data_15689 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15689 _Entry.Title ; Automated NMR Structure of the UBB by FAPSY ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2008-03-21 _Entry.Accession_date 2008-03-21 _Entry.Last_release_date 2009-05-12 _Entry.Original_release_date 2009-05-12 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.116 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _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 Woonghee Lee W. . . 15689 2 Jin-Won Jung J. . . 15689 3 Weontae Lee W. . . 15689 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 15689 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID AUTOMATION . 15689 FAPSY . 15689 MOAD . 15689 MOLYBDOPTERIN . 15689 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 15689 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 294 15689 '15N chemical shifts' 92 15689 '1H chemical shifts' 615 15689 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 . . 2009-05-12 2008-03-21 original author . 15689 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2K25 'BMRB Entry Tracking System' 15689 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 15689 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title 'The Automated Suite for Protein Structure by NMR Spectroscopy' _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _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 . _Citation.Page_last . _Citation.Year . _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 Woonghee Lee W. . . 15689 1 2 Jin-Won Jung J. . . 15689 1 3 Weontae Lee W. . . 15689 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15689 _Assembly.ID 1 _Assembly.Name UBB _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 no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 UBB 1 $UBB A . yes native no no . . . 15689 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_UBB _Entity.Sf_category entity _Entity.Sf_framecode UBB _Entity.Entry_ID 15689 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name UBB _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GSLVPRGSMQIFVKTLTGKT ITLEVEPSDTIENVKAKIQD KEGIPPDQQRLIFAGKQLED GRTLSEYNIQKESTLHLVLR LRGYADLREDPDRQDHHPGS GAQ ; _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 103 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state unknown _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 11539.073 _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 11505 . entity . . . . . 72.82 76 97.33 98.67 4.84e-43 . . . . 15689 1 2 no BMRB 11547 . ubiquitin . . . . . 72.82 76 97.33 98.67 4.84e-43 . . . . 15689 1 3 no BMRB 15047 . denatured_ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 4 no BMRB 15410 . Ubi . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 5 no BMRB 15907 . Ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 6 no BMRB 16582 . Ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 7 no BMRB 16626 . Ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 8 no BMRB 16895 . UBB+1 . . . . . 100.00 103 100.00 100.00 2.59e-67 . . . . 15689 1 9 no BMRB 17181 . ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 10 no BMRB 17439 . ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 11 no BMRB 17769 . Ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 12 no BMRB 17919 . entity . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 13 no BMRB 18582 . ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 14 no BMRB 18583 . ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 15 no BMRB 18584 . ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 16 no BMRB 18610 . Ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 17 no BMRB 18611 . Ubiquitin_A_state . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 18 no BMRB 18737 . UBIQUITIN . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 19 no BMRB 19406 . entity . . . . . 72.82 152 98.67 100.00 8.78e-43 . . . . 15689 1 20 no BMRB 19412 . entity . . . . . 72.82 152 98.67 100.00 8.78e-43 . . . . 15689 1 21 no BMRB 25070 . Ubiquitin . . . . . 72.82 79 98.67 100.00 1.11e-43 . . . . 15689 1 22 no BMRB 25123 . Ubiquitin . . . . . 69.90 72 98.61 100.00 1.32e-41 . . . . 15689 1 23 no BMRB 26604 . Ubiquitin_(microcrystalline) . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 24 no BMRB 4245 . ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 25 no BMRB 4375 . Ubiquitin . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 26 no PDB 1AAR . "Structure Of A Diubiquitin Conjugate And A Model For Interaction With Ubiquitin Conjugating Enzyme (E2)" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 27 no PDB 1CMX . "Structural Basis For The Specificity Of Ubiquitin C- Terminal Hydrolases" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 28 no PDB 1D3Z . "Ubiquitin Nmr Structure" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 29 no PDB 1F9J . "Structure Of A New Crystal Form Of Tetraubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 30 no PDB 1FXT . "Structure Of A Conjugating Enzyme-Ubiquitin Thiolester Complex" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 31 no PDB 1G6J . "Structure Of Recombinant Human Ubiquitin In Aot Reverse Micelles" . . . . . 71.84 76 98.65 100.00 1.08e-42 . . . . 15689 1 32 no PDB 1GJZ . "Solution Structure Of A Dimeric N-Terminal Fragment Of Human Ubiquitin" . . . . . 51.46 53 100.00 100.00 2.07e-27 . . . . 15689 1 33 no PDB 1NBF . "Crystal Structure Of A Ubp-Family Deubiquitinating Enzyme In Isolation And In Complex With Ubiquitin Aldehyde" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 34 no PDB 1P3Q . "Mechanism Of Ubiquitin Recognition By The Cue Domain Of Vps9" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 35 no PDB 1Q5W . "Ubiquitin Recognition By Npl4 Zinc-Fingers" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 36 no PDB 1S1Q . "Tsg101(Uev) Domain In Complex With Ubiquitin" . . . . . 71.84 76 98.65 100.00 1.08e-42 . . . . 15689 1 37 no PDB 1TBE . "Structure Of Tetraubiquitin Shows How Multiubiquitin Chains Can Be Formed" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 38 no PDB 1UBI . "Synthetic Structural And Biological Studies Of The Ubiquitin System. Part 1" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 39 no PDB 1UBQ . "Structure Of Ubiquitin Refined At 1.8 Angstroms Resolution" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 40 no PDB 1UZX . "A Complex Of The Vps23 Uev With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 41 no PDB 1V80 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 42 no PDB 1V81 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 43 no PDB 1WR6 . "Crystal Structure Of Gga3 Gat Domain In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 44 no PDB 1WRD . "Crystal Structure Of Tom1 Gat Domain In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 45 no PDB 1XD3 . "Crystal Structure Of Uchl3-Ubvme Complex" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 46 no PDB 1XQQ . "Simultaneous Determination Of Protein Structure And Dynamics" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 47 no PDB 1YD8 . "Complex Of Human Gga3 Gat Domain And Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 48 no PDB 1YIW . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin" . . . . . 72.82 76 97.33 100.00 4.59e-43 . . . . 15689 1 49 no PDB 1ZGU . "Solution Structure Of The Human Mms2-Ubiquitin Complex" . . . . . 72.82 76 97.33 100.00 3.07e-43 . . . . 15689 1 50 no PDB 2AYO . "Structure Of Usp14 Bound To Ubquitin Aldehyde" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 51 no PDB 2BGF . "Nmr Structure Of Lys48-Linked Di-Ubiquitin Using Chemical Shift Perturbation Data Together With Rdcs And 15n- Relaxation Data" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 52 no PDB 2C7M . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 53 no PDB 2C7N . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 54 no PDB 2D3G . "Double Sided Ubiquitin Binding Of Hrs-Uim" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 55 no PDB 2DEN . "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 56 no PDB 2DX5 . "The Complex Structure Between The Mouse Eap45-Glue Domain And Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 57 no PDB 2FCQ . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin With A Cubic Space Group" . . . . . 72.82 76 97.33 100.00 4.59e-43 . . . . 15689 1 58 no PDB 2FID . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 59 no PDB 2FIF . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 60 no PDB 2FUH . "Solution Structure Of The Ubch5cUB NON-Covalent Complex" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 61 no PDB 2G45 . "Co-Crystal Structure Of Znf Ubp Domain From The Deubiquitinating Enzyme Isopeptidase T (Isot) In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 62 no PDB 2GMI . Mms2UBC13~UBIQUITIN . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 63 no PDB 2HD5 . "Usp2 In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 64 no PDB 2HTH . "Structural Basis For Ubiquitin Recognition By The Human Eap45ESCRT-Ii Glue Domain" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 65 no PDB 2IBI . "Covalent Ubiquitin-Usp2 Complex" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 66 no PDB 2J7Q . "Crystal Structure Of The Ubiquitin-Specific Protease Encoded By Murine Cytomegalovirus Tegument Protein M48 In Complex With A U" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 67 no PDB 2JF5 . "Crystal Structure Of Lys63-Linked Di-Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 68 no PDB 2JRI . "Solution Structure Of The Josephin Domain Of Ataxin-3 In Complex With Ubiquitin Molecule." . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 69 no PDB 2JY6 . "Solution Structure Of The Complex Of Ubiquitin And Ubiquilin 1 Uba Domain" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 70 no PDB 2JZZ . "Solid-State Nmr Structure Of Microcrystalline Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 71 no PDB 2K25 . "Automated Nmr Structure Of The Ubb By Fapsy" . . . . . 100.00 103 100.00 100.00 2.59e-67 . . . . 15689 1 72 no PDB 2K39 . "Recognition Dynamics Up To Microseconds Revealed From Rdc Derived Ubiquitin Ensemble In Solution" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 73 no PDB 2K6D . "Cin85 Sh3-C Domain In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 6.70e-44 . . . . 15689 1 74 no PDB 2K8B . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Cis Isomer In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 75 no PDB 2K8C . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Trans Isomer In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 76 no PDB 2KDE . "Nmr Structure Of Major S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 77 no PDB 2KDF . "Nmr Structure Of Minor S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 78 no PDB 2KHW . "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" . . . . . 72.82 79 98.67 100.00 1.11e-43 . . . . 15689 1 79 no PDB 2KJH . "Nmr Based Structural Model Of The Ubch8-Ubiquitin Complex" . . . . . 72.82 76 98.67 100.00 6.70e-44 . . . . 15689 1 80 no PDB 2KLG . "Pere Nmr Structure Of Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 81 no PDB 2KN5 . "A Correspondence Between Solution-State Dynamics Of An Individual Protein And The Sequence And Conformational Diversity Of Its " . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 82 no PDB 2KOX . "Nmr Residual Dipolar Couplings Identify Long Range Correlated Motions In The Backbone Of The Protein Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 83 no PDB 2KTF . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 84 no PDB 2KWU . "Solution Structure Of Ubm2 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 85 no PDB 2KWV . "Solution Structure Of Ubm1 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 86 no PDB 2KX0 . "The Solution Structure Of Ubb+1, Frameshift Mutant Of Ubiquitin B" . . . . . 100.00 103 100.00 100.00 2.59e-67 . . . . 15689 1 87 no PDB 2L0F . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 (P692a Mutant) In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 88 no PDB 2L0T . "Solution Structure Of The Complex Of Ubiquitin And The Vhs Domain Of Stam2" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 89 no PDB 2L3Z . "Proton-Detected 4d Dream Solid-State Nmr Structure Of Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 90 no PDB 2LD9 . "Backbone Structure Of Ubiquitin Determined Using Backbone Amide Noes And Backbone N-H And N-C Rdcs" . . . . . 72.82 77 98.67 100.00 1.12e-43 . . . . 15689 1 91 no PDB 2LJ5 . "Description Of The Structural Fluctuations Of Proteins From Structure- Based Calculations Of Residual Dipolar Couplings" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 92 no PDB 2LVO . "Structure Of The Gp78cue Domain Bound To Monubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 93 no PDB 2LVP . "Gp78cue Domain Bound To The Distal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 94 no PDB 2LVQ . "Gp78cue Domain Bound To The Proximal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 95 no PDB 2LZ6 . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 96 no PDB 2MBB . "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" . . . . . 72.82 78 98.67 100.00 1.04e-43 . . . . 15689 1 97 no PDB 2MBH . "Nmr Structure Of Eklf(22-40)/ubiquitin Complex" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 98 no PDB 2MBO . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 0 Mm Nacl" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 99 no PDB 2MBQ . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 150 Mm Nacl" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 100 no PDB 2MCN . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 101 no PDB 2MJ5 . "Structure Of The Uba Domain Of Human Nbr1 In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 102 no PDB 2MJB . "Solution Nmr Structure Of Ubiquitin Refined Against Dipolar Couplings In 4 Media" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 103 no PDB 2MOR . "A Tensor-free Method For The Structural And Dynamical Refinement Of Proteins Using Residual Dipolar Couplings" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 104 no PDB 2MRE . "Nmr Structure Of The Rad18-ubz/ubiquitin Complex" . . . . . 72.82 79 98.67 100.00 1.11e-43 . . . . 15689 1 105 no PDB 2MRO . "Structure Of The Complex Of Ubiquitin And The Uba Domain From Dna- Damage-inducible 1 Protein (ddi1)" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 106 no PDB 2MSG . "Solid-state Nmr Structure Of Ubiquitin" . . . . . 69.90 72 98.61 100.00 1.32e-41 . . . . 15689 1 107 no PDB 2MUR . "Solution Structure Of The Human Faap20 Ubz-ubiquitin Complex" . . . . . 72.82 78 98.67 100.00 1.04e-43 . . . . 15689 1 108 no PDB 2MWS . "Structure Of The Complex Of Ubiquitin And The Ubiquitin-like (ubl) Domain Of Ddi1" . . . . . 72.82 76 97.33 98.67 7.01e-43 . . . . 15689 1 109 no PDB 2N2K . "Ensemble Structure Of The Closed State Of Lys63-linked Diubiquitin In The Absence Of A Ligand" . . . . . 68.93 71 98.59 100.00 9.78e-41 . . . . 15689 1 110 no PDB 2NR2 . "The Mumo (Minimal Under-Restraining Minimal Over- Restraining) Method For The Determination Of Native States Ensembles Of Prote" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 111 no PDB 2O6V . "Crystal Structure And Solution Nmr Studies Of Lys48-Linked Tetraubiquitin At Neutral Ph" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 112 no PDB 2OJR . "Structure Of Ubiquitin Solved By Sad Using The Lanthanide- Binding Tag" . . . . . 