . 25 I N . 7278 1 43 . 1 1 26 26 LEU H H 1 9.204 0.01 . 1 . . . . 26 L HN . 7278 1 44 . 1 1 26 26 LEU N N 15 129.527 0.1 . 1 . . . . 26 L N . 7278 1 45 . 1 1 27 27 ARG H H 1 9.894 0.01 . 1 . . . . 27 R HN . 7278 1 46 . 1 1 27 27 ARG N N 15 126.463 0.1 . 1 . . . . 27 R N . 7278 1 47 . 1 1 28 28 TYR H H 1 8.627 0.01 . 1 . . . . 28 Y HN . 7278 1 48 . 1 1 28 28 TYR N N 15 125.627 0.1 . 1 . . . . 28 Y N . 7278 1 49 . 1 1 29 29 ARG H H 1 9.334 0.01 . 1 . . . . 29 R HN . 7278 1 50 . 1 1 29 29 ARG N N 15 127.755 0.1 . 1 . . . . 29 R N . 7278 1 51 . 1 1 30 30 GLY H H 1 8.705 0.01 . 1 . . . . 30 G HN . 7278 1 52 . 1 1 30 30 GLY N N 15 105.675 0.1 . 1 . . . . 30 G N . 7278 1 53 . 1 1 31 31 ARG H H 1 7.995 0.01 . 1 . . . . 31 R HN . 7278 1 54 . 1 1 31 31 ARG N N 15 122.064 0.1 . 1 . . . . 31 R N . 7278 1 55 . 1 1 32 32 GLU H H 1 8.747 0.01 . 1 . . . . 32 E HN . 7278 1 56 . 1 1 32 32 GLU N N 15 123.276 0.1 . 1 . . . . 32 E N . 7278 1 57 . 1 1 33 33 LYS H H 1 9.217 0.01 . 1 . . . . 33 K HN . 7278 1 58 . 1 1 33 33 LYS N N 15 125.729 0.1 . 1 . . . . 33 K N . 7278 1 59 . 1 1 34 34 THR H H 1 8.128 0.01 . 1 . . . . 34 T HN . 7278 1 60 . 1 1 34 34 THR N N 15 115.580 0.1 . 1 . . . . 34 T N . 7278 1 61 . 1 1 35 35 PHE H H 1 9.347 0.01 . 1 . . . . 35 F HN . 7278 1 62 . 1 1 35 35 PHE N N 15 121.343 0.1 . 1 . . . . 35 F N . 7278 1 63 . 1 1 36 36 SER H H 1 8.397 0.01 . 1 . . . . 36 S HN . 7278 1 64 . 1 1 36 36 SER N N 15 114.521 0.1 . 1 . . . . 36 S N . 7278 1 65 . 1 1 37 37 ALA H H 1 6.370 0.01 . 1 . . . . 37 A HN . 7278 1 66 . 1 1 37 37 ALA N N 15 121.663 0.1 . 1 . . . . 37 A N . 7278 1 67 . 1 1 38 38 GLY H H 1 8.525 0.01 . 1 . . . . 38 G HN . 7278 1 68 . 1 1 38 38 GLY N N 15 106.773 0.1 . 1 . . . . 38 G N . 7278 1 69 . 1 1 39 39 TYR H H 1 9.695 0.01 . 1 . . . . 39 Y HN . 7278 1 70 . 1 1 39 39 TYR N N 15 123.573 0.1 . 1 . . . . 39 Y N . 7278 1 71 . 1 1 40 40 THR H H 1 8.822 0.01 . 1 . . . . 40 T HN . 7278 1 72 . 1 1 40 40 THR N N 15 114.178 0.1 . 1 . . . . 40 T N . 7278 1 73 . 1 1 41 41 ARG H H 1 7.754 0.01 . 1 . . . . 41 R HN . 7278 1 74 . 1 1 41 41 ARG N N 15 120.504 0.1 . 1 . . . . 41 R N . 7278 1 75 . 1 1 42 42 THR H H 1 8.853 0.01 . 1 . . . . 42 T HN . 7278 1 76 . 1 1 42 42 THR N N 15 125.720 0.1 . 1 . . . . 42 T N . 7278 1 77 . 1 1 43 43 THR H H 1 8.528 0.01 . 1 . . . . 43 T HN . 7278 1 78 . 1 1 43 43 THR N N 15 107.286 0.1 . 1 . . . . 43 T N . 7278 1 79 . 1 1 44 44 ASN H H 1 9.137 0.01 . 1 . . . . 44 N HN . 7278 1 80 . 1 1 44 44 ASN N N 15 121.199 0.1 . 1 . . . . 44 N N . 7278 1 81 . 1 1 45 45 ASN H H 1 8.584 0.01 . 1 . . . . 45 N HN . 7278 1 82 . 1 1 45 45 ASN N N 15 117.084 0.1 . 1 . . . . 45 N N . 7278 1 83 . 1 1 46 46 ARG H H 1 7.356 0.01 . 1 . . . . 46 R HN . 7278 1 84 . 1 1 46 46 ARG N N 15 116.820 0.1 . 1 . . . . 46 R N . 7278 1 85 . 1 1 47 47 MET H H 1 7.738 0.01 . 1 . . . . 47 M HN . 7278 1 86 . 1 1 47 47 MET N N 15 118.636 0.1 . 1 . . . . 47 M N . 7278 1 87 . 1 1 51 51 ALA H H 1 7.700 0.01 . 1 . . . . 51 A HN . 7278 1 88 . 1 1 51 51 ALA N N 15 117.626 0.1 . 1 . . . . 51 A N . 7278 1 89 . 