73.79 111 97.37 100.00 1.46e-43 . . . . 15689 1 113 no PDB 2OOB . "Crystal Structure Of The Uba Domain From Cbl-B Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 114 no PDB 2PE9 . "Nmr Based Structure Of The Open Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tenso" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 115 no PDB 2PEA . "Nmr Based Structure Of The Closed Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Ten" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 116 no PDB 2QHO . "Crystal Structure Of The Uba Domain From Edd Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 117 no PDB 2RR9 . "The Solution Structure Of The K63-Ub2:tuims Complex" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 118 no PDB 2RSU . "Alternative Structure Of Ubiquitin" . . . . . 72.82 76 97.33 98.67 4.84e-43 . . . . 15689 1 119 no PDB 2RU6 . "The Pure Alternative State Of Ubiquitin" . . . . . 72.82 76 97.33 98.67 4.84e-43 . . . . 15689 1 120 no PDB 2W9N . "Crystal Structure Of Linear Di-Ubiquitin" . . . . . 71.84 152 98.65 100.00 9.09e-42 . . . . 15689 1 121 no PDB 2WDT . "Crystal Structure Of Plasmodium Falciparum Uchl3 In Complex With The Suicide Inhibitor Ubvme" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 122 no PDB 2WWZ . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P212121" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 123 no PDB 2WX0 . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P21" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 124 no PDB 2WX1 . "Tab2 Nzf Domain In Complex With Lys63-Linked Tri-Ubiquitin, P212121" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 125 no PDB 2XBB . "Nedd4 Hect:ub Complex" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 126 no PDB 2XEW . "Crystal Structure Of K11-Linked Diubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 127 no PDB 2XK5 . "Crystal Structure Of K6-Linked Diubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 128 no PDB 2Z59 . "Complex Structures Of Mouse Rpn13 (22-130aa) And Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 129 no PDB 2ZCC . "Ubiquitin Crystallized Under High Pressure" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 130 no PDB 2ZNV . "Crystal Structure Of Human Amsh-Lp Dub Domain In Complex With Lys63-Linked Ubiquitin Dimer" . . . . . 72.82 77 98.67 100.00 1.01e-43 . . . . 15689 1 131 no PDB 2ZVN . "Nemo Cozi Domain Incomplex With Diubiquitin In P212121 Space Group" . . . . . 74.76 154 98.70 100.00 2.73e-44 . . . . 15689 1 132 no PDB 2ZVO . "Nemo Cozi Domain In Complex With Diubiquitin In C2 Space Group" . . . . . 74.76 154 98.70 100.00 2.73e-44 . . . . 15689 1 133 no PDB 3A1Q . "Crystal Structure Of The Mouse Rap80 Uims In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 72.82 77 98.67 100.00 1.01e-43 . . . . 15689 1 134 no PDB 3A33 . "Ubch5b~ubiquitin Conjugate" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 135 no PDB 3A9J . "Crystal Structure Of The Mouse Tab2-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 72.82 77 98.67 100.00 1.01e-43 . . . . 15689 1 136 no PDB 3A9K . "Crystal Structure Of The Mouse Tab3-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 72.82 77 98.67 100.00 1.01e-43 . . . . 15689 1 137 no PDB 3AI5 . "Crystal Structure Of Yeast Enhanced Green Fluorescent Protein- Ubiquitin Fusion Protein" . . . . . 73.79 307 98.68 100.00 8.99e-42 . . . . 15689 1 138 no PDB 3ALB . "Cyclic Lys48-Linked Tetraubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 139 no PDB 3AUL . "Crystal Structure Of Wild-Type Lys48-Linked Diubiquitin In An Open Conformation" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 140 no PDB 3AXC . "Crystal Structure Of Linear Diubiquitin" . . . . . 74.76 154 98.70 100.00 2.73e-44 . . . . 15689 1 141 no PDB 3B08 . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 72.82 152 98.67 100.00 8.78e-43 . . . . 15689 1 142 no PDB 3B0A . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 72.82 152 98.67 100.00 8.78e-43 . . . . 15689 1 143 no PDB 3BY4 . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 144 no PDB 3C0R . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 145 no PDB 3DVG . "Crystal Structure Of K63-Specific Fab Apu.3a8 Bound To K63-Linked Di- Ubiquitin" . . . . . 72.82 80 98.67 100.00 1.36e-43 . . . . 15689 1 146 no PDB 3DVN . "Crystal Structure Of K63-specific Fab Apu2.16 Bound To K63-linked Di- Ubiquitin" . . . . . 72.82 80 98.67 100.00 1.36e-43 . . . . 15689 1 147 no PDB 3EEC . "X-Ray Structure Of Human Ubiquitin Cd(Ii) Adduct" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 148 no PDB 3EFU . "X-Ray Structure Of Human Ubiquitin-Hg(Ii) Adduct" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 149 no PDB 3EHV . "X-Ray Structure Of Human Ubiquitin Zn(Ii) Adduct" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 150 no PDB 3H1U . "Structure Of Ubiquitin In Complex With Cd Ions" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 151 no PDB 3H7P . "Crystal Structure Of K63-Linked Di-Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 152 no PDB 3H7S . "Crystal Structures Of K63-Linked Di- And Tri-Ubiquitin Reveal A Highly Extended Chain Architecture" . . . . . 73.79 76 97.37 98.68 5.40e-42 . . . . 15689 1 153 no PDB 3HM3 . "The Structure And Conformation Of Lys-63 Linked Tetra-Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 154 no PDB 3I3T . "Crystal Structure Of Covalent Ubiquitin-usp21 Complex" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 155 no PDB 3IFW . "Crystal Structure Of The S18y Variant Of Ubiquitin Carboxy T Hydrolase L1 Bound To Ubiquitin Vinylmethylester." . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 156 no PDB 3IHP . "Covalent Ubiquitin-Usp5 Complex" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 157 no PDB 3JSV . "Crystal Structure Of Mouse Nemo Cozi In Complex With Lys63- Linked Di-Ubiquitin" . . . . . 72.82 77 98.67 100.00 1.01e-43 . . . . 15689 1 158 no PDB 3JVZ . E2~ubiquitin-Hect . . . . . 74.76 81 98.70 100.00 3.01e-45 . . . . 15689 1 159 no PDB 3JW0 . E2~ubiquitin-Hect . . . . . 74.76 81 98.70 100.00 3.01e-45 . . . . 15689 1 160 no PDB 3K9O . "The Crystal Structure Of E2-25k And Ubb+1 Complex" . . . . . 92.23 96 98.95 100.00 1.89e-60 . . . . 15689 1 161 no PDB 3K9P . "The Crystal Structure Of E2-25k And Ubiquitin Complex" . . . . . 72.82 79 98.67 100.00 1.11e-43 . . . . 15689 1 162 no PDB 3KVF . "Crystal Structure Of The I93m Mutant Of Ubiquitin Carboxy Te Hydrolase L1 Bound To Ubiquitin Vinylmethylester" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 163 no PDB 3KW5 . "Crystal Structure Of Ubiquitin Carboxy Terminal Hydrolase L1 Ubiquitin Vinylmethylester" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 164 no PDB 3LDZ . "Crystal Structure Of Human Stam1 Vhs Domain In Complex With Ubiquitin" . . . . . 70.87 73 98.63 100.00 3.30e-42 . . . . 15689 1 165 no PDB 3M3J . "A New Crystal Form Of Lys48-Linked Diubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 166 no PDB 3MHS . "Structure Of The Saga Ubp8SGF11SUS1SGF73 DUB MODULE BOUND Ubiquitin Aldehyde" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 167 no PDB 3N30 . "Crystal Structure Of Cubic Zn3-Hub (Human Ubiquitin) Adduct" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 168 no PDB 3N32 . "The Crystal Structure Of Human Ubiquitin Adduct With Zeise's Salt" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 169 no PDB 3NHE . "High Resolution Structure (1.26a) Of Usp2a In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 170 no PDB 3NOB . "Structure Of K11-linked Di-ubiquitin" . . . . . 72.82 78 98.67 100.00 1.04e-43 . . . . 15689 1 171 no PDB 3NS8 . "Crystal Structure Of An Open Conformation Of Lys48-Linked Diubiquitin At Ph 7.5" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 172 no PDB 3O65 . "Crystal Structure Of A Josephin-Ubiquitin Complex: Evolutionary Restraints On Ataxin-3 Deubiquitinating Activity" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 173 no PDB 3OFI . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 174 no PDB 3OJ3 . "Crystal Structure Of The A20 Znf4 And Ubiquitin Complex" . . . . . 72.82 79 98.67 100.00 1.11e-43 . . . . 15689 1 175 no PDB 3OJ4 . "Crystal Structure Of The A20 Znf4, Ubiquitin And Ubch5a Complex" . . . . . 72.82 79 98.67 100.00 1.11e-43 . . . . 15689 1 176 no PDB 3ONS . "Crystal Structure Of Human Ubiquitin In A New Crystal Form" . . . . . 69.90 72 98.61 100.00 1.32e-41 . . . . 15689 1 177 no PDB 3PHD . "Crystal Structure Of Human Hdac6 In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 178 no PDB 3PHW . "Otu Domain Of Crimean Congo Hemorrhagic Fever Virus In Complex With Ubiquitin" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 179 no PDB 3PRM . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 180 no PDB 3PRP . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 181 no PDB 3PT2 . "Structure Of A Viral Otu Domain Protease Bound To Ubiquitin" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 182 no PDB 3PTF . "X-Ray Structure Of The Non-Covalent Complex Between Ubch5a And Ubiquitin" . . . . . 72.82 79 98.67 100.00 1.11e-43 . . . . 15689 1 183 no PDB 3Q3F . "Engineering Domain-Swapped Binding Interfaces By Mutually Exclusive Folding: Insertion Of Ubiquitin Into Position 103 Of Barnas" . . . . . 71.84 189 98.65 100.00 5.88e-42 . . . . 15689 1 184 no PDB 3RUL . "New Strategy To Analyze Structures Of Glycopeptide-Target Complexes" . . . . . 72.82 79 98.67 100.00 8.75e-44 . . . . 15689 1 185 no PDB 3TBL . "Structure Of Mono-ubiquitinated Pcna: Implications For Dna Polymerase Switching And Okazaki Fragment Maturation" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 186 no PDB 3TMP . "The Catalytic Domain Of Human Deubiquitinase Duba In Complex With Ubiquitin Aldehyde" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 187 no PDB 3U30 . "Crystal Structure Of A Linear-Specific Ubiquitin Fab Bound To Linear Ubiquitin" . . . . . 75.73 172 97.44 98.72 3.73e-44 . . . . 15689 1 188 no PDB 3UGB . "Ubch5c~ubiquitin Conjugate" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 189 no PDB 3VDZ . "Tailoring Encodable Lanthanide-Binding Tags As Mri Contrast Agents: Xq-Dse3-Ubiquitin At 2.4 Angstroms" . . . . . 73.79 111 97.37 100.00 7.07e-44 . . . . 15689 1 190 no PDB 3VFK . "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Ubiquitin As A Ligand Carrier" . . . . . 72.82 79 98.67 100.00 8.75e-44 . . . . 15689 1 191 no PDB 3VHT . "Crystal Structure Of Gfp-Wrnip1 Ubz Domain Fusion Protein In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 192 no PDB 3VUW . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form I" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 193 no PDB 3VUX . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form Ii" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 194 no PDB 3VUY . "Crystal Structure Of A20 Zf7 In Complex With Linear Tetraubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 195 no PDB 3WWQ . "Crystal Structure Of Faap20 Ubz Domain In Complex With Lys63-linked Diubiquitin" . . . . . 72.82 77 98.67 100.00 1.01e-43 . . . . 15689 1 196 no PDB 3WXE . "Crystal Structure Of Cyld Usp Domain (c596s) In Complex With Met1- Linked Diubiquitin" . . . . . 72.82 148 97.33 98.67 3.30e-42 . . . . 15689 1 197 no PDB 3WXF . "Crystal Structure Of Cyld Usp Domain (c596s E674q) In Complex With Met1-linked Diubiquitin" . . . . . 72.82 148 97.33 98.67 3.30e-42 . . . . 15689 1 198 no PDB 3WXG . "Crystal Structure Of Cyld Usp Domain (c596a) In Complex With Lys63- Linked Diubiquitin" . . . . . 69.90 72 98.61 100.00 1.32e-41 . . . . 15689 1 199 no PDB 3ZLZ . "Lys6-linked Tri-ubiquitin" . . . . . 72.82 76 97.33 100.00 3.07e-43 . . . . 15689 1 200 no PDB 3ZNH . "Crimean Congo Hemorrhagic Fever Virus Otu Domain In Complex With Ubiquitin-propargyl." . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 201 no PDB 3ZNI . "Structure Of Phosphotyr363-cbl-b - Ubch5b-ub - Zap-70 Peptide Complex" . . . . . 74.76 81 98.70 100.00 3.01e-45 . . . . 15689 1 202 no PDB 3ZNZ . "Crystal Structure Of Otulin Otu Domain (c129a) In Complex With Met1-di Ubiquitin" . . . . . 72.82 152 98.67 100.00 8.78e-43 . . . . 15689 1 203 no PDB 4AP4 . "Rnf4 - Ubch5a - Ubiquitin Heterotrimeric Complex" . . . . . 72.82 80 98.67 100.00 8.43e-44 . . . . 15689 1 204 no PDB 4AUQ . "Structure Of Birc7-Ubch5b-Ub Complex." . . . . . 74.76 81 98.70 100.00 3.01e-45 . . . . 15689 1 205 no PDB 4BBN . "Nedd4 Hect-ub:ub Complex" . . . . . 72.82 76 98.67 100.00 6.70e-44 . . . . 15689 1 206 no PDB 4BOS . "Structure Of Otud2 Otu Domain In Complex With Ubiquitin K11- Linked Peptide" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 207 no PDB 4BOZ . "Structure Of Otud2 Otu Domain In Complex With K11-linked Di Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 208 no PDB 4BVU . "Structure Of Shigella Effector Ospg In Complex With Host Ubch5c-ubiquitin Conjugate" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 209 no PDB 4CXC . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 210 no PDB 4CXD . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 211 no PDB 4D5L . "Cryo-em Structures Of Ribosomal 80s Complexes With Termination Factors And Cricket Paralysis Virus Ires Reveal The Ires In The " . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 212 no PDB 4D61 . "Cryo-em Structures Of Ribosomal 80s Complexes With Termination Factors And Cricket Paralysis Virus Ires Reveal The Ires In The " . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 213 no PDB 4DDG . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 214 no PDB 4DDI . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 215 no PDB 4DHJ . "The Structure Of A Ceotub1 Ubiquitin Aldehyde Ubc13~ub Complex" . . . . . 72.82 76 98.67 100.00 6.70e-44 . . . . 15689 1 216 no PDB 4DHZ . "The Structure Of HCEOTUB1-Ubiquitin Aldehyde-Ubc13~ub" . . . . . 72.82 76 98.67 100.00 6.70e-44 . . . . 15689 1 217 no PDB 4FJV . "Crystal Structure Of Human Otubain2 And Ubiquitin Complex" . . . . . 72.82 86 98.67 100.00 1.93e-43 . . . . 15689 1 218 no PDB 4HXD . "Diversity Of Ubiquitin And Isg15 Specificity Amongst Nairoviruses Viral Ovarian Tumor Domain Proteases" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 219 no PDB 4I6N . "Crystal Structure Of Trichinella Spiralis Uch37 Catalytic Domain Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 71.84 75 98.65 100.00 9.44e-43 . . . . 15689 1 220 no PDB 4IG7 . "Crystal Structure Of Trichinella Spiralis Uch37 Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 221 no PDB 4IUM . "Equine Arteritis Virus Papain-like Protease 2 (plp2) Covalently Bound To Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 222 no PDB 4JIO . "Bro1 V Domain And Ubiquitin" . . . . . 72.82 76 97.33 98.67 5.64e-43 . . . . 15689 1 223 no PDB 4JQW . "Crystal Structure Of A Complex Of Nod1 Card And Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 224 no PDB 4K1R . "Crystal Structure Of Schizosaccharomyces Pombe Sst2 Catalytic Domain And Ubiquitin" . . . . . 76.70 81 97.47 98.73 8.08e-46 . . . . 15689 1 225 no PDB 4K7S . "Crystal Structure Of Zn2-hub (human Ubiquitin) Adduct From A Solution 35 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 226 no PDB 4K7U . "Crystal Structure Of Zn2.3-hub (human Ubiquitin) Adduct From A Solution 70 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 227 no PDB 4K7W . "Crystal Structure Of Zn3-hub(human Ubiquitin) Adduct From A Solution 100 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 228 no PDB 4KSK . "Gumby/fam105b In Complex With Ubiquitin" . . . . . 72.82 80 98.67 100.00 8.43e-44 . . . . 15689 1 229 no PDB 4KSL . "Gumby/fam105b In Complex With Linear Di-ubiquitin" . . . . . 72.82 156 98.67 100.00 1.02e-42 . . . . 15689 1 230 no PDB 4KZX . "Rabbit 40s Ribosomal Subunit In Complex With Eif1." . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 231 no PDB 4KZY . "Rabbit 40s Ribosomal Subunit In Complex With Eif1 And Eif1a." . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 232 no PDB 4KZZ . "Rabbit 40s Ribosomal Subunit In Complex With Mrna, Initiator Trna And Eif1a" . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 233 no PDB 4LCD . "Structure Of An Rsp5xubxsna3 Complex: Mechanism Of Ubiquitin Ligation And Lysine Prioritization By A Hect E3" . . . . . 71.84 83 98.65 100.00 5.16e-43 . . . . 15689 1 234 no PDB 4LDT . "The Structure Of H/ceotub1-ubiquitin Aldehyde-ubch5b~ub" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 235 no PDB 4LJO . "Structure Of An Active Ligase (hoip)/ubiquitin Transfer Complex" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 236 no PDB 4LJP . "Structure Of An Active Ligase (hoip-h889a)/ubiquitin Transfer Complex" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 237 no PDB 4M0W . "Crystal Structure Of Sars-cov Papain-like Protease C112s Mutant In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 238 no PDB 4MDK . "Cdc34-ubiquitin-cc0651 Complex" . . . . . 72.82 80 98.67 100.00 8.43e-44 . . . . 15689 1 239 no PDB 4MM3 . "Crystal Structure Of Sars-cov Papain-like Protease Plpro In Complex With Ubiquitin Aldehyde" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 240 no PDB 4MSM . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 E286a Mutant Bound To Ubiquitin" . . . . . 76.70 81 97.47 98.73 8.08e-46 . . . . 15689 1 241 no PDB 4MSQ . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 Catalytic Domain Bound To Ubiquitin" . . . . . 76.70 81 97.47 98.73 8.08e-46 . . . . 15689 1 242 no PDB 4NQK . "Structure Of An Ubiquitin Complex" . . . . . 72.82 79 98.67 100.00 1.93e-43 . . . . 15689 1 243 no PDB 4NQL . "The Crystal Structure Of The Dub Domain Of Amsh Orthologue, Sst2 From S. Pombe, In Complex With Lysine 63-linked Diubiquitin" . . . . . 72.82 77 98.67 100.00 1.01e-43 . . . . 15689 1 244 no PDB 4P4H . "Caught-in-action Signaling Complex Of Rig-i 2card Domain And Mavs Card Domain" . . . . . 72.82 79 98.67 100.00 1.93e-43 . . . . 15689 1 245 no PDB 4PIG . "Crystal Structure Of The Ubiquitin K11s Mutant" . . . . . 72.82 76 97.33 98.67 4.69e-43 . . . . 15689 1 246 no PDB 4PIH . "X-ray Crystal Structure Of The K33s Mutant Of Ubiquitin" . . . . . 72.82 76 97.33 98.67 4.69e-43 . . . . 15689 1 247 no PDB 4PQT . "Insights Into The Mechanism Of Deubiquitination By Jamm Deubiquitinases From Co-crystal Structures Of Enzyme With Substrate And" . . . . . 76.70 81 97.47 98.73 8.08e-46 . . . . 15689 1 248 no PDB 4R62 . "Structure Of Rad6~ub" . . . . . 72.82 78 98.67 100.00 1.07e-43 . . . . 15689 1 249 no PDB 4RF0 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 250 no PDB 4RF1 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 72.82 75 98.67 100.00 8.28e-44 . . . . 15689 1 251 no PDB 4S1Z . "Crystal Structure Of Trabid Nzf1 In Complex With K29 Linked Di- Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 252 no PDB 4S22 . "Crystal Structure Of K29 Linked Di-ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 253 no PDB 4UEL . "Uch-l5 In Complex With Ubiquitin-propargyl Bound To The Rpn13 Deubad Domain" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 254 no PDB 4UF6 . "Uch-l5 In Complex With Ubiquitin-propargyl Bound To An Activating Fragment Of Ino80g" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 255 no PDB 4UN2 . "Crystal Structure Of The Uba Domain Of Dsk2 In Complex With Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 256 no PDB 4UPX . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 257 no PDB 4UQ1 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 258 no PDB 4UQ4 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 259 no PDB 4UQ5 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 260 no PDB 4V3K . "Rnf38-ubch5b-ub Complex" . . . . . 74.76 81 98.70 100.00 3.01e-45 . . . . 15689 1 261 no PDB 4V3L . "Rnf38-ub-ubch5b-ub Complex" . . . . . 74.76 81 98.70 100.00 3.01e-45 . . . . 15689 1 262 no PDB 4W20 . "Structure Of The Mammalian 60s Ribosomal Subunit (this Entry Contains The Large Ribosomal Proteins)" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 263 no PDB 4W22 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 264 no PDB 4W23 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Small Ribosomal Subunit)" . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 265 no PDB 4W25 . "Structure Of The Idle Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 266 no PDB 4W27 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 267 no PDB 4W28 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Small Ribosomal Subunit)" . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 268 no PDB 4WHV . Rnf8/ubc13c87k~ub . . . . . 72.82 83 98.67 100.00 2.93e-43 . . . . 15689 1 269 no PDB 4WLR . "Crystal Structure Of Much37-hrpn13 Ctd-hub Complex" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 270 no PDB 4WUR . "The Crystal Structure Of The Mers-cov Papain-like Protease (c111s) With Human Ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 271 no PDB 4WZP . "Ser65 Phosphorylated Ubiquitin, Major Conformation" . . . . . 72.82 76 97.33 98.67 6.35e-43 . . . . 15689 1 272 no PDB 4XKL . "Crystal Structure Of Ndp52 Zf2 In Complex With Mono-ubiquitin" . . . . . 74.76 80 98.70 100.00 5.05e-45 . . . . 15689 1 273 no PDB 4XOF . "Observing The Overall Rocking Motion Of A Protein In A Crystal - Orthorhombic Ubiquitin Crystals Without Zinc." . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 274 no PDB 4XOK . "Observing The Overall Rocking Motion Of A Protein In A Crystal." . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 275 no PDB 4XOL . "Observing The Overall Rocking Motion Of A Protein In A Crystal - Cubic Ubiquitin Crystals." . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 276 no PDB 4XYZ . "Crystal Structure Of K33 Linked Di-ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 277 no PDB 4Y1H . "Crystal Structure Of K33 Linked Tri-ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 278 no PDB 4Z9S . "Non-covalent Assembly Of Monoubiquitin That Mimics K11 Poly-ubiquitin" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 279 no PDB 4ZFR . "Catalytic Domain Of Sst2 F403a Mutant Bound To Ubiquitin" . . . . . 76.70 81 97.47 98.73 8.08e-46 . . . . 15689 1 280 no PDB 4ZFT . "Catalytic Domain Of Sst2 F403w Mutant Bound To Ubiquitin" . . . . . 76.70 81 97.47 98.73 8.08e-46 . . . . 15689 1 281 no PDB 5A5B . "Structure Of The 26s Proteasome-ubp6 Complex" . . . . . 72.82 76 98.67 100.00 8.51e-44 . . . . 15689 1 282 no PDB 5AF4 . "Structure Of Lys33-linked Diub" . . . . . 72.82 76 97.33 100.00 3.07e-43 . . . . 15689 1 283 no PDB 5AF5 . "Structure Of Lys33-linked Triub S.g. P 212121" . . . . . 70.87 73 97.26 100.00 8.96e-42 . . . . 15689 1 284 no PDB 5AF6 . "Structure Of Lys33-linked Diub Bound To Trabid Nzf1" . . . . . 72.82 76 97.33 100.00 3.07e-43 . . . . 15689 1 285 no PDB 5AIT . "A Complex Of Of Rnf4-ring Domain, Ubev2, Ubc13-ub (isopeptide Crosslink)" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 286 no PDB 5AIU . "A Complex Of Rnf4-ring Domain, Ubc13-ub (isopeptide Crosslink)" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 287 no PDB 5CAW . "Structure Of Pediculus Humanus Parkin Bound To Phospho-ubiquitin" . . . . . 72.82 76 97.33 98.67 5.28e-43 . . . . 15689 1 288 no DBJ BAA03983 . "polyubiquitin [Rattus norvegicus]" . . . . . 72.82 305 98.67 100.00 4.97e-41 . . . . 15689 1 289 no DBJ BAA09860 . "polyubiquitin [Homo sapiens]" . . . . . 72.82 611 98.67 100.00 1.49e-39 . . . . 15689 1 290 no DBJ BAA11842 . "ubiquitin [Cavia porcellus]" . . . . . 72.82 311 98.67 100.00 5.61e-41 . . . . 15689 1 291 no DBJ BAA11843 . "ubiquitin extention protein [Cavia porcellus]" . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 292 no DBJ BAA23486 . "polyubiquitin [Homo sapiens]" . . . . . 72.82 609 98.67 100.00 1.71e-39 . . . . 15689 1 293 no EMBL CAA28495 . "ubiquitin [Homo sapiens]" . . . . . 72.82 229 98.67 100.00 7.27e-42 . . . . 15689 1 294 no EMBL CAA30815 . "unnamed protein product [Cricetulus sp.]" . . . . . 71.84 223 97.30 98.65 1.90e-40 . . . . 15689 1 295 no EMBL CAA35999 . "ubiquitin [Mus musculus]" . . . . . 72.82 305 98.67 100.00 4.97e-41 . . . . 15689 1 296 no EMBL CAA37227 . "unnamed protein product [Drosophila melanogaster]" . . . . . 72.82 128 98.67 100.00 9.57e-44 . . . . 15689 1 297 no EMBL CAA37599 . "unnamed protein product [Manduca sexta]" . . . . . 74.76 155 97.40 98.70 2.08e-43 . . . . 15689 1 298 no GB AAA28154 . "polyubiquitin [Caenorhabditis elegans]" . . . . . 72.82 838 97.33 98.67 3.59e-38 . . . . 15689 1 299 no GB AAA28997 . "ubiquitin [Drosophila melanogaster]" . . . . . 72.82 231 98.67 100.00 7.33e-42 . . . . 15689 1 300 no GB AAA28998 . "ubiquitin-hybrid protein precursor [Drosophila melanogaster]" . . . . . 74.76 156 97.40 98.70 3.06e-43 . . . . 15689 1 301 no GB AAA28999 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 302 no GB AAA29000 . "ubiquitin, partial [Drosophila melanogaster]" . . . . . 72.82 76 97.33 98.67 5.52e-43 . . . . 15689 1 303 no PIR I50437 . "polyubiquitin 4 - chicken [Gallus gallus]" . . . . . 72.82 305 98.67 100.00 4.97e-41 . . . . 15689 1 304 no PIR I51568 . "polyubiquitin - African clawed frog (fragment)" . . . . . 75.73 167 97.44 98.72 3.41e-44 . . . . 15689 1 305 no PIR I65237 . "ubiquitin / ribosomal protein L40, cytosolic [validated] - rat" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 306 no PIR S13928 . "ubiquitin precursor - chicken [Gallus gallus]" . . . . . 72.82 229 98.67 100.00 6.96e-42 . . . . 15689 1 307 no PIR S21083 . "polyubiquitin 5 - Chinese hamster" . . . . . 72.82 381 98.67 100.00 2.25e-40 . . . . 15689 1 308 no PRF 0412265A . ubiquitin . . . . . 72.82 75 97.33 98.67 2.89e-43 . . . . 15689 1 309 no PRF 1212243A . "ubiquitin S1" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 310 no PRF 1212243B . "ubiquitin S5" . . . . . 67.96 77 97.14 98.57 2.40e-39 . . . . 15689 1 311 no PRF 1212243C . "ubiquitin S3" . . . . . 72.82 76 98.67 100.00 8.41e-44 . . . . 15689 1 312 no PRF 1212243D . "ubiquitin S2" . . . . . 67.96 77 97.14 98.57 3.05e-39 . . . . 15689 1 313 no REF NP_001005123 . "ubiquitin-60S ribosomal protein L40 [Xenopus (Silurana) tropicalis]" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 314 no REF NP_001006688 . "ubiquitin C [Xenopus (Silurana) tropicalis]" . . . . . 72.82 609 98.67 100.00 1.73e-39 . . . . 15689 1 315 no REF NP_001009117 . "polyubiquitin-B [Pan troglodytes]" . . . . . 72.82 229 98.67 100.00 7.27e-42 . . . . 15689 1 316 no REF NP_001009202 . "polyubiquitin-B [Ovis aries]" . . . . . 72.82 305 97.33 100.00 9.21e-41 . . . . 15689 1 317 no REF NP_001009286 . "ubiquitin-60S ribosomal protein L40 [Ovis aries]" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 318 no SP P0C273 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 319 no SP P0C275 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 320 no SP P0C276 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 1 321 no SP P0CG47 . "RecName: Full=Polyubiquitin-B; Contains: RecName: Full=Ubiquitin; Flags: Precursor" . . . . . 72.82 229 98.67 100.00 7.27e-42 . . . . 15689 1 322 no SP P0CG48 . "RecName: Full=Polyubiquitin-C; Contains: RecName: Full=Ubiquitin; Flags: Precursor" . . . . . 72.82 685 98.67 100.00 2.80e-39 . . . . 15689 1 323 no TPE CEL68433 . "TPA: ubiquitin / ribosomal protein CEP52 fusion protein, putative [Neospora caninum Liverpool]" . . . . . 72.82 129 97.33 100.00 3.86e-43 . . . . 15689 1 324 no TPE CEL70397 . "TPA: Ubiquitin, related [Neospora caninum Liverpool]" . . . . . 72.82 535 97.33 100.00 3.89e-39 . . . . 15689 1 325 no TPE CEL75964 . "TPA: ubiquitin / ribosomal protein CEP52 fusion protein, putative [Toxoplasma gondii VEG]" . . . . . 72.82 129 97.33 100.00 3.86e-43 . . . . 15689 1 326 no TPE CEL78064 . "TPA: polyubiquitin, putative [Toxoplasma gondii VEG]" . . . . . 72.82 307 97.33 100.00 1.84e-40 . . . . 15689 1 327 no TPG DAA18802 . "TPA: polyubiquitin [Bos taurus]" . . . . . 72.82 305 98.67 100.00 5.03e-41 . . . . 15689 1 328 no TPG DAA20663 . "TPA: ubiquitin C [Bos taurus]" . . . . . 72.82 314 97.33 98.67 2.56e-40 . . . . 15689 1 329 no TPG DAA20672 . "TPA: ubiquitin B-like [Bos taurus]" . . . . . 72.82 77 97.33 98.67 7.12e-43 . . . . 15689 1 330 no TPG DAA24675 . "TPA: 40S ribosomal protein S27a [Bos taurus]" . . . . . 74.76 156 97.40 98.70 2.14e-43 . . . . 15689 1 331 no TPG DAA28295 . "TPA: ubiquitin and ribosomal protein L40 [Bos taurus]" . . . . . 72.82 128 98.67 100.00 9.67e-44 . . . . 15689 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 . GLY . 15689 1 2 . SER . 15689 1 3 . LEU . 15689 1 4 . VAL . 15689 1 5 . PRO . 15689 1 6 . ARG . 15689 1 7 . GLY . 15689 1 8 . SER . 15689 1 9 . MET . 15689 1 10 . GLN . 15689 1 11 . ILE . 15689 1 12 . PHE . 15689 1 13 . VAL . 15689 1 14 . LYS . 15689 1 15 . THR . 15689 1 16 . LEU . 15689 1 17 . THR . 15689 1 18 . GLY . 15689 1 19 . LYS . 15689 1 20 . THR . 15689 1 21 . ILE . 15689 1 22 . THR . 15689 1 23 . LEU . 15689 1 24 . GLU . 15689 1 25 . VAL . 15689 1 26 . GLU . 15689 1 27 . PRO . 15689 1 28 . SER . 15689 1 29 . ASP . 15689 1 30 . THR . 15689 1 31 . ILE . 15689 1 32 . GLU . 15689 1 33 . ASN . 15689 1 34 . VAL . 15689 1 35 . LYS . 15689 1 36 . ALA . 15689 1 37 . LYS . 15689 1 38 . ILE . 15689 1 39 . GLN . 15689 1 40 . ASP . 15689 1 41 . LYS . 15689 1 42 . GLU . 15689 1 43 . GLY . 15689 1 44 . ILE . 15689 1 45 . PRO . 15689 1 46 . PRO . 15689 1 47 . ASP . 15689 1 48 . GLN . 15689 1 49 . GLN . 15689 1 50 . ARG . 15689 1 51 . LEU . 15689 1 52 . ILE . 15689 1 53 . PHE . 15689 1 54 . ALA . 15689 1 55 . GLY . 15689 1 56 . LYS . 15689 1 57 . GLN . 15689 1 58 . LEU . 15689 1 59 . GLU . 15689 1 60 . ASP . 15689 1 61 . GLY . 15689 1 62 . ARG . 15689 1 63 . THR . 15689 1 64 . LEU . 15689 1 65 . SER . 15689 1 66 . GLU . 15689 1 67 . TYR . 15689 1 68 . ASN . 15689 1 69 . ILE . 15689 1 70 . GLN . 15689 1 71 . LYS . 15689 1 72 . GLU . 15689 1 73 . SER . 15689 1 74 . THR . 15689 1 75 . LEU . 15689 1 76 . HIS . 15689 1 77 . LEU . 15689 1 78 . VAL . 15689 1 79 . LEU . 15689 1 80 . ARG . 15689 1 81 . LEU . 15689 1 82 . ARG . 15689 1 83 . GLY . 15689 1 84 . TYR . 15689 1 85 . ALA . 15689 1 86 . ASP . 15689 1 87 . LEU . 15689 1 88 . ARG . 15689 1 89 . GLU . 15689 1 90 . ASP . 15689 1 91 . PRO . 15689 1 92 . ASP . 15689 1 93 . ARG . 15689 1 94 . GLN . 15689 1 95 . ASP . 15689 1 96 . HIS . 15689 1 97 . HIS . 15689 1 98 . PRO . 15689 1 99 . GLY . 15689 1 100 . SER . 15689 1 101 . GLY . 15689 1 102 . ALA . 15689 1 103 . GLN . 