1 1 52 52 ALA H H 1 6.443 0.01 . 1 . . . . 52 A HN . 7278 1 90 . 1 1 52 52 ALA N N 15 114.189 0.1 . 1 . . . . 52 A N . 7278 1 91 . 1 1 55 55 ALA H H 1 6.841 0.01 . 1 . . . . 55 A HN . 7278 1 92 . 1 1 55 55 ALA N N 15 119.995 0.1 . 1 . . . . 55 A N . 7278 1 93 . 1 1 58 58 ALA H H 1 7.083 0.01 . 1 . . . . 58 A HN . 7278 1 94 . 1 1 58 58 ALA N N 15 120.276 0.1 . 1 . . . . 58 A N . 7278 1 95 . 1 1 59 59 LEU H H 1 7.122 0.01 . 1 . . . . 59 L HN . 7278 1 96 . 1 1 59 59 LEU N N 15 118.611 0.1 . 1 . . . . 59 L N . 7278 1 97 . 1 1 60 60 LYS H H 1 8.548 0.01 . 1 . . . . 60 K HN . 7278 1 98 . 1 1 60 60 LYS N N 15 122.767 0.1 . 1 . . . . 60 K N . 7278 1 99 . 1 1 61 61 GLU H H 1 7.664 0.01 . 1 . . . . 61 E HN . 7278 1 100 . 1 1 61 61 GLU N N 15 117.382 0.1 . 1 . . . . 61 E N . 7278 1 101 . 1 1 62 62 HIS H H 1 8.417 0.01 . 1 . . . . 62 H HN . 7278 1 102 . 1 1 62 62 HIS N N 15 119.596 0.1 . 1 . . . . 62 H N . 7278 1 103 . 1 1 63 63 CYS H H 1 10.997 0.01 . 1 . . . . 63 C HN . 7278 1 104 . 1 1 63 63 CYS N N 15 126.965 0.1 . 1 . . . . 63 C N . 7278 1 105 . 1 1 64 64 GLU H H 1 8.692 0.01 . 1 . . . . 64 E HN . 7278 1 106 . 1 1 64 64 GLU N N 15 123.039 0.1 . 1 . . . . 64 E N . 7278 1 107 . 1 1 65 65 VAL H H 1 8.833 0.01 . 1 . . . . 65 V HN . 7278 1 108 . 1 1 65 65 VAL N N 15 126.072 0.1 . 1 . . . . 65 V N . 7278 1 109 . 1 1 67 67 LEU H H 1 8.624 0.01 . 1 . . . . 67 L HN . 7278 1 110 . 1 1 67 67 LEU N N 15 135.444 0.1 . 1 . . . . 67 L N . 7278 1 111 . 1 1 68 68 SER H H 1 8.775 0.01 . 1 . . . . 68 S HN . 7278 1 112 . 1 1 68 68 SER N N 15 121.622 0.1 . 1 . . . . 68 S N . 7278 1 113 . 1 1 69 69 THR H H 1 8.599 0.01 . 1 . . . . 69 T HN . 7278 1 114 . 1 1 69 69 THR N N 15 120.144 0.1 . 1 . . . . 69 T N . 7278 1 115 . 1 1 70 70 ASP H H 1 8.989 0.01 . 1 . . . . 70 D HN . 7278 1 116 . 1 1 70 70 ASP N N 15 129.384 0.1 . 1 . . . . 70 D N . 7278 1 117 . 1 1 71 71 SER H H 1 8.705 0.01 . 1 . . . . 71 S HN . 7278 1 118 . 1 1 71 71 SER N N 15 117.902 0.1 . 1 . . . . 71 S N . 7278 1 119 . 1 1 72 72 GLN H H 1 9.541 0.01 . 1 . . . . 72 Q HN . 7278 1 120 . 1 1 72 72 GLN N N 15 131.938 0.1 . 1 . . . . 72 Q N . 7278 1 121 . 1 1 73 73 TYR H H 1 9.004 0.01 . 1 . . . . 73 Y HN . 7278 1 122 . 1 1 73 73 TYR N N 15 124.882 0.1 . 1 . . . . 73 Y N . 7278 1 123 . 1 1 74 74 VAL H H 1 7.555 0.01 . 1 . . . . 74 V HN . 7278 1 124 . 1 1 74 74 VAL N N 15 116.743 0.1 . 1 . . . . 74 V N . 7278 1 125 . 1 1 75 75 ARG H H 1 6.905 0.01 . 1 . . . . 75 R HN . 7278 1 126 . 1 1 75 75 ARG N N 15 117.469 0.1 . 1 . . . . 75 R N . 7278 1 127 . 1 1 76 76 GLN H H 1 8.126 0.01 . 1 . . . . 76 Q HN . 7278 1 128 . 1 1 76 76 GLN N N 15 121.449 0.1 . 1 . . . . 76 Q N . 7278 1 129 . 1 1 77 77 GLY H H 1 7.181 0.01 . 1 . . . . 77 G HN . 7278 1 130 . 1 1 77 77 GLY N N 15 104.605 0.1 . 1 . . . . 77 G N . 7278 1 131 . 1 1 78 78 ILE H H 1 8.126 0.01 . 1 . . . . 78 I HN . 7278 1 132 . 1 1 78 78 ILE N N 15 120.774 0.1 . 1 . . . . 78 I N . 7278 1 133 . 1 1 79 79 THR H H 1 8.120 0.01 . 1 . . . . 79 T HN . 7278 1 134 . 1 1 79 79 THR N N 15 112.829 0.1 . 1 . . . . 79 T N . 7278 1 stop_ save_