15689 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 . GLY 1 1 15689 1 . SER 2 2 15689 1 . LEU 3 3 15689 1 . VAL 4 4 15689 1 . PRO 5 5 15689 1 . ARG 6 6 15689 1 . GLY 7 7 15689 1 . SER 8 8 15689 1 . MET 9 9 15689 1 . GLN 10 10 15689 1 . ILE 11 11 15689 1 . PHE 12 12 15689 1 . VAL 13 13 15689 1 . LYS 14 14 15689 1 . THR 15 15 15689 1 . LEU 16 16 15689 1 . THR 17 17 15689 1 . GLY 18 18 15689 1 . LYS 19 19 15689 1 . THR 20 20 15689 1 . ILE 21 21 15689 1 . THR 22 22 15689 1 . LEU 23 23 15689 1 . GLU 24 24 15689 1 . VAL 25 25 15689 1 . GLU 26 26 15689 1 . PRO 27 27 15689 1 . SER 28 28 15689 1 . ASP 29 29 15689 1 . THR 30 30 15689 1 . ILE 31 31 15689 1 . GLU 32 32 15689 1 . ASN 33 33 15689 1 . VAL 34 34 15689 1 . LYS 35 35 15689 1 . ALA 36 36 15689 1 . LYS 37 37 15689 1 . ILE 38 38 15689 1 . GLN 39 39 15689 1 . ASP 40 40 15689 1 . LYS 41 41 15689 1 . GLU 42 42 15689 1 . GLY 43 43 15689 1 . ILE 44 44 15689 1 . PRO 45 45 15689 1 . PRO 46 46 15689 1 . ASP 47 47 15689 1 . GLN 48 48 15689 1 . GLN 49 49 15689 1 . ARG 50 50 15689 1 . LEU 51 51 15689 1 . ILE 52 52 15689 1 . PHE 53 53 15689 1 . ALA 54 54 15689 1 . GLY 55 55 15689 1 . LYS 56 56 15689 1 . GLN 57 57 15689 1 . LEU 58 58 15689 1 . GLU 59 59 15689 1 . ASP 60 60 15689 1 . GLY 61 61 15689 1 . ARG 62 62 15689 1 . THR 63 63 15689 1 . LEU 64 64 15689 1 . SER 65 65 15689 1 . GLU 66 66 15689 1 . TYR 67 67 15689 1 . ASN 68 68 15689 1 . ILE 69 69 15689 1 . GLN 70 70 15689 1 . LYS 71 71 15689 1 . GLU 72 72 15689 1 . SER 73 73 15689 1 . THR 74 74 15689 1 . LEU 75 75 15689 1 . HIS 76 76 15689 1 . LEU 77 77 15689 1 . VAL 78 78 15689 1 . LEU 79 79 15689 1 . ARG 80 80 15689 1 . LEU 81 81 15689 1 . ARG 82 82 15689 1 . GLY 83 83 15689 1 . TYR 84 84 15689 1 . ALA 85 85 15689 1 . ASP 86 86 15689 1 . LEU 87 87 15689 1 . ARG 88 88 15689 1 . GLU 89 89 15689 1 . ASP 90 90 15689 1 . PRO 91 91 15689 1 . ASP 92 92 15689 1 . ARG 93 93 15689 1 . GLN 94 94 15689 1 . ASP 95 95 15689 1 . HIS 96 96 15689 1 . HIS 97 97 15689 1 . PRO 98 98 15689 1 . GLY 99 99 15689 1 . SER 100 100 15689 1 . GLY 101 101 15689 1 . ALA 102 102 15689 1 . GLN 103 103 15689 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 15689 _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 $UBB . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . TA0895 . . . . 15689 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 15689 _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 $UBB . 'recombinant technology' 'ESCHERICHIA COLI' . . . ESCHERICHIA COLI BL21(DE3) . . . . . . . . . . . . PLASMID . . PET . . . . . . 15689 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 15689 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _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 UBB '[U-98% 13C; U-98% 15N]' . . 1 $UBB . . 1 . . mM . . . . 15689 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 15689 _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' 50 . mM 15689 1 pH 7.0 . pH 15689 1 pressure 1 . atm 15689 1 temperature 298 . K 15689 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 15689 _Software.ID 1 _Software.Name CYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert P.' . . 15689 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 15689 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 15689 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_500 _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode 500 _NMR_spectrometer_list.Entry_ID 15689 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker DRX . 500 . . . 15689 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 15689 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15689 1 2 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15689 1 3 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15689 1 4 '3D HBHA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15689 1 5 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15689 1 6 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15689 1 7 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15689 1 8 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15689 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 15689 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.251449530 . . . . . . . . . 15689 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 15689 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . . . . . . . 15689 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 15689 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 15689 1 2 '3D HNCACB' . . . 15689 1 3 '3D HNCA' . . . 15689 1 4 '3D HBHA(CO)NH' . . . 15689 1 5 '3D HCCH-TOCSY' . . . 15689 1 6 '3D 1H-13C NOESY' . . . 15689 1 7 '3D 1H-15N NOESY' . . . 15689 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 GLY HA2 H 1 3.920 0.020 . 2 . . . . 1 GLY HA2 . 15689 1 2 . 1 1 1 1 GLY HA3 H 1 3.920 0.020 . 2 . . . . 1 GLY HA3 . 15689 1 3 . 1 1 1 1 GLY CA C 13 45.200 0.200 . 1 . . . . 1 GLY CA . 15689 1 4 . 1 1 2 2 SER H H 1 8.160 0.020 . 1 . . . . 2 SER H . 15689 1 5 . 1 1 2 2 SER HA H 1 4.370 0.020 . 1 . . . . 2 SER HA . 15689 1 6 . 1 1 2 2 SER HB2 H 1 3.760 0.020 . 2 . . . . 2 SER HB2 . 15689 1 7 . 1 1 2 2 SER HB3 H 1 3.762 0.020 . 2 . . . . 2 SER HB3 . 15689 1 8 . 1 1 2 2 SER HG H 1 5.044 0.020 . 1 . . . . 2 SER HG . 15689 1 9 . 1 1 2 2 SER CA C 13 58.300 0.200 . 1 . . . . 2 SER CA . 15689 1 10 . 1 1 2 2 SER CB C 13 63.900 0.200 . 1 . . . . 2 SER CB . 15689 1 11 . 1 1 2 2 SER N N 15 115.600 0.200 . 1 . . . . 2 SER N . 15689 1 12 . 1 1 3 3 LEU H H 1 8.250 0.020 . 1 . . . . 3 LEU H . 15689 1 13 . 1 1 3 3 LEU HA H 1 4.280 0.020 . 1 . . . . 3 LEU HA . 15689 1 14 . 1 1 3 3 LEU HB2 H 1 3.760 0.020 . 2 . . . . 3 LEU HB2 . 15689 1 15 . 1 1 3 3 LEU HB3 H 1 1.500 0.020 . 2 . . . . 3 LEU HB3 . 15689 1 16 . 1 1 3 3 LEU HG H 1 1.500 0.020 . 1 . . . . 3 LEU HG . 15689 1 17 . 1 1 3 3 LEU CA C 13 55.200 0.200 . 1 . . . . 3 LEU CA . 15689 1 18 . 1 1 3 3 LEU CB C 13 42.100 0.200 . 1 . . . . 3 LEU CB . 15689 1 19 . 1 1 3 3 LEU N N 15 124.100 0.200 . 1 . . . . 3 LEU N . 15689 1 20 . 1 1 4 4 VAL H H 1 7.950 0.020 . 1 . . . . 4 VAL H . 15689 1 21 . 1 1 4 4 VAL HA H 1 4.680 0.020 . 1 . . . . 4 VAL HA . 15689 1 22 . 1 1 4 4 VAL HB H 1 1.920 0.020 . 1 . . . . 4 VAL HB . 15689 1 23 . 1 1 4 4 VAL HG21 H 1 1.500 0.020 . 2 . . . . 4 VAL HG2 . 15689 1 24 . 1 1 4 4 VAL HG22 H 1 1.500 0.020 . 2 . . . . 4 VAL HG2 . 15689 1 25 . 1 1 4 4 VAL HG23 H 1 1.500 0.020 . 2 . . . . 4 VAL HG2 . 15689 1 26 . 1 1 4 4 VAL CA C 13 59.800 0.200 . 1 . . . . 4 VAL CA . 15689 1 27 . 1 1 4 4 VAL CB C 13 32.500 0.200 . 1 . . . . 4 VAL CB . 15689 1 28 . 1 1 4 4 VAL N N 15 122.600 0.200 . 1 . . . . 4 VAL N . 15689 1 29 . 1 1 5 5 PRO CA C 13 63.100 0.200 . 1 . . . . 5 PRO CA . 15689 1 30 . 1 1 5 5 PRO CB C 13 32.000 0.200 . 1 . . . . 5 PRO CB . 15689 1 31 . 1 1 5 5 PRO CG C 13 32.050 0.200 . 1 . . . . 5 PRO CG . 15689 1 32 . 1 1 6 6 ARG H H 1 8.360 0.020 . 1 . . . . 6 ARG H . 15689 1 33 . 1 1 6 6 ARG HA H 1 4.250 0.020 . 1 . . . . 6 ARG HA . 15689 1 34 . 1 1 6 6 ARG HB2 H 1 1.760 0.020 . 2 . . . . 6 ARG HB2 . 15689 1 35 . 1 1 6 6 ARG HB3 H 1 1.650 0.020 . 2 . . . . 6 ARG HB3 . 15689 1 36 . 1 1 6 6 ARG CA C 13 56.000 0.200 . 1 . . . . 6 ARG CA . 15689 1 37 . 1 1 6 6 ARG CB C 13 30.900 0.200 . 1 . . . . 6 ARG CB . 15689 1 38 . 1 1 6 6 ARG N N 15 121.800 0.200 . 1 . . . . 6 ARG N . 15689 1 39 . 1 1 7 7 GLY H H 1 8.460 0.020 . 1 . . . . 7 GLY H . 15689 1 40 . 1 1 7 7 GLY HA2 H 1 3.940 0.020 . 2 . . . . 7 GLY HA2 . 15689 1 41 . 1 1 7 7 GLY HA3 H 1 3.760 0.020 . 2 . . . . 7 GLY HA3 . 15689 1 42 . 1 1 7 7 GLY CA C 13 45.000 0.200 . 1 . . . . 7 GLY CA . 15689 1 43 . 1 1 7 7 GLY N N 15 110.700 0.200 . 1 . . . . 7 GLY N . 15689 1 44 . 1 1 8 8 SER H H 1 7.990 0.020 . 1 . . . . 8 SER H . 15689 1 45 . 1 1 8 8 SER HA H 1 4.450 0.020 . 1 . . . . 8 SER HA . 15689 1 46 . 1 1 8 8 SER HB2 H 1 3.745 0.020 . 2 . . . . 8 SER HB2 . 15689 1 47 . 1 1 8 8 SER HB3 H 1 3.745 0.020 . 2 . . . . 8 SER HB3 . 15689 1 48 . 1 1 8 8 SER CA C 13 58.900 0.200 . 1 . . . . 8 SER CA . 15689 1 49 . 1 1 8 8 SER CB C 13 64.200 0.200 . 1 . . . . 8 SER CB . 15689 1 50 . 1 1 8 8 SER N N 15 115.500 0.200 . 1 . . . . 8 SER N . 15689 1 51 . 1 1 9 9 MET H H 1 9.040 0.020 . 1 . . . . 9 MET H . 15689 1 52 . 1 1 9 9 MET HA H 1 4.610 0.020 . 1 . . . . 9 MET HA . 15689 1 53 . 1 1 9 9 MET HB2 H 1 1.840 0.020 . 2 . . . . 9 MET HB2 . 15689 1 54 . 1 1 9 9 MET HB3 H 1 1.979 0.020 . 2 . . . . 9 MET HB3 . 15689 1 55 . 1 1 9 9 MET HE1 H 1 1.850 0.020 . . . . . . 9 MET HE . 15689 1 56 . 1 1 9 9 MET HE2 H 1 1.850 0.020 . . . . . . 9 MET HE . 15689 1 57 . 1 1 9 9 MET HE3 H 1 1.850 0.020 . . . . . . 9 MET HE . 15689 1 58 . 1 1 9 9 MET HG2 H 1 2.263 0.020 . 2 . . . . 9 MET HG2 . 15689 1 59 . 1 1 9 9 MET HG3 H 1 2.238 0.020 . 2 . . . . 9 MET HG3 . 15689 1 60 . 1 1 9 9 MET CA C 13 54.400 0.200 . 1 . . . . 9 MET CA . 15689 1 61 . 1 1 9 9 MET CB C 13 35.400 0.200 . 1 . . . . 9 MET CB . 15689 1 62 . 1 1 9 9 MET CE C 13 27.010 0.200 . 1 . . . . 9 MET CE . 15689 1 63 . 1 1 9 9 MET CG C 13 31.631 0.200 . 1 . . . . 9 MET CG . 15689 1 64 . 1 1 9 9 MET N N 15 120.500 0.200 . 1 . . . . 9 MET N . 15689 1 65 . 1 1 10 10 GLN H H 1 8.270 0.020 . 1 . . . . 10 GLN H . 15689 1 66 . 1 1 10 10 GLN HA H 1 5.270 0.020 . 1 . . . . 10 GLN HA . 15689 1 67 . 1 1 10 10 GLN HB2 H 1 1.840 0.020 . 2 . . . . 10 GLN HB2 . 15689 1 68 . 1 1 10 10 GLN HB3 H 1 2.113 0.020 . 2 . . . . 10 GLN HB3 . 15689 1 69 . 1 1 10 10 GLN HG2 H 1 1.715 0.020 . 2 . . . . 10 GLN HG2 . 15689 1 70 . 1 1 10 10 GLN HG3 H 1 1.512 0.020 . 2 . . . . 10 GLN HG3 . 15689 1 71 . 1 1 10 10 GLN CA C 13 54.200 0.200 . 1 . . . . 10 GLN CA . 15689 1 72 . 1 1 10 10 GLN CB C 13 30.500 0.200 . 1 . . . . 10 GLN CB . 15689 1 73 . 1 1 10 10 GLN CG C 13 34.363 0.200 . 1 . . . . 10 GLN CG . 15689 1 74 . 1 1 10 10 GLN N N 15 121.000 0.200 . 1 . . . . 10 GLN N . 15689 1 75 . 1 1 11 11 ILE H H 1 8.270 0.020 . 1 . . . . 11 ILE H . 15689 1 76 . 1 1 11 11 ILE HA H 1 4.100 0.020 . 1 . . . . 11 ILE HA . 15689 1 77 . 1 1 11 11 ILE HB H 1 1.720 0.020 . 1 . . . . 11 ILE HB . 15689 1 78 . 1 1 11 11 ILE HD11 H 1 4.104 0.020 . 1 . . . . 11 ILE HD1 . 15689 1 79 . 1 1 11 11 ILE HD12 H 1 4.104 0.020 . 1 . . . . 11 ILE HD1 . 15689 1 80 . 1 1 11 11 ILE HD13 H 1 4.104 0.020 . 1 . . . . 11 ILE HD1 . 15689 1 81 . 1 1 11 11 ILE HG12 H 1 1.669 0.020 . 2 . . . . 11 ILE HG12 . 15689 1 82 . 1 1 11 11 ILE HG13 H 1 0.535 0.020 . 2 . . . . 11 ILE HG13 . 15689 1 83 . 1 1 11 11 ILE HG21 H 1 0.504 0.020 . 1 . . . . 11 ILE HG2 . 15689 1 84 . 1 1 11 11 ILE HG22 H 1 0.504 0.020 . 1 . . . . 11 ILE HG2 . 15689 1 85 . 1 1 11 11 ILE HG23 H 1 0.504 0.020 . 1 . . . . 11 ILE HG2 . 15689 1 86 . 1 1 11 11 ILE CA C 13 59.400 0.200 . 1 . . . . 11 ILE CA . 15689 1 87 . 1 1 11 11 ILE CB C 13 41.800 0.200 . 1 . . . . 11 ILE CB . 15689 1 88 . 1 1 11 11 ILE CD1 C 13 14.132 0.200 . 1 . . . . 11 ILE CD1 . 15689 1 89 . 1 1 11 11 ILE CG1 C 13 17.817 0.200 . 1 . . . . 11 ILE CG1 . 15689 1 90 . 1 1 11 11 ILE CG2 C 13 17.817 0.200 . 1 . . . . 11 ILE CG2 . 15689 1 91 . 1 1 11 11 ILE N N 15 114.600 0.200 . 1 . . . . 11 ILE N . 15689 1 92 . 1 1 12 12 PHE H H 1 8.520 0.020 . 1 . . . . 12 PHE H . 15689 1 93 . 1 1 12 12 PHE HA H 1 5.540 0.020 . 1 . . . . 12 PHE HA . 15689 1 94 . 1 1 12 12 PHE HB2 H 1 2.950 0.020 . 2 . . . . 12 PHE HB2 . 15689 1 95 . 1 1 12 12 PHE HB3 H 1 2.789 0.020 . 2 . . . . 12 PHE HB3 . 15689 1 96 . 1 1 12 12 PHE CA C 13 55.000 0.200 . 1 . . . . 12 PHE CA . 15689 1 97 . 1 1 12 12 PHE CB C 13 41.200 0.200 . 1 . . . . 12 PHE CB . 15689 1 98 . 1 1 12 12 PHE N N 15 118.600 0.200 . 1 . . . . 12 PHE N . 15689 1 99 . 1 1 13 13 VAL H H 1 9.230 0.020 . 1 . . . . 13 VAL H . 15689 1 100 . 1 1 13 13 VAL HA H 1 4.740 0.020 . 1 . . . . 13 VAL HA . 15689 1 101 . 1 1 13 13 VAL HB H 1 1.810 0.020 . 1 . . . . 13 VAL HB . 15689 1 102 . 1 1 13 13 VAL HG11 H 1 0.639 0.020 . 2 . . . . 13 VAL HG1 . 15689 1 103 . 1 1 13 13 VAL HG12 H 1 0.639 0.020 . 2 . . . . 13 VAL HG1 . 15689 1 104 . 1 1 13 13 VAL HG13 H 1 0.639 0.020 . 2 . . . . 13 VAL HG1 . 15689 1 105 . 1 1 13 13 VAL HG21 H 1 0.595 0.020 . 2 . . . . 13 VAL HG2 . 15689 1 106 . 1 1 13 13 VAL HG22 H 1 0.595 0.020 . 2 . . . . 13 VAL HG2 . 15689 1 107 . 1 1 13 13 VAL HG23 H 1 0.595 0.020 . 2 . . . . 13 VAL HG2 . 15689 1 108 . 1 1 13 13 VAL CA C 13 60.300 0.200 . 1 . . . . 13 VAL CA . 15689 1 109 . 1 1 13 13 VAL CB C 13 34.100 0.200 . 1 . . . . 13 VAL CB . 15689 1 110 . 1 1 13 13 VAL CG1 C 13 22.416 0.200 . 2 . . . . 13 VAL CG1 . 15689 1 111 . 1 1 13 13 VAL CG2 C 13 20.773 0.200 . 2 . . . . 13 VAL CG2 . 15689 1 112 . 1 1 13 13 VAL N N 15 121.400 0.200 . 1 . . . . 13 VAL N . 15689 1 113 . 1 1 14 14 LYS H H 1 8.910 0.020 . 1 . . . . 14 LYS H . 15689 1 114 . 1 1 14 14 LYS HA H 1 5.190 0.020 . 1 . . . . 14 LYS HA . 15689 1 115 . 1 1 14 14 LYS HB2 H 1 1.810 0.020 . 2 . . . . 14 LYS HB2 . 15689 1 116 . 1 1 14 14 LYS HD2 H 1 1.609 0.020 . 2 . . . . 14 LYS HD2 . 15689 1 117 . 1 1 14 14 LYS HD3 H 1 1.377 0.020 . 2 . . . . 14 LYS HD3 . 15689 1 118 . 1 1 14 14 LYS HE2 H 1 2.798 0.020 . 2 . . . . 14 LYS HE2 . 15689 1 119 . 1 1 14 14 LYS HE3 H 1 2.798 0.020 . 2 . . . . 14 LYS HE3 . 15689 1 120 . 1 1 14 14 LYS HG2 H 1 1.322 0.020 . 2 . . . . 14 LYS HG2 . 15689 1 121 . 1 1 14 14 LYS HG3 H 1 1.182 0.020 . 2 . . . . 14 LYS HG3 . 15689 1 122 . 1 1 14 14 LYS CA C 13 54.600 0.200 . 1 . . . . 14 LYS CA . 15689 1 123 . 1 1 14 14 LYS CB C 13 34.300 0.200 . 1 . . . . 14 LYS CB . 15689 1 124 . 1 1 14 14 LYS CD C 13 29.123 0.200 . 1 . . . . 14 LYS CD . 15689 1 125 . 1 1 14 14 LYS CG C 13 24.949 0.200 . 1 . . . . 14 LYS CG . 15689 1 126 . 1 1 14 14 LYS N N 15 128.000 0.200 . 1 . . . . 14 LYS N . 15689 1 127 . 1 1 15 15 THR H H 1 8.650 0.020 . 1 . . . . 15 THR H . 15689 1 128 . 1 1 15 15 THR HA H 1 4.870 0.020 . 1 . . . . 15 THR HA . 15689 1 129 . 1 1 15 15 THR HB H 1 4.700 0.020 . 1 . . . . 15 THR HB . 15689 1 130 . 1 1 15 15 THR HG21 H 1 1.086 0.020 . . . . . . 15 THR HG2 . 15689 1 131 . 1 1 15 15 THR HG22 H 1 1.086 0.020 . . . . . . 15 THR HG2 . 15689 1 132 . 1 1 15 15 THR HG23 H 1 1.086 0.020 . . . . . . 15 THR HG2 . 15689 1 133 . 1 1 15 15 THR CA C 13 60.300 0.200 . 1 . . . . 15 THR CA . 15689 1 134 . 1 1 15 15 THR CB C 13 70.600 0.200 . 1 . . . . 15 THR CB . 15689 1 135 . 1 1 15 15 THR CG2 C 13 21.486 0.200 . 1 . . . . 15 THR CG2 . 15689 1 136 . 1 1 15 15 THR N N 15 115.300 0.200 . 1 . . . . 15 THR N . 15689 1 137 . 1 1 16 16 LEU H H 1 9.070 0.020 . 1 . . . . 16 LEU H . 15689 1 138 . 1 1 16 16 LEU HA H 1 4.210 0.020 . 1 . . . . 16 LEU HA . 15689 1 139 . 1 1 16 16 LEU HB2 H 1 1.843 0.020 . 2 . . . . 16 LEU HB2 . 15689 1 140 . 1 1 16 16 LEU HB3 H 1 1.789 0.020 . 2 . . . . 16 LEU HB3 . 15689 1 141 . 1 1 16 16 LEU HD11 H 1 0.875 0.020 . 2 . . . . 16 LEU HD1 . 15689 1 142 . 1 1 16 16 LEU HD12 H 1 0.875 0.020 . 2 . . . . 16 LEU HD1 . 15689 1 143 . 1 1 16 16 LEU HD13 H 1 0.875 0.020 . 2 . . . . 16 LEU HD1 . 15689 1 144 . 1 1 16 16 LEU HD21 H 1 0.945 0.020 . 2 . . . . 16 LEU HD2 . 15689 1 145 . 1 1 16 16 LEU HD22 H 1 0.945 0.020 . 2 . . . . 16 LEU HD2 . 15689 1 146 . 1 1 16 16 LEU HD23 H 1 0.945 0.020 . 2 . . . . 16 LEU HD2 . 15689 1 147 . 1 1 16 16 LEU HG H 1 1.665 0.020 . 1 . . . . 16 LEU HG . 15689 1 148 . 1 1 16 16 LEU CA C 13 57.400 0.200 . 1 . . . . 16 LEU CA . 15689 1 149 . 1 1 16 16 LEU CB C 13 41.800 0.200 . 1 . . . . 16 LEU CB . 15689 1 150 . 1 1 16 16 LEU CD1 C 13 25.241 0.200 . 2 . . . . 16 LEU CD1 . 15689 1 151 . 1 1 16 16 LEU CD2 C 13 23.640 0.200 . 2 . . . . 16 LEU CD2 . 15689 1 152 . 1 1 16 16 LEU CG C 13 27.315 0.200 . 1 . . . . 16 LEU CG . 15689 1 153 . 1 1 16 16 LEU N N 15 121.400 0.200 . 1 . . . . 16 LEU N . 15689 1 154 . 1 1 17 17 THR H H 1 7.560 0.020 . 1 . . . . 17 THR H . 15689 1 155 . 1 1 17 17 THR HA H 1 4.330 0.020 . 1 . . . . 17 THR HA . 15689 1 156 . 1 1 17 17 THR HB H 1 4.480 0.020 . 1 . . . . 17 THR HB . 15689 1 157 . 1 1 17 17 THR HG21 H 1 1.159 0.020 . . . . . . 17 THR HG2 . 15689 1 158 . 1 1 17 17 THR HG22 H 1 1.159 0.020 . . . . . . 17 THR HG2 . 15689 1 159 . 1 1 17 17 THR HG23 H 1 1.159 0.020 . . . . . . 17 THR HG2 . 15689 1 160 . 1 1 17 17 THR CA C 13 61.400 0.200 . 1 . . . . 17 THR CA . 15689 1 161 . 1 1 17 17 THR CB C 13 68.900 0.200 . 1 . . . . 17 THR CB . 15689 1 162 . 1 1 17 17 THR CG2 C 13 21.750 0.200 . 1 . . . . 17 THR CG2 . 15689 1 163 . 1 1 17 17 THR N N 15 105.900 0.200 . 1 . . . . 17 THR N . 15689 1 164 . 1 1 18 18 GLY H H 1 7.750 0.020 . 1 . . . . 18 GLY H . 15689 1 165 . 1 1 18 18 GLY HA2 H 1 4.250 0.020 . 2 . . . . 18 GLY HA2 . 15689 1 166 . 1 1 18 18 GLY HA3 H 1 3.520 0.020 . 2 . . . . 18 GLY HA3 . 15689 1 167 . 1 1 18 18 GLY CA C 13 45.300 0.200 . 1 . . . . 18 GLY CA . 15689 1 168 . 1 1 18 18 GLY N N 15 109.300 0.200 . 1 . . . . 18 GLY N . 15689 1 169 . 1 1 19 19 LYS H H 1 7.210 0.020 . 1 . . . . 19 LYS H . 15689 1 170 . 1 1 19 19 LYS HA H 1 4.260 0.020 . 1 . . . . 19 LYS HA . 15689 1 171 . 1 1 19 19 LYS HB2 H 1 1.710 0.020 . 2 . . . . 19 LYS HB2 . 15689 1 172 . 1 1 19 19 LYS HB3 H 1 1.600 0.020 . 2 . . . . 19 LYS HB3 . 15689 1 173 . 1 1 19 19 LYS HG2 H 1 1.319 0.020 . 2 . . . . 19 LYS HG2 . 15689 1 174 . 1 1 19 19 LYS HG3 H 1 1.152 0.020 . 2 . . . . 19 LYS HG3 . 15689 1 175 . 1 1 19 19 LYS CA C 13 56.300 0.200 . 1 . . . . 19 LYS CA . 15689 1 176 . 1 1 19 19 LYS CB C 13 33.200 0.200 . 1 . . . . 19 LYS CB . 15689 1 177 . 1 1 19 19 LYS CD C 13 29.320 0.200 . 1 . . . . 19 LYS CD . 15689 1 178 . 1 1 19 19 LYS CG C 13 24.998 0.200 . 1 . . . . 19 LYS CG . 15689 1 179 . 1 1 19 19 LYS N N 15 122.000 0.200 . 1 . . . . 19 LYS N . 15689 1 180 . 1 1 20 20 THR H H 1 8.570 0.020 . 1 . . . . 20 THR H . 15689 1 181 . 1 1 20 20 THR HA H 1 4.950 0.020 . 1 . . . . 20 THR HA . 15689 1 182 . 1 1 20 20 THR HB H 1 3.830 0.020 . 1 . . . . 20 THR HB . 15689 1 183 . 1 1 20 20 THR HG21 H 1 0.968 0.020 . . . . . . 20 THR HG2 . 15689 1 184 . 1 1 20 20 THR HG22 H 1 0.968 0.020 . . . . . . 20 THR HG2 . 15689 1 185 . 1 1 20 20 THR HG23 H 1 0.968 0.020 . . . . . . 20 THR HG2 . 15689 1 186 . 1 1 20 20 THR CA C 13 62.200 0.200 . 1 . . . . 20 THR CA . 15689 1 187 . 1 1 20 20 THR CB C 13 69.700 0.200 . 1 . . . . 20 THR CB . 15689 1 188 . 1 1 20 20 THR CG2 C 13 21.839 0.200 . 1 . . . . 20 THR CG2 . 15689 1 189 . 1 1 20 20 THR N N 15 120.700 0.200 . 1 . . . . 20 THR N . 15689 1 190 . 1 1 21 21 ILE H H 1 9.510 0.020 . 1 . . . . 21 ILE H . 15689 1 191 . 1 1 21 21 ILE HA H 1 4.390 0.020 . 1 . . . . 21 ILE HA . 15689 1 192 . 1 1 21 21 ILE HB H 1 1.770 0.020 . 1 . . . . 21 ILE HB . 15689 1 193 . 1 1 21 21 ILE HD11 H 1 0.628 0.020 . 1 . . . . 21 ILE HD1 . 15689 1 194 . 1 1 21 21 ILE HD12 H 1 0.628 0.020 . 1 . . . . 21 ILE HD1 . 15689 1 195 . 1 1 21 21 ILE HD13 H 1 0.628 0.020 . 1 . . . . 21 ILE HD1 . 15689 1 196 . 1 1 21 21 ILE HG12 H 1 1.361 0.020 . 2 . . . . 21 ILE HG12 . 15689 1 197 . 1 1 21 21 ILE HG13 H 1 0.991 0.020 . 2 . . . . 21 ILE HG13 . 15689 1 198 . 1 1 21 21 ILE HG21 H 1 0.781 0.020 . 1 . . . . 21 ILE HG2 . 15689 1 199 . 1 1 21 21 ILE HG22 H 1 0.781 0.020 . 1 . . . . 21 ILE HG2 . 15689 1 200 . 1 1 21 21 ILE HG23 H 1 0.781 0.020 . 1 . . . . 21 ILE HG2 . 15689 1 201 . 1 1 21 21 ILE CA C 13 60.000 0.200 . 1 . . . . 21 ILE CA . 15689 1 202 . 1 1 21 21 ILE CB C 13 40.700 0.200 . 1 . . . . 21 ILE CB . 15689 1 203 . 1 1 21 21 ILE CD1 C 13 14.385 0.200 . 1 . . . . 21 ILE CD1 . 15689 1 204 . 1 1 21 21 ILE CG1 C 13 26.996 0.200 . 1 . . . . 21 ILE CG1 . 15689 1 205 . 1 1 21 21 ILE CG2 C 13 17.666 0.200 . 1 . . . . 21 ILE CG2 . 15689 1 206 . 1 1 21 21 ILE N N 15 128.200 0.200 . 1 . . . . 21 ILE N . 15689 1 207 . 1 1 22 22 THR H H 1 8.700 0.020 . 1 . . . . 22 THR H . 15689 1 208 . 1 1 22 22 THR HA H 1 4.860 0.020 . 1 . . . . 22 THR HA . 15689 1 209 . 1 1 22 22 THR HB H 1 3.930 0.020 . 1 . . . . 22 THR HB . 15689 1 210 . 1 1 22 22 THR HG21 H 1 1.017 0.020 . . . . . . 22 THR HG2 . 15689 1 211 . 1 1 22 22 THR HG22 H 1 1.017 0.020 . . . . . . 22 THR HG2 . 15689 1 212 . 1 1 22 22 THR HG23 H 1 1.017 0.020 . . . . . . 22 THR HG2 . 15689 1 213 . 1 1 22 22 THR CA C 13 62.100 0.200 . 1 . . . . 22 THR CA . 15689 1 214 . 1 1 22 22 THR CB C 13 69.500 0.200 . 1 . . . . 22 THR CB . 15689 1 215 . 1 1 22 22 THR CG2 C 13 21.660 0.200 . 1 . . . . 22 THR CG2 . 15689 1 216 . 1 1 22 22 THR N N 15 122.300 0.200 . 1 . . . . 22 THR N . 15689 1 217 . 1 1 23 23 LEU H H 1 8.720 0.020 . 1 . . . . 23 LEU H . 15689 1 218 . 1 1 23 23 LEU HA H 1 4.690 0.020 . 1 . . . . 23 LEU HA . 15689 1 219 . 1 1 23 23 LEU HB2 H 1 1.290 0.020 . 2 . . . . 23 LEU HB2 . 15689 1 220 . 1 1 23 23 LEU HB3 H 1 1.332 0.020 . 2 . . . . 23 LEU HB3 . 15689 1 221 . 1 1 23 23 LEU HD11 H 1 0.678 0.020 . 2 . . . . 23 LEU HD1 . 15689 1 222 . 1 1 23 23 LEU HD12 H 1 0.678 0.020 . 2 . . . . 23 LEU HD1 . 15689 1 223 . 1 1 23 23 LEU HD13 H 1 0.678 0.020 . 2 . . . . 23 LEU HD1 . 15689 1 224 . 1 1 23 23 LEU HD21 H 1 0.623 0.020 . 2 . . . . 23 LEU HD2 . 15689 1 225 . 1 1 23 23 LEU HD22 H 1 0.623 0.020 . 2 . . . . 23 LEU HD2 . 15689 1 226 . 1 1 23 23 LEU HD23 H 1 0.623 0.020 . 2 . . . . 23 LEU HD2 . 15689 1 227 . 1 1 23 23 LEU HG H 1 1.119 0.020 . 1 . . . . 23 LEU HG . 15689 1 228 . 1 1 23 23 LEU CA C 13 52.700 0.200 . 1 . . . . 23 LEU CA . 15689 1 229 . 1 1 23 23 LEU CB C 13 46.600 0.200 . 1 . . . . 23 LEU CB . 15689 1 230 . 1 1 23 23 LEU CD1 C 13 24.065 0.200 . 2 . . . . 23 LEU CD1 . 15689 1 231 . 1 1 23 23 LEU CD2 C 13 24.065 0.200 . 2 . . . . 23 LEU CD2 . 15689 1 232 . 1 1 23 23 LEU CG C 13 26.970 0.200 . 1 . . . . 23 LEU CG . 15689 1 233 . 1 1 23 23 LEU N N 15 125.400 0.200 . 1 . . . . 23 LEU N . 15689 1 234 . 1 1 24 24 GLU H H 1 8.080 0.020 . 1 . . . . 24 GLU H . 15689 1 235 . 1 1 24 24 GLU HA H 1 4.800 0.020 . 1 . . . . 24 GLU HA . 15689 1 236 . 1 1 24 24 GLU HB2 H 1 1.800 0.020 . 2 . . . . 24 GLU HB2 . 15689 1 237 . 1 1 24 24 GLU HB3 H 1 2.057 0.020 . 2 . . . . 24 GLU HB3 . 15689 1 238 . 1 1 24 24 GLU CA C 13 55.400 0.200 . 1 . . . . 24 GLU CA . 15689 1 239 . 1 1 24 24 GLU CB C 13 30.100 0.200 . 1 . . . . 24 GLU CB . 15689 1 240 . 1 1 24 24 GLU CG C 13 36.477 0.200 . 1 . . . . 24 GLU CG . 15689 1 241 . 1 1 24 24 GLU N N 15 121.800 0.200 . 1 . . . . 24 GLU N . 15689 1 242 . 1 1 25 25 VAL H H 1 8.800 0.020 . 1 . . . . 25 VAL H . 15689 1 243 . 1 1 25 25 VAL HA H 1 4.640 0.020 . 1 . . . . 25 VAL HA . 15689 1 244 . 1 1 25 25 VAL HB H 1 2.290 0.020 . 1 . . . . 25 VAL HB . 15689 1 245 . 1 1 25 25 VAL HG11 H 1 0.599 0.020 . 2 . . . . 25 VAL HG1 . 15689 1 246 . 1 1 25 25 VAL HG12 H 1 0.599 0.020 . 2 . . . . 25 VAL HG1 . 15689 1 247 . 1 1 25 25 VAL HG13 H 1 0.599 0.020 . 2 . . . . 25 VAL HG1 . 15689 1 248 . 1 1 25 25 VAL HG21 H 1 0.359 0.020 . 2 . . . . 25 VAL HG2 . 15689 1 249 . 1 1 25 25 VAL HG22 H 1 0.359 0.020 . 2 . . . . 25 VAL HG2 . 15689 1 250 . 1 1 25 25 VAL HG23 H 1 0.359 0.020 . 2 . . . . 25 VAL HG2 . 15689 1 251 . 1 1 25 25 VAL CA C 13 58.600 0.200 . 1 . . . . 25 VAL CA . 15689 1 252 . 1 1 25 25 VAL CB C 13 36.300 0.200 . 1 . . . . 25 VAL CB . 15689 1 253 . 1 1 25 25 VAL CG1 C 13 22.075 0.200 . 2 . . . . 25 VAL CG1 . 15689 1 254 . 1 1 25 25 VAL CG2 C 13 19.315 0.200 . 2 . . . . 25 VAL CG2 . 15689 1 255 . 1 1 25 25 VAL N N 15 116.700 0.200 . 1 . . . . 25 VAL N . 15689 1 256 . 1 1 26 26 GLU H H 1 8.500 0.020 . 1 . . . . 26 GLU H . 15689 1 257 . 1 1 26 26 GLU HA H 1 4.900 0.020 . 1 . . . . 26 GLU HA . 15689 1 258 . 1 1 26 26 GLU HB2 H 1 2.290 0.020 . 2 . . . . 26 GLU HB2 . 15689 1 259 . 1 1 26 26 GLU HB3 H 1 2.020 0.020 . 2 . . . . 26 GLU HB3 . 15689 1 260 . 1 1 26 26 GLU CA C 13 53.000 0.200 . 1 . . . . 26 GLU CA . 15689 1 261 . 1 1 26 26 GLU CB C 13 31.200 0.200 . 1 . . . . 26 GLU CB . 15689 1 262 . 1 1 26 26 GLU N N 15 117.900 0.200 . 1 . . . . 26 GLU N . 15689 1 263 . 1 1 27 27 PRO HA H 1 4.040 0.020 . 1 . . . . 27 PRO HA . 15689 1 264 . 1 1 27 27 PRO HB2 H 1 2.331 0.020 . 2 . . . . 27 PRO HB2 . 15689 1 265 . 1 1 27 27 PRO HB3 H 1 2.065 0.020 . 2 . . . . 27 PRO HB3 . 15689 1 266 . 1 1 27 27 PRO HD2 H 1 4.041 0.020 . 2 . . . . 27 PRO HD2 . 15689 1 267 . 1 1 27 27 PRO HD3 H 1 4.041 0.020 . 2 . . . . 27 PRO HD3 . 15689 1 268 . 1 1 27 27 PRO HG2 H 1 1.984 0.020 . 2 . . . . 27 PRO HG2 . 15689 1 269 . 1 1 27 27 PRO HG3 H 1 1.901 0.020 . 2 . . . . 27 PRO HG3 . 15689 1 270 . 1 1 27 27 PRO CA C 13 65.400 0.200 . 1 . . . . 27 PRO CA . 15689 1 271 . 1 1 27 27 PRO CB C 13 31.700 0.200 . 1 . . . . 27 PRO CB . 15689 1 272 . 1 1 27 27 PRO CD C 13 58.259 0.200 . 1 . . . . 27 PRO CD . 15689 1 273 . 1 1 27 27 PRO CG C 13 28.000 0.200 . 1 . . . . 27 PRO CG . 15689 1 274 . 1 1 28 28 SER H H 1 7.010 0.020 . 1 . . . . 28 SER H . 15689 1 275 . 1 1 28 28 SER HA H 1 4.280 0.020 . 1 . . . . 28 SER HA . 15689 1 276 . 1 1 28 28 SER HB2 H 1 3.690 0.020 . 2 . . . . 28 SER HB2 . 15689 1 277 . 1 1 28 28 SER HB3 H 1 4.054 0.020 . 2 . . . . 28 SER HB3 . 15689 1 278 . 1 1 28 28 SER CA C 13 57.400 0.200 . 1 . . . . 28 SER CA . 15689 1 279 . 1 1 28 28 SER CB C 13 63.400 0.200 . 1 . . . . 28 SER CB . 15689 1 280 . 1 1 28 28 SER N N 15 103.800 0.200 . 1 . . . . 28 SER N . 15689 1 281 . 1 1 29 29 ASP H H 1 7.960 0.020 . 1 . . . . 29 ASP H . 15689 1 282 . 1 1 29 29 ASP HA H 1 4.600 0.020 . 1 . . . . 29 ASP HA . 15689 1 283 . 1 1 29 29 ASP HB2 H 1 2.890 0.020 . 2 . . . . 29 ASP HB2 . 15689 1 284 . 1 1 29 29 ASP HB3 H 1 2.420 0.020 . 2 . . . . 29 ASP HB3 . 15689 1 285 . 1 1 29 29 ASP CA C 13 55.900 0.200 . 1 . . . . 29 ASP CA . 15689 1 286 . 1 1 29 29 ASP CB C 13 41.000 0.200 . 1 . . . . 29 ASP CB . 15689 1 287 . 1 1 29 29 ASP N N 15 123.700 0.200 . 1 . . . . 29 ASP N . 15689 1 288 . 1 1 30 30 THR H H 1 7.780 0.020 . 1 . . . . 30 THR H . 15689 1 289 . 1 1 30 30 THR HA H 1 4.850 0.020 . 1 . . . . 30 THR HA . 15689 1 290 . 1 1 30 30 THR HB H 1 4.104 0.020 . 1 . . . . 30 THR HB . 15689 1 291 . 1 1 30 30 THR HG21 H 1 1.132 0.020 . . . . . . 30 THR HG2 . 15689 1 292 . 1 1 30 30 THR HG22 H 1 1.132 0.020 . . . . . . 30 THR HG2 . 15689 1 293 . 1 1 30 30 THR HG23 H 1 1.132 0.020 . . . . . . 30 THR HG2 . 15689 1 294 . 1 1 30 30 THR CA C 13 59.400 0.200 . 1 . . . . 30 THR CA . 15689 1 295 . 1 1 30 30 THR CB C 13 71.100 0.200 . 1 . . . . 30 THR CB . 15689 1 296 . 1 1 30 30 THR CG2 C 13 22.087 0.200 . 1 . . . . 30 THR CG2 . 15689 1 297 . 1 1 30 30 THR N N 15 108.800 0.200 . 1 . . . . 30 THR N . 15689 1 298 . 1 1 31 31 ILE H H 1 8.320 0.020 . 1 . . . . 31 ILE H . 15689 1 299 . 1 1 31 31 ILE HA H 1 3.580 0.020 . 1 . . . . 31 ILE HA . 15689 1 300 . 1 1 31 31 ILE HB H 1 2.480 0.020 . 1 . . . . 31 ILE HB . 15689 1 301 . 1 1 31 31 ILE HD11 H 1 0.481 0.020 . 1 . . . . 31 ILE HD1 . 15689 1 302 . 1 1 31 31 ILE HD12 H 1 0.481 0.020 . 1 . . . . 31 ILE HD1 . 15689 1 303 . 1 1 31 31 ILE HD13 H 1 0.481 0.020 . 1 . . . . 31 ILE HD1 . 15689 1 304 . 1 1 31 31 ILE HG12 H 1 1.878 0.020 . 2 . . . . 31 ILE HG12 . 15689 1 305 . 1 1 31 31 ILE HG13 H 1 1.222 0.020 . 2 . . . . 31 ILE HG13 . 15689 1 306 . 1 1 31 31 ILE HG21 H 1 0.700 0.020 . 1 . . . . 31 ILE HG2 . 15689 1 307 . 1 1 31 31 ILE HG22 H 1 0.700 0.020 . 1 . . . . 31 ILE HG2 . 15689 1 308 . 1 1 31 31 ILE HG23 H 1 0.700 0.020 . 1 . . . . 31 ILE HG2 . 15689 1 309 . 1 1 31 31 ILE CA C 13 62.200 0.200 . 1 . . . . 31 ILE CA . 15689 1 310 . 1 1 31 31 ILE CB C 13 34.300 0.200 . 1 . . . . 31 ILE CB . 15689 1 311 . 1 1 31 31 ILE CD1 C 13 9.419 0.200 . 1 . . . . 31 ILE CD1 . 15689 1 312 . 1 1 31 31 ILE CG1 C 13 27.578 0.200 . 1 . . . . 31 ILE CG1 . 15689 1 313 . 1 1 31 31 ILE CG2 C 13 17.931 0.200 . 1 . . . . 31 ILE CG2 . 15689 1 314 . 1 1 31 31 ILE N N 15 121.300 0.200 . 1 . . . . 31 ILE N . 15689 1 315 . 1 1 32 32 GLU H H 1 9.850 0.020 . 1 . . . . 32 GLU H . 15689 1 316 . 1 1 32 32 GLU HA H 1 3.780 0.020 . 1 . . . . 32 GLU HA . 15689 1 317 . 1 1 32 32 GLU HB2 H 1 2.480 0.020 . 2 . . . . 32 GLU HB2 . 15689 1 318 . 1 1 32 32 GLU HB3 H 1 1.930 0.020 . 2 . . . . 32 GLU HB3 . 15689 1 319 . 1 1 32 32 GLU HG2 H 1 2.215 0.020 . 2 . . . . 32 GLU HG2 . 15689 1 320 . 1 1 32 32 GLU HG3 H 1 2.215 0.020 . 2 . . . . 32 GLU HG3 . 15689 1 321 . 1 1 32 32 GLU CA C 13 60.500 0.200 . 1 . . . . 32 GLU CA . 15689 1 322 . 1 1 32 32 GLU CB C 13 28.800 0.200 . 1 . . . . 32 GLU CB . 15689 1 323 . 1 1 32 32 GLU CG C 13 36.050 0.200 . 1 . . . . 32 GLU CG . 15689 1 324 . 1 1 32 32 GLU N N 15 121.600 0.200 . 1 . . . . 32 GLU N . 15689 1 325 . 1 1 33 33 ASN H H 1 7.810 0.020 . 1 . . . . 33 ASN H . 15689 1 326 . 1 1 33 33 ASN HA H 1 4.440 0.020 . 1 . . . . 33 ASN HA . 15689 1 327 . 1 1 33 33 ASN HB2 H 1 2.750 0.020 . 2 . . . . 33 ASN HB2 . 15689 1 328 . 1 1 33 33 ASN HB3 H 1 2.639 0.020 . 2 . . . . 33 ASN HB3 . 15689 1 329 . 1 1 33 33 ASN CA C 13 55.800 0.200 . 1 . . . . 33 ASN CA . 15689 1 330 . 1 1 33 33 ASN CB C 13 38.100 0.200 . 1 . . . . 33 ASN CB . 15689 1 331 . 1 1 33 33 ASN N N 15 121.000 0.200 . 1 . . . . 33 ASN N . 15689 1 332 . 1 1 34 34 VAL H H 1 8.000 0.020 . 1 . . . . 34 VAL H . 15689 1 333 . 1 1 34 34 VAL HA H 1 3.300 0.020 . 1 . . . . 34 VAL HA . 15689 1 334 . 1 1 34 34 VAL HB H 1 2.260 0.020 . 1 . . . . 34 VAL HB . 15689 1 335 . 1 1 34 34 VAL HG11 H 1 0.891 0.020 . 2 . . . . 34 VAL HG1 . 15689 1 336 . 1 1 34 34 VAL HG12 H 1 0.891 0.020 . 2 . . . . 34 VAL HG1 . 15689 1 337 . 1 1 34 34 VAL HG13 H 1 0.891 0.020 . 2 . . . . 34 VAL HG1 . 15689 1 338 . 1 1 34 34 VAL HG21 H 1 0.612 0.020 . 2 . . . . 34 VAL HG2 . 15689 1 339 . 1 1 34 34 VAL HG22 H 1 0.612 0.020 . 2 . . . . 34 VAL HG2 . 15689 1 340 . 1 1 34 34 VAL HG23 H 1 0.612 0.020 . 2 . . . . 34 VAL HG2 . 15689 1 341 . 1 1 34 34 VAL CA C 13 67.600 0.200 . 1 . . . . 34 VAL CA . 15689 1 342 . 1 1 34 34 VAL CB C 13 30.700 0.200 . 1 . . . . 34 VAL CB . 15689 1 343 . 1 1 34 34 VAL CG1 C 13 21.582 0.200 . 2 . . . . 34 VAL CG1 . 15689 1 344 . 1 1 34 34 VAL CG2 C 13 23.690 0.200 . 2 . . . . 34 VAL CG2 . 15689 1 345 . 1 1 34 34 VAL N N 15 122.200 0.200 . 1 . . . . 34 VAL N . 15689 1 346 . 1 1 35 35 LYS H H 1 8.490 0.020 . 1 . . . . 35 LYS H . 15689 1 347 . 1 1 35 35 LYS HA H 1 4.500 0.020 . 1 . . . . 35 LYS HA . 15689 1 348 . 1 1 35 35 LYS HB2 H 1 1.920 0.020 . 2 . . . . 35 LYS HB2 . 15689 1 349 . 1 1 35 35 LYS HB3 H 1 1.920 0.020 . 2 . . . . 35 LYS HB3 . 15689 1 350 . 1 1 35 35 LYS HG2 H 1 1.349 0.020 . 2 . . . . 35 LYS HG2 . 15689 1 351 . 1 1 35 35 LYS HG3 H 1 1.349 0.020 . 2 . . . . 35 LYS HG3 . 15689 1 352 . 1 1 35 35 LYS CA C 13 59.300 0.200 . 1 . . . . 35 LYS CA . 15689 1 353 . 1 1 35 35 LYS CB C 13 33.500 0.200 . 1 . . . . 35 LYS CB . 15689 1 354 . 1 1 35 35 LYS N N 15 119.200 0.200 . 1 . . . . 35 LYS N . 15689 1 355 . 1 1 36 36 ALA H H 1 7.880 0.020 . 1 . . . . 36 ALA H . 15689 1 356 . 1 1 36 36 ALA HA H 1 4.060 0.020 . 1 . . . . 36 ALA HA . 15689 1 357 . 1 1 36 36 ALA HB1 H 1 1.350 0.020 . 1 . . . . 36 ALA HB . 15689 1 358 . 1 1 36 36 ALA HB2 H 1 1.350 0.020 . 1 . . . . 36 ALA HB . 15689 1 359 . 1 1 36 36 ALA HB3 H 1 1.350 0.020 . 1 . . . . 36 ALA HB . 15689 1 360 . 1 1 36 36 ALA CA C 13 55.300 0.200 . 1 . . . . 36 ALA CA . 15689 1 361 . 1 1 36 36 ALA CB C 13 17.600 0.200 . 1 . . . . 36 ALA CB . 15689 1 362 . 1 1 36 36 ALA N N 15 123.300 0.200 . 1 . . . . 36 ALA N . 15689 1 363 . 1 1 37 37 LYS H H 1 7.790 0.020 . 1 . . . . 37 LYS H . 15689 1 364 . 1 1 37 37 LYS HA H 1 4.110 0.020 . 1 . . . . 37 LYS HA . 15689 1 365 . 1 1 37 37 LYS HB2 H 1 2.054 0.020 . 2 . . . . 37 LYS HB2 . 15689 1 366 . 1 1 37 37 LYS HB3 H 1 1.937 0.020 . 2 . . . . 37 LYS HB3 . 15689 1 367 . 1 1 37 37 LYS HD2 H 1 1.937 0.020 . 2 . . . . 37 LYS HD2 . 15689 1 368 . 1 1 37 37 LYS HD3 H 1 1.937 0.020 . 2 . . . . 37 LYS HD3 . 15689 1 369 . 1 1 37 37 LYS HE2 H 1 2.905 0.020 . 2 . . . . 37 LYS HE2 . 15689 1 370 . 1 1 37 37 LYS HE3 H 1 2.905 0.020 . 2 . . . . 37 LYS HE3 . 15689 1 371 . 1 1 37 37 LYS HG2 H 1 1.839 0.020 . 2 . . . . 37 LYS HG2 . 15689 1 372 . 1 1 37 37 LYS HG3 H 1 1.748 0.020 . 2 . . . . 37 LYS HG3 . 15689 1 373 . 1 1 37 37 LYS CA C 13 59.700 0.200 . 1 . . . . 37 LYS CA . 15689 1 374 . 1 1 37 37 LYS CB C 13 33.100 0.200 . 1 . . . . 37 LYS CB . 15689 1 375 . 1 1 37 37 LYS CD C 13 31.631 0.200 . 1 . . . . 37 LYS CD . 15689 1 376 . 1 1 37 37 LYS CE C 13 35.447 0.200 . 1 . . . . 37 LYS CE . 15689 1 377 . 1 1 37 37 LYS CG C 13 30.508 0.200 . 1 . . . . 37 LYS CG . 15689 1 378 . 1 1 37 37 LYS N N 15 120.400 0.200 . 1 . . . . 37 LYS N . 15689 1 379 . 1 1 38 38 ILE H H 1 8.240 0.020 . 1 . . . . 38 ILE H . 15689 1 380 . 1 1 38 38 ILE HA H 1 3.410 0.020 . 1 . . . . 38 ILE HA . 15689 1 381 . 1 1 38 38 ILE HB H 1 1.860 0.020 . 1 . . . . 38 ILE HB . 15689 1 382 . 1 1 38 38 ILE HD11 H 1 0.605 0.020 . 1 . . . . 38 ILE HD1 . 15689 1 383 . 1 1 38 38 ILE HD12 H 1 0.605 0.020 . 1 . . . . 38 ILE HD1 . 15689 1 384 . 1 1 38 38 ILE HD13 H 1 0.605 0.020 . 1 . . . . 38 ILE HD1 . 15689 1 385 . 1 1 38 38 ILE HG12 H 1 1.923 0.020 . 2 . . . . 38 ILE HG12 . 15689 1 386 . 1 1 38 38 ILE HG13 H 1 0.800 0.020 . 2 . . . . 38 ILE HG13 . 15689 1 387 . 1 1 38 38 ILE HG21 H 1 0.800 0.020 . 1 . . . . 38 ILE HG2 . 15689 1 388 . 1 1 38 38 ILE HG22 H 1 0.800 0.020 . 1 . . . . 38 ILE HG2 . 15689 1 389 . 1 1 38 38 ILE HG23 H 1 0.800 0.020 . 1 . . . . 38 ILE HG2 . 15689 1 390 . 1 1 38 38 ILE CA C 13 66.200 0.200 . 1 . . . . 38 ILE CA . 15689 1 391 . 1 1 38 38 ILE CB C 13 36.800 0.200 . 1 . . . . 38 ILE CB . 15689 1 392 . 1 1 38 38 ILE CD1 C 13 15.100 0.200 . 1 . . . . 38 ILE CD1 . 15689 1 393 . 1 1 38 38 ILE CG1 C 13 31.118 0.200 . 1 . . . . 38 ILE CG1 . 15689 1 394 . 1 1 38 38 ILE CG2 C 13 17.043 0.200 . 1 . . . . 38 ILE CG2 . 15689 1 395 . 1 1 38 38 ILE N N 15 121.400 0.200 . 1 . . . . 38 ILE N . 15689 1 396 . 1 1 39 39 GLN H H 1 8.460 0.020 . 1 . . . . 39 GLN H . 15689 1 397 . 1 1 39 39 GLN HA H 1 3.730 0.020 . 1 . . . . 39 GLN HA . 15689 1 398 . 1 1 39 39 GLN HB2 H 1 1.860 0.020 . 2 . . . . 39 GLN HB2 . 15689 1 399 . 1 1 39 39 GLN HB3 H 1 2.180 0.020 . 2 . . . . 39 GLN HB3 . 15689 1 400 . 1 1 39 39 GLN HG2 H 1 2.392 0.020 . 2 . . . . 39 GLN HG2 . 15689 1 401 . 1 1 39 39 GLN HG3 H 1 2.392 0.020 . 2 . . . . 39 GLN HG3 . 15689 1 402 . 1 1 39 39 GLN CA C 13 60.000 0.200 . 1 . . . . 39 GLN CA . 15689 1 403 . 1 1 39 39 GLN CB C 13 27.600 0.200 . 1 . . . . 39 GLN CB . 15689 1 404 . 1 1 39 39 GLN CG C 13 33.777 0.200 . 1 . . . . 39 GLN CG . 15689 1 405 . 1 1 39 39 GLN N N 15 123.500 0.200 . 1 . . . . 39 GLN N . 15689 1 406 . 1 1 40 40 ASP H H 1 7.970 0.020 . 1 . . . . 40 ASP H . 15689 1 407 . 1 1 40 40 ASP HA H 1 4.240 0.020 . 1 . . . . 40 ASP HA . 15689 1 408 . 1 1 40 40 ASP HB2 H 1 2.750 0.020 . 2 . . . . 40 ASP HB2 . 15689 1 409 . 1 1 40 40 ASP HB3 H 1 2.657 0.020 . 2 . . . . 40 ASP HB3 . 15689 1 410 . 1 1 40 40 ASP CA C 13 57.400 0.200 . 1 . . . . 40 ASP CA . 15689 1 411 . 1 1 40 40 ASP CB C 13 41.000 0.200 . 1 . . . . 40 ASP CB . 15689 1 412 . 1 1 40 40 ASP N N 15 119.900 0.200 . 1 . . . . 40 ASP N . 15689 1 413 . 1 1 41 41 LYS H H 1 7.420 0.020 . 1 . . . . 41 LYS H . 15689 1 414 . 1 1 41 41 LYS HA H 1 4.200 0.020 . 1 . . . . 41 LYS HA . 15689 1 415 . 1 1 41 41 LYS HB2 H 1 1.750 0.020 . 2 . . . . 41 LYS HB2 . 15689 1 416 . 1 1 41 41 LYS HB3 H 1 1.754 0.020 . 2 . . . . 41 LYS HB3 . 15689 1 417 . 1 1 41 41 LYS HD2 H 1 1.916 0.020 . 2 . . . . 41 LYS HD2 . 15689 1 418 . 1 1 41 41 LYS HD3 H 1 1.916 0.020 . 2 . . . . 41 LYS HD3 . 15689 1 419 . 1 1 41 41 LYS HE2 H 1 3.073 0.020 . 2 . . . . 41 LYS HE2 . 15689 1 420 . 1 1 41 41 LYS HE3 H 1 3.020 0.020 . 2 . . . . 41 LYS HE3 . 15689 1 421 . 1 1 41 41 LYS HG2 H 1 1.511 0.020 . 2 . . . . 41 LYS HG2 . 15689 1 422 . 1 1 41 41 LYS HG3 H 1 1.511 0.020 . 2 . . . . 41 LYS HG3 . 15689 1 423 . 1 1 41 41 LYS CA C 13 58.200 0.200 . 1 . . . . 41 LYS CA . 15689 1 424 . 1 1 41 41 LYS CB C 13 33.900 0.200 . 1 . . . . 41 LYS CB . 15689 1 425 . 1 1 41 41 LYS CD C 13 28.784 0.200 . 1 . . . . 41 LYS CD . 15689 1 426 . 1 1 41 41 LYS CG C 13 25.231 0.200 . 1 . . . . 41 LYS CG . 15689 1 427 . 1 1 41 41 LYS N N 15 115.700 0.200 . 1 . . . . 41 LYS N . 15689 1 428 . 1 1 42 42 GLU H H 1 8.650 0.020 . 1 . . . . 42 GLU H . 15689 1 429 . 1 1 42 42 GLU HA H 1 4.470 0.020 . 1 . . . . 42 GLU HA . 15689 1 430 . 1 1 42 42 GLU HB2 H 1 1.920 0.020 . 2 . . . . 42 GLU HB2 . 15689 1 431 . 1 1 42 42 GLU HB3 H 1 2.059 0.020 . 2 . . . . 42 GLU HB3 . 15689 1 432 . 1 1 42 42 GLU HG2 H 1 2.168 0.020 . 2 . . . . 42 GLU HG2 . 15689 1 433 . 1 1 42 42 GLU HG3 H 1 2.168 0.020 . 2 . . . . 42 GLU HG3 . 15689 1 434 . 1 1 42 42 GLU CA C 13 55.300 0.200 . 1 . . . . 42 GLU CA . 15689 1 435 . 1 1 42 42 GLU CB C 13 33.200 0.200 . 1 . . . . 42 GLU CB . 15689 1 436 . 1 1 42 42 GLU CG C 13 36.444 0.200 . 1 . . . . 42 GLU CG . 15689 1 437 . 1 1 42 42 GLU N N 15 114.200 0.200 . 1 . . . . 42 GLU N . 15689 1 438 . 1 1 43 43 GLY H H 1 8.400 0.020 . 1 . . . . 43 GLY H . 15689 1 439 . 1 1 43 43 GLY HA2 H 1 4.040 0.020 . 2 . . . . 43 GLY HA2 . 15689 1 440 . 1 1 43 43 GLY HA3 H 1 3.820 0.020 . 2 . . . . 43 GLY HA3 . 15689 1 441 . 1 1 43 43 GLY CA C 13 45.900 0.200 . 1 . . . . 43 GLY CA . 15689 1 442 . 1 1 43 43 GLY N N 15 109.000 0.200 . 1 . . . . 43 GLY N . 15689 1 443 . 1 1 44 44 ILE H H 1 6.080 0.020 . 1 . . . . 44 ILE H . 15689 1 444 . 1 1 44 44 ILE HA H 1 4.290 0.020 . 1 . . . . 44 ILE HA . 15689 1 445 . 1 1 44 44 ILE HB H 1 1.330 0.020 . 1 . . . . 44 ILE HB . 15689 1 446 . 1 1 44 44 ILE CA C 13 57.700 0.200 . 1 . . . . 44 ILE CA . 15689 1 447 . 1 1 44 44 ILE CB C 13 40.400 0.200 . 1 . . . . 44 ILE CB . 15689 1 448 . 1 1 44 44 ILE N N 15 120.500 0.200 . 1 . . . . 44 ILE N . 15689 1 449 . 1 1 46 46 PRO HA H 1 4.030 0.020 . 1 . . . . 46 PRO HA . 15689 1 450 . 1 1 46 46 PRO HB2 H 1 2.143 0.020 . 2 . . . . 46 PRO HB2 . 15689 1 451 . 1 1 46 46 PRO HB3 H 1 2.082 0.020 . 2 . . . . 46 PRO HB3 . 15689 1 452 . 1 1 46 46 PRO HG2 H 1 1.944 0.020 . 2 . . . . 46 PRO HG2 . 15689 1 453 . 1 1 46 46 PRO HG3 H 1 1.546 0.020 . 2 . . . . 46 PRO HG3 . 15689 1 454 . 1 1 46 46 PRO CA C 13 66.100 0.200 . 1 . . . . 46 PRO CA . 15689 1 455 . 1 1 46 46 PRO CB C 13 32.600 0.200 . 1 . . . . 46 PRO CB . 15689 1 456 . 1 1 46 46 PRO CD C 13 58.259 0.200 . 1 . . . . 46 PRO CD . 15689 1 457 . 1 1 46 46 PRO CG C 13 27.546 0.200 . 1 . . . . 46 PRO CG . 15689 1 458 . 1 1 47 47 ASP H H 1 8.470 0.020 . 1 . . . . 47 ASP H . 15689 1 459 . 1 1 47 47 ASP HA H 1 4.310 0.020 . 1 . . . . 47 ASP HA . 15689 1 460 . 1 1 47 47 ASP HB2 H 1 2.660 0.020 . 2 . . . . 47 ASP HB2 . 15689 1 461 . 1 1 47 47 ASP HB3 H 1 2.580 0.020 . 2 . . . . 47 ASP HB3 . 15689 1 462 . 1 1 47 47 ASP CA C 13 55.700 0.200 . 1 . . . . 47 ASP CA . 15689 1 463 . 1 1 47 47 ASP CB C 13 39.700 0.200 . 1 . . . . 47 ASP CB . 15689 1 464 . 1 1 47 47 ASP N N 15 113.700 0.200 . 1 . . . . 47 ASP N . 15689 1 465 . 1 1 48 48 GLN H H 1 7.720 0.020 . 1 . . . . 48 GLN H . 15689 1 466 . 1 1 48 48 GLN HA H 1 4.340 0.020 . 1 . . . . 48 GLN HA . 15689 1 467 . 1 1 48 48 GLN HB2 H 1 2.320 0.020 . 2 . . . . 48 GLN HB2 . 15689 1 468 . 1 1 48 48 GLN HB3 H 1 2.292 0.020 . 2 . . . . 48 GLN HB3 . 15689 1 469 . 1 1 48 48 GLN HG2 H 1 1.716 0.020 . 2 . . . . 48 GLN HG2 . 15689 1 470 . 1 1 48 48 GLN HG3 H 1 1.716 0.020 . 2 . . . . 48 GLN HG3 . 15689 1 471 . 1 1 48 48 GLN CA C 13 55.500 0.200 . 1 . . . . 48 GLN CA . 15689 1 472 . 1 1 48 48 GLN CB C 13 29.900 0.200 . 1 . . . . 48 GLN CB . 15689 1 473 . 1 1 48 48 GLN CG C 13 34.282 0.200 . 1 . . . . 48 GLN CG . 15689 1 474 . 1 1 48 48 GLN N N 15 116.900 0.200 . 1 . . . . 48 GLN N . 15689 1 475 . 1 1 49 49 GLN H H 1 7.410 0.020 . 1 . . . . 49 GLN H . 15689 1 476 . 1 1 49 49 GLN HA H 1 4.110 0.020 . 1 . . . . 49 GLN HA . 15689 1 477 . 1 1 49 49 GLN HB2 H 1 1.830 0.020 . 2 . . . . 49 GLN HB2 . 15689 1 478 . 1 1 49 49 GLN HB3 H 1 1.834 0.020 . 2 . . . . 49 GLN HB3 . 15689 1 479 . 1 1 49 49 GLN HG2 H 1 2.217 0.020 . 2 . . . . 49 GLN HG2 . 15689 1 480 . 1 1 49 49 GLN HG3 H 1 2.217 0.020 . 2 . . . . 49 GLN HG3 . 15689 1 481 . 1 1 49 49 GLN CA C 13 56.600 0.200 . 1 . . . . 49 GLN CA . 15689 1 482 . 1 1 49 49 GLN CB C 13 31.300 0.200 . 1 . . . . 49 GLN CB . 15689 1 483 . 1 1 49 49 GLN CG C 13 33.984 0.200 . 1 . . . . 49 GLN CG . 15689 1 484 . 1 1 49 49 GLN N N 15 118.000 0.200 . 1 . . . . 49 GLN N . 15689 1 485 . 1 1 50 50 ARG H H 1 8.400 0.020 . 1 . . . . 50 ARG H . 15689 1 486 . 1 1 50 50 ARG HA H 1 4.380 0.020 . 1 . . . . 50 ARG HA . 15689 1 487 . 1 1 50 50 ARG HB2 H 1 1.830 0.020 . 2 . . . . 50 ARG HB2 . 15689 1 488 . 1 1 50 50 ARG HB3 H 1 1.619 0.020 . 2 . . . . 50 ARG HB3 . 15689 1 489 . 1 1 50 50 ARG HG2 H 1 1.542 0.020 . 2 . . . . 50 ARG HG2 . 15689 1 490 . 1 1 50 50 ARG HG3 H 1 1.400 0.020 . 2 . . . . 50 ARG HG3 . 15689 1 491 . 1 1 50 50 ARG CA C 13 55.100 0.200 . 1 . . . . 50 ARG CA . 15689 1 492 . 1 1 50 50 ARG CB C 13 31.600 0.200 . 1 . . . . 50 ARG CB . 15689 1 493 . 1 1 50 50 ARG CG C 13 26.960 0.200 . 1 . . . . 50 ARG CG . 15689 1 494 . 1 1 50 50 ARG N N 15 123.100 0.200 . 1 . . . . 50 ARG N . 15689 1 495 . 1 1 51 51 LEU H H 1 8.710 0.020 . 1 . . . . 51 LEU H . 15689 1 496 . 1 1 51 51 LEU HA H 1 5.300 0.020 . 1 . . . . 51 LEU HA . 15689 1 497 . 1 1 51 51 LEU HB2 H 1 1.620 0.020 . 2 . . . . 51 LEU HB2 . 15689 1 498 . 1 1 51 51 LEU HB3 H 1 1.458 0.020 . 2 . . . . 51 LEU HB3 . 15689 1 499 . 1 1 51 51 LEU HD11 H 1 0.712 0.020 . 2 . . . . 51 LEU HD1 . 15689 1 500 . 1 1 51 51 LEU HD12 H 1 0.712 0.020 . 2 . . . . 51 LEU HD1 . 15689 1 501 . 1 1 51 51 LEU HD13 H 1 0.712 0.020 . 2 . . . . 51 LEU HD1 . 15689 1 502 . 1 1 51 51 LEU HD21 H 1 0.675 0.020 . 2 . . . . 51 LEU HD2 . 15689 1 503 . 1 1 51 51 LEU HD22 H 1 0.675 0.020 . 2 . . . . 51 LEU HD2 . 15689 1 504 . 1 1 51 51 LEU HD23 H 1 0.675 0.020 . 2 . . . . 51 LEU HD2 . 15689 1 505 . 1 1 51 51 LEU HG H 1 1.067 0.020 . 1 . . . . 51 LEU HG . 15689 1 506 . 1 1 51 51 LEU CA C 13 52.900 0.200 . 1 . . . . 51 LEU CA . 15689 1 507 . 1 1 51 51 LEU CB C 13 45.700 0.200 . 1 . . . . 51 LEU CB . 15689 1 508 . 1 1 51 51 LEU CD1 C 13 24.226 0.200 . 2 . . . . 51 LEU CD1 . 15689 1 509 . 1 1 51 51 LEU CD2 C 13 24.226 0.200 . 2 . . . . 51 LEU CD2 . 15689 1 510 . 1 1 51 51 LEU CG C 13 26.591 0.200 . 1 . . . . 51 LEU CG . 15689 1 511 . 1 1 51 51 LEU N N 15 124.400 0.200 . 1 . . . . 51 LEU N . 15689 1 512 . 1 1 52 52 ILE H H 1 9.060 0.020 . 1 . . . . 52 ILE H . 15689 1 513 . 1 1 52 52 ILE HA H 1 4.840 0.020 . 1 . . . . 52 ILE HA . 15689 1 514 . 1 1 52 52 ILE HB H 1 1.650 0.020 . 1 . . . . 52 ILE HB . 15689 1 515 . 1 1 52 52 ILE HD11 H 1 0.581 0.020 . 1 . . . . 52 ILE HD1 . 15689 1 516 . 1 1 52 52 ILE HD12 H 1 0.581 0.020 . 1 . . . . 52 ILE HD1 . 15689 1 517 . 1 1 52 52 ILE HD13 H 1 0.581 0.020 . 1 . . . . 52 ILE HD1 . 15689 1 518 . 1 1 52 52 ILE HG12 H 1 1.251 0.020 . 2 . . . . 52 ILE HG12 . 15689 1 519 . 1 1 52 52 ILE HG13 H 1 1.251 0.020 . 2 . . . . 52 ILE HG13 . 15689 1 520 . 1 1 52 52 ILE HG21 H 1 0.954 0.020 . 1 . . . . 52 ILE HG2 . 15689 1 521 . 1 1 52 52 ILE HG22 H 1 0.954 0.020 . 1 . . . . 52 ILE HG2 . 15689 1 522 . 1 1 52 52 ILE HG23 H 1 0.954 0.020 . 1 . . . . 52 ILE HG2 . 15689 1 523 . 1 1 52 52 ILE CA C 13 58.900 0.200 . 1 . . . . 52 ILE CA . 15689 1 524 . 1 1 52 52 ILE CB C 13 41.200 0.200 . 1 . . . . 52 ILE CB . 15689 1 525 . 1 1 52 52 ILE CD1 C 13 12.752 0.200 . 1 . . . . 52 ILE CD1 . 15689 1 526 . 1 1 52 52 ILE CG1 C 13 27.831 0.200 . 1 . . . . 52 ILE CG1 . 15689 1 527 . 1 1 52 52 ILE CG2 C 13 17.550 0.200 . 1 . . . . 52 ILE CG2 . 15689 1 528 . 1 1 52 52 ILE N N 15 122.500 0.200 . 1 . . . . 52 ILE N . 15689 1 529 . 1 1 53 53 PHE H H 1 8.730 0.020 . 1 . . . . 53 PHE H . 15689 1 530 . 1 1 53 53 PHE HA H 1 5.100 0.020 . 1 . . . . 53 PHE HA . 15689 1 531 . 1 1 53 53 PHE HB2 H 1 2.930 0.020 . 2 . . . . 53 PHE HB2 . 15689 1 532 . 1 1 53 53 PHE HB3 H 1 2.709 0.020 . 2 . . . . 53 PHE HB3 . 15689 1 533 . 1 1 53 53 PHE HE1 H 1 7.408 0.020 . 3 . . . . 53 PHE HE1 . 15689 1 534 . 1 1 53 53 PHE HE2 H 1 7.408 0.020 . 3 . . . . 53 PHE HE2 . 15689 1 535 . 1 1 53 53 PHE CA C 13 56.300 0.200 . 1 . . . . 53 PHE CA . 15689 1 536 . 1 1 53 53 PHE CB C 13 43.500 0.200 . 1 . . . . 53 PHE CB . 15689 1 537 . 1 1 53 53 PHE N N 15 124.800 0.200 . 1 . . . . 53 PHE N . 15689 1 538 . 1 1 54 54 ALA H H 1 8.940 0.020 . 1 . . . . 54 ALA H . 15689 1 539 . 1 1 54 54 ALA HA H 1 3.610 0.020 . 1 . . . . 54 ALA HA . 15689 1 540 . 1 1 54 54 ALA HB1 H 1 0.778 0.020 . 1 . . . . 54 ALA HB . 15689 1 541 . 1 1 54 54 ALA HB2 H 1 0.778 0.020 . 1 . . . . 54 ALA HB . 15689 1 542 . 1 1 54 54 ALA HB3 H 1 0.778 0.020 . 1 . . . . 54 ALA HB . 15689 1 543 . 1 1 54 54 ALA CA C 13 52.500 0.200 . 1 . . . . 54 ALA CA . 15689 1 544 . 1 1 54 54 ALA CB C 13 16.300 0.200 . 1 . . . . 54 ALA CB . 15689 1 545 . 1 1 54 54 ALA N N 15 133.100 0.200 . 1 . . . . 54 ALA N . 15689 1 546 . 1 1 55 55 GLY H H 1 8.070 0.020 . 1 . . . . 55 GLY H . 15689 1 547 . 1 1 55 55 GLY HA2 H 1 4.000 0.020 . 2 . . . . 55 GLY HA2 . 15689 1 548 . 1 1 55 55 GLY HA3 H 1 3.340 0.020 . 2 . . . . 55 GLY HA3 . 15689 1 549 . 1 1 55 55 GLY CA C 13 45.200 0.200 . 1 . . . . 55 GLY CA . 15689 1 550 . 1 1 55 55 GLY N N 15 102.500 0.200 . 1 . . . . 55 GLY N . 15689 1 551 . 1 1 56 56 LYS H H 1 7.860 0.020 . 1 . . . . 56 LYS H . 15689 1 552 . 1 1 56 56 LYS HA H 1 4.510 0.020 . 1 . . . . 56 LYS HA . 15689 1 553 . 1 1 56 56 LYS HB2 H 1 1.790 0.020 . 2 . . . . 56 LYS HB2 . 15689 1 554 . 1 1 56 56 LYS HE2 H 1 3.065 0.020 . 2 . . . . 56 LYS HE2 . 15689 1 555 . 1 1 56 56 LYS HE3 H 1 3.065 0.020 . 2 . . . . 56 LYS HE3 . 15689 1 556 . 1 1 56 56 LYS HG2 H 1 1.412 0.020 . 2 . . . . 56 LYS HG2 . 15689 1 557 . 1 1 56 56 LYS HG3 H 1 1.412 0.020 . 2 . . . . 56 LYS HG3 . 15689 1 558 . 1 1 56 56 LYS CA C 13 54.500 0.200 . 1 . . . . 56 LYS CA . 15689 1 559 . 1 1 56 56 LYS CB C 13 34.400 0.200 . 1 . . . . 56 LYS CB . 15689 1 560 . 1 1 56 56 LYS CG C 13 24.361 0.200 . 1 . . . . 56 LYS CG . 15689 1 561 . 1 1 56 56 LYS N N 15 121.800 0.200 . 1 . . . . 56 LYS N . 15689 1 562 . 1 1 57 57 GLN H H 1 8.600 0.020 . 1 . . . . 57 GLN H . 15689 1 563 . 1 1 57 57 GLN HA H 1 4.410 0.020 . 1 . . . . 57 GLN HA . 15689 1 564 . 1 1 57 57 GLN HB2 H 1 1.900 0.020 . 2 . . . . 57 GLN HB2 . 15689 1 565 . 1 1 57 57 GLN HB3 H 1 1.790 0.020 . 2 . . . . 57 GLN HB3 . 15689 1 566 . 1 1 57 57 GLN HG2 H 1 2.150 0.020 . 2 . . . . 57 GLN HG2 . 15689 1 567 . 1 1 57 57 GLN HG3 H 1 2.150 0.020 . 2 . . . . 57 GLN HG3 . 15689 1 568 . 1 1 57 57 GLN CA C 13 55.900 0.200 . 1 . . . . 57 GLN CA . 15689 1 569 . 1 1 57 57 GLN CB C 13 28.800 0.200 . 1 . . . . 57 GLN CB . 15689 1 570 . 1 1 57 57 GLN CG C 13 34.551 0.200 . 1 . . . . 57 GLN CG . 15689 1 571 . 1 1 57 57 GLN N N 15 123.200 0.200 . 1 . . . . 57 GLN N . 15689 1 572 . 1 1 58 58 LEU H H 1 8.480 0.020 . 1 . . . . 58 LEU H . 15689 1 573 . 1 1 58 58 LEU HA H 1 4.060 0.020 . 1 . . . . 58 LEU HA . 15689 1 574 . 1 1 58 58 LEU HB2 H 1 1.410 0.020 . 2 . . . . 58 LEU HB2 . 15689 1 575 . 1 1 58 58 LEU HB3 H 1 1.834 0.020 . 2 . . . . 58 LEU HB3 . 15689 1 576 . 1 1 58 58 LEU HD11 H 1 0.432 0.020 . 2 . . . . 58 LEU HD1 . 15689 1 577 . 1 1 58 58 LEU HD12 H 1 0.432 0.020 . 2 . . . . 58 LEU HD1 . 15689 1 578 . 1 1 58 58 LEU HD13 H 1 0.432 0.020 . 2 . . . . 58 LEU HD1 . 15689 1 579 . 1 1 58 58 LEU HD21 H 1 0.432 0.020 . 2 . . . . 58 LEU HD2 . 15689 1 580 . 1 1 58 58 LEU HD22 H 1 0.432 0.020 . 2 . . . . 58 LEU HD2 . 15689 1 581 . 1 1 58 58 LEU HD23 H 1 0.432 0.020 . 2 . . . . 58 LEU HD2 . 15689 1 582 . 1 1 58 58 LEU HG H 1 0.974 0.020 . 1 . . . . 58 LEU HG . 15689 1 583 . 1 1 58 58 LEU CA C 13 54.100 0.200 . 1 . . . . 58 LEU CA . 15689 1 584 . 1 1 58 58 LEU CB C 13 41.500 0.200 . 1 . . . . 58 LEU CB . 15689 1 585 . 1 1 58 58 LEU CD1 C 13 25.956 0.200 . 2 . . . . 58 LEU CD1 . 15689 1 586 . 1 1 58 58 LEU CD2 C 13 19.444 0.200 . 2 . . . . 58 LEU CD2 . 15689 1 587 . 1 1 58 58 LEU CG C 13 31.323 0.200 . 1 . . . . 58 LEU CG . 15689 1 588 . 1 1 58 58 LEU N N 15 125.900 0.200 . 1 . . . . 58 LEU N . 15689 1 589 . 1 1 59 59 GLU H H 1 8.400 0.020 . 1 . . . . 59 GLU H . 15689 1 590 . 1 1 59 59 GLU HA H 1 4.400 0.020 . 1 . . . . 59 GLU HA . 15689 1 591 . 1 1 59 59 GLU HB2 H 1 2.140 0.020 . 2 . . . . 59 GLU HB2 . 15689 1 592 . 1 1 59 59 GLU HB3 H 1 1.908 0.020 . 2 . . . . 59 GLU HB3 . 15689 1 593 . 1 1 59 59 GLU HG2 H 1 2.325 0.020 . 2 . . . . 59 GLU HG2 . 15689 1 594 . 1 1 59 59 GLU HG3 H 1 2.325 0.020 . 2 . . . . 59 GLU HG3 . 15689 1 595 . 1 1 59 59 GLU CA C 13 55.900 0.200 . 1 . . . . 59 GLU CA . 15689 1 596 . 1 1 59 59 GLU CB C 13 31.900 0.200 . 1 . . . . 59 GLU CB . 15689 1 597 . 1 1 59 59 GLU CG C 13 36.397 0.200 . 1 . . . . 59 GLU CG . 15689 1 598 . 1 1 59 59 GLU N N 15 123.100 0.200 . 1 . . . . 59 GLU N . 15689 1 599 . 1 1 60 60 ASP H H 1 8.110 0.020 . 1 . . . . 60 ASP H . 15689 1 600 . 1 1 60 60 ASP HA H 1 4.270 0.020 . 1 . . . . 60 ASP HA . 15689 1 601 . 1 1 60 60 ASP HB2 H 1 2.520 0.020 . 2 . . . . 60 ASP HB2 . 15689 1 602 . 1 1 60 60 ASP HB3 H 1 2.430 0.020 . 2 . . . . 60 ASP HB3 . 15689 1 603 . 1 1 60 60 ASP CA C 13 57.100 0.200 . 1 . . . . 60 ASP CA . 15689 1 604 . 1 1 60 60 ASP CB C 13 40.800 0.200 . 1 . . . . 60 ASP CB . 15689 1 605 . 1 1 60 60 ASP N N 15 120.300 0.200 . 1 . . . . 60 ASP N . 15689 1 606 . 1 1 61 61 GLY HA2 H 1 4.000 0.020 . 2 . . . . 61 GLY HA2 . 15689 1 607 . 1 1 61 61 GLY HA3 H 1 3.830 0.020 . 2 . . . . 61 GLY HA3 . 15689 1 608 . 1 1 61 61 GLY CA C 13 45.000 0.200 . 1 . . . . 61 GLY CA . 15689 1 609 . 1 1 62 62 ARG H H 1 7.350 0.020 . 1 . . . . 62 ARG H . 15689 1 610 . 1 1 62 62 ARG HA H 1 4.640 0.020 . 1 . . . . 62 ARG HA . 15689 1 611 . 1 1 62 62 ARG HB2 H 1 2.020 0.020 . 2 . . . . 62 ARG HB2 . 15689 1 612 . 1 1 62 62 ARG HB3 H 1 1.500 0.020 . 2 . . . . 62 ARG HB3 . 15689 1 613 . 1 1 62 62 ARG HG2 H 1 1.622 0.020 . 2 . . . . 62 ARG HG2 . 15689 1 614 . 1 1 62 62 ARG HG3 H 1 1.622 0.020 . 2 . . . . 62 ARG HG3 . 15689 1 615 . 1 1 62 62 ARG CA C 13 54.400 0.200 . 1 . . . . 62 ARG CA . 15689 1 616 . 1 1 62 62 ARG CB C 13 32.600 0.200 . 1 . . . . 62 ARG CB . 15689 1 617 . 1 1 62 62 ARG CG C 13 27.545 0.200 . 1 . . . . 62 ARG CG . 15689 1 618 . 1 1 62 62 ARG N N 15 119.300 0.200 . 1 . . . . 62 ARG N . 15689 1 619 . 1 1 63 63 THR H H 1 8.460 0.020 . 1 . . . . 63 THR H . 15689 1 620 . 1 1 63 63 THR HA H 1 5.060 0.020 . 1 . . . . 63 THR HA . 15689 1 621 . 1 1 63 63 THR HB H 1 4.460 0.020 . 1 . . . . 63 THR HB . 15689 1 622 . 1 1 63 63 THR HG21 H 1 1.073 0.020 . . . . . . 63 THR HG2 . 15689 1 623 . 1 1 63 63 THR HG22 H 1 1.073 0.020 . . . . . . 63 THR HG2 . 15689 1 624 . 1 1 63 63 THR HG23 H 1 1.073 0.020 . . . . . . 63 THR HG2 . 15689 1 625 . 1 1 63 63 THR CA C 13 59.700 0.200 . 1 . . . . 63 THR CA . 15689 1 626 . 1 1 63 63 THR CB C 13 72.000 0.200 . 1 . . . . 63 THR CB . 15689 1 627 . 1 1 63 63 THR CG2 C 13 22.261 0.200 . 1 . . . . 63 THR CG2 . 15689 1 628 . 1 1 63 63 THR N N 15 109.100 0.200 . 1 . . . . 63 THR N . 15689 1 629 . 1 1 64 64 LEU H H 1 8.190 0.020 . 1 . . . . 64 LEU H . 15689 1 630 . 1 1 64 64 LEU HA H 1 3.920 0.020 . 1 . . . . 64 LEU HA . 15689 1 631 . 1 1 64 64 LEU HB2 H 1 1.970 0.020 . 2 . . . . 64 LEU HB2 . 15689 1 632 . 1 1 64 64 LEU HB3 H 1 1.699 0.020 . 2 . . . . 64 LEU HB3 . 15689 1 633 . 1 1 64 64 LEU HD11 H 1 0.670 0.020 . 2 . . . . 64 LEU HD1 . 15689 1 634 . 1 1 64 64 LEU HD12 H 1 0.670 0.020 . 2 . . . . 64 LEU HD1 . 15689 1 635 . 1 1 64 64 LEU HD13 H 1 0.670 0.020 . 2 . . . . 64 LEU HD1 . 15689 1 636 . 1 1 64 64 LEU HD21 H 1 0.532 0.020 . 2 . . . . 64 LEU HD2 . 15689 1 637 . 1 1 64 64 LEU HD22 H 1 0.532 0.020 . 2 . . . . 64 LEU HD2 . 15689 1 638 . 1 1 64 64 LEU HD23 H 1 0.532 0.020 . 2 . . . . 64 LEU HD2 . 15689 1 639 . 1 1 64 64 LEU HG H 1 1.105 0.020 . 1 . . . . 64 LEU HG . 15689 1 640 . 1 1 64 64 LEU CA C 13 58.400 0.200 . 1 . . . . 64 LEU CA . 15689 1 641 . 1 1 64 64 LEU CB C 13 40.200 0.200 . 1 . . . . 64 LEU CB . 15689 1 642 . 1 1 64 64 LEU CD1 C 13 23.005 0.200 . 2 . . . . 64 LEU CD1 . 15689 1 643 . 1 1 64 64 LEU CD2 C 13 23.005 0.200 . 2 . . . . 64 LEU CD2 . 15689 1 644 . 1 1 64 64 LEU CG C 13 26.599 0.200 . 1 . . . . 64 LEU CG . 15689 1 645 . 1 1 64 64 LEU N N 15 118.100 0.200 . 1 . . . . 64 LEU N . 15689 1 646 . 1 1 65 65 SER H H 1 8.370 0.020 . 1 . . . . 65 SER H . 15689 1 647 . 1 1 65 65 SER HA H 1 4.150 0.020 . 1 . . . . 65 SER HA . 15689 1 648 . 1 1 65 65 SER HB2 H 1 3.750 0.020 . 2 . . . . 65 SER HB2 . 15689 1 649 . 1 1 65 65 SER HB3 H 1 3.664 0.020 . 2 . . . . 65 SER HB3 . 15689 1 650 . 1 1 65 65 SER CA C 13 60.900 0.200 . 1 . . . . 65 SER CA . 15689 1 651 . 1 1 65 65 SER CB C 13 62.500 0.200 . 1 . . . . 65 SER CB . 15689 1 652 . 1 1 65 65 SER N N 15 112.200 0.200 . 1 . . . . 65 SER N . 15689 1 653 . 1 1 66 66 GLU H H 1 7.780 0.020 . 1 . . . . 66 GLU H . 15689 1 654 . 1 1 66 66 GLU HA H 1 3.890 0.020 . 1 . . . . 66 GLU HA . 15689 1 655 . 1 1 66 66 GLU HB2 H 1 2.060 0.020 . 2 . . . . 66 GLU HB2 . 15689 1 656 . 1 1 66 66 GLU HB3 H 1 1.683 0.020 . 2 . . . . 66 GLU HB3 . 15689 1 657 . 1 1 66 66 GLU HG2 H 1 2.199 0.020 . 2 . . . . 66 GLU HG2 . 15689 1 658 . 1 1 66 66 GLU HG3 H 1 2.199 0.020 . 2 . . . . 66 GLU HG3 . 15689 1 659 . 1 1 66 66 GLU CA C 13 59.200 0.200 . 1 . . . . 66 GLU CA . 15689 1 660 . 1 1 66 66 GLU CB C 13 29.400 0.200 . 1 . . . . 66 GLU CB . 15689 1 661 . 1 1 66 66 GLU CG C 13 38.039 0.200 . 1 . . . . 66 GLU CG . 15689 1 662 . 1 1 66 66 GLU N N 15 123.600 0.200 . 1 . . . . 66 GLU N . 15689 1 663 . 1 1 67 67 TYR H H 1 7.290 0.020 . 1 . . . . 67 TYR H . 15689 1 664 . 1 1 67 67 TYR HA H 1 4.590 0.020 . 1 . . . . 67 TYR HA . 15689 1 665 . 1 1 67 67 TYR HB2 H 1 2.480 0.020 . 2 . . . . 67 TYR HB2 . 15689 1 666 . 1 1 67 67 TYR HB3 H 1 3.342 0.020 . 2 . . . . 67 TYR HB3 . 15689 1 667 . 1 1 67 67 TYR HD1 H 1 6.798 0.020 . 3 . . . . 67 TYR HD1 . 15689 1 668 . 1 1 67 67 TYR HD2 H 1 6.798 0.020 . 3 . . . . 67 TYR HD2 . 15689 1 669 . 1 1 67 67 TYR CA C 13 58.400 0.200 . 1 . . . . 67 TYR CA . 15689 1 670 . 1 1 67 67 TYR CB C 13 39.800 0.200 . 1 . . . . 67 TYR CB . 15689 1 671 . 1 1 67 67 TYR N N 15 116.400 0.200 . 1 . . . . 67 TYR N . 15689 1 672 . 1 1 68 68 ASN H H 1 8.040 0.020 . 1 . . . . 68 ASN H . 15689 1 673 . 1 1 68 68 ASN HA H 1 4.240 0.020 . 1 . . . . 68 ASN HA . 15689 1 674 . 1 1 68 68 ASN HB2 H 1 2.730 0.020 . 2 . . . . 68 ASN HB2 . 15689 1 675 . 1 1 68 68 ASN HB3 H 1 2.732 0.020 . 2 . . . . 68 ASN HB3 . 15689 1 676 . 1 1 68 68 ASN CA C 13 54.100 0.200 . 1 . . . . 68 ASN CA . 15689 1 677 . 1 1 68 68 ASN CB C 13 37.200 0.200 . 1 . . . . 68 ASN CB . 15689 1 678 . 1 1 68 68 ASN N N 15 115.600 0.200 . 1 . . . . 68 ASN N . 15689 1 679 . 1 1 69 69 ILE H H 1 7.200 0.020 . 1 . . . . 69 ILE H . 15689 1 680 . 1 1 69 69 ILE HA H 1 3.280 0.020 . 1 . . . . 69 ILE HA . 15689 1 681 . 1 1 69 69 ILE HB H 1 1.300 0.020 . 1 . . . . 69 ILE HB . 15689 1 682 . 1 1 69 69 ILE HD11 H 1 0.315 0.020 . 1 . . . . 69 ILE HD1 . 15689 1 683 . 1 1 69 69 ILE HD12 H 1 0.315 0.020 . 1 . . . . 69 ILE HD1 . 15689 1 684 . 1 1 69 69 ILE HD13 H 1 0.315 0.020 . 1 . . . . 69 ILE HD1 . 15689 1 685 . 1 1 69 69 ILE HG12 H 1 1.296 0.020 . 2 . . . . 69 ILE HG12 . 15689 1 686 . 1 1 69 69 ILE HG13 H 1 1.296 0.020 . 2 . . . . 69 ILE HG13 . 15689 1 687 . 1 1 69 69 ILE HG21 H 1 0.982 0.020 . 1 . . . . 69 ILE HG2 . 15689 1 688 . 1 1 69 69 ILE HG22 H 1 0.982 0.020 . 1 . . . . 69 ILE HG2 . 15689 1 689 . 1 1 69 69 ILE HG23 H 1 0.982 0.020 . 1 . . . . 69 ILE HG2 . 15689 1 690 . 1 1 69 69 ILE CA C 13 59.800 0.200 . 1 . . . . 69 ILE CA . 15689 1 691 . 1 1 69 69 ILE CB C 13 36.600 0.200 . 1 . . . . 69 ILE CB . 15689 1 692 . 1 1 69 69 ILE CD1 C 13 14.302 0.200 . 1 . . . . 69 ILE CD1 . 15689 1 693 . 1 1 69 69 ILE CG1 C 13 28.112 0.200 . 1 . . . . 69 ILE CG1 . 15689 1 694 . 1 1 69 69 ILE CG2 C 13 17.322 0.200 . 1 . . . . 69 ILE CG2 . 15689 1 695 . 1 1 69 69 ILE N N 15 119.100 0.200 . 1 . . . . 69 ILE N . 15689 1 696 . 1 1 70 70 GLN H H 1 7.570 0.020 . 1 . . . . 70 GLN H . 15689 1 697 . 1 1 70 70 GLN HA H 1 4.410 0.020 . 1 . . . . 70 GLN HA . 15689 1 698 . 1 1 70 70 GLN HB2 H 1 2.160 0.020 . 2 . . . . 70 GLN HB2 . 15689 1 699 . 1 1 70 70 GLN HB3 H 1 1.777 0.020 . 2 . . . . 70 GLN HB3 . 15689 1 700 . 1 1 70 70 GLN HG2 H 1 2.235 0.020 . 2 . . . . 70 GLN HG2 . 15689 1 701 . 1 1 70 70 GLN HG3 H 1 2.235 0.020 . 2 . . . . 70 GLN HG3 . 15689 1 702 . 1 1 70 70 GLN CA C 13 53.500 0.200 . 1 . . . . 70 GLN CA . 15689 1 703 . 1 1 70 70 GLN CB C 13 31.500 0.200 . 1 . . . . 70 GLN CB . 15689 1 704 . 1 1 70 70 GLN CG C 13 36.424 0.200 . 1 . . . . 70 GLN CG . 15689 1 705 . 1 1 70 70 GLN N N 15 124.800 0.200 . 1 . . . . 70 GLN N . 15689 1 706 . 1 1 71 71 LYS H H 1 8.370 0.020 . 1 . . . . 71 LYS H . 15689 1 707 . 1 1 71 71 LYS HA H 1 3.870 0.020 . 1 . . . . 71 LYS HA . 15689 1 708 . 1 1 71 71 LYS HB2 H 1 1.945 0.020 . 2 . . . . 71 LYS HB2 . 15689 1 709 . 1 1 71 71 LYS HB3 H 1 1.790 0.020 . 2 . . . . 71 LYS HB3 . 15689 1 710 . 1 1 71 71 LYS HD2 H 1 1.790 0.020 . 2 . . . . 71 LYS HD2 . 15689 1 711 . 1 1 71 71 LYS HD3 H 1 1.790 0.020 . 2 . . . . 71 LYS HD3 . 15689 1 712 . 1 1 71 71 LYS HE2 H 1 2.940 0.020 . 2 . . . . 71 LYS HE2 . 15689 1 713 . 1 1 71 71 LYS HE3 H 1 2.940 0.020 . 2 . . . . 71 LYS HE3 . 15689 1 714 . 1 1 71 71 LYS HG2 H 1 1.423 0.020 . 2 . . . . 71 LYS HG2 . 15689 1 715 . 1 1 71 71 LYS HG3 H 1 1.423 0.020 . 2 . . . . 71 LYS HG3 . 15689 1 716 . 1 1 71 71 LYS CA C 13 58.000 0.200 . 1 . . . . 71 LYS CA . 15689 1 717 . 1 1 71 71 LYS CB C 13 32.500 0.200 . 1 . . . . 71 LYS CB . 15689 1 718 . 1 1 71 71 LYS CD C 13 29.658 0.200 . 1 . . . . 71 LYS CD . 15689 1 719 . 1 1 71 71 LYS CG C 13 24.277 0.200 . 1 . . . . 71 LYS CG . 15689 1 720 . 1 1 71 71 LYS N N 15 120.200 0.200 . 1 . . . . 71 LYS N . 15689 1 721 . 1 1 72 72 GLU H H 1 9.230 0.020 . 1 . . . . 72 GLU H . 15689 1 722 . 1 1 72 72 GLU HA H 1 3.240 0.020 . 1 . . . . 72 GLU HA . 15689 1 723 . 1 1 72 72 GLU HB2 H 1 1.950 0.020 . 2 . . . . 72 GLU HB2 . 15689 1 724 . 1 1 72 72 GLU HB3 H 1 2.141 0.020 . 2 . . . . 72 GLU HB3 . 15689 1 725 . 1 1 72 72 GLU HG2 H 1 2.309 0.020 . 2 . . . . 72 GLU HG2 . 15689 1 726 . 1 1 72 72 GLU HG3 H 1 2.443 0.020 . 2 . . . . 72 GLU HG3 . 15689 1 727 . 1 1 72 72 GLU CA C 13 58.300 0.200 . 1 . . . . 72 GLU CA . 15689 1 728 . 1 1 72 72 GLU CB C 13 26.000 0.200 . 1 . . . . 72 GLU CB . 15689 1 729 . 1 1 72 72 GLU CG C 13 37.366 0.200 . 1 . . . . 72 GLU CG . 15689 1 730 . 1 1 72 72 GLU N N 15 115.100 0.200 . 1 . . . . 72 GLU N . 15689 1 731 . 1 1 73 73 SER H H 1 7.690 0.020 . 1 . . . . 73 SER H . 15689 1 732 . 1 1 73 73 SER HA H 1 4.520 0.020 . 1 . . . . 73 SER HA . 15689 1 733 . 1 1 73 73 SER HB2 H 1 3.810 0.020 . 2 . . . . 73 SER HB2 . 15689 1 734 . 1 1 73 73 SER HB3 H 1 3.577 0.020 . 2 . . . . 73 SER HB3 . 15689 1 735 . 1 1 73 73 SER CA C 13 61.100 0.200 . 1 . . . . 73 SER CA . 15689 1 736 . 1 1 73 73 SER CB C 13 64.800 0.200 . 1 . . . . 73 SER CB . 15689 1 737 . 1 1 73 73 SER N N 15 115.300 0.200 . 1 . . . . 73 SER N . 15689 1 738 . 1 1 74 74 THR H H 1 8.620 0.020 . 1 . . . . 74 THR H . 15689 1 739 . 1 1 74 74 THR HA H 1 5.200 0.020 . 1 . . . . 74 THR HA . 15689 1 740 . 1 1 74 74 THR HB H 1 3.960 0.020 . 1 . . . . 74 THR HB . 15689 1 741 . 1 1 74 74 THR HG21 H 1 0.840 0.020 . . . . . . 74 THR HG2 . 15689 1 742 . 1 1 74 74 THR HG22 H 1 0.840 0.020 . . . . . . 74 THR HG2 . 15689 1 743 . 1 1 74 74 THR HG23 H 1 0.840 0.020 . . . . . . 74 THR HG2 . 15689 1 744 . 1 1 74 74 THR CA C 13 62.400 0.200 . 1 . . . . 74 THR CA . 15689 1 745 . 1 1 74 74 THR CB C 13 70.200 0.200 . 1 . . . . 74 THR CB . 15689 1 746 . 1 1 74 74 THR CG2 C 13 21.406 0.200 . 1 . . . . 74 THR CG2 . 15689 1 747 . 1 1 74 74 THR N N 15 117.500 0.200 . 1 . . . . 74 THR N . 15689 1 748 . 1 1 75 75 LEU H H 1 9.350 0.020 . 1 . . . . 75 LEU H . 15689 1 749 . 1 1 75 75 LEU HA H 1 4.990 0.020 . 1 . . . . 75 LEU HA . 15689 1 750 . 1 1 75 75 LEU HB2 H 1 3.960 0.020 . 2 . . . . 75 LEU HB2 . 15689 1 751 . 1 1 75 75 LEU HB3 H 1 1.530 0.020 . 2 . . . . 75 LEU HB3 . 15689 1 752 . 1 1 75 75 LEU HD11 H 1 0.597 0.020 . 2 . . . . 75 LEU HD1 . 15689 1 753 . 1 1 75 75 LEU HD12 H 1 0.597 0.020 . 2 . . . . 75 LEU HD1 . 15689 1 754 . 1 1 75 75 LEU HD13 H 1 0.597 0.020 . 2 . . . . 75 LEU HD1 . 15689 1 755 . 1 1 75 75 LEU HD21 H 1 0.559 0.020 . 2 . . . . 75 LEU HD2 . 15689 1 756 . 1 1 75 75 LEU HD22 H 1 0.559 0.020 . 2 . . . . 75 LEU HD2 . 15689 1 757 . 1 1 75 75 LEU HD23 H 1 0.559 0.020 . 2 . . . . 75 LEU HD2 . 15689 1 758 . 1 1 75 75 LEU HG H 1 1.671 0.020 . 1 . . . . 75 LEU HG . 15689 1 759 . 1 1 75 75 LEU CA C 13 53.800 0.200 . 1 . . . . 75 LEU CA . 15689 1 760 . 1 1 75 75 LEU CB C 13 44.400 0.200 . 1 . . . . 75 LEU CB . 15689 1 761 . 1 1 75 75 LEU CD1 C 13 24.908 0.200 . 2 . . . . 75 LEU CD1 . 15689 1 762 . 1 1 75 75 LEU CD2 C 13 25.255 0.200 . 2 . . . . 75 LEU CD2 . 15689 1 763 . 1 1 75 75 LEU CG C 13 29.635 0.200 . 1 . . . . 75 LEU CG . 15689 1 764 . 1 1 75 75 LEU N N 15 128.000 0.200 . 1 . . . . 75 LEU N . 15689 1 765 . 1 1 76 76 HIS H H 1 9.140 0.020 . 1 . . . . 76 HIS H . 15689 1 766 . 1 1 76 76 HIS HA H 1 5.040 0.020 . 1 . . . . 76 HIS HA . 15689 1 767 . 1 1 76 76 HIS HB2 H 1 2.950 0.020 . 2 . . . . 76 HIS HB2 . 15689 1 768 . 1 1 76 76 HIS HB3 H 1 2.761 0.020 . 2 . . . . 76 HIS HB3 . 15689 1 769 . 1 1 76 76 HIS CA C 13 56.200 0.200 . 1 . . . . 76 HIS CA . 15689 1 770 . 1 1 76 76 HIS CB C 13 32.500 0.200 . 1 . . . . 76 HIS CB . 15689 1 771 . 1 1 76 76 HIS N N 15 119.600 0.200 . 1 . . . . 76 HIS N . 15689 1 772 . 1 1 77 77 LEU H H 1 8.240 0.020 . 1 . . . . 77 LEU H . 15689 1 773 . 1 1 77 77 LEU HA H 1 5.080 0.020 . 1 . . . . 77 LEU HA . 15689 1 774 . 1 1 77 77 LEU HB2 H 1 1.234 0.020 . 2 . . . . 77 LEU HB2 . 15689 1 775 . 1 1 77 77 LEU HB3 H 1 1.500 0.020 . 2 . . . . 77 LEU HB3 . 15689 1 776 . 1 1 77 77 LEU HD11 H 1 0.765 0.020 . 2 . . . . 77 LEU HD1 . 15689 1 777 . 1 1 77 77 LEU HD12 H 1 0.765 0.020 . 2 . . . . 77 LEU HD1 . 15689 1 778 . 1 1 77 77 LEU HD13 H 1 0.765 0.020 . 2 . . . . 77 LEU HD1 . 15689 1 779 . 1 1 77 77 LEU HD21 H 1 0.643 0.020 . 2 . . . . 77 LEU HD2 . 15689 1 780 . 1 1 77 77 LEU HD22 H 1 0.643 0.020 . 2 . . . . 77 LEU HD2 . 15689 1 781 . 1 1 77 77 LEU HD23 H 1 0.643 0.020 . 2 . . . . 77 LEU HD2 . 15689 1 782 . 1 1 77 77 LEU HG H 1 1.018 0.020 . 1 . . . . 77 LEU HG . 15689 1 783 . 1 1 77 77 LEU CA C 13 53.600 0.200 . 1 . . . . 77 LEU CA . 15689 1 784 . 1 1 77 77 LEU CB C 13 44.100 0.200 . 1 . . . . 77 LEU CB . 15689 1 785 . 1 1 77 77 LEU CD1 C 13 26.068 0.200 . 2 . . . . 77 LEU CD1 . 15689 1 786 . 1 1 77 77 LEU CD2 C 13 24.047 0.200 . 2 . . . . 77 LEU CD2 . 15689 1 787 . 1 1 77 77 LEU CG C 13 27.520 0.200 . 1 . . . . 77 LEU CG . 15689 1 788 . 1 1 77 77 LEU N N 15 123.800 0.200 . 1 . . . . 77 LEU N . 15689 1 789 . 1 1 78 78 VAL H H 1 9.110 0.020 . 1 . . . . 78 VAL H . 15689 1 790 . 1 1 78 78 VAL HA H 1 4.260 0.020 . 1 . . . . 78 VAL HA . 15689 1 791 . 1 1 78 78 VAL HB H 1 1.910 0.020 . 1 . . . . 78 VAL HB . 15689 1 792 . 1 1 78 78 VAL HG11 H 1 0.832 0.020 . 2 . . . . 78 VAL HG1 . 15689 1 793 . 1 1 78 78 VAL HG12 H 1 0.832 0.020 . 2 . . . . 78 VAL HG1 . 15689 1 794 . 1 1 78 78 VAL HG13 H 1 0.832 0.020 . 2 . . . . 78 VAL HG1 . 15689 1 795 . 1 1 78 78 VAL HG21 H 1 0.748 0.020 . 2 . . . . 78 VAL HG2 . 15689 1 796 . 1 1 78 78 VAL HG22 H 1 0.748 0.020 . 2 . . . . 78 VAL HG2 . 15689 1 797 . 1 1 78 78 VAL HG23 H 1 0.748 0.020 . 2 . . . . 78 VAL HG2 . 15689 1 798 . 1 1 78 78 VAL CA C 13 60.400 0.200 . 1 . . . . 78 VAL CA . 15689 1 799 . 1 1 78 78 VAL CB C 13 34.700 0.200 . 1 . . . . 78 VAL CB . 15689 1 800 . 1 1 78 78 VAL CG1 C 13 21.111 0.200 . 2 . . . . 78 VAL CG1 . 15689 1 801 . 1 1 78 78 VAL CG2 C 13 20.693 0.200 . 2 . . . . 78 VAL CG2 . 15689 1 802 . 1 1 78 78 VAL N N 15 127.100 0.200 . 1 . . . . 78 VAL N . 15689 1 803 . 1 1 79 79 LEU H H 1 8.050 0.020 . 1 . . . . 79 LEU H . 15689 1 804 . 1 1 79 79 LEU HA H 1 4.950 0.020 . 1 . . . . 79 LEU HA . 15689 1 805 . 1 1 79 79 LEU HB2 H 1 1.580 0.020 . 2 . . . . 79 LEU HB2 . 15689 1 806 . 1 1 79 79 LEU HD11 H 1 0.756 0.020 . 2 . . . . 79 LEU HD1 . 15689 1 807 . 1 1 79 79 LEU HD12 H 1 0.756 0.020 . 2 . . . . 79 LEU HD1 . 15689 1 808 . 1 1 79 79 LEU HD13 H 1 0.756 0.020 . 2 . . . . 79 LEU HD1 . 15689 1 809 . 1 1 79 79 LEU HD21 H 1 0.864 0.020 . 2 . . . . 79 LEU HD2 . 15689 1 810 . 1 1 79 79 LEU HD22 H 1 0.864 0.020 . 2 . . . . 79 LEU HD2 . 15689 1 811 . 1 1 79 79 LEU HD23 H 1 0.864 0.020 . 2 . . . . 79 LEU HD2 . 15689 1 812 . 1 1 79 79 LEU HG H 1 1.421 0.020 . 1 . . . . 79 LEU HG . 15689 1 813 . 1 1 79 79 LEU CA C 13 53.800 0.200 . 1 . . . . 79 LEU CA . 15689 1 814 . 1 1 79 79 LEU CB C 13 42.700 0.200 . 1 . . . . 79 LEU CB . 15689 1 815 . 1 1 79 79 LEU CD1 C 13 25.003 0.200 . 2 . . . . 79 LEU CD1 . 15689 1 816 . 1 1 79 79 LEU CD2 C 13 23.904 0.200 . 2 . . . . 79 LEU CD2 . 15689 1 817 . 1 1 79 79 LEU CG C 13 27.528 0.200 . 1 . . . . 79 LEU CG . 15689 1 818 . 1 1 79 79 LEU N N 15 123.400 0.200 . 1 . . . . 79 LEU N . 15689 1 819 . 1 1 80 80 ARG H H 1 8.540 0.020 . 1 . . . . 80 ARG H . 15689 1 820 . 1 1 80 80 ARG HA H 1 4.170 0.020 . 1 . . . . 80 ARG HA . 15689 1 821 . 1 1 80 80 ARG HB2 H 1 1.670 0.020 . 2 . . . . 80 ARG HB2 . 15689 1 822 . 1 1 80 80 ARG HB3 H 1 1.670 0.020 . 2 . . . . 80 ARG HB3 . 15689 1 823 . 1 1 80 80 ARG HD2 H 1 2.946 0.020 . 2 . . . . 80 ARG HD2 . 15689 1 824 . 1 1 80 80 ARG HD3 H 1 2.761 0.020 . 2 . . . . 80 ARG HD3 . 15689 1 825 . 1 1 80 80 ARG HG2 H 1 1.442 0.020 . 2 . . . . 80 ARG HG2 . 15689 1 826 . 1 1 80 80 ARG HG3 H 1 1.388 0.020 . 2 . . . . 80 ARG HG3 . 15689 1 827 . 1 1 80 80 ARG CA C 13 55.800 0.200 . 1 . . . . 80 ARG CA . 15689 1 828 . 1 1 80 80 ARG CB C 13 31.100 0.200 . 1 . . . . 80 ARG CB . 15689 1 829 . 1 1 80 80 ARG CG C 13 27.283 0.200 . 1 . . . . 80 ARG CG . 15689 1 830 . 1 1 80 80 ARG N N 15 123.500 0.200 . 1 . . . . 80 ARG N . 15689 1 831 . 1 1 81 81 LEU H H 1 8.250 0.020 . 1 . . . . 81 LEU H . 15689 1 832 . 1 1 81 81 LEU HA H 1 4.270 0.020 . 1 . . . . 81 LEU HA . 15689 1 833 . 1 1 81 81 LEU HB2 H 1 1.670 0.020 . 2 . . . . 81 LEU HB2 . 15689 1 834 . 1 1 81 81 LEU HB3 H 1 1.525 0.020 . 2 . . . . 81 LEU HB3 . 15689 1 835 . 1 1 81 81 LEU HD11 H 1 0.765 0.020 . 2 . . . . 81 LEU HD1 . 15689 1 836 . 1 1 81 81 LEU HD12 H 1 0.765 0.020 . 2 . . . . 81 LEU HD1 . 15689 1 837 . 1 1 81 81 LEU HD13 H 1 0.765 0.020 . 2 . . . . 81 LEU HD1 . 15689 1 838 . 1 1 81 81 LEU HD21 H 1 0.808 0.020 . 2 . . . . 81 LEU HD2 . 15689 1 839 . 1 1 81 81 LEU HD22 H 1 0.808 0.020 . 2 . . . . 81 LEU HD2 . 15689 1 840 . 1 1 81 81 LEU HD23 H 1 0.808 0.020 . 2 . . . . 81 LEU HD2 . 15689 1 841 . 1 1 81 81 LEU HG H 1 1.132 0.020 . 1 . . . . 81 LEU HG . 15689 1 842 . 1 1 81 81 LEU CA C 13 55.000 0.200 . 1 . . . . 81 LEU CA . 15689 1 843 . 1 1 81 81 LEU CB C 13 42.200 0.200 . 1 . . . . 81 LEU CB . 15689 1 844 . 1 1 81 81 LEU CD1 C 13 24.800 0.200 . 2 . . . . 81 LEU CD1 . 15689 1 845 . 1 1 81 81 LEU CD2 C 13 23.000 0.200 . 2 . . . . 81 LEU CD2 . 15689 1 846 . 1 1 81 81 LEU CG C 13 26.908 0.200 . 1 . . . . 81 LEU CG . 15689 1 847 . 1 1 81 81 LEU N N 15 124.100 0.200 . 1 . . . . 81 LEU N . 15689 1 848 . 1 1 82 82 ARG H H 1 8.310 0.020 . 1 . . . . 82 ARG H . 15689 1 849 . 1 1 82 82 ARG HA H 1 4.200 0.020 . 1 . . . . 82 ARG HA . 15689 1 850 . 1 1 82 82 ARG HB2 H 1 1.670 0.020 . 2 . . . . 82 ARG HB2 . 15689 1 851 . 1 1 82 82 ARG HB3 H 1 1.500 0.020 . 2 . . . . 82 ARG HB3 . 15689 1 852 . 1 1 82 82 ARG CA C 13 56.300 0.200 . 1 . . . . 82 ARG CA . 15689 1 853 . 1 1 82 82 ARG CB C 13 30.700 0.200 . 1 . . . . 82 ARG CB . 15689 1 854 . 1 1 82 82 ARG CG C 13 26.858 0.200 . 1 . . . . 82 ARG CG . 15689 1 855 . 1 1 82 82 ARG N N 15 121.500 0.200 . 1 . . . . 82 ARG N . 15689 1 856 . 1 1 83 83 GLY H H 1 8.410 0.020 . 1 . . . . 83 GLY H . 15689 1 857 . 1 1 83 83 GLY HA2 H 1 3.750 0.020 . 2 . . . . 83 GLY HA2 . 15689 1 858 . 1 1 83 83 GLY HA3 H 1 3.754 0.020 . 2 . . . . 83 GLY HA3 . 15689 1 859 . 1 1 83 83 GLY CA C 13 45.100 0.200 . 1 . . . . 83 GLY CA . 15689 1 860 . 1 1 83 83 GLY N N 15 110.200 0.200 . 1 . . . . 83 GLY N . 15689 1 861 . 1 1 84 84 TYR H H 1 7.950 0.020 . 1 . . . . 84 TYR H . 15689 1 862 . 1 1 84 84 TYR HA H 1 4.400 0.020 . 1 . . . . 84 TYR HA . 15689 1 863 . 1 1 84 84 TYR HB2 H 1 2.970 0.020 . 2 . . . . 84 TYR HB2 . 15689 1 864 . 1 1 84 84 TYR HB3 H 1 2.850 0.020 . 2 . . . . 84 TYR HB3 . 15689 1 865 . 1 1 84 84 TYR CA C 13 58.100 0.200 . 1 . . . . 84 TYR CA . 15689 1 866 . 1 1 84 84 TYR CB C 13 38.800 0.200 . 1 . . . . 84 TYR CB . 15689 1 867 . 1 1 84 84 TYR N N 15 119.900 0.200 . 1 . . . . 84 TYR N . 15689 1 868 . 1 1 85 85 ALA H H 1 8.150 0.020 . 1 . . . . 85 ALA H . 15689 1 869 . 1 1 85 85 ALA HA H 1 4.150 0.020 . 1 . . . . 85 ALA HA . 15689 1 870 . 1 1 85 85 ALA HB1 H 1 1.240 0.020 . 1 . . . . 85 ALA HB . 15689 1 871 . 1 1 85 85 ALA HB2 H 1 1.240 0.020 . 1 . . . . 85 ALA HB . 15689 1 872 . 1 1 85 85 ALA HB3 H 1 1.240 0.020 . 1 . . . . 85 ALA HB . 15689 1 873 . 1 1 85 85 ALA CA C 13 52.600 0.200 . 1 . . . . 85 ALA CA . 15689 1 874 . 1 1 85 85 ALA CB C 13 19.200 0.200 . 1 . . . . 85 ALA CB . 15689 1 875 . 1 1 85 85 ALA N N 15 124.800 0.200 . 1 . . . . 85 ALA N . 15689 1 876 . 1 1 86 86 ASP H H 1 8.020 0.020 . 1 . . . . 86 ASP H . 15689 1 877 . 1 1 86 86 ASP HA H 1 4.450 0.020 . 1 . . . . 86 ASP HA . 15689 1 878 . 1 1 86 86 ASP HB2 H 1 2.640 0.020 . 2 . . . . 86 ASP HB2 . 15689 1 879 . 1 1 86 86 ASP HB3 H 1 2.755 0.020 . 2 . . . . 86 ASP HB3 . 15689 1 880 . 1 1 86 86 ASP CA C 13 54.100 0.200 . 1 . . . . 86 ASP CA . 15689 1 881 . 1 1 86 86 ASP CB C 13 41.100 0.200 . 1 . . . . 86 ASP CB . 15689 1 882 . 1 1 86 86 ASP N N 15 118.900 0.200 . 1 . . . . 86 ASP N . 15689 1 883 . 1 1 87 87 LEU H H 1 8.010 0.020 . 1 . . . . 87 LEU H . 15689 1 884 . 1 1 87 87 LEU HA H 1 4.210 0.020 . 1 . . . . 87 LEU HA . 15689 1 885 . 1 1 87 87 LEU HB2 H 1 1.550 0.020 . 2 . . . . 87 LEU HB2 . 15689 1 886 . 1 1 87 87 LEU HD11 H 1 0.758 0.020 . 2 . . . . 87 LEU HD1 . 15689 1 887 . 1 1 87 87 LEU HD12 H 1 0.758 0.020 . 2 . . . . 87 LEU HD1 . 15689 1 888 . 1 1 87 87 LEU HD13 H 1 0.758 0.020 . 2 . . . . 87 LEU HD1 . 15689 1 889 . 1 1 87 87 LEU HD21 H 1 0.813 0.020 . 2 . . . . 87 LEU HD2 . 15689 1 890 . 1 1 87 87 LEU HD22 H 1 0.813 0.020 . 2 . . . . 87 LEU HD2 . 15689 1 891 . 1 1 87 87 LEU HD23 H 1 0.813 0.020 . 2 . . . . 87 LEU HD2 . 15689 1 892 . 1 1 87 87 LEU HG H 1 1.521 0.020 . 1 . . . . 87 LEU HG . 15689 1 893 . 1 1 87 87 LEU CA C 13 55.300 0.200 . 1 . . . . 87 LEU CA . 15689 1 894 . 1 1 87 87 LEU CB C 13 42.000 0.200 . 1 . . . . 87 LEU CB . 15689 1 895 . 1 1 87 87 LEU CD1 C 13 24.892 0.200 . 2 . . . . 87 LEU CD1 . 15689 1 896 . 1 1 87 87 LEU CD2 C 13 23.308 0.200 . 2 . . . . 87 LEU CD2 . 15689 1 897 . 1 1 87 87 LEU CG C 13 27.108 0.200 . 1 . . . . 87 LEU CG . 15689 1 898 . 1 1 87 87 LEU N N 15 122.400 0.200 . 1 . . . . 87 LEU N . 15689 1 899 . 1 1 88 88 ARG H H 1 8.170 0.020 . 1 . . . . 88 ARG H . 15689 1 900 . 1 1 88 88 ARG HA H 1 4.210 0.020 . 1 . . . . 88 ARG HA . 15689 1 901 . 1 1 88 88 ARG HB2 H 1 1.770 0.020 . 2 . . . . 88 ARG HB2 . 15689 1 902 . 1 1 88 88 ARG HB3 H 1 1.770 0.020 . 2 . . . . 88 ARG HB3 . 15689 1 903 . 1 1 88 88 ARG CA C 13 56.300 0.200 . 1 . . . . 88 ARG CA . 15689 1 904 . 1 1 88 88 ARG CB C 13 30.600 0.200 . 1 . . . . 88 ARG CB . 15689 1 905 . 1 1 88 88 ARG N N 15 121.200 0.200 . 1 . . . . 88 ARG N . 15689 1 906 . 1 1 91 91 PRO HA H 1 4.290 0.020 . 1 . . . . 91 PRO HA . 15689 1 907 . 1 1 91 91 PRO HB2 H 1 2.176 0.020 . 2 . . . . 91 PRO HB2 . 15689 1 908 . 1 1 91 91 PRO HB3 H 1 2.176 0.020 . 2 . . . . 91 PRO HB3 . 15689 1 909 . 1 1 91 91 PRO HG2 H 1 1.884 0.020 . 2 . . . . 91 PRO HG2 . 15689 1 910 . 1 1 91 91 PRO HG3 H 1 1.884 0.020 . 2 . . . . 91 PRO HG3 . 15689 1 911 . 1 1 91 91 PRO CA C 13 63.800 0.200 . 1 . . . . 91 PRO CA . 15689 1 912 . 1 1 91 91 PRO CB C 13 32.100 0.200 . 1 . . . . 91 PRO CB . 15689 1 913 . 1 1 91 91 PRO CD C 13 58.259 0.200 . 1 . . . . 91 PRO CD . 15689 1 914 . 1 1 91 91 PRO CG C 13 27.123 0.200 . 1 . . . . 91 PRO CG . 15689 1 915 . 1 1 92 92 ASP H H 1 8.280 0.020 . 1 . . . . 92 ASP H . 15689 1 916 . 1 1 92 92 ASP HA H 1 4.540 0.020 . 1 . . . . 92 ASP HA . 15689 1 917 . 1 1 92 92 ASP HB2 H 1 2.650 0.020 . 2 . . . . 92 ASP HB2 . 15689 1 918 . 1 1 92 92 ASP HB3 H 1 2.520 0.020 . 2 . . . . 92 ASP HB3 . 15689 1 919 . 1 1 92 92 ASP CA C 13 54.600 0.200 . 1 . . . . 92 ASP CA . 15689 1 920 . 1 1 92 92 ASP CB C 13 41.000 0.200 . 1 . . . . 92 ASP CB . 15689 1 921 . 1 1 92 92 ASP N N 15 118.700 0.200 . 1 . . . . 92 ASP N . 15689 1 922 . 1 1 93 93 ARG H H 1 7.780 0.020 . 1 . . . . 93 ARG H . 15689 1 923 . 1 1 93 93 ARG HA H 1 4.190 0.020 . 1 . . . . 93 ARG HA . 15689 1 924 . 1 1 93 93 ARG HB2 H 1 1.700 0.020 . 2 . . . . 93 ARG HB2 . 15689 1 925 . 1 1 93 93 ARG HB3 H 1 1.839 0.020 . 2 . . . . 93 ARG HB3 . 15689 1 926 . 1 1 93 93 ARG HD2 H 1 2.263 0.020 . 2 . . . . 93 ARG HD2 . 15689 1 927 . 1 1 93 93 ARG HD3 H 1 2.238 0.020 . 2 . . . . 93 ARG HD3 . 15689 1 928 . 1 1 93 93 ARG HG2 H 1 1.748 0.020 . 2 . . . . 93 ARG HG2 . 15689 1 929 . 1 1 93 93 ARG HG3 H 1 1.508 0.020 . 2 . . . . 93 ARG HG3 . 15689 1 930 . 1 1 93 93 ARG CA C 13 56.300 0.200 . 1 . . . . 93 ARG CA . 15689 1 931 . 1 1 93 93 ARG CB C 13 30.700 0.200 . 1 . . . . 93 ARG CB . 15689 1 932 . 1 1 93 93 ARG CD C 13 35.447 0.200 . 1 . . . . 93 ARG CD . 15689 1 933 . 1 1 93 93 ARG CG C 13 27.010 0.200 . 1 . . . . 93 ARG CG . 15689 1 934 . 1 1 93 93 ARG N N 15 120.700 0.200 . 1 . . . . 93 ARG N . 15689 1 935 . 1 1 94 94 GLN H H 1 8.280 0.020 . 1 . . . . 94 GLN H . 15689 1 936 . 1 1 94 94 GLN HA H 1 4.210 0.020 . 1 . . . . 94 GLN HA . 15689 1 937 . 1 1 94 94 GLN HB2 H 1 1.937 0.020 . 2 . . . . 94 GLN HB2 . 15689 1 938 . 1 1 94 94 GLN HB3 H 1 1.979 0.020 . 2 . . . . 94 GLN HB3 . 15689 1 939 . 1 1 94 94 GLN HG2 H 1 2.263 0.020 . 2 . . . . 94 GLN HG2 . 15689 1 940 . 1 1 94 94 GLN HG3 H 1 2.238 0.020 . 2 . . . . 94 GLN HG3 . 15689 1 941 . 1 1 94 94 GLN CA C 13 55.800 0.200 . 1 . . . . 94 GLN CA . 15689 1 942 . 1 1 94 94 GLN CB C 13 29.300 0.200 . 1 . . . . 94 GLN CB . 15689 1 943 . 1 1 94 94 GLN CG C 13 33.659 0.200 . 1 . . . . 94 GLN CG . 15689 1 944 . 1 1 94 94 GLN N N 15 121.000 0.200 . 1 . . . . 94 GLN N . 15689 1 945 . 1 1 95 95 ASP H H 1 8.270 0.020 . 1 . . . . 95 ASP H . 15689 1 946 . 1 1 95 95 ASP HA H 1 4.450 0.020 . 1 . . . . 95 ASP HA . 15689 1 947 . 1 1 95 95 ASP HB2 H 1 2.495 0.020 . 2 . . . . 95 ASP HB2 . 15689 1 948 . 1 1 95 95 ASP HB3 H 1 2.495 0.020 . 2 . . . . 95 ASP HB3 . 15689 1 949 . 1 1 95 95 ASP CA C 13 54.300 0.200 . 1 . . . . 95 ASP CA . 15689 1 950 . 1 1 95 95 ASP CB C 13 41.000 0.200 . 1 . . . . 95 ASP CB . 15689 1 951 . 1 1 95 95 ASP N N 15 121.000 0.200 . 1 . . . . 95 ASP N . 15689 1 952 . 1 1 96 96 HIS H H 1 8.090 0.020 . 1 . . . . 96 HIS H . 15689 1 953 . 1 1 96 96 HIS HA H 1 4.470 0.020 . 1 . . . . 96 HIS HA . 15689 1 954 . 1 1 96 96 HIS HB2 H 1 2.900 0.020 . 2 . . . . 96 HIS HB2 . 15689 1 955 . 1 1 96 96 HIS HB3 H 1 2.500 0.020 . 2 . . . . 96 HIS HB3 . 15689 1 956 . 1 1 96 96 HIS CA C 13 55.900 0.200 . 1 . . . . 96 HIS CA . 15689 1 957 . 1 1 96 96 HIS CB C 13 30.500 0.200 . 1 . . . . 96 HIS CB . 15689 1 958 . 1 1 96 96 HIS N N 15 119.300 0.200 . 1 . . . . 96 HIS N . 15689 1 959 . 1 1 97 97 HIS H H 1 8.240 0.020 . 1 . . . . 97 HIS H . 15689 1 960 . 1 1 97 97 HIS HA H 1 4.470 0.020 . 1 . . . . 97 HIS HA . 15689 1 961 . 1 1 97 97 HIS HB2 H 1 2.900 0.020 . 2 . . . . 97 HIS HB2 . 15689 1 962 . 1 1 97 97 HIS HB3 H 1 2.900 0.020 . 2 . . . . 97 HIS HB3 . 15689 1 963 . 1 1 97 97 HIS CA C 13 56.200 0.200 . 1 . . . . 97 HIS CA . 15689 1 964 . 1 1 97 97 HIS CB C 13 30.400 0.200 . 1 . . . . 97 HIS CB . 15689 1 965 . 1 1 97 97 HIS N N 15 121.300 0.200 . 1 . . . . 97 HIS N . 15689 1 966 . 1 1 98 98 PRO HA H 1 4.340 0.020 . 1 . . . . 98 PRO HA . 15689 1 967 . 1 1 98 98 PRO HB2 H 1 2.183 0.020 . 2 . . . . 98 PRO HB2 . 15689 1 968 . 1 1 98 98 PRO HB3 H 1 2.183 0.020 . 2 . . . . 98 PRO HB3 . 15689 1 969 . 1 1 98 98 PRO HD2 H 1 3.539 0.020 . 2 . . . . 98 PRO HD2 . 15689 1 970 . 1 1 98 98 PRO HD3 H 1 3.364 0.020 . 2 . . . . 98 PRO HD3 . 15689 1 971 . 1 1 98 98 PRO HG2 H 1 1.877 0.020 . 2 . . . . 98 PRO HG2 . 15689 1 972 . 1 1 98 98 PRO HG3 H 1 1.887 0.020 . 2 . . . . 98 PRO HG3 . 15689 1 973 . 1 1 98 98 PRO CA C 13 63.700 0.200 . 1 . . . . 98 PRO CA . 15689 1 974 . 1 1 98 98 PRO CB C 13 31.900 0.200 . 1 . . . . 98 PRO CB . 15689 1 975 . 1 1 98 98 PRO CD C 13 58.259 0.200 . 1 . . . . 98 PRO CD . 15689 1 976 . 1 1 98 98 PRO CG C 13 27.254 0.200 . 1 . . . . 98 PRO CG . 15689 1 977 . 1 1 99 99 GLY H H 1 8.660 0.020 . 1 . . . . 99 GLY H . 15689 1 978 . 1 1 99 99 GLY HA2 H 1 3.920 0.020 . 2 . . . . 99 GLY HA2 . 15689 1 979 . 1 1 99 99 GLY HA3 H 1 3.920 0.020 . 2 . . . . 99 GLY HA3 . 15689 1 980 . 1 1 99 99 GLY CA C 13 45.200 0.200 . 1 . . . . 99 GLY CA . 15689 1 981 . 1 1 99 99 GLY N N 15 110.000 0.200 . 1 . . . . 99 GLY N . 15689 1 982 . 1 1 100 100 SER H H 1 8.170 0.020 . 1 . . . . 100 SER H . 15689 1 983 . 1 1 100 100 SER HA H 1 4.360 0.020 . 1 . . . . 100 SER HA . 15689 1 984 . 1 1 100 100 SER HB2 H 1 3.800 0.020 . 2 . . . . 100 SER HB2 . 15689 1 985 . 1 1 100 100 SER HB3 H 1 3.801 0.020 . 2 . . . . 100 SER HB3 . 15689 1 986 . 1 1 100 100 SER CA C 13 58.500 0.200 . 1 . . . . 100 SER CA . 15689 1 987 . 1 1 100 100 SER CB C 13 64.000 0.200 . 1 . . . . 100 SER CB . 15689 1 988 . 1 1 100 100 SER N N 15 115.600 0.200 . 1 . . . . 100 SER N . 15689 1 989 . 1 1 101 101 GLY H H 1 8.420 0.020 . 1 . . . . 101 GLY H . 15689 1 990 . 1 1 101 101 GLY HA2 H 1 3.890 0.020 . 2 . . . . 101 GLY HA2 . 15689 1 991 . 1 1 101 101 GLY HA3 H 1 3.920 0.020 . 2 . . . . 101 GLY HA3 . 15689 1 992 . 1 1 101 101 GLY CA C 13 45.200 0.200 . 1 . . . . 101 GLY CA . 15689 1 993 . 1 1 101 101 GLY N N 15 111.000 0.200 . 1 . . . . 101 GLY N . 15689 1 994 . 1 1 102 102 ALA H H 1 8.030 0.020 . 1 . . . . 102 ALA H . 15689 1 995 . 1 1 102 102 ALA HA H 1 4.250 0.020 . 1 . . . . 102 ALA HA . 15689 1 996 . 1 1 102 102 ALA HB1 H 1 1.290 0.020 . 1 . . . . 102 ALA HB . 15689 1 997 . 1 1 102 102 ALA HB2 H 1 1.290 0.020 . 1 . . . . 102 ALA HB . 15689 1 998 . 1 1 102 102 ALA HB3 H 1 1.290 0.020 . 1 . . . . 102 ALA HB . 15689 1 999 . 1 1 102 102 ALA CA C 13 52.500 0.200 . 1 . . . . 102 ALA CA . 15689 1 1000 . 1 1 102 102 ALA CB C 13 19.200 0.200 . 1 . . . . 102 ALA CB . 15689 1 1001 . 1 1 102 102 ALA N N 15 124.100 0.200 . 1 . . . . 102 ALA N . 15689 1 stop_ save_